data_9DL2
# 
_entry.id   9DL2 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9DL2         pdb_00009dl2 10.2210/pdb9dl2/pdb 
WWPDB D_1000287809 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2024-11-27 
2 'Structure model' 1 1 2024-12-11 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
2 2 'Structure model' '_citation.title'                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9DL2 
_pdbx_database_status.recvd_initial_deposition_date   2024-09-10 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              tannerjj@missouri.edu 
_pdbx_contact_author.name_first         John 
_pdbx_contact_author.name_last          Tanner 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-8314-113X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Tanner, J.J.' 1 ? 
'Meeks, K.R.'  2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   CH 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Molecules 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1420-3049 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            29 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Crystallographic Fragment Screening of a Bifunctional Proline Catabolic Enzyme Reveals New Inhibitor Templates for Proline Dehydrogenase and L-Glutamate-gamma-semialdehyde Dehydrogenase.
;
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.3390/molecules29225408 
_citation.pdbx_database_id_PubMed   39598797 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Meeks, K.R.'  1 ? 
primary 'Bogner, A.N.' 2 ? 
primary 'Nix, J.C.'    3 ? 
primary 'Tanner, J.J.' 4 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1  polymer     man 'Bifunctional protein PutA'                      131961.656 2    1.5.5.2,1.2.1.88 ? ? ? 
2  non-polymer syn 'FLAVIN-ADENINE DINUCLEOTIDE'                    785.550    2    ?                ? ? ? 
3  non-polymer syn 'DI(HYDROXYETHYL)ETHER'                          106.120    6    ?                ? ? ? 
4  non-polymer syn '2,3-dihydro-1,4-benzodioxine-5-carboxylic acid' 180.157    2    ?                ? ? ? 
5  non-polymer syn 'FORMIC ACID'                                    46.025     4    ?                ? ? ? 
6  non-polymer syn NICOTINAMIDE-ADENINE-DINUCLEOTIDE                663.425    2    ?                ? ? ? 
7  non-polymer syn 'SULFATE ION'                                    96.063     7    ?                ? ? ? 
8  non-polymer syn 'MAGNESIUM ION'                                  24.305     2    ?                ? ? ? 
9  non-polymer syn 'TRIETHYLENE GLYCOL'                             150.173    1    ?                ? ? ? 
10 non-polymer syn 'TETRAETHYLENE GLYCOL'                           194.226    1    ?                ? ? ? 
11 water       nat water                                            18.015     2311 ?                ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SMMSPNPLQKPAIDAAPAPFADFAPPVRPQSTLRRAITAAYRRPETECLPPLVEAATQSKEIRDAAASTARKLIEALRGK
HSGSGVEGLVQEYSLSSQEGVALMCLAEALLRIPDTATRDALIRDKIADGNWKSHLGGSRSLFVNAATWGLVVTGKLTST
VNDRSLAAALTRLISRCGEPVIRRGVDMAMRMMGEQFVTGETIREALKRSKELEEKGFSYSYDMLGEAATTAADAERYYR
DYESAIHAIGKASAGRGIYEGPGISIKLSALHPRYSRAQAARVMGELLPRVKALALLAKNYDIGLNIDAEEADRLELSLD
LLEVLCLDGDLSGWNGMGFVVQAYGKRCPFVLDFIIDLARRSGRRIMVRLVKGAYWDAEIKRAQLDGLADFPVFTRKIHT
DVSYIACAAKLLAATDVVFPQFATHNAQTLAAIYHMAGKDFHVGKYEFQCLHGMGEPLYEEVVGRGKLDRPCRIYAPVGT
HETLLAYLVRRLLENGANSSFVHRINDPKVSIDELIADPVEVVRAMPVVGAKHDRIALPAELFGDARTNSAGLDLSNEET
LASLTEALRESAAMKWTALPQLATGPAAGETRTVLNPGDHRDVVGSVTETSEEDARRAVRLAADAAPDWAAVPPSERAAC
LDRAAELMQARMPTLLGLIIREAGKSALNAIAEVREAIDFLRYYAEQTRRTLGPGHGPLGPIVCISPWNFPLAIFTGQIA
AALVAGNPVLAKPAEETPLIAAEGVRILREAGIPASALQLLPGDGRVGAALVAAAETAGVMFTGSTEVARLIQAQLADRL
SPAGRPIPLIAETGGQNAMIVDSSALAEQVVGDVITSAFDSAGQRCSALRVLCLQEDVADRILTMLKGALHELHIGRTDR
LSVDVGPVITSEAKDNIEKHIERMRGLGRKVEQIGLASETGVGTFVPPTIIELEKLSDLQREVFGPVLHVIRYRRDDLDR
LVDDVNATGYGLTFGLHTRLDETIAHVTSRIKAGNLYINRNIIGAVVGVQPFGGRGLSGTGPKAGGPLYLGRLVTTAPVP
PQHSSVHTDPVLLDFAKWLDGKGARAEAEAARNAGSSSALGLDLELPGPVGERNLYTLHARGRILLVPATESGLYHQLAA
ALATGNSVAIDAASGLQASLKNLPQTVGLRVSWSKDWAADGPFAGALVEGDAERIRAVNKAIAALPGPLLLVQAASSGEI
ARNPDAYCLNWLVEEVSASINTAAAGGNASLMAIG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMMSPNPLQKPAIDAAPAPFADFAPPVRPQSTLRRAITAAYRRPETECLPPLVEAATQSKEIRDAAASTARKLIEALRGK
HSGSGVEGLVQEYSLSSQEGVALMCLAEALLRIPDTATRDALIRDKIADGNWKSHLGGSRSLFVNAATWGLVVTGKLTST
VNDRSLAAALTRLISRCGEPVIRRGVDMAMRMMGEQFVTGETIREALKRSKELEEKGFSYSYDMLGEAATTAADAERYYR
DYESAIHAIGKASAGRGIYEGPGISIKLSALHPRYSRAQAARVMGELLPRVKALALLAKNYDIGLNIDAEEADRLELSLD
LLEVLCLDGDLSGWNGMGFVVQAYGKRCPFVLDFIIDLARRSGRRIMVRLVKGAYWDAEIKRAQLDGLADFPVFTRKIHT
DVSYIACAAKLLAATDVVFPQFATHNAQTLAAIYHMAGKDFHVGKYEFQCLHGMGEPLYEEVVGRGKLDRPCRIYAPVGT
HETLLAYLVRRLLENGANSSFVHRINDPKVSIDELIADPVEVVRAMPVVGAKHDRIALPAELFGDARTNSAGLDLSNEET
LASLTEALRESAAMKWTALPQLATGPAAGETRTVLNPGDHRDVVGSVTETSEEDARRAVRLAADAAPDWAAVPPSERAAC
LDRAAELMQARMPTLLGLIIREAGKSALNAIAEVREAIDFLRYYAEQTRRTLGPGHGPLGPIVCISPWNFPLAIFTGQIA
AALVAGNPVLAKPAEETPLIAAEGVRILREAGIPASALQLLPGDGRVGAALVAAAETAGVMFTGSTEVARLIQAQLADRL
SPAGRPIPLIAETGGQNAMIVDSSALAEQVVGDVITSAFDSAGQRCSALRVLCLQEDVADRILTMLKGALHELHIGRTDR
LSVDVGPVITSEAKDNIEKHIERMRGLGRKVEQIGLASETGVGTFVPPTIIELEKLSDLQREVFGPVLHVIRYRRDDLDR
LVDDVNATGYGLTFGLHTRLDETIAHVTSRIKAGNLYINRNIIGAVVGVQPFGGRGLSGTGPKAGGPLYLGRLVTTAPVP
PQHSSVHTDPVLLDFAKWLDGKGARAEAEAARNAGSSSALGLDLELPGPVGERNLYTLHARGRILLVPATESGLYHQLAA
ALATGNSVAIDAASGLQASLKNLPQTVGLRVSWSKDWAADGPFAGALVEGDAERIRAVNKAIAALPGPLLLVQAASSGEI
ARNPDAYCLNWLVEEVSASINTAAAGGNASLMAIG
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2  'FLAVIN-ADENINE DINUCLEOTIDE'                    FAD 
3  'DI(HYDROXYETHYL)ETHER'                          PEG 
4  '2,3-dihydro-1,4-benzodioxine-5-carboxylic acid' 53E 
5  'FORMIC ACID'                                    FMT 
6  NICOTINAMIDE-ADENINE-DINUCLEOTIDE                NAD 
7  'SULFATE ION'                                    SO4 
8  'MAGNESIUM ION'                                  MG  
9  'TRIETHYLENE GLYCOL'                             PGE 
10 'TETRAETHYLENE GLYCOL'                           PG4 
11 water                                            HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1    SER n 
1 2    MET n 
1 3    MET n 
1 4    SER n 
1 5    PRO n 
1 6    ASN n 
1 7    PRO n 
1 8    LEU n 
1 9    GLN n 
1 10   LYS n 
1 11   PRO n 
1 12   ALA n 
1 13   ILE n 
1 14   ASP n 
1 15   ALA n 
1 16   ALA n 
1 17   PRO n 
1 18   ALA n 
1 19   PRO n 
1 20   PHE n 
1 21   ALA n 
1 22   ASP n 
1 23   PHE n 
1 24   ALA n 
1 25   PRO n 
1 26   PRO n 
1 27   VAL n 
1 28   ARG n 
1 29   PRO n 
1 30   GLN n 
1 31   SER n 
1 32   THR n 
1 33   LEU n 
1 34   ARG n 
1 35   ARG n 
1 36   ALA n 
1 37   ILE n 
1 38   THR n 
1 39   ALA n 
1 40   ALA n 
1 41   TYR n 
1 42   ARG n 
1 43   ARG n 
1 44   PRO n 
1 45   GLU n 
1 46   THR n 
1 47   GLU n 
1 48   CYS n 
1 49   LEU n 
1 50   PRO n 
1 51   PRO n 
1 52   LEU n 
1 53   VAL n 
1 54   GLU n 
1 55   ALA n 
1 56   ALA n 
1 57   THR n 
1 58   GLN n 
1 59   SER n 
1 60   LYS n 
1 61   GLU n 
1 62   ILE n 
1 63   ARG n 
1 64   ASP n 
1 65   ALA n 
1 66   ALA n 
1 67   ALA n 
1 68   SER n 
1 69   THR n 
1 70   ALA n 
1 71   ARG n 
1 72   LYS n 
1 73   LEU n 
1 74   ILE n 
1 75   GLU n 
1 76   ALA n 
1 77   LEU n 
1 78   ARG n 
1 79   GLY n 
1 80   LYS n 
1 81   HIS n 
1 82   SER n 
1 83   GLY n 
1 84   SER n 
1 85   GLY n 
1 86   VAL n 
1 87   GLU n 
1 88   GLY n 
1 89   LEU n 
1 90   VAL n 
1 91   GLN n 
1 92   GLU n 
1 93   TYR n 
1 94   SER n 
1 95   LEU n 
1 96   SER n 
1 97   SER n 
1 98   GLN n 
1 99   GLU n 
1 100  GLY n 
1 101  VAL n 
1 102  ALA n 
1 103  LEU n 
1 104  MET n 
1 105  CYS n 
1 106  LEU n 
1 107  ALA n 
1 108  GLU n 
1 109  ALA n 
1 110  LEU n 
1 111  LEU n 
1 112  ARG n 
1 113  ILE n 
1 114  PRO n 
1 115  ASP n 
1 116  THR n 
1 117  ALA n 
1 118  THR n 
1 119  ARG n 
1 120  ASP n 
1 121  ALA n 
1 122  LEU n 
1 123  ILE n 
1 124  ARG n 
1 125  ASP n 
1 126  LYS n 
1 127  ILE n 
1 128  ALA n 
1 129  ASP n 
1 130  GLY n 
1 131  ASN n 
1 132  TRP n 
1 133  LYS n 
1 134  SER n 
1 135  HIS n 
1 136  LEU n 
1 137  GLY n 
1 138  GLY n 
1 139  SER n 
1 140  ARG n 
1 141  SER n 
1 142  LEU n 
1 143  PHE n 
1 144  VAL n 
1 145  ASN n 
1 146  ALA n 
1 147  ALA n 
1 148  THR n 
1 149  TRP n 
1 150  GLY n 
1 151  LEU n 
1 152  VAL n 
1 153  VAL n 
1 154  THR n 
1 155  GLY n 
1 156  LYS n 
1 157  LEU n 
1 158  THR n 
1 159  SER n 
1 160  THR n 
1 161  VAL n 
1 162  ASN n 
1 163  ASP n 
1 164  ARG n 
1 165  SER n 
1 166  LEU n 
1 167  ALA n 
1 168  ALA n 
1 169  ALA n 
1 170  LEU n 
1 171  THR n 
1 172  ARG n 
1 173  LEU n 
1 174  ILE n 
1 175  SER n 
1 176  ARG n 
1 177  CYS n 
1 178  GLY n 
1 179  GLU n 
1 180  PRO n 
1 181  VAL n 
1 182  ILE n 
1 183  ARG n 
1 184  ARG n 
1 185  GLY n 
1 186  VAL n 
1 187  ASP n 
1 188  MET n 
1 189  ALA n 
1 190  MET n 
1 191  ARG n 
1 192  MET n 
1 193  MET n 
1 194  GLY n 
1 195  GLU n 
1 196  GLN n 
1 197  PHE n 
1 198  VAL n 
1 199  THR n 
1 200  GLY n 
1 201  GLU n 
1 202  THR n 
1 203  ILE n 
1 204  ARG n 
1 205  GLU n 
1 206  ALA n 
1 207  LEU n 
1 208  LYS n 
1 209  ARG n 
1 210  SER n 
1 211  LYS n 
1 212  GLU n 
1 213  LEU n 
1 214  GLU n 
1 215  GLU n 
1 216  LYS n 
1 217  GLY n 
1 218  PHE n 
1 219  SER n 
1 220  TYR n 
1 221  SER n 
1 222  TYR n 
1 223  ASP n 
1 224  MET n 
1 225  LEU n 
1 226  GLY n 
1 227  GLU n 
1 228  ALA n 
1 229  ALA n 
1 230  THR n 
1 231  THR n 
1 232  ALA n 
1 233  ALA n 
1 234  ASP n 
1 235  ALA n 
1 236  GLU n 
1 237  ARG n 
1 238  TYR n 
1 239  TYR n 
1 240  ARG n 
1 241  ASP n 
1 242  TYR n 
1 243  GLU n 
1 244  SER n 
1 245  ALA n 
1 246  ILE n 
1 247  HIS n 
1 248  ALA n 
1 249  ILE n 
1 250  GLY n 
1 251  LYS n 
1 252  ALA n 
1 253  SER n 
1 254  ALA n 
1 255  GLY n 
1 256  ARG n 
1 257  GLY n 
1 258  ILE n 
1 259  TYR n 
1 260  GLU n 
1 261  GLY n 
1 262  PRO n 
1 263  GLY n 
1 264  ILE n 
1 265  SER n 
1 266  ILE n 
1 267  LYS n 
1 268  LEU n 
1 269  SER n 
1 270  ALA n 
1 271  LEU n 
1 272  HIS n 
1 273  PRO n 
1 274  ARG n 
1 275  TYR n 
1 276  SER n 
1 277  ARG n 
1 278  ALA n 
1 279  GLN n 
1 280  ALA n 
1 281  ALA n 
1 282  ARG n 
1 283  VAL n 
1 284  MET n 
1 285  GLY n 
1 286  GLU n 
1 287  LEU n 
1 288  LEU n 
1 289  PRO n 
1 290  ARG n 
1 291  VAL n 
1 292  LYS n 
1 293  ALA n 
1 294  LEU n 
1 295  ALA n 
1 296  LEU n 
1 297  LEU n 
1 298  ALA n 
1 299  LYS n 
1 300  ASN n 
1 301  TYR n 
1 302  ASP n 
1 303  ILE n 
1 304  GLY n 
1 305  LEU n 
1 306  ASN n 
1 307  ILE n 
1 308  ASP n 
1 309  ALA n 
1 310  GLU n 
1 311  GLU n 
1 312  ALA n 
1 313  ASP n 
1 314  ARG n 
1 315  LEU n 
1 316  GLU n 
1 317  LEU n 
1 318  SER n 
1 319  LEU n 
1 320  ASP n 
1 321  LEU n 
1 322  LEU n 
1 323  GLU n 
1 324  VAL n 
1 325  LEU n 
1 326  CYS n 
1 327  LEU n 
1 328  ASP n 
1 329  GLY n 
1 330  ASP n 
1 331  LEU n 
1 332  SER n 
1 333  GLY n 
1 334  TRP n 
1 335  ASN n 
1 336  GLY n 
1 337  MET n 
1 338  GLY n 
1 339  PHE n 
1 340  VAL n 
1 341  VAL n 
1 342  GLN n 
1 343  ALA n 
1 344  TYR n 
1 345  GLY n 
1 346  LYS n 
1 347  ARG n 
1 348  CYS n 
1 349  PRO n 
1 350  PHE n 
1 351  VAL n 
1 352  LEU n 
1 353  ASP n 
1 354  PHE n 
1 355  ILE n 
1 356  ILE n 
1 357  ASP n 
1 358  LEU n 
1 359  ALA n 
1 360  ARG n 
1 361  ARG n 
1 362  SER n 
1 363  GLY n 
1 364  ARG n 
1 365  ARG n 
1 366  ILE n 
1 367  MET n 
1 368  VAL n 
1 369  ARG n 
1 370  LEU n 
1 371  VAL n 
1 372  LYS n 
1 373  GLY n 
1 374  ALA n 
1 375  TYR n 
1 376  TRP n 
1 377  ASP n 
1 378  ALA n 
1 379  GLU n 
1 380  ILE n 
1 381  LYS n 
1 382  ARG n 
1 383  ALA n 
1 384  GLN n 
1 385  LEU n 
1 386  ASP n 
1 387  GLY n 
1 388  LEU n 
1 389  ALA n 
1 390  ASP n 
1 391  PHE n 
1 392  PRO n 
1 393  VAL n 
1 394  PHE n 
1 395  THR n 
1 396  ARG n 
1 397  LYS n 
1 398  ILE n 
1 399  HIS n 
1 400  THR n 
1 401  ASP n 
1 402  VAL n 
1 403  SER n 
1 404  TYR n 
1 405  ILE n 
1 406  ALA n 
1 407  CYS n 
1 408  ALA n 
1 409  ALA n 
1 410  LYS n 
1 411  LEU n 
1 412  LEU n 
1 413  ALA n 
1 414  ALA n 
1 415  THR n 
1 416  ASP n 
1 417  VAL n 
1 418  VAL n 
1 419  PHE n 
1 420  PRO n 
1 421  GLN n 
1 422  PHE n 
1 423  ALA n 
1 424  THR n 
1 425  HIS n 
1 426  ASN n 
1 427  ALA n 
1 428  GLN n 
1 429  THR n 
1 430  LEU n 
1 431  ALA n 
1 432  ALA n 
1 433  ILE n 
1 434  TYR n 
1 435  HIS n 
1 436  MET n 
1 437  ALA n 
1 438  GLY n 
1 439  LYS n 
1 440  ASP n 
1 441  PHE n 
1 442  HIS n 
1 443  VAL n 
1 444  GLY n 
1 445  LYS n 
1 446  TYR n 
1 447  GLU n 
1 448  PHE n 
1 449  GLN n 
1 450  CYS n 
1 451  LEU n 
1 452  HIS n 
1 453  GLY n 
1 454  MET n 
1 455  GLY n 
1 456  GLU n 
1 457  PRO n 
1 458  LEU n 
1 459  TYR n 
1 460  GLU n 
1 461  GLU n 
1 462  VAL n 
1 463  VAL n 
1 464  GLY n 
1 465  ARG n 
1 466  GLY n 
1 467  LYS n 
1 468  LEU n 
1 469  ASP n 
1 470  ARG n 
1 471  PRO n 
1 472  CYS n 
1 473  ARG n 
1 474  ILE n 
1 475  TYR n 
1 476  ALA n 
1 477  PRO n 
1 478  VAL n 
1 479  GLY n 
1 480  THR n 
1 481  HIS n 
1 482  GLU n 
1 483  THR n 
1 484  LEU n 
1 485  LEU n 
1 486  ALA n 
1 487  TYR n 
1 488  LEU n 
1 489  VAL n 
1 490  ARG n 
1 491  ARG n 
1 492  LEU n 
1 493  LEU n 
1 494  GLU n 
1 495  ASN n 
1 496  GLY n 
1 497  ALA n 
1 498  ASN n 
1 499  SER n 
1 500  SER n 
1 501  PHE n 
1 502  VAL n 
1 503  HIS n 
1 504  ARG n 
1 505  ILE n 
1 506  ASN n 
1 507  ASP n 
1 508  PRO n 
1 509  LYS n 
1 510  VAL n 
1 511  SER n 
1 512  ILE n 
1 513  ASP n 
1 514  GLU n 
1 515  LEU n 
1 516  ILE n 
1 517  ALA n 
1 518  ASP n 
1 519  PRO n 
1 520  VAL n 
1 521  GLU n 
1 522  VAL n 
1 523  VAL n 
1 524  ARG n 
1 525  ALA n 
1 526  MET n 
1 527  PRO n 
1 528  VAL n 
1 529  VAL n 
1 530  GLY n 
1 531  ALA n 
1 532  LYS n 
1 533  HIS n 
1 534  ASP n 
1 535  ARG n 
1 536  ILE n 
1 537  ALA n 
1 538  LEU n 
1 539  PRO n 
1 540  ALA n 
1 541  GLU n 
1 542  LEU n 
1 543  PHE n 
1 544  GLY n 
1 545  ASP n 
1 546  ALA n 
1 547  ARG n 
1 548  THR n 
1 549  ASN n 
1 550  SER n 
1 551  ALA n 
1 552  GLY n 
1 553  LEU n 
1 554  ASP n 
1 555  LEU n 
1 556  SER n 
1 557  ASN n 
1 558  GLU n 
1 559  GLU n 
1 560  THR n 
1 561  LEU n 
1 562  ALA n 
1 563  SER n 
1 564  LEU n 
1 565  THR n 
1 566  GLU n 
1 567  ALA n 
1 568  LEU n 
1 569  ARG n 
1 570  GLU n 
1 571  SER n 
1 572  ALA n 
1 573  ALA n 
1 574  MET n 
1 575  LYS n 
1 576  TRP n 
1 577  THR n 
1 578  ALA n 
1 579  LEU n 
1 580  PRO n 
1 581  GLN n 
1 582  LEU n 
1 583  ALA n 
1 584  THR n 
1 585  GLY n 
1 586  PRO n 
1 587  ALA n 
1 588  ALA n 
1 589  GLY n 
1 590  GLU n 
1 591  THR n 
1 592  ARG n 
1 593  THR n 
1 594  VAL n 
1 595  LEU n 
1 596  ASN n 
1 597  PRO n 
1 598  GLY n 
1 599  ASP n 
1 600  HIS n 
1 601  ARG n 
1 602  ASP n 
1 603  VAL n 
1 604  VAL n 
1 605  GLY n 
1 606  SER n 
1 607  VAL n 
1 608  THR n 
1 609  GLU n 
1 610  THR n 
1 611  SER n 
1 612  GLU n 
1 613  GLU n 
1 614  ASP n 
1 615  ALA n 
1 616  ARG n 
1 617  ARG n 
1 618  ALA n 
1 619  VAL n 
1 620  ARG n 
1 621  LEU n 
1 622  ALA n 
1 623  ALA n 
1 624  ASP n 
1 625  ALA n 
1 626  ALA n 
1 627  PRO n 
1 628  ASP n 
1 629  TRP n 
1 630  ALA n 
1 631  ALA n 
1 632  VAL n 
1 633  PRO n 
1 634  PRO n 
1 635  SER n 
1 636  GLU n 
1 637  ARG n 
1 638  ALA n 
1 639  ALA n 
1 640  CYS n 
1 641  LEU n 
1 642  ASP n 
1 643  ARG n 
1 644  ALA n 
1 645  ALA n 
1 646  GLU n 
1 647  LEU n 
1 648  MET n 
1 649  GLN n 
1 650  ALA n 
1 651  ARG n 
1 652  MET n 
1 653  PRO n 
1 654  THR n 
1 655  LEU n 
1 656  LEU n 
1 657  GLY n 
1 658  LEU n 
1 659  ILE n 
1 660  ILE n 
1 661  ARG n 
1 662  GLU n 
1 663  ALA n 
1 664  GLY n 
1 665  LYS n 
1 666  SER n 
1 667  ALA n 
1 668  LEU n 
1 669  ASN n 
1 670  ALA n 
1 671  ILE n 
1 672  ALA n 
1 673  GLU n 
1 674  VAL n 
1 675  ARG n 
1 676  GLU n 
1 677  ALA n 
1 678  ILE n 
1 679  ASP n 
1 680  PHE n 
1 681  LEU n 
1 682  ARG n 
1 683  TYR n 
1 684  TYR n 
1 685  ALA n 
1 686  GLU n 
1 687  GLN n 
1 688  THR n 
1 689  ARG n 
1 690  ARG n 
1 691  THR n 
1 692  LEU n 
1 693  GLY n 
1 694  PRO n 
1 695  GLY n 
1 696  HIS n 
1 697  GLY n 
1 698  PRO n 
1 699  LEU n 
1 700  GLY n 
1 701  PRO n 
1 702  ILE n 
1 703  VAL n 
1 704  CYS n 
1 705  ILE n 
1 706  SER n 
1 707  PRO n 
1 708  TRP n 
1 709  ASN n 
1 710  PHE n 
1 711  PRO n 
1 712  LEU n 
1 713  ALA n 
1 714  ILE n 
1 715  PHE n 
1 716  THR n 
1 717  GLY n 
1 718  GLN n 
1 719  ILE n 
1 720  ALA n 
1 721  ALA n 
1 722  ALA n 
1 723  LEU n 
1 724  VAL n 
1 725  ALA n 
1 726  GLY n 
1 727  ASN n 
1 728  PRO n 
1 729  VAL n 
1 730  LEU n 
1 731  ALA n 
1 732  LYS n 
1 733  PRO n 
1 734  ALA n 
1 735  GLU n 
1 736  GLU n 
1 737  THR n 
1 738  PRO n 
1 739  LEU n 
1 740  ILE n 
1 741  ALA n 
1 742  ALA n 
1 743  GLU n 
1 744  GLY n 
1 745  VAL n 
1 746  ARG n 
1 747  ILE n 
1 748  LEU n 
1 749  ARG n 
1 750  GLU n 
1 751  ALA n 
1 752  GLY n 
1 753  ILE n 
1 754  PRO n 
1 755  ALA n 
1 756  SER n 
1 757  ALA n 
1 758  LEU n 
1 759  GLN n 
1 760  LEU n 
1 761  LEU n 
1 762  PRO n 
1 763  GLY n 
1 764  ASP n 
1 765  GLY n 
1 766  ARG n 
1 767  VAL n 
1 768  GLY n 
1 769  ALA n 
1 770  ALA n 
1 771  LEU n 
1 772  VAL n 
1 773  ALA n 
1 774  ALA n 
1 775  ALA n 
1 776  GLU n 
1 777  THR n 
1 778  ALA n 
1 779  GLY n 
1 780  VAL n 
1 781  MET n 
1 782  PHE n 
1 783  THR n 
1 784  GLY n 
1 785  SER n 
1 786  THR n 
1 787  GLU n 
1 788  VAL n 
1 789  ALA n 
1 790  ARG n 
1 791  LEU n 
1 792  ILE n 
1 793  GLN n 
1 794  ALA n 
1 795  GLN n 
1 796  LEU n 
1 797  ALA n 
1 798  ASP n 
1 799  ARG n 
1 800  LEU n 
1 801  SER n 
1 802  PRO n 
1 803  ALA n 
1 804  GLY n 
1 805  ARG n 
1 806  PRO n 
1 807  ILE n 
1 808  PRO n 
1 809  LEU n 
1 810  ILE n 
1 811  ALA n 
1 812  GLU n 
1 813  THR n 
1 814  GLY n 
1 815  GLY n 
1 816  GLN n 
1 817  ASN n 
1 818  ALA n 
1 819  MET n 
1 820  ILE n 
1 821  VAL n 
1 822  ASP n 
1 823  SER n 
1 824  SER n 
1 825  ALA n 
1 826  LEU n 
1 827  ALA n 
1 828  GLU n 
1 829  GLN n 
1 830  VAL n 
1 831  VAL n 
1 832  GLY n 
1 833  ASP n 
1 834  VAL n 
1 835  ILE n 
1 836  THR n 
1 837  SER n 
1 838  ALA n 
1 839  PHE n 
1 840  ASP n 
1 841  SER n 
1 842  ALA n 
1 843  GLY n 
1 844  GLN n 
1 845  ARG n 
1 846  CYS n 
1 847  SER n 
1 848  ALA n 
1 849  LEU n 
1 850  ARG n 
1 851  VAL n 
1 852  LEU n 
1 853  CYS n 
1 854  LEU n 
1 855  GLN n 
1 856  GLU n 
1 857  ASP n 
1 858  VAL n 
1 859  ALA n 
1 860  ASP n 
1 861  ARG n 
1 862  ILE n 
1 863  LEU n 
1 864  THR n 
1 865  MET n 
1 866  LEU n 
1 867  LYS n 
1 868  GLY n 
1 869  ALA n 
1 870  LEU n 
1 871  HIS n 
1 872  GLU n 
1 873  LEU n 
1 874  HIS n 
1 875  ILE n 
1 876  GLY n 
1 877  ARG n 
1 878  THR n 
1 879  ASP n 
1 880  ARG n 
1 881  LEU n 
1 882  SER n 
1 883  VAL n 
1 884  ASP n 
1 885  VAL n 
1 886  GLY n 
1 887  PRO n 
1 888  VAL n 
1 889  ILE n 
1 890  THR n 
1 891  SER n 
1 892  GLU n 
1 893  ALA n 
1 894  LYS n 
1 895  ASP n 
1 896  ASN n 
1 897  ILE n 
1 898  GLU n 
1 899  LYS n 
1 900  HIS n 
1 901  ILE n 
1 902  GLU n 
1 903  ARG n 
1 904  MET n 
1 905  ARG n 
1 906  GLY n 
1 907  LEU n 
1 908  GLY n 
1 909  ARG n 
1 910  LYS n 
1 911  VAL n 
1 912  GLU n 
1 913  GLN n 
1 914  ILE n 
1 915  GLY n 
1 916  LEU n 
1 917  ALA n 
1 918  SER n 
1 919  GLU n 
1 920  THR n 
1 921  GLY n 
1 922  VAL n 
1 923  GLY n 
1 924  THR n 
1 925  PHE n 
1 926  VAL n 
1 927  PRO n 
1 928  PRO n 
1 929  THR n 
1 930  ILE n 
1 931  ILE n 
1 932  GLU n 
1 933  LEU n 
1 934  GLU n 
1 935  LYS n 
1 936  LEU n 
1 937  SER n 
1 938  ASP n 
1 939  LEU n 
1 940  GLN n 
1 941  ARG n 
1 942  GLU n 
1 943  VAL n 
1 944  PHE n 
1 945  GLY n 
1 946  PRO n 
1 947  VAL n 
1 948  LEU n 
1 949  HIS n 
1 950  VAL n 
1 951  ILE n 
1 952  ARG n 
1 953  TYR n 
1 954  ARG n 
1 955  ARG n 
1 956  ASP n 
1 957  ASP n 
1 958  LEU n 
1 959  ASP n 
1 960  ARG n 
1 961  LEU n 
1 962  VAL n 
1 963  ASP n 
1 964  ASP n 
1 965  VAL n 
1 966  ASN n 
1 967  ALA n 
1 968  THR n 
1 969  GLY n 
1 970  TYR n 
1 971  GLY n 
1 972  LEU n 
1 973  THR n 
1 974  PHE n 
1 975  GLY n 
1 976  LEU n 
1 977  HIS n 
1 978  THR n 
1 979  ARG n 
1 980  LEU n 
1 981  ASP n 
1 982  GLU n 
1 983  THR n 
1 984  ILE n 
1 985  ALA n 
1 986  HIS n 
1 987  VAL n 
1 988  THR n 
1 989  SER n 
1 990  ARG n 
1 991  ILE n 
1 992  LYS n 
1 993  ALA n 
1 994  GLY n 
1 995  ASN n 
1 996  LEU n 
1 997  TYR n 
1 998  ILE n 
1 999  ASN n 
1 1000 ARG n 
1 1001 ASN n 
1 1002 ILE n 
1 1003 ILE n 
1 1004 GLY n 
1 1005 ALA n 
1 1006 VAL n 
1 1007 VAL n 
1 1008 GLY n 
1 1009 VAL n 
1 1010 GLN n 
1 1011 PRO n 
1 1012 PHE n 
1 1013 GLY n 
1 1014 GLY n 
1 1015 ARG n 
1 1016 GLY n 
1 1017 LEU n 
1 1018 SER n 
1 1019 GLY n 
1 1020 THR n 
1 1021 GLY n 
1 1022 PRO n 
1 1023 LYS n 
1 1024 ALA n 
1 1025 GLY n 
1 1026 GLY n 
1 1027 PRO n 
1 1028 LEU n 
1 1029 TYR n 
1 1030 LEU n 
1 1031 GLY n 
1 1032 ARG n 
1 1033 LEU n 
1 1034 VAL n 
1 1035 THR n 
1 1036 THR n 
1 1037 ALA n 
1 1038 PRO n 
1 1039 VAL n 
1 1040 PRO n 
1 1041 PRO n 
1 1042 GLN n 
1 1043 HIS n 
1 1044 SER n 
1 1045 SER n 
1 1046 VAL n 
1 1047 HIS n 
1 1048 THR n 
1 1049 ASP n 
1 1050 PRO n 
1 1051 VAL n 
1 1052 LEU n 
1 1053 LEU n 
1 1054 ASP n 
1 1055 PHE n 
1 1056 ALA n 
1 1057 LYS n 
1 1058 TRP n 
1 1059 LEU n 
1 1060 ASP n 
1 1061 GLY n 
1 1062 LYS n 
1 1063 GLY n 
1 1064 ALA n 
1 1065 ARG n 
1 1066 ALA n 
1 1067 GLU n 
1 1068 ALA n 
1 1069 GLU n 
1 1070 ALA n 
1 1071 ALA n 
1 1072 ARG n 
1 1073 ASN n 
1 1074 ALA n 
1 1075 GLY n 
1 1076 SER n 
1 1077 SER n 
1 1078 SER n 
1 1079 ALA n 
1 1080 LEU n 
1 1081 GLY n 
1 1082 LEU n 
1 1083 ASP n 
1 1084 LEU n 
1 1085 GLU n 
1 1086 LEU n 
1 1087 PRO n 
1 1088 GLY n 
1 1089 PRO n 
1 1090 VAL n 
1 1091 GLY n 
1 1092 GLU n 
1 1093 ARG n 
1 1094 ASN n 
1 1095 LEU n 
1 1096 TYR n 
1 1097 THR n 
1 1098 LEU n 
1 1099 HIS n 
1 1100 ALA n 
1 1101 ARG n 
1 1102 GLY n 
1 1103 ARG n 
1 1104 ILE n 
1 1105 LEU n 
1 1106 LEU n 
1 1107 VAL n 
1 1108 PRO n 
1 1109 ALA n 
1 1110 THR n 
1 1111 GLU n 
1 1112 SER n 
1 1113 GLY n 
1 1114 LEU n 
1 1115 TYR n 
1 1116 HIS n 
1 1117 GLN n 
1 1118 LEU n 
1 1119 ALA n 
1 1120 ALA n 
1 1121 ALA n 
1 1122 LEU n 
1 1123 ALA n 
1 1124 THR n 
1 1125 GLY n 
1 1126 ASN n 
1 1127 SER n 
1 1128 VAL n 
1 1129 ALA n 
1 1130 ILE n 
1 1131 ASP n 
1 1132 ALA n 
1 1133 ALA n 
1 1134 SER n 
1 1135 GLY n 
1 1136 LEU n 
1 1137 GLN n 
1 1138 ALA n 
1 1139 SER n 
1 1140 LEU n 
1 1141 LYS n 
1 1142 ASN n 
1 1143 LEU n 
1 1144 PRO n 
1 1145 GLN n 
1 1146 THR n 
1 1147 VAL n 
1 1148 GLY n 
1 1149 LEU n 
1 1150 ARG n 
1 1151 VAL n 
1 1152 SER n 
1 1153 TRP n 
1 1154 SER n 
1 1155 LYS n 
1 1156 ASP n 
1 1157 TRP n 
1 1158 ALA n 
1 1159 ALA n 
1 1160 ASP n 
1 1161 GLY n 
1 1162 PRO n 
1 1163 PHE n 
1 1164 ALA n 
1 1165 GLY n 
1 1166 ALA n 
1 1167 LEU n 
1 1168 VAL n 
1 1169 GLU n 
1 1170 GLY n 
1 1171 ASP n 
1 1172 ALA n 
1 1173 GLU n 
1 1174 ARG n 
1 1175 ILE n 
1 1176 ARG n 
1 1177 ALA n 
1 1178 VAL n 
1 1179 ASN n 
1 1180 LYS n 
1 1181 ALA n 
1 1182 ILE n 
1 1183 ALA n 
1 1184 ALA n 
1 1185 LEU n 
1 1186 PRO n 
1 1187 GLY n 
1 1188 PRO n 
1 1189 LEU n 
1 1190 LEU n 
1 1191 LEU n 
1 1192 VAL n 
1 1193 GLN n 
1 1194 ALA n 
1 1195 ALA n 
1 1196 SER n 
1 1197 SER n 
1 1198 GLY n 
1 1199 GLU n 
1 1200 ILE n 
1 1201 ALA n 
1 1202 ARG n 
1 1203 ASN n 
1 1204 PRO n 
1 1205 ASP n 
1 1206 ALA n 
1 1207 TYR n 
1 1208 CYS n 
1 1209 LEU n 
1 1210 ASN n 
1 1211 TRP n 
1 1212 LEU n 
1 1213 VAL n 
1 1214 GLU n 
1 1215 GLU n 
1 1216 VAL n 
1 1217 SER n 
1 1218 ALA n 
1 1219 SER n 
1 1220 ILE n 
1 1221 ASN n 
1 1222 THR n 
1 1223 ALA n 
1 1224 ALA n 
1 1225 ALA n 
1 1226 GLY n 
1 1227 GLY n 
1 1228 ASN n 
1 1229 ALA n 
1 1230 SER n 
1 1231 LEU n 
1 1232 MET n 
1 1233 ALA n 
1 1234 ILE n 
1 1235 GLY n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   1235 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'putA, SM11_chr0102' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    SM11 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Sinorhizobium meliloti' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     707241 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
53E non-polymer         . '2,3-dihydro-1,4-benzodioxine-5-carboxylic acid' ? 'C9 H8 O4'          180.157 
ALA 'L-peptide linking' y ALANINE                                          ? 'C3 H7 N O2'        89.093  
ARG 'L-peptide linking' y ARGININE                                         ? 'C6 H15 N4 O2 1'    175.209 
ASN 'L-peptide linking' y ASPARAGINE                                       ? 'C4 H8 N2 O3'       132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                  ? 'C4 H7 N O4'        133.103 
CYS 'L-peptide linking' y CYSTEINE                                         ? 'C3 H7 N O2 S'      121.158 
FAD non-polymer         . 'FLAVIN-ADENINE DINUCLEOTIDE'                    ? 'C27 H33 N9 O15 P2' 785.550 
FMT non-polymer         . 'FORMIC ACID'                                    ? 'C H2 O2'           46.025  
GLN 'L-peptide linking' y GLUTAMINE                                        ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                  ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                                          ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                                        ? 'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                                            ? 'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                       ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                                          ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                                           ? 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                                       ? 'C5 H11 N O2 S'     149.211 
MG  non-polymer         . 'MAGNESIUM ION'                                  ? 'Mg 2'              24.305  
NAD non-polymer         . NICOTINAMIDE-ADENINE-DINUCLEOTIDE                ? 'C21 H27 N7 O14 P2' 663.425 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER'                          ? 'C4 H10 O3'         106.120 
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   79   HIS HIS A . n 
A 1 82   SER 82   80   ?    ?   ?   A . n 
A 1 83   GLY 83   81   ?    ?   ?   A . n 
A 1 84   SER 84   82   82   SER SER A . n 
A 1 85   GLY 85   83   83   GLY GLY A . n 
A 1 86   VAL 86   84   84   VAL VAL A . n 
A 1 87   GLU 87   85   85   GLU GLU A . n 
A 1 88   GLY 88   86   86   GLY GLY A . n 
A 1 89   LEU 89   87   87   LEU LEU A . n 
A 1 90   VAL 90   88   88   VAL VAL A . n 
A 1 91   GLN 91   89   89   GLN GLN A . n 
A 1 92   GLU 92   90   90   GLU GLU A . n 
A 1 93   TYR 93   91   91   TYR TYR A . n 
A 1 94   SER 94   92   92   SER SER A . n 
A 1 95   LEU 95   93   93   LEU LEU A . n 
A 1 96   SER 96   94   94   SER SER A . n 
A 1 97   SER 97   95   95   SER SER A . n 
A 1 98   GLN 98   96   96   GLN GLN A . n 
A 1 99   GLU 99   97   97   GLU GLU A . n 
A 1 100  GLY 100  98   98   GLY GLY A . n 
A 1 101  VAL 101  99   99   VAL VAL A . n 
A 1 102  ALA 102  100  100  ALA ALA A . n 
A 1 103  LEU 103  101  101  LEU LEU A . n 
A 1 104  MET 104  102  102  MET MET A . n 
A 1 105  CYS 105  103  103  CYS CYS A . n 
A 1 106  LEU 106  104  104  LEU LEU A . n 
A 1 107  ALA 107  105  105  ALA ALA A . n 
A 1 108  GLU 108  106  106  GLU GLU A . n 
A 1 109  ALA 109  107  107  ALA ALA A . n 
A 1 110  LEU 110  108  108  LEU LEU A . n 
A 1 111  LEU 111  109  109  LEU LEU A . n 
A 1 112  ARG 112  110  110  ARG ARG A . n 
A 1 113  ILE 113  111  111  ILE ILE A . n 
A 1 114  PRO 114  112  112  PRO PRO A . n 
A 1 115  ASP 115  113  113  ASP ASP A . n 
A 1 116  THR 116  114  114  THR THR A . n 
A 1 117  ALA 117  115  115  ALA ALA A . n 
A 1 118  THR 118  116  116  THR THR A . n 
A 1 119  ARG 119  117  117  ARG ARG A . n 
A 1 120  ASP 120  118  118  ASP ASP A . n 
A 1 121  ALA 121  119  119  ALA ALA A . n 
A 1 122  LEU 122  120  120  LEU LEU A . n 
A 1 123  ILE 123  121  121  ILE ILE A . n 
A 1 124  ARG 124  122  122  ARG ARG A . n 
A 1 125  ASP 125  123  123  ASP ASP A . n 
A 1 126  LYS 126  124  124  LYS LYS A . n 
A 1 127  ILE 127  125  125  ILE ILE A . n 
A 1 128  ALA 128  126  126  ALA ALA A . n 
A 1 129  ASP 129  127  127  ASP ASP A . n 
A 1 130  GLY 130  128  128  GLY GLY A . n 
A 1 131  ASN 131  129  129  ASN ASN A . n 
A 1 132  TRP 132  130  130  TRP TRP A . n 
A 1 133  LYS 133  131  131  LYS LYS A . n 
A 1 134  SER 134  132  132  SER SER A . n 
A 1 135  HIS 135  133  133  HIS HIS A . n 
A 1 136  LEU 136  134  134  LEU LEU A . n 
A 1 137  GLY 137  135  ?    ?   ?   A . n 
A 1 138  GLY 138  136  ?    ?   ?   A . n 
A 1 139  SER 139  137  137  SER SER A . n 
A 1 140  ARG 140  138  138  ARG ARG A . n 
A 1 141  SER 141  139  139  SER SER A . n 
A 1 142  LEU 142  140  140  LEU LEU A . n 
A 1 143  PHE 143  141  141  PHE PHE A . n 
A 1 144  VAL 144  142  142  VAL VAL A . n 
A 1 145  ASN 145  143  143  ASN ASN A . n 
A 1 146  ALA 146  144  144  ALA ALA A . n 
A 1 147  ALA 147  145  145  ALA ALA A . n 
A 1 148  THR 148  146  146  THR THR A . n 
A 1 149  TRP 149  147  147  TRP TRP A . n 
A 1 150  GLY 150  148  148  GLY GLY A . n 
A 1 151  LEU 151  149  149  LEU LEU A . n 
A 1 152  VAL 152  150  150  VAL VAL A . n 
A 1 153  VAL 153  151  151  VAL VAL A . n 
A 1 154  THR 154  152  152  THR THR A . n 
A 1 155  GLY 155  153  153  GLY GLY A . n 
A 1 156  LYS 156  154  154  LYS LYS A . n 
A 1 157  LEU 157  155  155  LEU LEU A . n 
A 1 158  THR 158  156  156  THR THR A . n 
A 1 159  SER 159  157  157  SER SER A . n 
A 1 160  THR 160  158  158  THR THR A . n 
A 1 161  VAL 161  159  159  VAL VAL A . n 
A 1 162  ASN 162  160  160  ASN ASN A . n 
A 1 163  ASP 163  161  161  ASP ASP A . n 
A 1 164  ARG 164  162  162  ARG ARG A . n 
A 1 165  SER 165  163  163  SER SER A . n 
A 1 166  LEU 166  164  164  LEU LEU A . n 
A 1 167  ALA 167  165  165  ALA ALA A . n 
A 1 168  ALA 168  166  166  ALA ALA A . n 
A 1 169  ALA 169  167  167  ALA ALA A . n 
A 1 170  LEU 170  168  168  LEU LEU A . n 
A 1 171  THR 171  169  169  THR THR A . n 
A 1 172  ARG 172  170  170  ARG ARG A . n 
A 1 173  LEU 173  171  171  LEU LEU A . n 
A 1 174  ILE 174  172  172  ILE ILE A . n 
A 1 175  SER 175  173  173  SER SER A . n 
A 1 176  ARG 176  174  174  ARG ARG A . n 
A 1 177  CYS 177  175  175  CYS CYS A . n 
A 1 178  GLY 178  176  176  GLY GLY A . n 
A 1 179  GLU 179  177  177  GLU GLU A . n 
A 1 180  PRO 180  178  178  PRO PRO A . n 
A 1 181  VAL 181  179  179  VAL VAL A . n 
A 1 182  ILE 182  180  180  ILE ILE A . n 
A 1 183  ARG 183  181  181  ARG ARG A . n 
A 1 184  ARG 184  182  182  ARG ARG A . n 
A 1 185  GLY 185  183  183  GLY GLY A . n 
A 1 186  VAL 186  184  184  VAL VAL A . n 
A 1 187  ASP 187  185  185  ASP ASP A . n 
A 1 188  MET 188  186  186  MET MET A . n 
A 1 189  ALA 189  187  187  ALA ALA A . n 
A 1 190  MET 190  188  188  MET MET A . n 
A 1 191  ARG 191  189  189  ARG ARG A . n 
A 1 192  MET 192  190  190  MET MET A . n 
A 1 193  MET 193  191  191  MET MET A . n 
A 1 194  GLY 194  192  192  GLY GLY A . n 
A 1 195  GLU 195  193  193  GLU GLU A . n 
A 1 196  GLN 196  194  194  GLN GLN A . n 
A 1 197  PHE 197  195  195  PHE PHE A . n 
A 1 198  VAL 198  196  196  VAL VAL A . n 
A 1 199  THR 199  197  197  THR THR A . n 
A 1 200  GLY 200  198  198  GLY GLY A . n 
A 1 201  GLU 201  199  199  GLU GLU A . n 
A 1 202  THR 202  200  200  THR THR A . n 
A 1 203  ILE 203  201  201  ILE ILE A . n 
A 1 204  ARG 204  202  202  ARG ARG A . n 
A 1 205  GLU 205  203  203  GLU GLU A . n 
A 1 206  ALA 206  204  204  ALA ALA A . n 
A 1 207  LEU 207  205  205  LEU LEU A . n 
A 1 208  LYS 208  206  206  LYS LYS A . n 
A 1 209  ARG 209  207  207  ARG ARG A . n 
A 1 210  SER 210  208  208  SER SER A . n 
A 1 211  LYS 211  209  209  LYS LYS A . n 
A 1 212  GLU 212  210  210  GLU GLU A . n 
A 1 213  LEU 213  211  211  LEU LEU A . n 
A 1 214  GLU 214  212  212  GLU GLU A . n 
A 1 215  GLU 215  213  213  GLU GLU A . n 
A 1 216  LYS 216  214  214  LYS LYS A . n 
A 1 217  GLY 217  215  215  GLY GLY A . n 
A 1 218  PHE 218  216  216  PHE PHE A . n 
A 1 219  SER 219  217  217  SER SER A . n 
A 1 220  TYR 220  218  218  TYR TYR A . n 
A 1 221  SER 221  219  219  SER SER A . n 
A 1 222  TYR 222  220  220  TYR TYR A . n 
A 1 223  ASP 223  221  221  ASP ASP A . n 
A 1 224  MET 224  222  222  MET MET A . n 
A 1 225  LEU 225  223  223  LEU LEU A . n 
A 1 226  GLY 226  224  224  GLY GLY A . n 
A 1 227  GLU 227  225  225  GLU GLU A . n 
A 1 228  ALA 228  226  226  ALA ALA A . n 
A 1 229  ALA 229  227  227  ALA ALA A . n 
A 1 230  THR 230  228  228  THR THR A . n 
A 1 231  THR 231  229  229  THR THR A . n 
A 1 232  ALA 232  230  230  ALA ALA A . n 
A 1 233  ALA 233  231  231  ALA ALA A . n 
A 1 234  ASP 234  232  232  ASP ASP A . n 
A 1 235  ALA 235  233  233  ALA ALA A . n 
A 1 236  GLU 236  234  234  GLU GLU A . n 
A 1 237  ARG 237  235  235  ARG ARG A . n 
A 1 238  TYR 238  236  236  TYR TYR A . n 
A 1 239  TYR 239  237  237  TYR TYR A . n 
A 1 240  ARG 240  238  238  ARG ARG A . n 
A 1 241  ASP 241  239  239  ASP ASP A . n 
A 1 242  TYR 242  240  240  TYR TYR A . n 
A 1 243  GLU 243  241  241  GLU GLU A . n 
A 1 244  SER 244  242  242  SER SER A . n 
A 1 245  ALA 245  243  243  ALA ALA A . n 
A 1 246  ILE 246  244  244  ILE ILE A . n 
A 1 247  HIS 247  245  245  HIS HIS A . n 
A 1 248  ALA 248  246  246  ALA ALA A . n 
A 1 249  ILE 249  247  247  ILE ILE A . n 
A 1 250  GLY 250  248  248  GLY GLY A . n 
A 1 251  LYS 251  249  249  LYS LYS A . n 
A 1 252  ALA 252  250  250  ALA ALA A . n 
A 1 253  SER 253  251  251  SER SER A . n 
A 1 254  ALA 254  252  252  ALA ALA A . n 
A 1 255  GLY 255  253  253  GLY GLY A . n 
A 1 256  ARG 256  254  254  ARG ARG A . n 
A 1 257  GLY 257  255  255  GLY GLY A . n 
A 1 258  ILE 258  256  256  ILE ILE A . n 
A 1 259  TYR 259  257  257  TYR TYR A . n 
A 1 260  GLU 260  258  258  GLU GLU A . n 
A 1 261  GLY 261  259  259  GLY GLY A . n 
A 1 262  PRO 262  260  260  PRO PRO A . n 
A 1 263  GLY 263  261  261  GLY GLY A . n 
A 1 264  ILE 264  262  262  ILE ILE A . n 
A 1 265  SER 265  263  263  SER SER A . n 
A 1 266  ILE 266  264  264  ILE ILE A . n 
A 1 267  LYS 267  265  265  LYS LYS A . n 
A 1 268  LEU 268  266  266  LEU LEU A . n 
A 1 269  SER 269  267  267  SER SER A . n 
A 1 270  ALA 270  268  268  ALA ALA A . n 
A 1 271  LEU 271  269  269  LEU LEU A . n 
A 1 272  HIS 272  270  270  HIS HIS A . n 
A 1 273  PRO 273  271  271  PRO PRO A . n 
A 1 274  ARG 274  272  272  ARG ARG A . n 
A 1 275  TYR 275  273  273  TYR TYR A . n 
A 1 276  SER 276  274  274  SER SER A . n 
A 1 277  ARG 277  275  275  ARG ARG A . n 
A 1 278  ALA 278  276  276  ALA ALA A . n 
A 1 279  GLN 279  277  277  GLN GLN A . n 
A 1 280  ALA 280  278  278  ALA ALA A . n 
A 1 281  ALA 281  279  279  ALA ALA A . n 
A 1 282  ARG 282  280  280  ARG ARG A . n 
A 1 283  VAL 283  281  281  VAL VAL A . n 
A 1 284  MET 284  282  282  MET MET A . n 
A 1 285  GLY 285  283  283  GLY GLY A . n 
A 1 286  GLU 286  284  284  GLU GLU A . n 
A 1 287  LEU 287  285  285  LEU LEU A . n 
A 1 288  LEU 288  286  286  LEU LEU A . n 
A 1 289  PRO 289  287  287  PRO PRO A . n 
A 1 290  ARG 290  288  288  ARG ARG A . n 
A 1 291  VAL 291  289  289  VAL VAL A . n 
A 1 292  LYS 292  290  290  LYS LYS A . n 
A 1 293  ALA 293  291  291  ALA ALA A . n 
A 1 294  LEU 294  292  292  LEU LEU A . n 
A 1 295  ALA 295  293  293  ALA ALA A . n 
A 1 296  LEU 296  294  294  LEU LEU A . n 
A 1 297  LEU 297  295  295  LEU LEU A . n 
A 1 298  ALA 298  296  296  ALA ALA A . n 
A 1 299  LYS 299  297  297  LYS LYS A . n 
A 1 300  ASN 300  298  298  ASN ASN A . n 
A 1 301  TYR 301  299  299  TYR TYR A . n 
A 1 302  ASP 302  300  300  ASP ASP A . n 
A 1 303  ILE 303  301  301  ILE ILE A . n 
A 1 304  GLY 304  302  302  GLY GLY A . n 
A 1 305  LEU 305  303  303  LEU LEU A . n 
A 1 306  ASN 306  304  304  ASN ASN A . n 
A 1 307  ILE 307  305  305  ILE ILE A . n 
A 1 308  ASP 308  306  306  ASP ASP A . n 
A 1 309  ALA 309  307  307  ALA ALA A . n 
A 1 310  GLU 310  308  308  GLU GLU A . n 
A 1 311  GLU 311  309  309  GLU GLU A . n 
A 1 312  ALA 312  310  310  ALA ALA A . n 
A 1 313  ASP 313  311  311  ASP ASP A . n 
A 1 314  ARG 314  312  312  ARG ARG A . n 
A 1 315  LEU 315  313  313  LEU LEU A . n 
A 1 316  GLU 316  314  314  GLU GLU A . n 
A 1 317  LEU 317  315  315  LEU LEU A . n 
A 1 318  SER 318  316  316  SER SER A . n 
A 1 319  LEU 319  317  317  LEU LEU A . n 
A 1 320  ASP 320  318  318  ASP ASP A . n 
A 1 321  LEU 321  319  319  LEU LEU A . n 
A 1 322  LEU 322  320  320  LEU LEU A . n 
A 1 323  GLU 323  321  321  GLU GLU A . n 
A 1 324  VAL 324  322  322  VAL VAL A . n 
A 1 325  LEU 325  323  323  LEU LEU A . n 
A 1 326  CYS 326  324  324  CYS CYS A . n 
A 1 327  LEU 327  325  325  LEU LEU A . n 
A 1 328  ASP 328  326  326  ASP ASP A . n 
A 1 329  GLY 329  327  327  GLY GLY A . n 
A 1 330  ASP 330  328  328  ASP ASP A . n 
A 1 331  LEU 331  329  329  LEU LEU A . n 
A 1 332  SER 332  330  330  SER SER A . n 
A 1 333  GLY 333  331  331  GLY GLY A . n 
A 1 334  TRP 334  332  332  TRP TRP A . n 
A 1 335  ASN 335  333  333  ASN ASN A . n 
A 1 336  GLY 336  334  334  GLY GLY A . n 
A 1 337  MET 337  335  335  MET MET A . n 
A 1 338  GLY 338  336  336  GLY GLY A . n 
A 1 339  PHE 339  337  337  PHE PHE A . n 
A 1 340  VAL 340  338  338  VAL VAL A . n 
A 1 341  VAL 341  339  339  VAL VAL A . n 
A 1 342  GLN 342  340  340  GLN GLN A . n 
A 1 343  ALA 343  341  341  ALA ALA A . n 
A 1 344  TYR 344  342  342  TYR TYR A . n 
A 1 345  GLY 345  343  343  GLY GLY A . n 
A 1 346  LYS 346  344  344  LYS LYS A . n 
A 1 347  ARG 347  345  345  ARG ARG A . n 
A 1 348  CYS 348  346  346  CYS CYS A . n 
A 1 349  PRO 349  347  347  PRO PRO A . n 
A 1 350  PHE 350  348  348  PHE PHE A . n 
A 1 351  VAL 351  349  349  VAL VAL A . n 
A 1 352  LEU 352  350  350  LEU LEU A . n 
A 1 353  ASP 353  351  351  ASP ASP A . n 
A 1 354  PHE 354  352  352  PHE PHE A . n 
A 1 355  ILE 355  353  353  ILE ILE A . n 
A 1 356  ILE 356  354  354  ILE ILE A . n 
A 1 357  ASP 357  355  355  ASP ASP A . n 
A 1 358  LEU 358  356  356  LEU LEU A . n 
A 1 359  ALA 359  357  357  ALA ALA A . n 
A 1 360  ARG 360  358  358  ARG ARG A . n 
A 1 361  ARG 361  359  359  ARG ARG A . n 
A 1 362  SER 362  360  360  SER SER A . n 
A 1 363  GLY 363  361  361  GLY GLY A . n 
A 1 364  ARG 364  362  362  ARG ARG A . n 
A 1 365  ARG 365  363  363  ARG ARG A . n 
A 1 366  ILE 366  364  364  ILE ILE A . n 
A 1 367  MET 367  365  365  MET MET A . n 
A 1 368  VAL 368  366  366  VAL VAL A . n 
A 1 369  ARG 369  367  367  ARG ARG A . n 
A 1 370  LEU 370  368  368  LEU LEU A . n 
A 1 371  VAL 371  369  369  VAL VAL A . n 
A 1 372  LYS 372  370  370  LYS LYS A . n 
A 1 373  GLY 373  371  371  GLY GLY A . n 
A 1 374  ALA 374  372  372  ALA ALA A . n 
A 1 375  TYR 375  373  373  TYR TYR A . n 
A 1 376  TRP 376  374  374  TRP TRP A . n 
A 1 377  ASP 377  375  375  ASP ASP A . n 
A 1 378  ALA 378  376  376  ALA ALA A . n 
A 1 379  GLU 379  377  377  GLU GLU A . n 
A 1 380  ILE 380  378  378  ILE ILE A . n 
A 1 381  LYS 381  379  379  LYS LYS A . n 
A 1 382  ARG 382  380  380  ARG ARG A . n 
A 1 383  ALA 383  381  381  ALA ALA A . n 
A 1 384  GLN 384  382  382  GLN GLN A . n 
A 1 385  LEU 385  383  383  LEU LEU A . n 
A 1 386  ASP 386  384  384  ASP ASP A . n 
A 1 387  GLY 387  385  385  GLY GLY A . n 
A 1 388  LEU 388  386  386  LEU LEU A . n 
A 1 389  ALA 389  387  387  ALA ALA A . n 
A 1 390  ASP 390  388  388  ASP ASP A . n 
A 1 391  PHE 391  389  389  PHE PHE A . n 
A 1 392  PRO 392  390  390  PRO PRO A . n 
A 1 393  VAL 393  391  391  VAL VAL A . n 
A 1 394  PHE 394  392  392  PHE PHE A . n 
A 1 395  THR 395  393  393  THR THR A . n 
A 1 396  ARG 396  394  394  ARG ARG A . n 
A 1 397  LYS 397  395  395  LYS LYS A . n 
A 1 398  ILE 398  396  396  ILE ILE A . n 
A 1 399  HIS 399  397  397  HIS HIS A . n 
A 1 400  THR 400  398  398  THR THR A . n 
A 1 401  ASP 401  399  399  ASP ASP A . n 
A 1 402  VAL 402  400  400  VAL VAL A . n 
A 1 403  SER 403  401  401  SER SER A . n 
A 1 404  TYR 404  402  402  TYR TYR A . n 
A 1 405  ILE 405  403  403  ILE ILE A . n 
A 1 406  ALA 406  404  404  ALA ALA A . n 
A 1 407  CYS 407  405  405  CYS CYS A . n 
A 1 408  ALA 408  406  406  ALA ALA A . n 
A 1 409  ALA 409  407  407  ALA ALA A . n 
A 1 410  LYS 410  408  408  LYS LYS A . n 
A 1 411  LEU 411  409  409  LEU LEU A . n 
A 1 412  LEU 412  410  410  LEU LEU A . n 
A 1 413  ALA 413  411  411  ALA ALA A . n 
A 1 414  ALA 414  412  412  ALA ALA A . n 
A 1 415  THR 415  413  413  THR THR A . n 
A 1 416  ASP 416  414  414  ASP ASP A . n 
A 1 417  VAL 417  415  415  VAL VAL A . n 
A 1 418  VAL 418  416  416  VAL VAL A . n 
A 1 419  PHE 419  417  417  PHE PHE A . n 
A 1 420  PRO 420  418  418  PRO PRO A . n 
A 1 421  GLN 421  419  419  GLN GLN A . n 
A 1 422  PHE 422  420  420  PHE PHE A . n 
A 1 423  ALA 423  421  421  ALA ALA A . n 
A 1 424  THR 424  422  422  THR THR A . n 
A 1 425  HIS 425  423  423  HIS HIS A . n 
A 1 426  ASN 426  424  424  ASN ASN A . n 
A 1 427  ALA 427  425  425  ALA ALA A . n 
A 1 428  GLN 428  426  426  GLN GLN A . n 
A 1 429  THR 429  427  427  THR THR A . n 
A 1 430  LEU 430  428  428  LEU LEU A . n 
A 1 431  ALA 431  429  429  ALA ALA A . n 
A 1 432  ALA 432  430  430  ALA ALA A . n 
A 1 433  ILE 433  431  431  ILE ILE A . n 
A 1 434  TYR 434  432  432  TYR TYR A . n 
A 1 435  HIS 435  433  433  HIS HIS A . n 
A 1 436  MET 436  434  434  MET MET A . n 
A 1 437  ALA 437  435  435  ALA ALA A . n 
A 1 438  GLY 438  436  436  GLY GLY A . n 
A 1 439  LYS 439  437  437  LYS LYS A . n 
A 1 440  ASP 440  438  438  ASP ASP A . n 
A 1 441  PHE 441  439  439  PHE PHE A . n 
A 1 442  HIS 442  440  440  HIS HIS A . n 
A 1 443  VAL 443  441  441  VAL VAL A . n 
A 1 444  GLY 444  442  442  GLY GLY A . n 
A 1 445  LYS 445  443  443  LYS LYS A . n 
A 1 446  TYR 446  444  444  TYR TYR A . n 
A 1 447  GLU 447  445  445  GLU GLU A . n 
A 1 448  PHE 448  446  446  PHE PHE A . n 
A 1 449  GLN 449  447  447  GLN GLN A . n 
A 1 450  CYS 450  448  448  CYS CYS A . n 
A 1 451  LEU 451  449  449  LEU LEU A . n 
A 1 452  HIS 452  450  450  HIS HIS A . n 
A 1 453  GLY 453  451  451  GLY GLY A . n 
A 1 454  MET 454  452  452  MET MET A . n 
A 1 455  GLY 455  453  453  GLY GLY A . n 
A 1 456  GLU 456  454  454  GLU GLU A . n 
A 1 457  PRO 457  455  455  PRO PRO A . n 
A 1 458  LEU 458  456  456  LEU LEU A . n 
A 1 459  TYR 459  457  457  TYR TYR A . n 
A 1 460  GLU 460  458  458  GLU GLU A . n 
A 1 461  GLU 461  459  459  GLU GLU A . n 
A 1 462  VAL 462  460  460  VAL VAL A . n 
A 1 463  VAL 463  461  461  VAL VAL A . n 
A 1 464  GLY 464  462  462  GLY GLY A . n 
A 1 465  ARG 465  463  463  ARG ARG A . n 
A 1 466  GLY 466  464  464  GLY GLY A . n 
A 1 467  LYS 467  465  465  LYS LYS A . n 
A 1 468  LEU 468  466  466  LEU LEU A . n 
A 1 469  ASP 469  467  467  ASP ASP A . n 
A 1 470  ARG 470  468  468  ARG ARG A . n 
A 1 471  PRO 471  469  469  PRO PRO A . n 
A 1 472  CYS 472  470  470  CYS CYS A . n 
A 1 473  ARG 473  471  471  ARG ARG A . n 
A 1 474  ILE 474  472  472  ILE ILE A . n 
A 1 475  TYR 475  473  473  TYR TYR A . n 
A 1 476  ALA 476  474  474  ALA ALA A . n 
A 1 477  PRO 477  475  475  PRO PRO A . n 
A 1 478  VAL 478  476  476  VAL VAL A . n 
A 1 479  GLY 479  477  477  GLY GLY A . n 
A 1 480  THR 480  478  478  THR THR A . n 
A 1 481  HIS 481  479  479  HIS HIS A . n 
A 1 482  GLU 482  480  480  GLU GLU A . n 
A 1 483  THR 483  481  481  THR THR A . n 
A 1 484  LEU 484  482  482  LEU LEU A . n 
A 1 485  LEU 485  483  483  LEU LEU A . n 
A 1 486  ALA 486  484  484  ALA ALA A . n 
A 1 487  TYR 487  485  485  TYR TYR A . n 
A 1 488  LEU 488  486  486  LEU LEU A . n 
A 1 489  VAL 489  487  487  VAL VAL A . n 
A 1 490  ARG 490  488  488  ARG ARG A . n 
A 1 491  ARG 491  489  489  ARG ARG A . n 
A 1 492  LEU 492  490  490  LEU LEU A . n 
A 1 493  LEU 493  491  491  LEU LEU A . n 
A 1 494  GLU 494  492  492  GLU GLU A . n 
A 1 495  ASN 495  493  493  ASN ASN A . n 
A 1 496  GLY 496  494  494  GLY GLY A . n 
A 1 497  ALA 497  495  495  ALA ALA A . n 
A 1 498  ASN 498  496  496  ASN ASN A . n 
A 1 499  SER 499  497  497  SER SER A . n 
A 1 500  SER 500  498  498  SER SER A . n 
A 1 501  PHE 501  499  499  PHE PHE A . n 
A 1 502  VAL 502  500  500  VAL VAL A . n 
A 1 503  HIS 503  501  501  HIS HIS A . n 
A 1 504  ARG 504  502  502  ARG ARG A . n 
A 1 505  ILE 505  503  503  ILE ILE A . n 
A 1 506  ASN 506  504  504  ASN ASN A . n 
A 1 507  ASP 507  505  505  ASP ASP A . n 
A 1 508  PRO 508  506  506  PRO PRO A . n 
A 1 509  LYS 509  507  507  LYS LYS A . n 
A 1 510  VAL 510  508  508  VAL VAL A . n 
A 1 511  SER 511  509  509  SER SER A . n 
A 1 512  ILE 512  510  510  ILE ILE A . n 
A 1 513  ASP 513  511  511  ASP ASP A . n 
A 1 514  GLU 514  512  512  GLU GLU A . n 
A 1 515  LEU 515  513  513  LEU LEU A . n 
A 1 516  ILE 516  514  514  ILE ILE A . n 
A 1 517  ALA 517  515  515  ALA ALA A . n 
A 1 518  ASP 518  516  516  ASP ASP A . n 
A 1 519  PRO 519  517  517  PRO PRO A . n 
A 1 520  VAL 520  518  518  VAL VAL A . n 
A 1 521  GLU 521  519  519  GLU GLU A . n 
A 1 522  VAL 522  520  520  VAL VAL A . n 
A 1 523  VAL 523  521  521  VAL VAL A . n 
A 1 524  ARG 524  522  522  ARG ARG A . n 
A 1 525  ALA 525  523  523  ALA ALA A . n 
A 1 526  MET 526  524  524  MET MET A . n 
A 1 527  PRO 527  525  525  PRO PRO A . n 
A 1 528  VAL 528  526  526  VAL VAL A . n 
A 1 529  VAL 529  527  527  VAL VAL A . n 
A 1 530  GLY 530  528  528  GLY GLY A . n 
A 1 531  ALA 531  529  529  ALA ALA A . n 
A 1 532  LYS 532  530  530  LYS LYS A . n 
A 1 533  HIS 533  531  531  HIS HIS A . n 
A 1 534  ASP 534  532  532  ASP ASP A . n 
A 1 535  ARG 535  533  533  ARG ARG A . n 
A 1 536  ILE 536  534  534  ILE ILE A . n 
A 1 537  ALA 537  535  535  ALA ALA A . n 
A 1 538  LEU 538  536  536  LEU LEU A . n 
A 1 539  PRO 539  537  537  PRO PRO A . n 
A 1 540  ALA 540  538  538  ALA ALA A . n 
A 1 541  GLU 541  539  539  GLU GLU A . n 
A 1 542  LEU 542  540  540  LEU LEU A . n 
A 1 543  PHE 543  541  541  PHE PHE A . n 
A 1 544  GLY 544  542  542  GLY GLY A . n 
A 1 545  ASP 545  543  543  ASP ASP A . n 
A 1 546  ALA 546  544  544  ALA ALA A . n 
A 1 547  ARG 547  545  545  ARG ARG A . n 
A 1 548  THR 548  546  546  THR THR A . n 
A 1 549  ASN 549  547  547  ASN ASN A . n 
A 1 550  SER 550  548  548  SER SER A . n 
A 1 551  ALA 551  549  549  ALA ALA A . n 
A 1 552  GLY 552  550  550  GLY GLY A . n 
A 1 553  LEU 553  551  551  LEU LEU A . n 
A 1 554  ASP 554  552  552  ASP ASP A . n 
A 1 555  LEU 555  553  553  LEU LEU A . n 
A 1 556  SER 556  554  554  SER SER A . n 
A 1 557  ASN 557  555  555  ASN ASN A . n 
A 1 558  GLU 558  556  556  GLU GLU A . n 
A 1 559  GLU 559  557  557  GLU GLU A . n 
A 1 560  THR 560  558  558  THR THR A . n 
A 1 561  LEU 561  559  559  LEU LEU A . n 
A 1 562  ALA 562  560  560  ALA ALA A . n 
A 1 563  SER 563  561  561  SER SER A . n 
A 1 564  LEU 564  562  562  LEU LEU A . n 
A 1 565  THR 565  563  563  THR THR A . n 
A 1 566  GLU 566  564  564  GLU GLU A . n 
A 1 567  ALA 567  565  565  ALA ALA A . n 
A 1 568  LEU 568  566  566  LEU LEU A . n 
A 1 569  ARG 569  567  567  ARG ARG A . n 
A 1 570  GLU 570  568  568  GLU GLU A . n 
A 1 571  SER 571  569  569  SER SER A . n 
A 1 572  ALA 572  570  570  ALA ALA A . n 
A 1 573  ALA 573  571  571  ALA ALA A . n 
A 1 574  MET 574  572  572  MET MET A . n 
A 1 575  LYS 575  573  573  LYS LYS A . n 
A 1 576  TRP 576  574  574  TRP TRP A . n 
A 1 577  THR 577  575  575  THR THR A . n 
A 1 578  ALA 578  576  576  ALA ALA A . n 
A 1 579  LEU 579  577  577  LEU LEU A . n 
A 1 580  PRO 580  578  578  PRO PRO A . n 
A 1 581  GLN 581  579  579  GLN GLN A . n 
A 1 582  LEU 582  580  580  LEU LEU A . n 
A 1 583  ALA 583  581  581  ALA ALA A . n 
A 1 584  THR 584  582  582  THR THR A . n 
A 1 585  GLY 585  583  583  GLY GLY A . n 
A 1 586  PRO 586  584  584  PRO PRO A . n 
A 1 587  ALA 587  585  585  ALA ALA A . n 
A 1 588  ALA 588  586  586  ALA ALA A . n 
A 1 589  GLY 589  587  587  GLY GLY A . n 
A 1 590  GLU 590  588  588  GLU GLU A . n 
A 1 591  THR 591  589  589  THR THR A . n 
A 1 592  ARG 592  590  590  ARG ARG A . n 
A 1 593  THR 593  591  591  THR THR A . n 
A 1 594  VAL 594  592  592  VAL VAL A . n 
A 1 595  LEU 595  593  593  LEU LEU A . n 
A 1 596  ASN 596  594  594  ASN ASN A . n 
A 1 597  PRO 597  595  595  PRO PRO A . n 
A 1 598  GLY 598  596  596  GLY GLY A . n 
A 1 599  ASP 599  597  597  ASP ASP A . n 
A 1 600  HIS 600  598  598  HIS HIS A . n 
A 1 601  ARG 601  599  599  ARG ARG A . n 
A 1 602  ASP 602  600  600  ASP ASP A . n 
A 1 603  VAL 603  601  601  VAL VAL A . n 
A 1 604  VAL 604  602  602  VAL VAL A . n 
A 1 605  GLY 605  603  603  GLY GLY A . n 
A 1 606  SER 606  604  604  SER SER A . n 
A 1 607  VAL 607  605  605  VAL VAL A . n 
A 1 608  THR 608  606  606  THR THR A . n 
A 1 609  GLU 609  607  607  GLU GLU A . n 
A 1 610  THR 610  608  608  THR THR A . n 
A 1 611  SER 611  609  609  SER SER A . n 
A 1 612  GLU 612  610  610  GLU GLU A . n 
A 1 613  GLU 613  611  611  GLU GLU A . n 
A 1 614  ASP 614  612  612  ASP ASP A . n 
A 1 615  ALA 615  613  613  ALA ALA A . n 
A 1 616  ARG 616  614  614  ARG ARG A . n 
A 1 617  ARG 617  615  615  ARG ARG A . n 
A 1 618  ALA 618  616  616  ALA ALA A . n 
A 1 619  VAL 619  617  617  VAL VAL A . n 
A 1 620  ARG 620  618  618  ARG ARG A . n 
A 1 621  LEU 621  619  619  LEU LEU A . n 
A 1 622  ALA 622  620  620  ALA ALA A . n 
A 1 623  ALA 623  621  621  ALA ALA A . n 
A 1 624  ASP 624  622  622  ASP ASP A . n 
A 1 625  ALA 625  623  623  ALA ALA A . n 
A 1 626  ALA 626  624  624  ALA ALA A . n 
A 1 627  PRO 627  625  625  PRO PRO A . n 
A 1 628  ASP 628  626  626  ASP ASP A . n 
A 1 629  TRP 629  627  627  TRP TRP A . n 
A 1 630  ALA 630  628  628  ALA ALA A . n 
A 1 631  ALA 631  629  629  ALA ALA A . n 
A 1 632  VAL 632  630  630  VAL VAL A . n 
A 1 633  PRO 633  631  631  PRO PRO A . n 
A 1 634  PRO 634  632  632  PRO PRO A . n 
A 1 635  SER 635  633  633  SER SER A . n 
A 1 636  GLU 636  634  634  GLU GLU A . n 
A 1 637  ARG 637  635  635  ARG ARG A . n 
A 1 638  ALA 638  636  636  ALA ALA A . n 
A 1 639  ALA 639  637  637  ALA ALA A . n 
A 1 640  CYS 640  638  638  CYS CYS A . n 
A 1 641  LEU 641  639  639  LEU LEU A . n 
A 1 642  ASP 642  640  640  ASP ASP A . n 
A 1 643  ARG 643  641  641  ARG ARG A . n 
A 1 644  ALA 644  642  642  ALA ALA A . n 
A 1 645  ALA 645  643  643  ALA ALA A . n 
A 1 646  GLU 646  644  644  GLU GLU A . n 
A 1 647  LEU 647  645  645  LEU LEU A . n 
A 1 648  MET 648  646  646  MET MET A . n 
A 1 649  GLN 649  647  647  GLN GLN A . n 
A 1 650  ALA 650  648  648  ALA ALA A . n 
A 1 651  ARG 651  649  649  ARG ARG A . n 
A 1 652  MET 652  650  650  MET MET A . n 
A 1 653  PRO 653  651  651  PRO PRO A . n 
A 1 654  THR 654  652  652  THR THR A . n 
A 1 655  LEU 655  653  653  LEU LEU A . n 
A 1 656  LEU 656  654  654  LEU LEU A . n 
A 1 657  GLY 657  655  655  GLY GLY A . n 
A 1 658  LEU 658  656  656  LEU LEU A . n 
A 1 659  ILE 659  657  657  ILE ILE A . n 
A 1 660  ILE 660  658  658  ILE ILE A . n 
A 1 661  ARG 661  659  659  ARG ARG A . n 
A 1 662  GLU 662  660  660  GLU GLU A . n 
A 1 663  ALA 663  661  661  ALA ALA A . n 
A 1 664  GLY 664  662  662  GLY GLY A . n 
A 1 665  LYS 665  663  663  LYS LYS A . n 
A 1 666  SER 666  664  664  SER SER A . n 
A 1 667  ALA 667  665  665  ALA ALA A . n 
A 1 668  LEU 668  666  666  LEU LEU A . n 
A 1 669  ASN 669  667  667  ASN ASN A . n 
A 1 670  ALA 670  668  668  ALA ALA A . n 
A 1 671  ILE 671  669  669  ILE ILE A . n 
A 1 672  ALA 672  670  670  ALA ALA A . n 
A 1 673  GLU 673  671  671  GLU GLU A . n 
A 1 674  VAL 674  672  672  VAL VAL A . n 
A 1 675  ARG 675  673  673  ARG ARG A . n 
A 1 676  GLU 676  674  674  GLU GLU A . n 
A 1 677  ALA 677  675  675  ALA ALA A . n 
A 1 678  ILE 678  676  676  ILE ILE A . n 
A 1 679  ASP 679  677  677  ASP ASP A . n 
A 1 680  PHE 680  678  678  PHE PHE A . n 
A 1 681  LEU 681  679  679  LEU LEU A . n 
A 1 682  ARG 682  680  680  ARG ARG A . n 
A 1 683  TYR 683  681  681  TYR TYR A . n 
A 1 684  TYR 684  682  682  TYR TYR A . n 
A 1 685  ALA 685  683  683  ALA ALA A . n 
A 1 686  GLU 686  684  684  GLU GLU A . n 
A 1 687  GLN 687  685  685  GLN GLN A . n 
A 1 688  THR 688  686  686  THR THR A . n 
A 1 689  ARG 689  687  687  ARG ARG A . n 
A 1 690  ARG 690  688  688  ARG ARG A . n 
A 1 691  THR 691  689  689  THR THR A . n 
A 1 692  LEU 692  690  690  LEU LEU A . n 
A 1 693  GLY 693  691  691  GLY GLY A . n 
A 1 694  PRO 694  692  692  PRO PRO A . n 
A 1 695  GLY 695  693  693  GLY GLY A . n 
A 1 696  HIS 696  694  694  HIS HIS A . n 
A 1 697  GLY 697  695  695  GLY GLY A . n 
A 1 698  PRO 698  696  696  PRO PRO A . n 
A 1 699  LEU 699  697  697  LEU LEU A . n 
A 1 700  GLY 700  698  698  GLY GLY A . n 
A 1 701  PRO 701  699  699  PRO PRO A . n 
A 1 702  ILE 702  700  700  ILE ILE A . n 
A 1 703  VAL 703  701  701  VAL VAL A . n 
A 1 704  CYS 704  702  702  CYS CYS A . n 
A 1 705  ILE 705  703  703  ILE ILE A . n 
A 1 706  SER 706  704  704  SER SER A . n 
A 1 707  PRO 707  705  705  PRO PRO A . n 
A 1 708  TRP 708  706  706  TRP TRP A . n 
A 1 709  ASN 709  707  707  ASN ASN A . n 
A 1 710  PHE 710  708  708  PHE PHE A . n 
A 1 711  PRO 711  709  709  PRO PRO A . n 
A 1 712  LEU 712  710  710  LEU LEU A . n 
A 1 713  ALA 713  711  711  ALA ALA A . n 
A 1 714  ILE 714  712  712  ILE ILE A . n 
A 1 715  PHE 715  713  713  PHE PHE A . n 
A 1 716  THR 716  714  714  THR THR A . n 
A 1 717  GLY 717  715  715  GLY GLY A . n 
A 1 718  GLN 718  716  716  GLN GLN A . n 
A 1 719  ILE 719  717  717  ILE ILE A . n 
A 1 720  ALA 720  718  718  ALA ALA A . n 
A 1 721  ALA 721  719  719  ALA ALA A . n 
A 1 722  ALA 722  720  720  ALA ALA A . n 
A 1 723  LEU 723  721  721  LEU LEU A . n 
A 1 724  VAL 724  722  722  VAL VAL A . n 
A 1 725  ALA 725  723  723  ALA ALA A . n 
A 1 726  GLY 726  724  724  GLY GLY A . n 
A 1 727  ASN 727  725  725  ASN ASN A . n 
A 1 728  PRO 728  726  726  PRO PRO A . n 
A 1 729  VAL 729  727  727  VAL VAL A . n 
A 1 730  LEU 730  728  728  LEU LEU A . n 
A 1 731  ALA 731  729  729  ALA ALA A . n 
A 1 732  LYS 732  730  730  LYS LYS A . n 
A 1 733  PRO 733  731  731  PRO PRO A . n 
A 1 734  ALA 734  732  732  ALA ALA A . n 
A 1 735  GLU 735  733  733  GLU GLU A . n 
A 1 736  GLU 736  734  734  GLU GLU A . n 
A 1 737  THR 737  735  735  THR THR A . n 
A 1 738  PRO 738  736  736  PRO PRO A . n 
A 1 739  LEU 739  737  737  LEU LEU A . n 
A 1 740  ILE 740  738  738  ILE ILE A . n 
A 1 741  ALA 741  739  739  ALA ALA A . n 
A 1 742  ALA 742  740  740  ALA ALA A . n 
A 1 743  GLU 743  741  741  GLU GLU A . n 
A 1 744  GLY 744  742  742  GLY GLY A . n 
A 1 745  VAL 745  743  743  VAL VAL A . n 
A 1 746  ARG 746  744  744  ARG ARG A . n 
A 1 747  ILE 747  745  745  ILE ILE A . n 
A 1 748  LEU 748  746  746  LEU LEU A . n 
A 1 749  ARG 749  747  747  ARG ARG A . n 
A 1 750  GLU 750  748  748  GLU GLU A . n 
A 1 751  ALA 751  749  749  ALA ALA A . n 
A 1 752  GLY 752  750  750  GLY GLY A . n 
A 1 753  ILE 753  751  751  ILE ILE A . n 
A 1 754  PRO 754  752  752  PRO PRO A . n 
A 1 755  ALA 755  753  753  ALA ALA A . n 
A 1 756  SER 756  754  754  SER SER A . n 
A 1 757  ALA 757  755  755  ALA ALA A . n 
A 1 758  LEU 758  756  756  LEU LEU A . n 
A 1 759  GLN 759  757  757  GLN GLN A . n 
A 1 760  LEU 760  758  758  LEU LEU A . n 
A 1 761  LEU 761  759  759  LEU LEU A . n 
A 1 762  PRO 762  760  760  PRO PRO A . n 
A 1 763  GLY 763  761  761  GLY GLY A . n 
A 1 764  ASP 764  762  762  ASP ASP A . n 
A 1 765  GLY 765  763  763  GLY GLY A . n 
A 1 766  ARG 766  764  764  ARG ARG A . n 
A 1 767  VAL 767  765  765  VAL VAL A . n 
A 1 768  GLY 768  766  766  GLY GLY A . n 
A 1 769  ALA 769  767  767  ALA ALA A . n 
A 1 770  ALA 770  768  768  ALA ALA A . n 
A 1 771  LEU 771  769  769  LEU LEU A . n 
A 1 772  VAL 772  770  770  VAL VAL A . n 
A 1 773  ALA 773  771  771  ALA ALA A . n 
A 1 774  ALA 774  772  772  ALA ALA A . n 
A 1 775  ALA 775  773  773  ALA ALA A . n 
A 1 776  GLU 776  774  774  GLU GLU A . n 
A 1 777  THR 777  775  775  THR THR A . n 
A 1 778  ALA 778  776  776  ALA ALA A . n 
A 1 779  GLY 779  777  777  GLY GLY A . n 
A 1 780  VAL 780  778  778  VAL VAL A . n 
A 1 781  MET 781  779  779  MET MET A . n 
A 1 782  PHE 782  780  780  PHE PHE A . n 
A 1 783  THR 783  781  781  THR THR A . n 
A 1 784  GLY 784  782  782  GLY GLY A . n 
A 1 785  SER 785  783  783  SER SER A . n 
A 1 786  THR 786  784  784  THR THR A . n 
A 1 787  GLU 787  785  785  GLU GLU A . n 
A 1 788  VAL 788  786  786  VAL VAL A . n 
A 1 789  ALA 789  787  787  ALA ALA A . n 
A 1 790  ARG 790  788  788  ARG ARG A . n 
A 1 791  LEU 791  789  789  LEU LEU A . n 
A 1 792  ILE 792  790  790  ILE ILE A . n 
A 1 793  GLN 793  791  791  GLN GLN A . n 
A 1 794  ALA 794  792  792  ALA ALA A . n 
A 1 795  GLN 795  793  793  GLN GLN A . n 
A 1 796  LEU 796  794  794  LEU LEU A . n 
A 1 797  ALA 797  795  795  ALA ALA A . n 
A 1 798  ASP 798  796  796  ASP ASP A . n 
A 1 799  ARG 799  797  797  ARG ARG A . n 
A 1 800  LEU 800  798  798  LEU LEU A . n 
A 1 801  SER 801  799  799  SER SER A . n 
A 1 802  PRO 802  800  800  PRO PRO A . n 
A 1 803  ALA 803  801  801  ALA ALA A . n 
A 1 804  GLY 804  802  802  GLY GLY A . n 
A 1 805  ARG 805  803  803  ARG ARG A . n 
A 1 806  PRO 806  804  804  PRO PRO A . n 
A 1 807  ILE 807  805  805  ILE ILE A . n 
A 1 808  PRO 808  806  806  PRO PRO A . n 
A 1 809  LEU 809  807  807  LEU LEU A . n 
A 1 810  ILE 810  808  808  ILE ILE A . n 
A 1 811  ALA 811  809  809  ALA ALA A . n 
A 1 812  GLU 812  810  810  GLU GLU A . n 
A 1 813  THR 813  811  811  THR THR A . n 
A 1 814  GLY 814  812  812  GLY GLY A . n 
A 1 815  GLY 815  813  813  GLY GLY A . n 
A 1 816  GLN 816  814  814  GLN GLN A . n 
A 1 817  ASN 817  815  815  ASN ASN A . n 
A 1 818  ALA 818  816  816  ALA ALA A . n 
A 1 819  MET 819  817  817  MET MET A . n 
A 1 820  ILE 820  818  818  ILE ILE A . n 
A 1 821  VAL 821  819  819  VAL VAL A . n 
A 1 822  ASP 822  820  820  ASP ASP A . n 
A 1 823  SER 823  821  821  SER SER A . n 
A 1 824  SER 824  822  822  SER SER A . n 
A 1 825  ALA 825  823  823  ALA ALA A . n 
A 1 826  LEU 826  824  824  LEU LEU A . n 
A 1 827  ALA 827  825  825  ALA ALA A . n 
A 1 828  GLU 828  826  826  GLU GLU A . n 
A 1 829  GLN 829  827  827  GLN GLN A . n 
A 1 830  VAL 830  828  828  VAL VAL A . n 
A 1 831  VAL 831  829  829  VAL VAL A . n 
A 1 832  GLY 832  830  830  GLY GLY A . n 
A 1 833  ASP 833  831  831  ASP ASP A . n 
A 1 834  VAL 834  832  832  VAL VAL A . n 
A 1 835  ILE 835  833  833  ILE ILE A . n 
A 1 836  THR 836  834  834  THR THR A . n 
A 1 837  SER 837  835  835  SER SER A . n 
A 1 838  ALA 838  836  836  ALA ALA A . n 
A 1 839  PHE 839  837  837  PHE PHE A . n 
A 1 840  ASP 840  838  838  ASP ASP A . n 
A 1 841  SER 841  839  839  SER SER A . n 
A 1 842  ALA 842  840  840  ALA ALA A . n 
A 1 843  GLY 843  841  841  GLY GLY A . n 
A 1 844  GLN 844  842  842  GLN GLN A . n 
A 1 845  ARG 845  843  843  ARG ARG A . n 
A 1 846  CYS 846  844  844  CYS CYS A . n 
A 1 847  SER 847  845  845  SER SER A . n 
A 1 848  ALA 848  846  846  ALA ALA A . n 
A 1 849  LEU 849  847  847  LEU LEU A . n 
A 1 850  ARG 850  848  848  ARG ARG A . n 
A 1 851  VAL 851  849  849  VAL VAL A . n 
A 1 852  LEU 852  850  850  LEU LEU A . n 
A 1 853  CYS 853  851  851  CYS CYS A . n 
A 1 854  LEU 854  852  852  LEU LEU A . n 
A 1 855  GLN 855  853  853  GLN GLN A . n 
A 1 856  GLU 856  854  854  GLU GLU A . n 
A 1 857  ASP 857  855  855  ASP ASP A . n 
A 1 858  VAL 858  856  856  VAL VAL A . n 
A 1 859  ALA 859  857  857  ALA ALA A . n 
A 1 860  ASP 860  858  858  ASP ASP A . n 
A 1 861  ARG 861  859  859  ARG ARG A . n 
A 1 862  ILE 862  860  860  ILE ILE A . n 
A 1 863  LEU 863  861  861  LEU LEU A . n 
A 1 864  THR 864  862  862  THR THR A . n 
A 1 865  MET 865  863  863  MET MET A . n 
A 1 866  LEU 866  864  864  LEU LEU A . n 
A 1 867  LYS 867  865  865  LYS LYS A . n 
A 1 868  GLY 868  866  866  GLY GLY A . n 
A 1 869  ALA 869  867  867  ALA ALA A . n 
A 1 870  LEU 870  868  868  LEU LEU A . n 
A 1 871  HIS 871  869  869  HIS HIS A . n 
A 1 872  GLU 872  870  870  GLU GLU A . n 
A 1 873  LEU 873  871  871  LEU LEU A . n 
A 1 874  HIS 874  872  872  HIS HIS A . n 
A 1 875  ILE 875  873  873  ILE ILE A . n 
A 1 876  GLY 876  874  874  GLY GLY A . n 
A 1 877  ARG 877  875  875  ARG ARG A . n 
A 1 878  THR 878  876  876  THR THR A . n 
A 1 879  ASP 879  877  877  ASP ASP A . n 
A 1 880  ARG 880  878  878  ARG ARG A . n 
A 1 881  LEU 881  879  879  LEU LEU A . n 
A 1 882  SER 882  880  880  SER SER A . n 
A 1 883  VAL 883  881  881  VAL VAL A . n 
A 1 884  ASP 884  882  882  ASP ASP A . n 
A 1 885  VAL 885  883  883  VAL VAL A . n 
A 1 886  GLY 886  884  884  GLY GLY A . n 
A 1 887  PRO 887  885  885  PRO PRO A . n 
A 1 888  VAL 888  886  886  VAL VAL A . n 
A 1 889  ILE 889  887  887  ILE ILE A . n 
A 1 890  THR 890  888  888  THR THR A . n 
A 1 891  SER 891  889  889  SER SER A . n 
A 1 892  GLU 892  890  890  GLU GLU A . n 
A 1 893  ALA 893  891  891  ALA ALA A . n 
A 1 894  LYS 894  892  892  LYS LYS A . n 
A 1 895  ASP 895  893  893  ASP ASP A . n 
A 1 896  ASN 896  894  894  ASN ASN A . n 
A 1 897  ILE 897  895  895  ILE ILE A . n 
A 1 898  GLU 898  896  896  GLU GLU A . n 
A 1 899  LYS 899  897  897  LYS LYS A . n 
A 1 900  HIS 900  898  898  HIS HIS A . n 
A 1 901  ILE 901  899  899  ILE ILE A . n 
A 1 902  GLU 902  900  900  GLU GLU A . n 
A 1 903  ARG 903  901  901  ARG ARG A . n 
A 1 904  MET 904  902  902  MET MET A . n 
A 1 905  ARG 905  903  903  ARG ARG A . n 
A 1 906  GLY 906  904  904  GLY GLY A . n 
A 1 907  LEU 907  905  905  LEU LEU A . n 
A 1 908  GLY 908  906  906  GLY GLY A . n 
A 1 909  ARG 909  907  907  ARG ARG A . n 
A 1 910  LYS 910  908  908  LYS LYS A . n 
A 1 911  VAL 911  909  909  VAL VAL A . n 
A 1 912  GLU 912  910  910  GLU GLU A . n 
A 1 913  GLN 913  911  911  GLN GLN A . n 
A 1 914  ILE 914  912  912  ILE ILE A . n 
A 1 915  GLY 915  913  913  GLY GLY A . n 
A 1 916  LEU 916  914  914  LEU LEU A . n 
A 1 917  ALA 917  915  915  ALA ALA A . n 
A 1 918  SER 918  916  916  SER SER A . n 
A 1 919  GLU 919  917  917  GLU GLU A . n 
A 1 920  THR 920  918  918  THR THR A . n 
A 1 921  GLY 921  919  919  GLY GLY A . n 
A 1 922  VAL 922  920  920  VAL VAL A . n 
A 1 923  GLY 923  921  921  GLY GLY A . n 
A 1 924  THR 924  922  922  THR THR A . n 
A 1 925  PHE 925  923  923  PHE PHE A . n 
A 1 926  VAL 926  924  924  VAL VAL A . n 
A 1 927  PRO 927  925  925  PRO PRO A . n 
A 1 928  PRO 928  926  926  PRO PRO A . n 
A 1 929  THR 929  927  927  THR THR A . n 
A 1 930  ILE 930  928  928  ILE ILE A . n 
A 1 931  ILE 931  929  929  ILE ILE A . n 
A 1 932  GLU 932  930  930  GLU GLU A . n 
A 1 933  LEU 933  931  931  LEU LEU A . n 
A 1 934  GLU 934  932  932  GLU GLU A . n 
A 1 935  LYS 935  933  933  LYS LYS A . n 
A 1 936  LEU 936  934  934  LEU LEU A . n 
A 1 937  SER 937  935  935  SER SER A . n 
A 1 938  ASP 938  936  936  ASP ASP A . n 
A 1 939  LEU 939  937  937  LEU LEU A . n 
A 1 940  GLN 940  938  938  GLN GLN A . n 
A 1 941  ARG 941  939  939  ARG ARG A . n 
A 1 942  GLU 942  940  940  GLU GLU A . n 
A 1 943  VAL 943  941  941  VAL VAL A . n 
A 1 944  PHE 944  942  942  PHE PHE A . n 
A 1 945  GLY 945  943  943  GLY GLY A . n 
A 1 946  PRO 946  944  944  PRO PRO A . n 
A 1 947  VAL 947  945  945  VAL VAL A . n 
A 1 948  LEU 948  946  946  LEU LEU A . n 
A 1 949  HIS 949  947  947  HIS HIS A . n 
A 1 950  VAL 950  948  948  VAL VAL A . n 
A 1 951  ILE 951  949  949  ILE ILE A . n 
A 1 952  ARG 952  950  950  ARG ARG A . n 
A 1 953  TYR 953  951  951  TYR TYR A . n 
A 1 954  ARG 954  952  952  ARG ARG A . n 
A 1 955  ARG 955  953  953  ARG ARG A . n 
A 1 956  ASP 956  954  954  ASP ASP A . n 
A 1 957  ASP 957  955  955  ASP ASP A . n 
A 1 958  LEU 958  956  956  LEU LEU A . n 
A 1 959  ASP 959  957  957  ASP ASP A . n 
A 1 960  ARG 960  958  958  ARG ARG A . n 
A 1 961  LEU 961  959  959  LEU LEU A . n 
A 1 962  VAL 962  960  960  VAL VAL A . n 
A 1 963  ASP 963  961  961  ASP ASP A . n 
A 1 964  ASP 964  962  962  ASP ASP A . n 
A 1 965  VAL 965  963  963  VAL VAL A . n 
A 1 966  ASN 966  964  964  ASN ASN A . n 
A 1 967  ALA 967  965  965  ALA ALA A . n 
A 1 968  THR 968  966  966  THR THR A . n 
A 1 969  GLY 969  967  967  GLY GLY A . n 
A 1 970  TYR 970  968  968  TYR TYR A . n 
A 1 971  GLY 971  969  969  GLY GLY A . n 
A 1 972  LEU 972  970  970  LEU LEU A . n 
A 1 973  THR 973  971  971  THR THR A . n 
A 1 974  PHE 974  972  972  PHE PHE A . n 
A 1 975  GLY 975  973  973  GLY GLY A . n 
A 1 976  LEU 976  974  974  LEU LEU A . n 
A 1 977  HIS 977  975  975  HIS HIS A . n 
A 1 978  THR 978  976  976  THR THR A . n 
A 1 979  ARG 979  977  977  ARG ARG A . n 
A 1 980  LEU 980  978  978  LEU LEU A . n 
A 1 981  ASP 981  979  979  ASP ASP A . n 
A 1 982  GLU 982  980  980  GLU GLU A . n 
A 1 983  THR 983  981  981  THR THR A . n 
A 1 984  ILE 984  982  982  ILE ILE A . n 
A 1 985  ALA 985  983  983  ALA ALA A . n 
A 1 986  HIS 986  984  984  HIS HIS A . n 
A 1 987  VAL 987  985  985  VAL VAL A . n 
A 1 988  THR 988  986  986  THR THR A . n 
A 1 989  SER 989  987  987  SER SER A . n 
A 1 990  ARG 990  988  988  ARG ARG A . n 
A 1 991  ILE 991  989  989  ILE ILE A . n 
A 1 992  LYS 992  990  990  LYS LYS A . n 
A 1 993  ALA 993  991  991  ALA ALA A . n 
A 1 994  GLY 994  992  992  GLY GLY A . n 
A 1 995  ASN 995  993  993  ASN ASN A . n 
A 1 996  LEU 996  994  994  LEU LEU A . n 
A 1 997  TYR 997  995  995  TYR TYR A . n 
A 1 998  ILE 998  996  996  ILE ILE A . n 
A 1 999  ASN 999  997  997  ASN ASN A . n 
A 1 1000 ARG 1000 998  998  ARG ARG A . n 
A 1 1001 ASN 1001 999  999  ASN ASN A . n 
A 1 1002 ILE 1002 1000 1000 ILE ILE A . n 
A 1 1003 ILE 1003 1001 1001 ILE ILE A . n 
A 1 1004 GLY 1004 1002 1002 GLY GLY A . n 
A 1 1005 ALA 1005 1003 1003 ALA ALA A . n 
A 1 1006 VAL 1006 1004 1004 VAL VAL A . n 
A 1 1007 VAL 1007 1005 1005 VAL VAL A . n 
A 1 1008 GLY 1008 1006 1006 GLY GLY A . n 
A 1 1009 VAL 1009 1007 1007 VAL VAL A . n 
A 1 1010 GLN 1010 1008 1008 GLN GLN A . n 
A 1 1011 PRO 1011 1009 1009 PRO PRO A . n 
A 1 1012 PHE 1012 1010 1010 PHE PHE A . n 
A 1 1013 GLY 1013 1011 1011 GLY GLY A . n 
A 1 1014 GLY 1014 1012 1012 GLY GLY A . n 
A 1 1015 ARG 1015 1013 1013 ARG ARG A . n 
A 1 1016 GLY 1016 1014 1014 GLY GLY A . n 
A 1 1017 LEU 1017 1015 1015 LEU LEU A . n 
A 1 1018 SER 1018 1016 1016 SER SER A . n 
A 1 1019 GLY 1019 1017 1017 GLY GLY A . n 
A 1 1020 THR 1020 1018 1018 THR THR A . n 
A 1 1021 GLY 1021 1019 1019 GLY GLY A . n 
A 1 1022 PRO 1022 1020 1020 PRO PRO A . n 
A 1 1023 LYS 1023 1021 1021 LYS LYS A . n 
A 1 1024 ALA 1024 1022 1022 ALA ALA A . n 
A 1 1025 GLY 1025 1023 1023 GLY GLY A . n 
A 1 1026 GLY 1026 1024 1024 GLY GLY A . n 
A 1 1027 PRO 1027 1025 1025 PRO PRO A . n 
A 1 1028 LEU 1028 1026 1026 LEU LEU A . n 
A 1 1029 TYR 1029 1027 1027 TYR TYR A . n 
A 1 1030 LEU 1030 1028 1028 LEU LEU A . n 
A 1 1031 GLY 1031 1029 1029 GLY GLY A . n 
A 1 1032 ARG 1032 1030 1030 ARG ARG A . n 
A 1 1033 LEU 1033 1031 1031 LEU LEU A . n 
A 1 1034 VAL 1034 1032 1032 VAL VAL A . n 
A 1 1035 THR 1035 1033 1033 THR THR A . n 
A 1 1036 THR 1036 1034 1034 THR THR A . n 
A 1 1037 ALA 1037 1035 1035 ALA ALA A . n 
A 1 1038 PRO 1038 1036 1036 PRO PRO A . n 
A 1 1039 VAL 1039 1037 1037 VAL VAL A . n 
A 1 1040 PRO 1040 1038 1038 PRO PRO A . n 
A 1 1041 PRO 1041 1039 1039 PRO PRO A . n 
A 1 1042 GLN 1042 1040 1040 GLN GLN A . n 
A 1 1043 HIS 1043 1041 1041 HIS HIS A . n 
A 1 1044 SER 1044 1042 1042 SER SER A . n 
A 1 1045 SER 1045 1043 1043 SER SER A . n 
A 1 1046 VAL 1046 1044 1044 VAL VAL A . n 
A 1 1047 HIS 1047 1045 1045 HIS HIS A . n 
A 1 1048 THR 1048 1046 1046 THR THR A . n 
A 1 1049 ASP 1049 1047 1047 ASP ASP A . n 
A 1 1050 PRO 1050 1048 1048 PRO PRO A . n 
A 1 1051 VAL 1051 1049 1049 VAL VAL A . n 
A 1 1052 LEU 1052 1050 1050 LEU LEU A . n 
A 1 1053 LEU 1053 1051 1051 LEU LEU A . n 
A 1 1054 ASP 1054 1052 1052 ASP ASP A . n 
A 1 1055 PHE 1055 1053 1053 PHE PHE A . n 
A 1 1056 ALA 1056 1054 1054 ALA ALA A . n 
A 1 1057 LYS 1057 1055 1055 LYS LYS A . n 
A 1 1058 TRP 1058 1056 1056 TRP TRP A . n 
A 1 1059 LEU 1059 1057 1057 LEU LEU A . n 
A 1 1060 ASP 1060 1058 1058 ASP ASP A . n 
A 1 1061 GLY 1061 1059 1059 GLY GLY A . n 
A 1 1062 LYS 1062 1060 1060 LYS LYS A . n 
A 1 1063 GLY 1063 1061 1061 GLY GLY A . n 
A 1 1064 ALA 1064 1062 1062 ALA ALA A . n 
A 1 1065 ARG 1065 1063 1063 ARG ARG A . n 
A 1 1066 ALA 1066 1064 1064 ALA ALA A . n 
A 1 1067 GLU 1067 1065 1065 GLU GLU A . n 
A 1 1068 ALA 1068 1066 1066 ALA ALA A . n 
A 1 1069 GLU 1069 1067 1067 GLU GLU A . n 
A 1 1070 ALA 1070 1068 1068 ALA ALA A . n 
A 1 1071 ALA 1071 1069 1069 ALA ALA A . n 
A 1 1072 ARG 1072 1070 1070 ARG ARG A . n 
A 1 1073 ASN 1073 1071 1071 ASN ASN A . n 
A 1 1074 ALA 1074 1072 1072 ALA ALA A . n 
A 1 1075 GLY 1075 1073 1073 GLY GLY A . n 
A 1 1076 SER 1076 1074 1074 SER SER A . n 
A 1 1077 SER 1077 1075 1075 SER SER A . n 
A 1 1078 SER 1078 1076 1076 SER SER A . n 
A 1 1079 ALA 1079 1077 1077 ALA ALA A . n 
A 1 1080 LEU 1080 1078 1078 LEU LEU A . n 
A 1 1081 GLY 1081 1079 1079 GLY GLY A . n 
A 1 1082 LEU 1082 1080 1080 LEU LEU A . n 
A 1 1083 ASP 1083 1081 1081 ASP ASP A . n 
A 1 1084 LEU 1084 1082 1082 LEU LEU A . n 
A 1 1085 GLU 1085 1083 1083 GLU GLU A . n 
A 1 1086 LEU 1086 1084 1084 LEU LEU A . n 
A 1 1087 PRO 1087 1085 1085 PRO PRO A . n 
A 1 1088 GLY 1088 1086 1086 GLY GLY A . n 
A 1 1089 PRO 1089 1087 1087 PRO PRO A . n 
A 1 1090 VAL 1090 1088 1088 VAL VAL A . n 
A 1 1091 GLY 1091 1089 1089 GLY GLY A . n 
A 1 1092 GLU 1092 1090 1090 GLU GLU A . n 
A 1 1093 ARG 1093 1091 1091 ARG ARG A . n 
A 1 1094 ASN 1094 1092 1092 ASN ASN A . n 
A 1 1095 LEU 1095 1093 1093 LEU LEU A . n 
A 1 1096 TYR 1096 1094 1094 TYR TYR A . n 
A 1 1097 THR 1097 1095 1095 THR THR A . n 
A 1 1098 LEU 1098 1096 1096 LEU LEU A . n 
A 1 1099 HIS 1099 1097 1097 HIS HIS A . n 
A 1 1100 ALA 1100 1098 1098 ALA ALA A . n 
A 1 1101 ARG 1101 1099 1099 ARG ARG A . n 
A 1 1102 GLY 1102 1100 1100 GLY GLY A . n 
A 1 1103 ARG 1103 1101 1101 ARG ARG A . n 
A 1 1104 ILE 1104 1102 1102 ILE ILE A . n 
A 1 1105 LEU 1105 1103 1103 LEU LEU A . n 
A 1 1106 LEU 1106 1104 1104 LEU LEU A . n 
A 1 1107 VAL 1107 1105 1105 VAL VAL A . n 
A 1 1108 PRO 1108 1106 1106 PRO PRO A . n 
A 1 1109 ALA 1109 1107 1107 ALA ALA A . n 
A 1 1110 THR 1110 1108 1108 THR THR A . n 
A 1 1111 GLU 1111 1109 1109 GLU GLU A . n 
A 1 1112 SER 1112 1110 1110 SER SER A . n 
A 1 1113 GLY 1113 1111 1111 GLY GLY A . n 
A 1 1114 LEU 1114 1112 1112 LEU LEU A . n 
A 1 1115 TYR 1115 1113 1113 TYR TYR A . n 
A 1 1116 HIS 1116 1114 1114 HIS HIS A . n 
A 1 1117 GLN 1117 1115 1115 GLN GLN A . n 
A 1 1118 LEU 1118 1116 1116 LEU LEU A . n 
A 1 1119 ALA 1119 1117 1117 ALA ALA A . n 
A 1 1120 ALA 1120 1118 1118 ALA ALA A . n 
A 1 1121 ALA 1121 1119 1119 ALA ALA A . n 
A 1 1122 LEU 1122 1120 1120 LEU LEU A . n 
A 1 1123 ALA 1123 1121 1121 ALA ALA A . n 
A 1 1124 THR 1124 1122 1122 THR THR A . n 
A 1 1125 GLY 1125 1123 1123 GLY GLY A . n 
A 1 1126 ASN 1126 1124 1124 ASN ASN A . n 
A 1 1127 SER 1127 1125 1125 SER SER A . n 
A 1 1128 VAL 1128 1126 1126 VAL VAL A . n 
A 1 1129 ALA 1129 1127 1127 ALA ALA A . n 
A 1 1130 ILE 1130 1128 1128 ILE ILE A . n 
A 1 1131 ASP 1131 1129 1129 ASP ASP A . n 
A 1 1132 ALA 1132 1130 1130 ALA ALA A . n 
A 1 1133 ALA 1133 1131 1131 ALA ALA A . n 
A 1 1134 SER 1134 1132 1132 SER SER A . n 
A 1 1135 GLY 1135 1133 1133 GLY GLY A . n 
A 1 1136 LEU 1136 1134 1134 LEU LEU A . n 
A 1 1137 GLN 1137 1135 1135 GLN GLN A . n 
A 1 1138 ALA 1138 1136 1136 ALA ALA A . n 
A 1 1139 SER 1139 1137 1137 SER SER A . n 
A 1 1140 LEU 1140 1138 1138 LEU LEU A . n 
A 1 1141 LYS 1141 1139 1139 LYS LYS A . n 
A 1 1142 ASN 1142 1140 1140 ASN ASN A . n 
A 1 1143 LEU 1143 1141 1141 LEU LEU A . n 
A 1 1144 PRO 1144 1142 1142 PRO PRO A . n 
A 1 1145 GLN 1145 1143 1143 GLN GLN A . n 
A 1 1146 THR 1146 1144 1144 THR THR A . n 
A 1 1147 VAL 1147 1145 1145 VAL VAL A . n 
A 1 1148 GLY 1148 1146 1146 GLY GLY A . n 
A 1 1149 LEU 1149 1147 1147 LEU LEU A . n 
A 1 1150 ARG 1150 1148 1148 ARG ARG A . n 
A 1 1151 VAL 1151 1149 1149 VAL VAL A . n 
A 1 1152 SER 1152 1150 1150 SER SER A . n 
A 1 1153 TRP 1153 1151 1151 TRP TRP A . n 
A 1 1154 SER 1154 1152 1152 SER SER A . n 
A 1 1155 LYS 1155 1153 1153 LYS LYS A . n 
A 1 1156 ASP 1156 1154 1154 ASP ASP A . n 
A 1 1157 TRP 1157 1155 1155 TRP TRP A . n 
A 1 1158 ALA 1158 1156 1156 ALA ALA A . n 
A 1 1159 ALA 1159 1157 1157 ALA ALA A . n 
A 1 1160 ASP 1160 1158 1158 ASP ASP A . n 
A 1 1161 GLY 1161 1159 1159 GLY GLY A . n 
A 1 1162 PRO 1162 1160 1160 PRO PRO A . n 
A 1 1163 PHE 1163 1161 1161 PHE PHE A . n 
A 1 1164 ALA 1164 1162 1162 ALA ALA A . n 
A 1 1165 GLY 1165 1163 1163 GLY GLY A . n 
A 1 1166 ALA 1166 1164 1164 ALA ALA A . n 
A 1 1167 LEU 1167 1165 1165 LEU LEU A . n 
A 1 1168 VAL 1168 1166 1166 VAL VAL A . n 
A 1 1169 GLU 1169 1167 1167 GLU GLU A . n 
A 1 1170 GLY 1170 1168 1168 GLY GLY A . n 
A 1 1171 ASP 1171 1169 1169 ASP ASP A . n 
A 1 1172 ALA 1172 1170 1170 ALA ALA A . n 
A 1 1173 GLU 1173 1171 1171 GLU GLU A . n 
A 1 1174 ARG 1174 1172 1172 ARG ARG A . n 
A 1 1175 ILE 1175 1173 1173 ILE ILE A . n 
A 1 1176 ARG 1176 1174 1174 ARG ARG A . n 
A 1 1177 ALA 1177 1175 1175 ALA ALA A . n 
A 1 1178 VAL 1178 1176 1176 VAL VAL A . n 
A 1 1179 ASN 1179 1177 1177 ASN ASN A . n 
A 1 1180 LYS 1180 1178 1178 LYS LYS A . n 
A 1 1181 ALA 1181 1179 1179 ALA ALA A . n 
A 1 1182 ILE 1182 1180 1180 ILE ILE A . n 
A 1 1183 ALA 1183 1181 1181 ALA ALA A . n 
A 1 1184 ALA 1184 1182 1182 ALA ALA A . n 
A 1 1185 LEU 1185 1183 1183 LEU LEU A . n 
A 1 1186 PRO 1186 1184 1184 PRO PRO A . n 
A 1 1187 GLY 1187 1185 1185 GLY GLY A . n 
A 1 1188 PRO 1188 1186 1186 PRO PRO A . n 
A 1 1189 LEU 1189 1187 1187 LEU LEU A . n 
A 1 1190 LEU 1190 1188 1188 LEU LEU A . n 
A 1 1191 LEU 1191 1189 1189 LEU LEU A . n 
A 1 1192 VAL 1192 1190 1190 VAL VAL A . n 
A 1 1193 GLN 1193 1191 1191 GLN GLN A . n 
A 1 1194 ALA 1194 1192 1192 ALA ALA A . n 
A 1 1195 ALA 1195 1193 1193 ALA ALA A . n 
A 1 1196 SER 1196 1194 1194 SER SER A . n 
A 1 1197 SER 1197 1195 1195 SER SER A . n 
A 1 1198 GLY 1198 1196 1196 GLY GLY A . n 
A 1 1199 GLU 1199 1197 1197 GLU GLU A . n 
A 1 1200 ILE 1200 1198 1198 ILE ILE A . n 
A 1 1201 ALA 1201 1199 1199 ALA ALA A . n 
A 1 1202 ARG 1202 1200 1200 ARG ARG A . n 
A 1 1203 ASN 1203 1201 1201 ASN ASN A . n 
A 1 1204 PRO 1204 1202 1202 PRO PRO A . n 
A 1 1205 ASP 1205 1203 1203 ASP ASP A . n 
A 1 1206 ALA 1206 1204 1204 ALA ALA A . n 
A 1 1207 TYR 1207 1205 1205 TYR TYR A . n 
A 1 1208 CYS 1208 1206 1206 CYS CYS A . n 
A 1 1209 LEU 1209 1207 1207 LEU LEU A . n 
A 1 1210 ASN 1210 1208 1208 ASN ASN A . n 
A 1 1211 TRP 1211 1209 1209 TRP TRP A . n 
A 1 1212 LEU 1212 1210 1210 LEU LEU A . n 
A 1 1213 VAL 1213 1211 1211 VAL VAL A . n 
A 1 1214 GLU 1214 1212 1212 GLU GLU A . n 
A 1 1215 GLU 1215 1213 1213 GLU GLU A . n 
A 1 1216 VAL 1216 1214 1214 VAL VAL A . n 
A 1 1217 SER 1217 1215 1215 SER SER A . n 
A 1 1218 ALA 1218 1216 1216 ALA ALA A . n 
A 1 1219 SER 1219 1217 1217 SER SER A . n 
A 1 1220 ILE 1220 1218 1218 ILE ILE A . n 
A 1 1221 ASN 1221 1219 1219 ASN ASN A . n 
A 1 1222 THR 1222 1220 1220 THR THR A . n 
A 1 1223 ALA 1223 1221 1221 ALA ALA A . n 
A 1 1224 ALA 1224 1222 1222 ALA ALA A . n 
A 1 1225 ALA 1225 1223 1223 ALA ALA A . n 
A 1 1226 GLY 1226 1224 1224 GLY GLY A . n 
A 1 1227 GLY 1227 1225 1225 GLY GLY A . n 
A 1 1228 ASN 1228 1226 1226 ASN ASN A . n 
A 1 1229 ALA 1229 1227 1227 ALA ALA A . n 
A 1 1230 SER 1230 1228 1228 SER SER A . n 
A 1 1231 LEU 1231 1229 1229 LEU LEU A . n 
A 1 1232 MET 1232 1230 1230 MET MET A . n 
A 1 1233 ALA 1233 1231 1231 ALA ALA A . n 
A 1 1234 ILE 1234 1232 1232 ILE ILE A . n 
A 1 1235 GLY 1235 1233 1233 GLY GLY A . n 
B 1 1    SER 1    -1   ?    ?   ?   B . n 
B 1 2    MET 2    0    ?    ?   ?   B . n 
B 1 3    MET 3    1    ?    ?   ?   B . n 
B 1 4    SER 4    2    ?    ?   ?   B . n 
B 1 5    PRO 5    3    ?    ?   ?   B . n 
B 1 6    ASN 6    4    ?    ?   ?   B . n 
B 1 7    PRO 7    5    ?    ?   ?   B . n 
B 1 8    LEU 8    6    ?    ?   ?   B . n 
B 1 9    GLN 9    7    ?    ?   ?   B . n 
B 1 10   LYS 10   8    ?    ?   ?   B . n 
B 1 11   PRO 11   9    ?    ?   ?   B . n 
B 1 12   ALA 12   10   ?    ?   ?   B . n 
B 1 13   ILE 13   11   ?    ?   ?   B . n 
B 1 14   ASP 14   12   ?    ?   ?   B . n 
B 1 15   ALA 15   13   ?    ?   ?   B . n 
B 1 16   ALA 16   14   14   ALA ALA B . n 
B 1 17   PRO 17   15   15   PRO PRO B . n 
B 1 18   ALA 18   16   16   ALA ALA B . n 
B 1 19   PRO 19   17   17   PRO PRO B . n 
B 1 20   PHE 20   18   18   PHE PHE B . n 
B 1 21   ALA 21   19   19   ALA ALA B . n 
B 1 22   ASP 22   20   20   ASP ASP B . n 
B 1 23   PHE 23   21   21   PHE PHE B . n 
B 1 24   ALA 24   22   22   ALA ALA B . n 
B 1 25   PRO 25   23   23   PRO PRO B . n 
B 1 26   PRO 26   24   24   PRO PRO B . n 
B 1 27   VAL 27   25   25   VAL VAL B . n 
B 1 28   ARG 28   26   26   ARG ARG B . n 
B 1 29   PRO 29   27   27   PRO PRO B . n 
B 1 30   GLN 30   28   28   GLN GLN B . n 
B 1 31   SER 31   29   29   SER SER B . n 
B 1 32   THR 32   30   30   THR THR B . n 
B 1 33   LEU 33   31   31   LEU LEU B . n 
B 1 34   ARG 34   32   32   ARG ARG B . n 
B 1 35   ARG 35   33   33   ARG ARG B . n 
B 1 36   ALA 36   34   34   ALA ALA B . n 
B 1 37   ILE 37   35   35   ILE ILE B . n 
B 1 38   THR 38   36   36   THR THR B . n 
B 1 39   ALA 39   37   37   ALA ALA B . n 
B 1 40   ALA 40   38   38   ALA ALA B . n 
B 1 41   TYR 41   39   39   TYR TYR B . n 
B 1 42   ARG 42   40   40   ARG ARG B . n 
B 1 43   ARG 43   41   41   ARG ARG B . n 
B 1 44   PRO 44   42   42   PRO PRO B . n 
B 1 45   GLU 45   43   43   GLU GLU B . n 
B 1 46   THR 46   44   44   THR THR B . n 
B 1 47   GLU 47   45   45   GLU GLU B . n 
B 1 48   CYS 48   46   46   CYS CYS B . n 
B 1 49   LEU 49   47   47   LEU LEU B . n 
B 1 50   PRO 50   48   48   PRO PRO B . n 
B 1 51   PRO 51   49   49   PRO PRO B . n 
B 1 52   LEU 52   50   50   LEU LEU B . n 
B 1 53   VAL 53   51   51   VAL VAL B . n 
B 1 54   GLU 54   52   52   GLU GLU B . n 
B 1 55   ALA 55   53   53   ALA ALA B . n 
B 1 56   ALA 56   54   54   ALA ALA B . n 
B 1 57   THR 57   55   55   THR THR B . n 
B 1 58   GLN 58   56   56   GLN GLN B . n 
B 1 59   SER 59   57   57   SER SER B . n 
B 1 60   LYS 60   58   58   LYS LYS B . n 
B 1 61   GLU 61   59   59   GLU GLU B . n 
B 1 62   ILE 62   60   60   ILE ILE B . n 
B 1 63   ARG 63   61   61   ARG ARG B . n 
B 1 64   ASP 64   62   62   ASP ASP B . n 
B 1 65   ALA 65   63   63   ALA ALA B . n 
B 1 66   ALA 66   64   64   ALA ALA B . n 
B 1 67   ALA 67   65   65   ALA ALA B . n 
B 1 68   SER 68   66   66   SER SER B . n 
B 1 69   THR 69   67   67   THR THR B . n 
B 1 70   ALA 70   68   68   ALA ALA B . n 
B 1 71   ARG 71   69   69   ARG ARG B . n 
B 1 72   LYS 72   70   70   LYS LYS B . n 
B 1 73   LEU 73   71   71   LEU LEU B . n 
B 1 74   ILE 74   72   72   ILE ILE B . n 
B 1 75   GLU 75   73   73   GLU GLU B . n 
B 1 76   ALA 76   74   74   ALA ALA B . n 
B 1 77   LEU 77   75   75   LEU LEU B . n 
B 1 78   ARG 78   76   76   ARG ARG B . n 
B 1 79   GLY 79   77   77   GLY GLY B . n 
B 1 80   LYS 80   78   78   LYS LYS B . n 
B 1 81   HIS 81   79   ?    ?   ?   B . n 
B 1 82   SER 82   80   ?    ?   ?   B . n 
B 1 83   GLY 83   81   ?    ?   ?   B . n 
B 1 84   SER 84   82   82   SER SER B . n 
B 1 85   GLY 85   83   83   GLY GLY B . n 
B 1 86   VAL 86   84   84   VAL VAL B . n 
B 1 87   GLU 87   85   85   GLU GLU B . n 
B 1 88   GLY 88   86   86   GLY GLY B . n 
B 1 89   LEU 89   87   87   LEU LEU B . n 
B 1 90   VAL 90   88   88   VAL VAL B . n 
B 1 91   GLN 91   89   89   GLN GLN B . n 
B 1 92   GLU 92   90   90   GLU GLU B . n 
B 1 93   TYR 93   91   91   TYR TYR B . n 
B 1 94   SER 94   92   92   SER SER B . n 
B 1 95   LEU 95   93   93   LEU LEU B . n 
B 1 96   SER 96   94   94   SER SER B . n 
B 1 97   SER 97   95   95   SER SER B . n 
B 1 98   GLN 98   96   96   GLN GLN B . n 
B 1 99   GLU 99   97   97   GLU GLU B . n 
B 1 100  GLY 100  98   98   GLY GLY B . n 
B 1 101  VAL 101  99   99   VAL VAL B . n 
B 1 102  ALA 102  100  100  ALA ALA B . n 
B 1 103  LEU 103  101  101  LEU LEU B . n 
B 1 104  MET 104  102  102  MET MET B . n 
B 1 105  CYS 105  103  103  CYS CYS B . n 
B 1 106  LEU 106  104  104  LEU LEU B . n 
B 1 107  ALA 107  105  105  ALA ALA B . n 
B 1 108  GLU 108  106  106  GLU GLU B . n 
B 1 109  ALA 109  107  107  ALA ALA B . n 
B 1 110  LEU 110  108  108  LEU LEU B . n 
B 1 111  LEU 111  109  109  LEU LEU B . n 
B 1 112  ARG 112  110  110  ARG ARG B . n 
B 1 113  ILE 113  111  111  ILE ILE B . n 
B 1 114  PRO 114  112  112  PRO PRO B . n 
B 1 115  ASP 115  113  113  ASP ASP B . n 
B 1 116  THR 116  114  114  THR THR B . n 
B 1 117  ALA 117  115  115  ALA ALA B . n 
B 1 118  THR 118  116  116  THR THR B . n 
B 1 119  ARG 119  117  117  ARG ARG B . n 
B 1 120  ASP 120  118  118  ASP ASP B . n 
B 1 121  ALA 121  119  119  ALA ALA B . n 
B 1 122  LEU 122  120  120  LEU LEU B . n 
B 1 123  ILE 123  121  121  ILE ILE B . n 
B 1 124  ARG 124  122  122  ARG ARG B . n 
B 1 125  ASP 125  123  123  ASP ASP B . n 
B 1 126  LYS 126  124  124  LYS LYS B . n 
B 1 127  ILE 127  125  125  ILE ILE B . n 
B 1 128  ALA 128  126  126  ALA ALA B . n 
B 1 129  ASP 129  127  127  ASP ASP B . n 
B 1 130  GLY 130  128  128  GLY GLY B . n 
B 1 131  ASN 131  129  129  ASN ASN B . n 
B 1 132  TRP 132  130  130  TRP TRP B . n 
B 1 133  LYS 133  131  131  LYS LYS B . n 
B 1 134  SER 134  132  132  SER SER B . n 
B 1 135  HIS 135  133  133  HIS HIS B . n 
B 1 136  LEU 136  134  134  LEU LEU B . n 
B 1 137  GLY 137  135  ?    ?   ?   B . n 
B 1 138  GLY 138  136  ?    ?   ?   B . n 
B 1 139  SER 139  137  ?    ?   ?   B . n 
B 1 140  ARG 140  138  138  ARG ARG B . n 
B 1 141  SER 141  139  139  SER SER B . n 
B 1 142  LEU 142  140  140  LEU LEU B . n 
B 1 143  PHE 143  141  141  PHE PHE B . n 
B 1 144  VAL 144  142  142  VAL VAL B . n 
B 1 145  ASN 145  143  143  ASN ASN B . n 
B 1 146  ALA 146  144  144  ALA ALA B . n 
B 1 147  ALA 147  145  145  ALA ALA B . n 
B 1 148  THR 148  146  146  THR THR B . n 
B 1 149  TRP 149  147  147  TRP TRP B . n 
B 1 150  GLY 150  148  148  GLY GLY B . n 
B 1 151  LEU 151  149  149  LEU LEU B . n 
B 1 152  VAL 152  150  150  VAL VAL B . n 
B 1 153  VAL 153  151  151  VAL VAL B . n 
B 1 154  THR 154  152  152  THR THR B . n 
B 1 155  GLY 155  153  153  GLY GLY B . n 
B 1 156  LYS 156  154  154  LYS LYS B . n 
B 1 157  LEU 157  155  155  LEU LEU B . n 
B 1 158  THR 158  156  156  THR THR B . n 
B 1 159  SER 159  157  157  SER SER B . n 
B 1 160  THR 160  158  158  THR THR B . n 
B 1 161  VAL 161  159  159  VAL VAL B . n 
B 1 162  ASN 162  160  160  ASN ASN B . n 
B 1 163  ASP 163  161  161  ASP ASP B . n 
B 1 164  ARG 164  162  162  ARG ARG B . n 
B 1 165  SER 165  163  163  SER SER B . n 
B 1 166  LEU 166  164  164  LEU LEU B . n 
B 1 167  ALA 167  165  165  ALA ALA B . n 
B 1 168  ALA 168  166  166  ALA ALA B . n 
B 1 169  ALA 169  167  167  ALA ALA B . n 
B 1 170  LEU 170  168  168  LEU LEU B . n 
B 1 171  THR 171  169  169  THR THR B . n 
B 1 172  ARG 172  170  170  ARG ARG B . n 
B 1 173  LEU 173  171  171  LEU LEU B . n 
B 1 174  ILE 174  172  172  ILE ILE B . n 
B 1 175  SER 175  173  173  SER SER B . n 
B 1 176  ARG 176  174  174  ARG ARG B . n 
B 1 177  CYS 177  175  175  CYS CYS B . n 
B 1 178  GLY 178  176  176  GLY GLY B . n 
B 1 179  GLU 179  177  177  GLU GLU B . n 
B 1 180  PRO 180  178  178  PRO PRO B . n 
B 1 181  VAL 181  179  179  VAL VAL B . n 
B 1 182  ILE 182  180  180  ILE ILE B . n 
B 1 183  ARG 183  181  181  ARG ARG B . n 
B 1 184  ARG 184  182  182  ARG ARG B . n 
B 1 185  GLY 185  183  183  GLY GLY B . n 
B 1 186  VAL 186  184  184  VAL VAL B . n 
B 1 187  ASP 187  185  185  ASP ASP B . n 
B 1 188  MET 188  186  186  MET MET B . n 
B 1 189  ALA 189  187  187  ALA ALA B . n 
B 1 190  MET 190  188  188  MET MET B . n 
B 1 191  ARG 191  189  189  ARG ARG B . n 
B 1 192  MET 192  190  190  MET MET B . n 
B 1 193  MET 193  191  191  MET MET B . n 
B 1 194  GLY 194  192  192  GLY GLY B . n 
B 1 195  GLU 195  193  193  GLU GLU B . n 
B 1 196  GLN 196  194  194  GLN GLN B . n 
B 1 197  PHE 197  195  195  PHE PHE B . n 
B 1 198  VAL 198  196  196  VAL VAL B . n 
B 1 199  THR 199  197  197  THR THR B . n 
B 1 200  GLY 200  198  198  GLY GLY B . n 
B 1 201  GLU 201  199  199  GLU GLU B . n 
B 1 202  THR 202  200  200  THR THR B . n 
B 1 203  ILE 203  201  201  ILE ILE B . n 
B 1 204  ARG 204  202  202  ARG ARG B . n 
B 1 205  GLU 205  203  203  GLU GLU B . n 
B 1 206  ALA 206  204  204  ALA ALA B . n 
B 1 207  LEU 207  205  205  LEU LEU B . n 
B 1 208  LYS 208  206  206  LYS LYS B . n 
B 1 209  ARG 209  207  207  ARG ARG B . n 
B 1 210  SER 210  208  208  SER SER B . n 
B 1 211  LYS 211  209  209  LYS LYS B . n 
B 1 212  GLU 212  210  210  GLU GLU B . n 
B 1 213  LEU 213  211  211  LEU LEU B . n 
B 1 214  GLU 214  212  212  GLU GLU B . n 
B 1 215  GLU 215  213  213  GLU GLU B . n 
B 1 216  LYS 216  214  214  LYS LYS B . n 
B 1 217  GLY 217  215  215  GLY GLY B . n 
B 1 218  PHE 218  216  216  PHE PHE B . n 
B 1 219  SER 219  217  217  SER SER B . n 
B 1 220  TYR 220  218  218  TYR TYR B . n 
B 1 221  SER 221  219  219  SER SER B . n 
B 1 222  TYR 222  220  220  TYR TYR B . n 
B 1 223  ASP 223  221  221  ASP ASP B . n 
B 1 224  MET 224  222  222  MET MET B . n 
B 1 225  LEU 225  223  223  LEU LEU B . n 
B 1 226  GLY 226  224  224  GLY GLY B . n 
B 1 227  GLU 227  225  225  GLU GLU B . n 
B 1 228  ALA 228  226  226  ALA ALA B . n 
B 1 229  ALA 229  227  227  ALA ALA B . n 
B 1 230  THR 230  228  228  THR THR B . n 
B 1 231  THR 231  229  229  THR THR B . n 
B 1 232  ALA 232  230  230  ALA ALA B . n 
B 1 233  ALA 233  231  231  ALA ALA B . n 
B 1 234  ASP 234  232  232  ASP ASP B . n 
B 1 235  ALA 235  233  233  ALA ALA B . n 
B 1 236  GLU 236  234  234  GLU GLU B . n 
B 1 237  ARG 237  235  235  ARG ARG B . n 
B 1 238  TYR 238  236  236  TYR TYR B . n 
B 1 239  TYR 239  237  237  TYR TYR B . n 
B 1 240  ARG 240  238  238  ARG ARG B . n 
B 1 241  ASP 241  239  239  ASP ASP B . n 
B 1 242  TYR 242  240  240  TYR TYR B . n 
B 1 243  GLU 243  241  241  GLU GLU B . n 
B 1 244  SER 244  242  242  SER SER B . n 
B 1 245  ALA 245  243  243  ALA ALA B . n 
B 1 246  ILE 246  244  244  ILE ILE B . n 
B 1 247  HIS 247  245  245  HIS HIS B . n 
B 1 248  ALA 248  246  246  ALA ALA B . n 
B 1 249  ILE 249  247  247  ILE ILE B . n 
B 1 250  GLY 250  248  248  GLY GLY B . n 
B 1 251  LYS 251  249  249  LYS LYS B . n 
B 1 252  ALA 252  250  250  ALA ALA B . n 
B 1 253  SER 253  251  251  SER SER B . n 
B 1 254  ALA 254  252  252  ALA ALA B . n 
B 1 255  GLY 255  253  253  GLY GLY B . n 
B 1 256  ARG 256  254  254  ARG ARG B . n 
B 1 257  GLY 257  255  255  GLY GLY B . n 
B 1 258  ILE 258  256  256  ILE ILE B . n 
B 1 259  TYR 259  257  257  TYR TYR B . n 
B 1 260  GLU 260  258  258  GLU GLU B . n 
B 1 261  GLY 261  259  259  GLY GLY B . n 
B 1 262  PRO 262  260  260  PRO PRO B . n 
B 1 263  GLY 263  261  261  GLY GLY B . n 
B 1 264  ILE 264  262  262  ILE ILE B . n 
B 1 265  SER 265  263  263  SER SER B . n 
B 1 266  ILE 266  264  264  ILE ILE B . n 
B 1 267  LYS 267  265  265  LYS LYS B . n 
B 1 268  LEU 268  266  266  LEU LEU B . n 
B 1 269  SER 269  267  267  SER SER B . n 
B 1 270  ALA 270  268  268  ALA ALA B . n 
B 1 271  LEU 271  269  269  LEU LEU B . n 
B 1 272  HIS 272  270  270  HIS HIS B . n 
B 1 273  PRO 273  271  271  PRO PRO B . n 
B 1 274  ARG 274  272  272  ARG ARG B . n 
B 1 275  TYR 275  273  273  TYR TYR B . n 
B 1 276  SER 276  274  274  SER SER B . n 
B 1 277  ARG 277  275  275  ARG ARG B . n 
B 1 278  ALA 278  276  276  ALA ALA B . n 
B 1 279  GLN 279  277  277  GLN GLN B . n 
B 1 280  ALA 280  278  278  ALA ALA B . n 
B 1 281  ALA 281  279  279  ALA ALA B . n 
B 1 282  ARG 282  280  280  ARG ARG B . n 
B 1 283  VAL 283  281  281  VAL VAL B . n 
B 1 284  MET 284  282  282  MET MET B . n 
B 1 285  GLY 285  283  283  GLY GLY B . n 
B 1 286  GLU 286  284  284  GLU GLU B . n 
B 1 287  LEU 287  285  285  LEU LEU B . n 
B 1 288  LEU 288  286  286  LEU LEU B . n 
B 1 289  PRO 289  287  287  PRO PRO B . n 
B 1 290  ARG 290  288  288  ARG ARG B . n 
B 1 291  VAL 291  289  289  VAL VAL B . n 
B 1 292  LYS 292  290  290  LYS LYS B . n 
B 1 293  ALA 293  291  291  ALA ALA B . n 
B 1 294  LEU 294  292  292  LEU LEU B . n 
B 1 295  ALA 295  293  293  ALA ALA B . n 
B 1 296  LEU 296  294  294  LEU LEU B . n 
B 1 297  LEU 297  295  295  LEU LEU B . n 
B 1 298  ALA 298  296  296  ALA ALA B . n 
B 1 299  LYS 299  297  297  LYS LYS B . n 
B 1 300  ASN 300  298  298  ASN ASN B . n 
B 1 301  TYR 301  299  299  TYR TYR B . n 
B 1 302  ASP 302  300  300  ASP ASP B . n 
B 1 303  ILE 303  301  301  ILE ILE B . n 
B 1 304  GLY 304  302  302  GLY GLY B . n 
B 1 305  LEU 305  303  303  LEU LEU B . n 
B 1 306  ASN 306  304  304  ASN ASN B . n 
B 1 307  ILE 307  305  305  ILE ILE B . n 
B 1 308  ASP 308  306  306  ASP ASP B . n 
B 1 309  ALA 309  307  307  ALA ALA B . n 
B 1 310  GLU 310  308  308  GLU GLU B . n 
B 1 311  GLU 311  309  309  GLU GLU B . n 
B 1 312  ALA 312  310  310  ALA ALA B . n 
B 1 313  ASP 313  311  311  ASP ASP B . n 
B 1 314  ARG 314  312  312  ARG ARG B . n 
B 1 315  LEU 315  313  313  LEU LEU B . n 
B 1 316  GLU 316  314  314  GLU GLU B . n 
B 1 317  LEU 317  315  315  LEU LEU B . n 
B 1 318  SER 318  316  316  SER SER B . n 
B 1 319  LEU 319  317  317  LEU LEU B . n 
B 1 320  ASP 320  318  318  ASP ASP B . n 
B 1 321  LEU 321  319  319  LEU LEU B . n 
B 1 322  LEU 322  320  320  LEU LEU B . n 
B 1 323  GLU 323  321  321  GLU GLU B . n 
B 1 324  VAL 324  322  322  VAL VAL B . n 
B 1 325  LEU 325  323  323  LEU LEU B . n 
B 1 326  CYS 326  324  324  CYS CYS B . n 
B 1 327  LEU 327  325  325  LEU LEU B . n 
B 1 328  ASP 328  326  326  ASP ASP B . n 
B 1 329  GLY 329  327  327  GLY GLY B . n 
B 1 330  ASP 330  328  328  ASP ASP B . n 
B 1 331  LEU 331  329  329  LEU LEU B . n 
B 1 332  SER 332  330  330  SER SER B . n 
B 1 333  GLY 333  331  331  GLY GLY B . n 
B 1 334  TRP 334  332  332  TRP TRP B . n 
B 1 335  ASN 335  333  333  ASN ASN B . n 
B 1 336  GLY 336  334  334  GLY GLY B . n 
B 1 337  MET 337  335  335  MET MET B . n 
B 1 338  GLY 338  336  336  GLY GLY B . n 
B 1 339  PHE 339  337  337  PHE PHE B . n 
B 1 340  VAL 340  338  338  VAL VAL B . n 
B 1 341  VAL 341  339  339  VAL VAL B . n 
B 1 342  GLN 342  340  340  GLN GLN B . n 
B 1 343  ALA 343  341  341  ALA ALA B . n 
B 1 344  TYR 344  342  342  TYR TYR B . n 
B 1 345  GLY 345  343  343  GLY GLY B . n 
B 1 346  LYS 346  344  344  LYS LYS B . n 
B 1 347  ARG 347  345  345  ARG ARG B . n 
B 1 348  CYS 348  346  346  CYS CYS B . n 
B 1 349  PRO 349  347  347  PRO PRO B . n 
B 1 350  PHE 350  348  348  PHE PHE B . n 
B 1 351  VAL 351  349  349  VAL VAL B . n 
B 1 352  LEU 352  350  350  LEU LEU B . n 
B 1 353  ASP 353  351  351  ASP ASP B . n 
B 1 354  PHE 354  352  352  PHE PHE B . n 
B 1 355  ILE 355  353  353  ILE ILE B . n 
B 1 356  ILE 356  354  354  ILE ILE B . n 
B 1 357  ASP 357  355  355  ASP ASP B . n 
B 1 358  LEU 358  356  356  LEU LEU B . n 
B 1 359  ALA 359  357  357  ALA ALA B . n 
B 1 360  ARG 360  358  358  ARG ARG B . n 
B 1 361  ARG 361  359  359  ARG ARG B . n 
B 1 362  SER 362  360  360  SER SER B . n 
B 1 363  GLY 363  361  361  GLY GLY B . n 
B 1 364  ARG 364  362  362  ARG ARG B . n 
B 1 365  ARG 365  363  363  ARG ARG B . n 
B 1 366  ILE 366  364  364  ILE ILE B . n 
B 1 367  MET 367  365  365  MET MET B . n 
B 1 368  VAL 368  366  366  VAL VAL B . n 
B 1 369  ARG 369  367  367  ARG ARG B . n 
B 1 370  LEU 370  368  368  LEU LEU B . n 
B 1 371  VAL 371  369  369  VAL VAL B . n 
B 1 372  LYS 372  370  370  LYS LYS B . n 
B 1 373  GLY 373  371  371  GLY GLY B . n 
B 1 374  ALA 374  372  372  ALA ALA B . n 
B 1 375  TYR 375  373  373  TYR TYR B . n 
B 1 376  TRP 376  374  374  TRP TRP B . n 
B 1 377  ASP 377  375  375  ASP ASP B . n 
B 1 378  ALA 378  376  376  ALA ALA B . n 
B 1 379  GLU 379  377  377  GLU GLU B . n 
B 1 380  ILE 380  378  378  ILE ILE B . n 
B 1 381  LYS 381  379  379  LYS LYS B . n 
B 1 382  ARG 382  380  380  ARG ARG B . n 
B 1 383  ALA 383  381  381  ALA ALA B . n 
B 1 384  GLN 384  382  382  GLN GLN B . n 
B 1 385  LEU 385  383  383  LEU LEU B . n 
B 1 386  ASP 386  384  384  ASP ASP B . n 
B 1 387  GLY 387  385  385  GLY GLY B . n 
B 1 388  LEU 388  386  386  LEU LEU B . n 
B 1 389  ALA 389  387  387  ALA ALA B . n 
B 1 390  ASP 390  388  388  ASP ASP B . n 
B 1 391  PHE 391  389  389  PHE PHE B . n 
B 1 392  PRO 392  390  390  PRO PRO B . n 
B 1 393  VAL 393  391  391  VAL VAL B . n 
B 1 394  PHE 394  392  392  PHE PHE B . n 
B 1 395  THR 395  393  393  THR THR B . n 
B 1 396  ARG 396  394  394  ARG ARG B . n 
B 1 397  LYS 397  395  395  LYS LYS B . n 
B 1 398  ILE 398  396  396  ILE ILE B . n 
B 1 399  HIS 399  397  397  HIS HIS B . n 
B 1 400  THR 400  398  398  THR THR B . n 
B 1 401  ASP 401  399  399  ASP ASP B . n 
B 1 402  VAL 402  400  400  VAL VAL B . n 
B 1 403  SER 403  401  401  SER SER B . n 
B 1 404  TYR 404  402  402  TYR TYR B . n 
B 1 405  ILE 405  403  403  ILE ILE B . n 
B 1 406  ALA 406  404  404  ALA ALA B . n 
B 1 407  CYS 407  405  405  CYS CYS B . n 
B 1 408  ALA 408  406  406  ALA ALA B . n 
B 1 409  ALA 409  407  407  ALA ALA B . n 
B 1 410  LYS 410  408  408  LYS LYS B . n 
B 1 411  LEU 411  409  409  LEU LEU B . n 
B 1 412  LEU 412  410  410  LEU LEU B . n 
B 1 413  ALA 413  411  411  ALA ALA B . n 
B 1 414  ALA 414  412  412  ALA ALA B . n 
B 1 415  THR 415  413  413  THR THR B . n 
B 1 416  ASP 416  414  414  ASP ASP B . n 
B 1 417  VAL 417  415  415  VAL VAL B . n 
B 1 418  VAL 418  416  416  VAL VAL B . n 
B 1 419  PHE 419  417  417  PHE PHE B . n 
B 1 420  PRO 420  418  418  PRO PRO B . n 
B 1 421  GLN 421  419  419  GLN GLN B . n 
B 1 422  PHE 422  420  420  PHE PHE B . n 
B 1 423  ALA 423  421  421  ALA ALA B . n 
B 1 424  THR 424  422  422  THR THR B . n 
B 1 425  HIS 425  423  423  HIS HIS B . n 
B 1 426  ASN 426  424  424  ASN ASN B . n 
B 1 427  ALA 427  425  425  ALA ALA B . n 
B 1 428  GLN 428  426  426  GLN GLN B . n 
B 1 429  THR 429  427  427  THR THR B . n 
B 1 430  LEU 430  428  428  LEU LEU B . n 
B 1 431  ALA 431  429  429  ALA ALA B . n 
B 1 432  ALA 432  430  430  ALA ALA B . n 
B 1 433  ILE 433  431  431  ILE ILE B . n 
B 1 434  TYR 434  432  432  TYR TYR B . n 
B 1 435  HIS 435  433  433  HIS HIS B . n 
B 1 436  MET 436  434  434  MET MET B . n 
B 1 437  ALA 437  435  435  ALA ALA B . n 
B 1 438  GLY 438  436  436  GLY GLY B . n 
B 1 439  LYS 439  437  437  LYS LYS B . n 
B 1 440  ASP 440  438  438  ASP ASP B . n 
B 1 441  PHE 441  439  439  PHE PHE B . n 
B 1 442  HIS 442  440  440  HIS HIS B . n 
B 1 443  VAL 443  441  441  VAL VAL B . n 
B 1 444  GLY 444  442  442  GLY GLY B . n 
B 1 445  LYS 445  443  443  LYS LYS B . n 
B 1 446  TYR 446  444  444  TYR TYR B . n 
B 1 447  GLU 447  445  445  GLU GLU B . n 
B 1 448  PHE 448  446  446  PHE PHE B . n 
B 1 449  GLN 449  447  447  GLN GLN B . n 
B 1 450  CYS 450  448  448  CYS CYS B . n 
B 1 451  LEU 451  449  449  LEU LEU B . n 
B 1 452  HIS 452  450  450  HIS HIS B . n 
B 1 453  GLY 453  451  451  GLY GLY B . n 
B 1 454  MET 454  452  452  MET MET B . n 
B 1 455  GLY 455  453  453  GLY GLY B . n 
B 1 456  GLU 456  454  454  GLU GLU B . n 
B 1 457  PRO 457  455  455  PRO PRO B . n 
B 1 458  LEU 458  456  456  LEU LEU B . n 
B 1 459  TYR 459  457  457  TYR TYR B . n 
B 1 460  GLU 460  458  458  GLU GLU B . n 
B 1 461  GLU 461  459  459  GLU GLU B . n 
B 1 462  VAL 462  460  460  VAL VAL B . n 
B 1 463  VAL 463  461  461  VAL VAL B . n 
B 1 464  GLY 464  462  462  GLY GLY B . n 
B 1 465  ARG 465  463  463  ARG ARG B . n 
B 1 466  GLY 466  464  464  GLY GLY B . n 
B 1 467  LYS 467  465  465  LYS LYS B . n 
B 1 468  LEU 468  466  466  LEU LEU B . n 
B 1 469  ASP 469  467  467  ASP ASP B . n 
B 1 470  ARG 470  468  468  ARG ARG B . n 
B 1 471  PRO 471  469  469  PRO PRO B . n 
B 1 472  CYS 472  470  470  CYS CYS B . n 
B 1 473  ARG 473  471  471  ARG ARG B . n 
B 1 474  ILE 474  472  472  ILE ILE B . n 
B 1 475  TYR 475  473  473  TYR TYR B . n 
B 1 476  ALA 476  474  474  ALA ALA B . n 
B 1 477  PRO 477  475  475  PRO PRO B . n 
B 1 478  VAL 478  476  476  VAL VAL B . n 
B 1 479  GLY 479  477  477  GLY GLY B . n 
B 1 480  THR 480  478  478  THR THR B . n 
B 1 481  HIS 481  479  479  HIS HIS B . n 
B 1 482  GLU 482  480  480  GLU GLU B . n 
B 1 483  THR 483  481  481  THR THR B . n 
B 1 484  LEU 484  482  482  LEU LEU B . n 
B 1 485  LEU 485  483  483  LEU LEU B . n 
B 1 486  ALA 486  484  484  ALA ALA B . n 
B 1 487  TYR 487  485  485  TYR TYR B . n 
B 1 488  LEU 488  486  486  LEU LEU B . n 
B 1 489  VAL 489  487  487  VAL VAL B . n 
B 1 490  ARG 490  488  488  ARG ARG B . n 
B 1 491  ARG 491  489  489  ARG ARG B . n 
B 1 492  LEU 492  490  490  LEU LEU B . n 
B 1 493  LEU 493  491  491  LEU LEU B . n 
B 1 494  GLU 494  492  492  GLU GLU B . n 
B 1 495  ASN 495  493  ?    ?   ?   B . n 
B 1 496  GLY 496  494  ?    ?   ?   B . n 
B 1 497  ALA 497  495  495  ALA ALA B . n 
B 1 498  ASN 498  496  496  ASN ASN B . n 
B 1 499  SER 499  497  497  SER SER B . n 
B 1 500  SER 500  498  498  SER SER B . n 
B 1 501  PHE 501  499  499  PHE PHE B . n 
B 1 502  VAL 502  500  500  VAL VAL B . n 
B 1 503  HIS 503  501  501  HIS HIS B . n 
B 1 504  ARG 504  502  502  ARG ARG B . n 
B 1 505  ILE 505  503  503  ILE ILE B . n 
B 1 506  ASN 506  504  504  ASN ASN B . n 
B 1 507  ASP 507  505  505  ASP ASP B . n 
B 1 508  PRO 508  506  506  PRO PRO B . n 
B 1 509  LYS 509  507  507  LYS LYS B . n 
B 1 510  VAL 510  508  508  VAL VAL B . n 
B 1 511  SER 511  509  509  SER SER B . n 
B 1 512  ILE 512  510  510  ILE ILE B . n 
B 1 513  ASP 513  511  511  ASP ASP B . n 
B 1 514  GLU 514  512  512  GLU GLU B . n 
B 1 515  LEU 515  513  513  LEU LEU B . n 
B 1 516  ILE 516  514  514  ILE ILE B . n 
B 1 517  ALA 517  515  515  ALA ALA B . n 
B 1 518  ASP 518  516  516  ASP ASP B . n 
B 1 519  PRO 519  517  517  PRO PRO B . n 
B 1 520  VAL 520  518  518  VAL VAL B . n 
B 1 521  GLU 521  519  519  GLU GLU B . n 
B 1 522  VAL 522  520  520  VAL VAL B . n 
B 1 523  VAL 523  521  521  VAL VAL B . n 
B 1 524  ARG 524  522  522  ARG ARG B . n 
B 1 525  ALA 525  523  523  ALA ALA B . n 
B 1 526  MET 526  524  524  MET MET B . n 
B 1 527  PRO 527  525  525  PRO PRO B . n 
B 1 528  VAL 528  526  526  VAL VAL B . n 
B 1 529  VAL 529  527  527  VAL VAL B . n 
B 1 530  GLY 530  528  528  GLY GLY B . n 
B 1 531  ALA 531  529  529  ALA ALA B . n 
B 1 532  LYS 532  530  530  LYS LYS B . n 
B 1 533  HIS 533  531  531  HIS HIS B . n 
B 1 534  ASP 534  532  532  ASP ASP B . n 
B 1 535  ARG 535  533  533  ARG ARG B . n 
B 1 536  ILE 536  534  534  ILE ILE B . n 
B 1 537  ALA 537  535  535  ALA ALA B . n 
B 1 538  LEU 538  536  536  LEU LEU B . n 
B 1 539  PRO 539  537  537  PRO PRO B . n 
B 1 540  ALA 540  538  538  ALA ALA B . n 
B 1 541  GLU 541  539  539  GLU GLU B . n 
B 1 542  LEU 542  540  540  LEU LEU B . n 
B 1 543  PHE 543  541  541  PHE PHE B . n 
B 1 544  GLY 544  542  542  GLY GLY B . n 
B 1 545  ASP 545  543  543  ASP ASP B . n 
B 1 546  ALA 546  544  544  ALA ALA B . n 
B 1 547  ARG 547  545  545  ARG ARG B . n 
B 1 548  THR 548  546  546  THR THR B . n 
B 1 549  ASN 549  547  547  ASN ASN B . n 
B 1 550  SER 550  548  548  SER SER B . n 
B 1 551  ALA 551  549  549  ALA ALA B . n 
B 1 552  GLY 552  550  550  GLY GLY B . n 
B 1 553  LEU 553  551  551  LEU LEU B . n 
B 1 554  ASP 554  552  552  ASP ASP B . n 
B 1 555  LEU 555  553  553  LEU LEU B . n 
B 1 556  SER 556  554  554  SER SER B . n 
B 1 557  ASN 557  555  555  ASN ASN B . n 
B 1 558  GLU 558  556  556  GLU GLU B . n 
B 1 559  GLU 559  557  557  GLU GLU B . n 
B 1 560  THR 560  558  558  THR THR B . n 
B 1 561  LEU 561  559  559  LEU LEU B . n 
B 1 562  ALA 562  560  560  ALA ALA B . n 
B 1 563  SER 563  561  561  SER SER B . n 
B 1 564  LEU 564  562  562  LEU LEU B . n 
B 1 565  THR 565  563  563  THR THR B . n 
B 1 566  GLU 566  564  564  GLU GLU B . n 
B 1 567  ALA 567  565  565  ALA ALA B . n 
B 1 568  LEU 568  566  566  LEU LEU B . n 
B 1 569  ARG 569  567  567  ARG ARG B . n 
B 1 570  GLU 570  568  568  GLU GLU B . n 
B 1 571  SER 571  569  569  SER SER B . n 
B 1 572  ALA 572  570  570  ALA ALA B . n 
B 1 573  ALA 573  571  571  ALA ALA B . n 
B 1 574  MET 574  572  572  MET MET B . n 
B 1 575  LYS 575  573  573  LYS LYS B . n 
B 1 576  TRP 576  574  574  TRP TRP B . n 
B 1 577  THR 577  575  575  THR THR B . n 
B 1 578  ALA 578  576  576  ALA ALA B . n 
B 1 579  LEU 579  577  577  LEU LEU B . n 
B 1 580  PRO 580  578  578  PRO PRO B . n 
B 1 581  GLN 581  579  579  GLN GLN B . n 
B 1 582  LEU 582  580  580  LEU LEU B . n 
B 1 583  ALA 583  581  581  ALA ALA B . n 
B 1 584  THR 584  582  582  THR THR B . n 
B 1 585  GLY 585  583  583  GLY GLY B . n 
B 1 586  PRO 586  584  584  PRO PRO B . n 
B 1 587  ALA 587  585  585  ALA ALA B . n 
B 1 588  ALA 588  586  586  ALA ALA B . n 
B 1 589  GLY 589  587  587  GLY GLY B . n 
B 1 590  GLU 590  588  588  GLU GLU B . n 
B 1 591  THR 591  589  589  THR THR B . n 
B 1 592  ARG 592  590  590  ARG ARG B . n 
B 1 593  THR 593  591  591  THR THR B . n 
B 1 594  VAL 594  592  592  VAL VAL B . n 
B 1 595  LEU 595  593  593  LEU LEU B . n 
B 1 596  ASN 596  594  594  ASN ASN B . n 
B 1 597  PRO 597  595  595  PRO PRO B . n 
B 1 598  GLY 598  596  596  GLY GLY B . n 
B 1 599  ASP 599  597  597  ASP ASP B . n 
B 1 600  HIS 600  598  598  HIS HIS B . n 
B 1 601  ARG 601  599  599  ARG ARG B . n 
B 1 602  ASP 602  600  600  ASP ASP B . n 
B 1 603  VAL 603  601  601  VAL VAL B . n 
B 1 604  VAL 604  602  602  VAL VAL B . n 
B 1 605  GLY 605  603  603  GLY GLY B . n 
B 1 606  SER 606  604  604  SER SER B . n 
B 1 607  VAL 607  605  605  VAL VAL B . n 
B 1 608  THR 608  606  606  THR THR B . n 
B 1 609  GLU 609  607  607  GLU GLU B . n 
B 1 610  THR 610  608  608  THR THR B . n 
B 1 611  SER 611  609  609  SER SER B . n 
B 1 612  GLU 612  610  610  GLU GLU B . n 
B 1 613  GLU 613  611  611  GLU GLU B . n 
B 1 614  ASP 614  612  612  ASP ASP B . n 
B 1 615  ALA 615  613  613  ALA ALA B . n 
B 1 616  ARG 616  614  614  ARG ARG B . n 
B 1 617  ARG 617  615  615  ARG ARG B . n 
B 1 618  ALA 618  616  616  ALA ALA B . n 
B 1 619  VAL 619  617  617  VAL VAL B . n 
B 1 620  ARG 620  618  618  ARG ARG B . n 
B 1 621  LEU 621  619  619  LEU LEU B . n 
B 1 622  ALA 622  620  620  ALA ALA B . n 
B 1 623  ALA 623  621  621  ALA ALA B . n 
B 1 624  ASP 624  622  622  ASP ASP B . n 
B 1 625  ALA 625  623  623  ALA ALA B . n 
B 1 626  ALA 626  624  624  ALA ALA B . n 
B 1 627  PRO 627  625  625  PRO PRO B . n 
B 1 628  ASP 628  626  626  ASP ASP B . n 
B 1 629  TRP 629  627  627  TRP TRP B . n 
B 1 630  ALA 630  628  628  ALA ALA B . n 
B 1 631  ALA 631  629  629  ALA ALA B . n 
B 1 632  VAL 632  630  630  VAL VAL B . n 
B 1 633  PRO 633  631  631  PRO PRO B . n 
B 1 634  PRO 634  632  632  PRO PRO B . n 
B 1 635  SER 635  633  633  SER SER B . n 
B 1 636  GLU 636  634  634  GLU GLU B . n 
B 1 637  ARG 637  635  635  ARG ARG B . n 
B 1 638  ALA 638  636  636  ALA ALA B . n 
B 1 639  ALA 639  637  637  ALA ALA B . n 
B 1 640  CYS 640  638  638  CYS CYS B . n 
B 1 641  LEU 641  639  639  LEU LEU B . n 
B 1 642  ASP 642  640  640  ASP ASP B . n 
B 1 643  ARG 643  641  641  ARG ARG B . n 
B 1 644  ALA 644  642  642  ALA ALA B . n 
B 1 645  ALA 645  643  643  ALA ALA B . n 
B 1 646  GLU 646  644  644  GLU GLU B . n 
B 1 647  LEU 647  645  645  LEU LEU B . n 
B 1 648  MET 648  646  646  MET MET B . n 
B 1 649  GLN 649  647  647  GLN GLN B . n 
B 1 650  ALA 650  648  648  ALA ALA B . n 
B 1 651  ARG 651  649  649  ARG ARG B . n 
B 1 652  MET 652  650  650  MET MET B . n 
B 1 653  PRO 653  651  651  PRO PRO B . n 
B 1 654  THR 654  652  652  THR THR B . n 
B 1 655  LEU 655  653  653  LEU LEU B . n 
B 1 656  LEU 656  654  654  LEU LEU B . n 
B 1 657  GLY 657  655  655  GLY GLY B . n 
B 1 658  LEU 658  656  656  LEU LEU B . n 
B 1 659  ILE 659  657  657  ILE ILE B . n 
B 1 660  ILE 660  658  658  ILE ILE B . n 
B 1 661  ARG 661  659  659  ARG ARG B . n 
B 1 662  GLU 662  660  660  GLU GLU B . n 
B 1 663  ALA 663  661  661  ALA ALA B . n 
B 1 664  GLY 664  662  662  GLY GLY B . n 
B 1 665  LYS 665  663  663  LYS LYS B . n 
B 1 666  SER 666  664  664  SER SER B . n 
B 1 667  ALA 667  665  665  ALA ALA B . n 
B 1 668  LEU 668  666  666  LEU LEU B . n 
B 1 669  ASN 669  667  667  ASN ASN B . n 
B 1 670  ALA 670  668  668  ALA ALA B . n 
B 1 671  ILE 671  669  669  ILE ILE B . n 
B 1 672  ALA 672  670  670  ALA ALA B . n 
B 1 673  GLU 673  671  671  GLU GLU B . n 
B 1 674  VAL 674  672  672  VAL VAL B . n 
B 1 675  ARG 675  673  673  ARG ARG B . n 
B 1 676  GLU 676  674  674  GLU GLU B . n 
B 1 677  ALA 677  675  675  ALA ALA B . n 
B 1 678  ILE 678  676  676  ILE ILE B . n 
B 1 679  ASP 679  677  677  ASP ASP B . n 
B 1 680  PHE 680  678  678  PHE PHE B . n 
B 1 681  LEU 681  679  679  LEU LEU B . n 
B 1 682  ARG 682  680  680  ARG ARG B . n 
B 1 683  TYR 683  681  681  TYR TYR B . n 
B 1 684  TYR 684  682  682  TYR TYR B . n 
B 1 685  ALA 685  683  683  ALA ALA B . n 
B 1 686  GLU 686  684  684  GLU GLU B . n 
B 1 687  GLN 687  685  685  GLN GLN B . n 
B 1 688  THR 688  686  686  THR THR B . n 
B 1 689  ARG 689  687  687  ARG ARG B . n 
B 1 690  ARG 690  688  688  ARG ARG B . n 
B 1 691  THR 691  689  689  THR THR B . n 
B 1 692  LEU 692  690  690  LEU LEU B . n 
B 1 693  GLY 693  691  691  GLY GLY B . n 
B 1 694  PRO 694  692  692  PRO PRO B . n 
B 1 695  GLY 695  693  693  GLY GLY B . n 
B 1 696  HIS 696  694  694  HIS HIS B . n 
B 1 697  GLY 697  695  695  GLY GLY B . n 
B 1 698  PRO 698  696  696  PRO PRO B . n 
B 1 699  LEU 699  697  697  LEU LEU B . n 
B 1 700  GLY 700  698  698  GLY GLY B . n 
B 1 701  PRO 701  699  699  PRO PRO B . n 
B 1 702  ILE 702  700  700  ILE ILE B . n 
B 1 703  VAL 703  701  701  VAL VAL B . n 
B 1 704  CYS 704  702  702  CYS CYS B . n 
B 1 705  ILE 705  703  703  ILE ILE B . n 
B 1 706  SER 706  704  704  SER SER B . n 
B 1 707  PRO 707  705  705  PRO PRO B . n 
B 1 708  TRP 708  706  706  TRP TRP B . n 
B 1 709  ASN 709  707  707  ASN ASN B . n 
B 1 710  PHE 710  708  708  PHE PHE B . n 
B 1 711  PRO 711  709  709  PRO PRO B . n 
B 1 712  LEU 712  710  710  LEU LEU B . n 
B 1 713  ALA 713  711  711  ALA ALA B . n 
B 1 714  ILE 714  712  712  ILE ILE B . n 
B 1 715  PHE 715  713  713  PHE PHE B . n 
B 1 716  THR 716  714  714  THR THR B . n 
B 1 717  GLY 717  715  715  GLY GLY B . n 
B 1 718  GLN 718  716  716  GLN GLN B . n 
B 1 719  ILE 719  717  717  ILE ILE B . n 
B 1 720  ALA 720  718  718  ALA ALA B . n 
B 1 721  ALA 721  719  719  ALA ALA B . n 
B 1 722  ALA 722  720  720  ALA ALA B . n 
B 1 723  LEU 723  721  721  LEU LEU B . n 
B 1 724  VAL 724  722  722  VAL VAL B . n 
B 1 725  ALA 725  723  723  ALA ALA B . n 
B 1 726  GLY 726  724  724  GLY GLY B . n 
B 1 727  ASN 727  725  725  ASN ASN B . n 
B 1 728  PRO 728  726  726  PRO PRO B . n 
B 1 729  VAL 729  727  727  VAL VAL B . n 
B 1 730  LEU 730  728  728  LEU LEU B . n 
B 1 731  ALA 731  729  729  ALA ALA B . n 
B 1 732  LYS 732  730  730  LYS LYS B . n 
B 1 733  PRO 733  731  731  PRO PRO B . n 
B 1 734  ALA 734  732  732  ALA ALA B . n 
B 1 735  GLU 735  733  733  GLU GLU B . n 
B 1 736  GLU 736  734  734  GLU GLU B . n 
B 1 737  THR 737  735  735  THR THR B . n 
B 1 738  PRO 738  736  736  PRO PRO B . n 
B 1 739  LEU 739  737  737  LEU LEU B . n 
B 1 740  ILE 740  738  738  ILE ILE B . n 
B 1 741  ALA 741  739  739  ALA ALA B . n 
B 1 742  ALA 742  740  740  ALA ALA B . n 
B 1 743  GLU 743  741  741  GLU GLU B . n 
B 1 744  GLY 744  742  742  GLY GLY B . n 
B 1 745  VAL 745  743  743  VAL VAL B . n 
B 1 746  ARG 746  744  744  ARG ARG B . n 
B 1 747  ILE 747  745  745  ILE ILE B . n 
B 1 748  LEU 748  746  746  LEU LEU B . n 
B 1 749  ARG 749  747  747  ARG ARG B . n 
B 1 750  GLU 750  748  748  GLU GLU B . n 
B 1 751  ALA 751  749  749  ALA ALA B . n 
B 1 752  GLY 752  750  750  GLY GLY B . n 
B 1 753  ILE 753  751  751  ILE ILE B . n 
B 1 754  PRO 754  752  752  PRO PRO B . n 
B 1 755  ALA 755  753  753  ALA ALA B . n 
B 1 756  SER 756  754  754  SER SER B . n 
B 1 757  ALA 757  755  755  ALA ALA B . n 
B 1 758  LEU 758  756  756  LEU LEU B . n 
B 1 759  GLN 759  757  757  GLN GLN B . n 
B 1 760  LEU 760  758  758  LEU LEU B . n 
B 1 761  LEU 761  759  759  LEU LEU B . n 
B 1 762  PRO 762  760  760  PRO PRO B . n 
B 1 763  GLY 763  761  761  GLY GLY B . n 
B 1 764  ASP 764  762  762  ASP ASP B . n 
B 1 765  GLY 765  763  763  GLY GLY B . n 
B 1 766  ARG 766  764  764  ARG ARG B . n 
B 1 767  VAL 767  765  765  VAL VAL B . n 
B 1 768  GLY 768  766  766  GLY GLY B . n 
B 1 769  ALA 769  767  767  ALA ALA B . n 
B 1 770  ALA 770  768  768  ALA ALA B . n 
B 1 771  LEU 771  769  769  LEU LEU B . n 
B 1 772  VAL 772  770  770  VAL VAL B . n 
B 1 773  ALA 773  771  771  ALA ALA B . n 
B 1 774  ALA 774  772  772  ALA ALA B . n 
B 1 775  ALA 775  773  773  ALA ALA B . n 
B 1 776  GLU 776  774  774  GLU GLU B . n 
B 1 777  THR 777  775  775  THR THR B . n 
B 1 778  ALA 778  776  776  ALA ALA B . n 
B 1 779  GLY 779  777  777  GLY GLY B . n 
B 1 780  VAL 780  778  778  VAL VAL B . n 
B 1 781  MET 781  779  779  MET MET B . n 
B 1 782  PHE 782  780  780  PHE PHE B . n 
B 1 783  THR 783  781  781  THR THR B . n 
B 1 784  GLY 784  782  782  GLY GLY B . n 
B 1 785  SER 785  783  783  SER SER B . n 
B 1 786  THR 786  784  784  THR THR B . n 
B 1 787  GLU 787  785  785  GLU GLU B . n 
B 1 788  VAL 788  786  786  VAL VAL B . n 
B 1 789  ALA 789  787  787  ALA ALA B . n 
B 1 790  ARG 790  788  788  ARG ARG B . n 
B 1 791  LEU 791  789  789  LEU LEU B . n 
B 1 792  ILE 792  790  790  ILE ILE B . n 
B 1 793  GLN 793  791  791  GLN GLN B . n 
B 1 794  ALA 794  792  792  ALA ALA B . n 
B 1 795  GLN 795  793  793  GLN GLN B . n 
B 1 796  LEU 796  794  794  LEU LEU B . n 
B 1 797  ALA 797  795  795  ALA ALA B . n 
B 1 798  ASP 798  796  796  ASP ASP B . n 
B 1 799  ARG 799  797  797  ARG ARG B . n 
B 1 800  LEU 800  798  798  LEU LEU B . n 
B 1 801  SER 801  799  799  SER SER B . n 
B 1 802  PRO 802  800  800  PRO PRO B . n 
B 1 803  ALA 803  801  801  ALA ALA B . n 
B 1 804  GLY 804  802  802  GLY GLY B . n 
B 1 805  ARG 805  803  803  ARG ARG B . n 
B 1 806  PRO 806  804  804  PRO PRO B . n 
B 1 807  ILE 807  805  805  ILE ILE B . n 
B 1 808  PRO 808  806  806  PRO PRO B . n 
B 1 809  LEU 809  807  807  LEU LEU B . n 
B 1 810  ILE 810  808  808  ILE ILE B . n 
B 1 811  ALA 811  809  809  ALA ALA B . n 
B 1 812  GLU 812  810  810  GLU GLU B . n 
B 1 813  THR 813  811  811  THR THR B . n 
B 1 814  GLY 814  812  812  GLY GLY B . n 
B 1 815  GLY 815  813  813  GLY GLY B . n 
B 1 816  GLN 816  814  814  GLN GLN B . n 
B 1 817  ASN 817  815  815  ASN ASN B . n 
B 1 818  ALA 818  816  816  ALA ALA B . n 
B 1 819  MET 819  817  817  MET MET B . n 
B 1 820  ILE 820  818  818  ILE ILE B . n 
B 1 821  VAL 821  819  819  VAL VAL B . n 
B 1 822  ASP 822  820  820  ASP ASP B . n 
B 1 823  SER 823  821  821  SER SER B . n 
B 1 824  SER 824  822  822  SER SER B . n 
B 1 825  ALA 825  823  823  ALA ALA B . n 
B 1 826  LEU 826  824  824  LEU LEU B . n 
B 1 827  ALA 827  825  825  ALA ALA B . n 
B 1 828  GLU 828  826  826  GLU GLU B . n 
B 1 829  GLN 829  827  827  GLN GLN B . n 
B 1 830  VAL 830  828  828  VAL VAL B . n 
B 1 831  VAL 831  829  829  VAL VAL B . n 
B 1 832  GLY 832  830  830  GLY GLY B . n 
B 1 833  ASP 833  831  831  ASP ASP B . n 
B 1 834  VAL 834  832  832  VAL VAL B . n 
B 1 835  ILE 835  833  833  ILE ILE B . n 
B 1 836  THR 836  834  834  THR THR B . n 
B 1 837  SER 837  835  835  SER SER B . n 
B 1 838  ALA 838  836  836  ALA ALA B . n 
B 1 839  PHE 839  837  837  PHE PHE B . n 
B 1 840  ASP 840  838  838  ASP ASP B . n 
B 1 841  SER 841  839  839  SER SER B . n 
B 1 842  ALA 842  840  840  ALA ALA B . n 
B 1 843  GLY 843  841  841  GLY GLY B . n 
B 1 844  GLN 844  842  842  GLN GLN B . n 
B 1 845  ARG 845  843  843  ARG ARG B . n 
B 1 846  CYS 846  844  844  CYS CYS B . n 
B 1 847  SER 847  845  845  SER SER B . n 
B 1 848  ALA 848  846  846  ALA ALA B . n 
B 1 849  LEU 849  847  847  LEU LEU B . n 
B 1 850  ARG 850  848  848  ARG ARG B . n 
B 1 851  VAL 851  849  849  VAL VAL B . n 
B 1 852  LEU 852  850  850  LEU LEU B . n 
B 1 853  CYS 853  851  851  CYS CYS B . n 
B 1 854  LEU 854  852  852  LEU LEU B . n 
B 1 855  GLN 855  853  853  GLN GLN B . n 
B 1 856  GLU 856  854  854  GLU GLU B . n 
B 1 857  ASP 857  855  855  ASP ASP B . n 
B 1 858  VAL 858  856  856  VAL VAL B . n 
B 1 859  ALA 859  857  857  ALA ALA B . n 
B 1 860  ASP 860  858  858  ASP ASP B . n 
B 1 861  ARG 861  859  859  ARG ARG B . n 
B 1 862  ILE 862  860  860  ILE ILE B . n 
B 1 863  LEU 863  861  861  LEU LEU B . n 
B 1 864  THR 864  862  862  THR THR B . n 
B 1 865  MET 865  863  863  MET MET B . n 
B 1 866  LEU 866  864  864  LEU LEU B . n 
B 1 867  LYS 867  865  865  LYS LYS B . n 
B 1 868  GLY 868  866  866  GLY GLY B . n 
B 1 869  ALA 869  867  867  ALA ALA B . n 
B 1 870  LEU 870  868  868  LEU LEU B . n 
B 1 871  HIS 871  869  869  HIS HIS B . n 
B 1 872  GLU 872  870  870  GLU GLU B . n 
B 1 873  LEU 873  871  871  LEU LEU B . n 
B 1 874  HIS 874  872  872  HIS HIS B . n 
B 1 875  ILE 875  873  873  ILE ILE B . n 
B 1 876  GLY 876  874  874  GLY GLY B . n 
B 1 877  ARG 877  875  875  ARG ARG B . n 
B 1 878  THR 878  876  876  THR THR B . n 
B 1 879  ASP 879  877  877  ASP ASP B . n 
B 1 880  ARG 880  878  878  ARG ARG B . n 
B 1 881  LEU 881  879  879  LEU LEU B . n 
B 1 882  SER 882  880  880  SER SER B . n 
B 1 883  VAL 883  881  881  VAL VAL B . n 
B 1 884  ASP 884  882  882  ASP ASP B . n 
B 1 885  VAL 885  883  883  VAL VAL B . n 
B 1 886  GLY 886  884  884  GLY GLY B . n 
B 1 887  PRO 887  885  885  PRO PRO B . n 
B 1 888  VAL 888  886  886  VAL VAL B . n 
B 1 889  ILE 889  887  887  ILE ILE B . n 
B 1 890  THR 890  888  888  THR THR B . n 
B 1 891  SER 891  889  889  SER SER B . n 
B 1 892  GLU 892  890  890  GLU GLU B . n 
B 1 893  ALA 893  891  891  ALA ALA B . n 
B 1 894  LYS 894  892  892  LYS LYS B . n 
B 1 895  ASP 895  893  893  ASP ASP B . n 
B 1 896  ASN 896  894  894  ASN ASN B . n 
B 1 897  ILE 897  895  895  ILE ILE B . n 
B 1 898  GLU 898  896  896  GLU GLU B . n 
B 1 899  LYS 899  897  897  LYS LYS B . n 
B 1 900  HIS 900  898  898  HIS HIS B . n 
B 1 901  ILE 901  899  899  ILE ILE B . n 
B 1 902  GLU 902  900  900  GLU GLU B . n 
B 1 903  ARG 903  901  901  ARG ARG B . n 
B 1 904  MET 904  902  902  MET MET B . n 
B 1 905  ARG 905  903  903  ARG ARG B . n 
B 1 906  GLY 906  904  904  GLY GLY B . n 
B 1 907  LEU 907  905  905  LEU LEU B . n 
B 1 908  GLY 908  906  906  GLY GLY B . n 
B 1 909  ARG 909  907  907  ARG ARG B . n 
B 1 910  LYS 910  908  908  LYS LYS B . n 
B 1 911  VAL 911  909  909  VAL VAL B . n 
B 1 912  GLU 912  910  910  GLU GLU B . n 
B 1 913  GLN 913  911  911  GLN GLN B . n 
B 1 914  ILE 914  912  912  ILE ILE B . n 
B 1 915  GLY 915  913  913  GLY GLY B . n 
B 1 916  LEU 916  914  914  LEU LEU B . n 
B 1 917  ALA 917  915  915  ALA ALA B . n 
B 1 918  SER 918  916  916  SER SER B . n 
B 1 919  GLU 919  917  917  GLU GLU B . n 
B 1 920  THR 920  918  918  THR THR B . n 
B 1 921  GLY 921  919  919  GLY GLY B . n 
B 1 922  VAL 922  920  920  VAL VAL B . n 
B 1 923  GLY 923  921  921  GLY GLY B . n 
B 1 924  THR 924  922  922  THR THR B . n 
B 1 925  PHE 925  923  923  PHE PHE B . n 
B 1 926  VAL 926  924  924  VAL VAL B . n 
B 1 927  PRO 927  925  925  PRO PRO B . n 
B 1 928  PRO 928  926  926  PRO PRO B . n 
B 1 929  THR 929  927  927  THR THR B . n 
B 1 930  ILE 930  928  928  ILE ILE B . n 
B 1 931  ILE 931  929  929  ILE ILE B . n 
B 1 932  GLU 932  930  930  GLU GLU B . n 
B 1 933  LEU 933  931  931  LEU LEU B . n 
B 1 934  GLU 934  932  932  GLU GLU B . n 
B 1 935  LYS 935  933  933  LYS LYS B . n 
B 1 936  LEU 936  934  934  LEU LEU B . n 
B 1 937  SER 937  935  935  SER SER B . n 
B 1 938  ASP 938  936  936  ASP ASP B . n 
B 1 939  LEU 939  937  937  LEU LEU B . n 
B 1 940  GLN 940  938  938  GLN GLN B . n 
B 1 941  ARG 941  939  939  ARG ARG B . n 
B 1 942  GLU 942  940  940  GLU GLU B . n 
B 1 943  VAL 943  941  941  VAL VAL B . n 
B 1 944  PHE 944  942  942  PHE PHE B . n 
B 1 945  GLY 945  943  943  GLY GLY B . n 
B 1 946  PRO 946  944  944  PRO PRO B . n 
B 1 947  VAL 947  945  945  VAL VAL B . n 
B 1 948  LEU 948  946  946  LEU LEU B . n 
B 1 949  HIS 949  947  947  HIS HIS B . n 
B 1 950  VAL 950  948  948  VAL VAL B . n 
B 1 951  ILE 951  949  949  ILE ILE B . n 
B 1 952  ARG 952  950  950  ARG ARG B . n 
B 1 953  TYR 953  951  951  TYR TYR B . n 
B 1 954  ARG 954  952  952  ARG ARG B . n 
B 1 955  ARG 955  953  953  ARG ARG B . n 
B 1 956  ASP 956  954  954  ASP ASP B . n 
B 1 957  ASP 957  955  955  ASP ASP B . n 
B 1 958  LEU 958  956  956  LEU LEU B . n 
B 1 959  ASP 959  957  957  ASP ASP B . n 
B 1 960  ARG 960  958  958  ARG ARG B . n 
B 1 961  LEU 961  959  959  LEU LEU B . n 
B 1 962  VAL 962  960  960  VAL VAL B . n 
B 1 963  ASP 963  961  961  ASP ASP B . n 
B 1 964  ASP 964  962  962  ASP ASP B . n 
B 1 965  VAL 965  963  963  VAL VAL B . n 
B 1 966  ASN 966  964  964  ASN ASN B . n 
B 1 967  ALA 967  965  965  ALA ALA B . n 
B 1 968  THR 968  966  966  THR THR B . n 
B 1 969  GLY 969  967  967  GLY GLY B . n 
B 1 970  TYR 970  968  968  TYR TYR B . n 
B 1 971  GLY 971  969  969  GLY GLY B . n 
B 1 972  LEU 972  970  970  LEU LEU B . n 
B 1 973  THR 973  971  971  THR THR B . n 
B 1 974  PHE 974  972  972  PHE PHE B . n 
B 1 975  GLY 975  973  973  GLY GLY B . n 
B 1 976  LEU 976  974  974  LEU LEU B . n 
B 1 977  HIS 977  975  975  HIS HIS B . n 
B 1 978  THR 978  976  976  THR THR B . n 
B 1 979  ARG 979  977  977  ARG ARG B . n 
B 1 980  LEU 980  978  978  LEU LEU B . n 
B 1 981  ASP 981  979  979  ASP ASP B . n 
B 1 982  GLU 982  980  980  GLU GLU B . n 
B 1 983  THR 983  981  981  THR THR B . n 
B 1 984  ILE 984  982  982  ILE ILE B . n 
B 1 985  ALA 985  983  983  ALA ALA B . n 
B 1 986  HIS 986  984  984  HIS HIS B . n 
B 1 987  VAL 987  985  985  VAL VAL B . n 
B 1 988  THR 988  986  986  THR THR B . n 
B 1 989  SER 989  987  987  SER SER B . n 
B 1 990  ARG 990  988  988  ARG ARG B . n 
B 1 991  ILE 991  989  989  ILE ILE B . n 
B 1 992  LYS 992  990  990  LYS LYS B . n 
B 1 993  ALA 993  991  991  ALA ALA B . n 
B 1 994  GLY 994  992  992  GLY GLY B . n 
B 1 995  ASN 995  993  993  ASN ASN B . n 
B 1 996  LEU 996  994  994  LEU LEU B . n 
B 1 997  TYR 997  995  995  TYR TYR B . n 
B 1 998  ILE 998  996  996  ILE ILE B . n 
B 1 999  ASN 999  997  997  ASN ASN B . n 
B 1 1000 ARG 1000 998  998  ARG ARG B . n 
B 1 1001 ASN 1001 999  999  ASN ASN B . n 
B 1 1002 ILE 1002 1000 1000 ILE ILE B . n 
B 1 1003 ILE 1003 1001 1001 ILE ILE B . n 
B 1 1004 GLY 1004 1002 1002 GLY GLY B . n 
B 1 1005 ALA 1005 1003 1003 ALA ALA B . n 
B 1 1006 VAL 1006 1004 1004 VAL VAL B . n 
B 1 1007 VAL 1007 1005 1005 VAL VAL B . n 
B 1 1008 GLY 1008 1006 1006 GLY GLY B . n 
B 1 1009 VAL 1009 1007 1007 VAL VAL B . n 
B 1 1010 GLN 1010 1008 1008 GLN GLN B . n 
B 1 1011 PRO 1011 1009 1009 PRO PRO B . n 
B 1 1012 PHE 1012 1010 1010 PHE PHE B . n 
B 1 1013 GLY 1013 1011 1011 GLY GLY B . n 
B 1 1014 GLY 1014 1012 1012 GLY GLY B . n 
B 1 1015 ARG 1015 1013 1013 ARG ARG B . n 
B 1 1016 GLY 1016 1014 1014 GLY GLY B . n 
B 1 1017 LEU 1017 1015 1015 LEU LEU B . n 
B 1 1018 SER 1018 1016 1016 SER SER B . n 
B 1 1019 GLY 1019 1017 1017 GLY GLY B . n 
B 1 1020 THR 1020 1018 1018 THR THR B . n 
B 1 1021 GLY 1021 1019 1019 GLY GLY B . n 
B 1 1022 PRO 1022 1020 1020 PRO PRO B . n 
B 1 1023 LYS 1023 1021 1021 LYS LYS B . n 
B 1 1024 ALA 1024 1022 1022 ALA ALA B . n 
B 1 1025 GLY 1025 1023 1023 GLY GLY B . n 
B 1 1026 GLY 1026 1024 1024 GLY GLY B . n 
B 1 1027 PRO 1027 1025 1025 PRO PRO B . n 
B 1 1028 LEU 1028 1026 1026 LEU LEU B . n 
B 1 1029 TYR 1029 1027 1027 TYR TYR B . n 
B 1 1030 LEU 1030 1028 1028 LEU LEU B . n 
B 1 1031 GLY 1031 1029 1029 GLY GLY B . n 
B 1 1032 ARG 1032 1030 1030 ARG ARG B . n 
B 1 1033 LEU 1033 1031 1031 LEU LEU B . n 
B 1 1034 VAL 1034 1032 1032 VAL VAL B . n 
B 1 1035 THR 1035 1033 1033 THR THR B . n 
B 1 1036 THR 1036 1034 1034 THR THR B . n 
B 1 1037 ALA 1037 1035 1035 ALA ALA B . n 
B 1 1038 PRO 1038 1036 1036 PRO PRO B . n 
B 1 1039 VAL 1039 1037 1037 VAL VAL B . n 
B 1 1040 PRO 1040 1038 1038 PRO PRO B . n 
B 1 1041 PRO 1041 1039 1039 PRO PRO B . n 
B 1 1042 GLN 1042 1040 1040 GLN GLN B . n 
B 1 1043 HIS 1043 1041 1041 HIS HIS B . n 
B 1 1044 SER 1044 1042 1042 SER SER B . n 
B 1 1045 SER 1045 1043 1043 SER SER B . n 
B 1 1046 VAL 1046 1044 1044 VAL VAL B . n 
B 1 1047 HIS 1047 1045 1045 HIS HIS B . n 
B 1 1048 THR 1048 1046 1046 THR THR B . n 
B 1 1049 ASP 1049 1047 1047 ASP ASP B . n 
B 1 1050 PRO 1050 1048 1048 PRO PRO B . n 
B 1 1051 VAL 1051 1049 1049 VAL VAL B . n 
B 1 1052 LEU 1052 1050 1050 LEU LEU B . n 
B 1 1053 LEU 1053 1051 1051 LEU LEU B . n 
B 1 1054 ASP 1054 1052 1052 ASP ASP B . n 
B 1 1055 PHE 1055 1053 1053 PHE PHE B . n 
B 1 1056 ALA 1056 1054 1054 ALA ALA B . n 
B 1 1057 LYS 1057 1055 1055 LYS LYS B . n 
B 1 1058 TRP 1058 1056 1056 TRP TRP B . n 
B 1 1059 LEU 1059 1057 1057 LEU LEU B . n 
B 1 1060 ASP 1060 1058 1058 ASP ASP B . n 
B 1 1061 GLY 1061 1059 1059 GLY GLY B . n 
B 1 1062 LYS 1062 1060 1060 LYS LYS B . n 
B 1 1063 GLY 1063 1061 1061 GLY GLY B . n 
B 1 1064 ALA 1064 1062 1062 ALA ALA B . n 
B 1 1065 ARG 1065 1063 1063 ARG ARG B . n 
B 1 1066 ALA 1066 1064 1064 ALA ALA B . n 
B 1 1067 GLU 1067 1065 1065 GLU GLU B . n 
B 1 1068 ALA 1068 1066 1066 ALA ALA B . n 
B 1 1069 GLU 1069 1067 1067 GLU GLU B . n 
B 1 1070 ALA 1070 1068 1068 ALA ALA B . n 
B 1 1071 ALA 1071 1069 1069 ALA ALA B . n 
B 1 1072 ARG 1072 1070 1070 ARG ARG B . n 
B 1 1073 ASN 1073 1071 1071 ASN ASN B . n 
B 1 1074 ALA 1074 1072 1072 ALA ALA B . n 
B 1 1075 GLY 1075 1073 1073 GLY GLY B . n 
B 1 1076 SER 1076 1074 1074 SER SER B . n 
B 1 1077 SER 1077 1075 1075 SER SER B . n 
B 1 1078 SER 1078 1076 1076 SER SER B . n 
B 1 1079 ALA 1079 1077 1077 ALA ALA B . n 
B 1 1080 LEU 1080 1078 1078 LEU LEU B . n 
B 1 1081 GLY 1081 1079 1079 GLY GLY B . n 
B 1 1082 LEU 1082 1080 1080 LEU LEU B . n 
B 1 1083 ASP 1083 1081 1081 ASP ASP B . n 
B 1 1084 LEU 1084 1082 1082 LEU LEU B . n 
B 1 1085 GLU 1085 1083 1083 GLU GLU B . n 
B 1 1086 LEU 1086 1084 1084 LEU LEU B . n 
B 1 1087 PRO 1087 1085 1085 PRO PRO B . n 
B 1 1088 GLY 1088 1086 1086 GLY GLY B . n 
B 1 1089 PRO 1089 1087 1087 PRO PRO B . n 
B 1 1090 VAL 1090 1088 1088 VAL VAL B . n 
B 1 1091 GLY 1091 1089 1089 GLY GLY B . n 
B 1 1092 GLU 1092 1090 1090 GLU GLU B . n 
B 1 1093 ARG 1093 1091 1091 ARG ARG B . n 
B 1 1094 ASN 1094 1092 1092 ASN ASN B . n 
B 1 1095 LEU 1095 1093 1093 LEU LEU B . n 
B 1 1096 TYR 1096 1094 1094 TYR TYR B . n 
B 1 1097 THR 1097 1095 1095 THR THR B . n 
B 1 1098 LEU 1098 1096 1096 LEU LEU B . n 
B 1 1099 HIS 1099 1097 1097 HIS HIS B . n 
B 1 1100 ALA 1100 1098 1098 ALA ALA B . n 
B 1 1101 ARG 1101 1099 1099 ARG ARG B . n 
B 1 1102 GLY 1102 1100 1100 GLY GLY B . n 
B 1 1103 ARG 1103 1101 1101 ARG ARG B . n 
B 1 1104 ILE 1104 1102 1102 ILE ILE B . n 
B 1 1105 LEU 1105 1103 1103 LEU LEU B . n 
B 1 1106 LEU 1106 1104 1104 LEU LEU B . n 
B 1 1107 VAL 1107 1105 1105 VAL VAL B . n 
B 1 1108 PRO 1108 1106 1106 PRO PRO B . n 
B 1 1109 ALA 1109 1107 1107 ALA ALA B . n 
B 1 1110 THR 1110 1108 1108 THR THR B . n 
B 1 1111 GLU 1111 1109 1109 GLU GLU B . n 
B 1 1112 SER 1112 1110 1110 SER SER B . n 
B 1 1113 GLY 1113 1111 1111 GLY GLY B . n 
B 1 1114 LEU 1114 1112 1112 LEU LEU B . n 
B 1 1115 TYR 1115 1113 1113 TYR TYR B . n 
B 1 1116 HIS 1116 1114 1114 HIS HIS B . n 
B 1 1117 GLN 1117 1115 1115 GLN GLN B . n 
B 1 1118 LEU 1118 1116 1116 LEU LEU B . n 
B 1 1119 ALA 1119 1117 1117 ALA ALA B . n 
B 1 1120 ALA 1120 1118 1118 ALA ALA B . n 
B 1 1121 ALA 1121 1119 1119 ALA ALA B . n 
B 1 1122 LEU 1122 1120 1120 LEU LEU B . n 
B 1 1123 ALA 1123 1121 1121 ALA ALA B . n 
B 1 1124 THR 1124 1122 1122 THR THR B . n 
B 1 1125 GLY 1125 1123 1123 GLY GLY B . n 
B 1 1126 ASN 1126 1124 1124 ASN ASN B . n 
B 1 1127 SER 1127 1125 1125 SER SER B . n 
B 1 1128 VAL 1128 1126 1126 VAL VAL B . n 
B 1 1129 ALA 1129 1127 1127 ALA ALA B . n 
B 1 1130 ILE 1130 1128 1128 ILE ILE B . n 
B 1 1131 ASP 1131 1129 1129 ASP ASP B . n 
B 1 1132 ALA 1132 1130 1130 ALA ALA B . n 
B 1 1133 ALA 1133 1131 1131 ALA ALA B . n 
B 1 1134 SER 1134 1132 1132 SER SER B . n 
B 1 1135 GLY 1135 1133 1133 GLY GLY B . n 
B 1 1136 LEU 1136 1134 1134 LEU LEU B . n 
B 1 1137 GLN 1137 1135 1135 GLN GLN B . n 
B 1 1138 ALA 1138 1136 1136 ALA ALA B . n 
B 1 1139 SER 1139 1137 1137 SER SER B . n 
B 1 1140 LEU 1140 1138 1138 LEU LEU B . n 
B 1 1141 LYS 1141 1139 1139 LYS LYS B . n 
B 1 1142 ASN 1142 1140 1140 ASN ASN B . n 
B 1 1143 LEU 1143 1141 1141 LEU LEU B . n 
B 1 1144 PRO 1144 1142 1142 PRO PRO B . n 
B 1 1145 GLN 1145 1143 1143 GLN GLN B . n 
B 1 1146 THR 1146 1144 1144 THR THR B . n 
B 1 1147 VAL 1147 1145 1145 VAL VAL B . n 
B 1 1148 GLY 1148 1146 1146 GLY GLY B . n 
B 1 1149 LEU 1149 1147 1147 LEU LEU B . n 
B 1 1150 ARG 1150 1148 1148 ARG ARG B . n 
B 1 1151 VAL 1151 1149 1149 VAL VAL B . n 
B 1 1152 SER 1152 1150 1150 SER SER B . n 
B 1 1153 TRP 1153 1151 1151 TRP TRP B . n 
B 1 1154 SER 1154 1152 1152 SER SER B . n 
B 1 1155 LYS 1155 1153 1153 LYS LYS B . n 
B 1 1156 ASP 1156 1154 1154 ASP ASP B . n 
B 1 1157 TRP 1157 1155 1155 TRP TRP B . n 
B 1 1158 ALA 1158 1156 1156 ALA ALA B . n 
B 1 1159 ALA 1159 1157 1157 ALA ALA B . n 
B 1 1160 ASP 1160 1158 1158 ASP ASP B . n 
B 1 1161 GLY 1161 1159 1159 GLY GLY B . n 
B 1 1162 PRO 1162 1160 1160 PRO PRO B . n 
B 1 1163 PHE 1163 1161 1161 PHE PHE B . n 
B 1 1164 ALA 1164 1162 1162 ALA ALA B . n 
B 1 1165 GLY 1165 1163 1163 GLY GLY B . n 
B 1 1166 ALA 1166 1164 1164 ALA ALA B . n 
B 1 1167 LEU 1167 1165 1165 LEU LEU B . n 
B 1 1168 VAL 1168 1166 1166 VAL VAL B . n 
B 1 1169 GLU 1169 1167 1167 GLU GLU B . n 
B 1 1170 GLY 1170 1168 1168 GLY GLY B . n 
B 1 1171 ASP 1171 1169 1169 ASP ASP B . n 
B 1 1172 ALA 1172 1170 1170 ALA ALA B . n 
B 1 1173 GLU 1173 1171 1171 GLU GLU B . n 
B 1 1174 ARG 1174 1172 1172 ARG ARG B . n 
B 1 1175 ILE 1175 1173 1173 ILE ILE B . n 
B 1 1176 ARG 1176 1174 1174 ARG ARG B . n 
B 1 1177 ALA 1177 1175 1175 ALA ALA B . n 
B 1 1178 VAL 1178 1176 1176 VAL VAL B . n 
B 1 1179 ASN 1179 1177 1177 ASN ASN B . n 
B 1 1180 LYS 1180 1178 1178 LYS LYS B . n 
B 1 1181 ALA 1181 1179 1179 ALA ALA B . n 
B 1 1182 ILE 1182 1180 1180 ILE ILE B . n 
B 1 1183 ALA 1183 1181 1181 ALA ALA B . n 
B 1 1184 ALA 1184 1182 1182 ALA ALA B . n 
B 1 1185 LEU 1185 1183 1183 LEU LEU B . n 
B 1 1186 PRO 1186 1184 1184 PRO PRO B . n 
B 1 1187 GLY 1187 1185 1185 GLY GLY B . n 
B 1 1188 PRO 1188 1186 1186 PRO PRO B . n 
B 1 1189 LEU 1189 1187 1187 LEU LEU B . n 
B 1 1190 LEU 1190 1188 1188 LEU LEU B . n 
B 1 1191 LEU 1191 1189 1189 LEU LEU B . n 
B 1 1192 VAL 1192 1190 1190 VAL VAL B . n 
B 1 1193 GLN 1193 1191 1191 GLN GLN B . n 
B 1 1194 ALA 1194 1192 1192 ALA ALA B . n 
B 1 1195 ALA 1195 1193 1193 ALA ALA B . n 
B 1 1196 SER 1196 1194 1194 SER SER B . n 
B 1 1197 SER 1197 1195 1195 SER SER B . n 
B 1 1198 GLY 1198 1196 1196 GLY GLY B . n 
B 1 1199 GLU 1199 1197 1197 GLU GLU B . n 
B 1 1200 ILE 1200 1198 1198 ILE ILE B . n 
B 1 1201 ALA 1201 1199 1199 ALA ALA B . n 
B 1 1202 ARG 1202 1200 1200 ARG ARG B . n 
B 1 1203 ASN 1203 1201 1201 ASN ASN B . n 
B 1 1204 PRO 1204 1202 1202 PRO PRO B . n 
B 1 1205 ASP 1205 1203 1203 ASP ASP B . n 
B 1 1206 ALA 1206 1204 1204 ALA ALA B . n 
B 1 1207 TYR 1207 1205 1205 TYR TYR B . n 
B 1 1208 CYS 1208 1206 1206 CYS CYS B . n 
B 1 1209 LEU 1209 1207 1207 LEU LEU B . n 
B 1 1210 ASN 1210 1208 1208 ASN ASN B . n 
B 1 1211 TRP 1211 1209 1209 TRP TRP B . n 
B 1 1212 LEU 1212 1210 1210 LEU LEU B . n 
B 1 1213 VAL 1213 1211 1211 VAL VAL B . n 
B 1 1214 GLU 1214 1212 1212 GLU GLU B . n 
B 1 1215 GLU 1215 1213 1213 GLU GLU B . n 
B 1 1216 VAL 1216 1214 1214 VAL VAL B . n 
B 1 1217 SER 1217 1215 1215 SER SER B . n 
B 1 1218 ALA 1218 1216 1216 ALA ALA B . n 
B 1 1219 SER 1219 1217 1217 SER SER B . n 
B 1 1220 ILE 1220 1218 1218 ILE ILE B . n 
B 1 1221 ASN 1221 1219 1219 ASN ASN B . n 
B 1 1222 THR 1222 1220 1220 THR THR B . n 
B 1 1223 ALA 1223 1221 1221 ALA ALA B . n 
B 1 1224 ALA 1224 1222 1222 ALA ALA B . n 
B 1 1225 ALA 1225 1223 1223 ALA ALA B . n 
B 1 1226 GLY 1226 1224 1224 GLY GLY B . n 
B 1 1227 GLY 1227 1225 1225 GLY GLY B . n 
B 1 1228 ASN 1228 1226 1226 ASN ASN B . n 
B 1 1229 ALA 1229 1227 1227 ALA ALA B . n 
B 1 1230 SER 1230 1228 1228 SER SER B . n 
B 1 1231 LEU 1231 1229 1229 LEU LEU B . n 
B 1 1232 MET 1232 1230 ?    ?   ?   B . n 
B 1 1233 ALA 1233 1231 ?    ?   ?   B . n 
B 1 1234 ILE 1234 1232 ?    ?   ?   B . n 
B 1 1235 GLY 1235 1233 ?    ?   ?   B . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 53E ? ? 53E ? ? 'SUBJECT OF INVESTIGATION' ? 
2 FAD ? ? FAD ? ? 'SUBJECT OF INVESTIGATION' ? 
3 NAD ? ? NAD ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C  2  FAD 1    2001 2001 FAD FAD A . 
D  3  PEG 1    2002 2002 PEG PEG A . 
E  4  53E 1    2003 2003 53E 207 A . 
F  5  FMT 1    2004 2004 FMT FMT A . 
G  3  PEG 1    2005 2005 PEG PEG A . 
H  5  FMT 1    2006 2007 FMT FMT A . 
I  3  PEG 1    2007 2008 PEG PEG A . 
J  6  NAD 1    2008 2002 NAD NAD A . 
K  7  SO4 1    2009 2    SO4 SO4 A . 
L  7  SO4 1    2010 3    SO4 SO4 A . 
M  7  SO4 1    2011 4    SO4 SO4 A . 
N  7  SO4 1    2012 5    SO4 SO4 A . 
O  7  SO4 1    2013 7    SO4 SO4 A . 
P  8  MG  1    2014 2    MG  MG  A . 
Q  2  FAD 1    2001 2001 FAD FAD B . 
R  9  PGE 1    2002 2002 PGE PGE B . 
S  3  PEG 1    2003 2004 PEG PEG B . 
T  4  53E 1    2004 2005 53E 207 B . 
U  3  PEG 1    2005 2006 PEG PEG B . 
V  5  FMT 1    2006 2007 FMT FMT B . 
W  3  PEG 1    2007 2008 PEG PEG B . 
X  5  FMT 1    2008 2009 FMT FMT B . 
Y  10 PG4 1    2009 2010 PG4 PG4 B . 
Z  6  NAD 1    2010 2002 NAD NAD B . 
AA 7  SO4 1    2011 1    SO4 SO4 B . 
BA 7  SO4 1    2012 6    SO4 SO4 B . 
CA 8  MG  1    2013 1    MG  MG  B . 
DA 11 HOH 1    2101 1996 HOH HOH A . 
DA 11 HOH 2    2102 2107 HOH HOH A . 
DA 11 HOH 3    2103 1590 HOH HOH A . 
DA 11 HOH 4    2104 1229 HOH HOH A . 
DA 11 HOH 5    2105 2361 HOH HOH A . 
DA 11 HOH 6    2106 2467 HOH HOH A . 
DA 11 HOH 7    2107 1507 HOH HOH A . 
DA 11 HOH 8    2108 1457 HOH HOH A . 
DA 11 HOH 9    2109 340  HOH HOH A . 
DA 11 HOH 10   2110 2452 HOH HOH A . 
DA 11 HOH 11   2111 1602 HOH HOH A . 
DA 11 HOH 12   2112 1498 HOH HOH A . 
DA 11 HOH 13   2113 1775 HOH HOH A . 
DA 11 HOH 14   2114 1618 HOH HOH A . 
DA 11 HOH 15   2115 1076 HOH HOH A . 
DA 11 HOH 16   2116 810  HOH HOH A . 
DA 11 HOH 17   2117 687  HOH HOH A . 
DA 11 HOH 18   2118 2413 HOH HOH A . 
DA 11 HOH 19   2119 2265 HOH HOH A . 
DA 11 HOH 20   2120 2086 HOH HOH A . 
DA 11 HOH 21   2121 685  HOH HOH A . 
DA 11 HOH 22   2122 1404 HOH HOH A . 
DA 11 HOH 23   2123 62   HOH HOH A . 
DA 11 HOH 24   2124 1500 HOH HOH A . 
DA 11 HOH 25   2125 1851 HOH HOH A . 
DA 11 HOH 26   2126 2476 HOH HOH A . 
DA 11 HOH 27   2127 1488 HOH HOH A . 
DA 11 HOH 28   2128 921  HOH HOH A . 
DA 11 HOH 29   2129 1287 HOH HOH A . 
DA 11 HOH 30   2130 866  HOH HOH A . 
DA 11 HOH 31   2131 909  HOH HOH A . 
DA 11 HOH 32   2132 1988 HOH HOH A . 
DA 11 HOH 33   2133 1704 HOH HOH A . 
DA 11 HOH 34   2134 1265 HOH HOH A . 
DA 11 HOH 35   2135 818  HOH HOH A . 
DA 11 HOH 36   2136 2403 HOH HOH A . 
DA 11 HOH 37   2137 625  HOH HOH A . 
DA 11 HOH 38   2138 396  HOH HOH A . 
DA 11 HOH 39   2139 1371 HOH HOH A . 
DA 11 HOH 40   2140 754  HOH HOH A . 
DA 11 HOH 41   2141 868  HOH HOH A . 
DA 11 HOH 42   2142 2489 HOH HOH A . 
DA 11 HOH 43   2143 471  HOH HOH A . 
DA 11 HOH 44   2144 751  HOH HOH A . 
DA 11 HOH 45   2145 1559 HOH HOH A . 
DA 11 HOH 46   2146 431  HOH HOH A . 
DA 11 HOH 47   2147 405  HOH HOH A . 
DA 11 HOH 48   2148 1566 HOH HOH A . 
DA 11 HOH 49   2149 411  HOH HOH A . 
DA 11 HOH 50   2150 1804 HOH HOH A . 
DA 11 HOH 51   2151 2400 HOH HOH A . 
DA 11 HOH 52   2152 1810 HOH HOH A . 
DA 11 HOH 53   2153 1336 HOH HOH A . 
DA 11 HOH 54   2154 1513 HOH HOH A . 
DA 11 HOH 55   2155 701  HOH HOH A . 
DA 11 HOH 56   2156 731  HOH HOH A . 
DA 11 HOH 57   2157 996  HOH HOH A . 
DA 11 HOH 58   2158 1122 HOH HOH A . 
DA 11 HOH 59   2159 1501 HOH HOH A . 
DA 11 HOH 60   2160 2422 HOH HOH A . 
DA 11 HOH 61   2161 1769 HOH HOH A . 
DA 11 HOH 62   2162 828  HOH HOH A . 
DA 11 HOH 63   2163 706  HOH HOH A . 
DA 11 HOH 64   2164 1514 HOH HOH A . 
DA 11 HOH 65   2165 653  HOH HOH A . 
DA 11 HOH 66   2166 1183 HOH HOH A . 
DA 11 HOH 67   2167 18   HOH HOH A . 
DA 11 HOH 68   2168 791  HOH HOH A . 
DA 11 HOH 69   2169 202  HOH HOH A . 
DA 11 HOH 70   2170 558  HOH HOH A . 
DA 11 HOH 71   2171 1051 HOH HOH A . 
DA 11 HOH 72   2172 1730 HOH HOH A . 
DA 11 HOH 73   2173 550  HOH HOH A . 
DA 11 HOH 74   2174 1886 HOH HOH A . 
DA 11 HOH 75   2175 32   HOH HOH A . 
DA 11 HOH 76   2176 1619 HOH HOH A . 
DA 11 HOH 77   2177 1997 HOH HOH A . 
DA 11 HOH 78   2178 1961 HOH HOH A . 
DA 11 HOH 79   2179 113  HOH HOH A . 
DA 11 HOH 80   2180 1253 HOH HOH A . 
DA 11 HOH 81   2181 432  HOH HOH A . 
DA 11 HOH 82   2182 176  HOH HOH A . 
DA 11 HOH 83   2183 197  HOH HOH A . 
DA 11 HOH 84   2184 757  HOH HOH A . 
DA 11 HOH 85   2185 976  HOH HOH A . 
DA 11 HOH 86   2186 2454 HOH HOH A . 
DA 11 HOH 87   2187 2346 HOH HOH A . 
DA 11 HOH 88   2188 841  HOH HOH A . 
DA 11 HOH 89   2189 1197 HOH HOH A . 
DA 11 HOH 90   2190 76   HOH HOH A . 
DA 11 HOH 91   2191 1394 HOH HOH A . 
DA 11 HOH 92   2192 2155 HOH HOH A . 
DA 11 HOH 93   2193 467  HOH HOH A . 
DA 11 HOH 94   2194 555  HOH HOH A . 
DA 11 HOH 95   2195 1642 HOH HOH A . 
DA 11 HOH 96   2196 178  HOH HOH A . 
DA 11 HOH 97   2197 660  HOH HOH A . 
DA 11 HOH 98   2198 620  HOH HOH A . 
DA 11 HOH 99   2199 527  HOH HOH A . 
DA 11 HOH 100  2200 2028 HOH HOH A . 
DA 11 HOH 101  2201 420  HOH HOH A . 
DA 11 HOH 102  2202 1005 HOH HOH A . 
DA 11 HOH 103  2203 54   HOH HOH A . 
DA 11 HOH 104  2204 1968 HOH HOH A . 
DA 11 HOH 105  2205 758  HOH HOH A . 
DA 11 HOH 106  2206 2235 HOH HOH A . 
DA 11 HOH 107  2207 1952 HOH HOH A . 
DA 11 HOH 108  2208 1364 HOH HOH A . 
DA 11 HOH 109  2209 1734 HOH HOH A . 
DA 11 HOH 110  2210 1239 HOH HOH A . 
DA 11 HOH 111  2211 253  HOH HOH A . 
DA 11 HOH 112  2212 380  HOH HOH A . 
DA 11 HOH 113  2213 813  HOH HOH A . 
DA 11 HOH 114  2214 16   HOH HOH A . 
DA 11 HOH 115  2215 1750 HOH HOH A . 
DA 11 HOH 116  2216 2014 HOH HOH A . 
DA 11 HOH 117  2217 736  HOH HOH A . 
DA 11 HOH 118  2218 1986 HOH HOH A . 
DA 11 HOH 119  2219 715  HOH HOH A . 
DA 11 HOH 120  2220 1036 HOH HOH A . 
DA 11 HOH 121  2221 894  HOH HOH A . 
DA 11 HOH 122  2222 1271 HOH HOH A . 
DA 11 HOH 123  2223 500  HOH HOH A . 
DA 11 HOH 124  2224 924  HOH HOH A . 
DA 11 HOH 125  2225 408  HOH HOH A . 
DA 11 HOH 126  2226 1468 HOH HOH A . 
DA 11 HOH 127  2227 1765 HOH HOH A . 
DA 11 HOH 128  2228 816  HOH HOH A . 
DA 11 HOH 129  2229 1532 HOH HOH A . 
DA 11 HOH 130  2230 1756 HOH HOH A . 
DA 11 HOH 131  2231 570  HOH HOH A . 
DA 11 HOH 132  2232 1225 HOH HOH A . 
DA 11 HOH 133  2233 1738 HOH HOH A . 
DA 11 HOH 134  2234 806  HOH HOH A . 
DA 11 HOH 135  2235 12   HOH HOH A . 
DA 11 HOH 136  2236 413  HOH HOH A . 
DA 11 HOH 137  2237 462  HOH HOH A . 
DA 11 HOH 138  2238 269  HOH HOH A . 
DA 11 HOH 139  2239 441  HOH HOH A . 
DA 11 HOH 140  2240 1965 HOH HOH A . 
DA 11 HOH 141  2241 1043 HOH HOH A . 
DA 11 HOH 142  2242 990  HOH HOH A . 
DA 11 HOH 143  2243 852  HOH HOH A . 
DA 11 HOH 144  2244 1537 HOH HOH A . 
DA 11 HOH 145  2245 1846 HOH HOH A . 
DA 11 HOH 146  2246 2421 HOH HOH A . 
DA 11 HOH 147  2247 1203 HOH HOH A . 
DA 11 HOH 148  2248 2054 HOH HOH A . 
DA 11 HOH 149  2249 2308 HOH HOH A . 
DA 11 HOH 150  2250 1429 HOH HOH A . 
DA 11 HOH 151  2251 2142 HOH HOH A . 
DA 11 HOH 152  2252 60   HOH HOH A . 
DA 11 HOH 153  2253 907  HOH HOH A . 
DA 11 HOH 154  2254 1147 HOH HOH A . 
DA 11 HOH 155  2255 1659 HOH HOH A . 
DA 11 HOH 156  2256 779  HOH HOH A . 
DA 11 HOH 157  2257 862  HOH HOH A . 
DA 11 HOH 158  2258 587  HOH HOH A . 
DA 11 HOH 159  2259 1861 HOH HOH A . 
DA 11 HOH 160  2260 503  HOH HOH A . 
DA 11 HOH 161  2261 370  HOH HOH A . 
DA 11 HOH 162  2262 611  HOH HOH A . 
DA 11 HOH 163  2263 93   HOH HOH A . 
DA 11 HOH 164  2264 617  HOH HOH A . 
DA 11 HOH 165  2265 1152 HOH HOH A . 
DA 11 HOH 166  2266 1344 HOH HOH A . 
DA 11 HOH 167  2267 592  HOH HOH A . 
DA 11 HOH 168  2268 361  HOH HOH A . 
DA 11 HOH 169  2269 249  HOH HOH A . 
DA 11 HOH 170  2270 392  HOH HOH A . 
DA 11 HOH 171  2271 321  HOH HOH A . 
DA 11 HOH 172  2272 283  HOH HOH A . 
DA 11 HOH 173  2273 978  HOH HOH A . 
DA 11 HOH 174  2274 273  HOH HOH A . 
DA 11 HOH 175  2275 1273 HOH HOH A . 
DA 11 HOH 176  2276 544  HOH HOH A . 
DA 11 HOH 177  2277 1176 HOH HOH A . 
DA 11 HOH 178  2278 1848 HOH HOH A . 
DA 11 HOH 179  2279 1650 HOH HOH A . 
DA 11 HOH 180  2280 1007 HOH HOH A . 
DA 11 HOH 181  2281 1692 HOH HOH A . 
DA 11 HOH 182  2282 867  HOH HOH A . 
DA 11 HOH 183  2283 137  HOH HOH A . 
DA 11 HOH 184  2284 1045 HOH HOH A . 
DA 11 HOH 185  2285 1967 HOH HOH A . 
DA 11 HOH 186  2286 693  HOH HOH A . 
DA 11 HOH 187  2287 596  HOH HOH A . 
DA 11 HOH 188  2288 1575 HOH HOH A . 
DA 11 HOH 189  2289 922  HOH HOH A . 
DA 11 HOH 190  2290 359  HOH HOH A . 
DA 11 HOH 191  2291 135  HOH HOH A . 
DA 11 HOH 192  2292 191  HOH HOH A . 
DA 11 HOH 193  2293 241  HOH HOH A . 
DA 11 HOH 194  2294 2095 HOH HOH A . 
DA 11 HOH 195  2295 207  HOH HOH A . 
DA 11 HOH 196  2296 260  HOH HOH A . 
DA 11 HOH 197  2297 255  HOH HOH A . 
DA 11 HOH 198  2298 209  HOH HOH A . 
DA 11 HOH 199  2299 1135 HOH HOH A . 
DA 11 HOH 200  2300 1100 HOH HOH A . 
DA 11 HOH 201  2301 294  HOH HOH A . 
DA 11 HOH 202  2302 128  HOH HOH A . 
DA 11 HOH 203  2303 629  HOH HOH A . 
DA 11 HOH 204  2304 1161 HOH HOH A . 
DA 11 HOH 205  2305 1767 HOH HOH A . 
DA 11 HOH 206  2306 107  HOH HOH A . 
DA 11 HOH 207  2307 869  HOH HOH A . 
DA 11 HOH 208  2308 1842 HOH HOH A . 
DA 11 HOH 209  2309 1628 HOH HOH A . 
DA 11 HOH 210  2310 817  HOH HOH A . 
DA 11 HOH 211  2311 1226 HOH HOH A . 
DA 11 HOH 212  2312 616  HOH HOH A . 
DA 11 HOH 213  2313 966  HOH HOH A . 
DA 11 HOH 214  2314 1180 HOH HOH A . 
DA 11 HOH 215  2315 198  HOH HOH A . 
DA 11 HOH 216  2316 718  HOH HOH A . 
DA 11 HOH 217  2317 760  HOH HOH A . 
DA 11 HOH 218  2318 676  HOH HOH A . 
DA 11 HOH 219  2319 48   HOH HOH A . 
DA 11 HOH 220  2320 1300 HOH HOH A . 
DA 11 HOH 221  2321 945  HOH HOH A . 
DA 11 HOH 222  2322 1241 HOH HOH A . 
DA 11 HOH 223  2323 109  HOH HOH A . 
DA 11 HOH 224  2324 824  HOH HOH A . 
DA 11 HOH 225  2325 195  HOH HOH A . 
DA 11 HOH 226  2326 605  HOH HOH A . 
DA 11 HOH 227  2327 614  HOH HOH A . 
DA 11 HOH 228  2328 1606 HOH HOH A . 
DA 11 HOH 229  2329 2073 HOH HOH A . 
DA 11 HOH 230  2330 1486 HOH HOH A . 
DA 11 HOH 231  2331 1181 HOH HOH A . 
DA 11 HOH 232  2332 492  HOH HOH A . 
DA 11 HOH 233  2333 73   HOH HOH A . 
DA 11 HOH 234  2334 599  HOH HOH A . 
DA 11 HOH 235  2335 674  HOH HOH A . 
DA 11 HOH 236  2336 377  HOH HOH A . 
DA 11 HOH 237  2337 1294 HOH HOH A . 
DA 11 HOH 238  2338 292  HOH HOH A . 
DA 11 HOH 239  2339 501  HOH HOH A . 
DA 11 HOH 240  2340 332  HOH HOH A . 
DA 11 HOH 241  2341 1096 HOH HOH A . 
DA 11 HOH 242  2342 2488 HOH HOH A . 
DA 11 HOH 243  2343 2382 HOH HOH A . 
DA 11 HOH 244  2344 1063 HOH HOH A . 
DA 11 HOH 245  2345 157  HOH HOH A . 
DA 11 HOH 246  2346 2365 HOH HOH A . 
DA 11 HOH 247  2347 2062 HOH HOH A . 
DA 11 HOH 248  2348 1102 HOH HOH A . 
DA 11 HOH 249  2349 320  HOH HOH A . 
DA 11 HOH 250  2350 1574 HOH HOH A . 
DA 11 HOH 251  2351 301  HOH HOH A . 
DA 11 HOH 252  2352 2390 HOH HOH A . 
DA 11 HOH 253  2353 1092 HOH HOH A . 
DA 11 HOH 254  2354 1805 HOH HOH A . 
DA 11 HOH 255  2355 1323 HOH HOH A . 
DA 11 HOH 256  2356 1491 HOH HOH A . 
DA 11 HOH 257  2357 2127 HOH HOH A . 
DA 11 HOH 258  2358 2368 HOH HOH A . 
DA 11 HOH 259  2359 15   HOH HOH A . 
DA 11 HOH 260  2360 899  HOH HOH A . 
DA 11 HOH 261  2361 1770 HOH HOH A . 
DA 11 HOH 262  2362 79   HOH HOH A . 
DA 11 HOH 263  2363 1195 HOH HOH A . 
DA 11 HOH 264  2364 162  HOH HOH A . 
DA 11 HOH 265  2365 101  HOH HOH A . 
DA 11 HOH 266  2366 1553 HOH HOH A . 
DA 11 HOH 267  2367 2019 HOH HOH A . 
DA 11 HOH 268  2368 2070 HOH HOH A . 
DA 11 HOH 269  2369 44   HOH HOH A . 
DA 11 HOH 270  2370 589  HOH HOH A . 
DA 11 HOH 271  2371 251  HOH HOH A . 
DA 11 HOH 272  2372 1445 HOH HOH A . 
DA 11 HOH 273  2373 2164 HOH HOH A . 
DA 11 HOH 274  2374 1017 HOH HOH A . 
DA 11 HOH 275  2375 100  HOH HOH A . 
DA 11 HOH 276  2376 1200 HOH HOH A . 
DA 11 HOH 277  2377 181  HOH HOH A . 
DA 11 HOH 278  2378 151  HOH HOH A . 
DA 11 HOH 279  2379 854  HOH HOH A . 
DA 11 HOH 280  2380 1783 HOH HOH A . 
DA 11 HOH 281  2381 1731 HOH HOH A . 
DA 11 HOH 282  2382 652  HOH HOH A . 
DA 11 HOH 283  2383 2362 HOH HOH A . 
DA 11 HOH 284  2384 19   HOH HOH A . 
DA 11 HOH 285  2385 1206 HOH HOH A . 
DA 11 HOH 286  2386 184  HOH HOH A . 
DA 11 HOH 287  2387 1000 HOH HOH A . 
DA 11 HOH 288  2388 1964 HOH HOH A . 
DA 11 HOH 289  2389 455  HOH HOH A . 
DA 11 HOH 290  2390 277  HOH HOH A . 
DA 11 HOH 291  2391 246  HOH HOH A . 
DA 11 HOH 292  2392 778  HOH HOH A . 
DA 11 HOH 293  2393 243  HOH HOH A . 
DA 11 HOH 294  2394 2057 HOH HOH A . 
DA 11 HOH 295  2395 872  HOH HOH A . 
DA 11 HOH 296  2396 1383 HOH HOH A . 
DA 11 HOH 297  2397 516  HOH HOH A . 
DA 11 HOH 298  2398 658  HOH HOH A . 
DA 11 HOH 299  2399 11   HOH HOH A . 
DA 11 HOH 300  2400 1536 HOH HOH A . 
DA 11 HOH 301  2401 221  HOH HOH A . 
DA 11 HOH 302  2402 504  HOH HOH A . 
DA 11 HOH 303  2403 520  HOH HOH A . 
DA 11 HOH 304  2404 328  HOH HOH A . 
DA 11 HOH 305  2405 437  HOH HOH A . 
DA 11 HOH 306  2406 165  HOH HOH A . 
DA 11 HOH 307  2407 231  HOH HOH A . 
DA 11 HOH 308  2408 878  HOH HOH A . 
DA 11 HOH 309  2409 1386 HOH HOH A . 
DA 11 HOH 310  2410 1052 HOH HOH A . 
DA 11 HOH 311  2411 158  HOH HOH A . 
DA 11 HOH 312  2412 159  HOH HOH A . 
DA 11 HOH 313  2413 1613 HOH HOH A . 
DA 11 HOH 314  2414 782  HOH HOH A . 
DA 11 HOH 315  2415 2167 HOH HOH A . 
DA 11 HOH 316  2416 1525 HOH HOH A . 
DA 11 HOH 317  2417 312  HOH HOH A . 
DA 11 HOH 318  2418 80   HOH HOH A . 
DA 11 HOH 319  2419 61   HOH HOH A . 
DA 11 HOH 320  2420 2248 HOH HOH A . 
DA 11 HOH 321  2421 726  HOH HOH A . 
DA 11 HOH 322  2422 239  HOH HOH A . 
DA 11 HOH 323  2423 1396 HOH HOH A . 
DA 11 HOH 324  2424 387  HOH HOH A . 
DA 11 HOH 325  2425 802  HOH HOH A . 
DA 11 HOH 326  2426 226  HOH HOH A . 
DA 11 HOH 327  2427 689  HOH HOH A . 
DA 11 HOH 328  2428 343  HOH HOH A . 
DA 11 HOH 329  2429 2256 HOH HOH A . 
DA 11 HOH 330  2430 2192 HOH HOH A . 
DA 11 HOH 331  2431 610  HOH HOH A . 
DA 11 HOH 332  2432 105  HOH HOH A . 
DA 11 HOH 333  2433 530  HOH HOH A . 
DA 11 HOH 334  2434 63   HOH HOH A . 
DA 11 HOH 335  2435 2144 HOH HOH A . 
DA 11 HOH 336  2436 136  HOH HOH A . 
DA 11 HOH 337  2437 144  HOH HOH A . 
DA 11 HOH 338  2438 635  HOH HOH A . 
DA 11 HOH 339  2439 1360 HOH HOH A . 
DA 11 HOH 340  2440 351  HOH HOH A . 
DA 11 HOH 341  2441 454  HOH HOH A . 
DA 11 HOH 342  2442 1059 HOH HOH A . 
DA 11 HOH 343  2443 1545 HOH HOH A . 
DA 11 HOH 344  2444 1148 HOH HOH A . 
DA 11 HOH 345  2445 1298 HOH HOH A . 
DA 11 HOH 346  2446 933  HOH HOH A . 
DA 11 HOH 347  2447 1683 HOH HOH A . 
DA 11 HOH 348  2448 651  HOH HOH A . 
DA 11 HOH 349  2449 25   HOH HOH A . 
DA 11 HOH 350  2450 55   HOH HOH A . 
DA 11 HOH 351  2451 2341 HOH HOH A . 
DA 11 HOH 352  2452 1134 HOH HOH A . 
DA 11 HOH 353  2453 803  HOH HOH A . 
DA 11 HOH 354  2454 29   HOH HOH A . 
DA 11 HOH 355  2455 164  HOH HOH A . 
DA 11 HOH 356  2456 783  HOH HOH A . 
DA 11 HOH 357  2457 1696 HOH HOH A . 
DA 11 HOH 358  2458 23   HOH HOH A . 
DA 11 HOH 359  2459 2251 HOH HOH A . 
DA 11 HOH 360  2460 276  HOH HOH A . 
DA 11 HOH 361  2461 223  HOH HOH A . 
DA 11 HOH 362  2462 920  HOH HOH A . 
DA 11 HOH 363  2463 1741 HOH HOH A . 
DA 11 HOH 364  2464 2059 HOH HOH A . 
DA 11 HOH 365  2465 1481 HOH HOH A . 
DA 11 HOH 366  2466 1155 HOH HOH A . 
DA 11 HOH 367  2467 1289 HOH HOH A . 
DA 11 HOH 368  2468 633  HOH HOH A . 
DA 11 HOH 369  2469 194  HOH HOH A . 
DA 11 HOH 370  2470 551  HOH HOH A . 
DA 11 HOH 371  2471 213  HOH HOH A . 
DA 11 HOH 372  2472 708  HOH HOH A . 
DA 11 HOH 373  2473 2074 HOH HOH A . 
DA 11 HOH 374  2474 127  HOH HOH A . 
DA 11 HOH 375  2475 2412 HOH HOH A . 
DA 11 HOH 376  2476 1262 HOH HOH A . 
DA 11 HOH 377  2477 233  HOH HOH A . 
DA 11 HOH 378  2478 124  HOH HOH A . 
DA 11 HOH 379  2479 300  HOH HOH A . 
DA 11 HOH 380  2480 374  HOH HOH A . 
DA 11 HOH 381  2481 27   HOH HOH A . 
DA 11 HOH 382  2482 1329 HOH HOH A . 
DA 11 HOH 383  2483 600  HOH HOH A . 
DA 11 HOH 384  2484 1306 HOH HOH A . 
DA 11 HOH 385  2485 946  HOH HOH A . 
DA 11 HOH 386  2486 1157 HOH HOH A . 
DA 11 HOH 387  2487 28   HOH HOH A . 
DA 11 HOH 388  2488 212  HOH HOH A . 
DA 11 HOH 389  2489 1420 HOH HOH A . 
DA 11 HOH 390  2490 2126 HOH HOH A . 
DA 11 HOH 391  2491 1398 HOH HOH A . 
DA 11 HOH 392  2492 1034 HOH HOH A . 
DA 11 HOH 393  2493 728  HOH HOH A . 
DA 11 HOH 394  2494 497  HOH HOH A . 
DA 11 HOH 395  2495 217  HOH HOH A . 
DA 11 HOH 396  2496 161  HOH HOH A . 
DA 11 HOH 397  2497 1110 HOH HOH A . 
DA 11 HOH 398  2498 683  HOH HOH A . 
DA 11 HOH 399  2499 67   HOH HOH A . 
DA 11 HOH 400  2500 86   HOH HOH A . 
DA 11 HOH 401  2501 1990 HOH HOH A . 
DA 11 HOH 402  2502 450  HOH HOH A . 
DA 11 HOH 403  2503 1283 HOH HOH A . 
DA 11 HOH 404  2504 1084 HOH HOH A . 
DA 11 HOH 405  2505 318  HOH HOH A . 
DA 11 HOH 406  2506 1334 HOH HOH A . 
DA 11 HOH 407  2507 545  HOH HOH A . 
DA 11 HOH 408  2508 532  HOH HOH A . 
DA 11 HOH 409  2509 111  HOH HOH A . 
DA 11 HOH 410  2510 2338 HOH HOH A . 
DA 11 HOH 411  2511 339  HOH HOH A . 
DA 11 HOH 412  2512 2233 HOH HOH A . 
DA 11 HOH 413  2513 1194 HOH HOH A . 
DA 11 HOH 414  2514 2001 HOH HOH A . 
DA 11 HOH 415  2515 1972 HOH HOH A . 
DA 11 HOH 416  2516 156  HOH HOH A . 
DA 11 HOH 417  2517 2450 HOH HOH A . 
DA 11 HOH 418  2518 42   HOH HOH A . 
DA 11 HOH 419  2519 519  HOH HOH A . 
DA 11 HOH 420  2520 1129 HOH HOH A . 
DA 11 HOH 421  2521 957  HOH HOH A . 
DA 11 HOH 422  2522 358  HOH HOH A . 
DA 11 HOH 423  2523 214  HOH HOH A . 
DA 11 HOH 424  2524 2326 HOH HOH A . 
DA 11 HOH 425  2525 256  HOH HOH A . 
DA 11 HOH 426  2526 1044 HOH HOH A . 
DA 11 HOH 427  2527 2146 HOH HOH A . 
DA 11 HOH 428  2528 56   HOH HOH A . 
DA 11 HOH 429  2529 154  HOH HOH A . 
DA 11 HOH 430  2530 711  HOH HOH A . 
DA 11 HOH 431  2531 229  HOH HOH A . 
DA 11 HOH 432  2532 1753 HOH HOH A . 
DA 11 HOH 433  2533 1878 HOH HOH A . 
DA 11 HOH 434  2534 2328 HOH HOH A . 
DA 11 HOH 435  2535 1169 HOH HOH A . 
DA 11 HOH 436  2536 149  HOH HOH A . 
DA 11 HOH 437  2537 640  HOH HOH A . 
DA 11 HOH 438  2538 1073 HOH HOH A . 
DA 11 HOH 439  2539 473  HOH HOH A . 
DA 11 HOH 440  2540 2275 HOH HOH A . 
DA 11 HOH 441  2541 1499 HOH HOH A . 
DA 11 HOH 442  2542 547  HOH HOH A . 
DA 11 HOH 443  2543 1085 HOH HOH A . 
DA 11 HOH 444  2544 126  HOH HOH A . 
DA 11 HOH 445  2545 329  HOH HOH A . 
DA 11 HOH 446  2546 238  HOH HOH A . 
DA 11 HOH 447  2547 1780 HOH HOH A . 
DA 11 HOH 448  2548 1046 HOH HOH A . 
DA 11 HOH 449  2549 846  HOH HOH A . 
DA 11 HOH 450  2550 35   HOH HOH A . 
DA 11 HOH 451  2551 1407 HOH HOH A . 
DA 11 HOH 452  2552 1399 HOH HOH A . 
DA 11 HOH 453  2553 1949 HOH HOH A . 
DA 11 HOH 454  2554 425  HOH HOH A . 
DA 11 HOH 455  2555 313  HOH HOH A . 
DA 11 HOH 456  2556 714  HOH HOH A . 
DA 11 HOH 457  2557 1489 HOH HOH A . 
DA 11 HOH 458  2558 452  HOH HOH A . 
DA 11 HOH 459  2559 2089 HOH HOH A . 
DA 11 HOH 460  2560 793  HOH HOH A . 
DA 11 HOH 461  2561 842  HOH HOH A . 
DA 11 HOH 462  2562 484  HOH HOH A . 
DA 11 HOH 463  2563 368  HOH HOH A . 
DA 11 HOH 464  2564 612  HOH HOH A . 
DA 11 HOH 465  2565 2484 HOH HOH A . 
DA 11 HOH 466  2566 1668 HOH HOH A . 
DA 11 HOH 467  2567 1269 HOH HOH A . 
DA 11 HOH 468  2568 325  HOH HOH A . 
DA 11 HOH 469  2569 563  HOH HOH A . 
DA 11 HOH 470  2570 1653 HOH HOH A . 
DA 11 HOH 471  2571 962  HOH HOH A . 
DA 11 HOH 472  2572 1366 HOH HOH A . 
DA 11 HOH 473  2573 106  HOH HOH A . 
DA 11 HOH 474  2574 1166 HOH HOH A . 
DA 11 HOH 475  2575 391  HOH HOH A . 
DA 11 HOH 476  2576 426  HOH HOH A . 
DA 11 HOH 477  2577 304  HOH HOH A . 
DA 11 HOH 478  2578 634  HOH HOH A . 
DA 11 HOH 479  2579 22   HOH HOH A . 
DA 11 HOH 480  2580 1167 HOH HOH A . 
DA 11 HOH 481  2581 822  HOH HOH A . 
DA 11 HOH 482  2582 528  HOH HOH A . 
DA 11 HOH 483  2583 1332 HOH HOH A . 
DA 11 HOH 484  2584 427  HOH HOH A . 
DA 11 HOH 485  2585 1301 HOH HOH A . 
DA 11 HOH 486  2586 792  HOH HOH A . 
DA 11 HOH 487  2587 549  HOH HOH A . 
DA 11 HOH 488  2588 215  HOH HOH A . 
DA 11 HOH 489  2589 193  HOH HOH A . 
DA 11 HOH 490  2590 155  HOH HOH A . 
DA 11 HOH 491  2591 430  HOH HOH A . 
DA 11 HOH 492  2592 2163 HOH HOH A . 
DA 11 HOH 493  2593 904  HOH HOH A . 
DA 11 HOH 494  2594 942  HOH HOH A . 
DA 11 HOH 495  2595 477  HOH HOH A . 
DA 11 HOH 496  2596 1644 HOH HOH A . 
DA 11 HOH 497  2597 2002 HOH HOH A . 
DA 11 HOH 498  2598 419  HOH HOH A . 
DA 11 HOH 499  2599 179  HOH HOH A . 
DA 11 HOH 500  2600 2133 HOH HOH A . 
DA 11 HOH 501  2601 2405 HOH HOH A . 
DA 11 HOH 502  2602 1809 HOH HOH A . 
DA 11 HOH 503  2603 362  HOH HOH A . 
DA 11 HOH 504  2604 478  HOH HOH A . 
DA 11 HOH 505  2605 2333 HOH HOH A . 
DA 11 HOH 506  2606 447  HOH HOH A . 
DA 11 HOH 507  2607 984  HOH HOH A . 
DA 11 HOH 508  2608 1091 HOH HOH A . 
DA 11 HOH 509  2609 671  HOH HOH A . 
DA 11 HOH 510  2610 33   HOH HOH A . 
DA 11 HOH 511  2611 1685 HOH HOH A . 
DA 11 HOH 512  2612 258  HOH HOH A . 
DA 11 HOH 513  2613 170  HOH HOH A . 
DA 11 HOH 514  2614 2284 HOH HOH A . 
DA 11 HOH 515  2615 201  HOH HOH A . 
DA 11 HOH 516  2616 644  HOH HOH A . 
DA 11 HOH 517  2617 1829 HOH HOH A . 
DA 11 HOH 518  2618 2150 HOH HOH A . 
DA 11 HOH 519  2619 692  HOH HOH A . 
DA 11 HOH 520  2620 1605 HOH HOH A . 
DA 11 HOH 521  2621 344  HOH HOH A . 
DA 11 HOH 522  2622 703  HOH HOH A . 
DA 11 HOH 523  2623 1327 HOH HOH A . 
DA 11 HOH 524  2624 514  HOH HOH A . 
DA 11 HOH 525  2625 604  HOH HOH A . 
DA 11 HOH 526  2626 618  HOH HOH A . 
DA 11 HOH 527  2627 90   HOH HOH A . 
DA 11 HOH 528  2628 1958 HOH HOH A . 
DA 11 HOH 529  2629 1670 HOH HOH A . 
DA 11 HOH 530  2630 1    HOH HOH A . 
DA 11 HOH 531  2631 40   HOH HOH A . 
DA 11 HOH 532  2632 378  HOH HOH A . 
DA 11 HOH 533  2633 1256 HOH HOH A . 
DA 11 HOH 534  2634 1038 HOH HOH A . 
DA 11 HOH 535  2635 369  HOH HOH A . 
DA 11 HOH 536  2636 873  HOH HOH A . 
DA 11 HOH 537  2637 2081 HOH HOH A . 
DA 11 HOH 538  2638 2140 HOH HOH A . 
DA 11 HOH 539  2639 1744 HOH HOH A . 
DA 11 HOH 540  2640 2261 HOH HOH A . 
DA 11 HOH 541  2641 556  HOH HOH A . 
DA 11 HOH 542  2642 480  HOH HOH A . 
DA 11 HOH 543  2643 1390 HOH HOH A . 
DA 11 HOH 544  2644 1624 HOH HOH A . 
DA 11 HOH 545  2645 407  HOH HOH A . 
DA 11 HOH 546  2646 502  HOH HOH A . 
DA 11 HOH 547  2647 1854 HOH HOH A . 
DA 11 HOH 548  2648 267  HOH HOH A . 
DA 11 HOH 549  2649 402  HOH HOH A . 
DA 11 HOH 550  2650 244  HOH HOH A . 
DA 11 HOH 551  2651 673  HOH HOH A . 
DA 11 HOH 552  2652 290  HOH HOH A . 
DA 11 HOH 553  2653 1707 HOH HOH A . 
DA 11 HOH 554  2654 730  HOH HOH A . 
DA 11 HOH 555  2655 1716 HOH HOH A . 
DA 11 HOH 556  2656 790  HOH HOH A . 
DA 11 HOH 557  2657 1009 HOH HOH A . 
DA 11 HOH 558  2658 1083 HOH HOH A . 
DA 11 HOH 559  2659 1679 HOH HOH A . 
DA 11 HOH 560  2660 1165 HOH HOH A . 
DA 11 HOH 561  2661 120  HOH HOH A . 
DA 11 HOH 562  2662 345  HOH HOH A . 
DA 11 HOH 563  2663 1308 HOH HOH A . 
DA 11 HOH 564  2664 1222 HOH HOH A . 
DA 11 HOH 565  2665 1056 HOH HOH A . 
DA 11 HOH 566  2666 99   HOH HOH A . 
DA 11 HOH 567  2667 809  HOH HOH A . 
DA 11 HOH 568  2668 1295 HOH HOH A . 
DA 11 HOH 569  2669 9    HOH HOH A . 
DA 11 HOH 570  2670 330  HOH HOH A . 
DA 11 HOH 571  2671 81   HOH HOH A . 
DA 11 HOH 572  2672 1079 HOH HOH A . 
DA 11 HOH 573  2673 1275 HOH HOH A . 
DA 11 HOH 574  2674 357  HOH HOH A . 
DA 11 HOH 575  2675 4    HOH HOH A . 
DA 11 HOH 576  2676 958  HOH HOH A . 
DA 11 HOH 577  2677 1172 HOH HOH A . 
DA 11 HOH 578  2678 1027 HOH HOH A . 
DA 11 HOH 579  2679 1010 HOH HOH A . 
DA 11 HOH 580  2680 316  HOH HOH A . 
DA 11 HOH 581  2681 248  HOH HOH A . 
DA 11 HOH 582  2682 1163 HOH HOH A . 
DA 11 HOH 583  2683 720  HOH HOH A . 
DA 11 HOH 584  2684 1067 HOH HOH A . 
DA 11 HOH 585  2685 451  HOH HOH A . 
DA 11 HOH 586  2686 1324 HOH HOH A . 
DA 11 HOH 587  2687 2323 HOH HOH A . 
DA 11 HOH 588  2688 1039 HOH HOH A . 
DA 11 HOH 589  2689 360  HOH HOH A . 
DA 11 HOH 590  2690 103  HOH HOH A . 
DA 11 HOH 591  2691 1261 HOH HOH A . 
DA 11 HOH 592  2692 2006 HOH HOH A . 
DA 11 HOH 593  2693 1473 HOH HOH A . 
DA 11 HOH 594  2694 531  HOH HOH A . 
DA 11 HOH 595  2695 2240 HOH HOH A . 
DA 11 HOH 596  2696 1228 HOH HOH A . 
DA 11 HOH 597  2697 2436 HOH HOH A . 
DA 11 HOH 598  2698 1542 HOH HOH A . 
DA 11 HOH 599  2699 840  HOH HOH A . 
DA 11 HOH 600  2700 347  HOH HOH A . 
DA 11 HOH 601  2701 967  HOH HOH A . 
DA 11 HOH 602  2702 627  HOH HOH A . 
DA 11 HOH 603  2703 1057 HOH HOH A . 
DA 11 HOH 604  2704 695  HOH HOH A . 
DA 11 HOH 605  2705 1467 HOH HOH A . 
DA 11 HOH 606  2706 643  HOH HOH A . 
DA 11 HOH 607  2707 1291 HOH HOH A . 
DA 11 HOH 608  2708 2226 HOH HOH A . 
DA 11 HOH 609  2709 709  HOH HOH A . 
DA 11 HOH 610  2710 1139 HOH HOH A . 
DA 11 HOH 611  2711 1109 HOH HOH A . 
DA 11 HOH 612  2712 50   HOH HOH A . 
DA 11 HOH 613  2713 568  HOH HOH A . 
DA 11 HOH 614  2714 169  HOH HOH A . 
DA 11 HOH 615  2715 1573 HOH HOH A . 
DA 11 HOH 616  2716 422  HOH HOH A . 
DA 11 HOH 617  2717 567  HOH HOH A . 
DA 11 HOH 618  2718 274  HOH HOH A . 
DA 11 HOH 619  2719 1072 HOH HOH A . 
DA 11 HOH 620  2720 982  HOH HOH A . 
DA 11 HOH 621  2721 1137 HOH HOH A . 
DA 11 HOH 622  2722 1703 HOH HOH A . 
DA 11 HOH 623  2723 421  HOH HOH A . 
DA 11 HOH 624  2724 1054 HOH HOH A . 
DA 11 HOH 625  2725 2306 HOH HOH A . 
DA 11 HOH 626  2726 901  HOH HOH A . 
DA 11 HOH 627  2727 1446 HOH HOH A . 
DA 11 HOH 628  2728 853  HOH HOH A . 
DA 11 HOH 629  2729 608  HOH HOH A . 
DA 11 HOH 630  2730 858  HOH HOH A . 
DA 11 HOH 631  2731 723  HOH HOH A . 
DA 11 HOH 632  2732 1853 HOH HOH A . 
DA 11 HOH 633  2733 1175 HOH HOH A . 
DA 11 HOH 634  2734 2    HOH HOH A . 
DA 11 HOH 635  2735 2494 HOH HOH A . 
DA 11 HOH 636  2736 1190 HOH HOH A . 
DA 11 HOH 637  2737 1855 HOH HOH A . 
DA 11 HOH 638  2738 498  HOH HOH A . 
DA 11 HOH 639  2739 511  HOH HOH A . 
DA 11 HOH 640  2740 804  HOH HOH A . 
DA 11 HOH 641  2741 2048 HOH HOH A . 
DA 11 HOH 642  2742 975  HOH HOH A . 
DA 11 HOH 643  2743 465  HOH HOH A . 
DA 11 HOH 644  2744 965  HOH HOH A . 
DA 11 HOH 645  2745 705  HOH HOH A . 
DA 11 HOH 646  2746 1565 HOH HOH A . 
DA 11 HOH 647  2747 1614 HOH HOH A . 
DA 11 HOH 648  2748 236  HOH HOH A . 
DA 11 HOH 649  2749 583  HOH HOH A . 
DA 11 HOH 650  2750 1737 HOH HOH A . 
DA 11 HOH 651  2751 951  HOH HOH A . 
DA 11 HOH 652  2752 2003 HOH HOH A . 
DA 11 HOH 653  2753 1380 HOH HOH A . 
DA 11 HOH 654  2754 1876 HOH HOH A . 
DA 11 HOH 655  2755 1369 HOH HOH A . 
DA 11 HOH 656  2756 926  HOH HOH A . 
DA 11 HOH 657  2757 510  HOH HOH A . 
DA 11 HOH 658  2758 769  HOH HOH A . 
DA 11 HOH 659  2759 704  HOH HOH A . 
DA 11 HOH 660  2760 1920 HOH HOH A . 
DA 11 HOH 661  2761 1578 HOH HOH A . 
DA 11 HOH 662  2762 458  HOH HOH A . 
DA 11 HOH 663  2763 686  HOH HOH A . 
DA 11 HOH 664  2764 2068 HOH HOH A . 
DA 11 HOH 665  2765 2329 HOH HOH A . 
DA 11 HOH 666  2766 722  HOH HOH A . 
DA 11 HOH 667  2767 1274 HOH HOH A . 
DA 11 HOH 668  2768 364  HOH HOH A . 
DA 11 HOH 669  2769 515  HOH HOH A . 
DA 11 HOH 670  2770 1520 HOH HOH A . 
DA 11 HOH 671  2771 1236 HOH HOH A . 
DA 11 HOH 672  2772 486  HOH HOH A . 
DA 11 HOH 673  2773 439  HOH HOH A . 
DA 11 HOH 674  2774 1443 HOH HOH A . 
DA 11 HOH 675  2775 662  HOH HOH A . 
DA 11 HOH 676  2776 1511 HOH HOH A . 
DA 11 HOH 677  2777 2456 HOH HOH A . 
DA 11 HOH 678  2778 1419 HOH HOH A . 
DA 11 HOH 679  2779 21   HOH HOH A . 
DA 11 HOH 680  2780 153  HOH HOH A . 
DA 11 HOH 681  2781 400  HOH HOH A . 
DA 11 HOH 682  2782 177  HOH HOH A . 
DA 11 HOH 683  2783 1219 HOH HOH A . 
DA 11 HOH 684  2784 2157 HOH HOH A . 
DA 11 HOH 685  2785 147  HOH HOH A . 
DA 11 HOH 686  2786 1999 HOH HOH A . 
DA 11 HOH 687  2787 1458 HOH HOH A . 
DA 11 HOH 688  2788 463  HOH HOH A . 
DA 11 HOH 689  2789 2247 HOH HOH A . 
DA 11 HOH 690  2790 2438 HOH HOH A . 
DA 11 HOH 691  2791 1164 HOH HOH A . 
DA 11 HOH 692  2792 2441 HOH HOH A . 
DA 11 HOH 693  2793 2236 HOH HOH A . 
DA 11 HOH 694  2794 1340 HOH HOH A . 
DA 11 HOH 695  2795 571  HOH HOH A . 
DA 11 HOH 696  2796 1414 HOH HOH A . 
DA 11 HOH 697  2797 721  HOH HOH A . 
DA 11 HOH 698  2798 1478 HOH HOH A . 
DA 11 HOH 699  2799 698  HOH HOH A . 
DA 11 HOH 700  2800 559  HOH HOH A . 
DA 11 HOH 701  2801 2272 HOH HOH A . 
DA 11 HOH 702  2802 562  HOH HOH A . 
DA 11 HOH 703  2803 908  HOH HOH A . 
DA 11 HOH 704  2804 443  HOH HOH A . 
DA 11 HOH 705  2805 2069 HOH HOH A . 
DA 11 HOH 706  2806 1020 HOH HOH A . 
DA 11 HOH 707  2807 167  HOH HOH A . 
DA 11 HOH 708  2808 114  HOH HOH A . 
DA 11 HOH 709  2809 1866 HOH HOH A . 
DA 11 HOH 710  2810 150  HOH HOH A . 
DA 11 HOH 711  2811 1745 HOH HOH A . 
DA 11 HOH 712  2812 717  HOH HOH A . 
DA 11 HOH 713  2813 1985 HOH HOH A . 
DA 11 HOH 714  2814 1889 HOH HOH A . 
DA 11 HOH 715  2815 245  HOH HOH A . 
DA 11 HOH 716  2816 314  HOH HOH A . 
DA 11 HOH 717  2817 1196 HOH HOH A . 
DA 11 HOH 718  2818 678  HOH HOH A . 
DA 11 HOH 719  2819 2005 HOH HOH A . 
DA 11 HOH 720  2820 1808 HOH HOH A . 
DA 11 HOH 721  2821 1104 HOH HOH A . 
DA 11 HOH 722  2822 1315 HOH HOH A . 
DA 11 HOH 723  2823 1187 HOH HOH A . 
DA 11 HOH 724  2824 1645 HOH HOH A . 
DA 11 HOH 725  2825 585  HOH HOH A . 
DA 11 HOH 726  2826 1328 HOH HOH A . 
DA 11 HOH 727  2827 1701 HOH HOH A . 
DA 11 HOH 728  2828 1847 HOH HOH A . 
DA 11 HOH 729  2829 1815 HOH HOH A . 
DA 11 HOH 730  2830 355  HOH HOH A . 
DA 11 HOH 731  2831 1441 HOH HOH A . 
DA 11 HOH 732  2832 1080 HOH HOH A . 
DA 11 HOH 733  2833 934  HOH HOH A . 
DA 11 HOH 734  2834 1460 HOH HOH A . 
DA 11 HOH 735  2835 1403 HOH HOH A . 
DA 11 HOH 736  2836 205  HOH HOH A . 
DA 11 HOH 737  2837 2250 HOH HOH A . 
DA 11 HOH 738  2838 242  HOH HOH A . 
DA 11 HOH 739  2839 1841 HOH HOH A . 
DA 11 HOH 740  2840 395  HOH HOH A . 
DA 11 HOH 741  2841 308  HOH HOH A . 
DA 11 HOH 742  2842 2108 HOH HOH A . 
DA 11 HOH 743  2843 2172 HOH HOH A . 
DA 11 HOH 744  2844 655  HOH HOH A . 
DA 11 HOH 745  2845 331  HOH HOH A . 
DA 11 HOH 746  2846 947  HOH HOH A . 
DA 11 HOH 747  2847 1802 HOH HOH A . 
DA 11 HOH 748  2848 2080 HOH HOH A . 
DA 11 HOH 749  2849 324  HOH HOH A . 
DA 11 HOH 750  2850 1089 HOH HOH A . 
DA 11 HOH 751  2851 1098 HOH HOH A . 
DA 11 HOH 752  2852 1174 HOH HOH A . 
DA 11 HOH 753  2853 2246 HOH HOH A . 
DA 11 HOH 754  2854 2029 HOH HOH A . 
DA 11 HOH 755  2855 682  HOH HOH A . 
DA 11 HOH 756  2856 37   HOH HOH A . 
DA 11 HOH 757  2857 619  HOH HOH A . 
DA 11 HOH 758  2858 2076 HOH HOH A . 
DA 11 HOH 759  2859 1732 HOH HOH A . 
DA 11 HOH 760  2860 457  HOH HOH A . 
DA 11 HOH 761  2861 2171 HOH HOH A . 
DA 11 HOH 762  2862 1178 HOH HOH A . 
DA 11 HOH 763  2863 1205 HOH HOH A . 
DA 11 HOH 764  2864 2379 HOH HOH A . 
DA 11 HOH 765  2865 2264 HOH HOH A . 
DA 11 HOH 766  2866 938  HOH HOH A . 
DA 11 HOH 767  2867 1193 HOH HOH A . 
DA 11 HOH 768  2868 293  HOH HOH A . 
DA 11 HOH 769  2869 1763 HOH HOH A . 
DA 11 HOH 770  2870 187  HOH HOH A . 
DA 11 HOH 771  2871 1933 HOH HOH A . 
DA 11 HOH 772  2872 941  HOH HOH A . 
DA 11 HOH 773  2873 219  HOH HOH A . 
DA 11 HOH 774  2874 772  HOH HOH A . 
DA 11 HOH 775  2875 2061 HOH HOH A . 
DA 11 HOH 776  2876 1218 HOH HOH A . 
DA 11 HOH 777  2877 1662 HOH HOH A . 
DA 11 HOH 778  2878 1897 HOH HOH A . 
DA 11 HOH 779  2879 2058 HOH HOH A . 
DA 11 HOH 780  2880 1434 HOH HOH A . 
DA 11 HOH 781  2881 1430 HOH HOH A . 
DA 11 HOH 782  2882 977  HOH HOH A . 
DA 11 HOH 783  2883 886  HOH HOH A . 
DA 11 HOH 784  2884 750  HOH HOH A . 
DA 11 HOH 785  2885 1240 HOH HOH A . 
DA 11 HOH 786  2886 1884 HOH HOH A . 
DA 11 HOH 787  2887 323  HOH HOH A . 
DA 11 HOH 788  2888 1375 HOH HOH A . 
DA 11 HOH 789  2889 1192 HOH HOH A . 
DA 11 HOH 790  2890 1258 HOH HOH A . 
DA 11 HOH 791  2891 271  HOH HOH A . 
DA 11 HOH 792  2892 856  HOH HOH A . 
DA 11 HOH 793  2893 774  HOH HOH A . 
DA 11 HOH 794  2894 1549 HOH HOH A . 
DA 11 HOH 795  2895 972  HOH HOH A . 
DA 11 HOH 796  2896 74   HOH HOH A . 
DA 11 HOH 797  2897 543  HOH HOH A . 
DA 11 HOH 798  2898 681  HOH HOH A . 
DA 11 HOH 799  2899 1528 HOH HOH A . 
DA 11 HOH 800  2900 2282 HOH HOH A . 
DA 11 HOH 801  2901 112  HOH HOH A . 
DA 11 HOH 802  2902 560  HOH HOH A . 
DA 11 HOH 803  2903 2138 HOH HOH A . 
DA 11 HOH 804  2904 2136 HOH HOH A . 
DA 11 HOH 805  2905 278  HOH HOH A . 
DA 11 HOH 806  2906 2208 HOH HOH A . 
DA 11 HOH 807  2907 49   HOH HOH A . 
DA 11 HOH 808  2908 1097 HOH HOH A . 
DA 11 HOH 809  2909 1232 HOH HOH A . 
DA 11 HOH 810  2910 180  HOH HOH A . 
DA 11 HOH 811  2911 456  HOH HOH A . 
DA 11 HOH 812  2912 1740 HOH HOH A . 
DA 11 HOH 813  2913 1062 HOH HOH A . 
DA 11 HOH 814  2914 303  HOH HOH A . 
DA 11 HOH 815  2915 1799 HOH HOH A . 
DA 11 HOH 816  2916 1413 HOH HOH A . 
DA 11 HOH 817  2917 680  HOH HOH A . 
DA 11 HOH 818  2918 2278 HOH HOH A . 
DA 11 HOH 819  2919 2483 HOH HOH A . 
DA 11 HOH 820  2920 2065 HOH HOH A . 
DA 11 HOH 821  2921 2168 HOH HOH A . 
DA 11 HOH 822  2922 897  HOH HOH A . 
DA 11 HOH 823  2923 1095 HOH HOH A . 
DA 11 HOH 824  2924 548  HOH HOH A . 
DA 11 HOH 825  2925 2487 HOH HOH A . 
DA 11 HOH 826  2926 1527 HOH HOH A . 
DA 11 HOH 827  2927 1042 HOH HOH A . 
DA 11 HOH 828  2928 1395 HOH HOH A . 
DA 11 HOH 829  2929 1198 HOH HOH A . 
DA 11 HOH 830  2930 2191 HOH HOH A . 
DA 11 HOH 831  2931 1554 HOH HOH A . 
DA 11 HOH 832  2932 969  HOH HOH A . 
DA 11 HOH 833  2933 1372 HOH HOH A . 
DA 11 HOH 834  2934 1622 HOH HOH A . 
DA 11 HOH 835  2935 2393 HOH HOH A . 
DA 11 HOH 836  2936 1428 HOH HOH A . 
DA 11 HOH 837  2937 860  HOH HOH A . 
DA 11 HOH 838  2938 745  HOH HOH A . 
DA 11 HOH 839  2939 1690 HOH HOH A . 
DA 11 HOH 840  2940 1392 HOH HOH A . 
DA 11 HOH 841  2941 2466 HOH HOH A . 
DA 11 HOH 842  2942 1276 HOH HOH A . 
DA 11 HOH 843  2943 910  HOH HOH A . 
DA 11 HOH 844  2944 1609 HOH HOH A . 
DA 11 HOH 845  2945 1508 HOH HOH A . 
DA 11 HOH 846  2946 1577 HOH HOH A . 
DA 11 HOH 847  2947 1925 HOH HOH A . 
DA 11 HOH 848  2948 2257 HOH HOH A . 
DA 11 HOH 849  2949 2103 HOH HOH A . 
DA 11 HOH 850  2950 1041 HOH HOH A . 
DA 11 HOH 851  2951 2219 HOH HOH A . 
DA 11 HOH 852  2952 983  HOH HOH A . 
DA 11 HOH 853  2953 2053 HOH HOH A . 
DA 11 HOH 854  2954 2283 HOH HOH A . 
DA 11 HOH 855  2955 507  HOH HOH A . 
DA 11 HOH 856  2956 1436 HOH HOH A . 
DA 11 HOH 857  2957 2447 HOH HOH A . 
DA 11 HOH 858  2958 1454 HOH HOH A . 
DA 11 HOH 859  2959 2266 HOH HOH A . 
DA 11 HOH 860  2960 1904 HOH HOH A . 
DA 11 HOH 861  2961 2216 HOH HOH A . 
DA 11 HOH 862  2962 1898 HOH HOH A . 
DA 11 HOH 863  2963 2376 HOH HOH A . 
DA 11 HOH 864  2964 1691 HOH HOH A . 
DA 11 HOH 865  2965 1824 HOH HOH A . 
DA 11 HOH 866  2966 1557 HOH HOH A . 
DA 11 HOH 867  2967 2238 HOH HOH A . 
DA 11 HOH 868  2968 2118 HOH HOH A . 
DA 11 HOH 869  2969 1246 HOH HOH A . 
DA 11 HOH 870  2970 1189 HOH HOH A . 
DA 11 HOH 871  2971 2249 HOH HOH A . 
DA 11 HOH 872  2972 2474 HOH HOH A . 
DA 11 HOH 873  2973 1635 HOH HOH A . 
DA 11 HOH 874  2974 564  HOH HOH A . 
DA 11 HOH 875  2975 2114 HOH HOH A . 
DA 11 HOH 876  2976 2358 HOH HOH A . 
DA 11 HOH 877  2977 2298 HOH HOH A . 
DA 11 HOH 878  2978 2307 HOH HOH A . 
DA 11 HOH 879  2979 1661 HOH HOH A . 
DA 11 HOH 880  2980 1408 HOH HOH A . 
DA 11 HOH 881  2981 1819 HOH HOH A . 
DA 11 HOH 882  2982 1868 HOH HOH A . 
DA 11 HOH 883  2983 2017 HOH HOH A . 
DA 11 HOH 884  2984 1563 HOH HOH A . 
DA 11 HOH 885  2985 1533 HOH HOH A . 
DA 11 HOH 886  2986 1658 HOH HOH A . 
DA 11 HOH 887  2987 2345 HOH HOH A . 
DA 11 HOH 888  2988 2149 HOH HOH A . 
DA 11 HOH 889  2989 575  HOH HOH A . 
DA 11 HOH 890  2990 1466 HOH HOH A . 
DA 11 HOH 891  2991 2200 HOH HOH A . 
DA 11 HOH 892  2992 479  HOH HOH A . 
DA 11 HOH 893  2993 2372 HOH HOH A . 
DA 11 HOH 894  2994 1699 HOH HOH A . 
DA 11 HOH 895  2995 2322 HOH HOH A . 
DA 11 HOH 896  2996 594  HOH HOH A . 
DA 11 HOH 897  2997 1112 HOH HOH A . 
DA 11 HOH 898  2998 898  HOH HOH A . 
DA 11 HOH 899  2999 2425 HOH HOH A . 
DA 11 HOH 900  3000 641  HOH HOH A . 
DA 11 HOH 901  3001 2299 HOH HOH A . 
DA 11 HOH 902  3002 2389 HOH HOH A . 
DA 11 HOH 903  3003 311  HOH HOH A . 
DA 11 HOH 904  3004 1257 HOH HOH A . 
DA 11 HOH 905  3005 2385 HOH HOH A . 
DA 11 HOH 906  3006 1325 HOH HOH A . 
DA 11 HOH 907  3007 1214 HOH HOH A . 
DA 11 HOH 908  3008 1216 HOH HOH A . 
DA 11 HOH 909  3009 859  HOH HOH A . 
DA 11 HOH 910  3010 1726 HOH HOH A . 
DA 11 HOH 911  3011 566  HOH HOH A . 
DA 11 HOH 912  3012 2078 HOH HOH A . 
DA 11 HOH 913  3013 2449 HOH HOH A . 
DA 11 HOH 914  3014 1048 HOH HOH A . 
DA 11 HOH 915  3015 1179 HOH HOH A . 
DA 11 HOH 916  3016 1509 HOH HOH A . 
DA 11 HOH 917  3017 2128 HOH HOH A . 
DA 11 HOH 918  3018 1423 HOH HOH A . 
DA 11 HOH 919  3019 888  HOH HOH A . 
DA 11 HOH 920  3020 1908 HOH HOH A . 
DA 11 HOH 921  3021 2271 HOH HOH A . 
DA 11 HOH 922  3022 1204 HOH HOH A . 
DA 11 HOH 923  3023 2490 HOH HOH A . 
DA 11 HOH 924  3024 2473 HOH HOH A . 
DA 11 HOH 925  3025 2417 HOH HOH A . 
DA 11 HOH 926  3026 2131 HOH HOH A . 
DA 11 HOH 927  3027 1374 HOH HOH A . 
DA 11 HOH 928  3028 1517 HOH HOH A . 
DA 11 HOH 929  3029 2183 HOH HOH A . 
DA 11 HOH 930  3030 1377 HOH HOH A . 
DA 11 HOH 931  3031 1184 HOH HOH A . 
DA 11 HOH 932  3032 684  HOH HOH A . 
DA 11 HOH 933  3033 2386 HOH HOH A . 
DA 11 HOH 934  3034 1016 HOH HOH A . 
DA 11 HOH 935  3035 780  HOH HOH A . 
DA 11 HOH 936  3036 1885 HOH HOH A . 
DA 11 HOH 937  3037 1245 HOH HOH A . 
DA 11 HOH 938  3038 1615 HOH HOH A . 
DA 11 HOH 939  3039 1657 HOH HOH A . 
DA 11 HOH 940  3040 1916 HOH HOH A . 
DA 11 HOH 941  3041 815  HOH HOH A . 
DA 11 HOH 942  3042 2182 HOH HOH A . 
DA 11 HOH 943  3043 2407 HOH HOH A . 
DA 11 HOH 944  3044 2018 HOH HOH A . 
DA 11 HOH 945  3045 1811 HOH HOH A . 
DA 11 HOH 946  3046 442  HOH HOH A . 
DA 11 HOH 947  3047 1132 HOH HOH A . 
DA 11 HOH 948  3048 1782 HOH HOH A . 
DA 11 HOH 949  3049 912  HOH HOH A . 
DA 11 HOH 950  3050 733  HOH HOH A . 
DA 11 HOH 951  3051 1299 HOH HOH A . 
DA 11 HOH 952  3052 1352 HOH HOH A . 
DA 11 HOH 953  3053 2209 HOH HOH A . 
DA 11 HOH 954  3054 2036 HOH HOH A . 
DA 11 HOH 955  3055 1143 HOH HOH A . 
DA 11 HOH 956  3056 2366 HOH HOH A . 
DA 11 HOH 957  3057 1907 HOH HOH A . 
DA 11 HOH 958  3058 1546 HOH HOH A . 
DA 11 HOH 959  3059 1348 HOH HOH A . 
DA 11 HOH 960  3060 2130 HOH HOH A . 
DA 11 HOH 961  3061 1629 HOH HOH A . 
DA 11 HOH 962  3062 666  HOH HOH A . 
DA 11 HOH 963  3063 1401 HOH HOH A . 
DA 11 HOH 964  3064 2317 HOH HOH A . 
DA 11 HOH 965  3065 537  HOH HOH A . 
DA 11 HOH 966  3066 2468 HOH HOH A . 
DA 11 HOH 967  3067 2392 HOH HOH A . 
DA 11 HOH 968  3068 3    HOH HOH A . 
DA 11 HOH 969  3069 1111 HOH HOH A . 
DA 11 HOH 970  3070 2207 HOH HOH A . 
DA 11 HOH 971  3071 735  HOH HOH A . 
DA 11 HOH 972  3072 836  HOH HOH A . 
DA 11 HOH 973  3073 2217 HOH HOH A . 
DA 11 HOH 974  3074 712  HOH HOH A . 
DA 11 HOH 975  3075 2445 HOH HOH A . 
DA 11 HOH 976  3076 1761 HOH HOH A . 
DA 11 HOH 977  3077 1762 HOH HOH A . 
DA 11 HOH 978  3078 1142 HOH HOH A . 
DA 11 HOH 979  3079 1774 HOH HOH A . 
DA 11 HOH 980  3080 1989 HOH HOH A . 
DA 11 HOH 981  3081 2410 HOH HOH A . 
DA 11 HOH 982  3082 2189 HOH HOH A . 
DA 11 HOH 983  3083 2318 HOH HOH A . 
DA 11 HOH 984  3084 943  HOH HOH A . 
DA 11 HOH 985  3085 2427 HOH HOH A . 
DA 11 HOH 986  3086 2009 HOH HOH A . 
DA 11 HOH 987  3087 1521 HOH HOH A . 
DA 11 HOH 988  3088 2310 HOH HOH A . 
DA 11 HOH 989  3089 2033 HOH HOH A . 
DA 11 HOH 990  3090 2485 HOH HOH A . 
DA 11 HOH 991  3091 1714 HOH HOH A . 
DA 11 HOH 992  3092 2334 HOH HOH A . 
DA 11 HOH 993  3093 2378 HOH HOH A . 
DA 11 HOH 994  3094 1424 HOH HOH A . 
DA 11 HOH 995  3095 1297 HOH HOH A . 
DA 11 HOH 996  3096 1682 HOH HOH A . 
DA 11 HOH 997  3097 444  HOH HOH A . 
DA 11 HOH 998  3098 1919 HOH HOH A . 
DA 11 HOH 999  3099 1303 HOH HOH A . 
DA 11 HOH 1000 3100 2049 HOH HOH A . 
DA 11 HOH 1001 3101 1444 HOH HOH A . 
DA 11 HOH 1002 3102 210  HOH HOH A . 
DA 11 HOH 1003 3103 2285 HOH HOH A . 
DA 11 HOH 1004 3104 1397 HOH HOH A . 
DA 11 HOH 1005 3105 2196 HOH HOH A . 
DA 11 HOH 1006 3106 2221 HOH HOH A . 
DA 11 HOH 1007 3107 2087 HOH HOH A . 
DA 11 HOH 1008 3108 1515 HOH HOH A . 
DA 11 HOH 1009 3109 1343 HOH HOH A . 
DA 11 HOH 1010 3110 1890 HOH HOH A . 
DA 11 HOH 1011 3111 1681 HOH HOH A . 
DA 11 HOH 1012 3112 489  HOH HOH A . 
DA 11 HOH 1013 3113 2010 HOH HOH A . 
DA 11 HOH 1014 3114 2004 HOH HOH A . 
DA 11 HOH 1015 3115 1921 HOH HOH A . 
DA 11 HOH 1016 3116 483  HOH HOH A . 
DA 11 HOH 1017 3117 1012 HOH HOH A . 
DA 11 HOH 1018 3118 1040 HOH HOH A . 
DA 11 HOH 1019 3119 1113 HOH HOH A . 
DA 11 HOH 1020 3120 1905 HOH HOH A . 
DA 11 HOH 1021 3121 2475 HOH HOH A . 
DA 11 HOH 1022 3122 1093 HOH HOH A . 
DA 11 HOH 1023 3123 2416 HOH HOH A . 
DA 11 HOH 1024 3124 1687 HOH HOH A . 
DA 11 HOH 1025 3125 2234 HOH HOH A . 
DA 11 HOH 1026 3126 1834 HOH HOH A . 
DA 11 HOH 1027 3127 1754 HOH HOH A . 
DA 11 HOH 1028 3128 1784 HOH HOH A . 
DA 11 HOH 1029 3129 1940 HOH HOH A . 
DA 11 HOH 1030 3130 1781 HOH HOH A . 
DA 11 HOH 1031 3131 1820 HOH HOH A . 
DA 11 HOH 1032 3132 1671 HOH HOH A . 
DA 11 HOH 1033 3133 1018 HOH HOH A . 
DA 11 HOH 1034 3134 1900 HOH HOH A . 
DA 11 HOH 1035 3135 1338 HOH HOH A . 
DA 11 HOH 1036 3136 1531 HOH HOH A . 
DA 11 HOH 1037 3137 1015 HOH HOH A . 
DA 11 HOH 1038 3138 1881 HOH HOH A . 
DA 11 HOH 1039 3139 2409 HOH HOH A . 
DA 11 HOH 1040 3140 819  HOH HOH A . 
DA 11 HOH 1041 3141 1149 HOH HOH A . 
DA 11 HOH 1042 3142 1852 HOH HOH A . 
DA 11 HOH 1043 3143 1341 HOH HOH A . 
DA 11 HOH 1044 3144 1725 HOH HOH A . 
DA 11 HOH 1045 3145 1758 HOH HOH A . 
DA 11 HOH 1046 3146 1676 HOH HOH A . 
DA 11 HOH 1047 3147 1727 HOH HOH A . 
DA 11 HOH 1048 3148 877  HOH HOH A . 
DA 11 HOH 1049 3149 1927 HOH HOH A . 
DA 11 HOH 1050 3150 2132 HOH HOH A . 
DA 11 HOH 1051 3151 1751 HOH HOH A . 
DA 11 HOH 1052 3152 1140 HOH HOH A . 
DA 11 HOH 1053 3153 1008 HOH HOH A . 
DA 11 HOH 1054 3154 1388 HOH HOH A . 
DA 11 HOH 1055 3155 2008 HOH HOH A . 
DA 11 HOH 1056 3156 1665 HOH HOH A . 
DA 11 HOH 1057 3157 1518 HOH HOH A . 
DA 11 HOH 1058 3158 423  HOH HOH A . 
DA 11 HOH 1059 3159 830  HOH HOH A . 
DA 11 HOH 1060 3160 1935 HOH HOH A . 
DA 11 HOH 1061 3161 915  HOH HOH A . 
DA 11 HOH 1062 3162 1335 HOH HOH A . 
DA 11 HOH 1063 3163 1835 HOH HOH A . 
DA 11 HOH 1064 3164 2457 HOH HOH A . 
DA 11 HOH 1065 3165 1305 HOH HOH A . 
DA 11 HOH 1066 3166 1717 HOH HOH A . 
DA 11 HOH 1067 3167 1425 HOH HOH A . 
DA 11 HOH 1068 3168 2210 HOH HOH A . 
DA 11 HOH 1069 3169 980  HOH HOH A . 
DA 11 HOH 1070 3170 1482 HOH HOH A . 
DA 11 HOH 1071 3171 1223 HOH HOH A . 
DA 11 HOH 1072 3172 1272 HOH HOH A . 
DA 11 HOH 1073 3173 2279 HOH HOH A . 
DA 11 HOH 1074 3174 1400 HOH HOH A . 
DA 11 HOH 1075 3175 2321 HOH HOH A . 
DA 11 HOH 1076 3176 2011 HOH HOH A . 
DA 11 HOH 1077 3177 993  HOH HOH A . 
DA 11 HOH 1078 3178 1840 HOH HOH A . 
DA 11 HOH 1079 3179 424  HOH HOH A . 
DA 11 HOH 1080 3180 2245 HOH HOH A . 
DA 11 HOH 1081 3181 2190 HOH HOH A . 
DA 11 HOH 1082 3182 1472 HOH HOH A . 
DA 11 HOH 1083 3183 2455 HOH HOH A . 
DA 11 HOH 1084 3184 1028 HOH HOH A . 
DA 11 HOH 1085 3185 2243 HOH HOH A . 
DA 11 HOH 1086 3186 1746 HOH HOH A . 
DA 11 HOH 1087 3187 1593 HOH HOH A . 
DA 11 HOH 1088 3188 1449 HOH HOH A . 
DA 11 HOH 1089 3189 1516 HOH HOH A . 
DA 11 HOH 1090 3190 630  HOH HOH A . 
DA 11 HOH 1091 3191 1922 HOH HOH A . 
DA 11 HOH 1092 3192 1836 HOH HOH A . 
DA 11 HOH 1093 3193 1412 HOH HOH A . 
DA 11 HOH 1094 3194 2013 HOH HOH A . 
DA 11 HOH 1095 3195 851  HOH HOH A . 
DA 11 HOH 1096 3196 1033 HOH HOH A . 
DA 11 HOH 1097 3197 1924 HOH HOH A . 
DA 11 HOH 1098 3198 1235 HOH HOH A . 
DA 11 HOH 1099 3199 2440 HOH HOH A . 
DA 11 HOH 1100 3200 2223 HOH HOH A . 
DA 11 HOH 1101 3201 777  HOH HOH A . 
DA 11 HOH 1102 3202 2260 HOH HOH A . 
DA 11 HOH 1103 3203 1320 HOH HOH A . 
DA 11 HOH 1104 3204 1237 HOH HOH A . 
DA 11 HOH 1105 3205 2075 HOH HOH A . 
DA 11 HOH 1106 3206 1212 HOH HOH A . 
DA 11 HOH 1107 3207 1987 HOH HOH A . 
DA 11 HOH 1108 3208 1406 HOH HOH A . 
DA 11 HOH 1109 3209 2044 HOH HOH A . 
DA 11 HOH 1110 3210 615  HOH HOH A . 
DA 11 HOH 1111 3211 2027 HOH HOH A . 
DA 11 HOH 1112 3212 986  HOH HOH A . 
DA 11 HOH 1113 3213 2482 HOH HOH A . 
DA 11 HOH 1114 3214 1471 HOH HOH A . 
DA 11 HOH 1115 3215 1946 HOH HOH A . 
DA 11 HOH 1116 3216 2205 HOH HOH A . 
DA 11 HOH 1117 3217 1729 HOH HOH A . 
DA 11 HOH 1118 3218 1874 HOH HOH A . 
DA 11 HOH 1119 3219 747  HOH HOH A . 
DA 11 HOH 1120 3220 1794 HOH HOH A . 
DA 11 HOH 1121 3221 707  HOH HOH A . 
DA 11 HOH 1122 3222 2426 HOH HOH A . 
DA 11 HOH 1123 3223 2330 HOH HOH A . 
DA 11 HOH 1124 3224 998  HOH HOH A . 
DA 11 HOH 1125 3225 1667 HOH HOH A . 
DA 11 HOH 1126 3226 1267 HOH HOH A . 
DA 11 HOH 1127 3227 1002 HOH HOH A . 
DA 11 HOH 1128 3228 1623 HOH HOH A . 
DA 11 HOH 1129 3229 1141 HOH HOH A . 
DA 11 HOH 1130 3230 1888 HOH HOH A . 
DA 11 HOH 1131 3231 2375 HOH HOH A . 
DA 11 HOH 1132 3232 2077 HOH HOH A . 
DA 11 HOH 1133 3233 598  HOH HOH A . 
DA 11 HOH 1134 3234 1207 HOH HOH A . 
DA 11 HOH 1135 3235 1693 HOH HOH A . 
DA 11 HOH 1136 3236 1158 HOH HOH A . 
DA 11 HOH 1137 3237 1138 HOH HOH A . 
DA 11 HOH 1138 3238 140  HOH HOH A . 
DA 11 HOH 1139 3239 1926 HOH HOH A . 
DA 11 HOH 1140 3240 1816 HOH HOH A . 
DA 11 HOH 1141 3241 2404 HOH HOH A . 
DA 11 HOH 1142 3242 896  HOH HOH A . 
DA 11 HOH 1143 3243 1153 HOH HOH A . 
DA 11 HOH 1144 3244 1651 HOH HOH A . 
DA 11 HOH 1145 3245 1159 HOH HOH A . 
DA 11 HOH 1146 3246 1464 HOH HOH A . 
DA 11 HOH 1147 3247 1643 HOH HOH A . 
DA 11 HOH 1148 3248 1151 HOH HOH A . 
DA 11 HOH 1149 3249 1021 HOH HOH A . 
DA 11 HOH 1150 3250 2104 HOH HOH A . 
DA 11 HOH 1151 3251 2115 HOH HOH A . 
DA 11 HOH 1152 3252 1757 HOH HOH A . 
DA 11 HOH 1153 3253 937  HOH HOH A . 
DA 11 HOH 1154 3254 917  HOH HOH A . 
DA 11 HOH 1155 3255 1030 HOH HOH A . 
DA 11 HOH 1156 3256 1432 HOH HOH A . 
DA 11 HOH 1157 3257 1410 HOH HOH A . 
DA 11 HOH 1158 3258 2088 HOH HOH A . 
DA 11 HOH 1159 3259 2446 HOH HOH A . 
DA 11 HOH 1160 3260 857  HOH HOH A . 
DA 11 HOH 1161 3261 2397 HOH HOH A . 
DA 11 HOH 1162 3262 1721 HOH HOH A . 
DA 11 HOH 1163 3263 2222 HOH HOH A . 
DA 11 HOH 1164 3264 1923 HOH HOH A . 
DA 11 HOH 1165 3265 781  HOH HOH A . 
DA 11 HOH 1166 3266 650  HOH HOH A . 
DA 11 HOH 1167 3267 2174 HOH HOH A . 
DA 11 HOH 1168 3268 1103 HOH HOH A . 
DA 11 HOH 1169 3269 1817 HOH HOH A . 
DA 11 HOH 1170 3270 2218 HOH HOH A . 
DA 11 HOH 1171 3271 1504 HOH HOH A . 
DA 11 HOH 1172 3272 1185 HOH HOH A . 
DA 11 HOH 1173 3273 1648 HOH HOH A . 
DA 11 HOH 1174 3274 1321 HOH HOH A . 
DA 11 HOH 1175 3275 2113 HOH HOH A . 
DA 11 HOH 1176 3276 1777 HOH HOH A . 
DA 11 HOH 1177 3277 785  HOH HOH A . 
DA 11 HOH 1178 3278 2294 HOH HOH A . 
DA 11 HOH 1179 3279 2391 HOH HOH A . 
DA 11 HOH 1180 3280 1450 HOH HOH A . 
DA 11 HOH 1181 3281 1720 HOH HOH A . 
DA 11 HOH 1182 3282 2331 HOH HOH A . 
DA 11 HOH 1183 3283 1724 HOH HOH A . 
DA 11 HOH 1184 3284 688  HOH HOH A . 
DA 11 HOH 1185 3285 2051 HOH HOH A . 
DA 11 HOH 1186 3286 1586 HOH HOH A . 
DA 11 HOH 1187 3287 1123 HOH HOH A . 
DA 11 HOH 1188 3288 1362 HOH HOH A . 
DA 11 HOH 1189 3289 2396 HOH HOH A . 
DA 11 HOH 1190 3290 1346 HOH HOH A . 
DA 11 HOH 1191 3291 1918 HOH HOH A . 
EA 11 HOH 1    2101 2007 HOH HOH B . 
EA 11 HOH 2    2102 389  HOH HOH B . 
EA 11 HOH 3    2103 1368 HOH HOH B . 
EA 11 HOH 4    2104 1984 HOH HOH B . 
EA 11 HOH 5    2105 1843 HOH HOH B . 
EA 11 HOH 6    2106 797  HOH HOH B . 
EA 11 HOH 7    2107 1838 HOH HOH B . 
EA 11 HOH 8    2108 2363 HOH HOH B . 
EA 11 HOH 9    2109 1071 HOH HOH B . 
EA 11 HOH 10   2110 2165 HOH HOH B . 
EA 11 HOH 11   2111 1355 HOH HOH B . 
EA 11 HOH 12   2112 1663 HOH HOH B . 
EA 11 HOH 13   2113 2122 HOH HOH B . 
EA 11 HOH 14   2114 607  HOH HOH B . 
EA 11 HOH 15   2115 565  HOH HOH B . 
EA 11 HOH 16   2116 2337 HOH HOH B . 
EA 11 HOH 17   2117 826  HOH HOH B . 
EA 11 HOH 18   2118 844  HOH HOH B . 
EA 11 HOH 19   2119 1087 HOH HOH B . 
EA 11 HOH 20   2120 1550 HOH HOH B . 
EA 11 HOH 21   2121 738  HOH HOH B . 
EA 11 HOH 22   2122 196  HOH HOH B . 
EA 11 HOH 23   2123 1263 HOH HOH B . 
EA 11 HOH 24   2124 2046 HOH HOH B . 
EA 11 HOH 25   2125 2152 HOH HOH B . 
EA 11 HOH 26   2126 1313 HOH HOH B . 
EA 11 HOH 27   2127 2015 HOH HOH B . 
EA 11 HOH 28   2128 1991 HOH HOH B . 
EA 11 HOH 29   2129 485  HOH HOH B . 
EA 11 HOH 30   2130 837  HOH HOH B . 
EA 11 HOH 31   2131 371  HOH HOH B . 
EA 11 HOH 32   2132 776  HOH HOH B . 
EA 11 HOH 33   2133 1639 HOH HOH B . 
EA 11 HOH 34   2134 2420 HOH HOH B . 
EA 11 HOH 35   2135 1252 HOH HOH B . 
EA 11 HOH 36   2136 1319 HOH HOH B . 
EA 11 HOH 37   2137 1345 HOH HOH B . 
EA 11 HOH 38   2138 914  HOH HOH B . 
EA 11 HOH 39   2139 1620 HOH HOH B . 
EA 11 HOH 40   2140 1739 HOH HOH B . 
EA 11 HOH 41   2141 2288 HOH HOH B . 
EA 11 HOH 42   2142 2020 HOH HOH B . 
EA 11 HOH 43   2143 1339 HOH HOH B . 
EA 11 HOH 44   2144 1706 HOH HOH B . 
EA 11 HOH 45   2145 2477 HOH HOH B . 
EA 11 HOH 46   2146 1024 HOH HOH B . 
EA 11 HOH 47   2147 2220 HOH HOH B . 
EA 11 HOH 48   2148 1862 HOH HOH B . 
EA 11 HOH 49   2149 289  HOH HOH B . 
EA 11 HOH 50   2150 796  HOH HOH B . 
EA 11 HOH 51   2151 713  HOH HOH B . 
EA 11 HOH 52   2152 2123 HOH HOH B . 
EA 11 HOH 53   2153 1086 HOH HOH B . 
EA 11 HOH 54   2154 770  HOH HOH B . 
EA 11 HOH 55   2155 801  HOH HOH B . 
EA 11 HOH 56   2156 890  HOH HOH B . 
EA 11 HOH 57   2157 883  HOH HOH B . 
EA 11 HOH 58   2158 506  HOH HOH B . 
EA 11 HOH 59   2159 2025 HOH HOH B . 
EA 11 HOH 60   2160 916  HOH HOH B . 
EA 11 HOH 61   2161 573  HOH HOH B . 
EA 11 HOH 62   2162 87   HOH HOH B . 
EA 11 HOH 63   2163 829  HOH HOH B . 
EA 11 HOH 64   2164 131  HOH HOH B . 
EA 11 HOH 65   2165 1603 HOH HOH B . 
EA 11 HOH 66   2166 964  HOH HOH B . 
EA 11 HOH 67   2167 1217 HOH HOH B . 
EA 11 HOH 68   2168 661  HOH HOH B . 
EA 11 HOH 69   2169 1416 HOH HOH B . 
EA 11 HOH 70   2170 285  HOH HOH B . 
EA 11 HOH 71   2171 1099 HOH HOH B . 
EA 11 HOH 72   2172 1971 HOH HOH B . 
EA 11 HOH 73   2173 2431 HOH HOH B . 
EA 11 HOH 74   2174 870  HOH HOH B . 
EA 11 HOH 75   2175 1248 HOH HOH B . 
EA 11 HOH 76   2176 932  HOH HOH B . 
EA 11 HOH 77   2177 831  HOH HOH B . 
EA 11 HOH 78   2178 268  HOH HOH B . 
EA 11 HOH 79   2179 2110 HOH HOH B . 
EA 11 HOH 80   2180 1150 HOH HOH B . 
EA 11 HOH 81   2181 2342 HOH HOH B . 
EA 11 HOH 82   2182 795  HOH HOH B . 
EA 11 HOH 83   2183 626  HOH HOH B . 
EA 11 HOH 84   2184 2096 HOH HOH B . 
EA 11 HOH 85   2185 367  HOH HOH B . 
EA 11 HOH 86   2186 2377 HOH HOH B . 
EA 11 HOH 87   2187 1055 HOH HOH B . 
EA 11 HOH 88   2188 2    HOH HOH B . 
EA 11 HOH 89   2189 2091 HOH HOH B . 
EA 11 HOH 90   2190 1078 HOH HOH B . 
EA 11 HOH 91   2191 1455 HOH HOH B . 
EA 11 HOH 92   2192 835  HOH HOH B . 
EA 11 HOH 93   2193 2402 HOH HOH B . 
EA 11 HOH 94   2194 1082 HOH HOH B . 
EA 11 HOH 95   2195 2030 HOH HOH B . 
EA 11 HOH 96   2196 834  HOH HOH B . 
EA 11 HOH 97   2197 65   HOH HOH B . 
EA 11 HOH 98   2198 1065 HOH HOH B . 
EA 11 HOH 99   2199 1698 HOH HOH B . 
EA 11 HOH 100  2200 337  HOH HOH B . 
EA 11 HOH 101  2201 1718 HOH HOH B . 
EA 11 HOH 102  2202 216  HOH HOH B . 
EA 11 HOH 103  2203 327  HOH HOH B . 
EA 11 HOH 104  2204 623  HOH HOH B . 
EA 11 HOH 105  2205 2296 HOH HOH B . 
EA 11 HOH 106  2206 1350 HOH HOH B . 
EA 11 HOH 107  2207 968  HOH HOH B . 
EA 11 HOH 108  2208 2173 HOH HOH B . 
EA 11 HOH 109  2209 882  HOH HOH B . 
EA 11 HOH 110  2210 299  HOH HOH B . 
EA 11 HOH 111  2211 1227 HOH HOH B . 
EA 11 HOH 112  2212 305  HOH HOH B . 
EA 11 HOH 113  2213 2215 HOH HOH B . 
EA 11 HOH 114  2214 1435 HOH HOH B . 
EA 11 HOH 115  2215 1442 HOH HOH B . 
EA 11 HOH 116  2216 115  HOH HOH B . 
EA 11 HOH 117  2217 43   HOH HOH B . 
EA 11 HOH 118  2218 1632 HOH HOH B . 
EA 11 HOH 119  2219 930  HOH HOH B . 
EA 11 HOH 120  2220 513  HOH HOH B . 
EA 11 HOH 121  2221 36   HOH HOH B . 
EA 11 HOH 122  2222 1856 HOH HOH B . 
EA 11 HOH 123  2223 143  HOH HOH B . 
EA 11 HOH 124  2224 171  HOH HOH B . 
EA 11 HOH 125  2225 476  HOH HOH B . 
EA 11 HOH 126  2226 903  HOH HOH B . 
EA 11 HOH 127  2227 291  HOH HOH B . 
EA 11 HOH 128  2228 911  HOH HOH B . 
EA 11 HOH 129  2229 1011 HOH HOH B . 
EA 11 HOH 130  2230 435  HOH HOH B . 
EA 11 HOH 131  2231 142  HOH HOH B . 
EA 11 HOH 132  2232 336  HOH HOH B . 
EA 11 HOH 133  2233 173  HOH HOH B . 
EA 11 HOH 134  2234 1128 HOH HOH B . 
EA 11 HOH 135  2235 1962 HOH HOH B . 
EA 11 HOH 136  2236 449  HOH HOH B . 
EA 11 HOH 137  2237 1013 HOH HOH B . 
EA 11 HOH 138  2238 595  HOH HOH B . 
EA 11 HOH 139  2239 1561 HOH HOH B . 
EA 11 HOH 140  2240 2479 HOH HOH B . 
EA 11 HOH 141  2241 275  HOH HOH B . 
EA 11 HOH 142  2242 533  HOH HOH B . 
EA 11 HOH 143  2243 7    HOH HOH B . 
EA 11 HOH 144  2244 429  HOH HOH B . 
EA 11 HOH 145  2245 1317 HOH HOH B . 
EA 11 HOH 146  2246 129  HOH HOH B . 
EA 11 HOH 147  2247 1708 HOH HOH B . 
EA 11 HOH 148  2248 433  HOH HOH B . 
EA 11 HOH 149  2249 2237 HOH HOH B . 
EA 11 HOH 150  2250 1833 HOH HOH B . 
EA 11 HOH 151  2251 356  HOH HOH B . 
EA 11 HOH 152  2252 474  HOH HOH B . 
EA 11 HOH 153  2253 17   HOH HOH B . 
EA 11 HOH 154  2254 385  HOH HOH B . 
EA 11 HOH 155  2255 46   HOH HOH B . 
EA 11 HOH 156  2256 20   HOH HOH B . 
EA 11 HOH 157  2257 1584 HOH HOH B . 
EA 11 HOH 158  2258 624  HOH HOH B . 
EA 11 HOH 159  2259 397  HOH HOH B . 
EA 11 HOH 160  2260 466  HOH HOH B . 
EA 11 HOH 161  2261 52   HOH HOH B . 
EA 11 HOH 162  2262 281  HOH HOH B . 
EA 11 HOH 163  2263 125  HOH HOH B . 
EA 11 HOH 164  2264 654  HOH HOH B . 
EA 11 HOH 165  2265 348  HOH HOH B . 
EA 11 HOH 166  2266 622  HOH HOH B . 
EA 11 HOH 167  2267 334  HOH HOH B . 
EA 11 HOH 168  2268 526  HOH HOH B . 
EA 11 HOH 169  2269 913  HOH HOH B . 
EA 11 HOH 170  2270 282  HOH HOH B . 
EA 11 HOH 171  2271 306  HOH HOH B . 
EA 11 HOH 172  2272 183  HOH HOH B . 
EA 11 HOH 173  2273 1121 HOH HOH B . 
EA 11 HOH 174  2274 1646 HOH HOH B . 
EA 11 HOH 175  2275 1865 HOH HOH B . 
EA 11 HOH 176  2276 1322 HOH HOH B . 
EA 11 HOH 177  2277 445  HOH HOH B . 
EA 11 HOH 178  2278 2098 HOH HOH B . 
EA 11 HOH 179  2279 1270 HOH HOH B . 
EA 11 HOH 180  2280 1616 HOH HOH B . 
EA 11 HOH 181  2281 636  HOH HOH B . 
EA 11 HOH 182  2282 134  HOH HOH B . 
EA 11 HOH 183  2283 78   HOH HOH B . 
EA 11 HOH 184  2284 383  HOH HOH B . 
EA 11 HOH 185  2285 460  HOH HOH B . 
EA 11 HOH 186  2286 505  HOH HOH B . 
EA 11 HOH 187  2287 823  HOH HOH B . 
EA 11 HOH 188  2288 296  HOH HOH B . 
EA 11 HOH 189  2289 746  HOH HOH B . 
EA 11 HOH 190  2290 1427 HOH HOH B . 
EA 11 HOH 191  2291 1867 HOH HOH B . 
EA 11 HOH 192  2292 188  HOH HOH B . 
EA 11 HOH 193  2293 96   HOH HOH B . 
EA 11 HOH 194  2294 2492 HOH HOH B . 
EA 11 HOH 195  2295 69   HOH HOH B . 
EA 11 HOH 196  2296 2332 HOH HOH B . 
EA 11 HOH 197  2297 1806 HOH HOH B . 
EA 11 HOH 198  2298 1930 HOH HOH B . 
EA 11 HOH 199  2299 1188 HOH HOH B . 
EA 11 HOH 200  2300 39   HOH HOH B . 
EA 11 HOH 201  2301 821  HOH HOH B . 
EA 11 HOH 202  2302 66   HOH HOH B . 
EA 11 HOH 203  2303 139  HOH HOH B . 
EA 11 HOH 204  2304 2090 HOH HOH B . 
EA 11 HOH 205  2305 952  HOH HOH B . 
EA 11 HOH 206  2306 657  HOH HOH B . 
EA 11 HOH 207  2307 1006 HOH HOH B . 
EA 11 HOH 208  2308 468  HOH HOH B . 
EA 11 HOH 209  2309 1284 HOH HOH B . 
EA 11 HOH 210  2310 354  HOH HOH B . 
EA 11 HOH 211  2311 1053 HOH HOH B . 
EA 11 HOH 212  2312 1917 HOH HOH B . 
EA 11 HOH 213  2313 1304 HOH HOH B . 
EA 11 HOH 214  2314 1405 HOH HOH B . 
EA 11 HOH 215  2315 664  HOH HOH B . 
EA 11 HOH 216  2316 1733 HOH HOH B . 
EA 11 HOH 217  2317 561  HOH HOH B . 
EA 11 HOH 218  2318 740  HOH HOH B . 
EA 11 HOH 219  2319 1479 HOH HOH B . 
EA 11 HOH 220  2320 956  HOH HOH B . 
EA 11 HOH 221  2321 2047 HOH HOH B . 
EA 11 HOH 222  2322 2179 HOH HOH B . 
EA 11 HOH 223  2323 338  HOH HOH B . 
EA 11 HOH 224  2324 376  HOH HOH B . 
EA 11 HOH 225  2325 453  HOH HOH B . 
EA 11 HOH 226  2326 2158 HOH HOH B . 
EA 11 HOH 227  2327 1487 HOH HOH B . 
EA 11 HOH 228  2328 91   HOH HOH B . 
EA 11 HOH 229  2329 739  HOH HOH B . 
EA 11 HOH 230  2330 1880 HOH HOH B . 
EA 11 HOH 231  2331 724  HOH HOH B . 
EA 11 HOH 232  2332 409  HOH HOH B . 
EA 11 HOH 233  2333 1242 HOH HOH B . 
EA 11 HOH 234  2334 552  HOH HOH B . 
EA 11 HOH 235  2335 1105 HOH HOH B . 
EA 11 HOH 236  2336 186  HOH HOH B . 
EA 11 HOH 237  2337 2486 HOH HOH B . 
EA 11 HOH 238  2338 1431 HOH HOH B . 
EA 11 HOH 239  2339 771  HOH HOH B . 
EA 11 HOH 240  2340 174  HOH HOH B . 
EA 11 HOH 241  2341 954  HOH HOH B . 
EA 11 HOH 242  2342 523  HOH HOH B . 
EA 11 HOH 243  2343 787  HOH HOH B . 
EA 11 HOH 244  2344 110  HOH HOH B . 
EA 11 HOH 245  2345 2143 HOH HOH B . 
EA 11 HOH 246  2346 1863 HOH HOH B . 
EA 11 HOH 247  2347 737  HOH HOH B . 
EA 11 HOH 248  2348 1749 HOH HOH B . 
EA 11 HOH 249  2349 949  HOH HOH B . 
EA 11 HOH 250  2350 398  HOH HOH B . 
EA 11 HOH 251  2351 588  HOH HOH B . 
EA 11 HOH 252  2352 265  HOH HOH B . 
EA 11 HOH 253  2353 2137 HOH HOH B . 
EA 11 HOH 254  2354 927  HOH HOH B . 
EA 11 HOH 255  2355 459  HOH HOH B . 
EA 11 HOH 256  2356 394  HOH HOH B . 
EA 11 HOH 257  2357 13   HOH HOH B . 
EA 11 HOH 258  2358 264  HOH HOH B . 
EA 11 HOH 259  2359 1422 HOH HOH B . 
EA 11 HOH 260  2360 102  HOH HOH B . 
EA 11 HOH 261  2361 53   HOH HOH B . 
EA 11 HOH 262  2362 119  HOH HOH B . 
EA 11 HOH 263  2363 763  HOH HOH B . 
EA 11 HOH 264  2364 875  HOH HOH B . 
EA 11 HOH 265  2365 379  HOH HOH B . 
EA 11 HOH 266  2366 1117 HOH HOH B . 
EA 11 HOH 267  2367 748  HOH HOH B . 
EA 11 HOH 268  2368 8    HOH HOH B . 
EA 11 HOH 269  2369 72   HOH HOH B . 
EA 11 HOH 270  2370 168  HOH HOH B . 
EA 11 HOH 271  2371 448  HOH HOH B . 
EA 11 HOH 272  2372 68   HOH HOH B . 
EA 11 HOH 273  2373 670  HOH HOH B . 
EA 11 HOH 274  2374 987  HOH HOH B . 
EA 11 HOH 275  2375 572  HOH HOH B . 
EA 11 HOH 276  2376 5    HOH HOH B . 
EA 11 HOH 277  2377 847  HOH HOH B . 
EA 11 HOH 278  2378 1154 HOH HOH B . 
EA 11 HOH 279  2379 160  HOH HOH B . 
EA 11 HOH 280  2380 1118 HOH HOH B . 
EA 11 HOH 281  2381 284  HOH HOH B . 
EA 11 HOH 282  2382 224  HOH HOH B . 
EA 11 HOH 283  2383 1939 HOH HOH B . 
EA 11 HOH 284  2384 390  HOH HOH B . 
EA 11 HOH 285  2385 1208 HOH HOH B . 
EA 11 HOH 286  2386 1931 HOH HOH B . 
EA 11 HOH 287  2387 203  HOH HOH B . 
EA 11 HOH 288  2388 1349 HOH HOH B . 
EA 11 HOH 289  2389 669  HOH HOH B . 
EA 11 HOH 290  2390 2324 HOH HOH B . 
EA 11 HOH 291  2391 521  HOH HOH B . 
EA 11 HOH 292  2392 1850 HOH HOH B . 
EA 11 HOH 293  2393 1119 HOH HOH B . 
EA 11 HOH 294  2394 1001 HOH HOH B . 
EA 11 HOH 295  2395 83   HOH HOH B . 
EA 11 HOH 296  2396 384  HOH HOH B . 
EA 11 HOH 297  2397 699  HOH HOH B . 
EA 11 HOH 298  2398 1    HOH HOH B . 
EA 11 HOH 299  2399 509  HOH HOH B . 
EA 11 HOH 300  2400 2464 HOH HOH B . 
EA 11 HOH 301  2401 659  HOH HOH B . 
EA 11 HOH 302  2402 710  HOH HOH B . 
EA 11 HOH 303  2403 1631 HOH HOH B . 
EA 11 HOH 304  2404 1869 HOH HOH B . 
EA 11 HOH 305  2405 401  HOH HOH B . 
EA 11 HOH 306  2406 1069 HOH HOH B . 
EA 11 HOH 307  2407 230  HOH HOH B . 
EA 11 HOH 308  2408 434  HOH HOH B . 
EA 11 HOH 309  2409 1433 HOH HOH B . 
EA 11 HOH 310  2410 649  HOH HOH B . 
EA 11 HOH 311  2411 1019 HOH HOH B . 
EA 11 HOH 312  2412 1832 HOH HOH B . 
EA 11 HOH 313  2413 606  HOH HOH B . 
EA 11 HOH 314  2414 26   HOH HOH B . 
EA 11 HOH 315  2415 734  HOH HOH B . 
EA 11 HOH 316  2416 121  HOH HOH B . 
EA 11 HOH 317  2417 1124 HOH HOH B . 
EA 11 HOH 318  2418 979  HOH HOH B . 
EA 11 HOH 319  2419 546  HOH HOH B . 
EA 11 HOH 320  2420 59   HOH HOH B . 
EA 11 HOH 321  2421 1976 HOH HOH B . 
EA 11 HOH 322  2422 628  HOH HOH B . 
EA 11 HOH 323  2423 1612 HOH HOH B . 
EA 11 HOH 324  2424 270  HOH HOH B . 
EA 11 HOH 325  2425 2423 HOH HOH B . 
EA 11 HOH 326  2426 602  HOH HOH B . 
EA 11 HOH 327  2427 756  HOH HOH B . 
EA 11 HOH 328  2428 1014 HOH HOH B . 
EA 11 HOH 329  2429 1409 HOH HOH B . 
EA 11 HOH 330  2430 82   HOH HOH B . 
EA 11 HOH 331  2431 1029 HOH HOH B . 
EA 11 HOH 332  2432 789  HOH HOH B . 
EA 11 HOH 333  2433 814  HOH HOH B . 
EA 11 HOH 334  2434 576  HOH HOH B . 
EA 11 HOH 335  2435 1453 HOH HOH B . 
EA 11 HOH 336  2436 1870 HOH HOH B . 
EA 11 HOH 337  2437 1171 HOH HOH B . 
EA 11 HOH 338  2438 2384 HOH HOH B . 
EA 11 HOH 339  2439 1674 HOH HOH B . 
EA 11 HOH 340  2440 762  HOH HOH B . 
EA 11 HOH 341  2441 2347 HOH HOH B . 
EA 11 HOH 342  2442 1370 HOH HOH B . 
EA 11 HOH 343  2443 440  HOH HOH B . 
EA 11 HOH 344  2444 765  HOH HOH B . 
EA 11 HOH 345  2445 75   HOH HOH B . 
EA 11 HOH 346  2446 30   HOH HOH B . 
EA 11 HOH 347  2447 88   HOH HOH B . 
EA 11 HOH 348  2448 2370 HOH HOH B . 
EA 11 HOH 349  2449 700  HOH HOH B . 
EA 11 HOH 350  2450 10   HOH HOH B . 
EA 11 HOH 351  2451 133  HOH HOH B . 
EA 11 HOH 352  2452 254  HOH HOH B . 
EA 11 HOH 353  2453 2125 HOH HOH B . 
EA 11 HOH 354  2454 936  HOH HOH B . 
EA 11 HOH 355  2455 247  HOH HOH B . 
EA 11 HOH 356  2456 315  HOH HOH B . 
EA 11 HOH 357  2457 2432 HOH HOH B . 
EA 11 HOH 358  2458 222  HOH HOH B . 
EA 11 HOH 359  2459 141  HOH HOH B . 
EA 11 HOH 360  2460 263  HOH HOH B . 
EA 11 HOH 361  2461 382  HOH HOH B . 
EA 11 HOH 362  2462 2066 HOH HOH B . 
EA 11 HOH 363  2463 1576 HOH HOH B . 
EA 11 HOH 364  2464 786  HOH HOH B . 
EA 11 HOH 365  2465 1162 HOH HOH B . 
EA 11 HOH 366  2466 146  HOH HOH B . 
EA 11 HOH 367  2467 487  HOH HOH B . 
EA 11 HOH 368  2468 935  HOH HOH B . 
EA 11 HOH 369  2469 1992 HOH HOH B . 
EA 11 HOH 370  2470 349  HOH HOH B . 
EA 11 HOH 371  2471 811  HOH HOH B . 
EA 11 HOH 372  2472 288  HOH HOH B . 
EA 11 HOH 373  2473 1108 HOH HOH B . 
EA 11 HOH 374  2474 280  HOH HOH B . 
EA 11 HOH 375  2475 535  HOH HOH B . 
EA 11 HOH 376  2476 1634 HOH HOH B . 
EA 11 HOH 377  2477 386  HOH HOH B . 
EA 11 HOH 378  2478 1318 HOH HOH B . 
EA 11 HOH 379  2479 286  HOH HOH B . 
EA 11 HOH 380  2480 1630 HOH HOH B . 
EA 11 HOH 381  2481 333  HOH HOH B . 
EA 11 HOH 382  2482 1583 HOH HOH B . 
EA 11 HOH 383  2483 2228 HOH HOH B . 
EA 11 HOH 384  2484 287  HOH HOH B . 
EA 11 HOH 385  2485 906  HOH HOH B . 
EA 11 HOH 386  2486 1821 HOH HOH B . 
EA 11 HOH 387  2487 950  HOH HOH B . 
EA 11 HOH 388  2488 766  HOH HOH B . 
EA 11 HOH 389  2489 995  HOH HOH B . 
EA 11 HOH 390  2490 1288 HOH HOH B . 
EA 11 HOH 391  2491 694  HOH HOH B . 
EA 11 HOH 392  2492 261  HOH HOH B . 
EA 11 HOH 393  2493 2148 HOH HOH B . 
EA 11 HOH 394  2494 725  HOH HOH B . 
EA 11 HOH 395  2495 190  HOH HOH B . 
EA 11 HOH 396  2496 350  HOH HOH B . 
EA 11 HOH 397  2497 959  HOH HOH B . 
EA 11 HOH 398  2498 2185 HOH HOH B . 
EA 11 HOH 399  2499 690  HOH HOH B . 
EA 11 HOH 400  2500 206  HOH HOH B . 
EA 11 HOH 401  2501 352  HOH HOH B . 
EA 11 HOH 402  2502 353  HOH HOH B . 
EA 11 HOH 403  2503 2151 HOH HOH B . 
EA 11 HOH 404  2504 34   HOH HOH B . 
EA 11 HOH 405  2505 2023 HOH HOH B . 
EA 11 HOH 406  2506 1510 HOH HOH B . 
EA 11 HOH 407  2507 64   HOH HOH B . 
EA 11 HOH 408  2508 310  HOH HOH B . 
EA 11 HOH 409  2509 2071 HOH HOH B . 
EA 11 HOH 410  2510 1101 HOH HOH B . 
EA 11 HOH 411  2511 192  HOH HOH B . 
EA 11 HOH 412  2512 1244 HOH HOH B . 
EA 11 HOH 413  2513 1461 HOH HOH B . 
EA 11 HOH 414  2514 130  HOH HOH B . 
EA 11 HOH 415  2515 2067 HOH HOH B . 
EA 11 HOH 416  2516 346  HOH HOH B . 
EA 11 HOH 417  2517 2188 HOH HOH B . 
EA 11 HOH 418  2518 864  HOH HOH B . 
EA 11 HOH 419  2519 406  HOH HOH B . 
EA 11 HOH 420  2520 646  HOH HOH B . 
EA 11 HOH 421  2521 923  HOH HOH B . 
EA 11 HOH 422  2522 6    HOH HOH B . 
EA 11 HOH 423  2523 637  HOH HOH B . 
EA 11 HOH 424  2524 1666 HOH HOH B . 
EA 11 HOH 425  2525 591  HOH HOH B . 
EA 11 HOH 426  2526 539  HOH HOH B . 
EA 11 HOH 427  2527 182  HOH HOH B . 
EA 11 HOH 428  2528 2084 HOH HOH B . 
EA 11 HOH 429  2529 58   HOH HOH B . 
EA 11 HOH 430  2530 410  HOH HOH B . 
EA 11 HOH 431  2531 761  HOH HOH B . 
EA 11 HOH 432  2532 138  HOH HOH B . 
EA 11 HOH 433  2533 2340 HOH HOH B . 
EA 11 HOH 434  2534 893  HOH HOH B . 
EA 11 HOH 435  2535 257  HOH HOH B . 
EA 11 HOH 436  2536 2309 HOH HOH B . 
EA 11 HOH 437  2537 928  HOH HOH B . 
EA 11 HOH 438  2538 482  HOH HOH B . 
EA 11 HOH 439  2539 95   HOH HOH B . 
EA 11 HOH 440  2540 89   HOH HOH B . 
EA 11 HOH 441  2541 1177 HOH HOH B . 
EA 11 HOH 442  2542 104  HOH HOH B . 
EA 11 HOH 443  2543 2083 HOH HOH B . 
EA 11 HOH 444  2544 366  HOH HOH B . 
EA 11 HOH 445  2545 2253 HOH HOH B . 
EA 11 HOH 446  2546 57   HOH HOH B . 
EA 11 HOH 447  2547 1365 HOH HOH B . 
EA 11 HOH 448  2548 1254 HOH HOH B . 
EA 11 HOH 449  2549 295  HOH HOH B . 
EA 11 HOH 450  2550 1973 HOH HOH B . 
EA 11 HOH 451  2551 582  HOH HOH B . 
EA 11 HOH 452  2552 1004 HOH HOH B . 
EA 11 HOH 453  2553 279  HOH HOH B . 
EA 11 HOH 454  2554 220  HOH HOH B . 
EA 11 HOH 455  2555 1279 HOH HOH B . 
EA 11 HOH 456  2556 1493 HOH HOH B . 
EA 11 HOH 457  2557 118  HOH HOH B . 
EA 11 HOH 458  2558 70   HOH HOH B . 
EA 11 HOH 459  2559 117  HOH HOH B . 
EA 11 HOH 460  2560 152  HOH HOH B . 
EA 11 HOH 461  2561 863  HOH HOH B . 
EA 11 HOH 462  2562 1120 HOH HOH B . 
EA 11 HOH 463  2563 438  HOH HOH B . 
EA 11 HOH 464  2564 235  HOH HOH B . 
EA 11 HOH 465  2565 1047 HOH HOH B . 
EA 11 HOH 466  2566 1260 HOH HOH B . 
EA 11 HOH 467  2567 1914 HOH HOH B . 
EA 11 HOH 468  2568 1382 HOH HOH B . 
EA 11 HOH 469  2569 148  HOH HOH B . 
EA 11 HOH 470  2570 297  HOH HOH B . 
EA 11 HOH 471  2571 2159 HOH HOH B . 
EA 11 HOH 472  2572 2463 HOH HOH B . 
EA 11 HOH 473  2573 524  HOH HOH B . 
EA 11 HOH 474  2574 970  HOH HOH B . 
EA 11 HOH 475  2575 2129 HOH HOH B . 
EA 11 HOH 476  2576 200  HOH HOH B . 
EA 11 HOH 477  2577 319  HOH HOH B . 
EA 11 HOH 478  2578 47   HOH HOH B . 
EA 11 HOH 479  2579 1503 HOH HOH B . 
EA 11 HOH 480  2580 1535 HOH HOH B . 
EA 11 HOH 481  2581 399  HOH HOH B . 
EA 11 HOH 482  2582 839  HOH HOH B . 
EA 11 HOH 483  2583 491  HOH HOH B . 
EA 11 HOH 484  2584 697  HOH HOH B . 
EA 11 HOH 485  2585 234  HOH HOH B . 
EA 11 HOH 486  2586 800  HOH HOH B . 
EA 11 HOH 487  2587 1447 HOH HOH B . 
EA 11 HOH 488  2588 1588 HOH HOH B . 
EA 11 HOH 489  2589 534  HOH HOH B . 
EA 11 HOH 490  2590 985  HOH HOH B . 
EA 11 HOH 491  2591 1333 HOH HOH B . 
EA 11 HOH 492  2592 14   HOH HOH B . 
EA 11 HOH 493  2593 31   HOH HOH B . 
EA 11 HOH 494  2594 322  HOH HOH B . 
EA 11 HOH 495  2595 493  HOH HOH B . 
EA 11 HOH 496  2596 1115 HOH HOH B . 
EA 11 HOH 497  2597 2032 HOH HOH B . 
EA 11 HOH 498  2598 41   HOH HOH B . 
EA 11 HOH 499  2599 1502 HOH HOH B . 
EA 11 HOH 500  2600 38   HOH HOH B . 
EA 11 HOH 501  2601 228  HOH HOH B . 
EA 11 HOH 502  2602 773  HOH HOH B . 
EA 11 HOH 503  2603 960  HOH HOH B . 
EA 11 HOH 504  2604 973  HOH HOH B . 
EA 11 HOH 505  2605 1145 HOH HOH B . 
EA 11 HOH 506  2606 1168 HOH HOH B . 
EA 11 HOH 507  2607 820  HOH HOH B . 
EA 11 HOH 508  2608 1712 HOH HOH B . 
EA 11 HOH 509  2609 638  HOH HOH B . 
EA 11 HOH 510  2610 122  HOH HOH B . 
EA 11 HOH 511  2611 1037 HOH HOH B . 
EA 11 HOH 512  2612 1070 HOH HOH B . 
EA 11 HOH 513  2613 632  HOH HOH B . 
EA 11 HOH 514  2614 298  HOH HOH B . 
EA 11 HOH 515  2615 939  HOH HOH B . 
EA 11 HOH 516  2616 51   HOH HOH B . 
EA 11 HOH 517  2617 250  HOH HOH B . 
EA 11 HOH 518  2618 749  HOH HOH B . 
EA 11 HOH 519  2619 743  HOH HOH B . 
EA 11 HOH 520  2620 225  HOH HOH B . 
EA 11 HOH 521  2621 237  HOH HOH B . 
EA 11 HOH 522  2622 832  HOH HOH B . 
EA 11 HOH 523  2623 580  HOH HOH B . 
EA 11 HOH 524  2624 252  HOH HOH B . 
EA 11 HOH 525  2625 1025 HOH HOH B . 
EA 11 HOH 526  2626 843  HOH HOH B . 
EA 11 HOH 527  2627 668  HOH HOH B . 
EA 11 HOH 528  2628 240  HOH HOH B . 
EA 11 HOH 529  2629 1530 HOH HOH B . 
EA 11 HOH 530  2630 716  HOH HOH B . 
EA 11 HOH 531  2631 1660 HOH HOH B . 
EA 11 HOH 532  2632 2269 HOH HOH B . 
EA 11 HOH 533  2633 1310 HOH HOH B . 
EA 11 HOH 534  2634 1607 HOH HOH B . 
EA 11 HOH 535  2635 553  HOH HOH B . 
EA 11 HOH 536  2636 199  HOH HOH B . 
EA 11 HOH 537  2637 768  HOH HOH B . 
EA 11 HOH 538  2638 2442 HOH HOH B . 
EA 11 HOH 539  2639 94   HOH HOH B . 
EA 11 HOH 540  2640 2199 HOH HOH B . 
EA 11 HOH 541  2641 1351 HOH HOH B . 
EA 11 HOH 542  2642 1114 HOH HOH B . 
EA 11 HOH 543  2643 85   HOH HOH B . 
EA 11 HOH 544  2644 116  HOH HOH B . 
EA 11 HOH 545  2645 145  HOH HOH B . 
EA 11 HOH 546  2646 759  HOH HOH B . 
EA 11 HOH 547  2647 388  HOH HOH B . 
EA 11 HOH 548  2648 218  HOH HOH B . 
EA 11 HOH 549  2649 944  HOH HOH B . 
EA 11 HOH 550  2650 597  HOH HOH B . 
EA 11 HOH 551  2651 1363 HOH HOH B . 
EA 11 HOH 552  2652 363  HOH HOH B . 
EA 11 HOH 553  2653 1211 HOH HOH B . 
EA 11 HOH 554  2654 719  HOH HOH B . 
EA 11 HOH 555  2655 940  HOH HOH B . 
EA 11 HOH 556  2656 805  HOH HOH B . 
EA 11 HOH 557  2657 672  HOH HOH B . 
EA 11 HOH 558  2658 1579 HOH HOH B . 
EA 11 HOH 559  2659 372  HOH HOH B . 
EA 11 HOH 560  2660 1911 HOH HOH B . 
EA 11 HOH 561  2661 495  HOH HOH B . 
EA 11 HOH 562  2662 798  HOH HOH B . 
EA 11 HOH 563  2663 808  HOH HOH B . 
EA 11 HOH 564  2664 416  HOH HOH B . 
EA 11 HOH 565  2665 931  HOH HOH B . 
EA 11 HOH 566  2666 2280 HOH HOH B . 
EA 11 HOH 567  2667 919  HOH HOH B . 
EA 11 HOH 568  2668 262  HOH HOH B . 
EA 11 HOH 569  2669 227  HOH HOH B . 
EA 11 HOH 570  2670 1026 HOH HOH B . 
EA 11 HOH 571  2671 656  HOH HOH B . 
EA 11 HOH 572  2672 3    HOH HOH B . 
EA 11 HOH 573  2673 1421 HOH HOH B . 
EA 11 HOH 574  2674 77   HOH HOH B . 
EA 11 HOH 575  2675 375  HOH HOH B . 
EA 11 HOH 576  2676 1474 HOH HOH B . 
EA 11 HOH 577  2677 1060 HOH HOH B . 
EA 11 HOH 578  2678 132  HOH HOH B . 
EA 11 HOH 579  2679 1156 HOH HOH B . 
EA 11 HOH 580  2680 1186 HOH HOH B . 
EA 11 HOH 581  2681 593  HOH HOH B . 
EA 11 HOH 582  2682 1476 HOH HOH B . 
EA 11 HOH 583  2683 1088 HOH HOH B . 
EA 11 HOH 584  2684 767  HOH HOH B . 
EA 11 HOH 585  2685 496  HOH HOH B . 
EA 11 HOH 586  2686 92   HOH HOH B . 
EA 11 HOH 587  2687 1361 HOH HOH B . 
EA 11 HOH 588  2688 807  HOH HOH B . 
EA 11 HOH 589  2689 812  HOH HOH B . 
EA 11 HOH 590  2690 900  HOH HOH B . 
EA 11 HOH 591  2691 2460 HOH HOH B . 
EA 11 HOH 592  2692 393  HOH HOH B . 
EA 11 HOH 593  2693 902  HOH HOH B . 
EA 11 HOH 594  2694 232  HOH HOH B . 
EA 11 HOH 595  2695 848  HOH HOH B . 
EA 11 HOH 596  2696 1604 HOH HOH B . 
EA 11 HOH 597  2697 341  HOH HOH B . 
EA 11 HOH 598  2698 365  HOH HOH B . 
EA 11 HOH 599  2699 953  HOH HOH B . 
EA 11 HOH 600  2700 211  HOH HOH B . 
EA 11 HOH 601  2701 326  HOH HOH B . 
EA 11 HOH 602  2702 577  HOH HOH B . 
EA 11 HOH 603  2703 1825 HOH HOH B . 
EA 11 HOH 604  2704 1438 HOH HOH B . 
EA 11 HOH 605  2705 1572 HOH HOH B . 
EA 11 HOH 606  2706 307  HOH HOH B . 
EA 11 HOH 607  2707 417  HOH HOH B . 
EA 11 HOH 608  2708 84   HOH HOH B . 
EA 11 HOH 609  2709 518  HOH HOH B . 
EA 11 HOH 610  2710 45   HOH HOH B . 
EA 11 HOH 611  2711 1202 HOH HOH B . 
EA 11 HOH 612  2712 621  HOH HOH B . 
EA 11 HOH 613  2713 317  HOH HOH B . 
EA 11 HOH 614  2714 1969 HOH HOH B . 
EA 11 HOH 615  2715 2042 HOH HOH B . 
EA 11 HOH 616  2716 887  HOH HOH B . 
EA 11 HOH 617  2717 2451 HOH HOH B . 
EA 11 HOH 618  2718 1822 HOH HOH B . 
EA 11 HOH 619  2719 1074 HOH HOH B . 
EA 11 HOH 620  2720 838  HOH HOH B . 
EA 11 HOH 621  2721 639  HOH HOH B . 
EA 11 HOH 622  2722 2364 HOH HOH B . 
EA 11 HOH 623  2723 1243 HOH HOH B . 
EA 11 HOH 624  2724 569  HOH HOH B . 
EA 11 HOH 625  2725 373  HOH HOH B . 
EA 11 HOH 626  2726 403  HOH HOH B . 
EA 11 HOH 627  2727 259  HOH HOH B . 
EA 11 HOH 628  2728 1144 HOH HOH B . 
EA 11 HOH 629  2729 266  HOH HOH B . 
EA 11 HOH 630  2730 1571 HOH HOH B . 
EA 11 HOH 631  2731 1125 HOH HOH B . 
EA 11 HOH 632  2732 918  HOH HOH B . 
EA 11 HOH 633  2733 1982 HOH HOH B . 
EA 11 HOH 634  2734 464  HOH HOH B . 
EA 11 HOH 635  2735 490  HOH HOH B . 
EA 11 HOH 636  2736 1759 HOH HOH B . 
EA 11 HOH 637  2737 2154 HOH HOH B . 
EA 11 HOH 638  2738 538  HOH HOH B . 
EA 11 HOH 639  2739 741  HOH HOH B . 
EA 11 HOH 640  2740 794  HOH HOH B . 
EA 11 HOH 641  2741 880  HOH HOH B . 
EA 11 HOH 642  2742 2063 HOH HOH B . 
EA 11 HOH 643  2743 2493 HOH HOH B . 
EA 11 HOH 644  2744 1307 HOH HOH B . 
EA 11 HOH 645  2745 665  HOH HOH B . 
EA 11 HOH 646  2746 1633 HOH HOH B . 
EA 11 HOH 647  2747 163  HOH HOH B . 
EA 11 HOH 648  2748 309  HOH HOH B . 
EA 11 HOH 649  2749 1281 HOH HOH B . 
EA 11 HOH 650  2750 404  HOH HOH B . 
EA 11 HOH 651  2751 1452 HOH HOH B . 
EA 11 HOH 652  2752 2303 HOH HOH B . 
EA 11 HOH 653  2753 1617 HOH HOH B . 
EA 11 HOH 654  2754 2241 HOH HOH B . 
EA 11 HOH 655  2755 123  HOH HOH B . 
EA 11 HOH 656  2756 1524 HOH HOH B . 
EA 11 HOH 657  2757 517  HOH HOH B . 
EA 11 HOH 658  2758 590  HOH HOH B . 
EA 11 HOH 659  2759 2121 HOH HOH B . 
EA 11 HOH 660  2760 1302 HOH HOH B . 
EA 11 HOH 661  2761 24   HOH HOH B . 
EA 11 HOH 662  2762 208  HOH HOH B . 
EA 11 HOH 663  2763 1259 HOH HOH B . 
EA 11 HOH 664  2764 1311 HOH HOH B . 
EA 11 HOH 665  2765 512  HOH HOH B . 
EA 11 HOH 666  2766 1723 HOH HOH B . 
EA 11 HOH 667  2767 172  HOH HOH B . 
EA 11 HOH 668  2768 881  HOH HOH B . 
EA 11 HOH 669  2769 529  HOH HOH B . 
EA 11 HOH 670  2770 892  HOH HOH B . 
EA 11 HOH 671  2771 1541 HOH HOH B . 
EA 11 HOH 672  2772 414  HOH HOH B . 
EA 11 HOH 673  2773 895  HOH HOH B . 
EA 11 HOH 674  2774 488  HOH HOH B . 
EA 11 HOH 675  2775 508  HOH HOH B . 
EA 11 HOH 676  2776 2274 HOH HOH B . 
EA 11 HOH 677  2777 1906 HOH HOH B . 
EA 11 HOH 678  2778 1543 HOH HOH B . 
EA 11 HOH 679  2779 702  HOH HOH B . 
EA 11 HOH 680  2780 1828 HOH HOH B . 
EA 11 HOH 681  2781 342  HOH HOH B . 
EA 11 HOH 682  2782 2026 HOH HOH B . 
EA 11 HOH 683  2783 1951 HOH HOH B . 
EA 11 HOH 684  2784 994  HOH HOH B . 
EA 11 HOH 685  2785 1845 HOH HOH B . 
EA 11 HOH 686  2786 2206 HOH HOH B . 
EA 11 HOH 687  2787 71   HOH HOH B . 
EA 11 HOH 688  2788 1778 HOH HOH B . 
EA 11 HOH 689  2789 204  HOH HOH B . 
EA 11 HOH 690  2790 2031 HOH HOH B . 
EA 11 HOH 691  2791 1326 HOH HOH B . 
EA 11 HOH 692  2792 175  HOH HOH B . 
EA 11 HOH 693  2793 522  HOH HOH B . 
EA 11 HOH 694  2794 418  HOH HOH B . 
EA 11 HOH 695  2795 744  HOH HOH B . 
EA 11 HOH 696  2796 475  HOH HOH B . 
EA 11 HOH 697  2797 1677 HOH HOH B . 
EA 11 HOH 698  2798 2263 HOH HOH B . 
EA 11 HOH 699  2799 1844 HOH HOH B . 
EA 11 HOH 700  2800 1255 HOH HOH B . 
EA 11 HOH 701  2801 647  HOH HOH B . 
EA 11 HOH 702  2802 189  HOH HOH B . 
EA 11 HOH 703  2803 1673 HOH HOH B . 
EA 11 HOH 704  2804 108  HOH HOH B . 
EA 11 HOH 705  2805 554  HOH HOH B . 
EA 11 HOH 706  2806 2079 HOH HOH B . 
EA 11 HOH 707  2807 1126 HOH HOH B . 
EA 11 HOH 708  2808 2491 HOH HOH B . 
EA 11 HOH 709  2809 1439 HOH HOH B . 
EA 11 HOH 710  2810 97   HOH HOH B . 
EA 11 HOH 711  2811 1022 HOH HOH B . 
EA 11 HOH 712  2812 1191 HOH HOH B . 
EA 11 HOH 713  2813 2356 HOH HOH B . 
EA 11 HOH 714  2814 1669 HOH HOH B . 
EA 11 HOH 715  2815 470  HOH HOH B . 
EA 11 HOH 716  2816 2201 HOH HOH B . 
EA 11 HOH 717  2817 2312 HOH HOH B . 
EA 11 HOH 718  2818 1797 HOH HOH B . 
EA 11 HOH 719  2819 1342 HOH HOH B . 
EA 11 HOH 720  2820 436  HOH HOH B . 
EA 11 HOH 721  2821 557  HOH HOH B . 
EA 11 HOH 722  2822 586  HOH HOH B . 
EA 11 HOH 723  2823 974  HOH HOH B . 
EA 11 HOH 724  2824 1638 HOH HOH B . 
EA 11 HOH 725  2825 1049 HOH HOH B . 
EA 11 HOH 726  2826 1544 HOH HOH B . 
EA 11 HOH 727  2827 412  HOH HOH B . 
EA 11 HOH 728  2828 461  HOH HOH B . 
EA 11 HOH 729  2829 1068 HOH HOH B . 
EA 11 HOH 730  2830 955  HOH HOH B . 
EA 11 HOH 731  2831 2102 HOH HOH B . 
EA 11 HOH 732  2832 1210 HOH HOH B . 
EA 11 HOH 733  2833 1    HOH HOH B . 
EA 11 HOH 734  2834 1695 HOH HOH B . 
EA 11 HOH 735  2835 1023 HOH HOH B . 
EA 11 HOH 736  2836 961  HOH HOH B . 
EA 11 HOH 737  2837 98   HOH HOH B . 
EA 11 HOH 738  2838 1611 HOH HOH B . 
EA 11 HOH 739  2839 2360 HOH HOH B . 
EA 11 HOH 740  2840 1505 HOH HOH B . 
EA 11 HOH 741  2841 2085 HOH HOH B . 
EA 11 HOH 742  2842 302  HOH HOH B . 
EA 11 HOH 743  2843 1233 HOH HOH B . 
EA 11 HOH 744  2844 1656 HOH HOH B . 
EA 11 HOH 745  2845 1215 HOH HOH B . 
EA 11 HOH 746  2846 2252 HOH HOH B . 
EA 11 HOH 747  2847 631  HOH HOH B . 
EA 11 HOH 748  2848 1547 HOH HOH B . 
EA 11 HOH 749  2849 601  HOH HOH B . 
EA 11 HOH 750  2850 1636 HOH HOH B . 
EA 11 HOH 751  2851 2349 HOH HOH B . 
EA 11 HOH 752  2852 415  HOH HOH B . 
EA 11 HOH 753  2853 1807 HOH HOH B . 
EA 11 HOH 754  2854 1895 HOH HOH B . 
EA 11 HOH 755  2855 2380 HOH HOH B . 
EA 11 HOH 756  2856 2343 HOH HOH B . 
EA 11 HOH 757  2857 2433 HOH HOH B . 
EA 11 HOH 758  2858 992  HOH HOH B . 
EA 11 HOH 759  2859 2106 HOH HOH B . 
EA 11 HOH 760  2860 1512 HOH HOH B . 
EA 11 HOH 761  2861 2327 HOH HOH B . 
EA 11 HOH 762  2862 2041 HOH HOH B . 
EA 11 HOH 763  2863 1944 HOH HOH B . 
EA 11 HOH 764  2864 696  HOH HOH B . 
EA 11 HOH 765  2865 691  HOH HOH B . 
EA 11 HOH 766  2866 1705 HOH HOH B . 
EA 11 HOH 767  2867 784  HOH HOH B . 
EA 11 HOH 768  2868 1975 HOH HOH B . 
EA 11 HOH 769  2869 1680 HOH HOH B . 
EA 11 HOH 770  2870 679  HOH HOH B . 
EA 11 HOH 771  2871 2060 HOH HOH B . 
EA 11 HOH 772  2872 1849 HOH HOH B . 
EA 11 HOH 773  2873 1050 HOH HOH B . 
EA 11 HOH 774  2874 166  HOH HOH B . 
EA 11 HOH 775  2875 1359 HOH HOH B . 
EA 11 HOH 776  2876 2453 HOH HOH B . 
EA 11 HOH 777  2877 1353 HOH HOH B . 
EA 11 HOH 778  2878 1331 HOH HOH B . 
EA 11 HOH 779  2879 788  HOH HOH B . 
EA 11 HOH 780  2880 1558 HOH HOH B . 
EA 11 HOH 781  2881 885  HOH HOH B . 
EA 11 HOH 782  2882 1896 HOH HOH B . 
EA 11 HOH 783  2883 1182 HOH HOH B . 
EA 11 HOH 784  2884 1309 HOH HOH B . 
EA 11 HOH 785  2885 2153 HOH HOH B . 
EA 11 HOH 786  2886 2072 HOH HOH B . 
EA 11 HOH 787  2887 609  HOH HOH B . 
EA 11 HOH 788  2888 1459 HOH HOH B . 
EA 11 HOH 789  2889 1035 HOH HOH B . 
EA 11 HOH 790  2890 1522 HOH HOH B . 
EA 11 HOH 791  2891 1221 HOH HOH B . 
EA 11 HOH 792  2892 1641 HOH HOH B . 
EA 11 HOH 793  2893 1948 HOH HOH B . 
EA 11 HOH 794  2894 2193 HOH HOH B . 
EA 11 HOH 795  2895 1597 HOH HOH B . 
EA 11 HOH 796  2896 1873 HOH HOH B . 
EA 11 HOH 797  2897 1538 HOH HOH B . 
EA 11 HOH 798  2898 1292 HOH HOH B . 
EA 11 HOH 799  2899 1993 HOH HOH B . 
EA 11 HOH 800  2900 1672 HOH HOH B . 
EA 11 HOH 801  2901 2424 HOH HOH B . 
EA 11 HOH 802  2902 2287 HOH HOH B . 
EA 11 HOH 803  2903 1954 HOH HOH B . 
EA 11 HOH 804  2904 1224 HOH HOH B . 
EA 11 HOH 805  2905 499  HOH HOH B . 
EA 11 HOH 806  2906 1231 HOH HOH B . 
EA 11 HOH 807  2907 1506 HOH HOH B . 
EA 11 HOH 808  2908 1688 HOH HOH B . 
EA 11 HOH 809  2909 2302 HOH HOH B . 
EA 11 HOH 810  2910 1655 HOH HOH B . 
EA 11 HOH 811  2911 1523 HOH HOH B . 
EA 11 HOH 812  2912 1209 HOH HOH B . 
EA 11 HOH 813  2913 849  HOH HOH B . 
EA 11 HOH 814  2914 2160 HOH HOH B . 
EA 11 HOH 815  2915 1955 HOH HOH B . 
EA 11 HOH 816  2916 2435 HOH HOH B . 
EA 11 HOH 817  2917 1963 HOH HOH B . 
EA 11 HOH 818  2918 1282 HOH HOH B . 
EA 11 HOH 819  2919 2186 HOH HOH B . 
EA 11 HOH 820  2920 2255 HOH HOH B . 
EA 11 HOH 821  2921 1384 HOH HOH B . 
EA 11 HOH 822  2922 1970 HOH HOH B . 
EA 11 HOH 823  2923 1230 HOH HOH B . 
EA 11 HOH 824  2924 1556 HOH HOH B . 
EA 11 HOH 825  2925 1823 HOH HOH B . 
EA 11 HOH 826  2926 1882 HOH HOH B . 
EA 11 HOH 827  2927 2213 HOH HOH B . 
EA 11 HOH 828  2928 2406 HOH HOH B . 
EA 11 HOH 829  2929 2458 HOH HOH B . 
EA 11 HOH 830  2930 1581 HOH HOH B . 
EA 11 HOH 831  2931 2359 HOH HOH B . 
EA 11 HOH 832  2932 1742 HOH HOH B . 
EA 11 HOH 833  2933 525  HOH HOH B . 
EA 11 HOH 834  2934 1957 HOH HOH B . 
EA 11 HOH 835  2935 2145 HOH HOH B . 
EA 11 HOH 836  2936 2388 HOH HOH B . 
EA 11 HOH 837  2937 2339 HOH HOH B . 
EA 11 HOH 838  2938 541  HOH HOH B . 
EA 11 HOH 839  2939 1871 HOH HOH B . 
EA 11 HOH 840  2940 1064 HOH HOH B . 
EA 11 HOH 841  2941 742  HOH HOH B . 
EA 11 HOH 842  2942 1872 HOH HOH B . 
EA 11 HOH 843  2943 1893 HOH HOH B . 
EA 11 HOH 844  2944 1684 HOH HOH B . 
EA 11 HOH 845  2945 1356 HOH HOH B . 
EA 11 HOH 846  2946 1393 HOH HOH B . 
EA 11 HOH 847  2947 2119 HOH HOH B . 
EA 11 HOH 848  2948 2300 HOH HOH B . 
EA 11 HOH 849  2949 642  HOH HOH B . 
EA 11 HOH 850  2950 1077 HOH HOH B . 
EA 11 HOH 851  2951 2398 HOH HOH B . 
EA 11 HOH 852  2952 2040 HOH HOH B . 
EA 11 HOH 853  2953 2295 HOH HOH B . 
EA 11 HOH 854  2954 1979 HOH HOH B . 
EA 11 HOH 855  2955 1728 HOH HOH B . 
EA 11 HOH 856  2956 667  HOH HOH B . 
EA 11 HOH 857  2957 1170 HOH HOH B . 
EA 11 HOH 858  2958 2434 HOH HOH B . 
EA 11 HOH 859  2959 2472 HOH HOH B . 
EA 11 HOH 860  2960 578  HOH HOH B . 
EA 11 HOH 861  2961 675  HOH HOH B . 
EA 11 HOH 862  2962 1722 HOH HOH B . 
EA 11 HOH 863  2963 1268 HOH HOH B . 
EA 11 HOH 864  2964 1277 HOH HOH B . 
EA 11 HOH 865  2965 1357 HOH HOH B . 
EA 11 HOH 866  2966 1266 HOH HOH B . 
EA 11 HOH 867  2967 2348 HOH HOH B . 
EA 11 HOH 868  2968 2194 HOH HOH B . 
EA 11 HOH 869  2969 1938 HOH HOH B . 
EA 11 HOH 870  2970 2354 HOH HOH B . 
EA 11 HOH 871  2971 2120 HOH HOH B . 
EA 11 HOH 872  2972 1945 HOH HOH B . 
EA 11 HOH 873  2973 1387 HOH HOH B . 
EA 11 HOH 874  2974 1719 HOH HOH B . 
EA 11 HOH 875  2975 1953 HOH HOH B . 
EA 11 HOH 876  2976 2195 HOH HOH B . 
EA 11 HOH 877  2977 1146 HOH HOH B . 
EA 11 HOH 878  2978 2022 HOH HOH B . 
EA 11 HOH 879  2979 2187 HOH HOH B . 
EA 11 HOH 880  2980 2381 HOH HOH B . 
EA 11 HOH 881  2981 2262 HOH HOH B . 
EA 11 HOH 882  2982 2244 HOH HOH B . 
EA 11 HOH 883  2983 2227 HOH HOH B . 
EA 11 HOH 884  2984 948  HOH HOH B . 
EA 11 HOH 885  2985 2429 HOH HOH B . 
EA 11 HOH 886  2986 1127 HOH HOH B . 
EA 11 HOH 887  2987 925  HOH HOH B . 
EA 11 HOH 888  2988 1831 HOH HOH B . 
EA 11 HOH 889  2989 1285 HOH HOH B . 
EA 11 HOH 890  2990 2383 HOH HOH B . 
EA 11 HOH 891  2991 1379 HOH HOH B . 
EA 11 HOH 892  2992 1994 HOH HOH B . 
EA 11 HOH 893  2993 1286 HOH HOH B . 
EA 11 HOH 894  2994 729  HOH HOH B . 
EA 11 HOH 895  2995 1316 HOH HOH B . 
EA 11 HOH 896  2996 884  HOH HOH B . 
EA 11 HOH 897  2997 1485 HOH HOH B . 
EA 11 HOH 898  2998 472  HOH HOH B . 
EA 11 HOH 899  2999 2229 HOH HOH B . 
EA 11 HOH 900  3000 1116 HOH HOH B . 
EA 11 HOH 901  3001 2    HOH HOH B . 
EA 11 HOH 902  3002 2111 HOH HOH B . 
EA 11 HOH 903  3003 1107 HOH HOH B . 
EA 11 HOH 904  3004 2319 HOH HOH B . 
EA 11 HOH 905  3005 272  HOH HOH B . 
EA 11 HOH 906  3006 2293 HOH HOH B . 
EA 11 HOH 907  3007 1875 HOH HOH B . 
EA 11 HOH 908  3008 1697 HOH HOH B . 
EA 11 HOH 909  3009 732  HOH HOH B . 
EA 11 HOH 910  3010 1694 HOH HOH B . 
EA 11 HOH 911  3011 2184 HOH HOH B . 
EA 11 HOH 912  3012 2056 HOH HOH B . 
EA 11 HOH 913  3013 2478 HOH HOH B . 
EA 11 HOH 914  3014 1686 HOH HOH B . 
EA 11 HOH 915  3015 2267 HOH HOH B . 
EA 11 HOH 916  3016 1032 HOH HOH B . 
EA 11 HOH 917  3017 1755 HOH HOH B . 
EA 11 HOH 918  3018 579  HOH HOH B . 
EA 11 HOH 919  3019 1760 HOH HOH B . 
EA 11 HOH 920  3020 1594 HOH HOH B . 
EA 11 HOH 921  3021 1411 HOH HOH B . 
EA 11 HOH 922  3022 2112 HOH HOH B . 
EA 11 HOH 923  3023 2444 HOH HOH B . 
EA 11 HOH 924  3024 871  HOH HOH B . 
EA 11 HOH 925  3025 1592 HOH HOH B . 
EA 11 HOH 926  3026 1932 HOH HOH B . 
EA 11 HOH 927  3027 879  HOH HOH B . 
EA 11 HOH 928  3028 1330 HOH HOH B . 
EA 11 HOH 929  3029 2443 HOH HOH B . 
EA 11 HOH 930  3030 2176 HOH HOH B . 
EA 11 HOH 931  3031 2259 HOH HOH B . 
EA 11 HOH 932  3032 1381 HOH HOH B . 
EA 11 HOH 933  3033 1752 HOH HOH B . 
EA 11 HOH 934  3034 2419 HOH HOH B . 
EA 11 HOH 935  3035 1075 HOH HOH B . 
EA 11 HOH 936  3036 876  HOH HOH B . 
EA 11 HOH 937  3037 1637 HOH HOH B . 
EA 11 HOH 938  3038 2273 HOH HOH B . 
EA 11 HOH 939  3039 2408 HOH HOH B . 
EA 11 HOH 940  3040 1678 HOH HOH B . 
EA 11 HOH 941  3041 905  HOH HOH B . 
EA 11 HOH 942  3042 335  HOH HOH B . 
EA 11 HOH 943  3043 1402 HOH HOH B . 
EA 11 HOH 944  3044 1173 HOH HOH B . 
EA 11 HOH 945  3045 753  HOH HOH B . 
EA 11 HOH 946  3046 1354 HOH HOH B . 
EA 11 HOH 947  3047 1136 HOH HOH B . 
EA 11 HOH 948  3048 2055 HOH HOH B . 
EA 11 HOH 949  3049 1490 HOH HOH B . 
EA 11 HOH 950  3050 825  HOH HOH B . 
EA 11 HOH 951  3051 2097 HOH HOH B . 
EA 11 HOH 952  3052 1337 HOH HOH B . 
EA 11 HOH 953  3053 1793 HOH HOH B . 
EA 11 HOH 954  3054 2268 HOH HOH B . 
EA 11 HOH 955  3055 1391 HOH HOH B . 
EA 11 HOH 956  3056 1484 HOH HOH B . 
EA 11 HOH 957  3057 2336 HOH HOH B . 
EA 11 HOH 958  3058 2230 HOH HOH B . 
EA 11 HOH 959  3059 2289 HOH HOH B . 
EA 11 HOH 960  3060 1378 HOH HOH B . 
EA 11 HOH 961  3061 2162 HOH HOH B . 
EA 11 HOH 962  3062 2465 HOH HOH B . 
EA 11 HOH 963  3063 775  HOH HOH B . 
EA 11 HOH 964  3064 752  HOH HOH B . 
EA 11 HOH 965  3065 677  HOH HOH B . 
EA 11 HOH 966  3066 981  HOH HOH B . 
EA 11 HOH 967  3067 1792 HOH HOH B . 
EA 11 HOH 968  3068 2344 HOH HOH B . 
EA 11 HOH 969  3069 833  HOH HOH B . 
EA 11 HOH 970  3070 1877 HOH HOH B . 
EA 11 HOH 971  3071 613  HOH HOH B . 
EA 11 HOH 972  3072 2353 HOH HOH B . 
EA 11 HOH 973  3073 2418 HOH HOH B . 
EA 11 HOH 974  3074 4    HOH HOH B . 
EA 11 HOH 975  3075 1966 HOH HOH B . 
EA 11 HOH 976  3076 2290 HOH HOH B . 
EA 11 HOH 977  3077 827  HOH HOH B . 
EA 11 HOH 978  3078 971  HOH HOH B . 
EA 11 HOH 979  3079 2254 HOH HOH B . 
EA 11 HOH 980  3080 1293 HOH HOH B . 
EA 11 HOH 981  3081 1798 HOH HOH B . 
EA 11 HOH 982  3082 542  HOH HOH B . 
EA 11 HOH 983  3083 1959 HOH HOH B . 
EA 11 HOH 984  3084 1367 HOH HOH B . 
EA 11 HOH 985  3085 1094 HOH HOH B . 
EA 11 HOH 986  3086 1106 HOH HOH B . 
EA 11 HOH 987  3087 1689 HOH HOH B . 
EA 11 HOH 988  3088 1928 HOH HOH B . 
EA 11 HOH 989  3089 2170 HOH HOH B . 
EA 11 HOH 990  3090 1347 HOH HOH B . 
EA 11 HOH 991  3091 2315 HOH HOH B . 
EA 11 HOH 992  3092 889  HOH HOH B . 
EA 11 HOH 993  3093 2373 HOH HOH B . 
EA 11 HOH 994  3094 2258 HOH HOH B . 
EA 11 HOH 995  3095 1983 HOH HOH B . 
EA 11 HOH 996  3096 581  HOH HOH B . 
EA 11 HOH 997  3097 540  HOH HOH B . 
EA 11 HOH 998  3098 2109 HOH HOH B . 
EA 11 HOH 999  3099 663  HOH HOH B . 
EA 11 HOH 1000 3100 1031 HOH HOH B . 
EA 11 HOH 1001 3101 2101 HOH HOH B . 
EA 11 HOH 1002 3102 645  HOH HOH B . 
EA 11 HOH 1003 3103 2394 HOH HOH B . 
EA 11 HOH 1004 3104 2291 HOH HOH B . 
EA 11 HOH 1005 3105 2428 HOH HOH B . 
EA 11 HOH 1006 3106 185  HOH HOH B . 
EA 11 HOH 1007 3107 536  HOH HOH B . 
EA 11 HOH 1008 3108 2311 HOH HOH B . 
EA 11 HOH 1009 3109 2314 HOH HOH B . 
EA 11 HOH 1010 3110 988  HOH HOH B . 
EA 11 HOH 1011 3111 997  HOH HOH B . 
EA 11 HOH 1012 3112 2039 HOH HOH B . 
EA 11 HOH 1013 3113 2470 HOH HOH B . 
EA 11 HOH 1014 3114 574  HOH HOH B . 
EA 11 HOH 1015 3115 1003 HOH HOH B . 
EA 11 HOH 1016 3116 2052 HOH HOH B . 
EA 11 HOH 1017 3117 2175 HOH HOH B . 
EA 11 HOH 1018 3118 2212 HOH HOH B . 
EA 11 HOH 1019 3119 2124 HOH HOH B . 
EA 11 HOH 1020 3120 2038 HOH HOH B . 
EA 11 HOH 1021 3121 989  HOH HOH B . 
EA 11 HOH 1022 3122 2355 HOH HOH B . 
EA 11 HOH 1023 3123 1827 HOH HOH B . 
EA 11 HOH 1024 3124 2242 HOH HOH B . 
EA 11 HOH 1025 3125 1389 HOH HOH B . 
EA 11 HOH 1026 3126 1936 HOH HOH B . 
EA 11 HOH 1027 3127 1710 HOH HOH B . 
EA 11 HOH 1028 3128 1785 HOH HOH B . 
EA 11 HOH 1029 3129 891  HOH HOH B . 
EA 11 HOH 1030 3130 2024 HOH HOH B . 
EA 11 HOH 1031 3131 850  HOH HOH B . 
EA 11 HOH 1032 3132 2239 HOH HOH B . 
EA 11 HOH 1033 3133 2177 HOH HOH B . 
EA 11 HOH 1034 3134 2414 HOH HOH B . 
EA 11 HOH 1035 3135 1483 HOH HOH B . 
EA 11 HOH 1036 3136 2415 HOH HOH B . 
EA 11 HOH 1037 3137 1795 HOH HOH B . 
EA 11 HOH 1038 3138 963  HOH HOH B . 
EA 11 HOH 1039 3139 929  HOH HOH B . 
EA 11 HOH 1040 3140 2481 HOH HOH B . 
EA 11 HOH 1041 3141 1621 HOH HOH B . 
EA 11 HOH 1042 3142 1058 HOH HOH B . 
EA 11 HOH 1043 3143 2371 HOH HOH B . 
EA 11 HOH 1044 3144 2141 HOH HOH B . 
EA 11 HOH 1045 3145 1600 HOH HOH B . 
EA 11 HOH 1046 3146 2045 HOH HOH B . 
EA 11 HOH 1047 3147 1589 HOH HOH B . 
EA 11 HOH 1048 3148 2270 HOH HOH B . 
EA 11 HOH 1049 3149 2092 HOH HOH B . 
EA 11 HOH 1050 3150 1664 HOH HOH B . 
EA 11 HOH 1051 3151 1591 HOH HOH B . 
EA 11 HOH 1052 3152 991  HOH HOH B . 
EA 11 HOH 1053 3153 2203 HOH HOH B . 
EA 11 HOH 1054 3154 1131 HOH HOH B . 
EA 11 HOH 1055 3155 755  HOH HOH B . 
EA 11 HOH 1056 3156 1278 HOH HOH B . 
EA 11 HOH 1057 3157 2202 HOH HOH B . 
EA 11 HOH 1058 3158 999  HOH HOH B . 
EA 11 HOH 1059 3159 2395 HOH HOH B . 
EA 11 HOH 1060 3160 1649 HOH HOH B . 
EA 11 HOH 1061 3161 1814 HOH HOH B . 
EA 11 HOH 1062 3162 2116 HOH HOH B . 
EA 11 HOH 1063 3163 2351 HOH HOH B . 
EA 11 HOH 1064 3164 1249 HOH HOH B . 
EA 11 HOH 1065 3165 764  HOH HOH B . 
EA 11 HOH 1066 3166 1130 HOH HOH B . 
EA 11 HOH 1067 3167 2161 HOH HOH B . 
EA 11 HOH 1068 3168 1440 HOH HOH B . 
EA 11 HOH 1069 3169 1201 HOH HOH B . 
EA 11 HOH 1070 3170 1314 HOH HOH B . 
EA 11 HOH 1071 3171 2297 HOH HOH B . 
EA 11 HOH 1072 3172 446  HOH HOH B . 
EA 11 HOH 1073 3173 1748 HOH HOH B . 
EA 11 HOH 1074 3174 2050 HOH HOH B . 
EA 11 HOH 1075 3175 381  HOH HOH B . 
EA 11 HOH 1076 3176 1743 HOH HOH B . 
EA 11 HOH 1077 3177 2225 HOH HOH B . 
EA 11 HOH 1078 3178 1451 HOH HOH B . 
EA 11 HOH 1079 3179 1860 HOH HOH B . 
EA 11 HOH 1080 3180 1477 HOH HOH B . 
EA 11 HOH 1081 3181 1864 HOH HOH B . 
EA 11 HOH 1082 3182 1981 HOH HOH B . 
EA 11 HOH 1083 3183 1859 HOH HOH B . 
EA 11 HOH 1084 3184 1373 HOH HOH B . 
EA 11 HOH 1085 3185 2430 HOH HOH B . 
EA 11 HOH 1086 3186 2292 HOH HOH B . 
EA 11 HOH 1087 3187 2320 HOH HOH B . 
EA 11 HOH 1088 3188 2335 HOH HOH B . 
EA 11 HOH 1089 3189 1465 HOH HOH B . 
EA 11 HOH 1090 3190 1415 HOH HOH B . 
EA 11 HOH 1091 3191 1977 HOH HOH B . 
EA 11 HOH 1092 3192 1947 HOH HOH B . 
EA 11 HOH 1093 3193 584  HOH HOH B . 
EA 11 HOH 1094 3194 2471 HOH HOH B . 
EA 11 HOH 1095 3195 1647 HOH HOH B . 
EA 11 HOH 1096 3196 2100 HOH HOH B . 
EA 11 HOH 1097 3197 855  HOH HOH B . 
EA 11 HOH 1098 3198 1494 HOH HOH B . 
EA 11 HOH 1099 3199 2093 HOH HOH B . 
EA 11 HOH 1100 3200 2462 HOH HOH B . 
EA 11 HOH 1101 3201 2313 HOH HOH B . 
EA 11 HOH 1102 3202 1358 HOH HOH B . 
EA 11 HOH 1103 3203 603  HOH HOH B . 
EA 11 HOH 1104 3204 1463 HOH HOH B . 
EA 11 HOH 1105 3205 1061 HOH HOH B . 
EA 11 HOH 1106 3206 799  HOH HOH B . 
EA 11 HOH 1107 3207 1903 HOH HOH B . 
EA 11 HOH 1108 3208 1709 HOH HOH B . 
EA 11 HOH 1109 3209 1978 HOH HOH B . 
EA 11 HOH 1110 3210 2399 HOH HOH B . 
EA 11 HOH 1111 3211 1595 HOH HOH B . 
EA 11 HOH 1112 3212 2204 HOH HOH B . 
EA 11 HOH 1113 3213 1892 HOH HOH B . 
EA 11 HOH 1114 3214 1376 HOH HOH B . 
EA 11 HOH 1115 3215 1448 HOH HOH B . 
EA 11 HOH 1116 3216 2461 HOH HOH B . 
EA 11 HOH 1117 3217 1598 HOH HOH B . 
EA 11 HOH 1118 3218 1090 HOH HOH B . 
EA 11 HOH 1119 3219 1786 HOH HOH B . 
EA 11 HOH 1120 3220 1251 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A GLU 59   ? CG  ? A GLU 61   CG  
2   1 Y 1 A GLU 59   ? CD  ? A GLU 61   CD  
3   1 Y 1 A GLU 59   ? OE1 ? A GLU 61   OE1 
4   1 Y 1 A GLU 59   ? OE2 ? A GLU 61   OE2 
5   1 Y 1 A HIS 79   ? CG  ? A HIS 81   CG  
6   1 Y 1 A HIS 79   ? ND1 ? A HIS 81   ND1 
7   1 Y 1 A HIS 79   ? CD2 ? A HIS 81   CD2 
8   1 Y 1 A HIS 79   ? CE1 ? A HIS 81   CE1 
9   1 Y 1 A HIS 79   ? NE2 ? A HIS 81   NE2 
10  1 Y 1 A SER 82   ? OG  ? A SER 84   OG  
11  1 Y 1 A GLU 85   ? CG  ? A GLU 87   CG  
12  1 Y 1 A GLU 85   ? CD  ? A GLU 87   CD  
13  1 Y 1 A GLU 85   ? OE1 ? A GLU 87   OE1 
14  1 Y 1 A GLU 85   ? OE2 ? A GLU 87   OE2 
15  1 Y 1 A GLN 89   ? CG  ? A GLN 91   CG  
16  1 Y 1 A GLN 89   ? CD  ? A GLN 91   CD  
17  1 Y 1 A GLN 89   ? OE1 ? A GLN 91   OE1 
18  1 Y 1 A GLN 89   ? NE2 ? A GLN 91   NE2 
19  1 Y 1 A ARG 122  ? CG  ? A ARG 124  CG  
20  1 Y 1 A ARG 122  ? CD  ? A ARG 124  CD  
21  1 Y 1 A ARG 122  ? NE  ? A ARG 124  NE  
22  1 Y 1 A ARG 122  ? CZ  ? A ARG 124  CZ  
23  1 Y 1 A ARG 122  ? NH1 ? A ARG 124  NH1 
24  1 Y 1 A ARG 122  ? NH2 ? A ARG 124  NH2 
25  1 Y 1 A LYS 124  ? CG  ? A LYS 126  CG  
26  1 Y 1 A LYS 124  ? CD  ? A LYS 126  CD  
27  1 Y 1 A LYS 124  ? CE  ? A LYS 126  CE  
28  1 Y 1 A LYS 124  ? NZ  ? A LYS 126  NZ  
29  1 Y 1 A ASP 127  ? CG  ? A ASP 129  CG  
30  1 Y 1 A ASP 127  ? OD1 ? A ASP 129  OD1 
31  1 Y 1 A ASP 127  ? OD2 ? A ASP 129  OD2 
32  1 Y 1 A ASN 129  ? CG  ? A ASN 131  CG  
33  1 Y 1 A ASN 129  ? OD1 ? A ASN 131  OD1 
34  1 Y 1 A ASN 129  ? ND2 ? A ASN 131  ND2 
35  1 Y 1 A LYS 131  ? CG  ? A LYS 133  CG  
36  1 Y 1 A LYS 131  ? CD  ? A LYS 133  CD  
37  1 Y 1 A LYS 131  ? CE  ? A LYS 133  CE  
38  1 Y 1 A LYS 131  ? NZ  ? A LYS 133  NZ  
39  1 Y 1 A SER 132  ? OG  ? A SER 134  OG  
40  1 Y 1 A SER 137  ? OG  ? A SER 139  OG  
41  1 Y 1 A LYS 154  ? CG  ? A LYS 156  CG  
42  1 Y 1 A LYS 154  ? CD  ? A LYS 156  CD  
43  1 Y 1 A LYS 154  ? CE  ? A LYS 156  CE  
44  1 Y 1 A LYS 154  ? NZ  ? A LYS 156  NZ  
45  1 Y 1 A ARG 189  ? CG  ? A ARG 191  CG  
46  1 Y 1 A ARG 189  ? CD  ? A ARG 191  CD  
47  1 Y 1 A ARG 189  ? NE  ? A ARG 191  NE  
48  1 Y 1 A ARG 189  ? CZ  ? A ARG 191  CZ  
49  1 Y 1 A ARG 189  ? NH1 ? A ARG 191  NH1 
50  1 Y 1 A ARG 189  ? NH2 ? A ARG 191  NH2 
51  1 Y 1 A LYS 206  ? CG  ? A LYS 208  CG  
52  1 Y 1 A LYS 206  ? CD  ? A LYS 208  CD  
53  1 Y 1 A LYS 206  ? CE  ? A LYS 208  CE  
54  1 Y 1 A LYS 206  ? NZ  ? A LYS 208  NZ  
55  1 Y 1 A GLU 213  ? CG  ? A GLU 215  CG  
56  1 Y 1 A GLU 213  ? CD  ? A GLU 215  CD  
57  1 Y 1 A GLU 213  ? OE1 ? A GLU 215  OE1 
58  1 Y 1 A GLU 213  ? OE2 ? A GLU 215  OE2 
59  1 Y 1 A LYS 214  ? CG  ? A LYS 216  CG  
60  1 Y 1 A LYS 214  ? CD  ? A LYS 216  CD  
61  1 Y 1 A LYS 214  ? CE  ? A LYS 216  CE  
62  1 Y 1 A LYS 214  ? NZ  ? A LYS 216  NZ  
63  1 Y 1 A LYS 437  ? CG  ? A LYS 439  CG  
64  1 Y 1 A LYS 437  ? CD  ? A LYS 439  CD  
65  1 Y 1 A LYS 437  ? CE  ? A LYS 439  CE  
66  1 Y 1 A LYS 437  ? NZ  ? A LYS 439  NZ  
67  1 Y 1 A ARG 463  ? CG  ? A ARG 465  CG  
68  1 Y 1 A ARG 463  ? CD  ? A ARG 465  CD  
69  1 Y 1 A ARG 463  ? NE  ? A ARG 465  NE  
70  1 Y 1 A ARG 463  ? CZ  ? A ARG 465  CZ  
71  1 Y 1 A ARG 463  ? NH1 ? A ARG 465  NH1 
72  1 Y 1 A ARG 463  ? NH2 ? A ARG 465  NH2 
73  1 Y 1 A GLU 480  ? CG  ? A GLU 482  CG  
74  1 Y 1 A GLU 480  ? CD  ? A GLU 482  CD  
75  1 Y 1 A GLU 480  ? OE1 ? A GLU 482  OE1 
76  1 Y 1 A GLU 480  ? OE2 ? A GLU 482  OE2 
77  1 Y 1 A GLU 492  ? CG  ? A GLU 494  CG  
78  1 Y 1 A GLU 492  ? CD  ? A GLU 494  CD  
79  1 Y 1 A GLU 492  ? OE1 ? A GLU 494  OE1 
80  1 Y 1 A GLU 492  ? OE2 ? A GLU 494  OE2 
81  1 Y 1 A ASN 496  ? CG  ? A ASN 498  CG  
82  1 Y 1 A ASN 496  ? OD1 ? A ASN 498  OD1 
83  1 Y 1 A ASN 496  ? ND2 ? A ASN 498  ND2 
84  1 Y 1 A VAL 500  ? CG1 ? A VAL 502  CG1 
85  1 Y 1 A VAL 500  ? CG2 ? A VAL 502  CG2 
86  1 Y 1 A LYS 507  ? CG  ? A LYS 509  CG  
87  1 Y 1 A LYS 507  ? CD  ? A LYS 509  CD  
88  1 Y 1 A LYS 507  ? CE  ? A LYS 509  CE  
89  1 Y 1 A LYS 507  ? NZ  ? A LYS 509  NZ  
90  1 Y 1 A ARG 533  ? CG  ? A ARG 535  CG  
91  1 Y 1 A ARG 533  ? CD  ? A ARG 535  CD  
92  1 Y 1 A ARG 533  ? NE  ? A ARG 535  NE  
93  1 Y 1 A ARG 533  ? CZ  ? A ARG 535  CZ  
94  1 Y 1 A ARG 533  ? NH1 ? A ARG 535  NH1 
95  1 Y 1 A ARG 533  ? NH2 ? A ARG 535  NH2 
96  1 Y 1 A GLU 588  ? CG  ? A GLU 590  CG  
97  1 Y 1 A GLU 588  ? CD  ? A GLU 590  CD  
98  1 Y 1 A GLU 588  ? OE1 ? A GLU 590  OE1 
99  1 Y 1 A GLU 588  ? OE2 ? A GLU 590  OE2 
100 1 Y 1 A GLU 611  ? CG  ? A GLU 613  CG  
101 1 Y 1 A GLU 611  ? CD  ? A GLU 613  CD  
102 1 Y 1 A GLU 611  ? OE1 ? A GLU 613  OE1 
103 1 Y 1 A GLU 611  ? OE2 ? A GLU 613  OE2 
104 1 Y 1 A ARG 618  ? CG  ? A ARG 620  CG  
105 1 Y 1 A ARG 618  ? CD  ? A ARG 620  CD  
106 1 Y 1 A ARG 618  ? NE  ? A ARG 620  NE  
107 1 Y 1 A ARG 618  ? CZ  ? A ARG 620  CZ  
108 1 Y 1 A ARG 618  ? NH1 ? A ARG 620  NH1 
109 1 Y 1 A ARG 618  ? NH2 ? A ARG 620  NH2 
110 1 Y 1 A ARG 764  ? CG  ? A ARG 766  CG  
111 1 Y 1 A ARG 764  ? CD  ? A ARG 766  CD  
112 1 Y 1 A ARG 764  ? NE  ? A ARG 766  NE  
113 1 Y 1 A ARG 764  ? CZ  ? A ARG 766  CZ  
114 1 Y 1 A ARG 764  ? NH1 ? A ARG 766  NH1 
115 1 Y 1 A ARG 764  ? NH2 ? A ARG 766  NH2 
116 1 Y 1 A GLU 785  ? CG  ? A GLU 787  CG  
117 1 Y 1 A GLU 785  ? CD  ? A GLU 787  CD  
118 1 Y 1 A GLU 785  ? OE1 ? A GLU 787  OE1 
119 1 Y 1 A GLU 785  ? OE2 ? A GLU 787  OE2 
120 1 Y 1 A GLN 793  ? CG  ? A GLN 795  CG  
121 1 Y 1 A GLN 793  ? CD  ? A GLN 795  CD  
122 1 Y 1 A GLN 793  ? OE1 ? A GLN 795  OE1 
123 1 Y 1 A GLN 793  ? NE2 ? A GLN 795  NE2 
124 1 Y 1 A ASP 855  ? CG  ? A ASP 857  CG  
125 1 Y 1 A ASP 855  ? OD1 ? A ASP 857  OD1 
126 1 Y 1 A ASP 855  ? OD2 ? A ASP 857  OD2 
127 1 Y 1 A LYS 897  ? CG  ? A LYS 899  CG  
128 1 Y 1 A LYS 897  ? CD  ? A LYS 899  CD  
129 1 Y 1 A LYS 897  ? CE  ? A LYS 899  CE  
130 1 Y 1 A LYS 897  ? NZ  ? A LYS 899  NZ  
131 1 Y 1 A ARG 901  ? CG  ? A ARG 903  CG  
132 1 Y 1 A ARG 901  ? CD  ? A ARG 903  CD  
133 1 Y 1 A ARG 901  ? NE  ? A ARG 903  NE  
134 1 Y 1 A ARG 901  ? CZ  ? A ARG 903  CZ  
135 1 Y 1 A ARG 901  ? NH1 ? A ARG 903  NH1 
136 1 Y 1 A ARG 901  ? NH2 ? A ARG 903  NH2 
137 1 Y 1 A LYS 933  ? CG  ? A LYS 935  CG  
138 1 Y 1 A LYS 933  ? CD  ? A LYS 935  CD  
139 1 Y 1 A LYS 933  ? CE  ? A LYS 935  CE  
140 1 Y 1 A LYS 933  ? NZ  ? A LYS 935  NZ  
141 1 Y 1 A GLN 938  ? CG  ? A GLN 940  CG  
142 1 Y 1 A GLN 938  ? CD  ? A GLN 940  CD  
143 1 Y 1 A GLN 938  ? OE1 ? A GLN 940  OE1 
144 1 Y 1 A GLN 938  ? NE2 ? A GLN 940  NE2 
145 1 Y 1 A ARG 939  ? CG  ? A ARG 941  CG  
146 1 Y 1 A ARG 939  ? CD  ? A ARG 941  CD  
147 1 Y 1 A ARG 939  ? NE  ? A ARG 941  NE  
148 1 Y 1 A ARG 939  ? CZ  ? A ARG 941  CZ  
149 1 Y 1 A ARG 939  ? NH1 ? A ARG 941  NH1 
150 1 Y 1 A ARG 939  ? NH2 ? A ARG 941  NH2 
151 1 Y 1 A ARG 1063 ? CG  ? A ARG 1065 CG  
152 1 Y 1 A ARG 1063 ? CD  ? A ARG 1065 CD  
153 1 Y 1 A ARG 1063 ? NE  ? A ARG 1065 NE  
154 1 Y 1 A ARG 1063 ? CZ  ? A ARG 1065 CZ  
155 1 Y 1 A ARG 1063 ? NH1 ? A ARG 1065 NH1 
156 1 Y 1 A ARG 1063 ? NH2 ? A ARG 1065 NH2 
157 1 Y 1 A LYS 1139 ? CG  ? A LYS 1141 CG  
158 1 Y 1 A LYS 1139 ? CD  ? A LYS 1141 CD  
159 1 Y 1 A LYS 1139 ? CE  ? A LYS 1141 CE  
160 1 Y 1 A LYS 1139 ? NZ  ? A LYS 1141 NZ  
161 1 Y 1 A GLN 1143 ? CG  ? A GLN 1145 CG  
162 1 Y 1 A GLN 1143 ? CD  ? A GLN 1145 CD  
163 1 Y 1 A GLN 1143 ? OE1 ? A GLN 1145 OE1 
164 1 Y 1 A GLN 1143 ? NE2 ? A GLN 1145 NE2 
165 1 Y 1 A LYS 1153 ? CG  ? A LYS 1155 CG  
166 1 Y 1 A LYS 1153 ? CD  ? A LYS 1155 CD  
167 1 Y 1 A LYS 1153 ? CE  ? A LYS 1155 CE  
168 1 Y 1 A LYS 1153 ? NZ  ? A LYS 1155 NZ  
169 1 Y 1 B ASP 20   ? CG  ? B ASP 22   CG  
170 1 Y 1 B ASP 20   ? OD1 ? B ASP 22   OD1 
171 1 Y 1 B ASP 20   ? OD2 ? B ASP 22   OD2 
172 1 Y 1 B GLU 52   ? CG  ? B GLU 54   CG  
173 1 Y 1 B GLU 52   ? CD  ? B GLU 54   CD  
174 1 Y 1 B GLU 52   ? OE1 ? B GLU 54   OE1 
175 1 Y 1 B GLU 52   ? OE2 ? B GLU 54   OE2 
176 1 Y 1 B LYS 58   ? CG  ? B LYS 60   CG  
177 1 Y 1 B LYS 58   ? CD  ? B LYS 60   CD  
178 1 Y 1 B LYS 58   ? CE  ? B LYS 60   CE  
179 1 Y 1 B LYS 58   ? NZ  ? B LYS 60   NZ  
180 1 Y 1 B GLU 59   ? CG  ? B GLU 61   CG  
181 1 Y 1 B GLU 59   ? CD  ? B GLU 61   CD  
182 1 Y 1 B GLU 59   ? OE1 ? B GLU 61   OE1 
183 1 Y 1 B GLU 59   ? OE2 ? B GLU 61   OE2 
184 1 Y 1 B ILE 60   ? CG1 ? B ILE 62   CG1 
185 1 Y 1 B ILE 60   ? CG2 ? B ILE 62   CG2 
186 1 Y 1 B ILE 60   ? CD1 ? B ILE 62   CD1 
187 1 Y 1 B SER 66   ? OG  ? B SER 68   OG  
188 1 Y 1 B LYS 70   ? CG  ? B LYS 72   CG  
189 1 Y 1 B LYS 70   ? CD  ? B LYS 72   CD  
190 1 Y 1 B LYS 70   ? CE  ? B LYS 72   CE  
191 1 Y 1 B LYS 70   ? NZ  ? B LYS 72   NZ  
192 1 Y 1 B GLU 73   ? CG  ? B GLU 75   CG  
193 1 Y 1 B GLU 73   ? CD  ? B GLU 75   CD  
194 1 Y 1 B GLU 73   ? OE1 ? B GLU 75   OE1 
195 1 Y 1 B GLU 73   ? OE2 ? B GLU 75   OE2 
196 1 Y 1 B SER 82   ? OG  ? B SER 84   OG  
197 1 Y 1 B GLU 85   ? CG  ? B GLU 87   CG  
198 1 Y 1 B GLU 85   ? CD  ? B GLU 87   CD  
199 1 Y 1 B GLU 85   ? OE1 ? B GLU 87   OE1 
200 1 Y 1 B GLU 85   ? OE2 ? B GLU 87   OE2 
201 1 Y 1 B GLN 89   ? CG  ? B GLN 91   CG  
202 1 Y 1 B GLN 89   ? CD  ? B GLN 91   CD  
203 1 Y 1 B GLN 89   ? OE1 ? B GLN 91   OE1 
204 1 Y 1 B GLN 89   ? NE2 ? B GLN 91   NE2 
205 1 Y 1 B ARG 122  ? CG  ? B ARG 124  CG  
206 1 Y 1 B ARG 122  ? CD  ? B ARG 124  CD  
207 1 Y 1 B ARG 122  ? NE  ? B ARG 124  NE  
208 1 Y 1 B ARG 122  ? CZ  ? B ARG 124  CZ  
209 1 Y 1 B ARG 122  ? NH1 ? B ARG 124  NH1 
210 1 Y 1 B ARG 122  ? NH2 ? B ARG 124  NH2 
211 1 Y 1 B LYS 124  ? CG  ? B LYS 126  CG  
212 1 Y 1 B LYS 124  ? CD  ? B LYS 126  CD  
213 1 Y 1 B LYS 124  ? CE  ? B LYS 126  CE  
214 1 Y 1 B LYS 124  ? NZ  ? B LYS 126  NZ  
215 1 Y 1 B ASP 127  ? CG  ? B ASP 129  CG  
216 1 Y 1 B ASP 127  ? OD1 ? B ASP 129  OD1 
217 1 Y 1 B ASP 127  ? OD2 ? B ASP 129  OD2 
218 1 Y 1 B ASN 129  ? CG  ? B ASN 131  CG  
219 1 Y 1 B ASN 129  ? OD1 ? B ASN 131  OD1 
220 1 Y 1 B ASN 129  ? ND2 ? B ASN 131  ND2 
221 1 Y 1 B LYS 131  ? CG  ? B LYS 133  CG  
222 1 Y 1 B LYS 131  ? CD  ? B LYS 133  CD  
223 1 Y 1 B LYS 131  ? CE  ? B LYS 133  CE  
224 1 Y 1 B LYS 131  ? NZ  ? B LYS 133  NZ  
225 1 Y 1 B SER 132  ? OG  ? B SER 134  OG  
226 1 Y 1 B HIS 133  ? CG  ? B HIS 135  CG  
227 1 Y 1 B HIS 133  ? ND1 ? B HIS 135  ND1 
228 1 Y 1 B HIS 133  ? CD2 ? B HIS 135  CD2 
229 1 Y 1 B HIS 133  ? CE1 ? B HIS 135  CE1 
230 1 Y 1 B HIS 133  ? NE2 ? B HIS 135  NE2 
231 1 Y 1 B ARG 138  ? CG  ? B ARG 140  CG  
232 1 Y 1 B ARG 138  ? CD  ? B ARG 140  CD  
233 1 Y 1 B ARG 138  ? NE  ? B ARG 140  NE  
234 1 Y 1 B ARG 138  ? CZ  ? B ARG 140  CZ  
235 1 Y 1 B ARG 138  ? NH1 ? B ARG 140  NH1 
236 1 Y 1 B ARG 138  ? NH2 ? B ARG 140  NH2 
237 1 Y 1 B LYS 154  ? CG  ? B LYS 156  CG  
238 1 Y 1 B LYS 154  ? CD  ? B LYS 156  CD  
239 1 Y 1 B LYS 154  ? CE  ? B LYS 156  CE  
240 1 Y 1 B LYS 154  ? NZ  ? B LYS 156  NZ  
241 1 Y 1 B ARG 189  ? CG  ? B ARG 191  CG  
242 1 Y 1 B ARG 189  ? CD  ? B ARG 191  CD  
243 1 Y 1 B ARG 189  ? NE  ? B ARG 191  NE  
244 1 Y 1 B ARG 189  ? CZ  ? B ARG 191  CZ  
245 1 Y 1 B ARG 189  ? NH1 ? B ARG 191  NH1 
246 1 Y 1 B ARG 189  ? NH2 ? B ARG 191  NH2 
247 1 Y 1 B GLN 194  ? CG  ? B GLN 196  CG  
248 1 Y 1 B GLN 194  ? CD  ? B GLN 196  CD  
249 1 Y 1 B GLN 194  ? OE1 ? B GLN 196  OE1 
250 1 Y 1 B GLN 194  ? NE2 ? B GLN 196  NE2 
251 1 Y 1 B LYS 206  ? CG  ? B LYS 208  CG  
252 1 Y 1 B LYS 206  ? CD  ? B LYS 208  CD  
253 1 Y 1 B LYS 206  ? CE  ? B LYS 208  CE  
254 1 Y 1 B LYS 206  ? NZ  ? B LYS 208  NZ  
255 1 Y 1 B LYS 209  ? CG  ? B LYS 211  CG  
256 1 Y 1 B LYS 209  ? CD  ? B LYS 211  CD  
257 1 Y 1 B LYS 209  ? CE  ? B LYS 211  CE  
258 1 Y 1 B LYS 209  ? NZ  ? B LYS 211  NZ  
259 1 Y 1 B GLU 213  ? CG  ? B GLU 215  CG  
260 1 Y 1 B GLU 213  ? CD  ? B GLU 215  CD  
261 1 Y 1 B GLU 213  ? OE1 ? B GLU 215  OE1 
262 1 Y 1 B GLU 213  ? OE2 ? B GLU 215  OE2 
263 1 Y 1 B LYS 249  ? CG  ? B LYS 251  CG  
264 1 Y 1 B LYS 249  ? CD  ? B LYS 251  CD  
265 1 Y 1 B LYS 249  ? CE  ? B LYS 251  CE  
266 1 Y 1 B LYS 249  ? NZ  ? B LYS 251  NZ  
267 1 Y 1 B ASP 414  ? CG  ? B ASP 416  CG  
268 1 Y 1 B ASP 414  ? OD1 ? B ASP 416  OD1 
269 1 Y 1 B ASP 414  ? OD2 ? B ASP 416  OD2 
270 1 Y 1 B VAL 415  ? CG1 ? B VAL 417  CG1 
271 1 Y 1 B VAL 415  ? CG2 ? B VAL 417  CG2 
272 1 Y 1 B LYS 437  ? CG  ? B LYS 439  CG  
273 1 Y 1 B LYS 437  ? CD  ? B LYS 439  CD  
274 1 Y 1 B LYS 437  ? CE  ? B LYS 439  CE  
275 1 Y 1 B LYS 437  ? NZ  ? B LYS 439  NZ  
276 1 Y 1 B ASP 438  ? CG  ? B ASP 440  CG  
277 1 Y 1 B ASP 438  ? OD1 ? B ASP 440  OD1 
278 1 Y 1 B ASP 438  ? OD2 ? B ASP 440  OD2 
279 1 Y 1 B ARG 463  ? CG  ? B ARG 465  CG  
280 1 Y 1 B ARG 463  ? CD  ? B ARG 465  CD  
281 1 Y 1 B ARG 463  ? NE  ? B ARG 465  NE  
282 1 Y 1 B ARG 463  ? CZ  ? B ARG 465  CZ  
283 1 Y 1 B ARG 463  ? NH1 ? B ARG 465  NH1 
284 1 Y 1 B ARG 463  ? NH2 ? B ARG 465  NH2 
285 1 Y 1 B GLU 480  ? CG  ? B GLU 482  CG  
286 1 Y 1 B GLU 480  ? CD  ? B GLU 482  CD  
287 1 Y 1 B GLU 480  ? OE1 ? B GLU 482  OE1 
288 1 Y 1 B GLU 480  ? OE2 ? B GLU 482  OE2 
289 1 Y 1 B THR 481  ? OG1 ? B THR 483  OG1 
290 1 Y 1 B THR 481  ? CG2 ? B THR 483  CG2 
291 1 Y 1 B TYR 485  ? CG  ? B TYR 487  CG  
292 1 Y 1 B TYR 485  ? CD1 ? B TYR 487  CD1 
293 1 Y 1 B TYR 485  ? CD2 ? B TYR 487  CD2 
294 1 Y 1 B TYR 485  ? CE1 ? B TYR 487  CE1 
295 1 Y 1 B TYR 485  ? CE2 ? B TYR 487  CE2 
296 1 Y 1 B TYR 485  ? CZ  ? B TYR 487  CZ  
297 1 Y 1 B TYR 485  ? OH  ? B TYR 487  OH  
298 1 Y 1 B ARG 489  ? CG  ? B ARG 491  CG  
299 1 Y 1 B ARG 489  ? CD  ? B ARG 491  CD  
300 1 Y 1 B ARG 489  ? NE  ? B ARG 491  NE  
301 1 Y 1 B ARG 489  ? CZ  ? B ARG 491  CZ  
302 1 Y 1 B ARG 489  ? NH1 ? B ARG 491  NH1 
303 1 Y 1 B ARG 489  ? NH2 ? B ARG 491  NH2 
304 1 Y 1 B GLU 492  ? CG  ? B GLU 494  CG  
305 1 Y 1 B GLU 492  ? CD  ? B GLU 494  CD  
306 1 Y 1 B GLU 492  ? OE1 ? B GLU 494  OE1 
307 1 Y 1 B GLU 492  ? OE2 ? B GLU 494  OE2 
308 1 Y 1 B ASN 496  ? CG  ? B ASN 498  CG  
309 1 Y 1 B ASN 496  ? OD1 ? B ASN 498  OD1 
310 1 Y 1 B ASN 496  ? ND2 ? B ASN 498  ND2 
311 1 Y 1 B VAL 500  ? CG1 ? B VAL 502  CG1 
312 1 Y 1 B VAL 500  ? CG2 ? B VAL 502  CG2 
313 1 Y 1 B ILE 503  ? CG1 ? B ILE 505  CG1 
314 1 Y 1 B ILE 503  ? CG2 ? B ILE 505  CG2 
315 1 Y 1 B ILE 503  ? CD1 ? B ILE 505  CD1 
316 1 Y 1 B ASN 504  ? CG  ? B ASN 506  CG  
317 1 Y 1 B ASN 504  ? OD1 ? B ASN 506  OD1 
318 1 Y 1 B ASN 504  ? ND2 ? B ASN 506  ND2 
319 1 Y 1 B ASP 505  ? CG  ? B ASP 507  CG  
320 1 Y 1 B ASP 505  ? OD1 ? B ASP 507  OD1 
321 1 Y 1 B ASP 505  ? OD2 ? B ASP 507  OD2 
322 1 Y 1 B LYS 507  ? CG  ? B LYS 509  CG  
323 1 Y 1 B LYS 507  ? CD  ? B LYS 509  CD  
324 1 Y 1 B LYS 507  ? CE  ? B LYS 509  CE  
325 1 Y 1 B LYS 507  ? NZ  ? B LYS 509  NZ  
326 1 Y 1 B VAL 508  ? CG1 ? B VAL 510  CG1 
327 1 Y 1 B VAL 508  ? CG2 ? B VAL 510  CG2 
328 1 Y 1 B ILE 510  ? CG1 ? B ILE 512  CG1 
329 1 Y 1 B ILE 510  ? CG2 ? B ILE 512  CG2 
330 1 Y 1 B ILE 510  ? CD1 ? B ILE 512  CD1 
331 1 Y 1 B ARG 533  ? CG  ? B ARG 535  CG  
332 1 Y 1 B ARG 533  ? CD  ? B ARG 535  CD  
333 1 Y 1 B ARG 533  ? NE  ? B ARG 535  NE  
334 1 Y 1 B ARG 533  ? CZ  ? B ARG 535  CZ  
335 1 Y 1 B ARG 533  ? NH1 ? B ARG 535  NH1 
336 1 Y 1 B ARG 533  ? NH2 ? B ARG 535  NH2 
337 1 Y 1 B GLU 588  ? CG  ? B GLU 590  CG  
338 1 Y 1 B GLU 588  ? CD  ? B GLU 590  CD  
339 1 Y 1 B GLU 588  ? OE1 ? B GLU 590  OE1 
340 1 Y 1 B GLU 588  ? OE2 ? B GLU 590  OE2 
341 1 Y 1 B GLU 611  ? CG  ? B GLU 613  CG  
342 1 Y 1 B GLU 611  ? CD  ? B GLU 613  CD  
343 1 Y 1 B GLU 611  ? OE1 ? B GLU 613  OE1 
344 1 Y 1 B GLU 611  ? OE2 ? B GLU 613  OE2 
345 1 Y 1 B GLU 785  ? CG  ? B GLU 787  CG  
346 1 Y 1 B GLU 785  ? CD  ? B GLU 787  CD  
347 1 Y 1 B GLU 785  ? OE1 ? B GLU 787  OE1 
348 1 Y 1 B GLU 785  ? OE2 ? B GLU 787  OE2 
349 1 Y 1 B ASP 796  ? CG  ? B ASP 798  CG  
350 1 Y 1 B ASP 796  ? OD1 ? B ASP 798  OD1 
351 1 Y 1 B ASP 796  ? OD2 ? B ASP 798  OD2 
352 1 Y 1 B ASP 855  ? CG  ? B ASP 857  CG  
353 1 Y 1 B ASP 855  ? OD1 ? B ASP 857  OD1 
354 1 Y 1 B ASP 855  ? OD2 ? B ASP 857  OD2 
355 1 Y 1 B LEU 905  ? CG  ? B LEU 907  CG  
356 1 Y 1 B LEU 905  ? CD1 ? B LEU 907  CD1 
357 1 Y 1 B LEU 905  ? CD2 ? B LEU 907  CD2 
358 1 Y 1 B GLU 917  ? CG  ? B GLU 919  CG  
359 1 Y 1 B GLU 917  ? CD  ? B GLU 919  CD  
360 1 Y 1 B GLU 917  ? OE1 ? B GLU 919  OE1 
361 1 Y 1 B GLU 917  ? OE2 ? B GLU 919  OE2 
362 1 Y 1 B GLU 932  ? CG  ? B GLU 934  CG  
363 1 Y 1 B GLU 932  ? CD  ? B GLU 934  CD  
364 1 Y 1 B GLU 932  ? OE1 ? B GLU 934  OE1 
365 1 Y 1 B GLU 932  ? OE2 ? B GLU 934  OE2 
366 1 Y 1 B LYS 933  ? CG  ? B LYS 935  CG  
367 1 Y 1 B LYS 933  ? CD  ? B LYS 935  CD  
368 1 Y 1 B LYS 933  ? CE  ? B LYS 935  CE  
369 1 Y 1 B LYS 933  ? NZ  ? B LYS 935  NZ  
370 1 Y 1 B GLN 938  ? CG  ? B GLN 940  CG  
371 1 Y 1 B GLN 938  ? CD  ? B GLN 940  CD  
372 1 Y 1 B GLN 938  ? OE1 ? B GLN 940  OE1 
373 1 Y 1 B GLN 938  ? NE2 ? B GLN 940  NE2 
374 1 Y 1 B ARG 952  ? CG  ? B ARG 954  CG  
375 1 Y 1 B ARG 952  ? CD  ? B ARG 954  CD  
376 1 Y 1 B ARG 952  ? NE  ? B ARG 954  NE  
377 1 Y 1 B ARG 952  ? CZ  ? B ARG 954  CZ  
378 1 Y 1 B ARG 952  ? NH1 ? B ARG 954  NH1 
379 1 Y 1 B ARG 952  ? NH2 ? B ARG 954  NH2 
380 1 Y 1 B ARG 958  ? CG  ? B ARG 960  CG  
381 1 Y 1 B ARG 958  ? CD  ? B ARG 960  CD  
382 1 Y 1 B ARG 958  ? NE  ? B ARG 960  NE  
383 1 Y 1 B ARG 958  ? CZ  ? B ARG 960  CZ  
384 1 Y 1 B ARG 958  ? NH1 ? B ARG 960  NH1 
385 1 Y 1 B ARG 958  ? NH2 ? B ARG 960  NH2 
386 1 Y 1 B ARG 1063 ? CG  ? B ARG 1065 CG  
387 1 Y 1 B ARG 1063 ? CD  ? B ARG 1065 CD  
388 1 Y 1 B ARG 1063 ? NE  ? B ARG 1065 NE  
389 1 Y 1 B ARG 1063 ? CZ  ? B ARG 1065 CZ  
390 1 Y 1 B ARG 1063 ? NH1 ? B ARG 1065 NH1 
391 1 Y 1 B ARG 1063 ? NH2 ? B ARG 1065 NH2 
392 1 Y 1 B LYS 1139 ? CG  ? B LYS 1141 CG  
393 1 Y 1 B LYS 1139 ? CD  ? B LYS 1141 CD  
394 1 Y 1 B LYS 1139 ? CE  ? B LYS 1141 CE  
395 1 Y 1 B LYS 1139 ? NZ  ? B LYS 1141 NZ  
396 1 Y 1 B ASN 1140 ? CG  ? B ASN 1142 CG  
397 1 Y 1 B ASN 1140 ? OD1 ? B ASN 1142 OD1 
398 1 Y 1 B ASN 1140 ? ND2 ? B ASN 1142 ND2 
399 1 Y 1 B GLN 1143 ? CG  ? B GLN 1145 CG  
400 1 Y 1 B GLN 1143 ? CD  ? B GLN 1145 CD  
401 1 Y 1 B GLN 1143 ? OE1 ? B GLN 1145 OE1 
402 1 Y 1 B GLN 1143 ? NE2 ? B GLN 1145 NE2 
403 1 Y 1 B LYS 1153 ? CG  ? B LYS 1155 CG  
404 1 Y 1 B LYS 1153 ? CD  ? B LYS 1155 CD  
405 1 Y 1 B LYS 1153 ? CE  ? B LYS 1155 CE  
406 1 Y 1 B LYS 1153 ? NZ  ? B LYS 1155 NZ  
407 1 Y 1 B GLU 1171 ? CG  ? B GLU 1173 CG  
408 1 Y 1 B GLU 1171 ? CD  ? B GLU 1173 CD  
409 1 Y 1 B GLU 1171 ? OE1 ? B GLU 1173 OE1 
410 1 Y 1 B GLU 1171 ? OE2 ? B GLU 1173 OE2 
411 1 Y 1 B LYS 1178 ? CG  ? B LYS 1180 CG  
412 1 Y 1 B LYS 1178 ? CD  ? B LYS 1180 CD  
413 1 Y 1 B LYS 1178 ? CE  ? B LYS 1180 CE  
414 1 Y 1 B LYS 1178 ? NZ  ? B LYS 1180 NZ  
415 1 Y 1 B GLU 1197 ? CG  ? B GLU 1199 CG  
416 1 Y 1 B GLU 1197 ? CD  ? B GLU 1199 CD  
417 1 Y 1 B GLU 1197 ? OE1 ? B GLU 1199 OE1 
418 1 Y 1 B GLU 1197 ? OE2 ? B GLU 1199 OE2 
419 1 Y 1 B SER 1228 ? OG  ? B SER 1230 OG  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.21rc1_5156 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .            2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .            3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .            4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   106.23 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9DL2 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     100.396 
_cell.length_a_esd                 ? 
_cell.length_b                     101.723 
_cell.length_b_esd                 ? 
_cell.length_c                     126.293 
_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                         9DL2 
_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                   9DL2 
_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             2.35 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          47.57 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;Reservoir contained 0.1 M HEPES, pH 7.5, 0.1 M sodium formate, 0.1 M magnesium chloride, 0.25 M ammonium sulfate, and 18% (w/v) PEG 3350. Enzyme was incubated with 10 mM 2,3-dihydro-1,4-benzodioxine-5-carboxylic acid and 5 mM NAD+. Crystal was soaked in cryobuffer containing 50 mM 2,3-dihydro-1,4-benzodioxine-5-carboxylic acid and 20% PEG 200
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 S 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-10-21 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.000034 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ALS BEAMLINE 8.2.1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.000034 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   8.2.1 
_diffrn_source.pdbx_synchrotron_site       ALS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9DL2 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.55 
_reflns.d_resolution_low                               48.20 
_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                                     658070 
_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                                3.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.01 
_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                                0.055 
_reflns.pdbx_Rpim_I_all                                0.029 
_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                              0.046 
_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                                    1.55 
_reflns_shell.d_res_low                                     1.58 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           61933 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             17375 
_reflns_shell.percent_possible_obs                          99.6 
_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                               3.6 
_reflns_shell.pdbx_chi_squared                              0.68 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.6 
_reflns_shell.pdbx_Rrim_I_all                               0.844 
_reflns_shell.pdbx_Rpim_I_all                               0.442 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.650 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.716 
_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                                 9DL2 
_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                            1.55 
_refine.ls_d_res_low                             46.90 
_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                     658070 
_refine.ls_number_reflns_R_free                  32861 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    94.47 
_refine.ls_percent_reflns_R_free                 4.99 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1685 
_refine.ls_R_factor_R_free                       0.1896 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1674 
_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                          0.05 
_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                 20.19 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.17 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        17811 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         334 
_refine_hist.number_atoms_solvent             2311 
_refine_hist.number_atoms_total               20456 
_refine_hist.d_res_high                       1.55 
_refine_hist.d_res_low                        46.90 
# 
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  ? 18825 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.867  ? 25730 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 16.697 ? 7052  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.048  ? 3024  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008  ? 3322  ? 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' 1.55 1.57  . . 1146 21863 98.00 . . . . 0.2706 . . . . . . . . . . . 0.2876 
'X-RAY DIFFRACTION' 1.57 1.59  . . 1097 21698 98.00 . . . . 0.2645 . . . . . . . . . . . 0.2815 
'X-RAY DIFFRACTION' 1.59 1.61  . . 1107 21687 98.00 . . . . 0.2578 . . . . . . . . . . . 0.2891 
'X-RAY DIFFRACTION' 1.61 1.63  . . 1200 21504 98.00 . . . . 0.2559 . . . . . . . . . . . 0.2826 
'X-RAY DIFFRACTION' 1.63 1.65  . . 1036 21686 98.00 . . . . 0.2453 . . . . . . . . . . . 0.2572 
'X-RAY DIFFRACTION' 1.65 1.67  . . 1106 21606 98.00 . . . . 0.2407 . . . . . . . . . . . 0.2587 
'X-RAY DIFFRACTION' 1.67 1.69  . . 1206 21367 97.00 . . . . 0.2330 . . . . . . . . . . . 0.2611 
'X-RAY DIFFRACTION' 1.69 1.72  . . 1166 21339 97.00 . . . . 0.2310 . . . . . . . . . . . 0.2575 
'X-RAY DIFFRACTION' 1.72 1.75  . . 1191 21295 97.00 . . . . 0.2186 . . . . . . . . . . . 0.2401 
'X-RAY DIFFRACTION' 1.75 1.77  . . 1081 21150 96.00 . . . . 0.2116 . . . . . . . . . . . 0.2375 
'X-RAY DIFFRACTION' 1.77 1.80  . . 1147 21079 96.00 . . . . 0.2034 . . . . . . . . . . . 0.2382 
'X-RAY DIFFRACTION' 1.80 1.84  . . 1122 21073 96.00 . . . . 0.1981 . . . . . . . . . . . 0.2278 
'X-RAY DIFFRACTION' 1.84 1.87  . . 1123 20732 94.00 . . . . 0.2001 . . . . . . . . . . . 0.2164 
'X-RAY DIFFRACTION' 1.87 1.91  . . 1114 20111 91.00 . . . . 0.2035 . . . . . . . . . . . 0.2340 
'X-RAY DIFFRACTION' 1.91 1.95  . . 908  19759 89.00 . . . . 0.2047 . . . . . . . . . . . 0.2338 
'X-RAY DIFFRACTION' 1.95 2.00  . . 986  18807 85.00 . . . . 0.1878 . . . . . . . . . . . 0.2096 
'X-RAY DIFFRACTION' 2.00 2.05  . . 1156 20569 94.00 . . . . 0.1809 . . . . . . . . . . . 0.2167 
'X-RAY DIFFRACTION' 2.05 2.10  . . 1065 21070 95.00 . . . . 0.1788 . . . . . . . . . . . 0.2133 
'X-RAY DIFFRACTION' 2.10 2.17  . . 1175 21230 96.00 . . . . 0.1726 . . . . . . . . . . . 0.2093 
'X-RAY DIFFRACTION' 2.17 2.24  . . 1080 20824 95.00 . . . . 0.1725 . . . . . . . . . . . 0.1983 
'X-RAY DIFFRACTION' 2.24 2.32  . . 1123 20862 94.00 . . . . 0.1687 . . . . . . . . . . . 0.1972 
'X-RAY DIFFRACTION' 2.32 2.41  . . 1127 21048 96.00 . . . . 0.1648 . . . . . . . . . . . 0.2097 
'X-RAY DIFFRACTION' 2.41 2.52  . . 1110 21017 95.00 . . . . 0.1646 . . . . . . . . . . . 0.1972 
'X-RAY DIFFRACTION' 2.52 2.65  . . 1048 21013 95.00 . . . . 0.1630 . . . . . . . . . . . 0.1823 
'X-RAY DIFFRACTION' 2.65 2.82  . . 1111 20859 94.00 . . . . 0.1664 . . . . . . . . . . . 0.1941 
'X-RAY DIFFRACTION' 2.82 3.03  . . 1092 20740 94.00 . . . . 0.1603 . . . . . . . . . . . 0.1828 
'X-RAY DIFFRACTION' 3.03 3.34  . . 982  19886 90.00 . . . . 0.1582 . . . . . . . . . . . 0.1783 
'X-RAY DIFFRACTION' 3.34 3.82  . . 927  18475 84.00 . . . . 0.1436 . . . . . . . . . . . 0.1591 
'X-RAY DIFFRACTION' 3.82 4.81  . . 1099 20206 92.00 . . . . 0.1220 . . . . . . . . . . . 0.1258 
'X-RAY DIFFRACTION' 4.81 46.90 . . 1030 20654 93.00 . . . . 0.1423 . . . . . . . . . . . 0.1569 
# 
_struct.entry_id                     9DL2 
_struct.title                        
'Structure of proline utilization A complexed with 2,3-dihydro-1,4-benzodioxine-5-carboxylic acid' 
_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        9DL2 
_struct_keywords.text            
;FLAVOENZYME, ROSSMANN FOLD, PROLINE DEHYDROGENASE, ALDEHYDE DEHYDROGENASE, PROLINE CATABOLISM, SUBSTRATE CHANNELING, BIFUNCTIONAL ENZYME, OXIDOREDUCTASE
;
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1  ? 
B  N N 1  ? 
C  N N 2  ? 
D  N N 3  ? 
E  N N 4  ? 
F  N N 5  ? 
G  N N 3  ? 
H  N N 5  ? 
I  N N 3  ? 
J  N N 6  ? 
K  N N 7  ? 
L  N N 7  ? 
M  N N 7  ? 
N  N N 7  ? 
O  N N 7  ? 
P  N N 8  ? 
Q  N N 2  ? 
R  N N 9  ? 
S  N N 3  ? 
T  N N 4  ? 
U  N N 3  ? 
V  N N 5  ? 
W  N N 3  ? 
X  N N 5  ? 
Y  N N 10 ? 
Z  N N 6  ? 
AA N N 7  ? 
BA N N 7  ? 
CA N N 8  ? 
DA N N 11 ? 
EA N N 11 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    F7X6I3_SINMM 
_struct_ref.pdbx_db_accession          F7X6I3 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSPNPLQKPAIDAAPAPFADFAPPVRPQSTLRRAITAAYRRPETECLPPLVEAATQSKEIRDAAASTARKLIEALRGKHS
GSGVEGLVQEYSLSSQEGVALMCLAEALLRIPDTATRDALIRDKIADGNWKSHLGGSRSLFVNAATWGLVVTGKLTSTVN
DRSLAAALTRLISRCGEPVIRRGVDMAMRMMGEQFVTGETIREALKRSKELEEKGFSYSYDMLGEAATTAADAERYYRDY
ESAIHAIGKASAGRGIYEGPGISIKLSALHPRYSRAQAARVMGELLPRVKALALLAKNYDIGLNIDAEEADRLELSLDLL
EVLCLDGDLSGWNGMGFVVQAYGKRCPFVLDFIIDLARRSGRRIMVRLVKGAYWDAEIKRAQLDGLADFPVFTRKIHTDV
SYIACAAKLLAATDVVFPQFATHNAQTLAAIYHMAGKDFHVGKYEFQCLHGMGEPLYEEVVGRGKLDRPCRIYAPVGTHE
TLLAYLVRRLLENGANSSFVHRINDPKVSIDELIADPVEVVRAMPVVGAKHDRIALPAELFGDARTNSAGLDLSNEETLA
SLTEALRESAAMKWTALPQLATGPAAGETRTVLNPGDHRDVVGSVTETSEEDARRAVRLAADAAPDWAAVPPSERAACLD
RAAELMQARMPTLLGLIIREAGKSALNAIAEVREAIDFLRYYAEQTRRTLGPGHGPLGPIVCISPWNFPLAIFTGQIAAA
LVAGNPVLAKPAEETPLIAAEGVRILREAGIPASALQLLPGDGRVGAALVAAAETAGVMFTGSTEVARLIQAQLADRLSP
AGRPIPLIAETGGQNAMIVDSSALAEQVVGDVITSAFDSAGQRCSALRVLCLQEDVADRILTMLKGALHELHIGRTDRLS
VDVGPVITSEAKDNIEKHIERMRGLGRKVEQIGLASETGVGTFVPPTIIELEKLSDLQREVFGPVLHVIRYRRDDLDRLV
DDVNATGYGLTFGLHTRLDETIAHVTSRIKAGNLYINRNIIGAVVGVQPFGGRGLSGTGPKAGGPLYLGRLVTTAPVPPQ
HSSVHTDPVLLDFAKWLDGKGARAEAEAARNAGSSSALGLDLELPGPVGERNLYTLHARGRILLVPATESGLYHQLAAAL
ATGNSVAIDAASGLQASLKNLPQTVGLRVSWSKDWAADGPFAGALVEGDAERIRAVNKAIAALPGPLLLVQAASSGEIAR
NPDAYCLNWLVEEVSASINTAAAGGNASLMAIG
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9DL2 A 3 ? 1235 ? F7X6I3 1 ? 1233 ? 1 1233 
2 1 9DL2 B 3 ? 1235 ? F7X6I3 1 ? 1233 ? 1 1233 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9DL2 SER A 1 ? UNP F7X6I3 ? ? 'expression tag' -1 1 
1 9DL2 MET A 2 ? UNP F7X6I3 ? ? 'expression tag' 0  2 
2 9DL2 SER B 1 ? UNP F7X6I3 ? ? 'expression tag' -1 3 
2 9DL2 MET B 2 ? UNP F7X6I3 ? ? 'expression tag' 0  4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric   2 
2 author_defined_assembly              ?    monomeric 1 
3 author_defined_assembly              ?    monomeric 1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 12880 ? 
1 MORE         -138  ? 
1 'SSA (A^2)'  77160 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,DA,EA 
2 1 A,C,D,E,F,G,H,I,J,K,L,M,N,O,P,DA                                   
3 1 B,Q,R,S,T,U,V,W,X,Y,Z,AA,BA,CA,EA                                  
# 
_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   ? HIS A 81   ? SER A 57   HIS A 79   1 ? 23 
HELX_P HELX_P4   AA4 GLY A 85   ? TYR A 93   ? GLY A 83   TYR A 91   1 ? 9  
HELX_P HELX_P5   AA5 SER A 96   ? LEU A 111  ? SER A 94   LEU A 109  1 ? 16 
HELX_P HELX_P6   AA6 ASP A 115  ? LYS A 126  ? ASP A 113  LYS A 124  1 ? 12 
HELX_P HELX_P7   AA7 ASN A 145  ? GLY A 155  ? ASN A 143  GLY A 153  1 ? 11 
HELX_P HELX_P8   AA8 ASN A 162  ? GLN A 196  ? ASN A 160  GLN A 194  1 ? 35 
HELX_P HELX_P9   AA9 THR A 202  ? LYS A 216  ? THR A 200  LYS A 214  1 ? 15 
HELX_P HELX_P10  AB1 THR A 231  ? ALA A 254  ? THR A 229  ALA A 252  1 ? 24 
HELX_P HELX_P11  AB2 ARG A 256  ? GLY A 261  ? ARG A 254  GLY A 259  1 ? 6  
HELX_P HELX_P12  AB3 LYS A 267  ? LEU A 271  ? LYS A 265  LEU A 269  5 ? 5  
HELX_P HELX_P13  AB4 SER A 276  ? ALA A 278  ? SER A 274  ALA A 276  5 ? 3  
HELX_P HELX_P14  AB5 GLN A 279  ? ASP A 302  ? GLN A 277  ASP A 300  1 ? 24 
HELX_P HELX_P15  AB6 GLU A 311  ? ASP A 313  ? GLU A 309  ASP A 311  5 ? 3  
HELX_P HELX_P16  AB7 ARG A 314  ? ASP A 328  ? ARG A 312  ASP A 326  1 ? 15 
HELX_P HELX_P17  AB8 GLY A 329  ? SER A 332  ? GLY A 327  SER A 330  5 ? 4  
HELX_P HELX_P18  AB9 ARG A 347  ? GLY A 363  ? ARG A 345  GLY A 361  1 ? 17 
HELX_P HELX_P19  AC1 TYR A 375  ? ASP A 386  ? TYR A 373  ASP A 384  1 ? 12 
HELX_P HELX_P20  AC2 ARG A 396  ? ALA A 413  ? ARG A 394  ALA A 411  1 ? 18 
HELX_P HELX_P21  AC3 ASN A 426  ? GLY A 438  ? ASN A 424  GLY A 436  1 ? 13 
HELX_P HELX_P22  AC4 GLY A 455  ? GLU A 460  ? GLY A 453  GLU A 458  1 ? 6  
HELX_P HELX_P23  AC5 THR A 480  ? ALA A 486  ? THR A 478  ALA A 484  1 ? 7  
HELX_P HELX_P24  AC6 TYR A 487  ? ALA A 497  ? TYR A 485  ALA A 495  1 ? 11 
HELX_P HELX_P25  AC7 SER A 500  ? ASN A 506  ? SER A 498  ASN A 504  1 ? 7  
HELX_P HELX_P26  AC8 SER A 511  ? ILE A 516  ? SER A 509  ILE A 514  1 ? 6  
HELX_P HELX_P27  AC9 ASP A 518  ? MET A 526  ? ASP A 516  MET A 524  1 ? 9  
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  ? ALA A 967  ? ASP A 955  ALA A 965  1 ? 11 
HELX_P HELX_P46  AF1 LEU A 980  ? ILE A 991  ? LEU A 978  ILE A 989  1 ? 12 
HELX_P HELX_P47  AF2 ARG A 1015 ? GLY A 1019 ? ARG A 1013 GLY A 1017 5 ? 5  
HELX_P HELX_P48  AF3 TYR A 1029 ? VAL A 1034 ? TYR A 1027 VAL A 1032 5 ? 6  
HELX_P HELX_P49  AF4 ASP A 1049 ? LYS A 1062 ? ASP A 1047 LYS A 1060 1 ? 14 
HELX_P HELX_P50  AF5 ALA A 1064 ? SER A 1078 ? ALA A 1062 SER A 1076 1 ? 15 
HELX_P HELX_P51  AF6 THR A 1110 ? THR A 1124 ? THR A 1108 THR A 1122 1 ? 15 
HELX_P HELX_P52  AF7 ALA A 1133 ? GLY A 1135 ? ALA A 1131 GLY A 1133 5 ? 3  
HELX_P HELX_P53  AF8 LEU A 1136 ? LYS A 1141 ? LEU A 1134 LYS A 1139 5 ? 6  
HELX_P HELX_P54  AF9 PRO A 1144 ? LEU A 1149 ? PRO A 1142 LEU A 1147 1 ? 6  
HELX_P HELX_P55  AG1 ASP A 1171 ? ALA A 1184 ? ASP A 1169 ALA A 1182 1 ? 14 
HELX_P HELX_P56  AG2 SER A 1196 ? ASN A 1203 ? SER A 1194 ASN A 1201 1 ? 8  
HELX_P HELX_P57  AG3 CYS A 1208 ? TRP A 1211 ? CYS A 1206 TRP A 1209 5 ? 4  
HELX_P HELX_P58  AG4 ALA A 1229 ? ILE A 1234 ? ALA A 1227 ILE A 1232 5 ? 6  
HELX_P HELX_P59  AG5 SER B 31   ? ALA B 40   ? SER B 29   ALA B 38   1 ? 10 
HELX_P HELX_P60  AG6 PRO B 44   ? THR B 57   ? PRO B 42   THR B 55   1 ? 14 
HELX_P HELX_P61  AG7 SER B 59   ? LYS B 80   ? SER B 57   LYS B 78   1 ? 22 
HELX_P HELX_P62  AG8 GLY B 85   ? TYR B 93   ? GLY B 83   TYR B 91   1 ? 9  
HELX_P HELX_P63  AG9 SER B 96   ? ARG B 112  ? SER B 94   ARG B 110  1 ? 17 
HELX_P HELX_P64  AH1 ASP B 115  ? LYS B 126  ? ASP B 113  LYS B 124  1 ? 12 
HELX_P HELX_P65  AH2 ASN B 145  ? GLY B 155  ? ASN B 143  GLY B 153  1 ? 11 
HELX_P HELX_P66  AH3 ASN B 162  ? GLY B 178  ? ASN B 160  GLY B 176  1 ? 17 
HELX_P HELX_P67  AH4 GLY B 178  ? GLN B 196  ? GLY B 176  GLN B 194  1 ? 19 
HELX_P HELX_P68  AH5 THR B 202  ? GLY B 217  ? THR B 200  GLY B 215  1 ? 16 
HELX_P HELX_P69  AH6 THR B 231  ? ALA B 254  ? THR B 229  ALA B 252  1 ? 24 
HELX_P HELX_P70  AH7 ARG B 256  ? GLY B 261  ? ARG B 254  GLY B 259  1 ? 6  
HELX_P HELX_P71  AH8 LYS B 267  ? LEU B 271  ? LYS B 265  LEU B 269  5 ? 5  
HELX_P HELX_P72  AH9 SER B 276  ? ALA B 278  ? SER B 274  ALA B 276  5 ? 3  
HELX_P HELX_P73  AI1 GLN B 279  ? ASP B 302  ? GLN B 277  ASP B 300  1 ? 24 
HELX_P HELX_P74  AI2 GLU B 311  ? ASP B 313  ? GLU B 309  ASP B 311  5 ? 3  
HELX_P HELX_P75  AI3 ARG B 314  ? ASP B 328  ? ARG B 312  ASP B 326  1 ? 15 
HELX_P HELX_P76  AI4 GLY B 329  ? SER B 332  ? GLY B 327  SER B 330  5 ? 4  
HELX_P HELX_P77  AI5 ARG B 347  ? GLY B 363  ? ARG B 345  GLY B 361  1 ? 17 
HELX_P HELX_P78  AI6 TYR B 375  ? GLY B 387  ? TYR B 373  GLY B 385  1 ? 13 
HELX_P HELX_P79  AI7 ARG B 396  ? ALA B 413  ? ARG B 394  ALA B 411  1 ? 18 
HELX_P HELX_P80  AI8 ASN B 426  ? ALA B 437  ? ASN B 424  ALA B 435  1 ? 12 
HELX_P HELX_P81  AI9 GLY B 455  ? GLU B 460  ? GLY B 453  GLU B 458  1 ? 6  
HELX_P HELX_P82  AJ1 THR B 480  ? ALA B 486  ? THR B 478  ALA B 484  1 ? 7  
HELX_P HELX_P83  AJ2 TYR B 487  ? GLU B 494  ? TYR B 485  GLU B 492  1 ? 8  
HELX_P HELX_P84  AJ3 SER B 500  ? ASN B 506  ? SER B 498  ASN B 504  1 ? 7  
HELX_P HELX_P85  AJ4 SER B 511  ? ILE B 516  ? SER B 509  ILE B 514  1 ? 6  
HELX_P HELX_P86  AJ5 ASP B 518  ? MET B 526  ? ASP B 516  MET B 524  1 ? 9  
HELX_P HELX_P87  AJ6 LEU B 538  ? LEU B 542  ? LEU B 536  LEU B 540  5 ? 5  
HELX_P HELX_P88  AJ7 ASN B 557  ? ALA B 573  ? ASN B 555  ALA B 571  1 ? 17 
HELX_P HELX_P89  AJ8 SER B 611  ? ALA B 631  ? SER B 609  ALA B 629  1 ? 21 
HELX_P HELX_P90  AJ9 PRO B 633  ? ARG B 651  ? PRO B 631  ARG B 649  1 ? 19 
HELX_P HELX_P91  AK1 ARG B 651  ? GLY B 664  ? ARG B 649  GLY B 662  1 ? 14 
HELX_P HELX_P92  AK2 SER B 666  ? LEU B 692  ? SER B 664  LEU B 690  1 ? 27 
HELX_P HELX_P93  AK3 LEU B 712  ? ALA B 725  ? LEU B 710  ALA B 723  1 ? 14 
HELX_P HELX_P94  AK4 THR B 737  ? ALA B 751  ? THR B 735  ALA B 749  1 ? 15 
HELX_P HELX_P95  AK5 PRO B 754  ? SER B 756  ? PRO B 752  SER B 754  5 ? 3  
HELX_P HELX_P96  AK6 ASP B 764  ? ALA B 774  ? ASP B 762  ALA B 772  1 ? 11 
HELX_P HELX_P97  AK7 SER B 785  ? ASP B 798  ? SER B 783  ASP B 796  1 ? 14 
HELX_P HELX_P98  AK8 LEU B 826  ? ASP B 840  ? LEU B 824  ASP B 838  1 ? 15 
HELX_P HELX_P99  AK9 SER B 841  ? GLN B 844  ? SER B 839  GLN B 842  5 ? 4  
HELX_P HELX_P100 AL1 GLU B 856  ? HIS B 871  ? GLU B 854  HIS B 869  1 ? 16 
HELX_P HELX_P101 AL2 THR B 890  ? LEU B 907  ? THR B 888  LEU B 905  1 ? 18 
HELX_P HELX_P102 AL3 ALA B 917  ? GLY B 923  ? ALA B 915  GLY B 921  5 ? 7  
HELX_P HELX_P103 AL4 LYS B 935  ? LEU B 939  ? LYS B 933  LEU B 937  5 ? 5  
HELX_P HELX_P104 AL5 ARG B 954  ? ASP B 956  ? ARG B 952  ASP B 954  5 ? 3  
HELX_P HELX_P105 AL6 ASP B 957  ? ALA B 967  ? ASP B 955  ALA B 965  1 ? 11 
HELX_P HELX_P106 AL7 LEU B 980  ? ILE B 991  ? LEU B 978  ILE B 989  1 ? 12 
HELX_P HELX_P107 AL8 ARG B 1015 ? GLY B 1019 ? ARG B 1013 GLY B 1017 5 ? 5  
HELX_P HELX_P108 AL9 TYR B 1029 ? VAL B 1034 ? TYR B 1027 VAL B 1032 5 ? 6  
HELX_P HELX_P109 AM1 ASP B 1049 ? LYS B 1062 ? ASP B 1047 LYS B 1060 1 ? 14 
HELX_P HELX_P110 AM2 ALA B 1064 ? SER B 1078 ? ALA B 1062 SER B 1076 1 ? 15 
HELX_P HELX_P111 AM3 THR B 1110 ? THR B 1124 ? THR B 1108 THR B 1122 1 ? 15 
HELX_P HELX_P112 AM4 ALA B 1133 ? GLY B 1135 ? ALA B 1131 GLY B 1133 5 ? 3  
HELX_P HELX_P113 AM5 LEU B 1136 ? LYS B 1141 ? LEU B 1134 LYS B 1139 5 ? 6  
HELX_P HELX_P114 AM6 PRO B 1144 ? LEU B 1149 ? PRO B 1142 LEU B 1147 1 ? 6  
HELX_P HELX_P115 AM7 ASP B 1156 ? GLY B 1161 ? ASP B 1154 GLY B 1159 1 ? 6  
HELX_P HELX_P116 AM8 ASP B 1171 ? ALA B 1184 ? ASP B 1169 ALA B 1182 1 ? 14 
HELX_P HELX_P117 AM9 SER B 1196 ? ASN B 1203 ? SER B 1194 ASN B 1201 1 ? 8  
HELX_P HELX_P118 AN1 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 
metalc1  metalc ? ? J  NAD . O2A ? ? ? 1_555 P  MG  . MG ? ? A NAD 2008 A MG  2014 1_555 ? ? ? ? ? ? ? 2.264 ? ? 
metalc2  metalc ? ? P  MG  . MG  ? ? ? 1_555 DA HOH . O  ? ? A MG  2014 A HOH 2111 1_555 ? ? ? ? ? ? ? 2.168 ? ? 
metalc3  metalc ? ? P  MG  . MG  ? ? ? 1_555 DA HOH . O  ? ? A MG  2014 A HOH 2639 1_555 ? ? ? ? ? ? ? 2.359 ? ? 
metalc4  metalc ? ? P  MG  . MG  ? ? ? 1_555 DA HOH . O  ? ? A MG  2014 A HOH 2962 1_555 ? ? ? ? ? ? ? 2.306 ? ? 
metalc5  metalc ? ? P  MG  . MG  ? ? ? 1_555 DA HOH . O  ? ? A MG  2014 A HOH 3001 1_555 ? ? ? ? ? ? ? 2.195 ? ? 
metalc6  metalc ? ? P  MG  . MG  ? ? ? 1_555 DA HOH . O  ? ? A MG  2014 A HOH 3002 1_555 ? ? ? ? ? ? ? 2.156 ? ? 
metalc7  metalc ? ? Z  NAD . O2A ? ? ? 1_555 CA MG  . MG ? ? B NAD 2010 B MG  2013 1_555 ? ? ? ? ? ? ? 2.076 ? ? 
metalc8  metalc ? ? CA MG  . MG  ? ? ? 1_555 EA HOH . O  ? ? B MG  2013 B HOH 2128 1_555 ? ? ? ? ? ? ? 1.936 ? ? 
metalc9  metalc ? ? CA MG  . MG  ? ? ? 1_555 EA HOH . O  ? ? B MG  2013 B HOH 2469 1_555 ? ? ? ? ? ? ? 2.002 ? ? 
metalc10 metalc ? ? CA MG  . MG  ? ? ? 1_555 EA HOH . O  ? ? B MG  2013 B HOH 2899 1_555 ? ? ? ? ? ? ? 2.342 ? ? 
metalc11 metalc ? ? CA MG  . MG  ? ? ? 1_555 EA HOH . O  ? ? B MG  2013 B HOH 2992 1_555 ? ? ? ? ? ? ? 2.272 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O2A ? J  NAD . ? A NAD 2008 ? 1_555 MG ? P  MG . ? A MG 2014 ? 1_555 O ? DA HOH . ? A HOH 2111 ? 1_555 81.1  ? 
2  O2A ? J  NAD . ? A NAD 2008 ? 1_555 MG ? P  MG . ? A MG 2014 ? 1_555 O ? DA HOH . ? A HOH 2639 ? 1_555 83.5  ? 
3  O   ? DA HOH . ? A HOH 2111 ? 1_555 MG ? P  MG . ? A MG 2014 ? 1_555 O ? DA HOH . ? A HOH 2639 ? 1_555 130.9 ? 
4  O2A ? J  NAD . ? A NAD 2008 ? 1_555 MG ? P  MG . ? A MG 2014 ? 1_555 O ? DA HOH . ? A HOH 2962 ? 1_555 84.6  ? 
5  O   ? DA HOH . ? A HOH 2111 ? 1_555 MG ? P  MG . ? A MG 2014 ? 1_555 O ? DA HOH . ? A HOH 2962 ? 1_555 145.6 ? 
6  O   ? DA HOH . ? A HOH 2639 ? 1_555 MG ? P  MG . ? A MG 2014 ? 1_555 O ? DA HOH . ? A HOH 2962 ? 1_555 77.6  ? 
7  O2A ? J  NAD . ? A NAD 2008 ? 1_555 MG ? P  MG . ? A MG 2014 ? 1_555 O ? DA HOH . ? A HOH 3001 ? 1_555 169.2 ? 
8  O   ? DA HOH . ? A HOH 2111 ? 1_555 MG ? P  MG . ? A MG 2014 ? 1_555 O ? DA HOH . ? A HOH 3001 ? 1_555 106.1 ? 
9  O   ? DA HOH . ? A HOH 2639 ? 1_555 MG ? P  MG . ? A MG 2014 ? 1_555 O ? DA HOH . ? A HOH 3001 ? 1_555 85.7  ? 
10 O   ? DA HOH . ? A HOH 2962 ? 1_555 MG ? P  MG . ? A MG 2014 ? 1_555 O ? DA HOH . ? A HOH 3001 ? 1_555 93.3  ? 
11 O2A ? J  NAD . ? A NAD 2008 ? 1_555 MG ? P  MG . ? A MG 2014 ? 1_555 O ? DA HOH . ? A HOH 3002 ? 1_555 93.6  ? 
12 O   ? DA HOH . ? A HOH 2111 ? 1_555 MG ? P  MG . ? A MG 2014 ? 1_555 O ? DA HOH . ? A HOH 3002 ? 1_555 71.4  ? 
13 O   ? DA HOH . ? A HOH 2639 ? 1_555 MG ? P  MG . ? A MG 2014 ? 1_555 O ? DA HOH . ? A HOH 3002 ? 1_555 156.2 ? 
14 O   ? DA HOH . ? A HOH 2962 ? 1_555 MG ? P  MG . ? A MG 2014 ? 1_555 O ? DA HOH . ? A HOH 3002 ? 1_555 78.5  ? 
15 O   ? DA HOH . ? A HOH 3001 ? 1_555 MG ? P  MG . ? A MG 2014 ? 1_555 O ? DA HOH . ? A HOH 3002 ? 1_555 96.3  ? 
16 O2A ? Z  NAD . ? B NAD 2010 ? 1_555 MG ? CA MG . ? B MG 2013 ? 1_555 O ? EA HOH . ? B HOH 2128 ? 1_555 91.2  ? 
17 O2A ? Z  NAD . ? B NAD 2010 ? 1_555 MG ? CA MG . ? B MG 2013 ? 1_555 O ? EA HOH . ? B HOH 2469 ? 1_555 101.3 ? 
18 O   ? EA HOH . ? B HOH 2128 ? 1_555 MG ? CA MG . ? B MG 2013 ? 1_555 O ? EA HOH . ? B HOH 2469 ? 1_555 127.3 ? 
19 O2A ? Z  NAD . ? B NAD 2010 ? 1_555 MG ? CA MG . ? B MG 2013 ? 1_555 O ? EA HOH . ? B HOH 2899 ? 1_555 88.4  ? 
20 O   ? EA HOH . ? B HOH 2128 ? 1_555 MG ? CA MG . ? B MG 2013 ? 1_555 O ? EA HOH . ? B HOH 2899 ? 1_555 152.5 ? 
21 O   ? EA HOH . ? B HOH 2469 ? 1_555 MG ? CA MG . ? B MG 2013 ? 1_555 O ? EA HOH . ? B HOH 2899 ? 1_555 79.5  ? 
22 O2A ? Z  NAD . ? B NAD 2010 ? 1_555 MG ? CA MG . ? B MG 2013 ? 1_555 O ? EA HOH . ? B HOH 2992 ? 1_555 166.8 ? 
23 O   ? EA HOH . ? B HOH 2128 ? 1_555 MG ? CA MG . ? B MG 2013 ? 1_555 O ? EA HOH . ? B HOH 2992 ? 1_555 97.2  ? 
24 O   ? EA HOH . ? B HOH 2469 ? 1_555 MG ? CA MG . ? B MG 2013 ? 1_555 O ? EA HOH . ? B HOH 2992 ? 1_555 81.6  ? 
25 O   ? EA HOH . ? B HOH 2899 ? 1_555 MG ? CA MG . ? B MG 2013 ? 1_555 O ? EA HOH . ? B HOH 2992 ? 1_555 79.4  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLY 1021 A . ? GLY 1019 A PRO 1022 A ? PRO 1020 A 1 -2.82 
2 GLY 1161 A . ? GLY 1159 A PRO 1162 A ? PRO 1160 A 1 -0.85 
3 GLY 1021 B . ? GLY 1019 B PRO 1022 B ? PRO 1020 B 1 -0.52 
4 GLY 1161 B . ? GLY 1159 B PRO 1162 B ? PRO 1160 B 1 3.90  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 9  ? 
AA2 ? 3  ? 
AA3 ? 2  ? 
AA4 ? 5  ? 
AA5 ? 10 ? 
AA6 ? 5  ? 
AA7 ? 9  ? 
AA8 ? 3  ? 
AA9 ? 2  ? 
AB1 ? 5  ? 
AB2 ? 10 ? 
AB3 ? 5  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA1 2 3  ? parallel      
AA1 3 4  ? parallel      
AA1 4 5  ? parallel      
AA1 5 6  ? parallel      
AA1 6 7  ? parallel      
AA1 7 8  ? parallel      
AA1 8 9  ? parallel      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA4 1 2  ? parallel      
AA4 2 3  ? parallel      
AA4 3 4  ? parallel      
AA4 4 5  ? parallel      
AA5 1 2  ? anti-parallel 
AA5 2 3  ? parallel      
AA5 3 4  ? parallel      
AA5 4 5  ? parallel      
AA5 5 6  ? parallel      
AA5 6 7  ? parallel      
AA5 7 8  ? parallel      
AA5 8 9  ? anti-parallel 
AA5 9 10 ? anti-parallel 
AA6 1 2  ? parallel      
AA6 2 3  ? parallel      
AA6 3 4  ? parallel      
AA6 4 5  ? parallel      
AA7 1 2  ? parallel      
AA7 2 3  ? parallel      
AA7 3 4  ? parallel      
AA7 4 5  ? parallel      
AA7 5 6  ? parallel      
AA7 6 7  ? parallel      
AA7 7 8  ? parallel      
AA7 8 9  ? parallel      
AA8 1 2  ? parallel      
AA8 2 3  ? anti-parallel 
AA9 1 2  ? anti-parallel 
AB1 1 2  ? parallel      
AB1 2 3  ? parallel      
AB1 3 4  ? parallel      
AB1 4 5  ? parallel      
AB2 1 2  ? anti-parallel 
AB2 2 3  ? parallel      
AB2 3 4  ? parallel      
AB2 4 5  ? parallel      
AB2 5 6  ? parallel      
AB2 6 7  ? parallel      
AB2 7 8  ? parallel      
AB2 8 9  ? anti-parallel 
AB2 9 10 ? anti-parallel 
AB3 1 2  ? parallel      
AB3 2 3  ? parallel      
AB3 3 4  ? parallel      
AB3 4 5  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  PHE A 218  ? ASP A 223  ? PHE A 216  ASP A 221  
AA1 2  GLY A 263  ? ILE A 266  ? GLY A 261  ILE A 264  
AA1 3  GLY A 304  ? ILE A 307  ? GLY A 302  ILE A 305  
AA1 4  MET A 337  ? GLN A 342  ? MET A 335  GLN A 340  
AA1 5  ILE A 366  ? VAL A 371  ? ILE A 364  VAL A 369  
AA1 6  VAL A 418  ? ALA A 423  ? VAL A 416  ALA A 421  
AA1 7  GLU A 447  ? LEU A 451  ? GLU A 445  LEU A 449  
AA1 8  CYS A 472  ? PRO A 477  ? CYS A 470  PRO A 475  
AA1 9  PHE A 218  ? ASP A 223  ? PHE A 216  ASP A 221  
AA2 1  TRP A 576  ? ALA A 578  ? TRP A 574  ALA A 576  
AA2 2  ASP A 599  ? GLU A 609  ? ASP A 597  GLU A 607  
AA2 3  GLU A 590  ? ASN A 596  ? GLU A 588  ASN A 594  
AA3 1  GLN A 581  ? LEU A 582  ? GLN A 579  LEU A 580  
AA3 2  GLY A 585  ? PRO A 586  ? GLY A 583  PRO A 584  
AA4 1  LEU A 758  ? LEU A 760  ? LEU A 756  LEU A 758  
AA4 2  VAL A 729  ? LYS A 732  ? VAL A 727  LYS A 730  
AA4 3  ILE A 702  ? ILE A 705  ? ILE A 700  ILE A 703  
AA4 4  GLY A 779  ? THR A 783  ? GLY A 777  THR A 781  
AA4 5  LEU A 809  ? GLU A 812  ? LEU A 807  GLU A 810  
AA5 1  VAL A 911  ? GLN A 913  ? VAL A 909  GLN A 911  
AA5 2  THR A 929  ? GLU A 932  ? THR A 927  GLU A 930  
AA5 3  VAL A 947  ? TYR A 953  ? VAL A 945  TYR A 951  
AA5 4  LEU A 849  ? GLN A 855  ? LEU A 847  GLN A 853  
AA5 5  ASN A 817  ? VAL A 821  ? ASN A 815  VAL A 819  
AA5 6  THR A 973  ? HIS A 977  ? THR A 971  HIS A 975  
AA5 7  ASN A 995  ? ILE A 998  ? ASN A 993  ILE A 996  
AA5 8  VAL A 1213 ? ASN A 1221 ? VAL A 1211 ASN A 1219 
AA5 9  GLU A 1092 ? ALA A 1100 ? GLU A 1090 ALA A 1098 
AA5 10 ASP A 1083 ? LEU A 1086 ? ASP A 1081 LEU A 1084 
AA6 1  VAL A 1151 ? SER A 1154 ? VAL A 1149 SER A 1152 
AA6 2  SER A 1127 ? ASP A 1131 ? SER A 1125 ASP A 1129 
AA6 3  ARG A 1103 ? VAL A 1107 ? ARG A 1101 VAL A 1105 
AA6 4  GLY A 1165 ? GLU A 1169 ? GLY A 1163 GLU A 1167 
AA6 5  VAL A 1192 ? ALA A 1195 ? VAL A 1190 ALA A 1193 
AA7 1  PHE B 218  ? ASP B 223  ? PHE B 216  ASP B 221  
AA7 2  GLY B 263  ? ILE B 266  ? GLY B 261  ILE B 264  
AA7 3  LEU B 305  ? ILE B 307  ? LEU B 303  ILE B 305  
AA7 4  MET B 337  ? GLN B 342  ? MET B 335  GLN B 340  
AA7 5  ILE B 366  ? VAL B 371  ? ILE B 364  VAL B 369  
AA7 6  VAL B 418  ? ALA B 423  ? VAL B 416  ALA B 421  
AA7 7  GLU B 447  ? LEU B 451  ? GLU B 445  LEU B 449  
AA7 8  CYS B 472  ? PRO B 477  ? CYS B 470  PRO B 475  
AA7 9  PHE B 218  ? ASP B 223  ? PHE B 216  ASP B 221  
AA8 1  TRP B 576  ? ALA B 578  ? TRP B 574  ALA B 576  
AA8 2  ASP B 599  ? GLU B 609  ? ASP B 597  GLU B 607  
AA8 3  GLU B 590  ? ASN B 596  ? GLU B 588  ASN B 594  
AA9 1  GLN B 581  ? LEU B 582  ? GLN B 579  LEU B 580  
AA9 2  GLY B 585  ? PRO B 586  ? GLY B 583  PRO B 584  
AB1 1  LEU B 758  ? LEU B 760  ? LEU B 756  LEU B 758  
AB1 2  VAL B 729  ? LYS B 732  ? VAL B 727  LYS B 730  
AB1 3  ILE B 702  ? ILE B 705  ? ILE B 700  ILE B 703  
AB1 4  GLY B 779  ? THR B 783  ? GLY B 777  THR B 781  
AB1 5  LEU B 809  ? GLU B 812  ? LEU B 807  GLU B 810  
AB2 1  VAL B 911  ? GLN B 913  ? VAL B 909  GLN B 911  
AB2 2  THR B 929  ? GLU B 932  ? THR B 927  GLU B 930  
AB2 3  VAL B 947  ? TYR B 953  ? VAL B 945  TYR B 951  
AB2 4  LEU B 849  ? GLN B 855  ? LEU B 847  GLN B 853  
AB2 5  ASN B 817  ? VAL B 821  ? ASN B 815  VAL B 819  
AB2 6  THR B 973  ? HIS B 977  ? THR B 971  HIS B 975  
AB2 7  ASN B 995  ? ILE B 998  ? ASN B 993  ILE B 996  
AB2 8  VAL B 1213 ? ASN B 1221 ? VAL B 1211 ASN B 1219 
AB2 9  GLU B 1092 ? ALA B 1100 ? GLU B 1090 ALA B 1098 
AB2 10 ASP B 1083 ? 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 LEU A 370  ? N LEU A 368  O GLN A 421  ? O GLN A 419  
AA1 6 7  N PHE A 422  ? N PHE A 420  O GLU A 447  ? O GLU A 445  
AA1 7 8  N CYS A 450  ? N CYS A 448  O TYR A 475  ? O TYR A 473  
AA1 8 9  O ILE A 474  ? O ILE A 472  N SER A 219  ? N SER A 217  
AA2 1 2  N ALA A 578  ? N ALA A 576  O THR A 608  ? O THR A 606  
AA2 2 3  O VAL A 607  ? O VAL A 605  N ARG A 592  ? N ARG A 590  
AA3 1 2  N LEU A 582  ? N LEU A 580  O GLY A 585  ? O GLY A 583  
AA4 1 2  O GLN A 759  ? O GLN A 757  N ALA A 731  ? N ALA A 729  
AA4 2 3  O LYS A 732  ? O LYS A 730  N CYS A 704  ? N CYS A 702  
AA4 3 4  N ILE A 705  ? N ILE A 703  O MET A 781  ? O MET A 779  
AA4 4 5  N PHE A 782  ? N PHE A 780  O ILE A 810  ? O ILE A 808  
AA5 1 2  N GLU A 912  ? N GLU A 910  O ILE A 930  ? O ILE A 928  
AA5 2 3  N ILE A 931  ? N ILE A 929  O LEU A 948  ? O LEU A 946  
AA5 3 4  O HIS A 949  ? O HIS A 947  N LEU A 852  ? N LEU A 850  
AA5 4 5  O CYS A 853  ? O CYS A 851  N MET A 819  ? N MET A 817  
AA5 5 6  N ILE A 820  ? N ILE A 818  O HIS A 977  ? O HIS A 975  
AA5 6 7  N LEU A 976  ? N LEU A 974  O TYR A 997  ? O TYR A 995  
AA5 7 8  N LEU A 996  ? N LEU A 994  O SER A 1217 ? O SER A 1215 
AA5 8 9  O 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 1154 ? O SER A 1152 N ILE A 1130 ? N ILE A 1128 
AA6 2 3  O ALA A 1129 ? O ALA A 1127 N LEU A 1106 ? N LEU A 1104 
AA6 3 4  N VAL A 1107 ? N VAL A 1105 O LEU A 1167 ? O LEU A 1165 
AA6 4 5  N VAL A 1168 ? N VAL A 1166 O GLN A 1193 ? O GLN A 1191 
AA7 1 2  N TYR B 222  ? N TYR B 220  O SER B 265  ? O SER B 263  
AA7 2 3  N ILE B 266  ? N ILE B 264  O ASN B 306  ? O ASN B 304  
AA7 3 4  N LEU B 305  ? N LEU B 303  O GLY B 338  ? O GLY B 336  
AA7 4 5  N MET B 337  ? N MET B 335  O MET B 367  ? O MET B 365  
AA7 5 6  N VAL B 368  ? N VAL B 366  O GLN B 421  ? O GLN B 419  
AA7 6 7  N PHE B 422  ? N PHE B 420  O GLU B 447  ? O GLU B 445  
AA7 7 8  N CYS B 450  ? N CYS B 448  O TYR B 475  ? O TYR B 473  
AA7 8 9  O ILE B 474  ? O ILE B 472  N SER B 219  ? N SER B 217  
AA8 1 2  N ALA B 578  ? N ALA B 576  O THR B 608  ? O THR B 606  
AA8 2 3  O GLY B 605  ? O GLY B 603  N VAL B 594  ? N VAL B 592  
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                   9DL2 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 OE1 B GLU 674  ? ? O B HOH 2101 ? ? 1.98 
2  1 OE1 B GLU 539  ? ? O B HOH 2102 ? ? 2.10 
3  1 O4  A SO4 2012 ? ? O A HOH 2101 ? ? 2.15 
4  1 OE1 A GLU 458  ? ? O A HOH 2102 ? ? 2.16 
5  1 O   A LEU 1183 ? ? O A HOH 2103 ? ? 2.16 
6  1 OD1 B ASP 375  ? B O B HOH 2103 ? ? 2.16 
7  1 O   B GLU 480  ? ? O B HOH 2104 ? ? 2.18 
8  1 O   B HOH 2105 ? ? O B HOH 2486 ? ? 2.18 
9  1 O   A HOH 2103 ? ? O A HOH 2813 ? ? 2.19 
10 1 NZ  B LYS 663  ? B O B HOH 2105 ? ? 2.19 
11 1 O   B HOH 2691 ? ? O B HOH 2824 ? ? 2.19 
12 1 O   B HOH 2831 ? ? O B HOH 3101 ? ? 2.19 
13 1 ND2 B ASN 667  ? ? O B HOH 2106 ? ? 2.19 
14 1 OD1 B ASP 375  ? B O B HOH 2107 ? ? 2.19 
15 1 O   A HOH 2617 ? ? O A HOH 3178 ? ? 2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ALA A 22   ? ? -157.41 56.48   
2  1 LYS A 124  ? ? -121.74 -51.04  
3  1 GLU A 308  ? ? -122.62 -133.46 
4  1 MET A 452  ? ? -145.54 -49.35  
5  1 VAL A 460  ? ? -120.49 -51.62  
6  1 LYS A 465  ? ? -120.09 -125.01 
7  1 ASP A 597  ? ? -173.75 96.82   
8  1 THR A 689  ? ? -130.33 -47.26  
9  1 HIS A 694  ? ? -100.46 75.63   
10 1 THR A 811  ? ? -126.48 -158.14 
11 1 GLN A 842  ? ? -94.85  48.31   
12 1 LEU A 970  ? ? -99.93  -87.42  
13 1 ALA B 22   ? ? -156.12 60.29   
14 1 LYS B 124  ? ? -134.68 -42.39  
15 1 ASN B 129  ? ? -74.42  48.01   
16 1 SER B 132  ? ? -98.73  48.71   
17 1 HIS B 133  ? ? -165.97 -12.67  
18 1 GLU B 308  ? ? -119.07 -134.32 
19 1 MET B 452  ? ? -143.88 -45.28  
20 1 LYS B 465  ? ? -130.58 -142.97 
21 1 ASP B 467  ? ? -112.48 65.11   
22 1 TYR B 485  ? ? -140.17 16.98   
23 1 PRO B 578  ? ? -68.54  98.64   
24 1 ASP B 597  ? ? -170.58 98.24   
25 1 THR B 689  ? ? -131.40 -44.88  
26 1 HIS B 694  ? ? -100.68 78.67   
27 1 THR B 811  ? ? -125.19 -155.99 
28 1 GLN B 842  ? ? -93.23  50.52   
29 1 LEU B 970  ? ? -97.23  -86.88  
30 1 GLN B 1008 ? ? -118.72 78.98   
31 1 VAL B 1105 ? ? -119.77 79.78   
32 1 ASP B 1154 ? ? -159.82 87.59   
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -25.5906 66.1747 92.8750 0.1786 ? 0.0099  ? 0.0142  ? 0.1413 ? 0.0151  ? 0.1595 ? 0.5572 ? -0.0534 
? 0.1417 ? 0.1100 ? -0.0032 ? 0.1510 ? -0.0256 ? -0.0580 ? -0.0043 ? 0.0304 ? 0.0349 ? 0.0187  ? -0.0077 ? -0.0061 ? -0.0095 ? 
2 'X-RAY DIFFRACTION' ? refined 5.9432   31.5811 91.3666 0.1373 ? -0.0037 ? -0.0070 ? 0.1516 ? -0.0068 ? 0.1400 ? 0.2167 ? -0.0198 
? 0.1281 ? 0.2189 ? -0.0274 ? 0.5159 ? 0.0240  ? -0.0427 ? -0.0183 ? 0.0580 ? 0.0132 ? -0.0152 ? 0.0757  ? -0.1039 ? -0.0367 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? 'chain A and peptide' 
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? 'chain B and peptide' 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 3290 ? 5.81 . 
2 1 O ? A HOH 3291 ? 5.82 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A SER -1   ? A SER 1    
2  1 Y 1 A MET 0    ? A MET 2    
3  1 Y 1 A MET 1    ? A MET 3    
4  1 Y 1 A SER 2    ? A SER 4    
5  1 Y 1 A PRO 3    ? A PRO 5    
6  1 Y 1 A ASN 4    ? A ASN 6    
7  1 Y 1 A PRO 5    ? A PRO 7    
8  1 Y 1 A LEU 6    ? A LEU 8    
9  1 Y 1 A GLN 7    ? A GLN 9    
10 1 Y 1 A LYS 8    ? A LYS 10   
11 1 Y 1 A PRO 9    ? A PRO 11   
12 1 Y 1 A ALA 10   ? A ALA 12   
13 1 Y 1 A ILE 11   ? A ILE 13   
14 1 Y 1 A ASP 12   ? A ASP 14   
15 1 Y 1 A ALA 13   ? A ALA 15   
16 1 Y 1 A SER 80   ? A SER 82   
17 1 Y 1 A GLY 81   ? A GLY 83   
18 1 Y 1 A GLY 135  ? A GLY 137  
19 1 Y 1 A GLY 136  ? A GLY 138  
20 1 Y 1 B SER -1   ? B SER 1    
21 1 Y 1 B MET 0    ? B MET 2    
22 1 Y 1 B MET 1    ? B MET 3    
23 1 Y 1 B SER 2    ? B SER 4    
24 1 Y 1 B PRO 3    ? B PRO 5    
25 1 Y 1 B ASN 4    ? B ASN 6    
26 1 Y 1 B PRO 5    ? B PRO 7    
27 1 Y 1 B LEU 6    ? B LEU 8    
28 1 Y 1 B GLN 7    ? B GLN 9    
29 1 Y 1 B LYS 8    ? B LYS 10   
30 1 Y 1 B PRO 9    ? B PRO 11   
31 1 Y 1 B ALA 10   ? B ALA 12   
32 1 Y 1 B ILE 11   ? B ILE 13   
33 1 Y 1 B ASP 12   ? B ASP 14   
34 1 Y 1 B ALA 13   ? B ALA 15   
35 1 Y 1 B HIS 79   ? B HIS 81   
36 1 Y 1 B SER 80   ? B SER 82   
37 1 Y 1 B GLY 81   ? B GLY 83   
38 1 Y 1 B GLY 135  ? B GLY 137  
39 1 Y 1 B GLY 136  ? B GLY 138  
40 1 Y 1 B SER 137  ? B SER 139  
41 1 Y 1 B ASN 493  ? B ASN 495  
42 1 Y 1 B GLY 494  ? B GLY 496  
43 1 Y 1 B MET 1230 ? B MET 1232 
44 1 Y 1 B ALA 1231 ? B ALA 1233 
45 1 Y 1 B ILE 1232 ? B ILE 1234 
46 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 
53E C01    C  N N 1   
53E C02    C  N N 2   
53E O03    O  N N 3   
53E C04    C  Y N 4   
53E C05    C  Y N 5   
53E C06    C  Y N 6   
53E C07    C  Y N 7   
53E C08    C  Y N 8   
53E C09    C  Y N 9   
53E O10    O  N N 10  
53E C11    C  N N 11  
53E O12    O  N N 12  
53E O13    O  N N 13  
53E H1     H  N N 14  
53E H2     H  N N 15  
53E H3     H  N N 16  
53E H4     H  N N 17  
53E H5     H  N N 18  
53E H6     H  N N 19  
53E H7     H  N N 20  
53E H8     H  N N 21  
ALA N      N  N N 22  
ALA CA     C  N S 23  
ALA C      C  N N 24  
ALA O      O  N N 25  
ALA CB     C  N N 26  
ALA OXT    O  N N 27  
ALA H      H  N N 28  
ALA H2     H  N N 29  
ALA HA     H  N N 30  
ALA HB1    H  N N 31  
ALA HB2    H  N N 32  
ALA HB3    H  N N 33  
ALA HXT    H  N N 34  
ARG N      N  N N 35  
ARG CA     C  N S 36  
ARG C      C  N N 37  
ARG O      O  N N 38  
ARG CB     C  N N 39  
ARG CG     C  N N 40  
ARG CD     C  N N 41  
ARG NE     N  N N 42  
ARG CZ     C  N N 43  
ARG NH1    N  N N 44  
ARG NH2    N  N N 45  
ARG OXT    O  N N 46  
ARG H      H  N N 47  
ARG H2     H  N N 48  
ARG HA     H  N N 49  
ARG HB2    H  N N 50  
ARG HB3    H  N N 51  
ARG HG2    H  N N 52  
ARG HG3    H  N N 53  
ARG HD2    H  N N 54  
ARG HD3    H  N N 55  
ARG HE     H  N N 56  
ARG HH11   H  N N 57  
ARG HH12   H  N N 58  
ARG HH21   H  N N 59  
ARG HH22   H  N N 60  
ARG HXT    H  N N 61  
ASN N      N  N N 62  
ASN CA     C  N S 63  
ASN C      C  N N 64  
ASN O      O  N N 65  
ASN CB     C  N N 66  
ASN CG     C  N N 67  
ASN OD1    O  N N 68  
ASN ND2    N  N N 69  
ASN OXT    O  N N 70  
ASN H      H  N N 71  
ASN H2     H  N N 72  
ASN HA     H  N N 73  
ASN HB2    H  N N 74  
ASN HB3    H  N N 75  
ASN HD21   H  N N 76  
ASN HD22   H  N N 77  
ASN HXT    H  N N 78  
ASP N      N  N N 79  
ASP CA     C  N S 80  
ASP C      C  N N 81  
ASP O      O  N N 82  
ASP CB     C  N N 83  
ASP CG     C  N N 84  
ASP OD1    O  N N 85  
ASP OD2    O  N N 86  
ASP OXT    O  N N 87  
ASP H      H  N N 88  
ASP H2     H  N N 89  
ASP HA     H  N N 90  
ASP HB2    H  N N 91  
ASP HB3    H  N N 92  
ASP HD2    H  N N 93  
ASP HXT    H  N N 94  
CYS N      N  N N 95  
CYS CA     C  N R 96  
CYS C      C  N N 97  
CYS O      O  N N 98  
CYS CB     C  N N 99  
CYS SG     S  N N 100 
CYS OXT    O  N N 101 
CYS H      H  N N 102 
CYS H2     H  N N 103 
CYS HA     H  N N 104 
CYS HB2    H  N N 105 
CYS HB3    H  N N 106 
CYS HG     H  N N 107 
CYS HXT    H  N N 108 
FAD PA     P  N R 109 
FAD O1A    O  N N 110 
FAD O2A    O  N N 111 
FAD O5B    O  N N 112 
FAD C5B    C  N N 113 
FAD C4B    C  N R 114 
FAD O4B    O  N N 115 
FAD C3B    C  N S 116 
FAD O3B    O  N N 117 
FAD C2B    C  N R 118 
FAD O2B    O  N N 119 
FAD C1B    C  N R 120 
FAD N9A    N  Y N 121 
FAD C8A    C  Y N 122 
FAD N7A    N  Y N 123 
FAD C5A    C  Y N 124 
FAD C6A    C  Y N 125 
FAD N6A    N  N N 126 
FAD N1A    N  Y N 127 
FAD C2A    C  Y N 128 
FAD N3A    N  Y N 129 
FAD C4A    C  Y N 130 
FAD N1     N  N N 131 
FAD C2     C  N N 132 
FAD O2     O  N N 133 
FAD N3     N  N N 134 
FAD C4     C  N N 135 
FAD O4     O  N N 136 
FAD C4X    C  N N 137 
FAD N5     N  N N 138 
FAD C5X    C  Y N 139 
FAD C6     C  Y N 140 
FAD C7     C  Y N 141 
FAD C7M    C  N N 142 
FAD C8     C  Y N 143 
FAD C8M    C  N N 144 
FAD C9     C  Y N 145 
FAD C9A    C  Y N 146 
FAD N10    N  N N 147 
FAD C10    C  N N 148 
FAD "C1'"  C  N N 149 
FAD "C2'"  C  N S 150 
FAD "O2'"  O  N N 151 
FAD "C3'"  C  N S 152 
FAD "O3'"  O  N N 153 
FAD "C4'"  C  N R 154 
FAD "O4'"  O  N N 155 
FAD "C5'"  C  N N 156 
FAD "O5'"  O  N N 157 
FAD P      P  N R 158 
FAD O1P    O  N N 159 
FAD O2P    O  N N 160 
FAD O3P    O  N N 161 
FAD HOA2   H  N N 162 
FAD H51A   H  N N 163 
FAD H52A   H  N N 164 
FAD H4B    H  N N 165 
FAD H3B    H  N N 166 
FAD HO3A   H  N N 167 
FAD H2B    H  N N 168 
FAD HO2A   H  N N 169 
FAD H1B    H  N N 170 
FAD H8A    H  N N 171 
FAD H61A   H  N N 172 
FAD H62A   H  N N 173 
FAD H2A    H  N N 174 
FAD HN3    H  N N 175 
FAD H6     H  N N 176 
FAD HM71   H  N N 177 
FAD HM72   H  N N 178 
FAD HM73   H  N N 179 
FAD HM81   H  N N 180 
FAD HM82   H  N N 181 
FAD HM83   H  N N 182 
FAD H9     H  N N 183 
FAD "H1'1" H  N N 184 
FAD "H1'2" H  N N 185 
FAD "H2'"  H  N N 186 
FAD "HO2'" H  N N 187 
FAD "H3'"  H  N N 188 
FAD "HO3'" H  N N 189 
FAD "H4'"  H  N N 190 
FAD "HO4'" H  N N 191 
FAD "H5'1" H  N N 192 
FAD "H5'2" H  N N 193 
FAD HOP2   H  N N 194 
FMT C      C  N N 195 
FMT O1     O  N N 196 
FMT O2     O  N N 197 
FMT H      H  N N 198 
FMT HO2    H  N N 199 
GLN N      N  N N 200 
GLN CA     C  N S 201 
GLN C      C  N N 202 
GLN O      O  N N 203 
GLN CB     C  N N 204 
GLN CG     C  N N 205 
GLN CD     C  N N 206 
GLN OE1    O  N N 207 
GLN NE2    N  N N 208 
GLN OXT    O  N N 209 
GLN H      H  N N 210 
GLN H2     H  N N 211 
GLN HA     H  N N 212 
GLN HB2    H  N N 213 
GLN HB3    H  N N 214 
GLN HG2    H  N N 215 
GLN HG3    H  N N 216 
GLN HE21   H  N N 217 
GLN HE22   H  N N 218 
GLN HXT    H  N N 219 
GLU N      N  N N 220 
GLU CA     C  N S 221 
GLU C      C  N N 222 
GLU O      O  N N 223 
GLU CB     C  N N 224 
GLU CG     C  N N 225 
GLU CD     C  N N 226 
GLU OE1    O  N N 227 
GLU OE2    O  N N 228 
GLU OXT    O  N N 229 
GLU H      H  N N 230 
GLU H2     H  N N 231 
GLU HA     H  N N 232 
GLU HB2    H  N N 233 
GLU HB3    H  N N 234 
GLU HG2    H  N N 235 
GLU HG3    H  N N 236 
GLU HE2    H  N N 237 
GLU HXT    H  N N 238 
GLY N      N  N N 239 
GLY CA     C  N N 240 
GLY C      C  N N 241 
GLY O      O  N N 242 
GLY OXT    O  N N 243 
GLY H      H  N N 244 
GLY H2     H  N N 245 
GLY HA2    H  N N 246 
GLY HA3    H  N N 247 
GLY HXT    H  N N 248 
HIS N      N  N N 249 
HIS CA     C  N S 250 
HIS C      C  N N 251 
HIS O      O  N N 252 
HIS CB     C  N N 253 
HIS CG     C  Y N 254 
HIS ND1    N  Y N 255 
HIS CD2    C  Y N 256 
HIS CE1    C  Y N 257 
HIS NE2    N  Y N 258 
HIS OXT    O  N N 259 
HIS H      H  N N 260 
HIS H2     H  N N 261 
HIS HA     H  N N 262 
HIS HB2    H  N N 263 
HIS HB3    H  N N 264 
HIS HD1    H  N N 265 
HIS HD2    H  N N 266 
HIS HE1    H  N N 267 
HIS HE2    H  N N 268 
HIS HXT    H  N N 269 
HOH O      O  N N 270 
HOH H1     H  N N 271 
HOH H2     H  N N 272 
ILE N      N  N N 273 
ILE CA     C  N S 274 
ILE C      C  N N 275 
ILE O      O  N N 276 
ILE CB     C  N S 277 
ILE CG1    C  N N 278 
ILE CG2    C  N N 279 
ILE CD1    C  N N 280 
ILE OXT    O  N N 281 
ILE H      H  N N 282 
ILE H2     H  N N 283 
ILE HA     H  N N 284 
ILE HB     H  N N 285 
ILE HG12   H  N N 286 
ILE HG13   H  N N 287 
ILE HG21   H  N N 288 
ILE HG22   H  N N 289 
ILE HG23   H  N N 290 
ILE HD11   H  N N 291 
ILE HD12   H  N N 292 
ILE HD13   H  N N 293 
ILE HXT    H  N N 294 
LEU N      N  N N 295 
LEU CA     C  N S 296 
LEU C      C  N N 297 
LEU O      O  N N 298 
LEU CB     C  N N 299 
LEU CG     C  N N 300 
LEU CD1    C  N N 301 
LEU CD2    C  N N 302 
LEU OXT    O  N N 303 
LEU H      H  N N 304 
LEU H2     H  N N 305 
LEU HA     H  N N 306 
LEU HB2    H  N N 307 
LEU HB3    H  N N 308 
LEU HG     H  N N 309 
LEU HD11   H  N N 310 
LEU HD12   H  N N 311 
LEU HD13   H  N N 312 
LEU HD21   H  N N 313 
LEU HD22   H  N N 314 
LEU HD23   H  N N 315 
LEU HXT    H  N N 316 
LYS N      N  N N 317 
LYS CA     C  N S 318 
LYS C      C  N N 319 
LYS O      O  N N 320 
LYS CB     C  N N 321 
LYS CG     C  N N 322 
LYS CD     C  N N 323 
LYS CE     C  N N 324 
LYS NZ     N  N N 325 
LYS OXT    O  N N 326 
LYS H      H  N N 327 
LYS H2     H  N N 328 
LYS HA     H  N N 329 
LYS HB2    H  N N 330 
LYS HB3    H  N N 331 
LYS HG2    H  N N 332 
LYS HG3    H  N N 333 
LYS HD2    H  N N 334 
LYS HD3    H  N N 335 
LYS HE2    H  N N 336 
LYS HE3    H  N N 337 
LYS HZ1    H  N N 338 
LYS HZ2    H  N N 339 
LYS HZ3    H  N N 340 
LYS HXT    H  N N 341 
MET N      N  N N 342 
MET CA     C  N S 343 
MET C      C  N N 344 
MET O      O  N N 345 
MET CB     C  N N 346 
MET CG     C  N N 347 
MET SD     S  N N 348 
MET CE     C  N N 349 
MET OXT    O  N N 350 
MET H      H  N N 351 
MET H2     H  N N 352 
MET HA     H  N N 353 
MET HB2    H  N N 354 
MET HB3    H  N N 355 
MET HG2    H  N N 356 
MET HG3    H  N N 357 
MET HE1    H  N N 358 
MET HE2    H  N N 359 
MET HE3    H  N N 360 
MET HXT    H  N N 361 
MG  MG     MG N N 362 
NAD PA     P  N S 363 
NAD O1A    O  N N 364 
NAD O2A    O  N N 365 
NAD O5B    O  N N 366 
NAD C5B    C  N N 367 
NAD C4B    C  N R 368 
NAD O4B    O  N N 369 
NAD C3B    C  N S 370 
NAD O3B    O  N N 371 
NAD C2B    C  N R 372 
NAD O2B    O  N N 373 
NAD C1B    C  N R 374 
NAD N9A    N  Y N 375 
NAD C8A    C  Y N 376 
NAD N7A    N  Y N 377 
NAD C5A    C  Y N 378 
NAD C6A    C  Y N 379 
NAD N6A    N  N N 380 
NAD N1A    N  Y N 381 
NAD C2A    C  Y N 382 
NAD N3A    N  Y N 383 
NAD C4A    C  Y N 384 
NAD O3     O  N N 385 
NAD PN     P  N N 386 
NAD O1N    O  N N 387 
NAD O2N    O  N N 388 
NAD O5D    O  N N 389 
NAD C5D    C  N N 390 
NAD C4D    C  N R 391 
NAD O4D    O  N N 392 
NAD C3D    C  N S 393 
NAD O3D    O  N N 394 
NAD C2D    C  N R 395 
NAD O2D    O  N N 396 
NAD C1D    C  N R 397 
NAD N1N    N  Y N 398 
NAD C2N    C  Y N 399 
NAD C3N    C  Y N 400 
NAD C7N    C  N N 401 
NAD O7N    O  N N 402 
NAD N7N    N  N N 403 
NAD C4N    C  Y N 404 
NAD C5N    C  Y N 405 
NAD C6N    C  Y N 406 
NAD HOA2   H  N N 407 
NAD H51A   H  N N 408 
NAD H52A   H  N N 409 
NAD H4B    H  N N 410 
NAD H3B    H  N N 411 
NAD HO3A   H  N N 412 
NAD H2B    H  N N 413 
NAD HO2A   H  N N 414 
NAD H1B    H  N N 415 
NAD H8A    H  N N 416 
NAD H61A   H  N N 417 
NAD H62A   H  N N 418 
NAD H2A    H  N N 419 
NAD H51N   H  N N 420 
NAD H52N   H  N N 421 
NAD H4D    H  N N 422 
NAD H3D    H  N N 423 
NAD HO3N   H  N N 424 
NAD H2D    H  N N 425 
NAD HO2N   H  N N 426 
NAD H1D    H  N N 427 
NAD H2N    H  N N 428 
NAD H71N   H  N N 429 
NAD H72N   H  N N 430 
NAD H4N    H  N N 431 
NAD H5N    H  N N 432 
NAD H6N    H  N N 433 
PEG C1     C  N N 434 
PEG O1     O  N N 435 
PEG C2     C  N N 436 
PEG O2     O  N N 437 
PEG C3     C  N N 438 
PEG C4     C  N N 439 
PEG O4     O  N N 440 
PEG H11    H  N N 441 
PEG H12    H  N N 442 
PEG HO1    H  N N 443 
PEG H21    H  N N 444 
PEG H22    H  N N 445 
PEG H31    H  N N 446 
PEG H32    H  N N 447 
PEG H41    H  N N 448 
PEG H42    H  N N 449 
PEG HO4    H  N N 450 
PG4 O1     O  N N 451 
PG4 C1     C  N N 452 
PG4 C2     C  N N 453 
PG4 O2     O  N N 454 
PG4 C3     C  N N 455 
PG4 C4     C  N N 456 
PG4 O3     O  N N 457 
PG4 C5     C  N N 458 
PG4 C6     C  N N 459 
PG4 O4     O  N N 460 
PG4 C7     C  N N 461 
PG4 C8     C  N N 462 
PG4 O5     O  N N 463 
PG4 HO1    H  N N 464 
PG4 H11    H  N N 465 
PG4 H12    H  N N 466 
PG4 H21    H  N N 467 
PG4 H22    H  N N 468 
PG4 H31    H  N N 469 
PG4 H32    H  N N 470 
PG4 H41    H  N N 471 
PG4 H42    H  N N 472 
PG4 H51    H  N N 473 
PG4 H52    H  N N 474 
PG4 H61    H  N N 475 
PG4 H62    H  N N 476 
PG4 H71    H  N N 477 
PG4 H72    H  N N 478 
PG4 H81    H  N N 479 
PG4 H82    H  N N 480 
PG4 HO5    H  N N 481 
PGE C1     C  N N 482 
PGE O1     O  N N 483 
PGE C2     C  N N 484 
PGE O2     O  N N 485 
PGE C3     C  N N 486 
PGE C4     C  N N 487 
PGE O4     O  N N 488 
PGE C6     C  N N 489 
PGE C5     C  N N 490 
PGE O3     O  N N 491 
PGE H1     H  N N 492 
PGE H12    H  N N 493 
PGE HO1    H  N N 494 
PGE H2     H  N N 495 
PGE H22    H  N N 496 
PGE H3     H  N N 497 
PGE H32    H  N N 498 
PGE H4     H  N N 499 
PGE H42    H  N N 500 
PGE HO4    H  N N 501 
PGE H6     H  N N 502 
PGE H62    H  N N 503 
PGE H5     H  N N 504 
PGE H52    H  N N 505 
PHE N      N  N N 506 
PHE CA     C  N S 507 
PHE C      C  N N 508 
PHE O      O  N N 509 
PHE CB     C  N N 510 
PHE CG     C  Y N 511 
PHE CD1    C  Y N 512 
PHE CD2    C  Y N 513 
PHE CE1    C  Y N 514 
PHE CE2    C  Y N 515 
PHE CZ     C  Y N 516 
PHE OXT    O  N N 517 
PHE H      H  N N 518 
PHE H2     H  N N 519 
PHE HA     H  N N 520 
PHE HB2    H  N N 521 
PHE HB3    H  N N 522 
PHE HD1    H  N N 523 
PHE HD2    H  N N 524 
PHE HE1    H  N N 525 
PHE HE2    H  N N 526 
PHE HZ     H  N N 527 
PHE HXT    H  N N 528 
PRO N      N  N N 529 
PRO CA     C  N S 530 
PRO C      C  N N 531 
PRO O      O  N N 532 
PRO CB     C  N N 533 
PRO CG     C  N N 534 
PRO CD     C  N N 535 
PRO OXT    O  N N 536 
PRO H      H  N N 537 
PRO HA     H  N N 538 
PRO HB2    H  N N 539 
PRO HB3    H  N N 540 
PRO HG2    H  N N 541 
PRO HG3    H  N N 542 
PRO HD2    H  N N 543 
PRO HD3    H  N N 544 
PRO HXT    H  N N 545 
SER N      N  N N 546 
SER CA     C  N S 547 
SER C      C  N N 548 
SER O      O  N N 549 
SER CB     C  N N 550 
SER OG     O  N N 551 
SER OXT    O  N N 552 
SER H      H  N N 553 
SER H2     H  N N 554 
SER HA     H  N N 555 
SER HB2    H  N N 556 
SER HB3    H  N N 557 
SER HG     H  N N 558 
SER HXT    H  N N 559 
SO4 S      S  N N 560 
SO4 O1     O  N N 561 
SO4 O2     O  N N 562 
SO4 O3     O  N N 563 
SO4 O4     O  N N 564 
THR N      N  N N 565 
THR CA     C  N S 566 
THR C      C  N N 567 
THR O      O  N N 568 
THR CB     C  N R 569 
THR OG1    O  N N 570 
THR CG2    C  N N 571 
THR OXT    O  N N 572 
THR H      H  N N 573 
THR H2     H  N N 574 
THR HA     H  N N 575 
THR HB     H  N N 576 
THR HG1    H  N N 577 
THR HG21   H  N N 578 
THR HG22   H  N N 579 
THR HG23   H  N N 580 
THR HXT    H  N N 581 
TRP N      N  N N 582 
TRP CA     C  N S 583 
TRP C      C  N N 584 
TRP O      O  N N 585 
TRP CB     C  N N 586 
TRP CG     C  Y N 587 
TRP CD1    C  Y N 588 
TRP CD2    C  Y N 589 
TRP NE1    N  Y N 590 
TRP CE2    C  Y N 591 
TRP CE3    C  Y N 592 
TRP CZ2    C  Y N 593 
TRP CZ3    C  Y N 594 
TRP CH2    C  Y N 595 
TRP OXT    O  N N 596 
TRP H      H  N N 597 
TRP H2     H  N N 598 
TRP HA     H  N N 599 
TRP HB2    H  N N 600 
TRP HB3    H  N N 601 
TRP HD1    H  N N 602 
TRP HE1    H  N N 603 
TRP HE3    H  N N 604 
TRP HZ2    H  N N 605 
TRP HZ3    H  N N 606 
TRP HH2    H  N N 607 
TRP HXT    H  N N 608 
TYR N      N  N N 609 
TYR CA     C  N S 610 
TYR C      C  N N 611 
TYR O      O  N N 612 
TYR CB     C  N N 613 
TYR CG     C  Y N 614 
TYR CD1    C  Y N 615 
TYR CD2    C  Y N 616 
TYR CE1    C  Y N 617 
TYR CE2    C  Y N 618 
TYR CZ     C  Y N 619 
TYR OH     O  N N 620 
TYR OXT    O  N N 621 
TYR H      H  N N 622 
TYR H2     H  N N 623 
TYR HA     H  N N 624 
TYR HB2    H  N N 625 
TYR HB3    H  N N 626 
TYR HD1    H  N N 627 
TYR HD2    H  N N 628 
TYR HE1    H  N N 629 
TYR HE2    H  N N 630 
TYR HH     H  N N 631 
TYR HXT    H  N N 632 
VAL N      N  N N 633 
VAL CA     C  N S 634 
VAL C      C  N N 635 
VAL O      O  N N 636 
VAL CB     C  N N 637 
VAL CG1    C  N N 638 
VAL CG2    C  N N 639 
VAL OXT    O  N N 640 
VAL H      H  N N 641 
VAL H2     H  N N 642 
VAL HA     H  N N 643 
VAL HB     H  N N 644 
VAL HG11   H  N N 645 
VAL HG12   H  N N 646 
VAL HG13   H  N N 647 
VAL HG21   H  N N 648 
VAL HG22   H  N N 649 
VAL HG23   H  N N 650 
VAL HXT    H  N N 651 
# 
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 
53E C01   O10    sing N N 1   
53E C01   C02    sing N N 2   
53E C08   C07    doub Y N 3   
53E C08   C09    sing Y N 4   
53E O10   C09    sing N N 5   
53E C07   C06    sing Y N 6   
53E C09   C04    doub Y N 7   
53E C06   C05    doub Y N 8   
53E C04   C05    sing Y N 9   
53E C04   O03    sing N N 10  
53E O13   C11    doub N N 11  
53E C02   O03    sing N N 12  
53E C05   C11    sing N N 13  
53E C11   O12    sing N N 14  
53E C01   H1     sing N N 15  
53E C01   H2     sing N N 16  
53E C02   H3     sing N N 17  
53E C02   H4     sing N N 18  
53E C06   H5     sing N N 19  
53E C07   H6     sing N N 20  
53E C08   H7     sing N N 21  
53E O12   H8     sing N N 22  
ALA N     CA     sing N N 23  
ALA N     H      sing N N 24  
ALA N     H2     sing N N 25  
ALA CA    C      sing N N 26  
ALA CA    CB     sing N N 27  
ALA CA    HA     sing N N 28  
ALA C     O      doub N N 29  
ALA C     OXT    sing N N 30  
ALA CB    HB1    sing N N 31  
ALA CB    HB2    sing N N 32  
ALA CB    HB3    sing N N 33  
ALA OXT   HXT    sing N N 34  
ARG N     CA     sing N N 35  
ARG N     H      sing N N 36  
ARG N     H2     sing N N 37  
ARG CA    C      sing N N 38  
ARG CA    CB     sing N N 39  
ARG CA    HA     sing N N 40  
ARG C     O      doub N N 41  
ARG C     OXT    sing N N 42  
ARG CB    CG     sing N N 43  
ARG CB    HB2    sing N N 44  
ARG CB    HB3    sing N N 45  
ARG CG    CD     sing N N 46  
ARG CG    HG2    sing N N 47  
ARG CG    HG3    sing N N 48  
ARG CD    NE     sing N N 49  
ARG CD    HD2    sing N N 50  
ARG CD    HD3    sing N N 51  
ARG NE    CZ     sing N N 52  
ARG NE    HE     sing N N 53  
ARG CZ    NH1    sing N N 54  
ARG CZ    NH2    doub N N 55  
ARG NH1   HH11   sing N N 56  
ARG NH1   HH12   sing N N 57  
ARG NH2   HH21   sing N N 58  
ARG NH2   HH22   sing N N 59  
ARG OXT   HXT    sing N N 60  
ASN N     CA     sing N N 61  
ASN N     H      sing N N 62  
ASN N     H2     sing N N 63  
ASN CA    C      sing N N 64  
ASN CA    CB     sing N N 65  
ASN CA    HA     sing N N 66  
ASN C     O      doub N N 67  
ASN C     OXT    sing N N 68  
ASN CB    CG     sing N N 69  
ASN CB    HB2    sing N N 70  
ASN CB    HB3    sing N N 71  
ASN CG    OD1    doub N N 72  
ASN CG    ND2    sing N N 73  
ASN ND2   HD21   sing N N 74  
ASN ND2   HD22   sing N N 75  
ASN OXT   HXT    sing N N 76  
ASP N     CA     sing N N 77  
ASP N     H      sing N N 78  
ASP N     H2     sing N N 79  
ASP CA    C      sing N N 80  
ASP CA    CB     sing N N 81  
ASP CA    HA     sing N N 82  
ASP C     O      doub N N 83  
ASP C     OXT    sing N N 84  
ASP CB    CG     sing N N 85  
ASP CB    HB2    sing N N 86  
ASP CB    HB3    sing N N 87  
ASP CG    OD1    doub N N 88  
ASP CG    OD2    sing N N 89  
ASP OD2   HD2    sing N N 90  
ASP OXT   HXT    sing N N 91  
CYS N     CA     sing N N 92  
CYS N     H      sing N N 93  
CYS N     H2     sing N N 94  
CYS CA    C      sing N N 95  
CYS CA    CB     sing N N 96  
CYS CA    HA     sing N N 97  
CYS C     O      doub N N 98  
CYS C     OXT    sing N N 99  
CYS CB    SG     sing N N 100 
CYS CB    HB2    sing N N 101 
CYS CB    HB3    sing N N 102 
CYS SG    HG     sing N N 103 
CYS OXT   HXT    sing N N 104 
FAD PA    O1A    doub N N 105 
FAD PA    O2A    sing N N 106 
FAD PA    O5B    sing N N 107 
FAD PA    O3P    sing N N 108 
FAD O2A   HOA2   sing N N 109 
FAD O5B   C5B    sing N N 110 
FAD C5B   C4B    sing N N 111 
FAD C5B   H51A   sing N N 112 
FAD C5B   H52A   sing N N 113 
FAD C4B   O4B    sing N N 114 
FAD C4B   C3B    sing N N 115 
FAD C4B   H4B    sing N N 116 
FAD O4B   C1B    sing N N 117 
FAD C3B   O3B    sing N N 118 
FAD C3B   C2B    sing N N 119 
FAD C3B   H3B    sing N N 120 
FAD O3B   HO3A   sing N N 121 
FAD C2B   O2B    sing N N 122 
FAD C2B   C1B    sing N N 123 
FAD C2B   H2B    sing N N 124 
FAD O2B   HO2A   sing N N 125 
FAD C1B   N9A    sing N N 126 
FAD C1B   H1B    sing N N 127 
FAD N9A   C8A    sing Y N 128 
FAD N9A   C4A    sing Y N 129 
FAD C8A   N7A    doub Y N 130 
FAD C8A   H8A    sing N N 131 
FAD N7A   C5A    sing Y N 132 
FAD C5A   C6A    sing Y N 133 
FAD C5A   C4A    doub Y N 134 
FAD C6A   N6A    sing N N 135 
FAD C6A   N1A    doub Y N 136 
FAD N6A   H61A   sing N N 137 
FAD N6A   H62A   sing N N 138 
FAD N1A   C2A    sing Y N 139 
FAD C2A   N3A    doub Y N 140 
FAD C2A   H2A    sing N N 141 
FAD N3A   C4A    sing Y N 142 
FAD N1    C2     sing N N 143 
FAD N1    C10    doub N N 144 
FAD C2    O2     doub N N 145 
FAD C2    N3     sing N N 146 
FAD N3    C4     sing N N 147 
FAD N3    HN3    sing N N 148 
FAD C4    O4     doub N N 149 
FAD C4    C4X    sing N N 150 
FAD C4X   N5     doub N N 151 
FAD C4X   C10    sing N N 152 
FAD N5    C5X    sing N N 153 
FAD C5X   C6     doub Y N 154 
FAD C5X   C9A    sing Y N 155 
FAD C6    C7     sing Y N 156 
FAD C6    H6     sing N N 157 
FAD C7    C7M    sing N N 158 
FAD C7    C8     doub Y N 159 
FAD C7M   HM71   sing N N 160 
FAD C7M   HM72   sing N N 161 
FAD C7M   HM73   sing N N 162 
FAD C8    C8M    sing N N 163 
FAD C8    C9     sing Y N 164 
FAD C8M   HM81   sing N N 165 
FAD C8M   HM82   sing N N 166 
FAD C8M   HM83   sing N N 167 
FAD C9    C9A    doub Y N 168 
FAD C9    H9     sing N N 169 
FAD C9A   N10    sing N N 170 
FAD N10   C10    sing N N 171 
FAD N10   "C1'"  sing N N 172 
FAD "C1'" "C2'"  sing N N 173 
FAD "C1'" "H1'1" sing N N 174 
FAD "C1'" "H1'2" sing N N 175 
FAD "C2'" "O2'"  sing N N 176 
FAD "C2'" "C3'"  sing N N 177 
FAD "C2'" "H2'"  sing N N 178 
FAD "O2'" "HO2'" sing N N 179 
FAD "C3'" "O3'"  sing N N 180 
FAD "C3'" "C4'"  sing N N 181 
FAD "C3'" "H3'"  sing N N 182 
FAD "O3'" "HO3'" sing N N 183 
FAD "C4'" "O4'"  sing N N 184 
FAD "C4'" "C5'"  sing N N 185 
FAD "C4'" "H4'"  sing N N 186 
FAD "O4'" "HO4'" sing N N 187 
FAD "C5'" "O5'"  sing N N 188 
FAD "C5'" "H5'1" sing N N 189 
FAD "C5'" "H5'2" sing N N 190 
FAD "O5'" P      sing N N 191 
FAD P     O1P    doub N N 192 
FAD P     O2P    sing N N 193 
FAD P     O3P    sing N N 194 
FAD O2P   HOP2   sing N N 195 
FMT C     O1     doub N N 196 
FMT C     O2     sing N N 197 
FMT C     H      sing N N 198 
FMT O2    HO2    sing N N 199 
GLN N     CA     sing N N 200 
GLN N     H      sing N N 201 
GLN N     H2     sing N N 202 
GLN CA    C      sing N N 203 
GLN CA    CB     sing N N 204 
GLN CA    HA     sing N N 205 
GLN C     O      doub N N 206 
GLN C     OXT    sing N N 207 
GLN CB    CG     sing N N 208 
GLN CB    HB2    sing N N 209 
GLN CB    HB3    sing N N 210 
GLN CG    CD     sing N N 211 
GLN CG    HG2    sing N N 212 
GLN CG    HG3    sing N N 213 
GLN CD    OE1    doub N N 214 
GLN CD    NE2    sing N N 215 
GLN NE2   HE21   sing N N 216 
GLN NE2   HE22   sing N N 217 
GLN OXT   HXT    sing N N 218 
GLU N     CA     sing N N 219 
GLU N     H      sing N N 220 
GLU N     H2     sing N N 221 
GLU CA    C      sing N N 222 
GLU CA    CB     sing N N 223 
GLU CA    HA     sing N N 224 
GLU C     O      doub N N 225 
GLU C     OXT    sing N N 226 
GLU CB    CG     sing N N 227 
GLU CB    HB2    sing N N 228 
GLU CB    HB3    sing N N 229 
GLU CG    CD     sing N N 230 
GLU CG    HG2    sing N N 231 
GLU CG    HG3    sing N N 232 
GLU CD    OE1    doub N N 233 
GLU CD    OE2    sing N N 234 
GLU OE2   HE2    sing N N 235 
GLU OXT   HXT    sing N N 236 
GLY N     CA     sing N N 237 
GLY N     H      sing N N 238 
GLY N     H2     sing N N 239 
GLY CA    C      sing N N 240 
GLY CA    HA2    sing N N 241 
GLY CA    HA3    sing N N 242 
GLY C     O      doub N N 243 
GLY C     OXT    sing N N 244 
GLY OXT   HXT    sing N N 245 
HIS N     CA     sing N N 246 
HIS N     H      sing N N 247 
HIS N     H2     sing N N 248 
HIS CA    C      sing N N 249 
HIS CA    CB     sing N N 250 
HIS CA    HA     sing N N 251 
HIS C     O      doub N N 252 
HIS C     OXT    sing N N 253 
HIS CB    CG     sing N N 254 
HIS CB    HB2    sing N N 255 
HIS CB    HB3    sing N N 256 
HIS CG    ND1    sing Y N 257 
HIS CG    CD2    doub Y N 258 
HIS ND1   CE1    doub Y N 259 
HIS ND1   HD1    sing N N 260 
HIS CD2   NE2    sing Y N 261 
HIS CD2   HD2    sing N N 262 
HIS CE1   NE2    sing Y N 263 
HIS CE1   HE1    sing N N 264 
HIS NE2   HE2    sing N N 265 
HIS OXT   HXT    sing N N 266 
HOH O     H1     sing N N 267 
HOH O     H2     sing N N 268 
ILE N     CA     sing N N 269 
ILE N     H      sing N N 270 
ILE N     H2     sing N N 271 
ILE CA    C      sing N N 272 
ILE CA    CB     sing N N 273 
ILE CA    HA     sing N N 274 
ILE C     O      doub N N 275 
ILE C     OXT    sing N N 276 
ILE CB    CG1    sing N N 277 
ILE CB    CG2    sing N N 278 
ILE CB    HB     sing N N 279 
ILE CG1   CD1    sing N N 280 
ILE CG1   HG12   sing N N 281 
ILE CG1   HG13   sing N N 282 
ILE CG2   HG21   sing N N 283 
ILE CG2   HG22   sing N N 284 
ILE CG2   HG23   sing N N 285 
ILE CD1   HD11   sing N N 286 
ILE CD1   HD12   sing N N 287 
ILE CD1   HD13   sing N N 288 
ILE OXT   HXT    sing N N 289 
LEU N     CA     sing N N 290 
LEU N     H      sing N N 291 
LEU N     H2     sing N N 292 
LEU CA    C      sing N N 293 
LEU CA    CB     sing N N 294 
LEU CA    HA     sing N N 295 
LEU C     O      doub N N 296 
LEU C     OXT    sing N N 297 
LEU CB    CG     sing N N 298 
LEU CB    HB2    sing N N 299 
LEU CB    HB3    sing N N 300 
LEU CG    CD1    sing N N 301 
LEU CG    CD2    sing N N 302 
LEU CG    HG     sing N N 303 
LEU CD1   HD11   sing N N 304 
LEU CD1   HD12   sing N N 305 
LEU CD1   HD13   sing N N 306 
LEU CD2   HD21   sing N N 307 
LEU CD2   HD22   sing N N 308 
LEU CD2   HD23   sing N N 309 
LEU OXT   HXT    sing N N 310 
LYS N     CA     sing N N 311 
LYS N     H      sing N N 312 
LYS N     H2     sing N N 313 
LYS CA    C      sing N N 314 
LYS CA    CB     sing N N 315 
LYS CA    HA     sing N N 316 
LYS C     O      doub N N 317 
LYS C     OXT    sing N N 318 
LYS CB    CG     sing N N 319 
LYS CB    HB2    sing N N 320 
LYS CB    HB3    sing N N 321 
LYS CG    CD     sing N N 322 
LYS CG    HG2    sing N N 323 
LYS CG    HG3    sing N N 324 
LYS CD    CE     sing N N 325 
LYS CD    HD2    sing N N 326 
LYS CD    HD3    sing N N 327 
LYS CE    NZ     sing N N 328 
LYS CE    HE2    sing N N 329 
LYS CE    HE3    sing N N 330 
LYS NZ    HZ1    sing N N 331 
LYS NZ    HZ2    sing N N 332 
LYS NZ    HZ3    sing N N 333 
LYS OXT   HXT    sing N N 334 
MET N     CA     sing N N 335 
MET N     H      sing N N 336 
MET N     H2     sing N N 337 
MET CA    C      sing N N 338 
MET CA    CB     sing N N 339 
MET CA    HA     sing N N 340 
MET C     O      doub N N 341 
MET C     OXT    sing N N 342 
MET CB    CG     sing N N 343 
MET CB    HB2    sing N N 344 
MET CB    HB3    sing N N 345 
MET CG    SD     sing N N 346 
MET CG    HG2    sing N N 347 
MET CG    HG3    sing N N 348 
MET SD    CE     sing N N 349 
MET CE    HE1    sing N N 350 
MET CE    HE2    sing N N 351 
MET CE    HE3    sing N N 352 
MET OXT   HXT    sing N N 353 
NAD PA    O1A    doub N N 354 
NAD PA    O2A    sing N N 355 
NAD PA    O5B    sing N N 356 
NAD PA    O3     sing N N 357 
NAD O2A   HOA2   sing N N 358 
NAD O5B   C5B    sing N N 359 
NAD C5B   C4B    sing N N 360 
NAD C5B   H51A   sing N N 361 
NAD C5B   H52A   sing N N 362 
NAD C4B   O4B    sing N N 363 
NAD C4B   C3B    sing N N 364 
NAD C4B   H4B    sing N N 365 
NAD O4B   C1B    sing N N 366 
NAD C3B   O3B    sing N N 367 
NAD C3B   C2B    sing N N 368 
NAD C3B   H3B    sing N N 369 
NAD O3B   HO3A   sing N N 370 
NAD C2B   O2B    sing N N 371 
NAD C2B   C1B    sing N N 372 
NAD C2B   H2B    sing N N 373 
NAD O2B   HO2A   sing N N 374 
NAD C1B   N9A    sing N N 375 
NAD C1B   H1B    sing N N 376 
NAD N9A   C8A    sing Y N 377 
NAD N9A   C4A    sing Y N 378 
NAD C8A   N7A    doub Y N 379 
NAD C8A   H8A    sing N N 380 
NAD N7A   C5A    sing Y N 381 
NAD C5A   C6A    sing Y N 382 
NAD C5A   C4A    doub Y N 383 
NAD C6A   N6A    sing N N 384 
NAD C6A   N1A    doub Y N 385 
NAD N6A   H61A   sing N N 386 
NAD N6A   H62A   sing N N 387 
NAD N1A   C2A    sing Y N 388 
NAD C2A   N3A    doub Y N 389 
NAD C2A   H2A    sing N N 390 
NAD N3A   C4A    sing Y N 391 
NAD O3    PN     sing N N 392 
NAD PN    O1N    doub N N 393 
NAD PN    O2N    sing N N 394 
NAD PN    O5D    sing N N 395 
NAD O5D   C5D    sing N N 396 
NAD C5D   C4D    sing N N 397 
NAD C5D   H51N   sing N N 398 
NAD C5D   H52N   sing N N 399 
NAD C4D   O4D    sing N N 400 
NAD C4D   C3D    sing N N 401 
NAD C4D   H4D    sing N N 402 
NAD O4D   C1D    sing N N 403 
NAD C3D   O3D    sing N N 404 
NAD C3D   C2D    sing N N 405 
NAD C3D   H3D    sing N N 406 
NAD O3D   HO3N   sing N N 407 
NAD C2D   O2D    sing N N 408 
NAD C2D   C1D    sing N N 409 
NAD C2D   H2D    sing N N 410 
NAD O2D   HO2N   sing N N 411 
NAD C1D   N1N    sing N N 412 
NAD C1D   H1D    sing N N 413 
NAD N1N   C2N    sing Y N 414 
NAD N1N   C6N    doub Y N 415 
NAD C2N   C3N    doub Y N 416 
NAD C2N   H2N    sing N N 417 
NAD C3N   C7N    sing N N 418 
NAD C3N   C4N    sing Y N 419 
NAD C7N   O7N    doub N N 420 
NAD C7N   N7N    sing N N 421 
NAD N7N   H71N   sing N N 422 
NAD N7N   H72N   sing N N 423 
NAD C4N   C5N    doub Y N 424 
NAD C4N   H4N    sing N N 425 
NAD C5N   C6N    sing Y N 426 
NAD C5N   H5N    sing N N 427 
NAD C6N   H6N    sing N N 428 
PEG C1    O1     sing N N 429 
PEG C1    C2     sing N N 430 
PEG C1    H11    sing N N 431 
PEG C1    H12    sing N N 432 
PEG O1    HO1    sing N N 433 
PEG C2    O2     sing N N 434 
PEG C2    H21    sing N N 435 
PEG C2    H22    sing N N 436 
PEG O2    C3     sing N N 437 
PEG C3    C4     sing N N 438 
PEG C3    H31    sing N N 439 
PEG C3    H32    sing N N 440 
PEG C4    O4     sing N N 441 
PEG C4    H41    sing N N 442 
PEG C4    H42    sing N N 443 
PEG O4    HO4    sing N N 444 
PG4 O1    C1     sing N N 445 
PG4 O1    HO1    sing N N 446 
PG4 C1    C2     sing N N 447 
PG4 C1    H11    sing N N 448 
PG4 C1    H12    sing N N 449 
PG4 C2    O2     sing N N 450 
PG4 C2    H21    sing N N 451 
PG4 C2    H22    sing N N 452 
PG4 O2    C3     sing N N 453 
PG4 C3    C4     sing N N 454 
PG4 C3    H31    sing N N 455 
PG4 C3    H32    sing N N 456 
PG4 C4    O3     sing N N 457 
PG4 C4    H41    sing N N 458 
PG4 C4    H42    sing N N 459 
PG4 O3    C5     sing N N 460 
PG4 C5    C6     sing N N 461 
PG4 C5    H51    sing N N 462 
PG4 C5    H52    sing N N 463 
PG4 C6    O4     sing N N 464 
PG4 C6    H61    sing N N 465 
PG4 C6    H62    sing N N 466 
PG4 O4    C7     sing N N 467 
PG4 C7    C8     sing N N 468 
PG4 C7    H71    sing N N 469 
PG4 C7    H72    sing N N 470 
PG4 C8    O5     sing N N 471 
PG4 C8    H81    sing N N 472 
PG4 C8    H82    sing N N 473 
PG4 O5    HO5    sing N N 474 
PGE C1    O1     sing N N 475 
PGE C1    C2     sing N N 476 
PGE C1    H1     sing N N 477 
PGE C1    H12    sing N N 478 
PGE O1    HO1    sing N N 479 
PGE C2    O2     sing N N 480 
PGE C2    H2     sing N N 481 
PGE C2    H22    sing N N 482 
PGE O2    C3     sing N N 483 
PGE C3    C4     sing N N 484 
PGE C3    H3     sing N N 485 
PGE C3    H32    sing N N 486 
PGE C4    O3     sing N N 487 
PGE C4    H4     sing N N 488 
PGE C4    H42    sing N N 489 
PGE O4    C6     sing N N 490 
PGE O4    HO4    sing N N 491 
PGE C6    C5     sing N N 492 
PGE C6    H6     sing N N 493 
PGE C6    H62    sing N N 494 
PGE C5    O3     sing N N 495 
PGE C5    H5     sing N N 496 
PGE C5    H52    sing N N 497 
PHE N     CA     sing N N 498 
PHE N     H      sing N N 499 
PHE N     H2     sing N N 500 
PHE CA    C      sing N N 501 
PHE CA    CB     sing N N 502 
PHE CA    HA     sing N N 503 
PHE C     O      doub N N 504 
PHE C     OXT    sing N N 505 
PHE CB    CG     sing N N 506 
PHE CB    HB2    sing N N 507 
PHE CB    HB3    sing N N 508 
PHE CG    CD1    doub Y N 509 
PHE CG    CD2    sing Y N 510 
PHE CD1   CE1    sing Y N 511 
PHE CD1   HD1    sing N N 512 
PHE CD2   CE2    doub Y N 513 
PHE CD2   HD2    sing N N 514 
PHE CE1   CZ     doub Y N 515 
PHE CE1   HE1    sing N N 516 
PHE CE2   CZ     sing Y N 517 
PHE CE2   HE2    sing N N 518 
PHE CZ    HZ     sing N N 519 
PHE OXT   HXT    sing N N 520 
PRO N     CA     sing N N 521 
PRO N     CD     sing N N 522 
PRO N     H      sing N N 523 
PRO CA    C      sing N N 524 
PRO CA    CB     sing N N 525 
PRO CA    HA     sing N N 526 
PRO C     O      doub N N 527 
PRO C     OXT    sing N N 528 
PRO CB    CG     sing N N 529 
PRO CB    HB2    sing N N 530 
PRO CB    HB3    sing N N 531 
PRO CG    CD     sing N N 532 
PRO CG    HG2    sing N N 533 
PRO CG    HG3    sing N N 534 
PRO CD    HD2    sing N N 535 
PRO CD    HD3    sing N N 536 
PRO OXT   HXT    sing N N 537 
SER N     CA     sing N N 538 
SER N     H      sing N N 539 
SER N     H2     sing N N 540 
SER CA    C      sing N N 541 
SER CA    CB     sing N N 542 
SER CA    HA     sing N N 543 
SER C     O      doub N N 544 
SER C     OXT    sing N N 545 
SER CB    OG     sing N N 546 
SER CB    HB2    sing N N 547 
SER CB    HB3    sing N N 548 
SER OG    HG     sing N N 549 
SER OXT   HXT    sing N N 550 
SO4 S     O1     doub N N 551 
SO4 S     O2     doub N N 552 
SO4 S     O3     sing N N 553 
SO4 S     O4     sing N N 554 
THR N     CA     sing N N 555 
THR N     H      sing N N 556 
THR N     H2     sing N N 557 
THR CA    C      sing N N 558 
THR CA    CB     sing N N 559 
THR CA    HA     sing N N 560 
THR C     O      doub N N 561 
THR C     OXT    sing N N 562 
THR CB    OG1    sing N N 563 
THR CB    CG2    sing N N 564 
THR CB    HB     sing N N 565 
THR OG1   HG1    sing N N 566 
THR CG2   HG21   sing N N 567 
THR CG2   HG22   sing N N 568 
THR CG2   HG23   sing N N 569 
THR OXT   HXT    sing N N 570 
TRP N     CA     sing N N 571 
TRP N     H      sing N N 572 
TRP N     H2     sing N N 573 
TRP CA    C      sing N N 574 
TRP CA    CB     sing N N 575 
TRP CA    HA     sing N N 576 
TRP C     O      doub N N 577 
TRP C     OXT    sing N N 578 
TRP CB    CG     sing N N 579 
TRP CB    HB2    sing N N 580 
TRP CB    HB3    sing N N 581 
TRP CG    CD1    doub Y N 582 
TRP CG    CD2    sing Y N 583 
TRP CD1   NE1    sing Y N 584 
TRP CD1   HD1    sing N N 585 
TRP CD2   CE2    doub Y N 586 
TRP CD2   CE3    sing Y N 587 
TRP NE1   CE2    sing Y N 588 
TRP NE1   HE1    sing N N 589 
TRP CE2   CZ2    sing Y N 590 
TRP CE3   CZ3    doub Y N 591 
TRP CE3   HE3    sing N N 592 
TRP CZ2   CH2    doub Y N 593 
TRP CZ2   HZ2    sing N N 594 
TRP CZ3   CH2    sing Y N 595 
TRP CZ3   HZ3    sing N N 596 
TRP CH2   HH2    sing N N 597 
TRP OXT   HXT    sing N N 598 
TYR N     CA     sing N N 599 
TYR N     H      sing N N 600 
TYR N     H2     sing N N 601 
TYR CA    C      sing N N 602 
TYR CA    CB     sing N N 603 
TYR CA    HA     sing N N 604 
TYR C     O      doub N N 605 
TYR C     OXT    sing N N 606 
TYR CB    CG     sing N N 607 
TYR CB    HB2    sing N N 608 
TYR CB    HB3    sing N N 609 
TYR CG    CD1    doub Y N 610 
TYR CG    CD2    sing Y N 611 
TYR CD1   CE1    sing Y N 612 
TYR CD1   HD1    sing N N 613 
TYR CD2   CE2    doub Y N 614 
TYR CD2   HD2    sing N N 615 
TYR CE1   CZ     doub Y N 616 
TYR CE1   HE1    sing N N 617 
TYR CE2   CZ     sing Y N 618 
TYR CE2   HE2    sing N N 619 
TYR CZ    OH     sing N N 620 
TYR OH    HH     sing N N 621 
TYR OXT   HXT    sing N N 622 
VAL N     CA     sing N N 623 
VAL N     H      sing N N 624 
VAL N     H2     sing N N 625 
VAL CA    C      sing N N 626 
VAL CA    CB     sing N N 627 
VAL CA    HA     sing N N 628 
VAL C     O      doub N N 629 
VAL C     OXT    sing N N 630 
VAL CB    CG1    sing N N 631 
VAL CB    CG2    sing N N 632 
VAL CB    HB     sing N N 633 
VAL CG1   HG11   sing N N 634 
VAL CG1   HG12   sing N N 635 
VAL CG1   HG13   sing N N 636 
VAL CG2   HG21   sing N N 637 
VAL CG2   HG22   sing N N 638 
VAL CG2   HG23   sing N N 639 
VAL OXT   HXT    sing N N 640 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           1R01GM132640 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6X9A 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9DL2 
_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]   0.009961 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002900 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009831 
_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]   0.008247 
_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   ? -49.303 93.684  103.919 1.00 44.41 ? 14   ALA A N     1 
ATOM   2     C  CA    . ALA A  1  16   ? -48.198 92.730  104.004 1.00 47.54 ? 14   ALA A CA    1 
ATOM   3     C  C     . ALA A  1  16   ? -48.729 91.310  104.147 1.00 44.71 ? 14   ALA A C     1 
ATOM   4     O  O     . ALA A  1  16   ? -49.408 90.998  105.120 1.00 47.40 ? 14   ALA A O     1 
ATOM   5     C  CB    . ALA A  1  16   ? -47.282 93.075  105.168 1.00 51.18 ? 14   ALA A CB    1 
ATOM   6     N  N     . PRO A  1  17   ? -48.418 90.450  103.177 1.00 45.62 ? 15   PRO A N     1 
ATOM   7     C  CA    . PRO A  1  17   ? -48.936 89.077  103.221 1.00 37.53 ? 15   PRO A CA    1 
ATOM   8     C  C     . PRO A  1  17   ? -48.466 88.349  104.471 1.00 40.88 ? 15   PRO A C     1 
ATOM   9     O  O     . PRO A  1  17   ? -47.312 88.474  104.890 1.00 37.78 ? 15   PRO A O     1 
ATOM   10    C  CB    . PRO A  1  17   ? -48.365 88.439  101.950 1.00 41.55 ? 15   PRO A CB    1 
ATOM   11    C  CG    . PRO A  1  17   ? -48.042 89.600  101.052 1.00 45.26 ? 15   PRO A CG    1 
ATOM   12    C  CD    . PRO A  1  17   ? -47.616 90.704  101.970 1.00 41.29 ? 15   PRO A CD    1 
ATOM   13    N  N     . ALA A  1  18   ? -49.381 87.595  105.071 1.00 34.13 ? 16   ALA A N     1 
ATOM   14    C  CA    . ALA A  1  18   ? -49.052 86.854  106.275 1.00 31.84 ? 16   ALA A CA    1 
ATOM   15    C  C     . ALA A  1  18   ? -48.017 85.778  105.951 1.00 29.42 ? 16   ALA A C     1 
ATOM   16    O  O     . ALA A  1  18   ? -48.092 85.145  104.895 1.00 29.25 ? 16   ALA A O     1 
ATOM   17    C  CB    . ALA A  1  18   ? -50.307 86.222  106.875 1.00 33.84 ? 16   ALA A CB    1 
ATOM   18    N  N     . PRO A  1  19   ? -47.038 85.561  106.828 1.00 28.72 ? 17   PRO A N     1 
ATOM   19    C  CA    . PRO A  1  19   ? -45.979 84.588  106.531 1.00 25.93 ? 17   PRO A CA    1 
ATOM   20    C  C     . PRO A  1  19   ? -46.549 83.196  106.315 1.00 26.07 ? 17   PRO A C     1 
ATOM   21    O  O     . PRO A  1  19   ? -47.363 82.708  107.105 1.00 28.26 ? 17   PRO A O     1 
ATOM   22    C  CB    . PRO A  1  19   ? -45.084 84.649  107.776 1.00 29.04 ? 17   PRO A CB    1 
ATOM   23    C  CG    . PRO A  1  19   ? -45.336 85.999  108.356 1.00 31.30 ? 17   PRO A CG    1 
ATOM   24    C  CD    . PRO A  1  19   ? -46.796 86.276  108.093 1.00 28.31 ? 17   PRO A CD    1 
ATOM   25    N  N     . PHE A  1  20   ? -46.135 82.577  105.209 1.00 24.48 ? 18   PHE A N     1 
ATOM   26    C  CA    . PHE A  1  20   ? -46.460 81.205  104.833 1.00 25.69 ? 18   PHE A CA    1 
ATOM   27    C  C     . PHE A  1  20   ? -47.943 80.997  104.556 1.00 25.76 ? 18   PHE A C     1 
ATOM   28    O  O     . PHE A  1  20   ? -48.391 79.850  104.457 1.00 28.88 ? 18   PHE A O     1 
ATOM   29    C  CB    . PHE A  1  20   ? -45.982 80.209  105.896 1.00 25.91 ? 18   PHE A CB    1 
ATOM   30    C  CG    . PHE A  1  20   ? -44.512 80.288  106.178 1.00 24.02 ? 18   PHE A CG    1 
ATOM   31    C  CD1   . PHE A  1  20   ? -43.602 79.738  105.297 1.00 23.92 ? 18   PHE A CD1   1 
ATOM   32    C  CD2   . PHE A  1  20   ? -44.040 80.909  107.328 1.00 24.71 ? 18   PHE A CD2   1 
ATOM   33    C  CE1   . PHE A  1  20   ? -42.247 79.801  105.545 1.00 26.90 ? 18   PHE A CE1   1 
ATOM   34    C  CE2   . PHE A  1  20   ? -42.675 80.975  107.587 1.00 27.01 ? 18   PHE A CE2   1 
ATOM   35    C  CZ    . PHE A  1  20   ? -41.783 80.425  106.694 1.00 26.23 ? 18   PHE A CZ    1 
ATOM   36    N  N     . ALA A  1  21   ? -48.715 82.073  104.406 1.00 31.09 ? 19   ALA A N     1 
ATOM   37    C  CA    . ALA A  1  21   ? -50.135 81.928  104.099 1.00 30.95 ? 19   ALA A CA    1 
ATOM   38    C  C     . ALA A  1  21   ? -50.370 81.287  102.737 1.00 30.83 ? 19   ALA A C     1 
ATOM   39    O  O     . ALA A  1  21   ? -51.441 80.720  102.507 1.00 36.23 ? 19   ALA A O     1 
ATOM   40    C  CB    . ALA A  1  21   ? -50.823 83.295  104.164 1.00 34.62 ? 19   ALA A CB    1 
ATOM   41    N  N     . ASP A  1  22   ? -49.393 81.356  101.838 1.00 27.05 ? 20   ASP A N     1 
ATOM   42    C  CA    . ASP A  1  22   ? -49.496 80.814  100.489 1.00 33.41 ? 20   ASP A CA    1 
ATOM   43    C  C     . ASP A  1  22   ? -48.278 79.962  100.173 1.00 24.80 ? 20   ASP A C     1 
ATOM   44    O  O     . ASP A  1  22   ? -47.739 79.992  99.060  1.00 25.49 ? 20   ASP A O     1 
ATOM   45    C  CB    . ASP A  1  22   ? -49.655 81.934  99.466  1.00 32.13 ? 20   ASP A CB    1 
ATOM   46    C  CG    . ASP A  1  22   ? -50.995 82.633  99.579  1.00 45.89 ? 20   ASP A CG    1 
ATOM   47    O  OD1   . ASP A  1  22   ? -52.033 81.944  99.470  1.00 58.72 ? 20   ASP A OD1   1 
ATOM   48    O  OD2   . ASP A  1  22   ? -51.010 83.863  99.795  1.00 52.87 ? 20   ASP A OD2   1 
ATOM   49    N  N     . PHE A  1  23   ? -47.823 79.194  101.163 1.00 23.00 ? 21   PHE A N     1 
ATOM   50    C  CA    . PHE A  1  23   ? -46.554 78.489  101.027 1.00 21.03 ? 21   PHE A CA    1 
ATOM   51    C  C     . PHE A  1  23   ? -46.609 77.465  99.899  1.00 21.14 ? 21   PHE A C     1 
ATOM   52    O  O     . PHE A  1  23   ? -45.800 77.506  98.966  1.00 21.93 ? 21   PHE A O     1 
ATOM   53    C  CB    . PHE A  1  23   ? -46.170 77.817  102.349 1.00 22.18 ? 21   PHE A CB    1 
ATOM   54    C  CG    . PHE A  1  23   ? -44.958 76.946  102.222 1.00 20.23 ? 21   PHE A CG    1 
ATOM   55    C  CD1   . PHE A  1  23   ? -43.734 77.503  101.898 1.00 23.12 ? 21   PHE A CD1   1 
ATOM   56    C  CD2   . PHE A  1  23   ? -45.046 75.575  102.391 1.00 24.10 ? 21   PHE A CD2   1 
ATOM   57    C  CE1   . PHE A  1  23   ? -42.606 76.710  101.741 1.00 21.80 ? 21   PHE A CE1   1 
ATOM   58    C  CE2   . PHE A  1  23   ? -43.919 74.776  102.241 1.00 24.44 ? 21   PHE A CE2   1 
ATOM   59    C  CZ    . PHE A  1  23   ? -42.698 75.353  101.914 1.00 23.04 ? 21   PHE A CZ    1 
ATOM   60    N  N     . ALA A  1  24   ? -47.574 76.547  99.956  1.00 21.19 ? 22   ALA A N     1 
ATOM   61    C  CA    . ALA A  1  24   ? -47.614 75.483  98.960  1.00 21.71 ? 22   ALA A CA    1 
ATOM   62    C  C     . ALA A  1  24   ? -49.011 74.895  98.834  1.00 22.28 ? 22   ALA A C     1 
ATOM   63    O  O     . ALA A  1  24   ? -49.187 73.676  98.976  1.00 21.78 ? 22   ALA A O     1 
ATOM   64    C  CB    . ALA A  1  24   ? -46.614 74.381  99.316  1.00 24.56 ? 22   ALA A CB    1 
ATOM   65    N  N     . PRO A  1  25   ? -50.023 75.707  98.544  1.00 22.49 ? 23   PRO A N     1 
ATOM   66    C  CA    . PRO A  1  25   ? -51.379 75.171  98.424  1.00 23.35 ? 23   PRO A CA    1 
ATOM   67    C  C     . PRO A  1  25   ? -51.456 74.178  97.281  1.00 23.06 ? 23   PRO A C     1 
ATOM   68    O  O     . PRO A  1  25   ? -50.899 74.419  96.202  1.00 21.87 ? 23   PRO A O     1 
ATOM   69    C  CB    . PRO A  1  25   ? -52.226 76.420  98.140  1.00 29.10 ? 23   PRO A CB    1 
ATOM   70    C  CG    . PRO A  1  25   ? -51.287 77.334  97.439  1.00 26.32 ? 23   PRO A CG    1 
ATOM   71    C  CD    . PRO A  1  25   ? -49.954 77.117  98.118  1.00 27.46 ? 23   PRO A CD    1 
ATOM   72    N  N     . PRO A  1  26   ? -52.122 73.050  97.481  1.00 24.46 ? 24   PRO A N     1 
ATOM   73    C  CA    . PRO A  1  26   ? -52.248 72.065  96.400  1.00 24.11 ? 24   PRO A CA    1 
ATOM   74    C  C     . PRO A  1  26   ? -53.076 72.608  95.244  1.00 23.84 ? 24   PRO A C     1 
ATOM   75    O  O     . PRO A  1  26   ? -53.855 73.552  95.390  1.00 22.15 ? 24   PRO A O     1 
ATOM   76    C  CB    . PRO A  1  26   ? -52.946 70.883  97.079  1.00 25.40 ? 24   PRO A CB    1 
ATOM   77    C  CG    . PRO A  1  26   ? -53.707 71.515  98.232  1.00 27.44 ? 24   PRO A CG    1 
ATOM   78    C  CD    . PRO A  1  26   ? -52.835 72.650  98.704  1.00 24.75 ? 24   PRO A CD    1 
ATOM   79    N  N     . VAL A  1  27   ? -52.874 71.995  94.068  1.00 20.11 ? 25   VAL A N     1 
ATOM   80    C  CA    . VAL A  1  27   ? -53.645 72.362  92.881  1.00 21.64 ? 25   VAL A CA    1 
ATOM   81    C  C     . VAL A  1  27   ? -55.136 72.260  93.153  1.00 24.94 ? 25   VAL A C     1 
ATOM   82    O  O     . VAL A  1  27   ? -55.920 73.113  92.726  1.00 25.04 ? 25   VAL A O     1 
ATOM   83    C  CB    . VAL A  1  27   ? -53.227 71.476  91.691  1.00 22.82 ? 25   VAL A CB    1 
ATOM   84    C  CG1   . VAL A  1  27   ? -54.106 71.744  90.487  1.00 23.34 ? 25   VAL A CG1   1 
ATOM   85    C  CG2   . VAL A  1  27   ? -51.783 71.724  91.354  1.00 22.66 ? 25   VAL A CG2   1 
ATOM   86    N  N     . ARG A  1  28   ? -55.547 71.231  93.883  1.00 24.79 ? 26   ARG A N     1 
ATOM   87    C  CA    . ARG A  1  28   ? -56.947 70.983  94.189  1.00 29.85 ? 26   ARG A CA    1 
ATOM   88    C  C     . ARG A  1  28   ? -57.009 70.271  95.529  1.00 29.73 ? 26   ARG A C     1 
ATOM   89    O  O     . ARG A  1  28   ? -56.010 69.689  95.971  1.00 24.86 ? 26   ARG A O     1 
ATOM   90    C  CB    . ARG A  1  28   ? -57.607 70.129  93.099  1.00 30.10 ? 26   ARG A CB    1 
ATOM   91    C  CG    . ARG A  1  28   ? -57.119 68.685  93.102  1.00 32.89 ? 26   ARG A CG    1 
ATOM   92    C  CD    . ARG A  1  28   ? -57.694 67.876  91.942  1.00 37.26 ? 26   ARG A CD    1 
ATOM   93    N  NE    . ARG A  1  28   ? -57.003 68.159  90.688  1.00 39.92 ? 26   ARG A NE    1 
ATOM   94    C  CZ    . ARG A  1  28   ? -57.449 68.998  89.764  1.00 41.59 ? 26   ARG A CZ    1 
ATOM   95    N  NH1   . ARG A  1  28   ? -58.615 69.615  89.893  1.00 38.74 ? 26   ARG A NH1   1 
ATOM   96    N  NH2   . ARG A  1  28   ? -56.706 69.230  88.689  1.00 34.93 ? 26   ARG A NH2   1 
ATOM   97    N  N     . PRO A  1  29   ? -58.157 70.306  96.210  1.00 23.92 ? 27   PRO A N     1 
ATOM   98    C  CA    . PRO A  1  29   ? -58.293 69.504  97.427  1.00 29.04 ? 27   PRO A CA    1 
ATOM   99    C  C     . PRO A  1  29   ? -58.071 68.035  97.109  1.00 24.63 ? 27   PRO A C     1 
ATOM   100   O  O     . PRO A  1  29   ? -58.531 67.522  96.088  1.00 27.20 ? 27   PRO A O     1 
ATOM   101   C  CB    . PRO A  1  29   ? -59.731 69.782  97.884  1.00 29.81 ? 27   PRO A CB    1 
ATOM   102   C  CG    . PRO A  1  29   ? -60.037 71.126  97.321  1.00 30.57 ? 27   PRO A CG    1 
ATOM   103   C  CD    . PRO A  1  29   ? -59.349 71.142  95.974  1.00 27.58 ? 27   PRO A CD    1 
ATOM   104   N  N     . GLN A  1  30   ? -57.345 67.362  97.990  1.00 26.39 ? 28   GLN A N     1 
ATOM   105   C  CA    . GLN A  1  30   ? -56.948 65.986  97.737  1.00 29.01 ? 28   GLN A CA    1 
ATOM   106   C  C     . GLN A  1  30   ? -58.110 65.050  98.058  1.00 27.70 ? 28   GLN A C     1 
ATOM   107   O  O     . GLN A  1  30   ? -58.547 64.962  99.211  1.00 30.69 ? 28   GLN A O     1 
ATOM   108   C  CB    . GLN A  1  30   ? -55.712 65.644  98.564  1.00 27.05 ? 28   GLN A CB    1 
ATOM   109   C  CG    . GLN A  1  30   ? -54.534 66.571  98.287  1.00 23.51 ? 28   GLN A CG    1 
ATOM   110   C  CD    . GLN A  1  30   ? -54.004 66.418  96.874  1.00 24.72 ? 28   GLN A CD    1 
ATOM   111   O  OE1   . GLN A  1  30   ? -53.288 65.466  96.575  1.00 24.10 ? 28   GLN A OE1   1 
ATOM   112   N  NE2   . GLN A  1  30   ? -54.362 67.342  95.997  1.00 24.84 ? 28   GLN A NE2   1 
ATOM   113   N  N     . SER A  1  31   ? -58.607 64.359  97.037  1.00 26.52 ? 29   SER A N     1 
ATOM   114   C  CA    . SER A  1  31   ? -59.676 63.382  97.208  1.00 24.19 ? 29   SER A CA    1 
ATOM   115   C  C     . SER A  1  31   ? -59.180 62.196  98.028  1.00 25.84 ? 29   SER A C     1 
ATOM   116   O  O     . SER A  1  31   ? -57.980 62.015  98.236  1.00 24.83 ? 29   SER A O     1 
ATOM   117   C  CB    . SER A  1  31   ? -60.167 62.897  95.850  1.00 23.84 ? 29   SER A CB    1 
ATOM   118   O  OG    . SER A  1  31   ? -59.188 62.038  95.282  1.00 23.95 ? 29   SER A OG    1 
ATOM   119   N  N     . THR A  1  32   ? -60.127 61.379  98.503  1.00 23.44 ? 30   THR A N     1 
ATOM   120   C  CA    . THR A  1  32   ? -59.755 60.151  99.196  1.00 22.78 ? 30   THR A CA    1 
ATOM   121   C  C     . THR A  1  32   ? -58.811 59.309  98.344  1.00 24.45 ? 30   THR A C     1 
ATOM   122   O  O     . THR A  1  32   ? -57.811 58.786  98.844  1.00 25.95 ? 30   THR A O     1 
ATOM   123   C  CB    . THR A  1  32   ? -61.009 59.355  99.562  1.00 26.52 ? 30   THR A CB    1 
ATOM   124   O  OG1   . THR A  1  32   ? -61.809 60.137  100.457 1.00 33.28 ? 30   THR A OG1   1 
ATOM   125   C  CG2   . THR A  1  32   ? -60.646 58.031  100.222 1.00 31.85 ? 30   THR A CG2   1 
ATOM   126   N  N     . LEU A  1  33   ? -59.104 59.188  97.047  1.00 23.96 ? 31   LEU A N     1 
ATOM   127   C  CA    . LEU A  1  33   ? -58.246 58.399  96.171  1.00 22.19 ? 31   LEU A CA    1 
ATOM   128   C  C     . LEU A  1  33   ? -56.872 59.038  96.003  1.00 23.22 ? 31   LEU A C     1 
ATOM   129   O  O     . LEU A  1  33   ? -55.861 58.331  95.954  1.00 21.48 ? 31   LEU A O     1 
ATOM   130   C  CB    . LEU A  1  33   ? -58.922 58.215  94.814  1.00 20.83 ? 31   LEU A CB    1 
ATOM   131   C  CG    . LEU A  1  33   ? -60.089 57.232  94.838  1.00 26.08 ? 31   LEU A CG    1 
ATOM   132   C  CD1   . LEU A  1  33   ? -60.890 57.353  93.560  1.00 25.47 ? 31   LEU A CD1   1 
ATOM   133   C  CD2   . LEU A  1  33   ? -59.581 55.807  95.038  1.00 29.37 ? 31   LEU A CD2   1 
ATOM   134   N  N     . ARG A  1  34   ? -56.812 60.367  95.882  1.00 20.95 ? 32   ARG A N     1 
ATOM   135   C  CA    . ARG A  1  34   ? -55.514 61.027  95.787  1.00 19.84 ? 32   ARG A CA    1 
ATOM   136   C  C     . ARG A  1  34   ? -54.725 60.867  97.076  1.00 21.31 ? 32   ARG A C     1 
ATOM   137   O  O     . ARG A  1  34   ? -53.513 60.653  97.038  1.00 22.39 ? 32   ARG A O     1 
ATOM   138   C  CB    . ARG A  1  34   ? -55.692 62.506  95.452  1.00 22.26 ? 32   ARG A CB    1 
ATOM   139   C  CG    . ARG A  1  34   ? -56.108 62.787  94.015  1.00 23.26 ? 32   ARG A CG    1 
ATOM   140   C  CD    . ARG A  1  34   ? -54.986 62.520  93.012  1.00 22.38 ? 32   ARG A CD    1 
ATOM   141   N  NE    . ARG A  1  34   ? -53.861 63.442  93.154  1.00 20.55 ? 32   ARG A NE    1 
ATOM   142   C  CZ    . ARG A  1  34   ? -53.772 64.615  92.543  1.00 22.90 ? 32   ARG A CZ    1 
ATOM   143   N  NH1   . ARG A  1  34   ? -54.733 65.055  91.735  1.00 24.06 ? 32   ARG A NH1   1 
ATOM   144   N  NH2   . ARG A  1  34   ? -52.692 65.365  92.737  1.00 23.93 ? 32   ARG A NH2   1 
ATOM   145   N  N     . ARG A  1  35   ? -55.398 60.949  98.227  1.00 21.11 ? 33   ARG A N     1 
ATOM   146   C  CA    . ARG A  1  35   ? -54.698 60.795  99.497  1.00 20.39 ? 33   ARG A CA    1 
ATOM   147   C  C     . ARG A  1  35   ? -54.127 59.395  99.669  1.00 22.34 ? 33   ARG A C     1 
ATOM   148   O  O     . ARG A  1  35   ? -53.067 59.235  100.290 1.00 22.54 ? 33   ARG A O     1 
ATOM   149   C  CB    . ARG A  1  35   ? -55.640 61.126  100.655 1.00 25.20 ? 33   ARG A CB    1 
ATOM   150   C  CG    . ARG A  1  35   ? -55.991 62.592  100.709 1.00 27.07 ? 33   ARG A CG    1 
ATOM   151   C  CD    . ARG A  1  35   ? -56.896 62.928  101.883 1.00 37.39 ? 33   ARG A CD    1 
ATOM   152   N  NE    . ARG A  1  35   ? -57.294 64.329  101.803 1.00 44.26 ? 33   ARG A NE    1 
ATOM   153   C  CZ    . ARG A  1  35   ? -56.558 65.341  102.246 1.00 53.90 ? 33   ARG A CZ    1 
ATOM   154   N  NH1   . ARG A  1  35   ? -55.403 65.139  102.859 1.00 56.76 ? 33   ARG A NH1   1 
ATOM   155   N  NH2   . ARG A  1  35   ? -56.990 66.587  102.064 1.00 53.21 ? 33   ARG A NH2   1 
ATOM   156   N  N     . ALA A  1  36   ? -54.808 58.375  99.136  1.00 20.29 ? 34   ALA A N     1 
ATOM   157   C  CA    . ALA A  1  36   ? -54.279 57.016  99.232  1.00 23.25 ? 34   ALA A CA    1 
ATOM   158   C  C     . ALA A  1  36   ? -53.019 56.859  98.398  1.00 20.73 ? 34   ALA A C     1 
ATOM   159   O  O     . ALA A  1  36   ? -52.127 56.082  98.754  1.00 24.16 ? 34   ALA A O     1 
ATOM   160   C  CB    . ALA A  1  36   ? -55.327 56.000  98.780  1.00 23.33 ? 34   ALA A CB    1 
ATOM   161   N  N     . ILE A  1  37   ? -52.937 57.583  97.286  1.00 21.19 ? 35   ILE A N     1 
ATOM   162   C  CA    . ILE A  1  37   ? -51.703 57.602  96.512  1.00 18.96 ? 35   ILE A CA    1 
ATOM   163   C  C     . ILE A  1  37   ? -50.574 58.188  97.343  1.00 20.57 ? 35   ILE A C     1 
ATOM   164   O  O     . ILE A  1  37   ? -49.522 57.566  97.523  1.00 20.03 ? 35   ILE A O     1 
ATOM   165   C  CB    . ILE A  1  37   ? -51.905 58.389  95.208  1.00 19.03 ? 35   ILE A CB    1 
ATOM   166   C  CG1   . ILE A  1  37   ? -52.903 57.675  94.303  1.00 19.82 ? 35   ILE A CG1   1 
ATOM   167   C  CG2   . ILE A  1  37   ? -50.568 58.597  94.502  1.00 16.37 ? 35   ILE A CG2   1 
ATOM   168   C  CD1   . ILE A  1  37   ? -53.403 58.553  93.146  1.00 19.90 ? 35   ILE A CD1   1 
ATOM   169   N  N     . THR A  1  38   ? -50.781 59.394  97.877  1.00 21.58 ? 36   THR A N     1 
ATOM   170   C  CA    . THR A  1  38   ? -49.719 60.059  98.625  1.00 20.93 ? 36   THR A CA    1 
ATOM   171   C  C     . THR A  1  38   ? -49.290 59.223  99.820  1.00 21.37 ? 36   THR A C     1 
ATOM   172   O  O     . THR A  1  38   ? -48.097 59.146  100.143 1.00 20.69 ? 36   THR A O     1 
ATOM   173   C  CB    . THR A  1  38   ? -50.196 61.434  99.072  1.00 20.69 ? 36   THR A CB    1 
ATOM   174   O  OG1   . THR A  1  38   ? -50.728 62.129  97.941  1.00 20.15 ? 36   THR A OG1   1 
ATOM   175   C  CG2   . THR A  1  38   ? -49.058 62.235  99.652  1.00 20.10 ? 36   THR A CG2   1 
ATOM   176   N  N     . ALA A  1  39   ? -50.250 58.551  100.458 1.00 21.17 ? 37   ALA A N     1 
ATOM   177   C  CA    . ALA A  1  39   ? -49.953 57.743  101.634 1.00 22.64 ? 37   ALA A CA    1 
ATOM   178   C  C     . ALA A  1  39   ? -48.974 56.619  101.326 1.00 24.03 ? 37   ALA A C     1 
ATOM   179   O  O     . ALA A  1  39   ? -48.250 56.164  102.222 1.00 24.80 ? 37   ALA A O     1 
ATOM   180   C  CB    . ALA A  1  39   ? -51.249 57.164  102.206 1.00 19.51 ? 37   ALA A CB    1 
ATOM   181   N  N     . ALA A  1  40   ? -48.938 56.157  100.078 1.00 21.80 ? 38   ALA A N     1 
ATOM   182   C  CA    . ALA A  1  40   ? -48.098 55.037  99.683  1.00 21.67 ? 38   ALA A CA    1 
ATOM   183   C  C     . ALA A  1  40   ? -46.737 55.464  99.157  1.00 20.92 ? 38   ALA A C     1 
ATOM   184   O  O     . ALA A  1  40   ? -45.925 54.592  98.833  1.00 20.48 ? 38   ALA A O     1 
ATOM   185   C  CB    . ALA A  1  40   ? -48.809 54.203  98.616  1.00 19.10 ? 38   ALA A CB    1 
ATOM   186   N  N     . TYR A  1  41   ? -46.475 56.774  99.091  1.00 19.73 ? 39   TYR A N     1 
ATOM   187   C  CA    . TYR A  1  41   ? -45.303 57.305  98.391  1.00 20.32 ? 39   TYR A CA    1 
ATOM   188   C  C     . TYR A  1  41   ? -44.027 56.561  98.776  1.00 21.04 ? 39   TYR A C     1 
ATOM   189   O  O     . TYR A  1  41   ? -43.296 56.069  97.910  1.00 21.21 ? 39   TYR A O     1 
ATOM   190   C  CB    . TYR A  1  41   ? -45.188 58.800  98.697  1.00 19.58 ? 39   TYR A CB    1 
ATOM   191   C  CG    . TYR A  1  41   ? -44.418 59.672  97.710  1.00 19.23 ? 39   TYR A CG    1 
ATOM   192   C  CD1   . TYR A  1  41   ? -43.350 59.184  96.968  1.00 17.26 ? 39   TYR A CD1   1 
ATOM   193   C  CD2   . TYR A  1  41   ? -44.764 61.005  97.552  1.00 21.31 ? 39   TYR A CD2   1 
ATOM   194   C  CE1   . TYR A  1  41   ? -42.651 60.012  96.104  1.00 18.46 ? 39   TYR A CE1   1 
ATOM   195   C  CE2   . TYR A  1  41   ? -44.082 61.831  96.693  1.00 21.18 ? 39   TYR A CE2   1 
ATOM   196   C  CZ    . TYR A  1  41   ? -43.031 61.332  95.963  1.00 18.13 ? 39   TYR A CZ    1 
ATOM   197   O  OH    . TYR A  1  41   ? -42.338 62.159  95.096  1.00 18.73 ? 39   TYR A OH    1 
ATOM   198   N  N     . ARG A  1  42   ? -43.752 56.449  100.076 1.00 23.01 ? 40   ARG A N     1 
ATOM   199   C  CA    . ARG A  1  42   ? -42.531 55.792  100.531 1.00 22.65 ? 40   ARG A CA    1 
ATOM   200   C  C     . ARG A  1  42   ? -42.850 54.675  101.514 1.00 20.68 ? 40   ARG A C     1 
ATOM   201   O  O     . ARG A  1  42   ? -42.083 54.419  102.449 1.00 24.67 ? 40   ARG A O     1 
ATOM   202   C  CB    . ARG A  1  42   ? -41.561 56.812  101.126 1.00 24.19 ? 40   ARG A CB    1 
ATOM   203   C  CG    . ARG A  1  42   ? -41.090 57.783  100.043 1.00 22.47 ? 40   ARG A CG    1 
ATOM   204   C  CD    . ARG A  1  42   ? -40.281 58.939  100.532 1.00 24.95 ? 40   ARG A CD    1 
ATOM   205   N  NE    . ARG A  1  42   ? -40.298 59.955  99.486  1.00 21.94 ? 40   ARG A NE    1 
ATOM   206   C  CZ    . ARG A  1  42   ? -39.479 59.975  98.444  1.00 22.25 ? 40   ARG A CZ    1 
ATOM   207   N  NH1   . ARG A  1  42   ? -38.473 59.114  98.334  1.00 22.56 ? 40   ARG A NH1   1 
ATOM   208   N  NH2   . ARG A  1  42   ? -39.673 60.877  97.487  1.00 19.92 ? 40   ARG A NH2   1 
ATOM   209   N  N     . ARG A  1  43   ? -43.959 53.990  101.285 1.00 21.09 ? 41   ARG A N     1 
ATOM   210   C  CA    . ARG A  1  43   ? -44.390 52.921  102.179 1.00 21.73 ? 41   ARG A CA    1 
ATOM   211   C  C     . ARG A  1  43   ? -43.320 51.836  102.259 1.00 25.73 ? 41   ARG A C     1 
ATOM   212   O  O     . ARG A  1  43   ? -42.724 51.476  101.238 1.00 23.41 ? 41   ARG A O     1 
ATOM   213   C  CB    . ARG A  1  43   ? -45.707 52.330  101.677 1.00 23.12 ? 41   ARG A CB    1 
ATOM   214   C  CG    . ARG A  1  43   ? -46.212 51.123  102.449 1.00 23.31 ? 41   ARG A CG    1 
ATOM   215   C  CD    . ARG A  1  43   ? -47.636 50.849  102.043 1.00 25.98 ? 41   ARG A CD    1 
ATOM   216   N  NE    . ARG A  1  43   ? -48.485 51.981  102.397 1.00 27.19 ? 41   ARG A NE    1 
ATOM   217   C  CZ    . ARG A  1  43   ? -49.612 52.297  101.780 1.00 25.09 ? 41   ARG A CZ    1 
ATOM   218   N  NH1   . ARG A  1  43   ? -50.059 51.593  100.756 1.00 25.88 ? 41   ARG A NH1   1 
ATOM   219   N  NH2   . ARG A  1  43   ? -50.310 53.346  102.204 1.00 25.11 ? 41   ARG A NH2   1 
ATOM   220   N  N     . PRO A  1  44   ? -43.044 51.301  103.447 1.00 25.02 ? 42   PRO A N     1 
ATOM   221   C  CA    . PRO A  1  44   ? -42.047 50.232  103.561 1.00 27.00 ? 42   PRO A CA    1 
ATOM   222   C  C     . PRO A  1  44   ? -42.330 49.100  102.585 1.00 23.79 ? 42   PRO A C     1 
ATOM   223   O  O     . PRO A  1  44   ? -43.480 48.719  102.352 1.00 24.72 ? 42   PRO A O     1 
ATOM   224   C  CB    . PRO A  1  44   ? -42.186 49.772  105.017 1.00 27.50 ? 42   PRO A CB    1 
ATOM   225   C  CG    . PRO A  1  44   ? -42.654 50.986  105.742 1.00 29.12 ? 42   PRO A CG    1 
ATOM   226   C  CD    . PRO A  1  44   ? -43.544 51.741  104.761 1.00 26.12 ? 42   PRO A CD    1 
ATOM   227   N  N     . GLU A  1  45   ? -41.255 48.581  101.990 1.00 25.42 ? 43   GLU A N     1 
ATOM   228   C  CA    . GLU A  1  45   ? -41.387 47.554  100.964 1.00 24.41 ? 43   GLU A CA    1 
ATOM   229   C  C     . GLU A  1  45   ? -42.090 46.309  101.502 1.00 25.98 ? 43   GLU A C     1 
ATOM   230   O  O     . GLU A  1  45   ? -42.860 45.659  100.783 1.00 27.95 ? 43   GLU A O     1 
ATOM   231   C  CB    . GLU A  1  45   ? -39.994 47.223  100.420 1.00 30.04 ? 43   GLU A CB    1 
ATOM   232   C  CG    . GLU A  1  45   ? -39.996 46.720  99.010  1.00 30.01 ? 43   GLU A CG    1 
ATOM   233   C  CD    . GLU A  1  45   ? -38.689 46.987  98.270  1.00 25.51 ? 43   GLU A CD    1 
ATOM   234   O  OE1   . GLU A  1  45   ? -37.797 47.712  98.783  1.00 23.32 ? 43   GLU A OE1   1 
ATOM   235   O  OE2   . GLU A  1  45   ? -38.567 46.442  97.163  1.00 22.53 ? 43   GLU A OE2   1 
ATOM   236   N  N     . THR A  1  46   ? -41.846 45.965  102.769 1.00 30.61 ? 44   THR A N     1 
ATOM   237   C  CA    . THR A  1  46   ? -42.520 44.815  103.370 1.00 30.91 ? 44   THR A CA    1 
ATOM   238   C  C     . THR A  1  46   ? -44.031 45.007  103.480 1.00 27.62 ? 44   THR A C     1 
ATOM   239   O  O     . THR A  1  46   ? -44.770 44.017  103.524 1.00 31.14 ? 44   THR A O     1 
ATOM   240   C  CB    . THR A  1  46   ? -41.946 44.524  104.759 1.00 26.38 ? 44   THR A CB    1 
ATOM   241   O  OG1   . THR A  1  46   ? -42.015 45.707  105.562 1.00 28.78 ? 44   THR A OG1   1 
ATOM   242   C  CG2   . THR A  1  46   ? -40.495 44.061  104.654 1.00 26.78 ? 44   THR A CG2   1 
ATOM   243   N  N     . GLU A  1  47   ? -44.510 46.253  103.529 1.00 25.16 ? 45   GLU A N     1 
ATOM   244   C  CA    . GLU A  1  47   ? -45.948 46.496  103.574 1.00 28.25 ? 45   GLU A CA    1 
ATOM   245   C  C     . GLU A  1  47   ? -46.572 46.518  102.186 1.00 25.16 ? 45   GLU A C     1 
ATOM   246   O  O     . GLU A  1  47   ? -47.751 46.179  102.036 1.00 28.44 ? 45   GLU A O     1 
ATOM   247   C  CB    . GLU A  1  47   ? -46.244 47.814  104.292 1.00 32.77 ? 45   GLU A CB    1 
ATOM   248   C  CG    . GLU A  1  47   ? -45.721 47.870  105.715 1.00 39.87 ? 45   GLU A CG    1 
ATOM   249   C  CD    . GLU A  1  47   ? -45.978 49.208  106.376 1.00 41.17 ? 45   GLU A CD    1 
ATOM   250   O  OE1   . GLU A  1  47   ? -46.823 49.971  105.866 1.00 40.81 ? 45   GLU A OE1   1 
ATOM   251   O  OE2   . GLU A  1  47   ? -45.337 49.492  107.410 1.00 52.82 ? 45   GLU A OE2   1 
ATOM   252   N  N     . CYS A  1  48   ? -45.802 46.906  101.167 1.00 24.57 ? 46   CYS A N     1 
ATOM   253   C  CA    . CYS A  1  48   ? -46.352 46.993  99.816  1.00 24.40 ? 46   CYS A CA    1 
ATOM   254   C  C     . CYS A  1  48   ? -46.608 45.619  99.216  1.00 20.73 ? 46   CYS A C     1 
ATOM   255   O  O     . CYS A  1  48   ? -47.579 45.433  98.476  1.00 23.71 ? 46   CYS A O     1 
ATOM   256   C  CB    . CYS A  1  48   ? -45.395 47.755  98.902  1.00 23.36 ? 46   CYS A CB    1 
ATOM   257   S  SG    . CYS A  1  48   ? -45.111 49.485  99.288  1.00 25.10 ? 46   CYS A SG    1 
ATOM   258   N  N     . LEU A  1  49   ? -45.715 44.655  99.472  1.00 24.70 ? 47   LEU A N     1 
ATOM   259   C  CA    . LEU A  1  49   ? -45.724 43.438  98.669  1.00 27.71 ? 47   LEU A CA    1 
ATOM   260   C  C     . LEU A  1  49   ? -46.888 42.482  98.939  1.00 25.85 ? 47   LEU A C     1 
ATOM   261   O  O     . LEU A  1  49   ? -47.438 41.933  97.977  1.00 26.73 ? 47   LEU A O     1 
ATOM   262   C  CB    . LEU A  1  49   ? -44.395 42.694  98.827  1.00 29.01 ? 47   LEU A CB    1 
ATOM   263   C  CG    . LEU A  1  49   ? -43.376 42.973  97.713  1.00 26.29 ? 47   LEU A CG    1 
ATOM   264   C  CD1   . LEU A  1  49   ? -43.903 42.480  96.378  1.00 26.53 ? 47   LEU A CD1   1 
ATOM   265   C  CD2   . LEU A  1  49   ? -43.016 44.452  97.632  1.00 23.77 ? 47   LEU A CD2   1 
ATOM   266   N  N     . PRO A  1  50   ? -47.296 42.235  100.185 1.00 29.18 ? 48   PRO A N     1 
ATOM   267   C  CA    . PRO A  1  50   ? -48.328 41.204  100.432 1.00 29.83 ? 48   PRO A CA    1 
ATOM   268   C  C     . PRO A  1  50   ? -49.598 41.432  99.625  1.00 25.68 ? 48   PRO A C     1 
ATOM   269   O  O     . PRO A  1  50   ? -50.078 40.488  98.976  1.00 32.14 ? 48   PRO A O     1 
ATOM   270   C  CB    . PRO A  1  50   ? -48.578 41.309  101.945 1.00 27.81 ? 48   PRO A CB    1 
ATOM   271   C  CG    . PRO A  1  50   ? -47.248 41.706  102.486 1.00 29.21 ? 48   PRO A CG    1 
ATOM   272   C  CD    . PRO A  1  50   ? -46.701 42.701  101.451 1.00 25.49 ? 48   PRO A CD    1 
ATOM   273   N  N     . PRO A  1  51   ? -50.184 42.641  99.609  1.00 24.64 ? 49   PRO A N     1 
ATOM   274   C  CA    . PRO A  1  51   ? -51.394 42.810  98.786  1.00 27.59 ? 49   PRO A CA    1 
ATOM   275   C  C     . PRO A  1  51   ? -51.132 42.634  97.301  1.00 24.76 ? 49   PRO A C     1 
ATOM   276   O  O     . PRO A  1  51   ? -52.039 42.217  96.566  1.00 28.34 ? 49   PRO A O     1 
ATOM   277   C  CB    . PRO A  1  51   ? -51.865 44.234  99.118  1.00 26.79 ? 49   PRO A CB    1 
ATOM   278   C  CG    . PRO A  1  51   ? -50.678 44.926  99.598  1.00 28.51 ? 49   PRO A CG    1 
ATOM   279   C  CD    . PRO A  1  51   ? -49.834 43.897  100.300 1.00 27.56 ? 49   PRO A CD    1 
ATOM   280   N  N     . LEU A  1  52   ? -49.920 42.949  96.834  1.00 25.58 ? 50   LEU A N     1 
ATOM   281   C  CA    . LEU A  1  52   ? -49.593 42.717  95.431  1.00 23.84 ? 50   LEU A CA    1 
ATOM   282   C  C     . LEU A  1  52   ? -49.475 41.227  95.142  1.00 24.99 ? 50   LEU A C     1 
ATOM   283   O  O     . LEU A  1  52   ? -49.968 40.745  94.116  1.00 24.91 ? 50   LEU A O     1 
ATOM   284   C  CB    . LEU A  1  52   ? -48.301 43.449  95.065  1.00 23.58 ? 50   LEU A CB    1 
ATOM   285   C  CG    . LEU A  1  52   ? -48.336 44.967  95.253  1.00 25.40 ? 50   LEU A CG    1 
ATOM   286   C  CD1   . LEU A  1  52   ? -46.919 45.538  95.122  1.00 23.45 ? 50   LEU A CD1   1 
ATOM   287   C  CD2   . LEU A  1  52   ? -49.263 45.611  94.238  1.00 26.91 ? 50   LEU A CD2   1 
ATOM   288   N  N     . VAL A  1  53   ? -48.820 40.485  96.037  1.00 27.32 ? 51   VAL A N     1 
ATOM   289   C  CA    . VAL A  1  53   ? -48.783 39.027  95.920  1.00 28.38 ? 51   VAL A CA    1 
ATOM   290   C  C     . VAL A  1  53   ? -50.196 38.461  95.814  1.00 28.70 ? 51   VAL A C     1 
ATOM   291   O  O     . VAL A  1  53   ? -50.488 37.623  94.950  1.00 27.06 ? 51   VAL A O     1 
ATOM   292   C  CB    . VAL A  1  53   ? -48.019 38.420  97.109  1.00 27.32 ? 51   VAL A CB    1 
ATOM   293   C  CG1   . VAL A  1  53   ? -48.170 36.914  97.116  1.00 28.94 ? 51   VAL A CG1   1 
ATOM   294   C  CG2   . VAL A  1  53   ? -46.553 38.803  97.038  1.00 26.76 ? 51   VAL A CG2   1 
ATOM   295   N  N     . GLU A  1  54   ? -51.102 38.921  96.680  1.00 27.37 ? 52   GLU A N     1 
ATOM   296   C  CA    . GLU A  1  54   ? -52.457 38.376  96.648  1.00 30.94 ? 52   GLU A CA    1 
ATOM   297   C  C     . GLU A  1  54   ? -53.160 38.723  95.344  1.00 27.71 ? 52   GLU A C     1 
ATOM   298   O  O     . GLU A  1  54   ? -53.817 37.869  94.737  1.00 30.75 ? 52   GLU A O     1 
ATOM   299   C  CB    . GLU A  1  54   ? -53.271 38.873  97.843  1.00 32.26 ? 52   GLU A CB    1 
ATOM   300   C  CG    . GLU A  1  54   ? -54.724 38.383  97.830  1.00 43.76 ? 52   GLU A CG    1 
ATOM   301   C  CD    . GLU A  1  54   ? -54.854 36.857  97.757  1.00 51.11 ? 52   GLU A CD    1 
ATOM   302   O  OE1   . GLU A  1  54   ? -54.029 36.145  98.371  1.00 46.78 ? 52   GLU A OE1   1 
ATOM   303   O  OE2   . GLU A  1  54   ? -55.787 36.367  97.081  1.00 50.09 ? 52   GLU A OE2   1 
ATOM   304   N  N     . ALA A  1  55   ? -53.007 39.968  94.881  1.00 26.40 ? 53   ALA A N     1 
ATOM   305   C  CA    . ALA A  1  55   ? -53.683 40.393  93.664  1.00 25.93 ? 53   ALA A CA    1 
ATOM   306   C  C     . ALA A  1  55   ? -53.135 39.680  92.435  1.00 27.23 ? 53   ALA A C     1 
ATOM   307   O  O     . ALA A  1  55   ? -53.878 39.437  91.477  1.00 28.83 ? 53   ALA A O     1 
ATOM   308   C  CB    . ALA A  1  55   ? -53.544 41.905  93.503  1.00 25.52 ? 53   ALA A CB    1 
ATOM   309   N  N     . ALA A  1  56   ? -51.852 39.328  92.450  1.00 25.81 ? 54   ALA A N     1 
ATOM   310   C  CA    . ALA A  1  56   ? -51.200 38.688  91.316  1.00 25.08 ? 54   ALA A CA    1 
ATOM   311   C  C     . ALA A  1  56   ? -51.328 37.169  91.325  1.00 32.09 ? 54   ALA A C     1 
ATOM   312   O  O     . ALA A  1  56   ? -50.794 36.508  90.427  1.00 29.17 ? 54   ALA A O     1 
ATOM   313   C  CB    . ALA A  1  56   ? -49.717 39.065  91.287  1.00 24.61 ? 54   ALA A CB    1 
ATOM   314   N  N     . THR A  1  57   ? -52.013 36.600  92.308  1.00 30.35 ? 55   THR A N     1 
ATOM   315   C  CA    . THR A  1  57   ? -52.093 35.152  92.409  1.00 28.88 ? 55   THR A CA    1 
ATOM   316   C  C     . THR A  1  57   ? -53.021 34.603  91.336  1.00 32.01 ? 55   THR A C     1 
ATOM   317   O  O     . THR A  1  57   ? -54.059 35.196  91.029  1.00 32.21 ? 55   THR A O     1 
ATOM   318   C  CB    . THR A  1  57   ? -52.570 34.767  93.809  1.00 30.00 ? 55   THR A CB    1 
ATOM   319   O  OG1   . THR A  1  57   ? -51.561 35.138  94.757  1.00 31.61 ? 55   THR A OG1   1 
ATOM   320   C  CG2   . THR A  1  57   ? -52.840 33.266  93.921  1.00 34.63 ? 55   THR A CG2   1 
ATOM   321   N  N     . GLN A  1  58   ? -52.622 33.483  90.730  1.00 30.41 ? 56   GLN A N     1 
ATOM   322   C  CA    . GLN A  1  58   ? -53.441 32.808  89.737  1.00 30.49 ? 56   GLN A CA    1 
ATOM   323   C  C     . GLN A  1  58   ? -53.473 31.317  90.049  1.00 27.45 ? 56   GLN A C     1 
ATOM   324   O  O     . GLN A  1  58   ? -52.650 30.808  90.808  1.00 31.62 ? 56   GLN A O     1 
ATOM   325   C  CB    . GLN A  1  58   ? -52.925 33.050  88.313  1.00 30.45 ? 56   GLN A CB    1 
ATOM   326   C  CG    . GLN A  1  58   ? -52.794 34.521  87.962  1.00 28.04 ? 56   GLN A CG    1 
ATOM   327   C  CD    . GLN A  1  58   ? -52.668 34.759  86.471  1.00 28.23 ? 56   GLN A CD    1 
ATOM   328   O  OE1   . GLN A  1  58   ? -53.656 34.694  85.740  1.00 30.52 ? 56   GLN A OE1   1 
ATOM   329   N  NE2   . GLN A  1  58   ? -51.452 35.036  86.010  1.00 29.98 ? 56   GLN A NE2   1 
ATOM   330   N  N     . SER A  1  59   ? -54.442 30.630  89.451  1.00 33.13 ? 57   SER A N     1 
ATOM   331   C  CA    . SER A  1  59   ? -54.625 29.206  89.693  1.00 28.56 ? 57   SER A CA    1 
ATOM   332   C  C     . SER A  1  59   ? -53.391 28.426  89.258  1.00 35.58 ? 57   SER A C     1 
ATOM   333   O  O     . SER A  1  59   ? -52.607 28.867  88.409  1.00 35.58 ? 57   SER A O     1 
ATOM   334   C  CB    . SER A  1  59   ? -55.846 28.688  88.943  1.00 31.60 ? 57   SER A CB    1 
ATOM   335   O  OG    . SER A  1  59   ? -55.645 28.761  87.538  1.00 35.04 ? 57   SER A OG    1 
ATOM   336   N  N     . LYS A  1  60   ? -53.221 27.246  89.859  1.00 32.87 ? 58   LYS A N     1 
ATOM   337   C  CA    . LYS A  1  60   ? -52.123 26.375  89.456  1.00 36.99 ? 58   LYS A CA    1 
ATOM   338   C  C     . LYS A  1  60   ? -52.205 26.056  87.969  1.00 34.46 ? 58   LYS A C     1 
ATOM   339   O  O     . LYS A  1  60   ? -51.183 26.024  87.274  1.00 36.83 ? 58   LYS A O     1 
ATOM   340   C  CB    . LYS A  1  60   ? -52.136 25.094  90.300  1.00 33.54 ? 58   LYS A CB    1 
ATOM   341   C  CG    . LYS A  1  60   ? -51.159 24.016  89.848  1.00 38.23 ? 58   LYS A CG    1 
ATOM   342   C  CD    . LYS A  1  60   ? -49.714 24.420  90.049  1.00 43.21 ? 58   LYS A CD    1 
ATOM   343   C  CE    . LYS A  1  60   ? -48.776 23.255  89.737  1.00 42.85 ? 58   LYS A CE    1 
ATOM   344   N  NZ    . LYS A  1  60   ? -47.346 23.633  89.916  1.00 43.86 ? 58   LYS A NZ    1 
ATOM   345   N  N     . GLU A  1  61   ? -53.420 25.844  87.458  1.00 33.81 ? 59   GLU A N     1 
ATOM   346   C  CA    . GLU A  1  61   ? -53.592 25.564  86.036  1.00 36.40 ? 59   GLU A CA    1 
ATOM   347   C  C     . GLU A  1  61   ? -53.102 26.726  85.178  1.00 36.91 ? 59   GLU A C     1 
ATOM   348   O  O     . GLU A  1  61   ? -52.454 26.518  84.147  1.00 36.17 ? 59   GLU A O     1 
ATOM   349   C  CB    . GLU A  1  61   ? -55.059 25.261  85.736  1.00 34.27 ? 59   GLU A CB    1 
ATOM   350   N  N     . ILE A  1  62   ? -53.409 27.959  85.583  1.00 32.85 ? 60   ILE A N     1 
ATOM   351   C  CA    . ILE A  1  62   ? -52.980 29.112  84.797  1.00 32.14 ? 60   ILE A CA    1 
ATOM   352   C  C     . ILE A  1  62   ? -51.473 29.287  84.886  1.00 35.06 ? 60   ILE A C     1 
ATOM   353   O  O     . ILE A  1  62   ? -50.810 29.598  83.889  1.00 33.38 ? 60   ILE A O     1 
ATOM   354   C  CB    . ILE A  1  62   ? -53.729 30.378  85.245  1.00 33.08 ? 60   ILE A CB    1 
ATOM   355   C  CG1   . ILE A  1  62   ? -55.097 30.424  84.574  1.00 36.13 ? 60   ILE A CG1   1 
ATOM   356   C  CG2   . ILE A  1  62   ? -52.925 31.635  84.908  1.00 34.36 ? 60   ILE A CG2   1 
ATOM   357   C  CD1   . ILE A  1  62   ? -55.922 31.584  84.991  1.00 34.93 ? 60   ILE A CD1   1 
ATOM   358   N  N     . ARG A  1  63   ? -50.904 29.085  86.075  1.00 32.94 ? 61   ARG A N     1 
ATOM   359   C  CA    . ARG A  1  63   ? -49.464 29.236  86.228  1.00 35.49 ? 61   ARG A CA    1 
ATOM   360   C  C     . ARG A  1  63   ? -48.715 28.221  85.380  1.00 33.01 ? 61   ARG A C     1 
ATOM   361   O  O     . ARG A  1  63   ? -47.675 28.541  84.792  1.00 30.66 ? 61   ARG A O     1 
ATOM   362   C  CB    . ARG A  1  63   ? -49.081 29.123  87.700  1.00 32.46 ? 61   ARG A CB    1 
ATOM   363   C  CG    . ARG A  1  63   ? -49.636 30.272  88.507  1.00 40.19 ? 61   ARG A CG    1 
ATOM   364   C  CD    . ARG A  1  63   ? -49.139 30.292  89.934  1.00 45.28 ? 61   ARG A CD    1 
ATOM   365   N  NE    . ARG A  1  63   ? -49.816 29.310  90.767  1.00 44.50 ? 61   ARG A NE    1 
ATOM   366   C  CZ    . ARG A  1  63   ? -49.219 28.258  91.306  1.00 49.59 ? 61   ARG A CZ    1 
ATOM   367   N  NH1   . ARG A  1  63   ? -47.930 28.028  91.122  1.00 48.98 ? 61   ARG A NH1   1 
ATOM   368   N  NH2   . ARG A  1  63   ? -49.931 27.423  92.056  1.00 45.59 ? 61   ARG A NH2   1 
ATOM   369   N  N     . ASP A  1  64   ? -49.237 26.998  85.283  1.00 37.14 ? 62   ASP A N     1 
ATOM   370   C  CA    . ASP A  1  64   ? -48.608 26.009  84.414  1.00 35.14 ? 62   ASP A CA    1 
ATOM   371   C  C     . ASP A  1  64   ? -48.760 26.392  82.947  1.00 35.68 ? 62   ASP A C     1 
ATOM   372   O  O     . ASP A  1  64   ? -47.803 26.282  82.171  1.00 35.29 ? 62   ASP A O     1 
ATOM   373   C  CB    . ASP A  1  64   ? -49.202 24.626  84.679  1.00 34.94 ? 62   ASP A CB    1 
ATOM   374   C  CG    . ASP A  1  64   ? -48.817 24.080  86.041  1.00 31.56 ? 62   ASP A CG    1 
ATOM   375   O  OD1   . ASP A  1  64   ? -47.971 24.696  86.717  1.00 43.58 ? 62   ASP A OD1   1 
ATOM   376   O  OD2   . ASP A  1  64   ? -49.358 23.022  86.430  1.00 40.20 ? 62   ASP A OD2   1 
ATOM   377   N  N     . ALA A  1  65   ? -49.954 26.844  82.549  1.00 32.17 ? 63   ALA A N     1 
ATOM   378   C  CA    . ALA A  1  65   ? -50.153 27.287  81.173  1.00 32.67 ? 63   ALA A CA    1 
ATOM   379   C  C     . ALA A  1  65   ? -49.258 28.474  80.843  1.00 33.98 ? 63   ALA A C     1 
ATOM   380   O  O     . ALA A  1  65   ? -48.681 28.541  79.749  1.00 34.66 ? 63   ALA A O     1 
ATOM   381   C  CB    . ALA A  1  65   ? -51.623 27.638  80.938  1.00 35.36 ? 63   ALA A CB    1 
ATOM   382   N  N     . ALA A  1  66   ? -49.116 29.417  81.782  1.00 30.88 ? 64   ALA A N     1 
ATOM   383   C  CA    . ALA A  1  66   ? -48.267 30.581  81.534  1.00 35.46 ? 64   ALA A CA    1 
ATOM   384   C  C     . ALA A  1  66   ? -46.800 30.186  81.412  1.00 34.18 ? 64   ALA A C     1 
ATOM   385   O  O     . ALA A  1  66   ? -46.085 30.697  80.540  1.00 32.37 ? 64   ALA A O     1 
ATOM   386   C  CB    . ALA A  1  66   ? -48.444 31.617  82.643  1.00 28.57 ? 64   ALA A CB    1 
ATOM   387   N  N     . ALA A  1  67   ? -46.330 29.289  82.282  1.00 31.35 ? 65   ALA A N     1 
ATOM   388   C  CA    . ALA A  1  67   ? -44.956 28.813  82.173  1.00 35.03 ? 65   ALA A CA    1 
ATOM   389   C  C     . ALA A  1  67   ? -44.721 28.138  80.828  1.00 34.14 ? 65   ALA A C     1 
ATOM   390   O  O     . ALA A  1  67   ? -43.665 28.315  80.208  1.00 35.12 ? 65   ALA A O     1 
ATOM   391   C  CB    . ALA A  1  67   ? -44.640 27.855  83.323  1.00 34.60 ? 65   ALA A CB    1 
ATOM   392   N  N     . SER A  1  68   ? -45.702 27.374  80.354  1.00 33.16 ? 66   SER A N     1 
ATOM   393   C  CA    . SER A  1  68   ? -45.555 26.710  79.066  1.00 35.75 ? 66   SER A CA    1 
ATOM   394   C  C     . SER A  1  68   ? -45.519 27.723  77.930  1.00 39.06 ? 66   SER A C     1 
ATOM   395   O  O     . SER A  1  68   ? -44.718 27.591  76.996  1.00 36.83 ? 66   SER A O     1 
ATOM   396   C  CB    . SER A  1  68   ? -46.686 25.703  78.864  1.00 40.50 ? 66   SER A CB    1 
ATOM   397   O  OG    . SER A  1  68   ? -46.680 25.200  77.545  1.00 47.74 ? 66   SER A OG    1 
ATOM   398   N  N     . THR A  1  69   ? -46.373 28.748  77.996  1.00 34.97 ? 67   THR A N     1 
ATOM   399   C  CA    . THR A  1  69   ? -46.349 29.790  76.977  1.00 32.78 ? 67   THR A CA    1 
ATOM   400   C  C     . THR A  1  69   ? -45.034 30.556  77.007  1.00 27.61 ? 67   THR A C     1 
ATOM   401   O  O     . THR A  1  69   ? -44.438 30.823  75.957  1.00 31.65 ? 67   THR A O     1 
ATOM   402   C  CB    . THR A  1  69   ? -47.528 30.740  77.172  1.00 33.24 ? 67   THR A CB    1 
ATOM   403   O  OG1   . THR A  1  69   ? -48.746 30.023  76.964  1.00 33.60 ? 67   THR A OG1   1 
ATOM   404   C  CG2   . THR A  1  69   ? -47.453 31.899  76.179  1.00 26.98 ? 67   THR A CG2   1 
ATOM   405   N  N     . ALA A  1  70   ? -44.571 30.929  78.204  1.00 31.24 ? 68   ALA A N     1 
ATOM   406   C  CA    . ALA A  1  70   ? -43.314 31.660  78.312  1.00 32.25 ? 68   ALA A CA    1 
ATOM   407   C  C     . ALA A  1  70   ? -42.157 30.830  77.783  1.00 32.21 ? 68   ALA A C     1 
ATOM   408   O  O     . ALA A  1  70   ? -41.270 31.352  77.098  1.00 34.97 ? 68   ALA A O     1 
ATOM   409   C  CB    . ALA A  1  70   ? -43.054 32.072  79.762  1.00 30.53 ? 68   ALA A CB    1 
ATOM   410   N  N     . ARG A  1  71   ? -42.148 29.529  78.089  1.00 32.57 ? 69   ARG A N     1 
ATOM   411   C  CA    . ARG A  1  71   ? -41.100 28.665  77.558  1.00 34.98 ? 69   ARG A CA    1 
ATOM   412   C  C     . ARG A  1  71   ? -41.142 28.631  76.036  1.00 34.69 ? 69   ARG A C     1 
ATOM   413   O  O     . ARG A  1  71   ? -40.100 28.730  75.376  1.00 37.60 ? 69   ARG A O     1 
ATOM   414   C  CB    . ARG A  1  71   ? -41.235 27.256  78.136  1.00 33.20 ? 69   ARG A CB    1 
ATOM   415   C  CG    . ARG A  1  71   ? -40.338 26.253  77.454  1.00 33.56 ? 69   ARG A CG    1 
ATOM   416   C  CD    . ARG A  1  71   ? -40.368 24.901  78.151  1.00 36.50 ? 69   ARG A CD    1 
ATOM   417   N  NE    . ARG A  1  71   ? -39.511 24.915  79.327  1.00 39.68 ? 69   ARG A NE    1 
ATOM   418   C  CZ    . ARG A  1  71   ? -38.189 24.843  79.283  1.00 39.76 ? 69   ARG A CZ    1 
ATOM   419   N  NH1   . ARG A  1  71   ? -37.540 24.722  78.135  1.00 42.97 ? 69   ARG A NH1   1 
ATOM   420   N  NH2   . ARG A  1  71   ? -37.499 24.907  80.418  1.00 44.39 ? 69   ARG A NH2   1 
ATOM   421   N  N     . LYS A  1  72   ? -42.341 28.521  75.462  1.00 31.61 ? 70   LYS A N     1 
ATOM   422   C  CA    . LYS A  1  72   ? -42.478 28.515  74.008  1.00 35.68 ? 70   LYS A CA    1 
ATOM   423   C  C     . LYS A  1  72   ? -41.964 29.814  73.394  1.00 37.86 ? 70   LYS A C     1 
ATOM   424   O  O     . LYS A  1  72   ? -41.258 29.792  72.380  1.00 34.12 ? 70   LYS A O     1 
ATOM   425   C  CB    . LYS A  1  72   ? -43.938 28.280  73.622  1.00 33.72 ? 70   LYS A CB    1 
ATOM   426   C  CG    . LYS A  1  72   ? -44.196 28.328  72.125  1.00 37.27 ? 70   LYS A CG    1 
ATOM   427   C  CD    . LYS A  1  72   ? -45.608 27.883  71.795  1.00 42.04 ? 70   LYS A CD    1 
ATOM   428   C  CE    . LYS A  1  72   ? -45.788 27.704  70.295  1.00 51.19 ? 70   LYS A CE    1 
ATOM   429   N  NZ    . LYS A  1  72   ? -47.077 27.030  69.953  1.00 61.86 ? 70   LYS A NZ    1 
ATOM   430   N  N     . LEU A  1  73   ? -42.310 30.956  73.994  1.00 32.41 ? 71   LEU A N     1 
ATOM   431   C  CA    . LEU A  1  73   ? -41.817 32.237  73.496  1.00 34.21 ? 71   LEU A CA    1 
ATOM   432   C  C     . LEU A  1  73   ? -40.304 32.342  73.624  1.00 33.50 ? 71   LEU A C     1 
ATOM   433   O  O     . LEU A  1  73   ? -39.635 32.882  72.736  1.00 35.32 ? 71   LEU A O     1 
ATOM   434   C  CB    . LEU A  1  73   ? -42.482 33.387  74.253  1.00 30.88 ? 71   LEU A CB    1 
ATOM   435   C  CG    . LEU A  1  73   ? -43.995 33.491  74.111  1.00 29.66 ? 71   LEU A CG    1 
ATOM   436   C  CD1   . LEU A  1  73   ? -44.552 34.533  75.077  1.00 30.31 ? 71   LEU A CD1   1 
ATOM   437   C  CD2   . LEU A  1  73   ? -44.355 33.846  72.692  1.00 36.32 ? 71   LEU A CD2   1 
ATOM   438   N  N     . ILE A  1  74   ? -39.748 31.847  74.731  1.00 28.77 ? 72   ILE A N     1 
ATOM   439   C  CA    . ILE A  1  74   ? -38.315 31.976  74.964  1.00 31.56 ? 72   ILE A CA    1 
ATOM   440   C  C     . ILE A  1  74   ? -37.538 31.035  74.054  1.00 34.39 ? 72   ILE A C     1 
ATOM   441   O  O     . ILE A  1  74   ? -36.459 31.382  73.558  1.00 33.98 ? 72   ILE A O     1 
ATOM   442   C  CB    . ILE A  1  74   ? -38.003 31.736  76.451  1.00 33.25 ? 72   ILE A CB    1 
ATOM   443   C  CG1   . ILE A  1  74   ? -38.535 32.915  77.277  1.00 36.11 ? 72   ILE A CG1   1 
ATOM   444   C  CG2   . ILE A  1  74   ? -36.505 31.555  76.676  1.00 33.49 ? 72   ILE A CG2   1 
ATOM   445   C  CD1   . ILE A  1  74   ? -38.609 32.640  78.762  1.00 32.54 ? 72   ILE A CD1   1 
ATOM   446   N  N     . GLU A  1  75   ? -38.069 29.836  73.812  1.00 37.82 ? 73   GLU A N     1 
ATOM   447   C  CA    . GLU A  1  75   ? -37.419 28.931  72.871  1.00 41.03 ? 73   GLU A CA    1 
ATOM   448   C  C     . GLU A  1  75   ? -37.399 29.523  71.467  1.00 39.18 ? 73   GLU A C     1 
ATOM   449   O  O     . GLU A  1  75   ? -36.388 29.433  70.764  1.00 38.15 ? 73   GLU A O     1 
ATOM   450   C  CB    . GLU A  1  75   ? -38.111 27.568  72.892  1.00 36.82 ? 73   GLU A CB    1 
ATOM   451   C  CG    . GLU A  1  75   ? -37.655 26.718  74.068  1.00 38.81 ? 73   GLU A CG    1 
ATOM   452   C  CD    . GLU A  1  75   ? -38.539 25.520  74.347  1.00 46.95 ? 73   GLU A CD    1 
ATOM   453   O  OE1   . GLU A  1  75   ? -39.589 25.367  73.681  1.00 48.82 ? 73   GLU A OE1   1 
ATOM   454   O  OE2   . GLU A  1  75   ? -38.175 24.732  75.249  1.00 40.31 ? 73   GLU A OE2   1 
ATOM   455   N  N     . ALA A  1  76   ? -38.497 30.157  71.048  1.00 40.29 ? 74   ALA A N     1 
ATOM   456   C  CA    . ALA A  1  76   ? -38.499 30.827  69.751  1.00 39.00 ? 74   ALA A CA    1 
ATOM   457   C  C     . ALA A  1  76   ? -37.503 31.980  69.728  1.00 40.23 ? 74   ALA A C     1 
ATOM   458   O  O     . ALA A  1  76   ? -36.795 32.178  68.734  1.00 45.42 ? 74   ALA A O     1 
ATOM   459   C  CB    . ALA A  1  76   ? -39.903 31.324  69.414  1.00 44.38 ? 74   ALA A CB    1 
ATOM   460   N  N     . LEU A  1  77   ? -37.434 32.750  70.816  1.00 39.08 ? 75   LEU A N     1 
ATOM   461   C  CA    . LEU A  1  77   ? -36.489 33.860  70.889  1.00 37.90 ? 75   LEU A CA    1 
ATOM   462   C  C     . LEU A  1  77   ? -35.052 33.370  70.779  1.00 41.72 ? 75   LEU A C     1 
ATOM   463   O  O     . LEU A  1  77   ? -34.245 33.931  70.029  1.00 43.82 ? 75   LEU A O     1 
ATOM   464   C  CB    . LEU A  1  77   ? -36.679 34.629  72.194  1.00 33.86 ? 75   LEU A CB    1 
ATOM   465   C  CG    . LEU A  1  77   ? -37.750 35.712  72.225  1.00 35.23 ? 75   LEU A CG    1 
ATOM   466   C  CD1   . LEU A  1  77   ? -37.693 36.451  73.548  1.00 35.58 ? 75   LEU A CD1   1 
ATOM   467   C  CD2   . LEU A  1  77   ? -37.534 36.655  71.063  1.00 35.56 ? 75   LEU A CD2   1 
ATOM   468   N  N     . ARG A  1  78   ? -34.706 32.332  71.539  1.00 34.54 ? 76   ARG A N     1 
ATOM   469   C  CA    . ARG A  1  78   ? -33.338 31.839  71.510  1.00 39.49 ? 76   ARG A CA    1 
ATOM   470   C  C     . ARG A  1  78   ? -33.040 31.054  70.244  1.00 39.37 ? 76   ARG A C     1 
ATOM   471   O  O     . ARG A  1  78   ? -31.866 30.851  69.920  1.00 43.96 ? 76   ARG A O     1 
ATOM   472   C  CB    . ARG A  1  78   ? -33.067 30.982  72.746  1.00 39.42 ? 76   ARG A CB    1 
ATOM   473   C  CG    . ARG A  1  78   ? -32.982 31.789  74.025  1.00 40.53 ? 76   ARG A CG    1 
ATOM   474   C  CD    . ARG A  1  78   ? -32.544 30.934  75.200  1.00 34.11 ? 76   ARG A CD    1 
ATOM   475   N  NE    . ARG A  1  78   ? -31.967 31.761  76.249  1.00 34.20 ? 76   ARG A NE    1 
ATOM   476   C  CZ    . ARG A  1  78   ? -31.599 31.319  77.443  1.00 33.90 ? 76   ARG A CZ    1 
ATOM   477   N  NH1   . ARG A  1  78   ? -31.754 30.052  77.791  1.00 35.19 ? 76   ARG A NH1   1 
ATOM   478   N  NH2   . ARG A  1  78   ? -31.063 32.173  78.312  1.00 34.78 ? 76   ARG A NH2   1 
ATOM   479   N  N     . GLY A  1  79   ? -34.069 30.627  69.518  1.00 42.60 ? 77   GLY A N     1 
ATOM   480   C  CA    . GLY A  1  79   ? -33.886 29.808  68.336  1.00 46.51 ? 77   GLY A CA    1 
ATOM   481   C  C     . GLY A  1  79   ? -33.653 30.593  67.062  1.00 54.74 ? 77   GLY A C     1 
ATOM   482   O  O     . GLY A  1  79   ? -33.088 30.064  66.101  1.00 54.95 ? 77   GLY A O     1 
ATOM   483   N  N     . LYS A  1  80   ? -34.089 31.851  67.031  1.00 54.90 ? 78   LYS A N     1 
ATOM   484   C  CA    . LYS A  1  80   ? -33.858 32.717  65.884  1.00 56.07 ? 78   LYS A CA    1 
ATOM   485   C  C     . LYS A  1  80   ? -32.789 33.769  66.144  1.00 52.20 ? 78   LYS A C     1 
ATOM   486   O  O     . LYS A  1  80   ? -32.481 34.556  65.242  1.00 55.66 ? 78   LYS A O     1 
ATOM   487   C  CB    . LYS A  1  80   ? -35.164 33.396  65.457  1.00 56.14 ? 78   LYS A CB    1 
ATOM   488   C  CG    . LYS A  1  80   ? -35.791 34.284  66.516  1.00 53.50 ? 78   LYS A CG    1 
ATOM   489   C  CD    . LYS A  1  80   ? -37.166 34.741  66.067  1.00 50.36 ? 78   LYS A CD    1 
ATOM   490   C  CE    . LYS A  1  80   ? -37.867 35.575  67.126  1.00 45.34 ? 78   LYS A CE    1 
ATOM   491   N  NZ    . LYS A  1  80   ? -39.276 35.871  66.717  1.00 39.69 ? 78   LYS A NZ    1 
ATOM   492   N  N     . HIS A  1  81   ? -32.213 33.797  67.343  1.00 48.74 ? 79   HIS A N     1 
ATOM   493   C  CA    . HIS A  1  81   ? -31.185 34.772  67.693  1.00 53.88 ? 79   HIS A CA    1 
ATOM   494   C  C     . HIS A  1  81   ? -29.933 34.606  66.833  1.00 60.82 ? 79   HIS A C     1 
ATOM   495   O  O     . HIS A  1  81   ? -29.503 35.543  66.157  1.00 63.07 ? 79   HIS A O     1 
ATOM   496   C  CB    . HIS A  1  81   ? -30.819 34.650  69.175  1.00 50.15 ? 79   HIS A CB    1 
ATOM   497   N  N     . SER A  1  84   ? -25.175 39.815  66.729  1.00 58.11 ? 82   SER A N     1 
ATOM   498   C  CA    . SER A  1  84   ? -25.435 41.229  66.474  1.00 54.24 ? 82   SER A CA    1 
ATOM   499   C  C     . SER A  1  84   ? -24.672 41.712  65.248  1.00 48.13 ? 82   SER A C     1 
ATOM   500   O  O     . SER A  1  84   ? -23.710 41.077  64.817  1.00 42.62 ? 82   SER A O     1 
ATOM   501   C  CB    . SER A  1  84   ? -25.051 42.080  67.690  1.00 49.27 ? 82   SER A CB    1 
ATOM   502   N  N     . GLY A  1  85   ? -25.119 42.837  64.686  1.00 46.12 ? 83   GLY A N     1 
ATOM   503   C  CA    . GLY A  1  85   ? -24.350 43.472  63.630  1.00 35.93 ? 83   GLY A CA    1 
ATOM   504   C  C     . GLY A  1  85   ? -22.987 43.924  64.117  1.00 35.64 ? 83   GLY A C     1 
ATOM   505   O  O     . GLY A  1  85   ? -21.967 43.674  63.470  1.00 35.18 ? 83   GLY A O     1 
ATOM   506   N  N     . VAL A  1  86   ? -22.953 44.598  65.273  1.00 38.34 ? 84   VAL A N     1 
ATOM   507   C  CA    . VAL A  1  86   ? -21.678 45.013  65.855  1.00 33.13 ? 84   VAL A CA    1 
ATOM   508   C  C     . VAL A  1  86   ? -20.842 43.796  66.217  1.00 34.10 ? 84   VAL A C     1 
ATOM   509   O  O     . VAL A  1  86   ? -19.616 43.803  66.067  1.00 31.30 ? 84   VAL A O     1 
ATOM   510   C  CB    . VAL A  1  86   ? -21.903 45.921  67.080  1.00 40.17 ? 84   VAL A CB    1 
ATOM   511   C  CG1   . VAL A  1  86   ? -22.406 47.285  66.650  1.00 38.47 ? 84   VAL A CG1   1 
ATOM   512   C  CG2   . VAL A  1  86   ? -22.875 45.274  68.056  1.00 39.53 ? 84   VAL A CG2   1 
ATOM   513   N  N     . GLU A  1  87   ? -21.489 42.730  66.694  1.00 37.19 ? 85   GLU A N     1 
ATOM   514   C  CA    . GLU A  1  87   ? -20.745 41.544  67.099  1.00 37.18 ? 85   GLU A CA    1 
ATOM   515   C  C     . GLU A  1  87   ? -20.094 40.871  65.900  1.00 39.18 ? 85   GLU A C     1 
ATOM   516   O  O     . GLU A  1  87   ? -18.953 40.402  65.989  1.00 37.57 ? 85   GLU A O     1 
ATOM   517   C  CB    . GLU A  1  87   ? -21.662 40.567  67.837  1.00 45.86 ? 85   GLU A CB    1 
ATOM   518   N  N     . GLY A  1  88   ? -20.796 40.821  64.767  1.00 36.50 ? 86   GLY A N     1 
ATOM   519   C  CA    . GLY A  1  88   ? -20.191 40.268  63.569  1.00 33.16 ? 86   GLY A CA    1 
ATOM   520   C  C     . GLY A  1  88   ? -19.088 41.147  63.017  1.00 34.04 ? 86   GLY A C     1 
ATOM   521   O  O     . GLY A  1  88   ? -18.129 40.651  62.420  1.00 33.75 ? 86   GLY A O     1 
ATOM   522   N  N     . LEU A  1  89   ? -19.208 42.460  63.209  1.00 33.70 ? 87   LEU A N     1 
ATOM   523   C  CA    . LEU A  1  89   ? -18.153 43.375  62.795  1.00 30.80 ? 87   LEU A CA    1 
ATOM   524   C  C     . LEU A  1  89   ? -16.909 43.186  63.656  1.00 28.23 ? 87   LEU A C     1 
ATOM   525   O  O     . LEU A  1  89   ? -15.796 43.047  63.136  1.00 28.72 ? 87   LEU A O     1 
ATOM   526   C  CB    . LEU A  1  89   ? -18.677 44.807  62.878  1.00 31.53 ? 87   LEU A CB    1 
ATOM   527   C  CG    . LEU A  1  89   ? -17.770 45.962  62.483  1.00 38.12 ? 87   LEU A CG    1 
ATOM   528   C  CD1   . LEU A  1  89   ? -17.292 45.766  61.071  1.00 42.48 ? 87   LEU A CD1   1 
ATOM   529   C  CD2   . LEU A  1  89   ? -18.535 47.270  62.626  1.00 36.76 ? 87   LEU A CD2   1 
ATOM   530   N  N     . VAL A  1  90   ? -17.088 43.169  64.981  1.00 28.93 ? 88   VAL A N     1 
ATOM   531   C  CA    . VAL A  1  90   ? -15.993 42.863  65.900  1.00 27.74 ? 88   VAL A CA    1 
ATOM   532   C  C     . VAL A  1  90   ? -15.319 41.551  65.527  1.00 32.32 ? 88   VAL A C     1 
ATOM   533   O  O     . VAL A  1  90   ? -14.086 41.438  65.544  1.00 28.52 ? 88   VAL A O     1 
ATOM   534   C  CB    . VAL A  1  90   ? -16.522 42.827  67.343  1.00 26.00 ? 88   VAL A CB    1 
ATOM   535   C  CG1   . VAL A  1  90   ? -15.504 42.184  68.271  1.00 28.56 ? 88   VAL A CG1   1 
ATOM   536   C  CG2   . VAL A  1  90   ? -16.881 44.225  67.815  1.00 29.09 ? 88   VAL A CG2   1 
ATOM   537   N  N     . GLN A  1  91   ? -16.116 40.534  65.190  1.00 32.65 ? 89   GLN A N     1 
ATOM   538   C  CA    . GLN A  1  91   ? -15.552 39.231  64.853  1.00 34.90 ? 89   GLN A CA    1 
ATOM   539   C  C     . GLN A  1  91   ? -14.805 39.266  63.524  1.00 33.26 ? 89   GLN A C     1 
ATOM   540   O  O     . GLN A  1  91   ? -13.705 38.713  63.410  1.00 35.34 ? 89   GLN A O     1 
ATOM   541   C  CB    . GLN A  1  91   ? -16.656 38.173  64.818  1.00 39.87 ? 89   GLN A CB    1 
ATOM   542   N  N     . GLU A  1  92   ? -15.382 39.908  62.505  1.00 31.78 ? 90   GLU A N     1 
ATOM   543   C  CA    . GLU A  1  92   ? -14.758 39.892  61.184  1.00 32.95 ? 90   GLU A CA    1 
ATOM   544   C  C     . GLU A  1  92   ? -13.380 40.541  61.208  1.00 31.89 ? 90   GLU A C     1 
ATOM   545   O  O     . GLU A  1  92   ? -12.448 40.070  60.545  1.00 31.73 ? 90   GLU A O     1 
ATOM   546   C  CB    . GLU A  1  92   ? -15.662 40.591  60.167  1.00 33.24 ? 90   GLU A CB    1 
ATOM   547   C  CG    . GLU A  1  92   ? -15.042 40.706  58.778  1.00 33.40 ? 90   GLU A CG    1 
ATOM   548   C  CD    . GLU A  1  92   ? -15.981 41.328  57.761  1.00 42.83 ? 90   GLU A CD    1 
ATOM   549   O  OE1   . GLU A  1  92   ? -17.122 41.680  58.136  1.00 44.01 ? 90   GLU A OE1   1 
ATOM   550   O  OE2   . GLU A  1  92   ? -15.573 41.463  56.585  1.00 39.40 ? 90   GLU A OE2   1 
ATOM   551   N  N     . TYR A  1  93   ? -13.224 41.616  61.977  1.00 29.21 ? 91   TYR A N     1 
ATOM   552   C  CA    . TYR A  1  93   ? -11.981 42.372  61.988  1.00 28.13 ? 91   TYR A CA    1 
ATOM   553   C  C     . TYR A  1  93   ? -11.178 42.159  63.261  1.00 26.10 ? 91   TYR A C     1 
ATOM   554   O  O     . TYR A  1  93   ? -10.196 42.880  63.492  1.00 27.03 ? 91   TYR A O     1 
ATOM   555   C  CB    . TYR A  1  93   ? -12.277 43.856  61.777  1.00 25.97 ? 91   TYR A CB    1 
ATOM   556   C  CG    . TYR A  1  93   ? -12.764 44.129  60.378  1.00 27.46 ? 91   TYR A CG    1 
ATOM   557   C  CD1   . TYR A  1  93   ? -11.860 44.289  59.326  1.00 27.01 ? 91   TYR A CD1   1 
ATOM   558   C  CD2   . TYR A  1  93   ? -14.122 44.197  60.098  1.00 30.29 ? 91   TYR A CD2   1 
ATOM   559   C  CE1   . TYR A  1  93   ? -12.302 44.518  58.041  1.00 29.80 ? 91   TYR A CE1   1 
ATOM   560   C  CE2   . TYR A  1  93   ? -14.568 44.428  58.810  1.00 32.38 ? 91   TYR A CE2   1 
ATOM   561   C  CZ    . TYR A  1  93   ? -13.652 44.595  57.793  1.00 31.24 ? 91   TYR A CZ    1 
ATOM   562   O  OH    . TYR A  1  93   ? -14.100 44.821  56.512  1.00 34.02 ? 91   TYR A OH    1 
ATOM   563   N  N     . SER A  1  94   ? -11.566 41.183  64.081  1.00 26.93 ? 92   SER A N     1 
ATOM   564   C  CA    . SER A  1  94   ? -10.829 40.832  65.295  1.00 26.70 ? 92   SER A CA    1 
ATOM   565   C  C     . SER A  1  94   ? -10.603 42.065  66.163  1.00 22.01 ? 92   SER A C     1 
ATOM   566   O  O     . SER A  1  94   ? -9.500  42.310  66.661  1.00 25.09 ? 92   SER A O     1 
ATOM   567   C  CB    . SER A  1  94   ? -9.502  40.149  64.955  1.00 31.70 ? 92   SER A CB    1 
ATOM   568   O  OG    . SER A  1  94   ? -9.709  39.093  64.021  1.00 32.72 ? 92   SER A OG    1 
ATOM   569   N  N     . LEU A  1  95   ? -11.656 42.860  66.320  1.00 20.98 ? 93   LEU A N     1 
ATOM   570   C  CA    . LEU A  1  95   ? -11.572 44.081  67.100  1.00 22.65 ? 93   LEU A CA    1 
ATOM   571   C  C     . LEU A  1  95   ? -11.584 43.764  68.582  1.00 23.31 ? 93   LEU A C     1 
ATOM   572   O  O     . LEU A  1  95   ? -12.344 42.910  69.040  1.00 22.93 ? 93   LEU A O     1 
ATOM   573   C  CB    . LEU A  1  95   ? -12.754 44.999  66.782  1.00 21.32 ? 93   LEU A CB    1 
ATOM   574   C  CG    . LEU A  1  95   ? -12.856 45.434  65.323  1.00 20.97 ? 93   LEU A CG    1 
ATOM   575   C  CD1   . LEU A  1  95   ? -13.969 46.463  65.168  1.00 22.95 ? 93   LEU A CD1   1 
ATOM   576   C  CD2   . LEU A  1  95   ? -11.521 45.977  64.819  1.00 22.49 ? 93   LEU A CD2   1 
ATOM   577   N  N     . SER A  1  96   ? -10.753 44.474  69.335  1.00 20.35 ? 94   SER A N     1 
ATOM   578   C  CA    . SER A  1  96   ? -10.949 44.536  70.771  1.00 20.25 ? 94   SER A CA    1 
ATOM   579   C  C     . SER A  1  96   ? -12.214 45.340  71.088  1.00 20.73 ? 94   SER A C     1 
ATOM   580   O  O     . SER A  1  96   ? -12.794 46.010  70.226  1.00 20.07 ? 94   SER A O     1 
ATOM   581   C  CB    . SER A  1  96   ? -9.751  45.200  71.438  1.00 22.72 ? 94   SER A CB    1 
ATOM   582   O  OG    . SER A  1  96   ? -9.740  46.576  71.097  1.00 20.49 ? 94   SER A OG    1 
ATOM   583   N  N     . SER A  1  97   ? -12.628 45.291  72.352  1.00 19.46 ? 95   SER A N     1 
ATOM   584   C  CA    . SER A  1  97   ? -13.787 46.075  72.770  1.00 22.19 ? 95   SER A CA    1 
ATOM   585   C  C     . SER A  1  97   ? -13.539 47.558  72.551  1.00 19.89 ? 95   SER A C     1 
ATOM   586   O  O     . SER A  1  97   ? -14.386 48.268  71.997  1.00 19.48 ? 95   SER A O     1 
ATOM   587   C  CB    . SER A  1  97   ? -14.117 45.801  74.238  1.00 26.27 ? 95   SER A CB    1 
ATOM   588   O  OG    . SER A  1  97   ? -14.719 44.529  74.361  1.00 34.88 ? 95   SER A OG    1 
ATOM   589   N  N     . GLN A  1  98   ? -12.367 48.041  72.966  1.00 18.09 ? 96   GLN A N     1 
ATOM   590   C  CA    . GLN A  1  98   ? -12.067 49.450  72.776  1.00 17.16 ? 96   GLN A CA    1 
ATOM   591   C  C     . GLN A  1  98   ? -12.025 49.816  71.297  1.00 16.97 ? 96   GLN A C     1 
ATOM   592   O  O     . GLN A  1  98   ? -12.432 50.918  70.925  1.00 17.33 ? 96   GLN A O     1 
ATOM   593   C  CB    . GLN A  1  98   ? -10.751 49.801  73.468  1.00 18.67 ? 96   GLN A CB    1 
ATOM   594   C  CG    . GLN A  1  98   ? -10.891 49.892  74.992  1.00 20.42 ? 96   GLN A CG    1 
ATOM   595   C  CD    . GLN A  1  98   ? -11.848 50.989  75.446  1.00 19.01 ? 96   GLN A CD    1 
ATOM   596   O  OE1   . GLN A  1  98   ? -13.072 50.815  75.441  1.00 20.64 ? 96   GLN A OE1   1 
ATOM   597   N  NE2   . GLN A  1  98   ? -11.293 52.127  75.841  1.00 21.85 ? 96   GLN A NE2   1 
ATOM   598   N  N     . GLU A  1  99   ? -11.513 48.925  70.443  1.00 18.46 ? 97   GLU A N     1 
ATOM   599   C  CA    . GLU A  1  99   ? -11.533 49.215  69.011  1.00 16.52 ? 97   GLU A CA    1 
ATOM   600   C  C     . GLU A  1  99   ? -12.955 49.268  68.479  1.00 17.17 ? 97   GLU A C     1 
ATOM   601   O  O     . GLU A  1  99   ? -13.285 50.135  67.662  1.00 18.82 ? 97   GLU A O     1 
ATOM   602   C  CB    . GLU A  1  99   ? -10.716 48.180  68.240  1.00 17.39 ? 97   GLU A CB    1 
ATOM   603   C  CG    . GLU A  1  99   ? -9.223  48.309  68.530  1.00 18.05 ? 97   GLU A CG    1 
ATOM   604   C  CD    . GLU A  1  99   ? -8.409  47.131  68.004  1.00 20.66 ? 97   GLU A CD    1 
ATOM   605   O  OE1   . GLU A  1  99   ? -9.007  46.115  67.576  1.00 20.55 ? 97   GLU A OE1   1 
ATOM   606   O  OE2   . GLU A  1  99   ? -7.165  47.222  68.048  1.00 21.66 ? 97   GLU A OE2   1 
ATOM   607   N  N     . GLY A  1  100  ? -13.808 48.343  68.912  1.00 18.40 ? 98   GLY A N     1 
ATOM   608   C  CA    . GLY A  1  100  ? -15.199 48.399  68.491  1.00 17.71 ? 98   GLY A CA    1 
ATOM   609   C  C     . GLY A  1  100  ? -15.859 49.708  68.883  1.00 20.29 ? 98   GLY A C     1 
ATOM   610   O  O     . GLY A  1  100  ? -16.537 50.344  68.075  1.00 19.53 ? 98   GLY A O     1 
ATOM   611   N  N     . VAL A  1  101  ? -15.662 50.131  70.136  1.00 18.05 ? 99   VAL A N     1 
ATOM   612   C  CA    . VAL A  1  101  ? -16.209 51.408  70.585  1.00 19.26 ? 99   VAL A CA    1 
ATOM   613   C  C     . VAL A  1  101  ? -15.642 52.559  69.764  1.00 18.87 ? 99   VAL A C     1 
ATOM   614   O  O     . VAL A  1  101  ? -16.386 53.422  69.279  1.00 18.88 ? 99   VAL A O     1 
ATOM   615   C  CB    . VAL A  1  101  ? -15.932 51.611  72.080  1.00 16.87 ? 99   VAL A CB    1 
ATOM   616   C  CG1   . VAL A  1  101  ? -16.343 53.020  72.489  1.00 20.12 ? 99   VAL A CG1   1 
ATOM   617   C  CG2   . VAL A  1  101  ? -16.688 50.546  72.877  1.00 19.55 ? 99   VAL A CG2   1 
ATOM   618   N  N     . ALA A  1  102  ? -14.314 52.585  69.596  1.00 17.08 ? 100  ALA A N     1 
ATOM   619   C  CA    . ALA A  1  102  ? -13.683 53.679  68.861  1.00 16.32 ? 100  ALA A CA    1 
ATOM   620   C  C     . ALA A  1  102  ? -14.179 53.740  67.428  1.00 17.75 ? 100  ALA A C     1 
ATOM   621   O  O     . ALA A  1  102  ? -14.391 54.831  66.881  1.00 19.73 ? 100  ALA A O     1 
ATOM   622   C  CB    . ALA A  1  102  ? -12.160 53.519  68.878  1.00 17.06 ? 100  ALA A CB    1 
ATOM   623   N  N     . LEU A  1  103  ? -14.310 52.579  66.792  1.00 17.85 ? 101  LEU A N     1 
ATOM   624   C  CA    . LEU A  1  103  ? -14.847 52.508  65.437  1.00 18.29 ? 101  LEU A CA    1 
ATOM   625   C  C     . LEU A  1  103  ? -16.241 53.115  65.369  1.00 19.70 ? 101  LEU A C     1 
ATOM   626   O  O     . LEU A  1  103  ? -16.554 53.885  64.451  1.00 20.10 ? 101  LEU A O     1 
ATOM   627   C  CB    . LEU A  1  103  ? -14.877 51.058  64.965  1.00 19.16 ? 101  LEU A CB    1 
ATOM   628   C  CG    . LEU A  1  103  ? -15.485 50.862  63.573  1.00 18.84 ? 101  LEU A CG    1 
ATOM   629   C  CD1   . LEU A  1  103  ? -14.655 51.603  62.522  1.00 20.39 ? 101  LEU A CD1   1 
ATOM   630   C  CD2   . LEU A  1  103  ? -15.573 49.379  63.252  1.00 22.04 ? 101  LEU A CD2   1 
ATOM   631   N  N     . MET A  1  104  ? -17.109 52.753  66.312  1.00 18.24 ? 102  MET A N     1 
ATOM   632   C  CA    . MET A  1  104  ? -18.461 53.306  66.254  1.00 20.85 ? 102  MET A CA    1 
ATOM   633   C  C     . MET A  1  104  ? -18.452 54.807  66.511  1.00 19.13 ? 102  MET A C     1 
ATOM   634   O  O     . MET A  1  104  ? -19.243 55.540  65.901  1.00 21.17 ? 102  MET A O     1 
ATOM   635   C  CB    . MET A  1  104  ? -19.374 52.588  67.245  1.00 20.72 ? 102  MET A CB    1 
ATOM   636   C  CG    . MET A  1  104  ? -19.522 51.105  66.949  1.00 20.75 ? 102  MET A CG    1 
ATOM   637   S  SD    . MET A  1  104  ? -19.966 50.718  65.226  1.00 29.32 ? 102  MET A SD    1 
ATOM   638   C  CE    . MET A  1  104  ? -21.656 51.284  65.195  1.00 32.81 ? 102  MET A CE    1 
ATOM   639   N  N     . CYS A  1  105  ? -17.552 55.290  67.375  1.00 17.85 ? 103  CYS A N     1 
ATOM   640   C  CA    . CYS A  1  105  ? -17.432 56.735  67.563  1.00 18.61 ? 103  CYS A CA    1 
ATOM   641   C  C     . CYS A  1  105  ? -16.994 57.409  66.276  1.00 23.72 ? 103  CYS A C     1 
ATOM   642   O  O     . CYS A  1  105  ? -17.504 58.475  65.919  1.00 23.10 ? 103  CYS A O     1 
ATOM   643   C  CB    . CYS A  1  105  ? -16.442 57.050  68.674  1.00 22.36 ? 103  CYS A CB    1 
ATOM   644   S  SG    . CYS A  1  105  ? -17.032 56.578  70.278  1.00 20.38 ? 103  CYS A SG    1 
ATOM   645   N  N     . LEU A  1  106  ? -16.031 56.808  65.578  1.00 20.07 ? 104  LEU A N     1 
ATOM   646   C  CA    . LEU A  1  106  ? -15.605 57.353  64.295  1.00 22.23 ? 104  LEU A CA    1 
ATOM   647   C  C     . LEU A  1  106  ? -16.747 57.342  63.299  1.00 24.67 ? 104  LEU A C     1 
ATOM   648   O  O     . LEU A  1  106  ? -16.953 58.316  62.567  1.00 25.34 ? 104  LEU A O     1 
ATOM   649   C  CB    . LEU A  1  106  ? -14.436 56.549  63.745  1.00 20.57 ? 104  LEU A CB    1 
ATOM   650   C  CG    . LEU A  1  106  ? -14.091 56.871  62.282  1.00 23.22 ? 104  LEU A CG    1 
ATOM   651   C  CD1   . LEU A  1  106  ? -13.575 58.297  62.170  1.00 27.38 ? 104  LEU A CD1   1 
ATOM   652   C  CD2   . LEU A  1  106  ? -13.083 55.876  61.720  1.00 24.73 ? 104  LEU A CD2   1 
ATOM   653   N  N     . ALA A  1  107  ? -17.489 56.238  63.241  1.00 21.00 ? 105  ALA A N     1 
ATOM   654   C  CA    . ALA A  1  107  ? -18.611 56.169  62.318  1.00 23.03 ? 105  ALA A CA    1 
ATOM   655   C  C     . ALA A  1  107  ? -19.624 57.263  62.624  1.00 26.68 ? 105  ALA A C     1 
ATOM   656   O  O     . ALA A  1  107  ? -20.111 57.938  61.710  1.00 27.38 ? 105  ALA A O     1 
ATOM   657   C  CB    . ALA A  1  107  ? -19.253 54.785  62.374  1.00 24.22 ? 105  ALA A CB    1 
ATOM   658   N  N     . GLU A  1  108  ? -19.947 57.455  63.911  1.00 23.11 ? 106  GLU A N     1 
ATOM   659   C  CA    . GLU A  1  108  ? -20.845 58.534  64.317  1.00 24.93 ? 106  GLU A CA    1 
ATOM   660   C  C     . GLU A  1  108  ? -20.352 59.884  63.804  1.00 29.03 ? 106  GLU A C     1 
ATOM   661   O  O     . GLU A  1  108  ? -21.125 60.673  63.247  1.00 29.65 ? 106  GLU A O     1 
ATOM   662   C  CB    . GLU A  1  108  ? -20.983 58.553  65.845  1.00 23.47 ? 106  GLU A CB    1 
ATOM   663   C  CG    . GLU A  1  108  ? -21.806 59.718  66.389  1.00 26.57 ? 106  GLU A CG    1 
ATOM   664   C  CD    . GLU A  1  108  ? -21.545 59.995  67.867  1.00 31.18 ? 106  GLU A CD    1 
ATOM   665   O  OE1   . GLU A  1  108  ? -21.105 59.073  68.593  1.00 26.55 ? 106  GLU A OE1   1 
ATOM   666   O  OE2   . GLU A  1  108  ? -21.774 61.145  68.299  1.00 29.80 ? 106  GLU A OE2   1 
ATOM   667   N  N     . ALA A  1  109  ? -19.056 60.160  63.980  1.00 28.48 ? 107  ALA A N     1 
ATOM   668   C  CA    . ALA A  1  109  ? -18.487 61.423  63.515  1.00 28.26 ? 107  ALA A CA    1 
ATOM   669   C  C     . ALA A  1  109  ? -18.584 61.553  62.002  1.00 31.67 ? 107  ALA A C     1 
ATOM   670   O  O     . ALA A  1  109  ? -18.954 62.617  61.488  1.00 35.29 ? 107  ALA A O     1 
ATOM   671   C  CB    . ALA A  1  109  ? -17.032 61.541  63.966  1.00 31.81 ? 107  ALA A CB    1 
ATOM   672   N  N     . LEU A  1  110  ? -18.254 60.484  61.268  1.00 28.25 ? 108  LEU A N     1 
ATOM   673   C  CA    . LEU A  1  110  ? -18.338 60.531  59.810  1.00 26.65 ? 108  LEU A CA    1 
ATOM   674   C  C     . LEU A  1  110  ? -19.766 60.763  59.344  1.00 31.20 ? 108  LEU A C     1 
ATOM   675   O  O     . LEU A  1  110  ? -19.984 61.362  58.284  1.00 35.39 ? 108  LEU A O     1 
ATOM   676   C  CB    . LEU A  1  110  ? -17.784 59.239  59.198  1.00 27.31 ? 108  LEU A CB    1 
ATOM   677   C  CG    . LEU A  1  110  ? -16.265 59.123  59.304  1.00 32.61 ? 108  LEU A CG    1 
ATOM   678   C  CD1   . LEU A  1  110  ? -15.821 57.709  59.006  1.00 29.68 ? 108  LEU A CD1   1 
ATOM   679   C  CD2   . LEU A  1  110  ? -15.591 60.113  58.350  1.00 31.45 ? 108  LEU A CD2   1 
ATOM   680   N  N     . LEU A  1  111  ? -20.747 60.299  60.110  1.00 30.40 ? 109  LEU A N     1 
ATOM   681   C  CA    . LEU A  1  111  ? -22.138 60.547  59.760  1.00 31.97 ? 109  LEU A CA    1 
ATOM   682   C  C     . LEU A  1  111  ? -22.592 61.957  60.117  1.00 35.76 ? 109  LEU A C     1 
ATOM   683   O  O     . LEU A  1  111  ? -23.692 62.351  59.717  1.00 37.59 ? 109  LEU A O     1 
ATOM   684   C  CB    . LEU A  1  111  ? -23.031 59.507  60.439  1.00 27.98 ? 109  LEU A CB    1 
ATOM   685   C  CG    . LEU A  1  111  ? -22.786 58.091  59.912  1.00 31.90 ? 109  LEU A CG    1 
ATOM   686   C  CD1   . LEU A  1  111  ? -23.485 57.071  60.779  1.00 28.58 ? 109  LEU A CD1   1 
ATOM   687   C  CD2   . LEU A  1  111  ? -23.227 57.967  58.461  1.00 29.55 ? 109  LEU A CD2   1 
ATOM   688   N  N     . ARG A  1  112  ? -21.778 62.724  60.850  1.00 34.91 ? 110  ARG A N     1 
ATOM   689   C  CA    . ARG A  1  112  ? -22.053 64.149  61.002  1.00 30.58 ? 110  ARG A CA    1 
ATOM   690   C  C     . ARG A  1  112  ? -21.718 64.915  59.728  1.00 43.52 ? 110  ARG A C     1 
ATOM   691   O  O     . ARG A  1  112  ? -22.148 66.063  59.576  1.00 47.03 ? 110  ARG A O     1 
ATOM   692   C  CB    . ARG A  1  112  ? -21.283 64.715  62.199  1.00 37.87 ? 110  ARG A CB    1 
ATOM   693   C  CG    . ARG A  1  112  ? -21.697 64.100  63.532  1.00 35.42 ? 110  ARG A CG    1 
ATOM   694   C  CD    . ARG A  1  112  ? -20.746 64.462  64.675  1.00 36.78 ? 110  ARG A CD    1 
ATOM   695   N  NE    . ARG A  1  112  ? -20.779 65.880  65.015  1.00 47.88 ? 110  ARG A NE    1 
ATOM   696   C  CZ    . ARG A  1  112  ? -21.511 66.411  65.987  1.00 50.55 ? 110  ARG A CZ    1 
ATOM   697   N  NH1   . ARG A  1  112  ? -22.317 65.672  66.734  1.00 48.14 ? 110  ARG A NH1   1 
ATOM   698   N  NH2   . ARG A  1  112  ? -21.431 67.719  66.218  1.00 52.80 ? 110  ARG A NH2   1 
ATOM   699   N  N     . ILE A  1  113  ? -20.973 64.302  58.814  1.00 39.19 ? 111  ILE A N     1 
ATOM   700   C  CA    . ILE A  1  113  ? -20.765 64.842  57.470  1.00 42.79 ? 111  ILE A CA    1 
ATOM   701   C  C     . ILE A  1  113  ? -22.018 64.563  56.649  1.00 44.66 ? 111  ILE A C     1 
ATOM   702   O  O     . ILE A  1  113  ? -22.317 63.396  56.355  1.00 45.90 ? 111  ILE A O     1 
ATOM   703   C  CB    . ILE A  1  113  ? -19.523 64.233  56.802  1.00 40.30 ? 111  ILE A CB    1 
ATOM   704   C  CG1   . ILE A  1  113  ? -18.255 64.620  57.564  1.00 33.53 ? 111  ILE A CG1   1 
ATOM   705   C  CG2   . ILE A  1  113  ? -19.436 64.671  55.346  1.00 45.74 ? 111  ILE A CG2   1 
ATOM   706   C  CD1   . ILE A  1  113  ? -17.007 64.053  56.941  1.00 35.06 ? 111  ILE A CD1   1 
ATOM   707   N  N     . PRO A  1  114  ? -22.773 65.592  56.249  1.00 52.45 ? 112  PRO A N     1 
ATOM   708   C  CA    . PRO A  1  114  ? -24.092 65.325  55.648  1.00 52.51 ? 112  PRO A CA    1 
ATOM   709   C  C     . PRO A  1  114  ? -24.020 64.737  54.250  1.00 51.56 ? 112  PRO A C     1 
ATOM   710   O  O     . PRO A  1  114  ? -24.793 63.825  53.928  1.00 54.34 ? 112  PRO A O     1 
ATOM   711   C  CB    . PRO A  1  114  ? -24.766 66.708  55.650  1.00 45.80 ? 112  PRO A CB    1 
ATOM   712   C  CG    . PRO A  1  114  ? -23.907 67.580  56.534  1.00 55.37 ? 112  PRO A CG    1 
ATOM   713   C  CD    . PRO A  1  114  ? -22.523 67.030  56.420  1.00 54.58 ? 112  PRO A CD    1 
ATOM   714   N  N     . ASP A  1  115  ? -23.121 65.232  53.404  1.00 53.19 ? 113  ASP A N     1 
ATOM   715   C  CA    . ASP A  1  115  ? -23.062 64.783  52.020  1.00 54.10 ? 113  ASP A CA    1 
ATOM   716   C  C     . ASP A  1  115  ? -22.330 63.451  51.921  1.00 49.57 ? 113  ASP A C     1 
ATOM   717   O  O     . ASP A  1  115  ? -21.205 63.314  52.409  1.00 49.10 ? 113  ASP A O     1 
ATOM   718   C  CB    . ASP A  1  115  ? -22.373 65.829  51.147  1.00 50.29 ? 113  ASP A CB    1 
ATOM   719   C  CG    . ASP A  1  115  ? -22.081 65.317  49.760  1.00 56.41 ? 113  ASP A CG    1 
ATOM   720   O  OD1   . ASP A  1  115  ? -23.028 64.841  49.095  1.00 58.98 ? 113  ASP A OD1   1 
ATOM   721   O  OD2   . ASP A  1  115  ? -20.907 65.387  49.333  1.00 57.22 ? 113  ASP A OD2   1 
ATOM   722   N  N     . THR A  1  116  ? -22.962 62.479  51.261  1.00 48.68 ? 114  THR A N     1 
ATOM   723   C  CA    . THR A  1  116  ? -22.408 61.129  51.207  1.00 47.38 ? 114  THR A CA    1 
ATOM   724   C  C     . THR A  1  116  ? -21.089 61.093  50.443  1.00 53.64 ? 114  THR A C     1 
ATOM   725   O  O     . THR A  1  116  ? -20.119 60.473  50.894  1.00 49.52 ? 114  THR A O     1 
ATOM   726   C  CB    . THR A  1  116  ? -23.418 60.175  50.573  1.00 48.90 ? 114  THR A CB    1 
ATOM   727   O  OG1   . THR A  1  116  ? -24.646 60.226  51.307  1.00 52.37 ? 114  THR A OG1   1 
ATOM   728   C  CG2   . THR A  1  116  ? -22.885 58.751  50.589  1.00 52.40 ? 114  THR A CG2   1 
ATOM   729   N  N     . ALA A  1  117  ? -21.033 61.747  49.281  1.00 46.25 ? 115  ALA A N     1 
ATOM   730   C  CA    . ALA A  1  117  ? -19.819 61.697  48.471  1.00 45.14 ? 115  ALA A CA    1 
ATOM   731   C  C     . ALA A  1  117  ? -18.643 62.354  49.185  1.00 41.12 ? 115  ALA A C     1 
ATOM   732   O  O     . ALA A  1  117  ? -17.496 61.911  49.040  1.00 45.09 ? 115  ALA A O     1 
ATOM   733   C  CB    . ALA A  1  117  ? -20.061 62.358  47.113  1.00 49.49 ? 115  ALA A CB    1 
ATOM   734   N  N     . THR A  1  118  ? -18.902 63.417  49.950  1.00 40.46 ? 116  THR A N     1 
ATOM   735   C  CA    . THR A  1  118  ? -17.834 64.047  50.721  1.00 46.57 ? 116  THR A CA    1 
ATOM   736   C  C     . THR A  1  118  ? -17.305 63.091  51.782  1.00 40.98 ? 116  THR A C     1 
ATOM   737   O  O     . THR A  1  118  ? -16.092 62.897  51.915  1.00 43.62 ? 116  THR A O     1 
ATOM   738   C  CB    . THR A  1  118  ? -18.339 65.333  51.379  1.00 38.41 ? 116  THR A CB    1 
ATOM   739   O  OG1   . THR A  1  118  ? -18.931 66.184  50.389  1.00 54.05 ? 116  THR A OG1   1 
ATOM   740   C  CG2   . THR A  1  118  ? -17.194 66.067  52.047  1.00 39.40 ? 116  THR A CG2   1 
ATOM   741   N  N     . ARG A  1  119  ? -18.216 62.483  52.542  1.00 42.48 ? 117  ARG A N     1 
ATOM   742   C  CA    . ARG A  1  119  ? -17.838 61.522  53.572  1.00 44.87 ? 117  ARG A CA    1 
ATOM   743   C  C     . ARG A  1  119  ? -16.979 60.404  52.993  1.00 38.85 ? 117  ARG A C     1 
ATOM   744   O  O     . ARG A  1  119  ? -15.926 60.063  53.545  1.00 41.97 ? 117  ARG A O     1 
ATOM   745   C  CB    . ARG A  1  119  ? -19.103 60.955  54.220  1.00 40.17 ? 117  ARG A CB    1 
ATOM   746   C  CG    . ARG A  1  119  ? -18.855 60.039  55.400  1.00 35.16 ? 117  ARG A CG    1 
ATOM   747   C  CD    . ARG A  1  119  ? -20.116 59.265  55.761  1.00 38.66 ? 117  ARG A CD    1 
ATOM   748   N  NE    . ARG A  1  119  ? -21.278 60.135  55.904  1.00 40.53 ? 117  ARG A NE    1 
ATOM   749   C  CZ    . ARG A  1  119  ? -22.436 59.948  55.286  1.00 41.37 ? 117  ARG A CZ    1 
ATOM   750   N  NH1   . ARG A  1  119  ? -22.646 58.895  54.513  1.00 39.06 ? 117  ARG A NH1   1 
ATOM   751   N  NH2   . ARG A  1  119  ? -23.413 60.836  55.457  1.00 49.69 ? 117  ARG A NH2   1 
ATOM   752   N  N     . ASP A  1  120  ? -17.414 59.829  51.868  1.00 44.96 ? 118  ASP A N     1 
ATOM   753   C  CA    . ASP A  1  120  ? -16.693 58.711  51.269  1.00 43.32 ? 118  ASP A CA    1 
ATOM   754   C  C     . ASP A  1  120  ? -15.320 59.128  50.764  1.00 42.95 ? 118  ASP A C     1 
ATOM   755   O  O     . ASP A  1  120  ? -14.375 58.332  50.817  1.00 42.74 ? 118  ASP A O     1 
ATOM   756   C  CB    . ASP A  1  120  ? -17.516 58.102  50.136  1.00 38.89 ? 118  ASP A CB    1 
ATOM   757   C  CG    . ASP A  1  120  ? -18.880 57.626  50.602  1.00 47.27 ? 118  ASP A CG    1 
ATOM   758   O  OD1   . ASP A  1  120  ? -19.103 57.585  51.830  1.00 50.01 ? 118  ASP A OD1   1 
ATOM   759   O  OD2   . ASP A  1  120  ? -19.733 57.303  49.751  1.00 47.75 ? 118  ASP A OD2   1 
ATOM   760   N  N     . ALA A  1  121  ? -15.186 60.363  50.276  1.00 41.55 ? 119  ALA A N     1 
ATOM   761   C  CA    . ALA A  1  121  ? -13.873 60.848  49.865  1.00 46.77 ? 119  ALA A CA    1 
ATOM   762   C  C     . ALA A  1  121  ? -12.962 61.034  51.068  1.00 44.62 ? 119  ALA A C     1 
ATOM   763   O  O     . ALA A  1  121  ? -11.783 60.663  51.028  1.00 43.28 ? 119  ALA A O     1 
ATOM   764   C  CB    . ALA A  1  121  ? -14.011 62.160  49.093  1.00 49.49 ? 119  ALA A CB    1 
ATOM   765   N  N     . LEU A  1  122  ? -13.490 61.612  52.149  1.00 43.92 ? 120  LEU A N     1 
ATOM   766   C  CA    . LEU A  1  122  ? -12.693 61.761  53.356  1.00 43.07 ? 120  LEU A CA    1 
ATOM   767   C  C     . LEU A  1  122  ? -12.228 60.405  53.871  1.00 43.30 ? 120  LEU A C     1 
ATOM   768   O  O     . LEU A  1  122  ? -11.068 60.248  54.270  1.00 43.44 ? 120  LEU A O     1 
ATOM   769   C  CB    . LEU A  1  122  ? -13.493 62.501  54.425  1.00 45.05 ? 120  LEU A CB    1 
ATOM   770   C  CG    . LEU A  1  122  ? -12.640 62.992  55.590  1.00 43.41 ? 120  LEU A CG    1 
ATOM   771   C  CD1   . LEU A  1  122  ? -11.648 64.036  55.108  1.00 51.17 ? 120  LEU A CD1   1 
ATOM   772   C  CD2   . LEU A  1  122  ? -13.510 63.543  56.698  1.00 42.97 ? 120  LEU A CD2   1 
ATOM   773   N  N     . ILE A  1  123  ? -13.114 59.407  53.850  1.00 41.01 ? 121  ILE A N     1 
ATOM   774   C  CA    . ILE A  1  123  ? -12.734 58.065  54.283  1.00 40.38 ? 121  ILE A CA    1 
ATOM   775   C  C     . ILE A  1  123  ? -11.613 57.519  53.404  1.00 43.55 ? 121  ILE A C     1 
ATOM   776   O  O     . ILE A  1  123  ? -10.562 57.098  53.899  1.00 40.66 ? 121  ILE A O     1 
ATOM   777   C  CB    . ILE A  1  123  ? -13.957 57.134  54.274  1.00 36.09 ? 121  ILE A CB    1 
ATOM   778   C  CG1   . ILE A  1  123  ? -14.960 57.549  55.353  1.00 33.50 ? 121  ILE A CG1   1 
ATOM   779   C  CG2   . ILE A  1  123  ? -13.524 55.680  54.446  1.00 37.62 ? 121  ILE A CG2   1 
ATOM   780   C  CD1   . ILE A  1  123  ? -16.291 56.854  55.220  1.00 32.60 ? 121  ILE A CD1   1 
ATOM   781   N  N     . ARG A  1  124  ? -11.819 57.531  52.083  1.00 38.85 ? 122  ARG A N     1 
ATOM   782   C  CA    . ARG A  1  124  ? -10.864 56.897  51.174  1.00 39.78 ? 122  ARG A CA    1 
ATOM   783   C  C     . ARG A  1  124  ? -9.523  57.619  51.169  1.00 43.77 ? 122  ARG A C     1 
ATOM   784   O  O     . ARG A  1  124  ? -8.467  56.977  51.207  1.00 51.29 ? 122  ARG A O     1 
ATOM   785   C  CB    . ARG A  1  124  ? -11.437 56.845  49.757  1.00 42.28 ? 122  ARG A CB    1 
ATOM   786   N  N     . ASP A  1  125  ? -9.541  58.951  51.128  1.00 50.91 ? 123  ASP A N     1 
ATOM   787   C  CA    . ASP A  1  125  ? -8.334  59.718  50.857  1.00 50.65 ? 123  ASP A CA    1 
ATOM   788   C  C     . ASP A  1  125  ? -7.628  60.222  52.105  1.00 49.86 ? 123  ASP A C     1 
ATOM   789   O  O     . ASP A  1  125  ? -6.419  60.475  52.048  1.00 55.68 ? 123  ASP A O     1 
ATOM   790   C  CB    . ASP A  1  125  ? -8.659  60.915  49.953  1.00 59.00 ? 123  ASP A CB    1 
ATOM   791   C  CG    . ASP A  1  125  ? -9.320  60.501  48.648  1.00 60.04 ? 123  ASP A CG    1 
ATOM   792   O  OD1   . ASP A  1  125  ? -8.991  59.411  48.131  1.00 60.37 ? 123  ASP A OD1   1 
ATOM   793   O  OD2   . ASP A  1  125  ? -10.171 61.264  48.139  1.00 58.44 ? 123  ASP A OD2   1 
ATOM   794   N  N     . LYS A  1  126  ? -8.332  60.372  53.224  1.00 46.38 ? 124  LYS A N     1 
ATOM   795   C  CA    . LYS A  1  126  ? -7.744  60.987  54.407  1.00 43.84 ? 124  LYS A CA    1 
ATOM   796   C  C     . LYS A  1  126  ? -7.769  60.083  55.630  1.00 47.04 ? 124  LYS A C     1 
ATOM   797   O  O     . LYS A  1  126  ? -6.730  59.900  56.278  1.00 50.73 ? 124  LYS A O     1 
ATOM   798   C  CB    . LYS A  1  126  ? -8.463  62.311  54.714  1.00 51.78 ? 124  LYS A CB    1 
ATOM   799   N  N     . ILE A  1  127  ? -8.924  59.513  55.976  1.00 43.96 ? 125  ILE A N     1 
ATOM   800   C  CA    . ILE A  1  127  ? -9.015  58.722  57.203  1.00 42.78 ? 125  ILE A CA    1 
ATOM   801   C  C     . ILE A  1  127  ? -8.242  57.418  57.056  1.00 42.23 ? 125  ILE A C     1 
ATOM   802   O  O     . ILE A  1  127  ? -7.403  57.076  57.895  1.00 47.95 ? 125  ILE A O     1 
ATOM   803   C  CB    . ILE A  1  127  ? -10.485 58.446  57.569  1.00 35.54 ? 125  ILE A CB    1 
ATOM   804   C  CG1   . ILE A  1  127  ? -11.332 59.718  57.481  1.00 43.00 ? 125  ILE A CG1   1 
ATOM   805   C  CG2   . ILE A  1  127  ? -10.572 57.839  58.970  1.00 38.99 ? 125  ILE A CG2   1 
ATOM   806   C  CD1   . ILE A  1  127  ? -10.902 60.801  58.422  1.00 45.11 ? 125  ILE A CD1   1 
ATOM   807   N  N     . ALA A  1  128  ? -8.529  56.665  55.991  1.00 37.04 ? 126  ALA A N     1 
ATOM   808   C  CA    . ALA A  1  128  ? -8.015  55.306  55.870  1.00 35.44 ? 126  ALA A CA    1 
ATOM   809   C  C     . ALA A  1  128  ? -6.501  55.287  55.721  1.00 46.03 ? 126  ALA A C     1 
ATOM   810   O  O     . ALA A  1  128  ? -5.833  54.401  56.265  1.00 44.33 ? 126  ALA A O     1 
ATOM   811   C  CB    . ALA A  1  128  ? -8.671  54.602  54.683  1.00 37.42 ? 126  ALA A CB    1 
ATOM   812   N  N     . ASP A  1  129  ? -5.943  56.251  54.986  1.00 63.67 ? 127  ASP A N     1 
ATOM   813   C  CA    . ASP A  1  129  ? -4.527  56.232  54.642  1.00 68.01 ? 127  ASP A CA    1 
ATOM   814   C  C     . ASP A  1  129  ? -3.632  56.775  55.747  1.00 66.18 ? 127  ASP A C     1 
ATOM   815   O  O     . ASP A  1  129  ? -2.413  56.583  55.681  1.00 74.03 ? 127  ASP A O     1 
ATOM   816   C  CB    . ASP A  1  129  ? -4.288  57.024  53.352  1.00 62.38 ? 127  ASP A CB    1 
ATOM   817   N  N     . GLY A  1  130  ? -4.191  57.441  56.753  1.00 53.88 ? 128  GLY A N     1 
ATOM   818   C  CA    . GLY A  1  130  ? -3.355  57.947  57.820  1.00 60.57 ? 128  GLY A CA    1 
ATOM   819   C  C     . GLY A  1  130  ? -4.083  58.571  58.989  1.00 61.49 ? 128  GLY A C     1 
ATOM   820   O  O     . GLY A  1  130  ? -4.923  57.933  59.633  1.00 60.70 ? 128  GLY A O     1 
ATOM   821   N  N     . ASN A  1  131  ? -3.761  59.833  59.265  1.00 62.45 ? 129  ASN A N     1 
ATOM   822   C  CA    . ASN A  1  131  ? -4.165  60.486  60.506  1.00 64.12 ? 129  ASN A CA    1 
ATOM   823   C  C     . ASN A  1  131  ? -5.649  60.829  60.467  1.00 58.07 ? 129  ASN A C     1 
ATOM   824   O  O     . ASN A  1  131  ? -6.067  61.748  59.756  1.00 61.00 ? 129  ASN A O     1 
ATOM   825   C  CB    . ASN A  1  131  ? -3.320  61.738  60.730  1.00 64.41 ? 129  ASN A CB    1 
ATOM   826   N  N     . TRP A  1  132  ? -6.448  60.092  61.243  1.00 49.29 ? 130  TRP A N     1 
ATOM   827   C  CA    . TRP A  1  132  ? -7.849  60.462  61.421  1.00 47.07 ? 130  TRP A CA    1 
ATOM   828   C  C     . TRP A  1  132  ? -7.991  61.722  62.263  1.00 41.08 ? 130  TRP A C     1 
ATOM   829   O  O     . TRP A  1  132  ? -8.964  62.468  62.103  1.00 43.06 ? 130  TRP A O     1 
ATOM   830   C  CB    . TRP A  1  132  ? -8.617  59.316  62.077  1.00 42.45 ? 130  TRP A CB    1 
ATOM   831   C  CG    . TRP A  1  132  ? -8.041  58.915  63.403  1.00 35.55 ? 130  TRP A CG    1 
ATOM   832   C  CD1   . TRP A  1  132  ? -7.095  57.955  63.629  1.00 32.83 ? 130  TRP A CD1   1 
ATOM   833   C  CD2   . TRP A  1  132  ? -8.366  59.466  64.682  1.00 27.85 ? 130  TRP A CD2   1 
ATOM   834   N  NE1   . TRP A  1  132  ? -6.819  57.869  64.972  1.00 32.84 ? 130  TRP A NE1   1 
ATOM   835   C  CE2   . TRP A  1  132  ? -7.582  58.788  65.642  1.00 27.83 ? 130  TRP A CE2   1 
ATOM   836   C  CE3   . TRP A  1  132  ? -9.241  60.464  65.111  1.00 30.47 ? 130  TRP A CE3   1 
ATOM   837   C  CZ2   . TRP A  1  132  ? -7.648  59.079  67.000  1.00 27.98 ? 130  TRP A CZ2   1 
ATOM   838   C  CZ3   . TRP A  1  132  ? -9.307  60.752  66.457  1.00 28.30 ? 130  TRP A CZ3   1 
ATOM   839   C  CH2   . TRP A  1  132  ? -8.518  60.062  67.391  1.00 27.72 ? 130  TRP A CH2   1 
ATOM   840   N  N     . LYS A  1  133  ? -7.047  61.963  63.174  1.00 47.34 ? 131  LYS A N     1 
ATOM   841   C  CA    . LYS A  1  133  ? -7.152  63.120  64.056  1.00 53.62 ? 131  LYS A CA    1 
ATOM   842   C  C     . LYS A  1  133  ? -7.086  64.421  63.267  1.00 62.77 ? 131  LYS A C     1 
ATOM   843   O  O     . LYS A  1  133  ? -7.837  65.364  63.548  1.00 67.90 ? 131  LYS A O     1 
ATOM   844   C  CB    . LYS A  1  133  ? -6.051  63.070  65.116  1.00 44.54 ? 131  LYS A CB    1 
ATOM   845   N  N     . SER A  1  134  ? -6.212  64.479  62.257  1.00 64.10 ? 132  SER A N     1 
ATOM   846   C  CA    . SER A  1  134  ? -6.039  65.695  61.468  1.00 63.36 ? 132  SER A CA    1 
ATOM   847   C  C     . SER A  1  134  ? -7.328  66.158  60.799  1.00 64.36 ? 132  SER A C     1 
ATOM   848   O  O     . SER A  1  134  ? -7.466  67.351  60.509  1.00 67.42 ? 132  SER A O     1 
ATOM   849   C  CB    . SER A  1  134  ? -4.957  65.474  60.408  1.00 63.27 ? 132  SER A CB    1 
ATOM   850   N  N     . HIS A  1  135  ? -8.281  65.254  60.557  1.00 63.61 ? 133  HIS A N     1 
ATOM   851   C  CA    . HIS A  1  135  ? -9.472  65.592  59.791  1.00 63.24 ? 133  HIS A CA    1 
ATOM   852   C  C     . HIS A  1  135  ? -10.760 65.574  60.599  1.00 61.04 ? 133  HIS A C     1 
ATOM   853   O  O     . HIS A  1  135  ? -11.742 66.183  60.165  1.00 57.94 ? 133  HIS A O     1 
ATOM   854   C  CB    . HIS A  1  135  ? -9.622  64.638  58.596  1.00 58.15 ? 133  HIS A CB    1 
ATOM   855   C  CG    . HIS A  1  135  ? -8.369  64.486  57.790  1.00 64.76 ? 133  HIS A CG    1 
ATOM   856   N  ND1   . HIS A  1  135  ? -7.393  63.562  58.101  1.00 67.11 ? 133  HIS A ND1   1 
ATOM   857   C  CD2   . HIS A  1  135  ? -7.923  65.150  56.697  1.00 63.30 ? 133  HIS A CD2   1 
ATOM   858   C  CE1   . HIS A  1  135  ? -6.404  63.659  57.231  1.00 65.68 ? 133  HIS A CE1   1 
ATOM   859   N  NE2   . HIS A  1  135  ? -6.700  64.616  56.369  1.00 68.18 ? 133  HIS A NE2   1 
ATOM   860   N  N     . LEU A  1  136  ? -10.786 64.905  61.747  1.00 63.32 ? 134  LEU A N     1 
ATOM   861   C  CA    . LEU A  1  136  ? -12.005 64.824  62.548  1.00 65.21 ? 134  LEU A CA    1 
ATOM   862   C  C     . LEU A  1  136  ? -11.731 65.098  64.025  1.00 71.66 ? 134  LEU A C     1 
ATOM   863   O  O     . LEU A  1  136  ? -12.563 65.680  64.726  1.00 72.08 ? 134  LEU A O     1 
ATOM   864   C  CB    . LEU A  1  136  ? -12.662 63.452  62.378  1.00 57.40 ? 134  LEU A CB    1 
ATOM   865   C  CG    . LEU A  1  136  ? -13.290 63.153  61.015  1.00 59.17 ? 134  LEU A CG    1 
ATOM   866   C  CD1   . LEU A  1  136  ? -13.628 61.682  60.899  1.00 47.61 ? 134  LEU A CD1   1 
ATOM   867   C  CD2   . LEU A  1  136  ? -14.533 64.001  60.793  1.00 45.64 ? 134  LEU A CD2   1 
ATOM   868   N  N     . SER A  1  139  ? -12.499 70.348  67.606  1.00 43.47 ? 137  SER A N     1 
ATOM   869   C  CA    . SER A  1  139  ? -13.271 71.122  68.581  1.00 43.91 ? 137  SER A CA    1 
ATOM   870   C  C     . SER A  1  139  ? -14.105 70.216  69.483  1.00 41.02 ? 137  SER A C     1 
ATOM   871   O  O     . SER A  1  139  ? -14.463 70.589  70.602  1.00 42.25 ? 137  SER A O     1 
ATOM   872   C  CB    . SER A  1  139  ? -14.181 72.127  67.870  1.00 40.61 ? 137  SER A CB    1 
ATOM   873   N  N     . ARG A  1  140  ? -14.411 69.019  68.992  1.00 29.61 ? 138  ARG A N     1 
ATOM   874   C  CA    . ARG A  1  140  ? -15.228 68.053  69.718  1.00 26.62 ? 138  ARG A CA    1 
ATOM   875   C  C     . ARG A  1  140  ? -14.548 66.698  69.621  1.00 32.21 ? 138  ARG A C     1 
ATOM   876   O  O     . ARG A  1  140  ? -14.262 66.228  68.515  1.00 30.75 ? 138  ARG A O     1 
ATOM   877   C  CB    . ARG A  1  140  ? -16.645 68.015  69.135  1.00 32.74 ? 138  ARG A CB    1 
ATOM   878   C  CG    . ARG A  1  140  ? -17.521 66.817  69.501  1.00 38.73 ? 138  ARG A CG    1 
ATOM   879   C  CD    . ARG A  1  140  ? -18.676 66.719  68.495  1.00 40.24 ? 138  ARG A CD    1 
ATOM   880   N  NE    . ARG A  1  140  ? -19.648 65.673  68.797  1.00 45.31 ? 138  ARG A NE    1 
ATOM   881   C  CZ    . ARG A  1  140  ? -19.592 64.433  68.325  1.00 49.19 ? 138  ARG A CZ    1 
ATOM   882   N  NH1   . ARG A  1  140  ? -18.574 64.018  67.585  1.00 45.89 ? 138  ARG A NH1   1 
ATOM   883   N  NH2   . ARG A  1  140  ? -20.583 63.588  68.601  1.00 47.17 ? 138  ARG A NH2   1 
ATOM   884   N  N     . SER A  1  141  ? -14.263 66.088  70.772  1.00 28.32 ? 139  SER A N     1 
ATOM   885   C  CA    . SER A  1  141  ? -13.703 64.744  70.789  1.00 26.74 ? 139  SER A CA    1 
ATOM   886   C  C     . SER A  1  141  ? -14.552 63.797  69.951  1.00 24.89 ? 139  SER A C     1 
ATOM   887   O  O     . SER A  1  141  ? -15.781 63.868  69.948  1.00 24.18 ? 139  SER A O     1 
ATOM   888   C  CB    . SER A  1  141  ? -13.623 64.223  72.224  1.00 23.89 ? 139  SER A CB    1 
ATOM   889   O  OG    . SER A  1  141  ? -13.161 62.875  72.250  1.00 24.85 ? 139  SER A OG    1 
ATOM   890   N  N     . LEU A  1  142  ? -13.887 62.904  69.220  1.00 22.90 ? 140  LEU A N     1 
ATOM   891   C  CA    . LEU A  1  142  ? -14.631 61.863  68.527  1.00 18.72 ? 140  LEU A CA    1 
ATOM   892   C  C     . LEU A  1  142  ? -15.432 61.008  69.493  1.00 19.40 ? 140  LEU A C     1 
ATOM   893   O  O     . LEU A  1  142  ? -16.423 60.385  69.103  1.00 21.05 ? 140  LEU A O     1 
ATOM   894   C  CB    . LEU A  1  142  ? -13.657 60.969  67.762  1.00 22.05 ? 140  LEU A CB    1 
ATOM   895   C  CG    . LEU A  1  142  ? -13.924 60.765  66.285  1.00 31.96 ? 140  LEU A CG    1 
ATOM   896   C  CD1   . LEU A  1  142  ? -13.654 62.057  65.550  1.00 35.54 ? 140  LEU A CD1   1 
ATOM   897   C  CD2   . LEU A  1  142  ? -13.033 59.653  65.785  1.00 33.45 ? 140  LEU A CD2   1 
ATOM   898   N  N     . PHE A  1  143  ? -15.018 60.972  70.749  1.00 19.46 ? 141  PHE A N     1 
ATOM   899   C  CA    . PHE A  1  143  ? -15.465 59.960  71.683  1.00 20.21 ? 141  PHE A CA    1 
ATOM   900   C  C     . PHE A  1  143  ? -16.458 60.517  72.692  1.00 21.84 ? 141  PHE A C     1 
ATOM   901   O  O     . PHE A  1  143  ? -16.668 59.909  73.741  1.00 22.13 ? 141  PHE A O     1 
ATOM   902   C  CB    . PHE A  1  143  ? -14.236 59.353  72.363  1.00 19.95 ? 141  PHE A CB    1 
ATOM   903   C  CG    . PHE A  1  143  ? -13.180 58.923  71.377  1.00 18.48 ? 141  PHE A CG    1 
ATOM   904   C  CD1   . PHE A  1  143  ? -13.469 57.938  70.440  1.00 16.30 ? 141  PHE A CD1   1 
ATOM   905   C  CD2   . PHE A  1  143  ? -11.925 59.520  71.357  1.00 19.74 ? 141  PHE A CD2   1 
ATOM   906   C  CE1   . PHE A  1  143  ? -12.524 57.536  69.523  1.00 20.07 ? 141  PHE A CE1   1 
ATOM   907   C  CE2   . PHE A  1  143  ? -10.976 59.126  70.424  1.00 21.77 ? 141  PHE A CE2   1 
ATOM   908   C  CZ    . PHE A  1  143  ? -11.271 58.133  69.508  1.00 19.32 ? 141  PHE A CZ    1 
ATOM   909   N  N     . VAL A  1  144  ? -17.109 61.642  72.367  1.00 20.65 ? 142  VAL A N     1 
ATOM   910   C  CA    A VAL A  1  144  ? -18.057 62.267  73.293  0.53 21.63 ? 142  VAL A CA    1 
ATOM   911   C  CA    B VAL A  1  144  ? -18.023 62.246  73.331  0.47 21.64 ? 142  VAL A CA    1 
ATOM   912   C  C     . VAL A  1  144  ? -19.136 61.279  73.716  1.00 23.09 ? 142  VAL A C     1 
ATOM   913   O  O     . VAL A  1  144  ? -19.567 61.258  74.876  1.00 23.55 ? 142  VAL A O     1 
ATOM   914   C  CB    A VAL A  1  144  ? -18.673 63.526  72.654  0.53 22.41 ? 142  VAL A CB    1 
ATOM   915   C  CB    B VAL A  1  144  ? -18.586 63.575  72.793  0.47 22.43 ? 142  VAL A CB    1 
ATOM   916   C  CG1   A VAL A  1  144  ? -19.893 64.000  73.447  0.53 22.33 ? 142  VAL A CG1   1 
ATOM   917   C  CG1   B VAL A  1  144  ? -17.474 64.597  72.643  0.47 26.55 ? 142  VAL A CG1   1 
ATOM   918   C  CG2   A VAL A  1  144  ? -17.637 64.629  72.558  0.53 26.60 ? 142  VAL A CG2   1 
ATOM   919   C  CG2   B VAL A  1  144  ? -19.285 63.363  71.478  0.47 24.66 ? 142  VAL A CG2   1 
ATOM   920   N  N     . ASN A  1  145  ? -19.599 60.450  72.785  1.00 20.85 ? 143  ASN A N     1 
ATOM   921   C  CA    . ASN A  1  145  ? -20.659 59.501  73.096  1.00 23.55 ? 143  ASN A CA    1 
ATOM   922   C  C     . ASN A  1  145  ? -20.146 58.080  73.274  1.00 22.85 ? 143  ASN A C     1 
ATOM   923   O  O     . ASN A  1  145  ? -20.920 57.125  73.134  1.00 21.86 ? 143  ASN A O     1 
ATOM   924   C  CB    . ASN A  1  145  ? -21.731 59.555  72.012  1.00 23.60 ? 143  ASN A CB    1 
ATOM   925   C  CG    . ASN A  1  145  ? -22.510 60.845  72.052  1.00 26.75 ? 143  ASN A CG    1 
ATOM   926   O  OD1   . ASN A  1  145  ? -23.028 61.230  73.103  1.00 28.53 ? 143  ASN A OD1   1 
ATOM   927   N  ND2   . ASN A  1  145  ? -22.567 61.537  70.928  1.00 25.89 ? 143  ASN A ND2   1 
ATOM   928   N  N     . ALA A  1  146  ? -18.866 57.917  73.618  1.00 20.99 ? 144  ALA A N     1 
ATOM   929   C  CA    . ALA A  1  146  ? -18.314 56.573  73.724  1.00 20.75 ? 144  ALA A CA    1 
ATOM   930   C  C     . ALA A  1  146  ? -18.913 55.766  74.872  1.00 20.22 ? 144  ALA A C     1 
ATOM   931   O  O     . ALA A  1  146  ? -18.861 54.536  74.821  1.00 22.32 ? 144  ALA A O     1 
ATOM   932   C  CB    . ALA A  1  146  ? -16.797 56.641  73.885  1.00 19.08 ? 144  ALA A CB    1 
ATOM   933   N  N     . ALA A  1  147  ? -19.463 56.408  75.912  1.00 20.95 ? 145  ALA A N     1 
ATOM   934   C  CA    . ALA A  1  147  ? -20.145 55.632  76.945  1.00 23.57 ? 145  ALA A CA    1 
ATOM   935   C  C     . ALA A  1  147  ? -21.346 54.908  76.363  1.00 24.98 ? 145  ALA A C     1 
ATOM   936   O  O     . ALA A  1  147  ? -21.622 53.753  76.707  1.00 24.85 ? 145  ALA A O     1 
ATOM   937   C  CB    . ALA A  1  147  ? -20.569 56.536  78.105  1.00 26.86 ? 145  ALA A CB    1 
ATOM   938   N  N     . THR A  1  148  ? -22.057 55.569  75.453  1.00 20.96 ? 146  THR A N     1 
ATOM   939   C  CA    . THR A  1  148  ? -23.181 54.937  74.779  1.00 20.78 ? 146  THR A CA    1 
ATOM   940   C  C     . THR A  1  148  ? -22.713 53.788  73.902  1.00 21.66 ? 146  THR A C     1 
ATOM   941   O  O     . THR A  1  148  ? -23.223 52.667  73.998  1.00 22.98 ? 146  THR A O     1 
ATOM   942   C  CB    . THR A  1  148  ? -23.924 55.985  73.952  1.00 24.19 ? 146  THR A CB    1 
ATOM   943   O  OG1   . THR A  1  148  ? -24.339 57.042  74.824  1.00 24.54 ? 146  THR A OG1   1 
ATOM   944   C  CG2   . THR A  1  148  ? -25.134 55.379  73.265  1.00 29.79 ? 146  THR A CG2   1 
ATOM   945   N  N     . TRP A  1  149  ? -21.730 54.046  73.040  1.00 20.51 ? 147  TRP A N     1 
ATOM   946   C  CA    . TRP A  1  149  ? -21.222 52.981  72.187  1.00 21.13 ? 147  TRP A CA    1 
ATOM   947   C  C     . TRP A  1  149  ? -20.583 51.867  72.997  1.00 19.48 ? 147  TRP A C     1 
ATOM   948   O  O     . TRP A  1  149  ? -20.613 50.708  72.573  1.00 22.23 ? 147  TRP A O     1 
ATOM   949   C  CB    . TRP A  1  149  ? -20.224 53.546  71.179  1.00 22.04 ? 147  TRP A CB    1 
ATOM   950   C  CG    . TRP A  1  149  ? -20.886 54.463  70.192  1.00 20.14 ? 147  TRP A CG    1 
ATOM   951   C  CD1   . TRP A  1  149  ? -20.656 55.791  70.036  1.00 24.88 ? 147  TRP A CD1   1 
ATOM   952   C  CD2   . TRP A  1  149  ? -21.903 54.112  69.243  1.00 22.30 ? 147  TRP A CD2   1 
ATOM   953   N  NE1   . TRP A  1  149  ? -21.456 56.296  69.036  1.00 22.69 ? 147  TRP A NE1   1 
ATOM   954   C  CE2   . TRP A  1  149  ? -22.232 55.284  68.536  1.00 22.72 ? 147  TRP A CE2   1 
ATOM   955   C  CE3   . TRP A  1  149  ? -22.561 52.920  68.918  1.00 25.74 ? 147  TRP A CE3   1 
ATOM   956   C  CZ2   . TRP A  1  149  ? -23.189 55.303  67.521  1.00 24.82 ? 147  TRP A CZ2   1 
ATOM   957   C  CZ3   . TRP A  1  149  ? -23.511 52.941  67.910  1.00 27.62 ? 147  TRP A CZ3   1 
ATOM   958   C  CH2   . TRP A  1  149  ? -23.817 54.126  67.227  1.00 30.95 ? 147  TRP A CH2   1 
ATOM   959   N  N     . GLY A  1  150  ? -19.989 52.195  74.150  1.00 19.88 ? 148  GLY A N     1 
ATOM   960   C  CA    . GLY A  1  150  ? -19.510 51.153  75.042  1.00 21.75 ? 148  GLY A CA    1 
ATOM   961   C  C     . GLY A  1  150  ? -20.621 50.222  75.485  1.00 21.84 ? 148  GLY A C     1 
ATOM   962   O  O     . GLY A  1  150  ? -20.438 49.005  75.547  1.00 26.81 ? 148  GLY A O     1 
ATOM   963   N  N     . LEU A  1  151  ? -21.789 50.783  75.810  1.00 23.57 ? 149  LEU A N     1 
ATOM   964   C  CA    A LEU A  1  151  ? -22.925 49.937  76.166  0.48 25.24 ? 149  LEU A CA    1 
ATOM   965   C  CA    B LEU A  1  151  ? -22.927 49.943  76.166  0.52 25.24 ? 149  LEU A CA    1 
ATOM   966   C  C     . LEU A  1  151  ? -23.342 49.060  74.994  1.00 25.17 ? 149  LEU A C     1 
ATOM   967   O  O     . LEU A  1  151  ? -23.675 47.884  75.176  1.00 29.82 ? 149  LEU A O     1 
ATOM   968   C  CB    A LEU A  1  151  ? -24.098 50.795  76.639  0.48 27.44 ? 149  LEU A CB    1 
ATOM   969   C  CB    B LEU A  1  151  ? -24.080 50.831  76.624  0.52 27.45 ? 149  LEU A CB    1 
ATOM   970   C  CG    A LEU A  1  151  ? -24.233 50.983  78.148  0.48 29.21 ? 149  LEU A CG    1 
ATOM   971   C  CG    B LEU A  1  151  ? -25.136 50.269  77.562  0.52 26.63 ? 149  LEU A CG    1 
ATOM   972   C  CD1   A LEU A  1  151  ? -25.332 51.987  78.461  0.48 29.21 ? 149  LEU A CD1   1 
ATOM   973   C  CD1   B LEU A  1  151  ? -24.498 49.476  78.690  0.52 29.97 ? 149  LEU A CD1   1 
ATOM   974   C  CD2   A LEU A  1  151  ? -24.520 49.649  78.828  0.48 29.97 ? 149  LEU A CD2   1 
ATOM   975   C  CD2   B LEU A  1  151  ? -25.912 51.442  78.114  0.52 29.51 ? 149  LEU A CD2   1 
ATOM   976   N  N     . VAL A  1  152  ? -23.315 49.610  73.779  1.00 22.67 ? 150  VAL A N     1 
ATOM   977   C  CA    . VAL A  1  152  ? -23.689 48.845  72.589  1.00 23.77 ? 150  VAL A CA    1 
ATOM   978   C  C     . VAL A  1  152  ? -22.710 47.706  72.344  1.00 28.29 ? 150  VAL A C     1 
ATOM   979   O  O     . VAL A  1  152  ? -23.111 46.571  72.046  1.00 28.32 ? 150  VAL A O     1 
ATOM   980   C  CB    . VAL A  1  152  ? -23.771 49.782  71.371  1.00 25.99 ? 150  VAL A CB    1 
ATOM   981   C  CG1   . VAL A  1  152  ? -23.874 48.979  70.088  1.00 32.92 ? 150  VAL A CG1   1 
ATOM   982   C  CG2   . VAL A  1  152  ? -24.938 50.746  71.527  1.00 28.49 ? 150  VAL A CG2   1 
ATOM   983   N  N     . VAL A  1  153  ? -21.413 47.988  72.461  1.00 24.03 ? 151  VAL A N     1 
ATOM   984   C  CA    . VAL A  1  153  ? -20.396 47.002  72.111  1.00 24.75 ? 151  VAL A CA    1 
ATOM   985   C  C     . VAL A  1  153  ? -20.212 45.982  73.226  1.00 23.75 ? 151  VAL A C     1 
ATOM   986   O  O     . VAL A  1  153  ? -20.142 44.775  72.967  1.00 28.71 ? 151  VAL A O     1 
ATOM   987   C  CB    . VAL A  1  153  ? -19.067 47.703  71.768  1.00 23.09 ? 151  VAL A CB    1 
ATOM   988   C  CG1   . VAL A  1  153  ? -17.960 46.684  71.592  1.00 25.51 ? 151  VAL A CG1   1 
ATOM   989   C  CG2   . VAL A  1  153  ? -19.225 48.536  70.509  1.00 24.71 ? 151  VAL A CG2   1 
ATOM   990   N  N     . THR A  1  154  ? -20.127 46.444  74.476  1.00 25.71 ? 152  THR A N     1 
ATOM   991   C  CA    . THR A  1  154  ? -19.723 45.586  75.584  1.00 27.42 ? 152  THR A CA    1 
ATOM   992   C  C     . THR A  1  154  ? -20.853 45.214  76.530  1.00 31.55 ? 152  THR A C     1 
ATOM   993   O  O     . THR A  1  154  ? -20.667 44.312  77.353  1.00 33.54 ? 152  THR A O     1 
ATOM   994   C  CB    . THR A  1  154  ? -18.610 46.246  76.414  1.00 27.78 ? 152  THR A CB    1 
ATOM   995   O  OG1   . THR A  1  154  ? -19.148 47.333  77.186  1.00 29.72 ? 152  THR A OG1   1 
ATOM   996   C  CG2   . THR A  1  154  ? -17.502 46.767  75.523  1.00 26.60 ? 152  THR A CG2   1 
ATOM   997   N  N     . GLY A  1  155  ? -22.000 45.885  76.459  1.00 28.47 ? 153  GLY A N     1 
ATOM   998   C  CA    . GLY A  1  155  ? -23.039 45.688  77.449  1.00 28.80 ? 153  GLY A CA    1 
ATOM   999   C  C     . GLY A  1  155  ? -22.766 46.314  78.796  1.00 35.06 ? 153  GLY A C     1 
ATOM   1000  O  O     . GLY A  1  155  ? -23.614 46.212  79.693  1.00 34.14 ? 153  GLY A O     1 
ATOM   1001  N  N     . LYS A  1  156  ? -21.618 46.961  78.971  1.00 29.33 ? 154  LYS A N     1 
ATOM   1002  C  CA    . LYS A  1  156  ? -21.226 47.555  80.237  1.00 33.47 ? 154  LYS A CA    1 
ATOM   1003  C  C     . LYS A  1  156  ? -21.243 49.070  80.116  1.00 29.83 ? 154  LYS A C     1 
ATOM   1004  O  O     . LYS A  1  156  ? -20.914 49.626  79.064  1.00 28.64 ? 154  LYS A O     1 
ATOM   1005  C  CB    . LYS A  1  156  ? -19.835 47.078  80.665  1.00 35.43 ? 154  LYS A CB    1 
ATOM   1006  N  N     . LEU A  1  157  ? -21.639 49.731  81.188  1.00 30.07 ? 155  LEU A N     1 
ATOM   1007  C  CA    . LEU A  1  157  ? -21.697 51.180  81.221  1.00 34.76 ? 155  LEU A CA    1 
ATOM   1008  C  C     . LEU A  1  157  ? -20.475 51.723  81.947  1.00 39.87 ? 155  LEU A C     1 
ATOM   1009  O  O     . LEU A  1  157  ? -20.110 51.226  83.018  1.00 39.07 ? 155  LEU A O     1 
ATOM   1010  C  CB    . LEU A  1  157  ? -22.978 51.646  81.907  1.00 32.24 ? 155  LEU A CB    1 
ATOM   1011  C  CG    . LEU A  1  157  ? -23.112 53.147  82.108  1.00 38.82 ? 155  LEU A CG    1 
ATOM   1012  C  CD1   . LEU A  1  157  ? -23.205 53.869  80.762  1.00 37.52 ? 155  LEU A CD1   1 
ATOM   1013  C  CD2   . LEU A  1  157  ? -24.336 53.399  82.960  1.00 36.15 ? 155  LEU A CD2   1 
ATOM   1014  N  N     . THR A  1  158  ? -19.832 52.718  81.348  1.00 41.05 ? 156  THR A N     1 
ATOM   1015  C  CA    . THR A  1  158  ? -18.819 53.524  82.011  1.00 44.93 ? 156  THR A CA    1 
ATOM   1016  C  C     . THR A  1  158  ? -19.280 54.973  81.978  1.00 44.35 ? 156  THR A C     1 
ATOM   1017  O  O     . THR A  1  158  ? -19.776 55.447  80.954  1.00 49.98 ? 156  THR A O     1 
ATOM   1018  C  CB    . THR A  1  158  ? -17.450 53.379  81.337  1.00 52.02 ? 156  THR A CB    1 
ATOM   1019  O  OG1   . THR A  1  158  ? -17.207 51.999  81.031  1.00 53.58 ? 156  THR A OG1   1 
ATOM   1020  C  CG2   . THR A  1  158  ? -16.348 53.877  82.262  1.00 49.80 ? 156  THR A CG2   1 
ATOM   1021  N  N     . SER A  1  159  ? -19.142 55.672  83.106  1.00 32.12 ? 157  SER A N     1 
ATOM   1022  C  CA    . SER A  1  159  ? -19.673 57.028  83.186  1.00 31.12 ? 157  SER A CA    1 
ATOM   1023  C  C     . SER A  1  159  ? -18.821 58.021  82.404  1.00 31.75 ? 157  SER A C     1 
ATOM   1024  O  O     . SER A  1  159  ? -19.353 58.979  81.835  1.00 33.84 ? 157  SER A O     1 
ATOM   1025  C  CB    . SER A  1  159  ? -19.784 57.456  84.646  1.00 39.76 ? 157  SER A CB    1 
ATOM   1026  O  OG    . SER A  1  159  ? -18.743 56.876  85.408  1.00 45.45 ? 157  SER A OG    1 
ATOM   1027  N  N     . THR A  1  160  ? -17.512 57.821  82.372  1.00 31.18 ? 158  THR A N     1 
ATOM   1028  C  CA    . THR A  1  160  ? -16.623 58.678  81.609  1.00 23.74 ? 158  THR A CA    1 
ATOM   1029  C  C     . THR A  1  160  ? -15.844 57.833  80.614  1.00 27.23 ? 158  THR A C     1 
ATOM   1030  O  O     . THR A  1  160  ? -15.786 56.605  80.710  1.00 27.61 ? 158  THR A O     1 
ATOM   1031  C  CB    . THR A  1  160  ? -15.657 59.453  82.515  1.00 27.31 ? 158  THR A CB    1 
ATOM   1032  O  OG1   . THR A  1  160  ? -14.843 58.534  83.245  1.00 30.20 ? 158  THR A OG1   1 
ATOM   1033  C  CG2   . THR A  1  160  ? -16.422 60.329  83.489  1.00 35.70 ? 158  THR A CG2   1 
ATOM   1034  N  N     . VAL A  1  161  ? -15.244 58.522  79.653  1.00 19.47 ? 159  VAL A N     1 
ATOM   1035  C  CA    . VAL A  1  161  ? -14.679 57.912  78.456  1.00 20.77 ? 159  VAL A CA    1 
ATOM   1036  C  C     . VAL A  1  161  ? -13.166 57.937  78.582  1.00 19.67 ? 159  VAL A C     1 
ATOM   1037  O  O     . VAL A  1  161  ? -12.588 58.996  78.839  1.00 18.78 ? 159  VAL A O     1 
ATOM   1038  C  CB    . VAL A  1  161  ? -15.140 58.689  77.209  1.00 22.11 ? 159  VAL A CB    1 
ATOM   1039  C  CG1   . VAL A  1  161  ? -14.379 58.273  75.998  1.00 25.29 ? 159  VAL A CG1   1 
ATOM   1040  C  CG2   . VAL A  1  161  ? -16.654 58.540  77.026  1.00 26.81 ? 159  VAL A CG2   1 
ATOM   1041  N  N     . ASN A  1  162  ? -12.514 56.788  78.391  1.00 17.56 ? 160  ASN A N     1 
ATOM   1042  C  CA    . ASN A  1  162  ? -11.054 56.823  78.342  1.00 19.84 ? 160  ASN A CA    1 
ATOM   1043  C  C     . ASN A  1  162  ? -10.681 57.172  76.913  1.00 16.69 ? 160  ASN A C     1 
ATOM   1044  O  O     . ASN A  1  162  ? -10.475 56.299  76.056  1.00 16.85 ? 160  ASN A O     1 
ATOM   1045  C  CB    . ASN A  1  162  ? -10.427 55.510  78.786  1.00 18.70 ? 160  ASN A CB    1 
ATOM   1046  C  CG    . ASN A  1  162  ? -8.906  55.595  78.835  1.00 19.24 ? 160  ASN A CG    1 
ATOM   1047  O  OD1   . ASN A  1  162  ? -8.301  56.440  78.168  1.00 18.96 ? 160  ASN A OD1   1 
ATOM   1048  N  ND2   . ASN A  1  162  ? -8.288  54.720  79.617  1.00 23.24 ? 160  ASN A ND2   1 
ATOM   1049  N  N     . ASP A  1  163  ? -10.609 58.475  76.644  1.00 16.38 ? 161  ASP A N     1 
ATOM   1050  C  CA    . ASP A  1  163  ? -10.434 58.921  75.276  1.00 18.36 ? 161  ASP A CA    1 
ATOM   1051  C  C     . ASP A  1  163  ? -9.032  58.657  74.748  1.00 17.07 ? 161  ASP A C     1 
ATOM   1052  O  O     . ASP A  1  163  ? -8.855  58.539  73.534  1.00 17.80 ? 161  ASP A O     1 
ATOM   1053  C  CB    . ASP A  1  163  ? -10.828 60.406  75.131  1.00 19.77 ? 161  ASP A CB    1 
ATOM   1054  C  CG    . ASP A  1  163  ? -10.168 61.336  76.149  1.00 22.40 ? 161  ASP A CG    1 
ATOM   1055  O  OD1   . ASP A  1  163  ? -9.984  60.973  77.328  1.00 19.68 ? 161  ASP A OD1   1 
ATOM   1056  O  OD2   . ASP A  1  163  ? -9.880  62.489  75.745  1.00 22.44 ? 161  ASP A OD2   1 
ATOM   1057  N  N     . ARG A  1  164  ? -8.036  58.511  75.621  1.00 17.91 ? 162  ARG A N     1 
ATOM   1058  C  CA    A ARG A  1  164  ? -6.709  58.166  75.127  0.58 16.09 ? 162  ARG A CA    1 
ATOM   1059  C  CA    B ARG A  1  164  ? -6.702  58.160  75.147  0.42 16.14 ? 162  ARG A CA    1 
ATOM   1060  C  C     . ARG A  1  164  ? -6.639  56.696  74.734  1.00 15.43 ? 162  ARG A C     1 
ATOM   1061  O  O     . ARG A  1  164  ? -5.970  56.346  73.756  1.00 17.33 ? 162  ARG A O     1 
ATOM   1062  C  CB    A ARG A  1  164  ? -5.645  58.504  76.170  0.58 18.28 ? 162  ARG A CB    1 
ATOM   1063  C  CB    B ARG A  1  164  ? -5.668  58.464  76.230  0.42 18.29 ? 162  ARG A CB    1 
ATOM   1064  C  CG    A ARG A  1  164  ? -5.485  59.997  76.429  0.58 20.86 ? 162  ARG A CG    1 
ATOM   1065  C  CG    B ARG A  1  164  ? -5.497  59.948  76.535  0.42 20.87 ? 162  ARG A CG    1 
ATOM   1066  C  CD    A ARG A  1  164  ? -5.577  60.814  75.145  0.58 26.09 ? 162  ARG A CD    1 
ATOM   1067  C  CD    B ARG A  1  164  ? -4.870  60.682  75.361  0.42 20.27 ? 162  ARG A CD    1 
ATOM   1068  N  NE    A ARG A  1  164  ? -4.614  60.402  74.130  0.58 21.31 ? 162  ARG A NE    1 
ATOM   1069  N  NE    B ARG A  1  164  ? -5.874  61.138  74.404  0.42 28.39 ? 162  ARG A NE    1 
ATOM   1070  C  CZ    A ARG A  1  164  ? -4.701  60.704  72.840  0.58 31.68 ? 162  ARG A CZ    1 
ATOM   1071  C  CZ    B ARG A  1  164  ? -5.670  61.244  73.099  0.42 27.11 ? 162  ARG A CZ    1 
ATOM   1072  N  NH1   A ARG A  1  164  ? -5.699  61.435  72.364  0.58 28.33 ? 162  ARG A NH1   1 
ATOM   1073  N  NH1   B ARG A  1  164  ? -4.515  60.902  72.548  0.42 31.81 ? 162  ARG A NH1   1 
ATOM   1074  N  NH2   A ARG A  1  164  ? -3.766  60.257  72.003  0.58 23.13 ? 162  ARG A NH2   1 
ATOM   1075  N  NH2   B ARG A  1  164  ? -6.652  61.693  72.324  0.42 29.87 ? 162  ARG A NH2   1 
ATOM   1076  N  N     . SER A  1  165  ? -7.330  55.828  75.472  1.00 15.22 ? 163  SER A N     1 
ATOM   1077  C  CA    . SER A  1  165  ? -7.418  54.428  75.068  1.00 15.63 ? 163  SER A CA    1 
ATOM   1078  C  C     . SER A  1  165  ? -8.165  54.286  73.752  1.00 15.31 ? 163  SER A C     1 
ATOM   1079  O  O     . SER A  1  165  ? -7.760  53.506  72.874  1.00 15.50 ? 163  SER A O     1 
ATOM   1080  C  CB    . SER A  1  165  ? -8.117  53.619  76.164  1.00 16.69 ? 163  SER A CB    1 
ATOM   1081  O  OG    . SER A  1  165  ? -8.422  52.305  75.721  1.00 19.44 ? 163  SER A OG    1 
ATOM   1082  N  N     . LEU A  1  166  ? -9.262  55.044  73.595  1.00 16.35 ? 164  LEU A N     1 
ATOM   1083  C  CA    . LEU A  1  166  ? -10.026 54.988  72.354  1.00 16.52 ? 164  LEU A CA    1 
ATOM   1084  C  C     . LEU A  1  166  ? -9.231  55.545  71.184  1.00 14.98 ? 164  LEU A C     1 
ATOM   1085  O  O     . LEU A  1  166  ? -9.307  55.020  70.069  1.00 16.32 ? 164  LEU A O     1 
ATOM   1086  C  CB    . LEU A  1  166  ? -11.322 55.760  72.518  1.00 15.99 ? 164  LEU A CB    1 
ATOM   1087  C  CG    . LEU A  1  166  ? -12.264 55.045  73.471  1.00 16.05 ? 164  LEU A CG    1 
ATOM   1088  C  CD1   . LEU A  1  166  ? -13.461 55.907  73.709  1.00 19.05 ? 164  LEU A CD1   1 
ATOM   1089  C  CD2   . LEU A  1  166  ? -12.685 53.698  72.900  1.00 17.98 ? 164  LEU A CD2   1 
ATOM   1090  N  N     . ALA A  1  167  ? -8.481  56.623  71.410  1.00 15.97 ? 165  ALA A N     1 
ATOM   1091  C  CA    . ALA A  1  167  ? -7.675  57.167  70.323  1.00 18.27 ? 165  ALA A CA    1 
ATOM   1092  C  C     . ALA A  1  167  ? -6.615  56.166  69.888  1.00 15.58 ? 165  ALA A C     1 
ATOM   1093  O  O     . ALA A  1  167  ? -6.350  56.011  68.695  1.00 17.94 ? 165  ALA A O     1 
ATOM   1094  C  CB    . ALA A  1  167  ? -7.021  58.477  70.751  1.00 18.34 ? 165  ALA A CB    1 
ATOM   1095  N  N     . ALA A  1  168  ? -5.986  55.498  70.855  1.00 16.05 ? 166  ALA A N     1 
ATOM   1096  C  CA    . ALA A  1  168  ? -4.989  54.489  70.523  1.00 18.21 ? 166  ALA A CA    1 
ATOM   1097  C  C     . ALA A  1  168  ? -5.629  53.344  69.748  1.00 16.38 ? 166  ALA A C     1 
ATOM   1098  O  O     . ALA A  1  168  ? -5.083  52.869  68.742  1.00 17.30 ? 166  ALA A O     1 
ATOM   1099  C  CB    . ALA A  1  168  ? -4.337  53.983  71.816  1.00 15.40 ? 166  ALA A CB    1 
ATOM   1100  N  N     . ALA A  1  169  ? -6.805  52.908  70.204  1.00 16.97 ? 167  ALA A N     1 
ATOM   1101  C  CA    . ALA A  1  169  ? -7.496  51.802  69.563  1.00 15.83 ? 167  ALA A CA    1 
ATOM   1102  C  C     . ALA A  1  169  ? -7.904  52.154  68.137  1.00 16.05 ? 167  ALA A C     1 
ATOM   1103  O  O     . ALA A  1  169  ? -7.828  51.312  67.234  1.00 16.58 ? 167  ALA A O     1 
ATOM   1104  C  CB    . ALA A  1  169  ? -8.723  51.413  70.393  1.00 17.19 ? 167  ALA A CB    1 
ATOM   1105  N  N     . LEU A  1  170  ? -8.357  53.388  67.926  1.00 17.52 ? 168  LEU A N     1 
ATOM   1106  C  CA    . LEU A  1  170  ? -8.785  53.801  66.596  1.00 16.93 ? 168  LEU A CA    1 
ATOM   1107  C  C     . LEU A  1  170  ? -7.605  53.858  65.642  1.00 18.25 ? 168  LEU A C     1 
ATOM   1108  O  O     . LEU A  1  170  ? -7.685  53.367  64.509  1.00 18.47 ? 168  LEU A O     1 
ATOM   1109  C  CB    . LEU A  1  170  ? -9.482  55.157  66.695  1.00 17.36 ? 168  LEU A CB    1 
ATOM   1110  C  CG    . LEU A  1  170  ? -10.058 55.664  65.378  1.00 17.53 ? 168  LEU A CG    1 
ATOM   1111  C  CD1   . LEU A  1  170  ? -11.036 54.638  64.852  1.00 21.39 ? 168  LEU A CD1   1 
ATOM   1112  C  CD2   . LEU A  1  170  ? -10.750 56.981  65.621  1.00 22.13 ? 168  LEU A CD2   1 
ATOM   1113  N  N     . THR A  1  171  ? -6.486  54.441  66.089  1.00 17.26 ? 169  THR A N     1 
ATOM   1114  C  CA    . THR A  1  171  ? -5.291  54.437  65.258  1.00 18.71 ? 169  THR A CA    1 
ATOM   1115  C  C     . THR A  1  171  ? -4.879  53.014  64.932  1.00 18.17 ? 169  THR A C     1 
ATOM   1116  O  O     . THR A  1  171  ? -4.544  52.696  63.790  1.00 19.82 ? 169  THR A O     1 
ATOM   1117  C  CB    . THR A  1  171  ? -4.154  55.155  65.970  1.00 20.18 ? 169  THR A CB    1 
ATOM   1118  O  OG1   . THR A  1  171  ? -4.524  56.524  66.186  1.00 22.31 ? 169  THR A OG1   1 
ATOM   1119  C  CG2   . THR A  1  171  ? -2.857  55.074  65.173  1.00 23.91 ? 169  THR A CG2   1 
ATOM   1120  N  N     . ARG A  1  172  ? -4.915  52.140  65.936  1.00 17.35 ? 170  ARG A N     1 
ATOM   1121  C  CA    . ARG A  1  172  ? -4.491  50.763  65.732  1.00 17.20 ? 170  ARG A CA    1 
ATOM   1122  C  C     . ARG A  1  172  ? -5.385  50.060  64.720  1.00 18.07 ? 170  ARG A C     1 
ATOM   1123  O  O     . ARG A  1  172  ? -4.901  49.387  63.806  1.00 18.38 ? 170  ARG A O     1 
ATOM   1124  C  CB    . ARG A  1  172  ? -4.495  50.018  67.075  1.00 17.30 ? 170  ARG A CB    1 
ATOM   1125  C  CG    . ARG A  1  172  ? -3.778  48.682  67.005  1.00 19.26 ? 170  ARG A CG    1 
ATOM   1126  C  CD    . ARG A  1  172  ? -3.956  47.881  68.293  1.00 19.84 ? 170  ARG A CD    1 
ATOM   1127  N  NE    . ARG A  1  172  ? -3.704  48.675  69.488  1.00 17.81 ? 170  ARG A NE    1 
ATOM   1128  C  CZ    . ARG A  1  172  ? -4.645  49.124  70.312  1.00 16.38 ? 170  ARG A CZ    1 
ATOM   1129  N  NH1   . ARG A  1  172  ? -5.933  48.875  70.098  1.00 17.67 ? 170  ARG A NH1   1 
ATOM   1130  N  NH2   . ARG A  1  172  ? -4.287  49.839  71.374  1.00 16.89 ? 170  ARG A NH2   1 
ATOM   1131  N  N     . LEU A  1  173  ? -6.702  50.207  64.860  1.00 18.27 ? 171  LEU A N     1 
ATOM   1132  C  CA    . LEU A  1  173  ? -7.589  49.450  63.991  1.00 18.07 ? 171  LEU A CA    1 
ATOM   1133  C  C     . LEU A  1  173  ? -7.540  49.991  62.568  1.00 18.10 ? 171  LEU A C     1 
ATOM   1134  O  O     . LEU A  1  173  ? -7.609  49.223  61.606  1.00 18.98 ? 171  LEU A O     1 
ATOM   1135  C  CB    . LEU A  1  173  ? -9.017  49.462  64.547  1.00 19.28 ? 171  LEU A CB    1 
ATOM   1136  C  CG    . LEU A  1  173  ? -9.907  50.707  64.469  1.00 20.72 ? 171  LEU A CG    1 
ATOM   1137  C  CD1   . LEU A  1  173  ? -10.664 50.748  63.140  1.00 22.58 ? 171  LEU A CD1   1 
ATOM   1138  C  CD2   . LEU A  1  173  ? -10.895 50.739  65.624  1.00 21.78 ? 171  LEU A CD2   1 
ATOM   1139  N  N     . ILE A  1  174  ? -7.394  51.309  62.415  1.00 18.74 ? 172  ILE A N     1 
ATOM   1140  C  CA    . ILE A  1  174  ? -7.308  51.862  61.064  1.00 18.90 ? 172  ILE A CA    1 
ATOM   1141  C  C     . ILE A  1  174  ? -6.003  51.440  60.406  1.00 20.24 ? 172  ILE A C     1 
ATOM   1142  O  O     . ILE A  1  174  ? -5.986  51.021  59.241  1.00 22.12 ? 172  ILE A O     1 
ATOM   1143  C  CB    . ILE A  1  174  ? -7.464  53.393  61.107  1.00 20.28 ? 172  ILE A CB    1 
ATOM   1144  C  CG1   . ILE A  1  174  ? -8.903  53.747  61.449  1.00 22.90 ? 172  ILE A CG1   1 
ATOM   1145  C  CG2   . ILE A  1  174  ? -7.082  53.996  59.735  1.00 22.65 ? 172  ILE A CG2   1 
ATOM   1146  C  CD1   . ILE A  1  174  ? -9.114  55.207  61.766  1.00 24.17 ? 172  ILE A CD1   1 
ATOM   1147  N  N     . SER A  1  175  ? -4.892  51.513  61.144  1.00 18.75 ? 173  SER A N     1 
ATOM   1148  C  CA    . SER A  1  175  ? -3.609  51.131  60.552  1.00 19.66 ? 173  SER A CA    1 
ATOM   1149  C  C     . SER A  1  175  ? -3.563  49.645  60.251  1.00 22.39 ? 173  SER A C     1 
ATOM   1150  O  O     . SER A  1  175  ? -2.854  49.217  59.330  1.00 25.10 ? 173  SER A O     1 
ATOM   1151  C  CB    . SER A  1  175  ? -2.453  51.507  61.474  1.00 24.04 ? 173  SER A CB    1 
ATOM   1152  O  OG    . SER A  1  175  ? -2.347  52.906  61.617  1.00 28.63 ? 173  SER A OG    1 
ATOM   1153  N  N     . ARG A  1  176  ? -4.344  48.849  60.978  1.00 20.55 ? 174  ARG A N     1 
ATOM   1154  C  CA    . ARG A  1  176  ? -4.352  47.411  60.754  1.00 19.98 ? 174  ARG A CA    1 
ATOM   1155  C  C     . ARG A  1  176  ? -5.308  47.008  59.640  1.00 24.46 ? 174  ARG A C     1 
ATOM   1156  O  O     . ARG A  1  176  ? -4.955  46.181  58.791  1.00 25.65 ? 174  ARG A O     1 
ATOM   1157  C  CB    . ARG A  1  176  ? -4.731  46.698  62.060  1.00 22.03 ? 174  ARG A CB    1 
ATOM   1158  C  CG    . ARG A  1  176  ? -4.583  45.180  62.005  1.00 23.76 ? 174  ARG A CG    1 
ATOM   1159  C  CD    . ARG A  1  176  ? -4.820  44.554  63.381  1.00 23.65 ? 174  ARG A CD    1 
ATOM   1160  N  NE    . ARG A  1  176  ? -6.233  44.534  63.735  1.00 22.16 ? 174  ARG A NE    1 
ATOM   1161  C  CZ    . ARG A  1  176  ? -6.800  45.249  64.703  1.00 22.51 ? 174  ARG A CZ    1 
ATOM   1162  N  NH1   . ARG A  1  176  ? -6.088  46.014  65.532  1.00 19.80 ? 174  ARG A NH1   1 
ATOM   1163  N  NH2   . ARG A  1  176  ? -8.122  45.192  64.854  1.00 28.11 ? 174  ARG A NH2   1 
ATOM   1164  N  N     . CYS A  1  177  ? -6.505  47.597  59.610  1.00 23.47 ? 175  CYS A N     1 
ATOM   1165  C  CA    . CYS A  1  177  ? -7.568  47.131  58.736  1.00 23.91 ? 175  CYS A CA    1 
ATOM   1166  C  C     . CYS A  1  177  ? -7.974  48.119  57.654  1.00 26.19 ? 175  CYS A C     1 
ATOM   1167  O  O     . CYS A  1  177  ? -8.624  47.704  56.695  1.00 28.05 ? 175  CYS A O     1 
ATOM   1168  C  CB    . CYS A  1  177  ? -8.809  46.759  59.559  1.00 26.22 ? 175  CYS A CB    1 
ATOM   1169  S  SG    . CYS A  1  177  ? -8.433  45.547  60.863  1.00 27.00 ? 175  CYS A SG    1 
ATOM   1170  N  N     . GLY A  1  178  ? -7.654  49.404  57.800  1.00 26.57 ? 176  GLY A N     1 
ATOM   1171  C  CA    . GLY A  1  178  ? -7.846  50.348  56.712  1.00 26.38 ? 176  GLY A CA    1 
ATOM   1172  C  C     . GLY A  1  178  ? -9.293  50.671  56.369  1.00 23.47 ? 176  GLY A C     1 
ATOM   1173  O  O     . GLY A  1  178  ? -10.218 50.533  57.167  1.00 23.60 ? 176  GLY A O     1 
ATOM   1174  N  N     . GLU A  1  179  ? -9.470  51.126  55.134  1.00 28.57 ? 177  GLU A N     1 
ATOM   1175  C  CA    . GLU A  1  179  ? -10.786 51.567  54.684  1.00 26.31 ? 177  GLU A CA    1 
ATOM   1176  C  C     . GLU A  1  179  ? -11.891 50.531  54.861  1.00 23.88 ? 177  GLU A C     1 
ATOM   1177  O  O     . GLU A  1  179  ? -12.999 50.924  55.266  1.00 27.90 ? 177  GLU A O     1 
ATOM   1178  C  CB    . GLU A  1  179  ? -10.700 52.014  53.217  1.00 27.41 ? 177  GLU A CB    1 
ATOM   1179  C  CG    . GLU A  1  179  ? -11.995 52.644  52.712  1.00 33.96 ? 177  GLU A CG    1 
ATOM   1180  C  CD    . GLU A  1  179  ? -12.897 51.654  51.993  1.00 50.35 ? 177  GLU A CD    1 
ATOM   1181  O  OE1   . GLU A  1  179  ? -12.397 50.589  51.568  1.00 49.55 ? 177  GLU A OE1   1 
ATOM   1182  O  OE2   . GLU A  1  179  ? -14.108 51.943  51.850  1.00 58.76 ? 177  GLU A OE2   1 
ATOM   1183  N  N     . PRO A  1  180  ? -11.689 49.237  54.582  1.00 22.78 ? 178  PRO A N     1 
ATOM   1184  C  CA    . PRO A  1  180  ? -12.810 48.297  54.721  1.00 25.23 ? 178  PRO A CA    1 
ATOM   1185  C  C     . PRO A  1  180  ? -13.459 48.300  56.094  1.00 24.70 ? 178  PRO A C     1 
ATOM   1186  O  O     . PRO A  1  180  ? -14.692 48.201  56.182  1.00 25.90 ? 178  PRO A O     1 
ATOM   1187  C  CB    . PRO A  1  180  ? -12.164 46.947  54.395  1.00 27.49 ? 178  PRO A CB    1 
ATOM   1188  C  CG    . PRO A  1  180  ? -11.082 47.295  53.433  1.00 26.37 ? 178  PRO A CG    1 
ATOM   1189  C  CD    . PRO A  1  180  ? -10.524 48.591  53.949  1.00 27.51 ? 178  PRO A CD    1 
ATOM   1190  N  N     . VAL A  1  181  ? -12.679 48.417  57.173  1.00 23.10 ? 179  VAL A N     1 
ATOM   1191  C  CA    . VAL A  1  181  ? -13.311 48.408  58.487  1.00 21.33 ? 179  VAL A CA    1 
ATOM   1192  C  C     . VAL A  1  181  ? -14.050 49.723  58.741  1.00 24.88 ? 179  VAL A C     1 
ATOM   1193  O  O     . VAL A  1  181  ? -15.090 49.733  59.404  1.00 23.52 ? 179  VAL A O     1 
ATOM   1194  C  CB    . VAL A  1  181  ? -12.278 48.088  59.591  1.00 21.27 ? 179  VAL A CB    1 
ATOM   1195  C  CG1   . VAL A  1  181  ? -11.335 49.262  59.860  1.00 22.36 ? 179  VAL A CG1   1 
ATOM   1196  C  CG2   . VAL A  1  181  ? -12.992 47.686  60.874  1.00 26.06 ? 179  VAL A CG2   1 
ATOM   1197  N  N     . ILE A  1  182  ? -13.543 50.844  58.213  1.00 23.81 ? 180  ILE A N     1 
ATOM   1198  C  CA    . ILE A  1  182  ? -14.227 52.121  58.378  1.00 25.30 ? 180  ILE A CA    1 
ATOM   1199  C  C     . ILE A  1  182  ? -15.558 52.091  57.649  1.00 27.71 ? 180  ILE A C     1 
ATOM   1200  O  O     . ILE A  1  182  ? -16.589 52.520  58.182  1.00 25.18 ? 180  ILE A O     1 
ATOM   1201  C  CB    . ILE A  1  182  ? -13.348 53.280  57.876  1.00 24.04 ? 180  ILE A CB    1 
ATOM   1202  C  CG1   . ILE A  1  182  ? -12.029 53.338  58.640  1.00 23.63 ? 180  ILE A CG1   1 
ATOM   1203  C  CG2   . ILE A  1  182  ? -14.086 54.603  58.045  1.00 24.80 ? 180  ILE A CG2   1 
ATOM   1204  C  CD1   . ILE A  1  182  ? -10.966 54.176  57.946  1.00 29.25 ? 180  ILE A CD1   1 
ATOM   1205  N  N     . ARG A  1  183  ? -15.549 51.580  56.421  1.00 25.88 ? 181  ARG A N     1 
ATOM   1206  C  CA    . ARG A  1  183  ? -16.780 51.455  55.647  1.00 28.43 ? 181  ARG A CA    1 
ATOM   1207  C  C     . ARG A  1  183  ? -17.808 50.610  56.390  1.00 30.76 ? 181  ARG A C     1 
ATOM   1208  O  O     . ARG A  1  183  ? -18.983 50.989  56.496  1.00 29.69 ? 181  ARG A O     1 
ATOM   1209  C  CB    . ARG A  1  183  ? -16.455 50.860  54.275  1.00 32.05 ? 181  ARG A CB    1 
ATOM   1210  C  CG    . ARG A  1  183  ? -17.649 50.445  53.416  1.00 39.22 ? 181  ARG A CG    1 
ATOM   1211  C  CD    . ARG A  1  183  ? -18.722 51.521  53.357  1.00 42.13 ? 181  ARG A CD    1 
ATOM   1212  N  NE    . ARG A  1  183  ? -18.203 52.814  52.938  1.00 43.27 ? 181  ARG A NE    1 
ATOM   1213  C  CZ    . ARG A  1  183  ? -18.819 53.965  53.165  1.00 48.02 ? 181  ARG A CZ    1 
ATOM   1214  N  NH1   . ARG A  1  183  ? -19.956 54.019  53.841  1.00 43.38 ? 181  ARG A NH1   1 
ATOM   1215  N  NH2   . ARG A  1  183  ? -18.279 55.091  52.706  1.00 47.00 ? 181  ARG A NH2   1 
ATOM   1216  N  N     . ARG A  1  184  ? -17.380 49.466  56.924  1.00 24.89 ? 182  ARG A N     1 
ATOM   1217  C  CA    . ARG A  1  184  ? -18.309 48.600  57.643  1.00 27.52 ? 182  ARG A CA    1 
ATOM   1218  C  C     . ARG A  1  184  ? -18.820 49.268  58.913  1.00 24.75 ? 182  ARG A C     1 
ATOM   1219  O  O     . ARG A  1  184  ? -19.996 49.120  59.268  1.00 27.69 ? 182  ARG A O     1 
ATOM   1220  C  CB    . ARG A  1  184  ? -17.638 47.270  57.964  1.00 29.59 ? 182  ARG A CB    1 
ATOM   1221  C  CG    . ARG A  1  184  ? -17.604 46.307  56.786  1.00 36.31 ? 182  ARG A CG    1 
ATOM   1222  C  CD    . ARG A  1  184  ? -18.850 45.419  56.757  1.00 34.07 ? 182  ARG A CD    1 
ATOM   1223  N  NE    . ARG A  1  184  ? -18.697 44.256  57.625  1.00 39.15 ? 182  ARG A NE    1 
ATOM   1224  C  CZ    . ARG A  1  184  ? -19.457 43.983  58.677  1.00 37.36 ? 182  ARG A CZ    1 
ATOM   1225  N  NH1   . ARG A  1  184  ? -20.473 44.761  59.023  1.00 38.39 ? 182  ARG A NH1   1 
ATOM   1226  N  NH2   . ARG A  1  184  ? -19.197 42.894  59.397  1.00 35.93 ? 182  ARG A NH2   1 
ATOM   1227  N  N     . GLY A  1  185  ? -17.958 50.008  59.606  1.00 24.60 ? 183  GLY A N     1 
ATOM   1228  C  CA    . GLY A  1  185  ? -18.404 50.731  60.786  1.00 23.53 ? 183  GLY A CA    1 
ATOM   1229  C  C     . GLY A  1  185  ? -19.408 51.817  60.447  1.00 27.81 ? 183  GLY A C     1 
ATOM   1230  O  O     . GLY A  1  185  ? -20.410 51.985  61.145  1.00 26.55 ? 183  GLY A O     1 
ATOM   1231  N  N     . VAL A  1  186  ? -19.154 52.566  59.371  1.00 25.84 ? 184  VAL A N     1 
ATOM   1232  C  CA    . VAL A  1  186  ? -20.080 53.617  58.957  1.00 28.22 ? 184  VAL A CA    1 
ATOM   1233  C  C     . VAL A  1  186  ? -21.430 53.022  58.593  1.00 25.60 ? 184  VAL A C     1 
ATOM   1234  O  O     . VAL A  1  186  ? -22.481 53.533  59.001  1.00 26.19 ? 184  VAL A O     1 
ATOM   1235  C  CB    . VAL A  1  186  ? -19.487 54.423  57.787  1.00 29.47 ? 184  VAL A CB    1 
ATOM   1236  C  CG1   . VAL A  1  186  ? -20.573 55.279  57.112  1.00 29.34 ? 184  VAL A CG1   1 
ATOM   1237  C  CG2   . VAL A  1  186  ? -18.360 55.290  58.273  1.00 28.23 ? 184  VAL A CG2   1 
ATOM   1238  N  N     . ASP A  1  187  ? -21.427 51.934  57.827  1.00 28.64 ? 185  ASP A N     1 
ATOM   1239  C  CA    . ASP A  1  187  ? -22.690 51.323  57.424  1.00 28.98 ? 185  ASP A CA    1 
ATOM   1240  C  C     . ASP A  1  187  ? -23.441 50.772  58.629  1.00 32.80 ? 185  ASP A C     1 
ATOM   1241  O  O     . ASP A  1  187  ? -24.675 50.855  58.692  1.00 29.30 ? 185  ASP A O     1 
ATOM   1242  C  CB    . ASP A  1  187  ? -22.440 50.226  56.394  1.00 34.35 ? 185  ASP A CB    1 
ATOM   1243  C  CG    . ASP A  1  187  ? -21.902 50.772  55.081  1.00 35.27 ? 185  ASP A CG    1 
ATOM   1244  O  OD1   . ASP A  1  187  ? -22.030 51.993  54.847  1.00 39.67 ? 185  ASP A OD1   1 
ATOM   1245  O  OD2   . ASP A  1  187  ? -21.354 49.984  54.287  1.00 36.30 ? 185  ASP A OD2   1 
ATOM   1246  N  N     . MET A  1  188  ? -22.711 50.219  59.600  1.00 28.19 ? 186  MET A N     1 
ATOM   1247  C  CA    . MET A  1  188  ? -23.334 49.720  60.823  1.00 27.46 ? 186  MET A CA    1 
ATOM   1248  C  C     . MET A  1  188  ? -23.942 50.851  61.642  1.00 31.34 ? 186  MET A C     1 
ATOM   1249  O  O     . MET A  1  188  ? -25.099 50.766  62.077  1.00 30.02 ? 186  MET A O     1 
ATOM   1250  C  CB    . MET A  1  188  ? -22.297 48.961  61.649  1.00 31.83 ? 186  MET A CB    1 
ATOM   1251  C  CG    . MET A  1  188  ? -22.841 48.334  62.914  1.00 36.10 ? 186  MET A CG    1 
ATOM   1252  S  SD    . MET A  1  188  ? -23.995 47.022  62.502  1.00 45.76 ? 186  MET A SD    1 
ATOM   1253  C  CE    . MET A  1  188  ? -22.964 46.035  61.404  1.00 36.61 ? 186  MET A CE    1 
ATOM   1254  N  N     . ALA A  1  189  ? -23.172 51.914  61.881  1.00 27.30 ? 187  ALA A N     1 
ATOM   1255  C  CA    . ALA A  1  189  ? -23.688 53.025  62.670  1.00 26.26 ? 187  ALA A CA    1 
ATOM   1256  C  C     . ALA A  1  189  ? -24.847 53.708  61.960  1.00 29.81 ? 187  ALA A C     1 
ATOM   1257  O  O     . ALA A  1  189  ? -25.791 54.172  62.611  1.00 25.55 ? 187  ALA A O     1 
ATOM   1258  C  CB    . ALA A  1  189  ? -22.576 54.028  62.968  1.00 26.85 ? 187  ALA A CB    1 
ATOM   1259  N  N     . MET A  1  190  ? -24.789 53.784  60.626  1.00 26.25 ? 188  MET A N     1 
ATOM   1260  C  CA    . MET A  1  190  ? -25.891 54.376  59.871  1.00 27.23 ? 188  MET A CA    1 
ATOM   1261  C  C     . MET A  1  190  ? -27.174 53.580  60.061  1.00 29.38 ? 188  MET A C     1 
ATOM   1262  O  O     . MET A  1  190  ? -28.242 54.158  60.295  1.00 31.36 ? 188  MET A O     1 
ATOM   1263  C  CB    . MET A  1  190  ? -25.537 54.460  58.386  1.00 28.54 ? 188  MET A CB    1 
ATOM   1264  C  CG    . MET A  1  190  ? -26.502 55.295  57.564  1.00 37.57 ? 188  MET A CG    1 
ATOM   1265  S  SD    . MET A  1  190  ? -26.120 55.271  55.794  1.00 44.52 ? 188  MET A SD    1 
ATOM   1266  C  CE    . MET A  1  190  ? -24.407 55.785  55.791  1.00 40.36 ? 188  MET A CE    1 
ATOM   1267  N  N     . ARG A  1  191  ? -27.084 52.252  59.976  1.00 27.81 ? 189  ARG A N     1 
ATOM   1268  C  CA    . ARG A  1  191  ? -28.254 51.409  60.200  1.00 28.25 ? 189  ARG A CA    1 
ATOM   1269  C  C     . ARG A  1  191  ? -28.760 51.533  61.631  1.00 30.61 ? 189  ARG A C     1 
ATOM   1270  O  O     . ARG A  1  191  ? -29.971 51.645  61.869  1.00 31.90 ? 189  ARG A O     1 
ATOM   1271  C  CB    . ARG A  1  191  ? -27.917 49.954  59.876  1.00 27.67 ? 189  ARG A CB    1 
ATOM   1272  N  N     . MET A  1  192  ? -27.850 51.508  62.605  1.00 27.59 ? 190  MET A N     1 
ATOM   1273  C  CA    . MET A  1  192  ? -28.286 51.503  63.997  1.00 23.76 ? 190  MET A CA    1 
ATOM   1274  C  C     . MET A  1  192  ? -28.943 52.821  64.370  1.00 28.77 ? 190  MET A C     1 
ATOM   1275  O  O     . MET A  1  192  ? -30.001 52.841  65.007  1.00 25.96 ? 190  MET A O     1 
ATOM   1276  C  CB    . MET A  1  192  ? -27.102 51.212  64.918  1.00 26.38 ? 190  MET A CB    1 
ATOM   1277  C  CG    . MET A  1  192  ? -26.579 49.795  64.772  1.00 25.59 ? 190  MET A CG    1 
ATOM   1278  S  SD    . MET A  1  192  ? -25.272 49.485  65.967  1.00 40.43 ? 190  MET A SD    1 
ATOM   1279  C  CE    . MET A  1  192  ? -26.252 49.187  67.427  1.00 38.55 ? 190  MET A CE    1 
ATOM   1280  N  N     . MET A  1  193  ? -28.330 53.935  63.995  1.00 26.55 ? 191  MET A N     1 
ATOM   1281  C  CA    A MET A  1  193  ? -28.856 55.234  64.389  0.51 28.67 ? 191  MET A CA    1 
ATOM   1282  C  CA    B MET A  1  193  ? -28.868 55.224  64.399  0.49 28.67 ? 191  MET A CA    1 
ATOM   1283  C  C     . MET A  1  193  ? -30.023 55.683  63.523  1.00 27.49 ? 191  MET A C     1 
ATOM   1284  O  O     . MET A  1  193  ? -30.779 56.565  63.939  1.00 29.58 ? 191  MET A O     1 
ATOM   1285  C  CB    A MET A  1  193  ? -27.746 56.282  64.339  0.51 28.00 ? 191  MET A CB    1 
ATOM   1286  C  CB    B MET A  1  193  ? -27.761 56.275  64.401  0.49 27.99 ? 191  MET A CB    1 
ATOM   1287  C  CG    A MET A  1  193  ? -26.493 55.881  65.091  0.51 25.78 ? 191  MET A CG    1 
ATOM   1288  C  CG    B MET A  1  193  ? -26.757 56.078  65.518  0.49 24.71 ? 191  MET A CG    1 
ATOM   1289  S  SD    A MET A  1  193  ? -25.201 57.114  64.889  0.51 28.67 ? 191  MET A SD    1 
ATOM   1290  S  SD    B MET A  1  193  ? -25.670 57.498  65.695  0.49 29.63 ? 191  MET A SD    1 
ATOM   1291  C  CE    A MET A  1  193  ? -25.748 58.339  66.076  0.51 34.14 ? 191  MET A CE    1 
ATOM   1292  C  CE    B MET A  1  193  ? -24.738 57.414  64.165  0.49 30.15 ? 191  MET A CE    1 
ATOM   1293  N  N     . GLY A  1  194  ? -30.187 55.104  62.339  1.00 29.11 ? 192  GLY A N     1 
ATOM   1294  C  CA    . GLY A  1  194  ? -31.259 55.520  61.458  1.00 27.17 ? 192  GLY A CA    1 
ATOM   1295  C  C     . GLY A  1  194  ? -32.456 54.590  61.462  1.00 33.73 ? 192  GLY A C     1 
ATOM   1296  O  O     . GLY A  1  194  ? -33.572 55.019  61.148  1.00 33.06 ? 192  GLY A O     1 
ATOM   1297  N  N     . GLU A  1  195  ? -32.248 53.320  61.824  1.00 25.98 ? 193  GLU A N     1 
ATOM   1298  C  CA    . GLU A  1  195  ? -33.296 52.310  61.719  1.00 29.78 ? 193  GLU A CA    1 
ATOM   1299  C  C     . GLU A  1  195  ? -33.510 51.474  62.970  1.00 26.37 ? 193  GLU A C     1 
ATOM   1300  O  O     . GLU A  1  195  ? -34.557 50.822  63.071  1.00 24.95 ? 193  GLU A O     1 
ATOM   1301  C  CB    . GLU A  1  195  ? -33.001 51.357  60.548  1.00 29.31 ? 193  GLU A CB    1 
ATOM   1302  C  CG    . GLU A  1  195  ? -32.788 52.064  59.222  1.00 46.09 ? 193  GLU A CG    1 
ATOM   1303  C  CD    . GLU A  1  195  ? -32.367 51.116  58.115  1.00 45.76 ? 193  GLU A CD    1 
ATOM   1304  O  OE1   . GLU A  1  195  ? -31.733 50.082  58.418  1.00 50.22 ? 193  GLU A OE1   1 
ATOM   1305  O  OE2   . GLU A  1  195  ? -32.676 51.409  56.941  1.00 56.82 ? 193  GLU A OE2   1 
ATOM   1306  N  N     . GLN A  1  196  ? -32.578 51.462  63.920  1.00 27.97 ? 194  GLN A N     1 
ATOM   1307  C  CA    . GLN A  1  196  ? -32.674 50.595  65.088  1.00 26.91 ? 194  GLN A CA    1 
ATOM   1308  C  C     . GLN A  1  196  ? -32.968 51.356  66.372  1.00 29.57 ? 194  GLN A C     1 
ATOM   1309  O  O     . GLN A  1  196  ? -33.919 51.027  67.085  1.00 34.61 ? 194  GLN A O     1 
ATOM   1310  C  CB    . GLN A  1  196  ? -31.375 49.791  65.243  1.00 33.08 ? 194  GLN A CB    1 
ATOM   1311  C  CG    . GLN A  1  196  ? -31.370 48.851  66.432  1.00 45.46 ? 194  GLN A CG    1 
ATOM   1312  C  CD    . GLN A  1  196  ? -30.096 48.037  66.513  1.00 43.53 ? 194  GLN A CD    1 
ATOM   1313  O  OE1   . GLN A  1  196  ? -29.428 47.806  65.503  1.00 45.28 ? 194  GLN A OE1   1 
ATOM   1314  N  NE2   . GLN A  1  196  ? -29.749 47.601  67.720  1.00 51.14 ? 194  GLN A NE2   1 
ATOM   1315  N  N     . PHE A  1  197  ? -32.166 52.369  66.692  1.00 27.25 ? 195  PHE A N     1 
ATOM   1316  C  CA    . PHE A  1  197  ? -32.438 53.182  67.869  1.00 27.00 ? 195  PHE A CA    1 
ATOM   1317  C  C     . PHE A  1  197  ? -33.608 54.110  67.646  1.00 24.90 ? 195  PHE A C     1 
ATOM   1318  O  O     . PHE A  1  197  ? -34.201 54.597  68.616  1.00 26.59 ? 195  PHE A O     1 
ATOM   1319  C  CB    . PHE A  1  197  ? -31.220 54.013  68.238  1.00 26.10 ? 195  PHE A CB    1 
ATOM   1320  C  CG    . PHE A  1  197  ? -30.012 53.195  68.565  1.00 36.51 ? 195  PHE A CG    1 
ATOM   1321  C  CD1   . PHE A  1  197  ? -30.128 52.042  69.319  1.00 35.09 ? 195  PHE A CD1   1 
ATOM   1322  C  CD2   . PHE A  1  197  ? -28.764 53.579  68.114  1.00 34.79 ? 195  PHE A CD2   1 
ATOM   1323  C  CE1   . PHE A  1  197  ? -29.015 51.285  69.624  1.00 40.08 ? 195  PHE A CE1   1 
ATOM   1324  C  CE2   . PHE A  1  197  ? -27.646 52.823  68.415  1.00 37.09 ? 195  PHE A CE2   1 
ATOM   1325  C  CZ    . PHE A  1  197  ? -27.779 51.678  69.170  1.00 33.37 ? 195  PHE A CZ    1 
ATOM   1326  N  N     . VAL A  1  198  ? -33.920 54.394  66.391  1.00 25.31 ? 196  VAL A N     1 
ATOM   1327  C  CA    . VAL A  1  198  ? -35.111 55.141  66.031  1.00 23.63 ? 196  VAL A CA    1 
ATOM   1328  C  C     . VAL A  1  198  ? -35.813 54.383  64.919  1.00 23.30 ? 196  VAL A C     1 
ATOM   1329  O  O     . VAL A  1  198  ? -35.198 53.621  64.168  1.00 25.90 ? 196  VAL A O     1 
ATOM   1330  C  CB    . VAL A  1  198  ? -34.793 56.595  65.600  1.00 23.54 ? 196  VAL A CB    1 
ATOM   1331  C  CG1   . VAL A  1  198  ? -34.115 57.351  66.734  1.00 22.76 ? 196  VAL A CG1   1 
ATOM   1332  C  CG2   . VAL A  1  198  ? -33.950 56.632  64.325  1.00 23.00 ? 196  VAL A CG2   1 
ATOM   1333  N  N     . THR A  1  199  ? -37.124 54.565  64.843  1.00 20.17 ? 197  THR A N     1 
ATOM   1334  C  CA    . THR A  1  199  ? -37.845 54.049  63.694  1.00 21.62 ? 197  THR A CA    1 
ATOM   1335  C  C     . THR A  1  199  ? -37.542 54.891  62.470  1.00 25.21 ? 197  THR A C     1 
ATOM   1336  O  O     . THR A  1  199  ? -37.506 54.370  61.354  1.00 27.44 ? 197  THR A O     1 
ATOM   1337  C  CB    . THR A  1  199  ? -39.344 54.020  63.996  1.00 25.23 ? 197  THR A CB    1 
ATOM   1338  O  OG1   . THR A  1  199  ? -39.554 53.265  65.198  1.00 25.21 ? 197  THR A OG1   1 
ATOM   1339  C  CG2   . THR A  1  199  ? -40.111 53.368  62.862  1.00 26.36 ? 197  THR A CG2   1 
ATOM   1340  N  N     . GLY A  1  200  ? -37.286 56.175  62.666  1.00 24.10 ? 198  GLY A N     1 
ATOM   1341  C  CA    . GLY A  1  200  ? -36.882 57.032  61.572  1.00 23.81 ? 198  GLY A CA    1 
ATOM   1342  C  C     . GLY A  1  200  ? -36.329 58.333  62.102  1.00 27.60 ? 198  GLY A C     1 
ATOM   1343  O  O     . GLY A  1  200  ? -36.527 58.685  63.269  1.00 24.02 ? 198  GLY A O     1 
ATOM   1344  N  N     . GLU A  1  201  ? -35.612 59.037  61.226  1.00 26.31 ? 199  GLU A N     1 
ATOM   1345  C  CA    . GLU A  1  201  ? -35.037 60.323  61.607  1.00 26.68 ? 199  GLU A CA    1 
ATOM   1346  C  C     . GLU A  1  201  ? -36.113 61.390  61.740  1.00 23.12 ? 199  GLU A C     1 
ATOM   1347  O  O     . GLU A  1  201  ? -36.002 62.292  62.578  1.00 27.13 ? 199  GLU A O     1 
ATOM   1348  C  CB    . GLU A  1  201  ? -33.993 60.748  60.570  1.00 24.64 ? 199  GLU A CB    1 
ATOM   1349  C  CG    . GLU A  1  201  ? -33.403 62.125  60.810  1.00 34.18 ? 199  GLU A CG    1 
ATOM   1350  C  CD    . GLU A  1  201  ? -32.464 62.551  59.692  1.00 50.33 ? 199  GLU A CD    1 
ATOM   1351  O  OE1   . GLU A  1  201  ? -32.098 61.692  58.861  1.00 49.91 ? 199  GLU A OE1   1 
ATOM   1352  O  OE2   . GLU A  1  201  ? -32.098 63.745  59.642  1.00 58.14 ? 199  GLU A OE2   1 
ATOM   1353  N  N     . THR A  1  202  ? -37.154 61.299  60.924  1.00 24.09 ? 200  THR A N     1 
ATOM   1354  C  CA    . THR A  1  202  ? -38.269 62.229  60.939  1.00 22.76 ? 200  THR A CA    1 
ATOM   1355  C  C     . THR A  1  202  ? -39.556 61.428  61.034  1.00 21.59 ? 200  THR A C     1 
ATOM   1356  O  O     . THR A  1  202  ? -39.585 60.229  60.749  1.00 22.90 ? 200  THR A O     1 
ATOM   1357  C  CB    . THR A  1  202  ? -38.320 63.072  59.672  1.00 24.72 ? 200  THR A CB    1 
ATOM   1358  O  OG1   . THR A  1  202  ? -38.613 62.201  58.571  1.00 27.97 ? 200  THR A OG1   1 
ATOM   1359  C  CG2   . THR A  1  202  ? -36.968 63.762  59.424  1.00 28.83 ? 200  THR A CG2   1 
ATOM   1360  N  N     . ILE A  1  203  ? -40.640 62.113  61.398  1.00 19.83 ? 201  ILE A N     1 
ATOM   1361  C  CA    . ILE A  1  203  ? -41.910 61.410  61.555  1.00 20.74 ? 201  ILE A CA    1 
ATOM   1362  C  C     . ILE A  1  203  ? -42.379 60.850  60.215  1.00 21.14 ? 201  ILE A C     1 
ATOM   1363  O  O     . ILE A  1  203  ? -42.916 59.741  60.151  1.00 22.29 ? 201  ILE A O     1 
ATOM   1364  C  CB    . ILE A  1  203  ? -42.959 62.325  62.223  1.00 21.29 ? 201  ILE A CB    1 
ATOM   1365  C  CG1   . ILE A  1  203  ? -44.238 61.542  62.558  1.00 18.63 ? 201  ILE A CG1   1 
ATOM   1366  C  CG2   . ILE A  1  203  ? -43.292 63.539  61.350  1.00 24.27 ? 201  ILE A CG2   1 
ATOM   1367  C  CD1   . ILE A  1  203  ? -43.990 60.347  63.467  1.00 18.91 ? 201  ILE A CD1   1 
ATOM   1368  N  N     . ARG A  1  204  ? -42.115 61.563  59.114  1.00 24.23 ? 202  ARG A N     1 
ATOM   1369  C  CA    . ARG A  1  204  ? -42.484 61.038  57.801  1.00 23.84 ? 202  ARG A CA    1 
ATOM   1370  C  C     . ARG A  1  204  ? -41.736 59.754  57.480  1.00 24.43 ? 202  ARG A C     1 
ATOM   1371  O  O     . ARG A  1  204  ? -42.327 58.790  56.981  1.00 23.63 ? 202  ARG A O     1 
ATOM   1372  C  CB    . ARG A  1  204  ? -42.215 62.082  56.725  1.00 29.37 ? 202  ARG A CB    1 
ATOM   1373  C  CG    . ARG A  1  204  ? -43.369 63.004  56.504  1.00 38.85 ? 202  ARG A CG    1 
ATOM   1374  C  CD    . ARG A  1  204  ? -42.929 64.316  55.880  1.00 38.26 ? 202  ARG A CD    1 
ATOM   1375  N  NE    . ARG A  1  204  ? -44.066 65.221  55.809  1.00 36.97 ? 202  ARG A NE    1 
ATOM   1376  C  CZ    . ARG A  1  204  ? -44.578 65.855  56.855  1.00 40.43 ? 202  ARG A CZ    1 
ATOM   1377  N  NH1   . ARG A  1  204  ? -44.044 65.737  58.065  1.00 28.45 ? 202  ARG A NH1   1 
ATOM   1378  N  NH2   . ARG A  1  204  ? -45.654 66.619  56.684  1.00 32.89 ? 202  ARG A NH2   1 
ATOM   1379  N  N     . GLU A  1  205  ? -40.431 59.728  57.751  1.00 25.02 ? 203  GLU A N     1 
ATOM   1380  C  CA    . GLU A  1  205  ? -39.660 58.508  57.547  1.00 24.72 ? 203  GLU A CA    1 
ATOM   1381  C  C     . GLU A  1  205  ? -40.152 57.396  58.459  1.00 24.92 ? 203  GLU A C     1 
ATOM   1382  O  O     . GLU A  1  205  ? -40.285 56.243  58.029  1.00 25.09 ? 203  GLU A O     1 
ATOM   1383  C  CB    . GLU A  1  205  ? -38.182 58.787  57.796  1.00 26.68 ? 203  GLU A CB    1 
ATOM   1384  C  CG    . GLU A  1  205  ? -37.258 57.672  57.408  1.00 33.48 ? 203  GLU A CG    1 
ATOM   1385  C  CD    . GLU A  1  205  ? -35.808 58.080  57.566  1.00 43.79 ? 203  GLU A CD    1 
ATOM   1386  O  OE1   . GLU A  1  205  ? -35.336 58.140  58.718  1.00 34.46 ? 203  GLU A OE1   1 
ATOM   1387  O  OE2   . GLU A  1  205  ? -35.150 58.367  56.541  1.00 47.41 ? 203  GLU A OE2   1 
ATOM   1388  N  N     . ALA A  1  206  ? -40.444 57.726  59.721  1.00 22.24 ? 204  ALA A N     1 
ATOM   1389  C  CA    . ALA A  1  206  ? -40.910 56.708  60.653  1.00 24.55 ? 204  ALA A CA    1 
ATOM   1390  C  C     . ALA A  1  206  ? -42.227 56.114  60.193  1.00 21.62 ? 204  ALA A C     1 
ATOM   1391  O  O     . ALA A  1  206  ? -42.422 54.892  60.255  1.00 24.70 ? 204  ALA A O     1 
ATOM   1392  C  CB    . ALA A  1  206  ? -41.051 57.301  62.054  1.00 22.49 ? 204  ALA A CB    1 
ATOM   1393  N  N     . LEU A  1  207  ? -43.140 56.966  59.719  1.00 22.00 ? 205  LEU A N     1 
ATOM   1394  C  CA    . LEU A  1  207  ? -44.430 56.483  59.233  1.00 21.33 ? 205  LEU A CA    1 
ATOM   1395  C  C     . LEU A  1  207  ? -44.265 55.587  58.017  1.00 26.98 ? 205  LEU A C     1 
ATOM   1396  O  O     . LEU A  1  207  ? -44.978 54.586  57.878  1.00 29.36 ? 205  LEU A O     1 
ATOM   1397  C  CB    . LEU A  1  207  ? -45.338 57.666  58.906  1.00 23.38 ? 205  LEU A CB    1 
ATOM   1398  C  CG    . LEU A  1  207  ? -45.844 58.423  60.131  1.00 23.17 ? 205  LEU A CG    1 
ATOM   1399  C  CD1   . LEU A  1  207  ? -46.425 59.767  59.717  1.00 22.26 ? 205  LEU A CD1   1 
ATOM   1400  C  CD2   . LEU A  1  207  ? -46.870 57.570  60.885  1.00 19.98 ? 205  LEU A CD2   1 
ATOM   1401  N  N     . LYS A  1  208  ? -43.338 55.937  57.117  1.00 25.43 ? 206  LYS A N     1 
ATOM   1402  C  CA    . LYS A  1  208  ? -43.084 55.094  55.955  1.00 27.64 ? 206  LYS A CA    1 
ATOM   1403  C  C     . LYS A  1  208  ? -42.637 53.706  56.382  1.00 27.27 ? 206  LYS A C     1 
ATOM   1404  O  O     . LYS A  1  208  ? -43.087 52.701  55.820  1.00 31.82 ? 206  LYS A O     1 
ATOM   1405  C  CB    . LYS A  1  208  ? -42.033 55.744  55.051  1.00 27.40 ? 206  LYS A CB    1 
ATOM   1406  N  N     . ARG A  1  209  ? -41.779 53.629  57.395  1.00 26.20 ? 207  ARG A N     1 
ATOM   1407  C  CA    . ARG A  1  209  ? -41.222 52.362  57.840  1.00 28.95 ? 207  ARG A CA    1 
ATOM   1408  C  C     . ARG A  1  209  ? -42.162 51.577  58.742  1.00 31.30 ? 207  ARG A C     1 
ATOM   1409  O  O     . ARG A  1  209  ? -41.832 50.447  59.115  1.00 31.97 ? 207  ARG A O     1 
ATOM   1410  C  CB    . ARG A  1  209  ? -39.899 52.612  58.552  1.00 29.34 ? 207  ARG A CB    1 
ATOM   1411  C  CG    . ARG A  1  209  ? -38.845 53.113  57.593  1.00 33.85 ? 207  ARG A CG    1 
ATOM   1412  C  CD    . ARG A  1  209  ? -37.686 53.716  58.334  1.00 31.95 ? 207  ARG A CD    1 
ATOM   1413  N  NE    . ARG A  1  209  ? -36.606 54.082  57.430  1.00 41.19 ? 207  ARG A NE    1 
ATOM   1414  C  CZ    . ARG A  1  209  ? -35.429 54.535  57.835  1.00 44.16 ? 207  ARG A CZ    1 
ATOM   1415  N  NH1   . ARG A  1  209  ? -35.158 54.695  59.119  1.00 37.14 ? 207  ARG A NH1   1 
ATOM   1416  N  NH2   . ARG A  1  209  ? -34.501 54.833  56.928  1.00 46.90 ? 207  ARG A NH2   1 
ATOM   1417  N  N     . SER A  1  210  ? -43.317 52.138  59.095  1.00 28.11 ? 208  SER A N     1 
ATOM   1418  C  CA    . SER A  1  210  ? -44.249 51.457  59.982  1.00 26.59 ? 208  SER A CA    1 
ATOM   1419  C  C     . SER A  1  210  ? -45.235 50.557  59.250  1.00 29.90 ? 208  SER A C     1 
ATOM   1420  O  O     . SER A  1  210  ? -45.848 49.693  59.885  1.00 26.96 ? 208  SER A O     1 
ATOM   1421  C  CB    . SER A  1  210  ? -45.019 52.487  60.808  1.00 26.23 ? 208  SER A CB    1 
ATOM   1422  O  OG    . SER A  1  210  ? -44.104 53.264  61.559  1.00 26.03 ? 208  SER A OG    1 
ATOM   1423  N  N     . LYS A  1  211  ? -45.391 50.729  57.937  1.00 29.89 ? 209  LYS A N     1 
ATOM   1424  C  CA    . LYS A  1  211  ? -46.440 50.021  57.207  1.00 32.77 ? 209  LYS A CA    1 
ATOM   1425  C  C     . LYS A  1  211  ? -46.234 48.511  57.243  1.00 29.49 ? 209  LYS A C     1 
ATOM   1426  O  O     . LYS A  1  211  ? -47.204 47.754  57.368  1.00 30.14 ? 209  LYS A O     1 
ATOM   1427  C  CB    . LYS A  1  211  ? -46.489 50.525  55.768  1.00 37.08 ? 209  LYS A CB    1 
ATOM   1428  C  CG    . LYS A  1  211  ? -46.165 52.008  55.648  1.00 39.37 ? 209  LYS A CG    1 
ATOM   1429  C  CD    . LYS A  1  211  ? -46.802 52.645  54.431  1.00 44.90 ? 209  LYS A CD    1 
ATOM   1430  C  CE    . LYS A  1  211  ? -48.197 53.148  54.765  1.00 51.90 ? 209  LYS A CE    1 
ATOM   1431  N  NZ    . LYS A  1  211  ? -48.189 53.939  56.032  1.00 52.73 ? 209  LYS A NZ    1 
ATOM   1432  N  N     . GLU A  1  212  ? -44.982 48.060  57.157  1.00 31.13 ? 210  GLU A N     1 
ATOM   1433  C  CA    . GLU A  1  212  ? -44.700 46.629  57.094  1.00 35.73 ? 210  GLU A CA    1 
ATOM   1434  C  C     . GLU A  1  212  ? -45.275 45.890  58.298  1.00 32.62 ? 210  GLU A C     1 
ATOM   1435  O  O     . GLU A  1  212  ? -45.981 44.887  58.145  1.00 34.05 ? 210  GLU A O     1 
ATOM   1436  C  CB    . GLU A  1  212  ? -43.192 46.404  56.992  1.00 37.75 ? 210  GLU A CB    1 
ATOM   1437  C  CG    . GLU A  1  212  ? -42.780 44.948  56.976  1.00 44.00 ? 210  GLU A CG    1 
ATOM   1438  C  CD    . GLU A  1  212  ? -41.281 44.786  56.856  1.00 54.30 ? 210  GLU A CD    1 
ATOM   1439  O  OE1   . GLU A  1  212  ? -40.599 45.798  56.595  1.00 59.13 ? 210  GLU A OE1   1 
ATOM   1440  O  OE2   . GLU A  1  212  ? -40.785 43.652  57.026  1.00 64.00 ? 210  GLU A OE2   1 
ATOM   1441  N  N     . LEU A  1  213  ? -44.989 46.376  59.507  1.00 31.33 ? 211  LEU A N     1 
ATOM   1442  C  CA    . LEU A  1  213  ? -45.479 45.687  60.695  1.00 32.92 ? 211  LEU A CA    1 
ATOM   1443  C  C     . LEU A  1  213  ? -46.930 46.029  61.000  1.00 28.94 ? 211  LEU A C     1 
ATOM   1444  O  O     . LEU A  1  213  ? -47.632 45.222  61.614  1.00 28.95 ? 211  LEU A O     1 
ATOM   1445  C  CB    . LEU A  1  213  ? -44.588 45.998  61.896  1.00 27.49 ? 211  LEU A CB    1 
ATOM   1446  C  CG    . LEU A  1  213  ? -43.198 45.358  61.816  1.00 28.22 ? 211  LEU A CG    1 
ATOM   1447  C  CD1   . LEU A  1  213  ? -42.398 45.607  63.086  1.00 32.67 ? 211  LEU A CD1   1 
ATOM   1448  C  CD2   . LEU A  1  213  ? -43.323 43.869  61.541  1.00 30.86 ? 211  LEU A CD2   1 
ATOM   1449  N  N     . GLU A  1  214  ? -47.419 47.192  60.567  1.00 27.34 ? 212  GLU A N     1 
ATOM   1450  C  CA    . GLU A  1  214  ? -48.851 47.442  60.700  1.00 25.79 ? 212  GLU A CA    1 
ATOM   1451  C  C     . GLU A  1  214  ? -49.658 46.431  59.899  1.00 30.03 ? 212  GLU A C     1 
ATOM   1452  O  O     . GLU A  1  214  ? -50.730 45.997  60.335  1.00 32.14 ? 212  GLU A O     1 
ATOM   1453  C  CB    . GLU A  1  214  ? -49.188 48.862  60.263  1.00 25.34 ? 212  GLU A CB    1 
ATOM   1454  C  CG    . GLU A  1  214  ? -48.753 49.894  61.269  1.00 27.10 ? 212  GLU A CG    1 
ATOM   1455  C  CD    . GLU A  1  214  ? -49.203 51.274  60.893  1.00 29.38 ? 212  GLU A CD    1 
ATOM   1456  O  OE1   . GLU A  1  214  ? -49.451 51.515  59.686  1.00 28.40 ? 212  GLU A OE1   1 
ATOM   1457  O  OE2   . GLU A  1  214  ? -49.303 52.120  61.805  1.00 29.09 ? 212  GLU A OE2   1 
ATOM   1458  N  N     . GLU A  1  215  ? -49.152 46.039  58.729  1.00 29.34 ? 213  GLU A N     1 
ATOM   1459  C  CA    . GLU A  1  215  ? -49.835 45.037  57.923  1.00 33.77 ? 213  GLU A CA    1 
ATOM   1460  C  C     . GLU A  1  215  ? -49.855 43.680  58.615  1.00 38.90 ? 213  GLU A C     1 
ATOM   1461  O  O     . GLU A  1  215  ? -50.748 42.868  58.348  1.00 41.12 ? 213  GLU A O     1 
ATOM   1462  C  CB    . GLU A  1  215  ? -49.170 44.927  56.549  1.00 36.38 ? 213  GLU A CB    1 
ATOM   1463  N  N     . LYS A  1  216  ? -48.894 43.418  59.501  1.00 36.73 ? 214  LYS A N     1 
ATOM   1464  C  CA    . LYS A  1  216  ? -48.848 42.171  60.255  1.00 37.67 ? 214  LYS A CA    1 
ATOM   1465  C  C     . LYS A  1  216  ? -49.684 42.209  61.529  1.00 39.85 ? 214  LYS A C     1 
ATOM   1466  O  O     . LYS A  1  216  ? -49.809 41.180  62.199  1.00 43.45 ? 214  LYS A O     1 
ATOM   1467  C  CB    . LYS A  1  216  ? -47.401 41.820  60.612  1.00 35.23 ? 214  LYS A CB    1 
ATOM   1468  N  N     . GLY A  1  217  ? -50.256 43.360  61.879  1.00 33.81 ? 215  GLY A N     1 
ATOM   1469  C  CA    . GLY A  1  217  ? -51.097 43.483  63.053  1.00 31.31 ? 215  GLY A CA    1 
ATOM   1470  C  C     . GLY A  1  217  ? -50.512 44.311  64.177  1.00 30.48 ? 215  GLY A C     1 
ATOM   1471  O  O     . GLY A  1  217  ? -51.154 44.431  65.225  1.00 30.34 ? 215  GLY A O     1 
ATOM   1472  N  N     . PHE A  1  218  ? -49.317 44.864  64.010  1.00 25.94 ? 216  PHE A N     1 
ATOM   1473  C  CA    . PHE A  1  218  ? -48.781 45.786  65.000  1.00 25.81 ? 216  PHE A CA    1 
ATOM   1474  C  C     . PHE A  1  218  ? -49.416 47.159  64.837  1.00 23.34 ? 216  PHE A C     1 
ATOM   1475  O  O     . PHE A  1  218  ? -49.983 47.495  63.795  1.00 25.02 ? 216  PHE A O     1 
ATOM   1476  C  CB    . PHE A  1  218  ? -47.261 45.920  64.868  1.00 23.01 ? 216  PHE A CB    1 
ATOM   1477  C  CG    . PHE A  1  218  ? -46.493 44.708  65.316  1.00 24.75 ? 216  PHE A CG    1 
ATOM   1478  C  CD1   . PHE A  1  218  ? -46.338 43.614  64.477  1.00 28.72 ? 216  PHE A CD1   1 
ATOM   1479  C  CD2   . PHE A  1  218  ? -45.909 44.676  66.567  1.00 25.92 ? 216  PHE A CD2   1 
ATOM   1480  C  CE1   . PHE A  1  218  ? -45.624 42.507  64.889  1.00 28.08 ? 216  PHE A CE1   1 
ATOM   1481  C  CE2   . PHE A  1  218  ? -45.191 43.570  66.986  1.00 28.93 ? 216  PHE A CE2   1 
ATOM   1482  C  CZ    . PHE A  1  218  ? -45.044 42.491  66.150  1.00 27.22 ? 216  PHE A CZ    1 
ATOM   1483  N  N     . SER A  1  219  ? -49.306 47.963  65.888  1.00 23.40 ? 217  SER A N     1 
ATOM   1484  C  CA    . SER A  1  219  ? -49.629 49.379  65.828  1.00 20.76 ? 217  SER A CA    1 
ATOM   1485  C  C     . SER A  1  219  ? -48.425 50.158  66.342  1.00 19.36 ? 217  SER A C     1 
ATOM   1486  O  O     . SER A  1  219  ? -47.405 49.577  66.734  1.00 20.66 ? 217  SER A O     1 
ATOM   1487  C  CB    . SER A  1  219  ? -50.887 49.710  66.639  1.00 25.32 ? 217  SER A CB    1 
ATOM   1488  O  OG    . SER A  1  219  ? -50.680 49.405  68.004  1.00 24.61 ? 217  SER A OG    1 
ATOM   1489  N  N     . TYR A  1  220  ? -48.533 51.488  66.333  1.00 20.24 ? 218  TYR A N     1 
ATOM   1490  C  CA    . TYR A  1  220  ? -47.398 52.337  66.675  1.00 19.22 ? 218  TYR A CA    1 
ATOM   1491  C  C     . TYR A  1  220  ? -47.820 53.466  67.597  1.00 19.45 ? 218  TYR A C     1 
ATOM   1492  O  O     . TYR A  1  220  ? -48.943 53.964  67.518  1.00 19.13 ? 218  TYR A O     1 
ATOM   1493  C  CB    . TYR A  1  220  ? -46.736 52.943  65.417  1.00 19.21 ? 218  TYR A CB    1 
ATOM   1494  C  CG    . TYR A  1  220  ? -45.802 51.979  64.738  1.00 19.38 ? 218  TYR A CG    1 
ATOM   1495  C  CD1   . TYR A  1  220  ? -46.289 51.002  63.880  1.00 23.29 ? 218  TYR A CD1   1 
ATOM   1496  C  CD2   . TYR A  1  220  ? -44.438 52.032  64.974  1.00 22.07 ? 218  TYR A CD2   1 
ATOM   1497  C  CE1   . TYR A  1  220  ? -45.439 50.104  63.271  1.00 21.78 ? 218  TYR A CE1   1 
ATOM   1498  C  CE2   . TYR A  1  220  ? -43.578 51.143  64.362  1.00 21.38 ? 218  TYR A CE2   1 
ATOM   1499  C  CZ    . TYR A  1  220  ? -44.082 50.183  63.520  1.00 23.86 ? 218  TYR A CZ    1 
ATOM   1500  O  OH    . TYR A  1  220  ? -43.215 49.297  62.920  1.00 24.10 ? 218  TYR A OH    1 
ATOM   1501  N  N     . SER A  1  221  ? -46.893 53.857  68.473  1.00 19.57 ? 219  SER A N     1 
ATOM   1502  C  CA    . SER A  1  221  ? -46.955 55.113  69.213  1.00 18.71 ? 219  SER A CA    1 
ATOM   1503  C  C     . SER A  1  221  ? -45.612 55.794  69.047  1.00 21.67 ? 219  SER A C     1 
ATOM   1504  O  O     . SER A  1  221  ? -44.583 55.232  69.438  1.00 23.66 ? 219  SER A O     1 
ATOM   1505  C  CB    . SER A  1  221  ? -47.258 54.895  70.698  1.00 20.39 ? 219  SER A CB    1 
ATOM   1506  O  OG    . SER A  1  221  ? -47.286 56.141  71.390  1.00 23.70 ? 219  SER A OG    1 
ATOM   1507  N  N     . TYR A  1  222  ? -45.608 56.988  68.471  1.00 16.45 ? 220  TYR A N     1 
ATOM   1508  C  CA    . TYR A  1  222  ? -44.345 57.637  68.138  1.00 19.07 ? 220  TYR A CA    1 
ATOM   1509  C  C     . TYR A  1  222  ? -43.846 58.508  69.279  1.00 18.89 ? 220  TYR A C     1 
ATOM   1510  O  O     . TYR A  1  222  ? -44.593 59.315  69.835  1.00 20.55 ? 220  TYR A O     1 
ATOM   1511  C  CB    . TYR A  1  222  ? -44.490 58.453  66.854  1.00 18.32 ? 220  TYR A CB    1 
ATOM   1512  C  CG    . TYR A  1  222  ? -44.819 57.541  65.712  1.00 18.05 ? 220  TYR A CG    1 
ATOM   1513  C  CD1   . TYR A  1  222  ? -43.826 56.798  65.093  1.00 17.48 ? 220  TYR A CD1   1 
ATOM   1514  C  CD2   . TYR A  1  222  ? -46.139 57.367  65.292  1.00 18.63 ? 220  TYR A CD2   1 
ATOM   1515  C  CE1   . TYR A  1  222  ? -44.139 55.914  64.078  1.00 19.37 ? 220  TYR A CE1   1 
ATOM   1516  C  CE2   . TYR A  1  222  ? -46.451 56.502  64.270  1.00 19.35 ? 220  TYR A CE2   1 
ATOM   1517  C  CZ    . TYR A  1  222  ? -45.444 55.779  63.669  1.00 18.38 ? 220  TYR A CZ    1 
ATOM   1518  O  OH    . TYR A  1  222  ? -45.737 54.906  62.656  1.00 22.49 ? 220  TYR A OH    1 
ATOM   1519  N  N     . ASP A  1  223  ? -42.568 58.346  69.596  1.00 21.04 ? 221  ASP A N     1 
ATOM   1520  C  CA    . ASP A  1  223  ? -41.871 59.071  70.653  1.00 24.42 ? 221  ASP A CA    1 
ATOM   1521  C  C     . ASP A  1  223  ? -40.908 60.060  69.999  1.00 26.65 ? 221  ASP A C     1 
ATOM   1522  O  O     . ASP A  1  223  ? -39.884 59.657  69.433  1.00 22.87 ? 221  ASP A O     1 
ATOM   1523  C  CB    . ASP A  1  223  ? -41.148 58.063  71.543  1.00 29.97 ? 221  ASP A CB    1 
ATOM   1524  C  CG    . ASP A  1  223  ? -40.169 58.704  72.512  1.00 30.42 ? 221  ASP A CG    1 
ATOM   1525  O  OD1   . ASP A  1  223  ? -40.325 59.895  72.851  1.00 31.22 ? 221  ASP A OD1   1 
ATOM   1526  O  OD2   . ASP A  1  223  ? -39.241 57.985  72.931  1.00 34.03 ? 221  ASP A OD2   1 
ATOM   1527  N  N     . MET A  1  224  ? -41.233 61.349  70.064  1.00 24.47 ? 222  MET A N     1 
ATOM   1528  C  CA    . MET A  1  224  ? -40.417 62.368  69.413  1.00 26.61 ? 222  MET A CA    1 
ATOM   1529  C  C     . MET A  1  224  ? -39.168 62.730  70.211  1.00 27.00 ? 222  MET A C     1 
ATOM   1530  O  O     . MET A  1  224  ? -38.464 63.672  69.837  1.00 38.27 ? 222  MET A O     1 
ATOM   1531  C  CB    . MET A  1  224  ? -41.254 63.615  69.127  1.00 29.22 ? 222  MET A CB    1 
ATOM   1532  C  CG    . MET A  1  224  ? -42.502 63.313  68.294  1.00 28.98 ? 222  MET A CG    1 
ATOM   1533  S  SD    . MET A  1  224  ? -42.186 62.373  66.777  1.00 33.03 ? 222  MET A SD    1 
ATOM   1534  C  CE    . MET A  1  224  ? -41.154 63.545  65.946  1.00 29.99 ? 222  MET A CE    1 
ATOM   1535  N  N     . LEU A  1  225  ? -38.888 61.998  71.285  1.00 34.06 ? 223  LEU A N     1 
ATOM   1536  C  CA    . LEU A  1  225  ? -37.616 61.985  72.006  1.00 30.51 ? 223  LEU A CA    1 
ATOM   1537  C  C     . LEU A  1  225  ? -37.320 63.286  72.747  1.00 35.30 ? 223  LEU A C     1 
ATOM   1538  O  O     . LEU A  1  225  ? -36.209 63.460  73.246  1.00 36.49 ? 223  LEU A O     1 
ATOM   1539  C  CB    . LEU A  1  225  ? -36.446 61.639  71.074  1.00 28.45 ? 223  LEU A CB    1 
ATOM   1540  C  CG    . LEU A  1  225  ? -36.369 60.164  70.647  1.00 27.87 ? 223  LEU A CG    1 
ATOM   1541  C  CD1   . LEU A  1  225  ? -35.222 59.918  69.669  1.00 29.07 ? 223  LEU A CD1   1 
ATOM   1542  C  CD2   . LEU A  1  225  ? -36.238 59.252  71.861  1.00 27.95 ? 223  LEU A CD2   1 
ATOM   1543  N  N     . GLY A  1  226  ? -38.288 64.191  72.860  1.00 36.06 ? 224  GLY A N     1 
ATOM   1544  C  CA    . GLY A  1  226  ? -38.080 65.386  73.645  1.00 29.65 ? 224  GLY A CA    1 
ATOM   1545  C  C     . GLY A  1  226  ? -38.293 65.129  75.127  1.00 27.12 ? 224  GLY A C     1 
ATOM   1546  O  O     . GLY A  1  226  ? -39.126 64.320  75.530  1.00 27.34 ? 224  GLY A O     1 
ATOM   1547  N  N     . GLU A  1  227  ? -37.500 65.815  75.946  1.00 26.47 ? 225  GLU A N     1 
ATOM   1548  C  CA    . GLU A  1  227  ? -37.705 65.799  77.389  1.00 24.81 ? 225  GLU A CA    1 
ATOM   1549  C  C     . GLU A  1  227  ? -36.830 66.864  78.020  1.00 25.43 ? 225  GLU A C     1 
ATOM   1550  O  O     . GLU A  1  227  ? -35.885 67.370  77.402  1.00 24.49 ? 225  GLU A O     1 
ATOM   1551  C  CB    . GLU A  1  227  ? -37.390 64.435  77.999  1.00 27.50 ? 225  GLU A CB    1 
ATOM   1552  C  CG    . GLU A  1  227  ? -35.932 64.061  77.967  1.00 28.82 ? 225  GLU A CG    1 
ATOM   1553  C  CD    . GLU A  1  227  ? -35.723 62.635  78.415  1.00 39.78 ? 225  GLU A CD    1 
ATOM   1554  O  OE1   . GLU A  1  227  ? -35.891 61.722  77.580  1.00 31.26 ? 225  GLU A OE1   1 
ATOM   1555  O  OE2   . GLU A  1  227  ? -35.421 62.428  79.608  1.00 33.20 ? 225  GLU A OE2   1 
ATOM   1556  N  N     . ALA A  1  228  ? -37.177 67.203  79.260  1.00 23.86 ? 226  ALA A N     1 
ATOM   1557  C  CA    . ALA A  1  228  ? -36.382 68.089  80.101  1.00 25.31 ? 226  ALA A CA    1 
ATOM   1558  C  C     . ALA A  1  228  ? -36.047 69.395  79.379  1.00 25.73 ? 226  ALA A C     1 
ATOM   1559  O  O     . ALA A  1  228  ? -34.885 69.758  79.198  1.00 25.25 ? 226  ALA A O     1 
ATOM   1560  C  CB    . ALA A  1  228  ? -35.109 67.378  80.574  1.00 31.04 ? 226  ALA A CB    1 
ATOM   1561  N  N     . ALA A  1  229  ? -37.092 70.114  78.971  1.00 20.88 ? 227  ALA A N     1 
ATOM   1562  C  CA    . ALA A  1  229  ? -36.882 71.452  78.435  1.00 20.34 ? 227  ALA A CA    1 
ATOM   1563  C  C     . ALA A  1  229  ? -36.182 72.316  79.476  1.00 21.05 ? 227  ALA A C     1 
ATOM   1564  O  O     . ALA A  1  229  ? -36.547 72.305  80.655  1.00 20.14 ? 227  ALA A O     1 
ATOM   1565  C  CB    . ALA A  1  229  ? -38.211 72.092  78.041  1.00 19.83 ? 227  ALA A CB    1 
ATOM   1566  N  N     . THR A  1  230  ? -35.174 73.066  79.034  1.00 19.82 ? 228  THR A N     1 
ATOM   1567  C  CA    . THR A  1  230  ? -34.427 73.946  79.922  1.00 21.95 ? 228  THR A CA    1 
ATOM   1568  C  C     . THR A  1  230  ? -34.863 75.400  79.808  1.00 19.90 ? 228  THR A C     1 
ATOM   1569  O  O     . THR A  1  230  ? -34.681 76.172  80.756  1.00 20.56 ? 228  THR A O     1 
ATOM   1570  C  CB    . THR A  1  230  ? -32.929 73.829  79.603  1.00 26.99 ? 228  THR A CB    1 
ATOM   1571  O  OG1   . THR A  1  230  ? -32.551 72.445  79.640  1.00 30.44 ? 228  THR A OG1   1 
ATOM   1572  C  CG2   . THR A  1  230  ? -32.096 74.583  80.608  1.00 31.52 ? 228  THR A CG2   1 
ATOM   1573  N  N     . THR A  1  231  ? -35.449 75.782  78.679  1.00 21.52 ? 229  THR A N     1 
ATOM   1574  C  CA    . THR A  1  231  ? -35.817 77.161  78.416  1.00 16.46 ? 229  THR A CA    1 
ATOM   1575  C  C     . THR A  1  231  ? -37.204 77.181  77.798  1.00 17.99 ? 229  THR A C     1 
ATOM   1576  O  O     . THR A  1  231  ? -37.708 76.155  77.331  1.00 20.14 ? 229  THR A O     1 
ATOM   1577  C  CB    . THR A  1  231  ? -34.844 77.835  77.440  1.00 22.42 ? 229  THR A CB    1 
ATOM   1578  O  OG1   . THR A  1  231  ? -35.033 77.270  76.132  1.00 21.72 ? 229  THR A OG1   1 
ATOM   1579  C  CG2   . THR A  1  231  ? -33.382 77.611  77.873  1.00 21.47 ? 229  THR A CG2   1 
ATOM   1580  N  N     . ALA A  1  232  ? -37.816 78.365  77.813  1.00 20.39 ? 230  ALA A N     1 
ATOM   1581  C  CA    . ALA A  1  232  ? -39.080 78.551  77.108  1.00 20.46 ? 230  ALA A CA    1 
ATOM   1582  C  C     . ALA A  1  232  ? -38.936 78.192  75.638  1.00 23.78 ? 230  ALA A C     1 
ATOM   1583  O  O     . ALA A  1  232  ? -39.811 77.532  75.067  1.00 22.91 ? 230  ALA A O     1 
ATOM   1584  C  CB    . ALA A  1  232  ? -39.566 79.988  77.263  1.00 21.21 ? 230  ALA A CB    1 
ATOM   1585  N  N     . ALA A  1  233  ? -37.830 78.596  75.013  1.00 23.79 ? 231  ALA A N     1 
ATOM   1586  C  CA    . ALA A  1  233  ? -37.650 78.303  73.596  1.00 25.89 ? 231  ALA A CA    1 
ATOM   1587  C  C     . ALA A  1  233  ? -37.563 76.802  73.344  1.00 24.67 ? 231  ALA A C     1 
ATOM   1588  O  O     . ALA A  1  233  ? -38.125 76.305  72.361  1.00 26.29 ? 231  ALA A O     1 
ATOM   1589  C  CB    . ALA A  1  233  ? -36.408 79.016  73.060  1.00 28.05 ? 231  ALA A CB    1 
ATOM   1590  N  N     . ASP A  1  234  ? -36.862 76.064  74.216  1.00 23.22 ? 232  ASP A N     1 
ATOM   1591  C  CA    . ASP A  1  234  ? -36.821 74.605  74.112  1.00 23.57 ? 232  ASP A CA    1 
ATOM   1592  C  C     . ASP A  1  234  ? -38.222 74.023  74.174  1.00 23.07 ? 232  ASP A C     1 
ATOM   1593  O  O     . ASP A  1  234  ? -38.583 73.146  73.384  1.00 22.32 ? 232  ASP A O     1 
ATOM   1594  C  CB    . ASP A  1  234  ? -36.003 73.990  75.251  1.00 29.29 ? 232  ASP A CB    1 
ATOM   1595  C  CG    . ASP A  1  234  ? -34.515 74.102  75.060  1.00 39.64 ? 232  ASP A CG    1 
ATOM   1596  O  OD1   . ASP A  1  234  ? -34.066 74.497  73.970  1.00 38.29 ? 232  ASP A OD1   1 
ATOM   1597  O  OD2   . ASP A  1  234  ? -33.797 73.775  76.036  1.00 46.98 ? 232  ASP A OD2   1 
ATOM   1598  N  N     . ALA A  1  235  ? -39.004 74.457  75.161  1.00 20.14 ? 233  ALA A N     1 
ATOM   1599  C  CA    . ALA A  1  235  ? -40.349 73.927  75.325  1.00 19.32 ? 233  ALA A CA    1 
ATOM   1600  C  C     . ALA A  1  235  ? -41.211 74.237  74.111  1.00 22.24 ? 233  ALA A C     1 
ATOM   1601  O  O     . ALA A  1  235  ? -42.019 73.400  73.688  1.00 21.52 ? 233  ALA A O     1 
ATOM   1602  C  CB    . ALA A  1  235  ? -40.982 74.499  76.593  1.00 19.57 ? 233  ALA A CB    1 
ATOM   1603  N  N     . GLU A  1  236  ? -41.061 75.440  73.541  1.00 20.52 ? 234  GLU A N     1 
ATOM   1604  C  CA    . GLU A  1  236  ? -41.806 75.787  72.332  1.00 21.77 ? 234  GLU A CA    1 
ATOM   1605  C  C     . GLU A  1  236  ? -41.375 74.928  71.151  1.00 19.52 ? 234  GLU A C     1 
ATOM   1606  O  O     . GLU A  1  236  ? -42.216 74.525  70.336  1.00 22.72 ? 234  GLU A O     1 
ATOM   1607  C  CB    . GLU A  1  236  ? -41.618 77.272  71.994  1.00 23.41 ? 234  GLU A CB    1 
ATOM   1608  C  CG    . GLU A  1  236  ? -42.262 78.235  72.955  1.00 33.58 ? 234  GLU A CG    1 
ATOM   1609  C  CD    . GLU A  1  236  ? -41.579 79.590  72.963  1.00 44.62 ? 234  GLU A CD    1 
ATOM   1610  O  OE1   . GLU A  1  236  ? -40.760 79.844  72.049  1.00 49.87 ? 234  GLU A OE1   1 
ATOM   1611  O  OE2   . GLU A  1  236  ? -41.852 80.390  73.886  1.00 52.49 ? 234  GLU A OE2   1 
ATOM   1612  N  N     . ARG A  1  237  ? -40.075 74.638  71.040  1.00 20.61 ? 235  ARG A N     1 
ATOM   1613  C  CA    . ARG A  1  237  ? -39.596 73.754  69.979  1.00 22.33 ? 235  ARG A CA    1 
ATOM   1614  C  C     . ARG A  1  237  ? -40.172 72.352  70.128  1.00 25.11 ? 235  ARG A C     1 
ATOM   1615  O  O     . ARG A  1  237  ? -40.616 71.745  69.147  1.00 23.27 ? 235  ARG A O     1 
ATOM   1616  C  CB    . ARG A  1  237  ? -38.068 73.704  69.974  1.00 24.60 ? 235  ARG A CB    1 
ATOM   1617  C  CG    . ARG A  1  237  ? -37.487 72.614  69.067  1.00 34.07 ? 235  ARG A CG    1 
ATOM   1618  C  CD    . ARG A  1  237  ? -35.991 72.818  68.818  1.00 41.75 ? 235  ARG A CD    1 
ATOM   1619  N  NE    . ARG A  1  237  ? -35.228 72.713  70.055  1.00 49.20 ? 235  ARG A NE    1 
ATOM   1620  C  CZ    . ARG A  1  237  ? -34.763 71.576  70.551  1.00 43.45 ? 235  ARG A CZ    1 
ATOM   1621  N  NH1   . ARG A  1  237  ? -34.943 70.424  69.923  1.00 50.36 ? 235  ARG A NH1   1 
ATOM   1622  N  NH2   . ARG A  1  237  ? -34.103 71.595  71.705  1.00 47.18 ? 235  ARG A NH2   1 
ATOM   1623  N  N     . TYR A  1  238  ? -40.166 71.812  71.345  1.00 19.95 ? 236  TYR A N     1 
ATOM   1624  C  CA    . TYR A  1  238  ? -40.756 70.494  71.551  1.00 19.40 ? 236  TYR A CA    1 
ATOM   1625  C  C     . TYR A  1  238  ? -42.247 70.512  71.256  1.00 19.16 ? 236  TYR A C     1 
ATOM   1626  O  O     . TYR A  1  238  ? -42.783 69.550  70.694  1.00 23.50 ? 236  TYR A O     1 
ATOM   1627  C  CB    . TYR A  1  238  ? -40.502 70.011  72.980  1.00 20.18 ? 236  TYR A CB    1 
ATOM   1628  C  CG    . TYR A  1  238  ? -39.068 69.615  73.246  1.00 20.36 ? 236  TYR A CG    1 
ATOM   1629  C  CD1   . TYR A  1  238  ? -38.351 68.870  72.322  1.00 23.88 ? 236  TYR A CD1   1 
ATOM   1630  C  CD2   . TYR A  1  238  ? -38.435 69.993  74.416  1.00 22.57 ? 236  TYR A CD2   1 
ATOM   1631  C  CE1   . TYR A  1  238  ? -37.031 68.510  72.562  1.00 28.99 ? 236  TYR A CE1   1 
ATOM   1632  C  CE2   . TYR A  1  238  ? -37.127 69.635  74.668  1.00 25.75 ? 236  TYR A CE2   1 
ATOM   1633  C  CZ    . TYR A  1  238  ? -36.432 68.894  73.744  1.00 29.67 ? 236  TYR A CZ    1 
ATOM   1634  O  OH    . TYR A  1  238  ? -35.127 68.545  74.008  1.00 32.06 ? 236  TYR A OH    1 
ATOM   1635  N  N     . TYR A  1  239  ? -42.928 71.604  71.612  1.00 19.79 ? 237  TYR A N     1 
ATOM   1636  C  CA    . TYR A  1  239  ? -44.347 71.717  71.310  1.00 17.16 ? 237  TYR A CA    1 
ATOM   1637  C  C     . TYR A  1  239  ? -44.592 71.654  69.812  1.00 20.99 ? 237  TYR A C     1 
ATOM   1638  O  O     . TYR A  1  239  ? -45.430 70.877  69.344  1.00 19.13 ? 237  TYR A O     1 
ATOM   1639  C  CB    . TYR A  1  239  ? -44.927 73.007  71.874  1.00 20.79 ? 237  TYR A CB    1 
ATOM   1640  C  CG    . TYR A  1  239  ? -46.380 73.123  71.526  1.00 21.93 ? 237  TYR A CG    1 
ATOM   1641  C  CD1   . TYR A  1  239  ? -46.782 73.678  70.318  1.00 22.56 ? 237  TYR A CD1   1 
ATOM   1642  C  CD2   . TYR A  1  239  ? -47.355 72.629  72.374  1.00 21.16 ? 237  TYR A CD2   1 
ATOM   1643  C  CE1   . TYR A  1  239  ? -48.099 73.753  69.971  1.00 24.69 ? 237  TYR A CE1   1 
ATOM   1644  C  CE2   . TYR A  1  239  ? -48.675 72.711  72.042  1.00 24.09 ? 237  TYR A CE2   1 
ATOM   1645  C  CZ    . TYR A  1  239  ? -49.048 73.269  70.843  1.00 26.32 ? 237  TYR A CZ    1 
ATOM   1646  O  OH    . TYR A  1  239  ? -50.378 73.349  70.506  1.00 29.45 ? 237  TYR A OH    1 
ATOM   1647  N  N     . ARG A  1  240  ? -43.885 72.474  69.032  1.00 19.18 ? 238  ARG A N     1 
ATOM   1648  C  CA    A ARG A  1  240  ? -44.166 72.460  67.601  0.57 20.19 ? 238  ARG A CA    1 
ATOM   1649  C  CA    B ARG A  1  240  ? -44.159 72.461  67.599  0.43 20.21 ? 238  ARG A CA    1 
ATOM   1650  C  C     . ARG A  1  240  ? -43.735 71.142  66.965  1.00 19.93 ? 238  ARG A C     1 
ATOM   1651  O  O     . ARG A  1  240  ? -44.325 70.721  65.967  1.00 20.88 ? 238  ARG A O     1 
ATOM   1652  C  CB    A ARG A  1  240  ? -43.525 73.669  66.904  0.57 23.89 ? 238  ARG A CB    1 
ATOM   1653  C  CB    B ARG A  1  240  ? -43.505 73.663  66.903  0.43 23.86 ? 238  ARG A CB    1 
ATOM   1654  C  CG    A ARG A  1  240  ? -42.026 73.690  66.899  0.57 24.41 ? 238  ARG A CG    1 
ATOM   1655  C  CG    B ARG A  1  240  ? -41.996 73.750  66.965  0.43 24.40 ? 238  ARG A CG    1 
ATOM   1656  C  CD    A ARG A  1  240  ? -41.491 74.848  66.050  0.57 23.29 ? 238  ARG A CD    1 
ATOM   1657  C  CD    B ARG A  1  240  ? -41.550 75.075  66.339  0.43 23.42 ? 238  ARG A CD    1 
ATOM   1658  N  NE    A ARG A  1  240  ? -40.053 74.991  66.227  0.57 18.82 ? 238  ARG A NE    1 
ATOM   1659  N  NE    B ARG A  1  240  ? -42.395 76.149  66.842  0.43 24.75 ? 238  ARG A NE    1 
ATOM   1660  C  CZ    A ARG A  1  240  ? -39.481 75.754  67.149  0.57 21.43 ? 238  ARG A CZ    1 
ATOM   1661  C  CZ    B ARG A  1  240  ? -42.021 77.055  67.733  0.43 20.65 ? 238  ARG A CZ    1 
ATOM   1662  N  NH1   A ARG A  1  240  ? -40.189 76.564  67.917  0.57 20.89 ? 238  ARG A NH1   1 
ATOM   1663  N  NH1   B ARG A  1  240  ? -40.755 77.187  68.099  0.43 23.30 ? 238  ARG A NH1   1 
ATOM   1664  N  NH2   A ARG A  1  240  ? -38.163 75.701  67.308  0.57 24.23 ? 238  ARG A NH2   1 
ATOM   1665  N  NH2   B ARG A  1  240  ? -42.942 77.836  68.283  0.43 18.94 ? 238  ARG A NH2   1 
ATOM   1666  N  N     . ASP A  1  241  ? -42.755 70.446  67.556  1.00 19.79 ? 239  ASP A N     1 
ATOM   1667  C  CA    A ASP A  1  241  ? -42.403 69.108  67.087  0.55 21.85 ? 239  ASP A CA    1 
ATOM   1668  C  CA    B ASP A  1  241  ? -42.403 69.111  67.086  0.45 21.87 ? 239  ASP A CA    1 
ATOM   1669  C  C     . ASP A  1  241  ? -43.545 68.124  67.323  1.00 21.12 ? 239  ASP A C     1 
ATOM   1670  O  O     . ASP A  1  241  ? -43.889 67.335  66.437  1.00 22.40 ? 239  ASP A O     1 
ATOM   1671  C  CB    A ASP A  1  241  ? -41.132 68.611  67.778  0.55 27.43 ? 239  ASP A CB    1 
ATOM   1672  C  CB    B ASP A  1  241  ? -41.124 68.644  67.777  0.45 27.42 ? 239  ASP A CB    1 
ATOM   1673  C  CG    A ASP A  1  241  ? -39.892 69.386  67.368  0.55 27.77 ? 239  ASP A CG    1 
ATOM   1674  C  CG    B ASP A  1  241  ? -40.506 67.445  67.105  0.45 30.25 ? 239  ASP A CG    1 
ATOM   1675  O  OD1   A ASP A  1  241  ? -39.969 70.209  66.427  0.55 31.06 ? 239  ASP A OD1   1 
ATOM   1676  O  OD1   B ASP A  1  241  ? -40.311 67.488  65.869  0.45 30.97 ? 239  ASP A OD1   1 
ATOM   1677  O  OD2   A ASP A  1  241  ? -38.839 69.174  68.007  0.55 35.39 ? 239  ASP A OD2   1 
ATOM   1678  O  OD2   B ASP A  1  241  ? -40.206 66.462  67.815  0.45 34.86 ? 239  ASP A OD2   1 
ATOM   1679  N  N     . TYR A  1  242  ? -44.146 68.148  68.521  1.00 19.67 ? 240  TYR A N     1 
ATOM   1680  C  CA    . TYR A  1  242  ? -45.296 67.274  68.775  1.00 18.48 ? 240  TYR A CA    1 
ATOM   1681  C  C     . TYR A  1  242  ? -46.465 67.625  67.870  1.00 18.38 ? 240  TYR A C     1 
ATOM   1682  O  O     . TYR A  1  242  ? -47.150 66.733  67.351  1.00 17.88 ? 240  TYR A O     1 
ATOM   1683  C  CB    . TYR A  1  242  ? -45.766 67.381  70.225  1.00 15.91 ? 240  TYR A CB    1 
ATOM   1684  C  CG    . TYR A  1  242  ? -44.881 66.766  71.271  1.00 16.93 ? 240  TYR A CG    1 
ATOM   1685  C  CD1   . TYR A  1  242  ? -44.265 65.542  71.074  1.00 22.27 ? 240  TYR A CD1   1 
ATOM   1686  C  CD2   . TYR A  1  242  ? -44.713 67.400  72.494  1.00 19.94 ? 240  TYR A CD2   1 
ATOM   1687  C  CE1   . TYR A  1  242  ? -43.468 64.981  72.073  1.00 23.02 ? 240  TYR A CE1   1 
ATOM   1688  C  CE2   . TYR A  1  242  ? -43.918 66.858  73.478  1.00 19.42 ? 240  TYR A CE2   1 
ATOM   1689  C  CZ    . TYR A  1  242  ? -43.306 65.654  73.267  1.00 19.43 ? 240  TYR A CZ    1 
ATOM   1690  O  OH    . TYR A  1  242  ? -42.522 65.125  74.268  1.00 18.84 ? 240  TYR A OH    1 
ATOM   1691  N  N     . GLU A  1  243  ? -46.744 68.920  67.722  1.00 17.15 ? 241  GLU A N     1 
ATOM   1692  C  CA    . GLU A  1  243  ? -47.867 69.353  66.902  1.00 16.61 ? 241  GLU A CA    1 
ATOM   1693  C  C     . GLU A  1  243  ? -47.694 68.877  65.467  1.00 19.37 ? 241  GLU A C     1 
ATOM   1694  O  O     . GLU A  1  243  ? -48.619 68.303  64.876  1.00 18.60 ? 241  GLU A O     1 
ATOM   1695  C  CB    . GLU A  1  243  ? -47.983 70.873  66.978  1.00 20.32 ? 241  GLU A CB    1 
ATOM   1696  C  CG    . GLU A  1  243  ? -49.070 71.475  66.123  1.00 22.46 ? 241  GLU A CG    1 
ATOM   1697  C  CD    . GLU A  1  243  ? -48.974 73.006  66.068  1.00 22.42 ? 241  GLU A CD    1 
ATOM   1698  O  OE1   . GLU A  1  243  ? -47.848 73.571  66.145  1.00 31.43 ? 241  GLU A OE1   1 
ATOM   1699  O  OE2   . GLU A  1  243  ? -50.028 73.632  65.941  1.00 24.60 ? 241  GLU A OE2   1 
ATOM   1700  N  N     . SER A  1  244  ? -46.495 69.081  64.899  1.00 18.63 ? 242  SER A N     1 
ATOM   1701  C  CA    . SER A  1  244  ? -46.255 68.642  63.527  1.00 17.77 ? 242  SER A CA    1 
ATOM   1702  C  C     . SER A  1  244  ? -46.322 67.122  63.415  1.00 18.40 ? 242  SER A C     1 
ATOM   1703  O  O     . SER A  1  244  ? -46.817 66.589  62.413  1.00 21.74 ? 242  SER A O     1 
ATOM   1704  C  CB    . SER A  1  244  ? -44.908 69.162  63.022  1.00 21.43 ? 242  SER A CB    1 
ATOM   1705  O  OG    . SER A  1  244  ? -43.842 68.589  63.756  1.00 25.41 ? 242  SER A OG    1 
ATOM   1706  N  N     . ALA A  1  245  ? -45.861 66.407  64.451  1.00 16.97 ? 243  ALA A N     1 
ATOM   1707  C  CA    . ALA A  1  245  ? -45.956 64.953  64.446  1.00 19.82 ? 243  ALA A CA    1 
ATOM   1708  C  C     . ALA A  1  245  ? -47.409 64.496  64.503  1.00 17.49 ? 243  ALA A C     1 
ATOM   1709  O  O     . ALA A  1  245  ? -47.796 63.558  63.805  1.00 18.78 ? 243  ALA A O     1 
ATOM   1710  C  CB    . ALA A  1  245  ? -45.164 64.370  65.610  1.00 20.07 ? 243  ALA A CB    1 
ATOM   1711  N  N     . ILE A  1  246  ? -48.229 65.135  65.336  1.00 16.56 ? 244  ILE A N     1 
ATOM   1712  C  CA    . ILE A  1  246  ? -49.631 64.744  65.400  1.00 15.82 ? 244  ILE A CA    1 
ATOM   1713  C  C     . ILE A  1  246  ? -50.292 64.891  64.038  1.00 18.62 ? 244  ILE A C     1 
ATOM   1714  O  O     . ILE A  1  246  ? -51.060 64.025  63.618  1.00 19.71 ? 244  ILE A O     1 
ATOM   1715  C  CB    . ILE A  1  246  ? -50.362 65.551  66.479  1.00 15.84 ? 244  ILE A CB    1 
ATOM   1716  C  CG1   . ILE A  1  246  ? -49.893 65.086  67.856  1.00 15.67 ? 244  ILE A CG1   1 
ATOM   1717  C  CG2   . ILE A  1  246  ? -51.866 65.375  66.332  1.00 18.38 ? 244  ILE A CG2   1 
ATOM   1718  C  CD1   . ILE A  1  246  ? -50.327 66.005  68.975  1.00 17.85 ? 244  ILE A CD1   1 
ATOM   1719  N  N     . HIS A  1  247  ? -49.999 65.977  63.317  1.00 17.06 ? 245  HIS A N     1 
ATOM   1720  C  CA    . HIS A  1  247  ? -50.560 66.114  61.975  1.00 16.45 ? 245  HIS A CA    1 
ATOM   1721  C  C     . HIS A  1  247  ? -50.125 64.964  61.075  1.00 18.04 ? 245  HIS A C     1 
ATOM   1722  O  O     . HIS A  1  247  ? -50.950 64.366  60.374  1.00 20.27 ? 245  HIS A O     1 
ATOM   1723  C  CB    . HIS A  1  247  ? -50.149 67.452  61.351  1.00 18.90 ? 245  HIS A CB    1 
ATOM   1724  C  CG    . HIS A  1  247  ? -50.867 68.635  61.915  1.00 19.69 ? 245  HIS A CG    1 
ATOM   1725  N  ND1   . HIS A  1  247  ? -52.228 68.807  61.803  1.00 18.41 ? 245  HIS A ND1   1 
ATOM   1726  C  CD2   . HIS A  1  247  ? -50.404 69.721  62.581  1.00 21.69 ? 245  HIS A CD2   1 
ATOM   1727  C  CE1   . HIS A  1  247  ? -52.578 69.938  62.390  1.00 21.94 ? 245  HIS A CE1   1 
ATOM   1728  N  NE2   . HIS A  1  247  ? -51.489 70.511  62.867  1.00 21.66 ? 245  HIS A NE2   1 
ATOM   1729  N  N     . ALA A  1  248  ? -48.827 64.655  61.057  1.00 16.34 ? 246  ALA A N     1 
ATOM   1730  C  CA    . ALA A  1  248  ? -48.350 63.591  60.181  1.00 19.91 ? 246  ALA A CA    1 
ATOM   1731  C  C     . ALA A  1  248  ? -48.958 62.253  60.570  1.00 21.29 ? 246  ALA A C     1 
ATOM   1732  O  O     . ALA A  1  248  ? -49.374 61.478  59.704  1.00 19.68 ? 246  ALA A O     1 
ATOM   1733  C  CB    . ALA A  1  248  ? -46.820 63.517  60.221  1.00 21.67 ? 246  ALA A CB    1 
ATOM   1734  N  N     . ILE A  1  249  ? -49.015 61.970  61.873  1.00 18.55 ? 247  ILE A N     1 
ATOM   1735  C  CA    . ILE A  1  249  ? -49.575 60.714  62.353  1.00 19.11 ? 247  ILE A CA    1 
ATOM   1736  C  C     . ILE A  1  249  ? -51.067 60.653  62.069  1.00 18.63 ? 247  ILE A C     1 
ATOM   1737  O  O     . ILE A  1  249  ? -51.593 59.613  61.666  1.00 20.13 ? 247  ILE A O     1 
ATOM   1738  C  CB    . ILE A  1  249  ? -49.279 60.557  63.853  1.00 17.52 ? 247  ILE A CB    1 
ATOM   1739  C  CG1   . ILE A  1  249  ? -47.773 60.438  64.090  1.00 18.11 ? 247  ILE A CG1   1 
ATOM   1740  C  CG2   . ILE A  1  249  ? -50.001 59.330  64.430  1.00 19.92 ? 247  ILE A CG2   1 
ATOM   1741  C  CD1   . ILE A  1  249  ? -47.378 60.709  65.533  1.00 18.65 ? 247  ILE A CD1   1 
ATOM   1742  N  N     . GLY A  1  250  ? -51.776 61.754  62.301  1.00 18.33 ? 248  GLY A N     1 
ATOM   1743  C  CA    . GLY A  1  250  ? -53.210 61.754  62.081  1.00 20.78 ? 248  GLY A CA    1 
ATOM   1744  C  C     . GLY A  1  250  ? -53.558 61.639  60.614  1.00 20.75 ? 248  GLY A C     1 
ATOM   1745  O  O     . GLY A  1  250  ? -54.553 61.006  60.251  1.00 21.13 ? 248  GLY A O     1 
ATOM   1746  N  N     . LYS A  1  251  ? -52.757 62.271  59.753  1.00 19.33 ? 249  LYS A N     1 
ATOM   1747  C  CA    . LYS A  1  251  ? -52.956 62.122  58.318  1.00 18.06 ? 249  LYS A CA    1 
ATOM   1748  C  C     . LYS A  1  251  ? -52.770 60.679  57.893  1.00 20.11 ? 249  LYS A C     1 
ATOM   1749  O  O     . LYS A  1  251  ? -53.529 60.166  57.059  1.00 22.99 ? 249  LYS A O     1 
ATOM   1750  C  CB    . LYS A  1  251  ? -51.970 62.996  57.552  1.00 19.61 ? 249  LYS A CB    1 
ATOM   1751  C  CG    . LYS A  1  251  ? -52.250 64.480  57.570  1.00 22.81 ? 249  LYS A CG    1 
ATOM   1752  C  CD    . LYS A  1  251  ? -51.102 65.158  56.852  1.00 25.41 ? 249  LYS A CD    1 
ATOM   1753  C  CE    . LYS A  1  251  ? -51.155 66.655  57.007  1.00 22.21 ? 249  LYS A CE    1 
ATOM   1754  N  NZ    . LYS A  1  251  ? -49.877 67.226  56.465  1.00 21.03 ? 249  LYS A NZ    1 
ATOM   1755  N  N     . ALA A  1  252  ? -51.741 60.026  58.440  1.00 19.80 ? 250  ALA A N     1 
ATOM   1756  C  CA    . ALA A  1  252  ? -51.441 58.638  58.109  1.00 19.52 ? 250  ALA A CA    1 
ATOM   1757  C  C     . ALA A  1  252  ? -52.460 57.700  58.725  1.00 21.68 ? 250  ALA A C     1 
ATOM   1758  O  O     . ALA A  1  252  ? -52.834 56.691  58.114  1.00 22.45 ? 250  ALA A O     1 
ATOM   1759  C  CB    . ALA A  1  252  ? -50.039 58.275  58.599  1.00 24.69 ? 250  ALA A CB    1 
ATOM   1760  N  N     . SER A  1  253  ? -52.913 58.011  59.939  1.00 21.10 ? 251  SER A N     1 
ATOM   1761  C  CA    . SER A  1  253  ? -53.929 57.178  60.568  1.00 19.76 ? 251  SER A CA    1 
ATOM   1762  C  C     . SER A  1  253  ? -55.140 57.039  59.669  1.00 22.67 ? 251  SER A C     1 
ATOM   1763  O  O     . SER A  1  253  ? -55.693 55.943  59.529  1.00 23.79 ? 251  SER A O     1 
ATOM   1764  C  CB    . SER A  1  253  ? -54.345 57.757  61.914  1.00 19.26 ? 251  SER A CB    1 
ATOM   1765  O  OG    . SER A  1  253  ? -55.372 56.965  62.471  1.00 21.83 ? 251  SER A OG    1 
ATOM   1766  N  N     . ALA A  1  254  ? -55.569 58.146  59.063  1.00 19.52 ? 252  ALA A N     1 
ATOM   1767  C  CA    . ALA A  1  254  ? -56.614 58.150  58.043  1.00 21.18 ? 252  ALA A CA    1 
ATOM   1768  C  C     . ALA A  1  254  ? -57.875 57.451  58.540  1.00 25.06 ? 252  ALA A C     1 
ATOM   1769  O  O     . ALA A  1  254  ? -58.476 56.623  57.848  1.00 24.44 ? 252  ALA A O     1 
ATOM   1770  C  CB    . ALA A  1  254  ? -56.108 57.519  56.744  1.00 25.96 ? 252  ALA A CB    1 
ATOM   1771  N  N     . GLY A  1  255  ? -58.276 57.791  59.760  1.00 21.65 ? 253  GLY A N     1 
ATOM   1772  C  CA    . GLY A  1  255  ? -59.514 57.278  60.306  1.00 24.35 ? 253  GLY A CA    1 
ATOM   1773  C  C     . GLY A  1  255  ? -59.456 55.883  60.886  1.00 25.81 ? 253  GLY A C     1 
ATOM   1774  O  O     . GLY A  1  255  ? -60.512 55.325  61.196  1.00 25.81 ? 253  GLY A O     1 
ATOM   1775  N  N     . ARG A  1  256  ? -58.264 55.300  61.060  1.00 24.17 ? 254  ARG A N     1 
ATOM   1776  C  CA    . ARG A  1  256  ? -58.185 53.967  61.648  1.00 24.37 ? 254  ARG A CA    1 
ATOM   1777  C  C     . ARG A  1  256  ? -58.551 53.948  63.123  1.00 25.27 ? 254  ARG A C     1 
ATOM   1778  O  O     . ARG A  1  256  ? -58.810 52.870  63.665  1.00 23.98 ? 254  ARG A O     1 
ATOM   1779  C  CB    . ARG A  1  256  ? -56.792 53.384  61.462  1.00 22.46 ? 254  ARG A CB    1 
ATOM   1780  C  CG    . ARG A  1  256  ? -56.612 52.741  60.093  1.00 26.84 ? 254  ARG A CG    1 
ATOM   1781  C  CD    . ARG A  1  256  ? -55.210 52.227  59.936  1.00 24.93 ? 254  ARG A CD    1 
ATOM   1782  N  NE    . ARG A  1  256  ? -54.271 53.326  59.770  1.00 24.11 ? 254  ARG A NE    1 
ATOM   1783  C  CZ    . ARG A  1  256  ? -52.958 53.172  59.712  1.00 27.45 ? 254  ARG A CZ    1 
ATOM   1784  N  NH1   . ARG A  1  256  ? -52.392 51.995  59.933  1.00 25.21 ? 254  ARG A NH1   1 
ATOM   1785  N  NH2   . ARG A  1  256  ? -52.196 54.219  59.409  1.00 23.31 ? 254  ARG A NH2   1 
ATOM   1786  N  N     . GLY A  1  257  ? -58.573 55.102  63.785  1.00 23.33 ? 255  GLY A N     1 
ATOM   1787  C  CA    . GLY A  1  257  ? -58.979 55.143  65.174  1.00 20.88 ? 255  GLY A CA    1 
ATOM   1788  C  C     . GLY A  1  257  ? -57.827 54.895  66.131  1.00 19.73 ? 255  GLY A C     1 
ATOM   1789  O  O     . GLY A  1  257  ? -56.683 54.634  65.755  1.00 20.92 ? 255  GLY A O     1 
ATOM   1790  N  N     . ILE A  1  258  ? -58.158 54.940  67.419  1.00 18.22 ? 256  ILE A N     1 
ATOM   1791  C  CA    . ILE A  1  258  ? -57.105 54.971  68.425  1.00 19.88 ? 256  ILE A CA    1 
ATOM   1792  C  C     . ILE A  1  258  ? -56.515 53.604  68.738  1.00 18.54 ? 256  ILE A C     1 
ATOM   1793  O  O     . ILE A  1  258  ? -55.434 53.537  69.336  1.00 19.14 ? 256  ILE A O     1 
ATOM   1794  C  CB    . ILE A  1  258  ? -57.641 55.624  69.703  1.00 19.27 ? 256  ILE A CB    1 
ATOM   1795  C  CG1   . ILE A  1  258  ? -58.783 54.788  70.299  1.00 18.93 ? 256  ILE A CG1   1 
ATOM   1796  C  CG2   . ILE A  1  258  ? -58.085 57.069  69.411  1.00 19.24 ? 256  ILE A CG2   1 
ATOM   1797  C  CD1   . ILE A  1  258  ? -59.309 55.385  71.609  1.00 20.65 ? 256  ILE A CD1   1 
ATOM   1798  N  N     . TYR A  1  259  ? -57.182 52.510  68.367  1.00 20.23 ? 257  TYR A N     1 
ATOM   1799  C  CA    . TYR A  1  259  ? -56.672 51.171  68.659  1.00 17.99 ? 257  TYR A CA    1 
ATOM   1800  C  C     . TYR A  1  259  ? -55.911 50.576  67.482  1.00 21.20 ? 257  TYR A C     1 
ATOM   1801  O  O     . TYR A  1  259  ? -54.777 50.118  67.647  1.00 24.12 ? 257  TYR A O     1 
ATOM   1802  C  CB    . TYR A  1  259  ? -57.827 50.244  69.077  1.00 23.02 ? 257  TYR A CB    1 
ATOM   1803  C  CG    . TYR A  1  259  ? -58.633 50.818  70.219  1.00 23.37 ? 257  TYR A CG    1 
ATOM   1804  C  CD1   . TYR A  1  259  ? -58.036 51.099  71.444  1.00 24.56 ? 257  TYR A CD1   1 
ATOM   1805  C  CD2   . TYR A  1  259  ? -59.980 51.134  70.062  1.00 23.65 ? 257  TYR A CD2   1 
ATOM   1806  C  CE1   . TYR A  1  259  ? -58.763 51.644  72.491  1.00 22.48 ? 257  TYR A CE1   1 
ATOM   1807  C  CE2   . TYR A  1  259  ? -60.715 51.683  71.107  1.00 22.91 ? 257  TYR A CE2   1 
ATOM   1808  C  CZ    . TYR A  1  259  ? -60.098 51.939  72.316  1.00 21.79 ? 257  TYR A CZ    1 
ATOM   1809  O  OH    . TYR A  1  259  ? -60.822 52.495  73.341  1.00 23.15 ? 257  TYR A OH    1 
ATOM   1810  N  N     . GLU A  1  260  ? -56.502 50.598  66.284  1.00 20.89 ? 258  GLU A N     1 
ATOM   1811  C  CA    . GLU A  1  260  ? -55.797 50.087  65.115  1.00 24.48 ? 258  GLU A CA    1 
ATOM   1812  C  C     . GLU A  1  260  ? -54.753 51.069  64.609  1.00 23.62 ? 258  GLU A C     1 
ATOM   1813  O  O     . GLU A  1  260  ? -53.703 50.653  64.101  1.00 29.24 ? 258  GLU A O     1 
ATOM   1814  C  CB    . GLU A  1  260  ? -56.780 49.771  63.981  1.00 28.62 ? 258  GLU A CB    1 
ATOM   1815  C  CG    . GLU A  1  260  ? -56.073 49.223  62.735  1.00 33.50 ? 258  GLU A CG    1 
ATOM   1816  C  CD    . GLU A  1  260  ? -56.951 49.170  61.492  1.00 41.66 ? 258  GLU A CD    1 
ATOM   1817  O  OE1   . GLU A  1  260  ? -58.194 49.167  61.626  1.00 44.53 ? 258  GLU A OE1   1 
ATOM   1818  O  OE2   . GLU A  1  260  ? -56.385 49.130  60.374  1.00 40.69 ? 258  GLU A OE2   1 
ATOM   1819  N  N     . GLY A  1  261  ? -55.011 52.367  64.743  1.00 20.58 ? 259  GLY A N     1 
ATOM   1820  C  CA    . GLY A  1  261  ? -54.166 53.359  64.133  1.00 17.78 ? 259  GLY A CA    1 
ATOM   1821  C  C     . GLY A  1  261  ? -53.102 53.859  65.081  1.00 20.73 ? 259  GLY A C     1 
ATOM   1822  O  O     . GLY A  1  261  ? -53.125 53.606  66.286  1.00 20.23 ? 259  GLY A O     1 
ATOM   1823  N  N     . PRO A  1  262  ? -52.146 54.593  64.534  1.00 18.93 ? 260  PRO A N     1 
ATOM   1824  C  CA    . PRO A  1  262  ? -51.007 55.047  65.330  1.00 18.47 ? 260  PRO A CA    1 
ATOM   1825  C  C     . PRO A  1  262  ? -51.377 56.188  66.259  1.00 17.71 ? 260  PRO A C     1 
ATOM   1826  O  O     . PRO A  1  262  ? -52.389 56.868  66.096  1.00 21.84 ? 260  PRO A O     1 
ATOM   1827  C  CB    . PRO A  1  262  ? -50.006 55.508  64.266  1.00 21.60 ? 260  PRO A CB    1 
ATOM   1828  C  CG    . PRO A  1  262  ? -50.877 55.914  63.117  1.00 19.85 ? 260  PRO A CG    1 
ATOM   1829  C  CD    . PRO A  1  262  ? -52.020 54.955  63.113  1.00 23.66 ? 260  PRO A CD    1 
ATOM   1830  N  N     . GLY A  1  263  ? -50.526 56.384  67.262  1.00 18.85 ? 261  GLY A N     1 
ATOM   1831  C  CA    . GLY A  1  263  ? -50.681 57.510  68.156  1.00 19.47 ? 261  GLY A CA    1 
ATOM   1832  C  C     . GLY A  1  263  ? -49.347 58.151  68.466  1.00 18.89 ? 261  GLY A C     1 
ATOM   1833  O  O     . GLY A  1  263  ? -48.335 57.832  67.829  1.00 17.25 ? 261  GLY A O     1 
ATOM   1834  N  N     . ILE A  1  264  ? -49.341 59.075  69.420  1.00 18.11 ? 262  ILE A N     1 
ATOM   1835  C  CA    . ILE A  1  264  ? -48.132 59.782  69.807  1.00 17.77 ? 262  ILE A CA    1 
ATOM   1836  C  C     . ILE A  1  264  ? -47.960 59.663  71.316  1.00 19.05 ? 262  ILE A C     1 
ATOM   1837  O  O     . ILE A  1  264  ? -48.929 59.486  72.062  1.00 17.91 ? 262  ILE A O     1 
ATOM   1838  C  CB    . ILE A  1  264  ? -48.166 61.267  69.363  1.00 16.43 ? 262  ILE A CB    1 
ATOM   1839  C  CG1   . ILE A  1  264  ? -46.763 61.865  69.427  1.00 17.55 ? 262  ILE A CG1   1 
ATOM   1840  C  CG2   . ILE A  1  264  ? -49.161 62.070  70.220  1.00 18.25 ? 262  ILE A CG2   1 
ATOM   1841  C  CD1   . ILE A  1  264  ? -46.698 63.306  68.872  1.00 19.57 ? 262  ILE A CD1   1 
ATOM   1842  N  N     . SER A  1  265  ? -46.710 59.746  71.760  1.00 16.22 ? 263  SER A N     1 
ATOM   1843  C  CA    . SER A  1  265  ? -46.379 59.792  73.174  1.00 17.24 ? 263  SER A CA    1 
ATOM   1844  C  C     . SER A  1  265  ? -45.644 61.093  73.432  1.00 20.83 ? 263  SER A C     1 
ATOM   1845  O  O     . SER A  1  265  ? -44.801 61.505  72.623  1.00 22.96 ? 263  SER A O     1 
ATOM   1846  C  CB    . SER A  1  265  ? -45.505 58.612  73.609  1.00 19.11 ? 263  SER A CB    1 
ATOM   1847  O  OG    . SER A  1  265  ? -46.233 57.393  73.603  1.00 23.25 ? 263  SER A OG    1 
ATOM   1848  N  N     . ILE A  1  266  ? -45.966 61.742  74.548  1.00 17.88 ? 264  ILE A N     1 
ATOM   1849  C  CA    . ILE A  1  266  ? -45.342 63.010  74.903  1.00 16.47 ? 264  ILE A CA    1 
ATOM   1850  C  C     . ILE A  1  266  ? -44.789 62.905  76.312  1.00 17.14 ? 264  ILE A C     1 
ATOM   1851  O  O     . ILE A  1  266  ? -45.206 62.068  77.114  1.00 17.94 ? 264  ILE A O     1 
ATOM   1852  C  CB    . ILE A  1  266  ? -46.311 64.207  74.813  1.00 18.38 ? 264  ILE A CB    1 
ATOM   1853  C  CG1   . ILE A  1  266  ? -47.410 64.099  75.873  1.00 20.41 ? 264  ILE A CG1   1 
ATOM   1854  C  CG2   . ILE A  1  266  ? -46.913 64.297  73.406  1.00 20.05 ? 264  ILE A CG2   1 
ATOM   1855  C  CD1   . ILE A  1  266  ? -48.234 65.375  76.019  1.00 21.37 ? 264  ILE A CD1   1 
ATOM   1856  N  N     . LYS A  1  267  ? -43.832 63.775  76.606  1.00 16.38 ? 265  LYS A N     1 
ATOM   1857  C  CA    . LYS A  1  267  ? -43.296 63.907  77.950  1.00 17.16 ? 265  LYS A CA    1 
ATOM   1858  C  C     . LYS A  1  267  ? -43.612 65.304  78.440  1.00 16.47 ? 265  LYS A C     1 
ATOM   1859  O  O     . LYS A  1  267  ? -43.316 66.290  77.755  1.00 16.94 ? 265  LYS A O     1 
ATOM   1860  C  CB    . LYS A  1  267  ? -41.790 63.642  77.983  1.00 18.98 ? 265  LYS A CB    1 
ATOM   1861  C  CG    . LYS A  1  267  ? -41.438 62.158  77.965  1.00 22.81 ? 265  LYS A CG    1 
ATOM   1862  C  CD    . LYS A  1  267  ? -39.931 61.961  78.038  1.00 25.40 ? 265  LYS A CD    1 
ATOM   1863  C  CE    . LYS A  1  267  ? -39.574 60.496  78.236  1.00 32.31 ? 265  LYS A CE    1 
ATOM   1864  N  NZ    . LYS A  1  267  ? -40.187 59.622  77.199  1.00 31.31 ? 265  LYS A NZ    1 
ATOM   1865  N  N     . LEU A  1  268  ? -44.264 65.390  79.597  1.00 17.44 ? 266  LEU A N     1 
ATOM   1866  C  CA    . LEU A  1  268  ? -44.635 66.708  80.092  1.00 15.92 ? 266  LEU A CA    1 
ATOM   1867  C  C     . LEU A  1  268  ? -43.410 67.567  80.351  1.00 15.50 ? 266  LEU A C     1 
ATOM   1868  O  O     . LEU A  1  268  ? -43.474 68.793  80.211  1.00 18.24 ? 266  LEU A O     1 
ATOM   1869  C  CB    . LEU A  1  268  ? -45.481 66.591  81.360  1.00 16.10 ? 266  LEU A CB    1 
ATOM   1870  C  CG    . LEU A  1  268  ? -46.818 65.867  81.161  1.00 17.72 ? 266  LEU A CG    1 
ATOM   1871  C  CD1   . LEU A  1  268  ? -47.574 65.718  82.456  1.00 17.90 ? 266  LEU A CD1   1 
ATOM   1872  C  CD2   . LEU A  1  268  ? -47.657 66.603  80.121  1.00 21.13 ? 266  LEU A CD2   1 
ATOM   1873  N  N     . SER A  1  269  ? -42.280 66.950  80.715  1.00 16.39 ? 267  SER A N     1 
ATOM   1874  C  CA    . SER A  1  269  ? -41.091 67.746  80.971  1.00 17.55 ? 267  SER A CA    1 
ATOM   1875  C  C     . SER A  1  269  ? -40.561 68.416  79.714  1.00 19.70 ? 267  SER A C     1 
ATOM   1876  O  O     . SER A  1  269  ? -39.772 69.351  79.824  1.00 18.37 ? 267  SER A O     1 
ATOM   1877  C  CB    . SER A  1  269  ? -39.989 66.890  81.599  1.00 17.63 ? 267  SER A CB    1 
ATOM   1878  O  OG    . SER A  1  269  ? -39.453 65.986  80.660  1.00 20.17 ? 267  SER A OG    1 
ATOM   1879  N  N     . ALA A  1  270  ? -40.969 67.956  78.526  1.00 17.97 ? 268  ALA A N     1 
ATOM   1880  C  CA    . ALA A  1  270  ? -40.572 68.623  77.295  1.00 17.21 ? 268  ALA A CA    1 
ATOM   1881  C  C     . ALA A  1  270  ? -41.340 69.912  77.059  1.00 18.04 ? 268  ALA A C     1 
ATOM   1882  O  O     . ALA A  1  270  ? -40.898 70.751  76.270  1.00 17.70 ? 268  ALA A O     1 
ATOM   1883  C  CB    . ALA A  1  270  ? -40.794 67.685  76.104  1.00 17.26 ? 268  ALA A CB    1 
ATOM   1884  N  N     . LEU A  1  271  ? -42.481 70.081  77.710  1.00 17.24 ? 269  LEU A N     1 
ATOM   1885  C  CA    . LEU A  1  271  ? -43.407 71.130  77.333  1.00 18.46 ? 269  LEU A CA    1 
ATOM   1886  C  C     . LEU A  1  271  ? -43.372 72.313  78.277  1.00 16.47 ? 269  LEU A C     1 
ATOM   1887  O  O     . LEU A  1  271  ? -44.074 73.296  78.044  1.00 19.18 ? 269  LEU A O     1 
ATOM   1888  C  CB    . LEU A  1  271  ? -44.818 70.564  77.241  1.00 18.24 ? 269  LEU A CB    1 
ATOM   1889  C  CG    . LEU A  1  271  ? -45.004 69.631  76.054  1.00 19.63 ? 269  LEU A CG    1 
ATOM   1890  C  CD1   . LEU A  1  271  ? -46.392 69.015  76.127  1.00 22.58 ? 269  LEU A CD1   1 
ATOM   1891  C  CD2   . LEU A  1  271  ? -44.825 70.437  74.787  1.00 18.96 ? 269  LEU A CD2   1 
ATOM   1892  N  N     . HIS A  1  272  ? -42.543 72.256  79.322  1.00 18.33 ? 270  HIS A N     1 
ATOM   1893  C  CA    . HIS A  1  272  ? -42.389 73.417  80.179  1.00 17.78 ? 270  HIS A CA    1 
ATOM   1894  C  C     . HIS A  1  272  ? -41.038 73.311  80.853  1.00 18.15 ? 270  HIS A C     1 
ATOM   1895  O  O     . HIS A  1  272  ? -40.677 72.220  81.308  1.00 18.58 ? 270  HIS A O     1 
ATOM   1896  C  CB    . HIS A  1  272  ? -43.498 73.498  81.227  1.00 18.39 ? 270  HIS A CB    1 
ATOM   1897  C  CG    . HIS A  1  272  ? -43.628 74.854  81.829  1.00 19.81 ? 270  HIS A CG    1 
ATOM   1898  N  ND1   . HIS A  1  272  ? -42.717 75.351  82.737  1.00 23.38 ? 270  HIS A ND1   1 
ATOM   1899  C  CD2   . HIS A  1  272  ? -44.541 75.833  81.630  1.00 22.57 ? 270  HIS A CD2   1 
ATOM   1900  C  CE1   . HIS A  1  272  ? -43.064 76.584  83.068  1.00 22.32 ? 270  HIS A CE1   1 
ATOM   1901  N  NE2   . HIS A  1  272  ? -44.166 76.901  82.409  1.00 24.10 ? 270  HIS A NE2   1 
ATOM   1902  N  N     . PRO A  1  273  ? -40.276 74.402  80.954  1.00 18.35 ? 271  PRO A N     1 
ATOM   1903  C  CA    . PRO A  1  273  ? -38.951 74.324  81.586  1.00 16.65 ? 271  PRO A CA    1 
ATOM   1904  C  C     . PRO A  1  273  ? -38.996 74.217  83.101  1.00 21.57 ? 271  PRO A C     1 
ATOM   1905  O  O     . PRO A  1  273  ? -37.969 73.878  83.704  1.00 21.51 ? 271  PRO A O     1 
ATOM   1906  C  CB    . PRO A  1  273  ? -38.280 75.633  81.145  1.00 19.59 ? 271  PRO A CB    1 
ATOM   1907  C  CG    . PRO A  1  273  ? -39.422 76.586  80.967  1.00 20.70 ? 271  PRO A CG    1 
ATOM   1908  C  CD    . PRO A  1  273  ? -40.564 75.738  80.407  1.00 20.97 ? 271  PRO A CD    1 
ATOM   1909  N  N     . ARG A  1  274  ? -40.142 74.474  83.729  1.00 18.24 ? 272  ARG A N     1 
ATOM   1910  C  CA    . ARG A  1  274  ? -40.256 74.353  85.178  1.00 17.17 ? 272  ARG A CA    1 
ATOM   1911  C  C     . ARG A  1  274  ? -41.373 73.392  85.562  1.00 17.03 ? 272  ARG A C     1 
ATOM   1912  O  O     . ARG A  1  274  ? -42.297 73.740  86.311  1.00 20.04 ? 272  ARG A O     1 
ATOM   1913  C  CB    . ARG A  1  274  ? -40.504 75.714  85.810  1.00 16.80 ? 272  ARG A CB    1 
ATOM   1914  C  CG    . ARG A  1  274  ? -39.413 76.747  85.515  1.00 17.89 ? 272  ARG A CG    1 
ATOM   1915  C  CD    . ARG A  1  274  ? -38.040 76.273  86.036  1.00 19.09 ? 272  ARG A CD    1 
ATOM   1916  N  NE    . ARG A  1  274  ? -38.087 75.827  87.427  1.00 21.56 ? 272  ARG A NE    1 
ATOM   1917  C  CZ    . ARG A  1  274  ? -38.072 76.640  88.478  1.00 19.44 ? 272  ARG A CZ    1 
ATOM   1918  N  NH1   . ARG A  1  274  ? -38.044 77.955  88.336  1.00 20.08 ? 272  ARG A NH1   1 
ATOM   1919  N  NH2   . ARG A  1  274  ? -38.085 76.121  89.704  1.00 22.09 ? 272  ARG A NH2   1 
ATOM   1920  N  N     . TYR A  1  275  ? -41.297 72.174  85.046  1.00 15.88 ? 273  TYR A N     1 
ATOM   1921  C  CA    . TYR A  1  275  ? -42.299 71.157  85.334  1.00 15.15 ? 273  TYR A CA    1 
ATOM   1922  C  C     . TYR A  1  275  ? -41.941 70.520  86.667  1.00 17.60 ? 273  TYR A C     1 
ATOM   1923  O  O     . TYR A  1  275  ? -41.127 69.599  86.733  1.00 18.51 ? 273  TYR A O     1 
ATOM   1924  C  CB    . TYR A  1  275  ? -42.342 70.150  84.190  1.00 17.01 ? 273  TYR A CB    1 
ATOM   1925  C  CG    . TYR A  1  275  ? -43.267 69.001  84.445  1.00 16.43 ? 273  TYR A CG    1 
ATOM   1926  C  CD1   . TYR A  1  275  ? -44.552 69.217  84.880  1.00 16.73 ? 273  TYR A CD1   1 
ATOM   1927  C  CD2   . TYR A  1  275  ? -42.837 67.696  84.251  1.00 16.82 ? 273  TYR A CD2   1 
ATOM   1928  C  CE1   . TYR A  1  275  ? -45.396 68.162  85.148  1.00 18.59 ? 273  TYR A CE1   1 
ATOM   1929  C  CE2   . TYR A  1  275  ? -43.667 66.632  84.504  1.00 16.95 ? 273  TYR A CE2   1 
ATOM   1930  C  CZ    . TYR A  1  275  ? -44.947 66.876  84.958  1.00 17.14 ? 273  TYR A CZ    1 
ATOM   1931  O  OH    . TYR A  1  275  ? -45.802 65.833  85.219  1.00 19.81 ? 273  TYR A OH    1 
ATOM   1932  N  N     . SER A  1  276  ? -42.542 71.025  87.741  1.00 16.58 ? 274  SER A N     1 
ATOM   1933  C  CA    . SER A  1  276  ? -42.255 70.513  89.072  1.00 16.19 ? 274  SER A CA    1 
ATOM   1934  C  C     . SER A  1  276  ? -43.383 70.922  90.002  1.00 18.09 ? 274  SER A C     1 
ATOM   1935  O  O     . SER A  1  276  ? -44.087 71.909  89.756  1.00 18.02 ? 274  SER A O     1 
ATOM   1936  C  CB    . SER A  1  276  ? -40.922 71.041  89.607  1.00 20.72 ? 274  SER A CB    1 
ATOM   1937  O  OG    . SER A  1  276  ? -41.033 72.418  89.899  1.00 24.08 ? 274  SER A OG    1 
ATOM   1938  N  N     . ARG A  1  277  ? -43.534 70.147  91.083  1.00 18.61 ? 275  ARG A N     1 
ATOM   1939  C  CA    . ARG A  1  277  ? -44.517 70.478  92.111  1.00 15.95 ? 275  ARG A CA    1 
ATOM   1940  C  C     . ARG A  1  277  ? -44.294 71.881  92.668  1.00 17.97 ? 275  ARG A C     1 
ATOM   1941  O  O     . ARG A  1  277  ? -45.260 72.600  92.937  1.00 18.44 ? 275  ARG A O     1 
ATOM   1942  C  CB    . ARG A  1  277  ? -44.474 69.442  93.240  1.00 18.82 ? 275  ARG A CB    1 
ATOM   1943  C  CG    . ARG A  1  277  ? -45.344 69.791  94.442  1.00 18.79 ? 275  ARG A CG    1 
ATOM   1944  C  CD    . ARG A  1  277  ? -46.816 69.987  94.056  1.00 19.27 ? 275  ARG A CD    1 
ATOM   1945  N  NE    . ARG A  1  277  ? -47.650 70.307  95.210  1.00 18.18 ? 275  ARG A NE    1 
ATOM   1946  C  CZ    . ARG A  1  277  ? -47.832 71.531  95.691  1.00 19.49 ? 275  ARG A CZ    1 
ATOM   1947  N  NH1   . ARG A  1  277  ? -47.215 72.581  95.168  1.00 19.24 ? 275  ARG A NH1   1 
ATOM   1948  N  NH2   . ARG A  1  277  ? -48.667 71.711  96.715  1.00 19.32 ? 275  ARG A NH2   1 
ATOM   1949  N  N     . ALA A  1  278  ? -43.032 72.292  92.841  1.00 19.35 ? 276  ALA A N     1 
ATOM   1950  C  CA    . ALA A  1  278  ? -42.766 73.627  93.384  1.00 20.14 ? 276  ALA A CA    1 
ATOM   1951  C  C     . ALA A  1  278  ? -43.336 74.716  92.489  1.00 18.96 ? 276  ALA A C     1 
ATOM   1952  O  O     . ALA A  1  278  ? -43.690 75.803  92.965  1.00 20.68 ? 276  ALA A O     1 
ATOM   1953  C  CB    . ALA A  1  278  ? -41.259 73.838  93.572  1.00 19.95 ? 276  ALA A CB    1 
ATOM   1954  N  N     . GLN A  1  279  ? -43.428 74.446  91.194  1.00 17.58 ? 277  GLN A N     1 
ATOM   1955  C  CA    . GLN A  1  279  ? -43.947 75.390  90.220  1.00 16.47 ? 277  GLN A CA    1 
ATOM   1956  C  C     . GLN A  1  279  ? -45.333 74.981  89.738  1.00 22.08 ? 277  GLN A C     1 
ATOM   1957  O  O     . GLN A  1  279  ? -45.685 75.233  88.590  1.00 18.89 ? 277  GLN A O     1 
ATOM   1958  C  CB    . GLN A  1  279  ? -42.983 75.490  89.040  1.00 18.48 ? 277  GLN A CB    1 
ATOM   1959  C  CG    . GLN A  1  279  ? -41.582 75.952  89.429  1.00 20.33 ? 277  GLN A CG    1 
ATOM   1960  C  CD    . GLN A  1  279  ? -41.591 77.362  89.960  1.00 25.89 ? 277  GLN A CD    1 
ATOM   1961  O  OE1   . GLN A  1  279  ? -42.214 78.244  89.378  1.00 30.42 ? 277  GLN A OE1   1 
ATOM   1962  N  NE2   . GLN A  1  279  ? -40.920 77.581  91.088  1.00 20.26 ? 277  GLN A NE2   1 
ATOM   1963  N  N     . ALA A  1  280  ? -46.132 74.358  90.610  1.00 19.18 ? 278  ALA A N     1 
ATOM   1964  C  CA    . ALA A  1  280  ? -47.397 73.773  90.165  1.00 19.29 ? 278  ALA A CA    1 
ATOM   1965  C  C     . ALA A  1  280  ? -48.322 74.811  89.537  1.00 17.59 ? 278  ALA A C     1 
ATOM   1966  O  O     . ALA A  1  280  ? -49.036 74.508  88.575  1.00 19.91 ? 278  ALA A O     1 
ATOM   1967  C  CB    . ALA A  1  280  ? -48.099 73.081  91.329  1.00 20.50 ? 278  ALA A CB    1 
ATOM   1968  N  N     . ALA A  1  281  ? -48.343 76.033  90.072  1.00 17.94 ? 279  ALA A N     1 
ATOM   1969  C  CA    . ALA A  1  281  ? -49.223 77.048  89.504  1.00 20.44 ? 279  ALA A CA    1 
ATOM   1970  C  C     . ALA A  1  281  ? -48.825 77.386  88.072  1.00 20.61 ? 279  ALA A C     1 
ATOM   1971  O  O     . ALA A  1  281  ? -49.693 77.549  87.205  1.00 20.28 ? 279  ALA A O     1 
ATOM   1972  C  CB    . ALA A  1  281  ? -49.226 78.305  90.375  1.00 22.57 ? 279  ALA A CB    1 
ATOM   1973  N  N     . ARG A  1  282  ? -47.523 77.492  87.799  1.00 16.75 ? 280  ARG A N     1 
ATOM   1974  C  CA    . ARG A  1  282  ? -47.103 77.731  86.419  1.00 19.80 ? 280  ARG A CA    1 
ATOM   1975  C  C     . ARG A  1  282  ? -47.411 76.526  85.544  1.00 18.83 ? 280  ARG A C     1 
ATOM   1976  O  O     . ARG A  1  282  ? -47.746 76.678  84.364  1.00 19.68 ? 280  ARG A O     1 
ATOM   1977  C  CB    . ARG A  1  282  ? -45.610 78.050  86.353  1.00 20.56 ? 280  ARG A CB    1 
ATOM   1978  C  CG    . ARG A  1  282  ? -45.222 79.360  87.000  1.00 25.29 ? 280  ARG A CG    1 
ATOM   1979  C  CD    . ARG A  1  282  ? -43.802 79.720  86.605  1.00 22.54 ? 280  ARG A CD    1 
ATOM   1980  N  NE    . ARG A  1  282  ? -43.705 79.871  85.158  1.00 23.05 ? 280  ARG A NE    1 
ATOM   1981  C  CZ    . ARG A  1  282  ? -42.574 79.835  84.466  1.00 20.74 ? 280  ARG A CZ    1 
ATOM   1982  N  NH1   . ARG A  1  282  ? -41.400 79.660  85.060  1.00 19.59 ? 280  ARG A NH1   1 
ATOM   1983  N  NH2   . ARG A  1  282  ? -42.622 79.968  83.142  1.00 20.77 ? 280  ARG A NH2   1 
ATOM   1984  N  N     . VAL A  1  283  ? -47.274 75.321  86.101  1.00 17.95 ? 281  VAL A N     1 
ATOM   1985  C  CA    . VAL A  1  283  ? -47.589 74.110  85.350  1.00 17.25 ? 281  VAL A CA    1 
ATOM   1986  C  C     . VAL A  1  283  ? -49.053 74.110  84.926  1.00 19.87 ? 281  VAL A C     1 
ATOM   1987  O  O     . VAL A  1  283  ? -49.375 73.880  83.758  1.00 19.34 ? 281  VAL A O     1 
ATOM   1988  C  CB    . VAL A  1  283  ? -47.237 72.870  86.184  1.00 16.33 ? 281  VAL A CB    1 
ATOM   1989  C  CG1   . VAL A  1  283  ? -47.813 71.609  85.542  1.00 21.05 ? 281  VAL A CG1   1 
ATOM   1990  C  CG2   . VAL A  1  283  ? -45.726 72.772  86.331  1.00 18.86 ? 281  VAL A CG2   1 
ATOM   1991  N  N     . MET A  1  284  ? -49.962 74.386  85.860  1.00 18.15 ? 282  MET A N     1 
ATOM   1992  C  CA    . MET A  1  284  ? -51.380 74.361  85.501  1.00 18.26 ? 282  MET A CA    1 
ATOM   1993  C  C     . MET A  1  284  ? -51.751 75.533  84.608  1.00 19.10 ? 282  MET A C     1 
ATOM   1994  O  O     . MET A  1  284  ? -52.639 75.408  83.758  1.00 21.88 ? 282  MET A O     1 
ATOM   1995  C  CB    . MET A  1  284  ? -52.260 74.356  86.754  1.00 19.33 ? 282  MET A CB    1 
ATOM   1996  C  CG    . MET A  1  284  ? -51.997 73.199  87.715  1.00 21.08 ? 282  MET A CG    1 
ATOM   1997  S  SD    . MET A  1  284  ? -52.128 71.562  86.962  1.00 22.45 ? 282  MET A SD    1 
ATOM   1998  C  CE    . MET A  1  284  ? -53.870 71.495  86.555  1.00 22.53 ? 282  MET A CE    1 
ATOM   1999  N  N     . GLY A  1  285  ? -51.097 76.678  84.784  1.00 18.90 ? 283  GLY A N     1 
ATOM   2000  C  CA    . GLY A  1  285  ? -51.438 77.831  83.977  1.00 19.01 ? 283  GLY A CA    1 
ATOM   2001  C  C     . GLY A  1  285  ? -50.822 77.814  82.599  1.00 20.30 ? 283  GLY A C     1 
ATOM   2002  O  O     . GLY A  1  285  ? -51.394 78.384  81.663  1.00 21.72 ? 283  GLY A O     1 
ATOM   2003  N  N     . GLU A  1  286  ? -49.661 77.174  82.441  1.00 18.68 ? 284  GLU A N     1 
ATOM   2004  C  CA    . GLU A  1  286  ? -48.894 77.336  81.212  1.00 19.31 ? 284  GLU A CA    1 
ATOM   2005  C  C     . GLU A  1  286  ? -48.643 76.028  80.490  1.00 20.88 ? 284  GLU A C     1 
ATOM   2006  O  O     . GLU A  1  286  ? -48.627 75.994  79.254  1.00 21.90 ? 284  GLU A O     1 
ATOM   2007  C  CB    . GLU A  1  286  ? -47.537 78.005  81.506  1.00 20.82 ? 284  GLU A CB    1 
ATOM   2008  C  CG    . GLU A  1  286  ? -47.625 79.352  82.196  1.00 22.89 ? 284  GLU A CG    1 
ATOM   2009  C  CD    . GLU A  1  286  ? -46.286 79.796  82.758  1.00 25.36 ? 284  GLU A CD    1 
ATOM   2010  O  OE1   . GLU A  1  286  ? -45.250 79.392  82.204  1.00 26.68 ? 284  GLU A OE1   1 
ATOM   2011  O  OE2   . GLU A  1  286  ? -46.276 80.555  83.752  1.00 26.15 ? 284  GLU A OE2   1 
ATOM   2012  N  N     . LEU A  1  287  ? -48.394 74.951  81.228  1.00 17.96 ? 285  LEU A N     1 
ATOM   2013  C  CA    A LEU A  1  287  ? -48.170 73.662  80.594  0.66 18.18 ? 285  LEU A CA    1 
ATOM   2014  C  CA    B LEU A  1  287  ? -48.172 73.663  80.596  0.34 18.23 ? 285  LEU A CA    1 
ATOM   2015  C  C     . LEU A  1  287  ? -49.492 73.028  80.184  1.00 20.71 ? 285  LEU A C     1 
ATOM   2016  O  O     . LEU A  1  287  ? -49.628 72.551  79.056  1.00 19.63 ? 285  LEU A O     1 
ATOM   2017  C  CB    A LEU A  1  287  ? -47.386 72.741  81.539  0.66 17.78 ? 285  LEU A CB    1 
ATOM   2018  C  CB    B LEU A  1  287  ? -47.391 72.752  81.544  0.34 17.82 ? 285  LEU A CB    1 
ATOM   2019  C  CG    A LEU A  1  287  ? -46.512 71.620  80.954  0.66 20.04 ? 285  LEU A CG    1 
ATOM   2020  C  CG    B LEU A  1  287  ? -47.413 71.253  81.254  0.34 19.82 ? 285  LEU A CG    1 
ATOM   2021  C  CD1   A LEU A  1  287  ? -45.708 70.931  82.033  0.66 18.15 ? 285  LEU A CD1   1 
ATOM   2022  C  CD1   B LEU A  1  287  ? -46.909 70.966  79.862  0.34 22.47 ? 285  LEU A CD1   1 
ATOM   2023  C  CD2   A LEU A  1  287  ? -47.318 70.591  80.201  0.66 23.57 ? 285  LEU A CD2   1 
ATOM   2024  C  CD2   B LEU A  1  287  ? -46.584 70.508  82.283  0.34 18.55 ? 285  LEU A CD2   1 
ATOM   2025  N  N     . LEU A  1  288  ? -50.469 73.021  81.091  1.00 18.29 ? 286  LEU A N     1 
ATOM   2026  C  CA    . LEU A  1  288  ? -51.770 72.415  80.800  1.00 20.17 ? 286  LEU A CA    1 
ATOM   2027  C  C     . LEU A  1  288  ? -52.390 72.900  79.494  1.00 20.42 ? 286  LEU A C     1 
ATOM   2028  O  O     . LEU A  1  288  ? -52.815 72.049  78.696  1.00 19.81 ? 286  LEU A O     1 
ATOM   2029  C  CB    . LEU A  1  288  ? -52.725 72.646  81.978  1.00 22.22 ? 286  LEU A CB    1 
ATOM   2030  C  CG    . LEU A  1  288  ? -54.178 72.254  81.703  1.00 26.38 ? 286  LEU A CG    1 
ATOM   2031  C  CD1   . LEU A  1  288  ? -54.298 70.747  81.505  1.00 22.62 ? 286  LEU A CD1   1 
ATOM   2032  C  CD2   . LEU A  1  288  ? -55.061 72.728  82.844  1.00 37.13 ? 286  LEU A CD2   1 
ATOM   2033  N  N     . PRO A  1  289  ? -52.460 74.204  79.197  1.00 18.82 ? 287  PRO A N     1 
ATOM   2034  C  CA    . PRO A  1  289  ? -53.059 74.614  77.914  1.00 17.38 ? 287  PRO A CA    1 
ATOM   2035  C  C     . PRO A  1  289  ? -52.336 74.053  76.709  1.00 18.71 ? 287  PRO A C     1 
ATOM   2036  O  O     . PRO A  1  289  ? -52.968 73.821  75.666  1.00 19.05 ? 287  PRO A O     1 
ATOM   2037  C  CB    . PRO A  1  289  ? -52.969 76.144  77.955  1.00 20.73 ? 287  PRO A CB    1 
ATOM   2038  C  CG    . PRO A  1  289  ? -52.922 76.475  79.400  1.00 25.46 ? 287  PRO A CG    1 
ATOM   2039  C  CD    . PRO A  1  289  ? -52.144 75.372  80.042  1.00 21.68 ? 287  PRO A CD    1 
ATOM   2040  N  N     . ARG A  1  290  ? -51.021 73.863  76.806  1.00 18.37 ? 288  ARG A N     1 
ATOM   2041  C  CA    . ARG A  1  290  ? -50.271 73.280  75.700  1.00 18.80 ? 288  ARG A CA    1 
ATOM   2042  C  C     . ARG A  1  290  ? -50.652 71.830  75.489  1.00 17.96 ? 288  ARG A C     1 
ATOM   2043  O  O     . ARG A  1  290  ? -50.853 71.400  74.350  1.00 17.38 ? 288  ARG A O     1 
ATOM   2044  C  CB    . ARG A  1  290  ? -48.770 73.414  75.953  1.00 19.58 ? 288  ARG A CB    1 
ATOM   2045  C  CG    . ARG A  1  290  ? -48.358 74.854  76.105  1.00 20.76 ? 288  ARG A CG    1 
ATOM   2046  C  CD    . ARG A  1  290  ? -46.888 74.995  76.444  1.00 23.99 ? 288  ARG A CD    1 
ATOM   2047  N  NE    . ARG A  1  290  ? -46.574 76.406  76.656  1.00 28.98 ? 288  ARG A NE    1 
ATOM   2048  C  CZ    . ARG A  1  290  ? -45.604 76.847  77.446  1.00 30.12 ? 288  ARG A CZ    1 
ATOM   2049  N  NH1   . ARG A  1  290  ? -44.812 76.013  78.100  1.00 24.73 ? 288  ARG A NH1   1 
ATOM   2050  N  NH2   . ARG A  1  290  ? -45.429 78.159  77.588  1.00 36.06 ? 288  ARG A NH2   1 
ATOM   2051  N  N     . VAL A  1  291  ? -50.757 71.056  76.570  1.00 17.63 ? 289  VAL A N     1 
ATOM   2052  C  CA    . VAL A  1  291  ? -51.201 69.678  76.411  1.00 17.35 ? 289  VAL A CA    1 
ATOM   2053  C  C     . VAL A  1  291  ? -52.610 69.646  75.851  1.00 17.71 ? 289  VAL A C     1 
ATOM   2054  O  O     . VAL A  1  291  ? -52.926 68.825  74.983  1.00 17.33 ? 289  VAL A O     1 
ATOM   2055  C  CB    . VAL A  1  291  ? -51.118 68.909  77.738  1.00 18.25 ? 289  VAL A CB    1 
ATOM   2056  C  CG1   . VAL A  1  291  ? -51.466 67.454  77.500  1.00 17.68 ? 289  VAL A CG1   1 
ATOM   2057  C  CG2   . VAL A  1  291  ? -49.738 69.033  78.307  1.00 20.34 ? 289  VAL A CG2   1 
ATOM   2058  N  N     . LYS A  1  292  ? -53.470 70.543  76.331  1.00 16.96 ? 290  LYS A N     1 
ATOM   2059  C  CA    . LYS A  1  292  ? -54.836 70.585  75.822  1.00 16.77 ? 290  LYS A CA    1 
ATOM   2060  C  C     . LYS A  1  292  ? -54.853 70.850  74.325  1.00 18.66 ? 290  LYS A C     1 
ATOM   2061  O  O     . LYS A  1  292  ? -55.594 70.192  73.582  1.00 16.05 ? 290  LYS A O     1 
ATOM   2062  C  CB    . LYS A  1  292  ? -55.656 71.635  76.564  1.00 17.46 ? 290  LYS A CB    1 
ATOM   2063  C  CG    . LYS A  1  292  ? -57.081 71.735  76.007  1.00 19.62 ? 290  LYS A CG    1 
ATOM   2064  C  CD    . LYS A  1  292  ? -57.921 72.799  76.672  1.00 19.46 ? 290  LYS A CD    1 
ATOM   2065  C  CE    . LYS A  1  292  ? -59.288 72.824  75.999  1.00 21.25 ? 290  LYS A CE    1 
ATOM   2066  N  NZ    . LYS A  1  292  ? -60.218 73.665  76.787  1.00 23.12 ? 290  LYS A NZ    1 
ATOM   2067  N  N     . ALA A  1  293  ? -54.028 71.791  73.857  1.00 17.14 ? 291  ALA A N     1 
ATOM   2068  C  CA    . ALA A  1  293  ? -54.015 72.086  72.428  1.00 17.37 ? 291  ALA A CA    1 
ATOM   2069  C  C     . ALA A  1  293  ? -53.541 70.887  71.620  1.00 15.14 ? 291  ALA A C     1 
ATOM   2070  O  O     . ALA A  1  293  ? -54.087 70.598  70.549  1.00 18.56 ? 291  ALA A O     1 
ATOM   2071  C  CB    . ALA A  1  293  ? -53.148 73.317  72.144  1.00 16.76 ? 291  ALA A CB    1 
ATOM   2072  N  N     . LEU A  1  294  ? -52.525 70.169  72.110  1.00 15.82 ? 292  LEU A N     1 
ATOM   2073  C  CA    . LEU A  1  294  ? -52.098 68.961  71.411  1.00 16.70 ? 292  LEU A CA    1 
ATOM   2074  C  C     . LEU A  1  294  ? -53.188 67.902  71.458  1.00 15.57 ? 292  LEU A C     1 
ATOM   2075  O  O     . LEU A  1  294  ? -53.443 67.219  70.464  1.00 16.45 ? 292  LEU A O     1 
ATOM   2076  C  CB    . LEU A  1  294  ? -50.813 68.415  72.024  1.00 17.51 ? 292  LEU A CB    1 
ATOM   2077  C  CG    . LEU A  1  294  ? -49.614 69.344  71.894  1.00 16.69 ? 292  LEU A CG    1 
ATOM   2078  C  CD1   . LEU A  1  294  ? -48.456 68.714  72.658  1.00 17.99 ? 292  LEU A CD1   1 
ATOM   2079  C  CD2   . LEU A  1  294  ? -49.247 69.576  70.423  1.00 18.37 ? 292  LEU A CD2   1 
ATOM   2080  N  N     . ALA A  1  295  ? -53.846 67.761  72.607  1.00 15.86 ? 293  ALA A N     1 
ATOM   2081  C  CA    . ALA A  1  295  ? -54.898 66.755  72.732  1.00 17.67 ? 293  ALA A CA    1 
ATOM   2082  C  C     . ALA A  1  295  ? -56.081 67.073  71.823  1.00 18.78 ? 293  ALA A C     1 
ATOM   2083  O  O     . ALA A  1  295  ? -56.689 66.161  71.250  1.00 16.66 ? 293  ALA A O     1 
ATOM   2084  C  CB    . ALA A  1  295  ? -55.348 66.650  74.192  1.00 17.70 ? 293  ALA A CB    1 
ATOM   2085  N  N     . LEU A  1  296  ? -56.412 68.361  71.670  1.00 15.45 ? 294  LEU A N     1 
ATOM   2086  C  CA    . LEU A  1  296  ? -57.482 68.741  70.755  1.00 16.72 ? 294  LEU A CA    1 
ATOM   2087  C  C     . LEU A  1  296  ? -57.169 68.317  69.331  1.00 17.27 ? 294  LEU A C     1 
ATOM   2088  O  O     . LEU A  1  296  ? -58.063 67.894  68.592  1.00 17.63 ? 294  LEU A O     1 
ATOM   2089  C  CB    . LEU A  1  296  ? -57.723 70.249  70.801  1.00 17.10 ? 294  LEU A CB    1 
ATOM   2090  C  CG    . LEU A  1  296  ? -58.419 70.762  72.059  1.00 20.45 ? 294  LEU A CG    1 
ATOM   2091  C  CD1   . LEU A  1  296  ? -58.307 72.289  72.122  1.00 21.31 ? 294  LEU A CD1   1 
ATOM   2092  C  CD2   . LEU A  1  296  ? -59.880 70.324  72.089  1.00 20.42 ? 294  LEU A CD2   1 
ATOM   2093  N  N     . LEU A  1  297  ? -55.908 68.435  68.923  1.00 15.91 ? 295  LEU A N     1 
ATOM   2094  C  CA    . LEU A  1  297  ? -55.541 68.013  67.578  1.00 18.54 ? 295  LEU A CA    1 
ATOM   2095  C  C     . LEU A  1  297  ? -55.588 66.496  67.460  1.00 17.54 ? 295  LEU A C     1 
ATOM   2096  O  O     . LEU A  1  297  ? -56.073 65.962  66.460  1.00 18.70 ? 295  LEU A O     1 
ATOM   2097  C  CB    . LEU A  1  297  ? -54.154 68.554  67.230  1.00 23.24 ? 295  LEU A CB    1 
ATOM   2098  C  CG    . LEU A  1  297  ? -53.740 68.450  65.767  1.00 24.06 ? 295  LEU A CG    1 
ATOM   2099  C  CD1   . LEU A  1  297  ? -54.692 69.267  64.876  1.00 25.19 ? 295  LEU A CD1   1 
ATOM   2100  C  CD2   . LEU A  1  297  ? -52.293 68.934  65.657  1.00 25.46 ? 295  LEU A CD2   1 
ATOM   2101  N  N     . ALA A  1  298  ? -55.096 65.784  68.484  1.00 17.20 ? 296  ALA A N     1 
ATOM   2102  C  CA    . ALA A  1  298  ? -55.213 64.332  68.488  1.00 18.52 ? 296  ALA A CA    1 
ATOM   2103  C  C     . ALA A  1  298  ? -56.672 63.902  68.428  1.00 18.14 ? 296  ALA A C     1 
ATOM   2104  O  O     . ALA A  1  298  ? -57.011 62.950  67.716  1.00 17.96 ? 296  ALA A O     1 
ATOM   2105  C  CB    . ALA A  1  298  ? -54.527 63.746  69.722  1.00 19.31 ? 296  ALA A CB    1 
ATOM   2106  N  N     . LYS A  1  299  ? -57.551 64.597  69.163  1.00 16.41 ? 297  LYS A N     1 
ATOM   2107  C  CA    . LYS A  1  299  ? -58.979 64.302  69.086  1.00 16.32 ? 297  LYS A CA    1 
ATOM   2108  C  C     . LYS A  1  299  ? -59.504 64.448  67.662  1.00 20.18 ? 297  LYS A C     1 
ATOM   2109  O  O     . LYS A  1  299  ? -60.272 63.598  67.189  1.00 20.30 ? 297  LYS A O     1 
ATOM   2110  C  CB    . LYS A  1  299  ? -59.753 65.216  70.042  1.00 15.68 ? 297  LYS A CB    1 
ATOM   2111  C  CG    . LYS A  1  299  ? -61.224 65.348  69.702  1.00 18.26 ? 297  LYS A CG    1 
ATOM   2112  C  CD    . LYS A  1  299  ? -61.999 66.117  70.761  1.00 20.13 ? 297  LYS A CD    1 
ATOM   2113  C  CE    . LYS A  1  299  ? -63.334 66.589  70.193  1.00 21.22 ? 297  LYS A CE    1 
ATOM   2114  N  NZ    . LYS A  1  299  ? -64.172 67.232  71.237  1.00 28.40 ? 297  LYS A NZ    1 
ATOM   2115  N  N     . ASN A  1  300  ? -59.096 65.509  66.954  1.00 17.86 ? 298  ASN A N     1 
ATOM   2116  C  CA    . ASN A  1  300  ? -59.668 65.719  65.632  1.00 18.55 ? 298  ASN A CA    1 
ATOM   2117  C  C     . ASN A  1  300  ? -59.259 64.618  64.663  1.00 17.82 ? 298  ASN A C     1 
ATOM   2118  O  O     . ASN A  1  300  ? -60.069 64.188  63.829  1.00 20.56 ? 298  ASN A O     1 
ATOM   2119  C  CB    . ASN A  1  300  ? -59.276 67.076  65.073  1.00 22.18 ? 298  ASN A CB    1 
ATOM   2120  C  CG    . ASN A  1  300  ? -60.097 67.420  63.846  1.00 27.04 ? 298  ASN A CG    1 
ATOM   2121  O  OD1   . ASN A  1  300  ? -61.275 67.803  63.948  1.00 33.85 ? 298  ASN A OD1   1 
ATOM   2122  N  ND2   . ASN A  1  300  ? -59.505 67.241  62.688  1.00 23.76 ? 298  ASN A ND2   1 
ATOM   2123  N  N     . TYR A  1  301  ? -58.020 64.146  64.757  1.00 16.87 ? 299  TYR A N     1 
ATOM   2124  C  CA    . TYR A  1  301  ? -57.579 63.032  63.931  1.00 17.89 ? 299  TYR A CA    1 
ATOM   2125  C  C     . TYR A  1  301  ? -57.977 61.677  64.500  1.00 19.02 ? 299  TYR A C     1 
ATOM   2126  O  O     . TYR A  1  301  ? -57.811 60.663  63.809  1.00 20.41 ? 299  TYR A O     1 
ATOM   2127  C  CB    . TYR A  1  301  ? -56.065 63.063  63.778  1.00 18.02 ? 299  TYR A CB    1 
ATOM   2128  C  CG    . TYR A  1  301  ? -55.522 64.136  62.881  1.00 17.93 ? 299  TYR A CG    1 
ATOM   2129  C  CD1   . TYR A  1  301  ? -55.683 64.072  61.509  1.00 19.87 ? 299  TYR A CD1   1 
ATOM   2130  C  CD2   . TYR A  1  301  ? -54.785 65.177  63.412  1.00 17.95 ? 299  TYR A CD2   1 
ATOM   2131  C  CE1   . TYR A  1  301  ? -55.133 65.045  60.679  1.00 19.08 ? 299  TYR A CE1   1 
ATOM   2132  C  CE2   . TYR A  1  301  ? -54.225 66.145  62.599  1.00 18.92 ? 299  TYR A CE2   1 
ATOM   2133  C  CZ    . TYR A  1  301  ? -54.418 66.086  61.232  1.00 23.53 ? 299  TYR A CZ    1 
ATOM   2134  O  OH    . TYR A  1  301  ? -53.856 67.058  60.417  1.00 20.14 ? 299  TYR A OH    1 
ATOM   2135  N  N     . ASP A  1  302  ? -58.468 61.646  65.738  1.00 17.49 ? 300  ASP A N     1 
ATOM   2136  C  CA    . ASP A  1  302  ? -58.812 60.427  66.461  1.00 18.24 ? 300  ASP A CA    1 
ATOM   2137  C  C     . ASP A  1  302  ? -57.616 59.474  66.556  1.00 18.47 ? 300  ASP A C     1 
ATOM   2138  O  O     . ASP A  1  302  ? -57.672 58.315  66.148  1.00 18.90 ? 300  ASP A O     1 
ATOM   2139  C  CB    . ASP A  1  302  ? -60.027 59.727  65.835  1.00 19.57 ? 300  ASP A CB    1 
ATOM   2140  C  CG    . ASP A  1  302  ? -60.729 58.821  66.822  1.00 23.36 ? 300  ASP A CG    1 
ATOM   2141  O  OD1   . ASP A  1  302  ? -60.683 59.131  68.037  1.00 21.98 ? 300  ASP A OD1   1 
ATOM   2142  O  OD2   . ASP A  1  302  ? -61.311 57.802  66.394  1.00 25.41 ? 300  ASP A OD2   1 
ATOM   2143  N  N     . ILE A  1  303  ? -56.527 59.982  67.133  1.00 17.65 ? 301  ILE A N     1 
ATOM   2144  C  CA    . ILE A  1  303  ? -55.351 59.173  67.429  1.00 17.87 ? 301  ILE A CA    1 
ATOM   2145  C  C     . ILE A  1  303  ? -55.100 59.180  68.930  1.00 18.41 ? 301  ILE A C     1 
ATOM   2146  O  O     . ILE A  1  303  ? -55.595 60.027  69.671  1.00 17.50 ? 301  ILE A O     1 
ATOM   2147  C  CB    . ILE A  1  303  ? -54.086 59.661  66.688  1.00 17.05 ? 301  ILE A CB    1 
ATOM   2148  C  CG1   . ILE A  1  303  ? -53.630 61.028  67.211  1.00 16.67 ? 301  ILE A CG1   1 
ATOM   2149  C  CG2   . ILE A  1  303  ? -54.357 59.744  65.184  1.00 17.18 ? 301  ILE A CG2   1 
ATOM   2150  C  CD1   . ILE A  1  303  ? -52.305 61.493  66.610  1.00 19.11 ? 301  ILE A CD1   1 
ATOM   2151  N  N     . GLY A  1  304  ? -54.297 58.223  69.373  1.00 18.72 ? 302  GLY A N     1 
ATOM   2152  C  CA    . GLY A  1  304  ? -53.906 58.203  70.774  1.00 16.92 ? 302  GLY A CA    1 
ATOM   2153  C  C     . GLY A  1  304  ? -52.896 59.299  71.072  1.00 17.82 ? 302  GLY A C     1 
ATOM   2154  O  O     . GLY A  1  304  ? -52.064 59.661  70.232  1.00 18.04 ? 302  GLY A O     1 
ATOM   2155  N  N     . LEU A  1  305  ? -52.994 59.851  72.281  1.00 15.90 ? 303  LEU A N     1 
ATOM   2156  C  CA    . LEU A  1  305  ? -51.994 60.773  72.811  1.00 14.99 ? 303  LEU A CA    1 
ATOM   2157  C  C     . LEU A  1  305  ? -51.670 60.293  74.213  1.00 18.16 ? 303  LEU A C     1 
ATOM   2158  O  O     . LEU A  1  305  ? -52.506 60.408  75.112  1.00 17.60 ? 303  LEU A O     1 
ATOM   2159  C  CB    . LEU A  1  305  ? -52.498 62.218  72.824  1.00 17.73 ? 303  LEU A CB    1 
ATOM   2160  C  CG    . LEU A  1  305  ? -51.458 63.264  73.237  1.00 20.00 ? 303  LEU A CG    1 
ATOM   2161  C  CD1   . LEU A  1  305  ? -51.720 64.606  72.569  1.00 19.42 ? 303  LEU A CD1   1 
ATOM   2162  C  CD2   . LEU A  1  305  ? -51.426 63.461  74.737  1.00 24.52 ? 303  LEU A CD2   1 
ATOM   2163  N  N     . ASN A  1  306  ? -50.466 59.773  74.402  1.00 17.69 ? 304  ASN A N     1 
ATOM   2164  C  CA    . ASN A  1  306  ? -50.066 59.150  75.654  1.00 18.61 ? 304  ASN A CA    1 
ATOM   2165  C  C     . ASN A  1  306  ? -49.140 60.087  76.413  1.00 18.30 ? 304  ASN A C     1 
ATOM   2166  O  O     . ASN A  1  306  ? -48.203 60.634  75.828  1.00 18.50 ? 304  ASN A O     1 
ATOM   2167  C  CB    . ASN A  1  306  ? -49.340 57.837  75.396  1.00 16.62 ? 304  ASN A CB    1 
ATOM   2168  C  CG    . ASN A  1  306  ? -48.709 57.287  76.644  1.00 18.01 ? 304  ASN A CG    1 
ATOM   2169  O  OD1   . ASN A  1  306  ? -47.511 57.484  76.903  1.00 23.48 ? 304  ASN A OD1   1 
ATOM   2170  N  ND2   . ASN A  1  306  ? -49.506 56.618  77.447  1.00 17.62 ? 304  ASN A ND2   1 
ATOM   2171  N  N     . ILE A  1  307  ? -49.388 60.251  77.707  1.00 16.06 ? 305  ILE A N     1 
ATOM   2172  C  CA    . ILE A  1  307  ? -48.490 60.996  78.585  1.00 15.73 ? 305  ILE A CA    1 
ATOM   2173  C  C     . ILE A  1  307  ? -47.516 60.021  79.234  1.00 15.99 ? 305  ILE A C     1 
ATOM   2174  O  O     . ILE A  1  307  ? -47.904 59.219  80.096  1.00 16.74 ? 305  ILE A O     1 
ATOM   2175  C  CB    . ILE A  1  307  ? -49.264 61.785  79.644  1.00 17.53 ? 305  ILE A CB    1 
ATOM   2176  C  CG1   . ILE A  1  307  ? -50.204 62.785  78.955  1.00 20.10 ? 305  ILE A CG1   1 
ATOM   2177  C  CG2   . ILE A  1  307  ? -48.277 62.493  80.596  1.00 19.45 ? 305  ILE A CG2   1 
ATOM   2178  C  CD1   . ILE A  1  307  ? -51.167 63.449  79.909  1.00 23.22 ? 305  ILE A CD1   1 
ATOM   2179  N  N     . ASP A  1  308  ? -46.245 60.112  78.837  1.00 15.95 ? 306  ASP A N     1 
ATOM   2180  C  CA    . ASP A  1  308  ? -45.205 59.260  79.393  1.00 15.57 ? 306  ASP A CA    1 
ATOM   2181  C  C     . ASP A  1  308  ? -44.979 59.585  80.868  1.00 17.40 ? 306  ASP A C     1 
ATOM   2182  O  O     . ASP A  1  308  ? -45.192 60.713  81.317  1.00 17.68 ? 306  ASP A O     1 
ATOM   2183  C  CB    . ASP A  1  308  ? -43.894 59.457  78.632  1.00 19.38 ? 306  ASP A CB    1 
ATOM   2184  C  CG    . ASP A  1  308  ? -43.872 58.766  77.288  1.00 21.75 ? 306  ASP A CG    1 
ATOM   2185  O  OD1   . ASP A  1  308  ? -44.822 58.038  76.942  1.00 21.22 ? 306  ASP A OD1   1 
ATOM   2186  O  OD2   . ASP A  1  308  ? -42.877 58.943  76.560  1.00 25.45 ? 306  ASP A OD2   1 
ATOM   2187  N  N     . ALA A  1  309  ? -44.564 58.576  81.634  1.00 16.63 ? 307  ALA A N     1 
ATOM   2188  C  CA    . ALA A  1  309  ? -44.276 58.773  83.048  1.00 16.93 ? 307  ALA A CA    1 
ATOM   2189  C  C     . ALA A  1  309  ? -42.791 59.028  83.253  1.00 17.46 ? 307  ALA A C     1 
ATOM   2190  O  O     . ALA A  1  309  ? -41.947 58.378  82.630  1.00 18.01 ? 307  ALA A O     1 
ATOM   2191  C  CB    . ALA A  1  309  ? -44.699 57.566  83.872  1.00 15.92 ? 307  ALA A CB    1 
ATOM   2192  N  N     . GLU A  1  310  ? -42.482 59.956  84.158  1.00 16.90 ? 308  GLU A N     1 
ATOM   2193  C  CA    . GLU A  1  310  ? -41.088 60.341  84.350  1.00 17.56 ? 308  GLU A CA    1 
ATOM   2194  C  C     . GLU A  1  310  ? -40.683 60.123  85.801  1.00 17.00 ? 308  GLU A C     1 
ATOM   2195  O  O     . GLU A  1  310  ? -40.965 59.057  86.362  1.00 17.43 ? 308  GLU A O     1 
ATOM   2196  C  CB    . GLU A  1  310  ? -40.897 61.789  83.884  1.00 18.23 ? 308  GLU A CB    1 
ATOM   2197  C  CG    . GLU A  1  310  ? -41.306 61.954  82.416  1.00 19.08 ? 308  GLU A CG    1 
ATOM   2198  C  CD    . GLU A  1  310  ? -41.016 63.337  81.857  1.00 19.68 ? 308  GLU A CD    1 
ATOM   2199  O  OE1   . GLU A  1  310  ? -39.821 63.646  81.639  1.00 21.87 ? 308  GLU A OE1   1 
ATOM   2200  O  OE2   . GLU A  1  310  ? -41.982 64.099  81.637  1.00 19.59 ? 308  GLU A OE2   1 
ATOM   2201  N  N     . GLU A  1  311  ? -40.020 61.094  86.418  1.00 17.41 ? 309  GLU A N     1 
ATOM   2202  C  CA    . GLU A  1  311  ? -39.500 60.870  87.761  1.00 17.86 ? 309  GLU A CA    1 
ATOM   2203  C  C     . GLU A  1  311  ? -40.624 60.777  88.790  1.00 15.42 ? 309  GLU A C     1 
ATOM   2204  O  O     . GLU A  1  311  ? -41.721 61.305  88.613  1.00 17.53 ? 309  GLU A O     1 
ATOM   2205  C  CB    . GLU A  1  311  ? -38.545 61.992  88.160  1.00 18.23 ? 309  GLU A CB    1 
ATOM   2206  C  CG    . GLU A  1  311  ? -37.284 62.071  87.291  1.00 19.52 ? 309  GLU A CG    1 
ATOM   2207  C  CD    . GLU A  1  311  ? -37.445 62.970  86.069  1.00 23.24 ? 309  GLU A CD    1 
ATOM   2208  O  OE1   . GLU A  1  311  ? -38.589 63.299  85.687  1.00 19.46 ? 309  GLU A OE1   1 
ATOM   2209  O  OE2   . GLU A  1  311  ? -36.410 63.355  85.481  1.00 29.87 ? 309  GLU A OE2   1 
ATOM   2210  N  N     . ALA A  1  312  ? -40.322 60.107  89.902  1.00 16.09 ? 310  ALA A N     1 
ATOM   2211  C  CA    . ALA A  1  312  ? -41.351 59.861  90.905  1.00 15.97 ? 310  ALA A CA    1 
ATOM   2212  C  C     . ALA A  1  312  ? -41.919 61.156  91.467  1.00 15.57 ? 310  ALA A C     1 
ATOM   2213  O  O     . ALA A  1  312  ? -43.093 61.192  91.845  1.00 17.55 ? 310  ALA A O     1 
ATOM   2214  C  CB    . ALA A  1  312  ? -40.784 58.992  92.037  1.00 17.11 ? 310  ALA A CB    1 
ATOM   2215  N  N     . ASP A  1  313  ? -41.119 62.228  91.520  1.00 18.55 ? 311  ASP A N     1 
ATOM   2216  C  CA    . ASP A  1  313  ? -41.651 63.459  92.091  1.00 18.68 ? 311  ASP A CA    1 
ATOM   2217  C  C     . ASP A  1  313  ? -42.512 64.231  91.107  1.00 17.26 ? 311  ASP A C     1 
ATOM   2218  O  O     . ASP A  1  313  ? -42.989 65.316  91.456  1.00 17.61 ? 311  ASP A O     1 
ATOM   2219  C  CB    . ASP A  1  313  ? -40.535 64.360  92.662  1.00 16.63 ? 311  ASP A CB    1 
ATOM   2220  C  CG    . ASP A  1  313  ? -39.562 64.882  91.610  1.00 21.50 ? 311  ASP A CG    1 
ATOM   2221  O  OD1   . ASP A  1  313  ? -39.743 64.613  90.409  1.00 20.46 ? 311  ASP A OD1   1 
ATOM   2222  O  OD2   . ASP A  1  313  ? -38.583 65.562  91.998  1.00 26.03 ? 311  ASP A OD2   1 
ATOM   2223  N  N     . ARG A  1  314  ? -42.748 63.683  89.916  1.00 17.25 ? 312  ARG A N     1 
ATOM   2224  C  CA    . ARG A  1  314  ? -43.673 64.280  88.962  1.00 16.66 ? 312  ARG A CA    1 
ATOM   2225  C  C     . ARG A  1  314  ? -44.957 63.489  88.809  1.00 15.93 ? 312  ARG A C     1 
ATOM   2226  O  O     . ARG A  1  314  ? -45.884 63.967  88.150  1.00 16.83 ? 312  ARG A O     1 
ATOM   2227  C  CB    . ARG A  1  314  ? -42.989 64.434  87.593  1.00 16.07 ? 312  ARG A CB    1 
ATOM   2228  C  CG    . ARG A  1  314  ? -42.004 65.593  87.613  1.00 18.05 ? 312  ARG A CG    1 
ATOM   2229  C  CD    . ARG A  1  314  ? -40.962 65.458  86.550  1.00 19.82 ? 312  ARG A CD    1 
ATOM   2230  N  NE    . ARG A  1  314  ? -40.389 66.765  86.256  1.00 20.94 ? 312  ARG A NE    1 
ATOM   2231  C  CZ    . ARG A  1  314  ? -39.407 66.966  85.388  1.00 19.34 ? 312  ARG A CZ    1 
ATOM   2232  N  NH1   . ARG A  1  314  ? -38.824 65.957  84.760  1.00 19.16 ? 312  ARG A NH1   1 
ATOM   2233  N  NH2   . ARG A  1  314  ? -39.001 68.210  85.146  1.00 21.43 ? 312  ARG A NH2   1 
ATOM   2234  N  N     . LEU A  1  315  ? -45.056 62.317  89.434  1.00 15.71 ? 313  LEU A N     1 
ATOM   2235  C  CA    . LEU A  1  315  ? -46.229 61.470  89.254  1.00 16.64 ? 313  LEU A CA    1 
ATOM   2236  C  C     . LEU A  1  315  ? -47.503 62.192  89.673  1.00 17.45 ? 313  LEU A C     1 
ATOM   2237  O  O     . LEU A  1  315  ? -48.442 62.337  88.880  1.00 16.98 ? 313  LEU A O     1 
ATOM   2238  C  CB    . LEU A  1  315  ? -46.051 60.175  90.048  1.00 16.70 ? 313  LEU A CB    1 
ATOM   2239  C  CG    . LEU A  1  315  ? -46.884 58.961  89.606  1.00 16.55 ? 313  LEU A CG    1 
ATOM   2240  C  CD1   . LEU A  1  315  ? -46.495 57.760  90.448  1.00 18.61 ? 313  LEU A CD1   1 
ATOM   2241  C  CD2   . LEU A  1  315  ? -48.394 59.170  89.682  1.00 19.39 ? 313  LEU A CD2   1 
ATOM   2242  N  N     . GLU A  1  316  ? -47.578 62.619  90.934  1.00 18.30 ? 314  GLU A N     1 
ATOM   2243  C  CA    . GLU A  1  316  ? -48.850 63.155  91.399  1.00 17.26 ? 314  GLU A CA    1 
ATOM   2244  C  C     . GLU A  1  316  ? -49.182 64.475  90.715  1.00 17.96 ? 314  GLU A C     1 
ATOM   2245  O  O     . GLU A  1  316  ? -50.352 64.739  90.411  1.00 18.65 ? 314  GLU A O     1 
ATOM   2246  C  CB    . GLU A  1  316  ? -48.836 63.273  92.922  1.00 18.99 ? 314  GLU A CB    1 
ATOM   2247  C  CG    . GLU A  1  316  ? -48.819 61.891  93.531  1.00 19.72 ? 314  GLU A CG    1 
ATOM   2248  C  CD    . GLU A  1  316  ? -48.844 61.888  95.027  1.00 16.74 ? 314  GLU A CD    1 
ATOM   2249  O  OE1   . GLU A  1  316  ? -49.593 62.687  95.606  1.00 21.65 ? 314  GLU A OE1   1 
ATOM   2250  O  OE2   . GLU A  1  316  ? -48.105 61.077  95.623  1.00 20.18 ? 314  GLU A OE2   1 
ATOM   2251  N  N     . LEU A  1  317  ? -48.170 65.293  90.419  1.00 17.97 ? 315  LEU A N     1 
ATOM   2252  C  CA    . LEU A  1  317  ? -48.425 66.510  89.654  1.00 19.04 ? 315  LEU A CA    1 
ATOM   2253  C  C     . LEU A  1  317  ? -49.063 66.188  88.304  1.00 17.95 ? 315  LEU A C     1 
ATOM   2254  O  O     . LEU A  1  317  ? -50.011 66.864  87.877  1.00 17.47 ? 315  LEU A O     1 
ATOM   2255  C  CB    . LEU A  1  317  ? -47.123 67.280  89.465  1.00 19.63 ? 315  LEU A CB    1 
ATOM   2256  C  CG    . LEU A  1  317  ? -47.227 68.541  88.611  1.00 20.21 ? 315  LEU A CG    1 
ATOM   2257  C  CD1   . LEU A  1  317  ? -48.185 69.560  89.233  1.00 22.28 ? 315  LEU A CD1   1 
ATOM   2258  C  CD2   . LEU A  1  317  ? -45.835 69.121  88.441  1.00 25.12 ? 315  LEU A CD2   1 
ATOM   2259  N  N     . SER A  1  318  ? -48.560 65.156  87.613  1.00 17.37 ? 316  SER A N     1 
ATOM   2260  C  CA    . SER A  1  318  ? -49.116 64.810  86.308  1.00 16.75 ? 316  SER A CA    1 
ATOM   2261  C  C     . SER A  1  318  ? -50.566 64.374  86.429  1.00 18.22 ? 316  SER A C     1 
ATOM   2262  O  O     . SER A  1  318  ? -51.338 64.549  85.480  1.00 17.91 ? 316  SER A O     1 
ATOM   2263  C  CB    . SER A  1  318  ? -48.291 63.706  85.633  1.00 16.21 ? 316  SER A CB    1 
ATOM   2264  O  OG    . SER A  1  318  ? -48.489 62.441  86.250  1.00 16.26 ? 316  SER A OG    1 
ATOM   2265  N  N     . LEU A  1  319  ? -50.960 63.824  87.585  1.00 17.14 ? 317  LEU A N     1 
ATOM   2266  C  CA    . LEU A  1  319  ? -52.358 63.448  87.774  1.00 19.38 ? 317  LEU A CA    1 
ATOM   2267  C  C     . LEU A  1  319  ? -53.265 64.663  87.767  1.00 18.02 ? 317  LEU A C     1 
ATOM   2268  O  O     . LEU A  1  319  ? -54.407 64.569  87.314  1.00 17.81 ? 317  LEU A O     1 
ATOM   2269  C  CB    . LEU A  1  319  ? -52.545 62.673  89.080  1.00 17.83 ? 317  LEU A CB    1 
ATOM   2270  C  CG    . LEU A  1  319  ? -51.849 61.312  89.158  1.00 19.54 ? 317  LEU A CG    1 
ATOM   2271  C  CD1   . LEU A  1  319  ? -52.074 60.674  90.538  1.00 19.87 ? 317  LEU A CD1   1 
ATOM   2272  C  CD2   . LEU A  1  319  ? -52.341 60.393  88.072  1.00 19.98 ? 317  LEU A CD2   1 
ATOM   2273  N  N     . ASP A  1  320  ? -52.781 65.812  88.246  1.00 17.96 ? 318  ASP A N     1 
ATOM   2274  C  CA    . ASP A  1  320  ? -53.608 67.013  88.190  1.00 17.98 ? 318  ASP A CA    1 
ATOM   2275  C  C     . ASP A  1  320  ? -53.863 67.437  86.754  1.00 19.05 ? 318  ASP A C     1 
ATOM   2276  O  O     . ASP A  1  320  ? -54.955 67.921  86.432  1.00 21.54 ? 318  ASP A O     1 
ATOM   2277  C  CB    . ASP A  1  320  ? -52.968 68.137  88.996  1.00 18.76 ? 318  ASP A CB    1 
ATOM   2278  C  CG    . ASP A  1  320  ? -53.151 67.929  90.485  1.00 25.48 ? 318  ASP A CG    1 
ATOM   2279  O  OD1   . ASP A  1  320  ? -54.319 67.780  90.907  1.00 25.94 ? 318  ASP A OD1   1 
ATOM   2280  O  OD2   . ASP A  1  320  ? -52.134 67.868  91.213  1.00 25.93 ? 318  ASP A OD2   1 
ATOM   2281  N  N     . LEU A  1  321  ? -52.875 67.264  85.871  1.00 18.00 ? 319  LEU A N     1 
ATOM   2282  C  CA    A LEU A  1  321  ? -53.095 67.559  84.460  0.45 19.66 ? 319  LEU A CA    1 
ATOM   2283  C  CA    B LEU A  1  321  ? -53.104 67.563  84.461  0.55 19.67 ? 319  LEU A CA    1 
ATOM   2284  C  C     . LEU A  1  321  ? -54.033 66.537  83.833  1.00 19.75 ? 319  LEU A C     1 
ATOM   2285  O  O     . LEU A  1  321  ? -54.937 66.899  83.073  1.00 19.91 ? 319  LEU A O     1 
ATOM   2286  C  CB    A LEU A  1  321  ? -51.758 67.595  83.727  0.45 20.09 ? 319  LEU A CB    1 
ATOM   2287  C  CB    B LEU A  1  321  ? -51.782 67.618  83.703  0.55 20.10 ? 319  LEU A CB    1 
ATOM   2288  C  CG    A LEU A  1  321  ? -50.816 68.665  84.285  0.45 20.52 ? 319  LEU A CG    1 
ATOM   2289  C  CG    B LEU A  1  321  ? -50.966 68.892  83.921  0.55 20.51 ? 319  LEU A CG    1 
ATOM   2290  C  CD1   A LEU A  1  321  ? -49.381 68.395  83.884  0.45 18.70 ? 319  LEU A CD1   1 
ATOM   2291  C  CD1   B LEU A  1  321  ? -49.993 68.721  85.068  0.55 18.51 ? 319  LEU A CD1   1 
ATOM   2292  C  CD2   A LEU A  1  321  ? -51.255 70.031  83.808  0.45 23.74 ? 319  LEU A CD2   1 
ATOM   2293  C  CD2   B LEU A  1  321  ? -50.237 69.260  82.656  0.55 18.89 ? 319  LEU A CD2   1 
ATOM   2294  N  N     . LEU A  1  322  ? -53.834 65.256  84.149  1.00 18.32 ? 320  LEU A N     1 
ATOM   2295  C  CA    . LEU A  1  322  ? -54.722 64.221  83.624  1.00 17.29 ? 320  LEU A CA    1 
ATOM   2296  C  C     . LEU A  1  322  ? -56.165 64.486  84.029  1.00 18.84 ? 320  LEU A C     1 
ATOM   2297  O  O     . LEU A  1  322  ? -57.081 64.363  83.209  1.00 18.38 ? 320  LEU A O     1 
ATOM   2298  C  CB    . LEU A  1  322  ? -54.274 62.850  84.128  1.00 15.72 ? 320  LEU A CB    1 
ATOM   2299  C  CG    . LEU A  1  322  ? -55.127 61.697  83.577  1.00 18.05 ? 320  LEU A CG    1 
ATOM   2300  C  CD1   . LEU A  1  322  ? -54.924 61.537  82.077  1.00 17.02 ? 320  LEU A CD1   1 
ATOM   2301  C  CD2   . LEU A  1  322  ? -54.787 60.397  84.301  1.00 18.82 ? 320  LEU A CD2   1 
ATOM   2302  N  N     . GLU A  1  323  ? -56.377 64.894  85.278  1.00 18.38 ? 321  GLU A N     1 
ATOM   2303  C  CA    . GLU A  1  323  ? -57.729 65.142  85.771  1.00 19.66 ? 321  GLU A CA    1 
ATOM   2304  C  C     . GLU A  1  323  ? -58.388 66.282  85.005  1.00 18.81 ? 321  GLU A C     1 
ATOM   2305  O  O     . GLU A  1  323  ? -59.511 66.142  84.509  1.00 20.06 ? 321  GLU A O     1 
ATOM   2306  C  CB    . GLU A  1  323  ? -57.689 65.453  87.267  1.00 20.64 ? 321  GLU A CB    1 
ATOM   2307  C  CG    . GLU A  1  323  ? -58.984 66.045  87.816  1.00 30.10 ? 321  GLU A CG    1 
ATOM   2308  C  CD    . GLU A  1  323  ? -59.706 65.115  88.762  1.00 30.89 ? 321  GLU A CD    1 
ATOM   2309  O  OE1   . GLU A  1  323  ? -59.112 64.113  89.184  1.00 33.93 ? 321  GLU A OE1   1 
ATOM   2310  O  OE2   . GLU A  1  323  ? -60.882 65.385  89.086  1.00 32.44 ? 321  GLU A OE2   1 
ATOM   2311  N  N     . VAL A  1  324  ? -57.695 67.423  84.885  1.00 18.53 ? 322  VAL A N     1 
ATOM   2312  C  CA    . VAL A  1  324  ? -58.296 68.559  84.193  1.00 19.04 ? 322  VAL A CA    1 
ATOM   2313  C  C     . VAL A  1  324  ? -58.602 68.200  82.747  1.00 18.96 ? 322  VAL A C     1 
ATOM   2314  O  O     . VAL A  1  324  ? -59.681 68.513  82.227  1.00 20.29 ? 322  VAL A O     1 
ATOM   2315  C  CB    . VAL A  1  324  ? -57.392 69.799  84.280  1.00 22.57 ? 322  VAL A CB    1 
ATOM   2316  C  CG1   . VAL A  1  324  ? -58.033 70.927  83.488  1.00 24.74 ? 322  VAL A CG1   1 
ATOM   2317  C  CG2   . VAL A  1  324  ? -57.233 70.229  85.713  1.00 24.67 ? 322  VAL A CG2   1 
ATOM   2318  N  N     . LEU A  1  325  ? -57.666 67.526  82.079  1.00 17.69 ? 323  LEU A N     1 
ATOM   2319  C  CA    . LEU A  1  325  ? -57.872 67.179  80.677  1.00 16.56 ? 323  LEU A CA    1 
ATOM   2320  C  C     . LEU A  1  325  ? -59.055 66.243  80.509  1.00 18.19 ? 323  LEU A C     1 
ATOM   2321  O  O     . LEU A  1  325  ? -59.870 66.423  79.597  1.00 17.48 ? 323  LEU A O     1 
ATOM   2322  C  CB    . LEU A  1  325  ? -56.615 66.533  80.100  1.00 16.59 ? 323  LEU A CB    1 
ATOM   2323  C  CG    . LEU A  1  325  ? -55.414 67.477  80.000  1.00 21.20 ? 323  LEU A CG    1 
ATOM   2324  C  CD1   . LEU A  1  325  ? -54.145 66.656  79.796  1.00 19.50 ? 323  LEU A CD1   1 
ATOM   2325  C  CD2   . LEU A  1  325  ? -55.617 68.443  78.860  1.00 21.13 ? 323  LEU A CD2   1 
ATOM   2326  N  N     . CYS A  1  326  ? -59.178 65.246  81.385  1.00 17.31 ? 324  CYS A N     1 
ATOM   2327  C  CA    . CYS A  1  326  ? -60.266 64.289  81.220  1.00 15.05 ? 324  CYS A CA    1 
ATOM   2328  C  C     . CYS A  1  326  ? -61.620 64.882  81.572  1.00 18.58 ? 324  CYS A C     1 
ATOM   2329  O  O     . CYS A  1  326  ? -62.633 64.379  81.079  1.00 19.15 ? 324  CYS A O     1 
ATOM   2330  C  CB    . CYS A  1  326  ? -60.027 63.044  82.066  1.00 17.71 ? 324  CYS A CB    1 
ATOM   2331  S  SG    . CYS A  1  326  ? -58.671 62.043  81.412  1.00 21.83 ? 324  CYS A SG    1 
ATOM   2332  N  N     . LEU A  1  327  ? -61.655 65.937  82.382  1.00 18.38 ? 325  LEU A N     1 
ATOM   2333  C  CA    . LEU A  1  327  ? -62.898 66.620  82.717  1.00 19.70 ? 325  LEU A CA    1 
ATOM   2334  C  C     . LEU A  1  327  ? -63.204 67.769  81.770  1.00 18.76 ? 325  LEU A C     1 
ATOM   2335  O  O     . LEU A  1  327  ? -64.268 68.378  81.879  1.00 19.72 ? 325  LEU A O     1 
ATOM   2336  C  CB    . LEU A  1  327  ? -62.840 67.129  84.161  1.00 21.62 ? 325  LEU A CB    1 
ATOM   2337  C  CG    . LEU A  1  327  ? -62.713 66.016  85.209  1.00 24.67 ? 325  LEU A CG    1 
ATOM   2338  C  CD1   . LEU A  1  327  ? -62.625 66.614  86.608  1.00 29.49 ? 325  LEU A CD1   1 
ATOM   2339  C  CD2   . LEU A  1  327  ? -63.857 65.027  85.109  1.00 26.29 ? 325  LEU A CD2   1 
ATOM   2340  N  N     . ASP A  1  328  ? -62.328 68.050  80.815  1.00 18.60 ? 326  ASP A N     1 
ATOM   2341  C  CA    . ASP A  1  328  ? -62.493 69.208  79.941  1.00 18.00 ? 326  ASP A CA    1 
ATOM   2342  C  C     . ASP A  1  328  ? -63.433 68.845  78.802  1.00 17.13 ? 326  ASP A C     1 
ATOM   2343  O  O     . ASP A  1  328  ? -63.089 68.026  77.944  1.00 19.05 ? 326  ASP A O     1 
ATOM   2344  C  CB    . ASP A  1  328  ? -61.134 69.653  79.414  1.00 18.55 ? 326  ASP A CB    1 
ATOM   2345  C  CG    . ASP A  1  328  ? -61.197 70.970  78.669  1.00 22.49 ? 326  ASP A CG    1 
ATOM   2346  O  OD1   . ASP A  1  328  ? -62.178 71.213  77.936  1.00 23.12 ? 326  ASP A OD1   1 
ATOM   2347  O  OD2   . ASP A  1  328  ? -60.262 71.774  78.840  1.00 24.00 ? 326  ASP A OD2   1 
ATOM   2348  N  N     . GLY A  1  329  ? -64.611 69.463  78.784  1.00 18.89 ? 327  GLY A N     1 
ATOM   2349  C  CA    . GLY A  1  329  ? -65.600 69.133  77.769  1.00 19.78 ? 327  GLY A CA    1 
ATOM   2350  C  C     . GLY A  1  329  ? -65.121 69.331  76.343  1.00 20.18 ? 327  GLY A C     1 
ATOM   2351  O  O     . GLY A  1  329  ? -65.620 68.678  75.426  1.00 20.48 ? 327  GLY A O     1 
ATOM   2352  N  N     . ASP A  1  330  ? -64.144 70.216  76.126  1.00 18.69 ? 328  ASP A N     1 
ATOM   2353  C  CA    . ASP A  1  330  ? -63.663 70.421  74.764  1.00 20.08 ? 328  ASP A CA    1 
ATOM   2354  C  C     . ASP A  1  330  ? -63.021 69.173  74.192  1.00 17.93 ? 328  ASP A C     1 
ATOM   2355  O  O     . ASP A  1  330  ? -62.894 69.068  72.970  1.00 20.16 ? 328  ASP A O     1 
ATOM   2356  C  CB    . ASP A  1  330  ? -62.642 71.551  74.689  1.00 18.99 ? 328  ASP A CB    1 
ATOM   2357  C  CG    . ASP A  1  330  ? -63.249 72.900  74.949  1.00 26.24 ? 328  ASP A CG    1 
ATOM   2358  O  OD1   . ASP A  1  330  ? -64.477 73.047  74.762  1.00 27.31 ? 328  ASP A OD1   1 
ATOM   2359  O  OD2   . ASP A  1  330  ? -62.490 73.809  75.334  1.00 24.39 ? 328  ASP A OD2   1 
ATOM   2360  N  N     . LEU A  1  331  ? -62.597 68.239  75.046  1.00 16.39 ? 329  LEU A N     1 
ATOM   2361  C  CA    . LEU A  1  331  ? -61.964 67.010  74.593  1.00 18.45 ? 329  LEU A CA    1 
ATOM   2362  C  C     . LEU A  1  331  ? -62.934 65.843  74.576  1.00 18.74 ? 329  LEU A C     1 
ATOM   2363  O  O     . LEU A  1  331  ? -62.517 64.711  74.303  1.00 19.41 ? 329  LEU A O     1 
ATOM   2364  C  CB    . LEU A  1  331  ? -60.752 66.663  75.470  1.00 18.46 ? 329  LEU A CB    1 
ATOM   2365  C  CG    . LEU A  1  331  ? -59.551 67.595  75.281  1.00 18.82 ? 329  LEU A CG    1 
ATOM   2366  C  CD1   . LEU A  1  331  ? -58.489 67.384  76.349  1.00 19.18 ? 329  LEU A CD1   1 
ATOM   2367  C  CD2   . LEU A  1  331  ? -58.930 67.391  73.914  1.00 19.74 ? 329  LEU A CD2   1 
ATOM   2368  N  N     . SER A  1  332  ? -64.214 66.090  74.853  1.00 18.57 ? 330  SER A N     1 
ATOM   2369  C  CA    . SER A  1  332  ? -65.167 64.996  74.923  1.00 21.32 ? 330  SER A CA    1 
ATOM   2370  C  C     . SER A  1  332  ? -65.350 64.355  73.549  1.00 21.45 ? 330  SER A C     1 
ATOM   2371  O  O     . SER A  1  332  ? -65.142 64.978  72.502  1.00 21.87 ? 330  SER A O     1 
ATOM   2372  C  CB    . SER A  1  332  ? -66.509 65.485  75.471  1.00 22.73 ? 330  SER A CB    1 
ATOM   2373  O  OG    . SER A  1  332  ? -67.116 66.393  74.589  1.00 24.98 ? 330  SER A OG    1 
ATOM   2374  N  N     . GLY A  1  333  ? -65.726 63.083  73.563  1.00 18.77 ? 331  GLY A N     1 
ATOM   2375  C  CA    . GLY A  1  333  ? -65.926 62.336  72.344  1.00 19.25 ? 331  GLY A CA    1 
ATOM   2376  C  C     . GLY A  1  333  ? -64.712 61.570  71.887  1.00 19.34 ? 331  GLY A C     1 
ATOM   2377  O  O     . GLY A  1  333  ? -64.811 60.777  70.941  1.00 25.60 ? 331  GLY A O     1 
ATOM   2378  N  N     . TRP A  1  334  ? -63.577 61.766  72.542  1.00 18.56 ? 332  TRP A N     1 
ATOM   2379  C  CA    . TRP A  1  334  ? -62.316 61.163  72.151  1.00 19.67 ? 332  TRP A CA    1 
ATOM   2380  C  C     . TRP A  1  334  ? -61.788 60.352  73.317  1.00 17.93 ? 332  TRP A C     1 
ATOM   2381  O  O     . TRP A  1  334  ? -61.709 60.860  74.440  1.00 18.95 ? 332  TRP A O     1 
ATOM   2382  C  CB    . TRP A  1  334  ? -61.333 62.262  71.755  1.00 19.23 ? 332  TRP A CB    1 
ATOM   2383  C  CG    . TRP A  1  334  ? -59.895 61.892  71.601  1.00 16.05 ? 332  TRP A CG    1 
ATOM   2384  C  CD1   . TRP A  1  334  ? -59.338 61.127  70.619  1.00 17.25 ? 332  TRP A CD1   1 
ATOM   2385  C  CD2   . TRP A  1  334  ? -58.818 62.367  72.404  1.00 16.04 ? 332  TRP A CD2   1 
ATOM   2386  N  NE1   . TRP A  1  334  ? -57.974 61.080  70.772  1.00 17.40 ? 332  TRP A NE1   1 
ATOM   2387  C  CE2   . TRP A  1  334  ? -57.625 61.835  71.861  1.00 16.22 ? 332  TRP A CE2   1 
ATOM   2388  C  CE3   . TRP A  1  334  ? -58.740 63.181  73.539  1.00 17.20 ? 332  TRP A CE3   1 
ATOM   2389  C  CZ2   . TRP A  1  334  ? -56.367 62.088  72.421  1.00 17.07 ? 332  TRP A CZ2   1 
ATOM   2390  C  CZ3   . TRP A  1  334  ? -57.493 63.439  74.089  1.00 17.54 ? 332  TRP A CZ3   1 
ATOM   2391  C  CH2   . TRP A  1  334  ? -56.322 62.886  73.534  1.00 18.13 ? 332  TRP A CH2   1 
ATOM   2392  N  N     . ASN A  1  335  ? -61.430 59.096  73.046  1.00 17.58 ? 333  ASN A N     1 
ATOM   2393  C  CA    . ASN A  1  335  ? -60.915 58.177  74.050  1.00 16.18 ? 333  ASN A CA    1 
ATOM   2394  C  C     . ASN A  1  335  ? -59.417 57.942  73.912  1.00 16.83 ? 333  ASN A C     1 
ATOM   2395  O  O     . ASN A  1  335  ? -58.898 56.953  74.444  1.00 18.32 ? 333  ASN A O     1 
ATOM   2396  C  CB    . ASN A  1  335  ? -61.654 56.841  73.958  1.00 19.50 ? 333  ASN A CB    1 
ATOM   2397  C  CG    . ASN A  1  335  ? -63.006 56.873  74.649  1.00 21.57 ? 333  ASN A CG    1 
ATOM   2398  O  OD1   . ASN A  1  335  ? -63.245 57.671  75.556  1.00 20.56 ? 333  ASN A OD1   1 
ATOM   2399  N  ND2   . ASN A  1  335  ? -63.895 55.979  74.232  1.00 25.69 ? 333  ASN A ND2   1 
ATOM   2400  N  N     . GLY A  1  336  ? -58.721 58.818  73.187  1.00 17.41 ? 334  GLY A N     1 
ATOM   2401  C  CA    . GLY A  1  336  ? -57.320 58.617  72.879  1.00 15.08 ? 334  GLY A CA    1 
ATOM   2402  C  C     . GLY A  1  336  ? -56.346 59.082  73.931  1.00 15.77 ? 334  GLY A C     1 
ATOM   2403  O  O     . GLY A  1  336  ? -55.151 58.804  73.792  1.00 16.90 ? 334  GLY A O     1 
ATOM   2404  N  N     . MET A  1  337  ? -56.799 59.778  74.974  1.00 17.48 ? 335  MET A N     1 
ATOM   2405  C  CA    A MET A  1  337  ? -55.877 60.208  76.018  0.54 17.61 ? 335  MET A CA    1 
ATOM   2406  C  CA    B MET A  1  337  ? -55.874 60.207  76.015  0.46 17.62 ? 335  MET A CA    1 
ATOM   2407  C  C     . MET A  1  337  ? -55.318 59.000  76.755  1.00 15.79 ? 335  MET A C     1 
ATOM   2408  O  O     . MET A  1  337  ? -56.075 58.130  77.221  1.00 18.86 ? 335  MET A O     1 
ATOM   2409  C  CB    A MET A  1  337  ? -56.567 61.155  76.995  0.54 18.93 ? 335  MET A CB    1 
ATOM   2410  C  CB    B MET A  1  337  ? -56.557 61.159  76.989  0.46 18.92 ? 335  MET A CB    1 
ATOM   2411  C  CG    A MET A  1  337  ? -55.624 61.726  78.028  0.54 20.87 ? 335  MET A CG    1 
ATOM   2412  C  CG    B MET A  1  337  ? -55.695 61.496  78.184  0.46 21.48 ? 335  MET A CG    1 
ATOM   2413  S  SD    A MET A  1  337  ? -54.504 62.920  77.299  0.54 27.15 ? 335  MET A SD    1 
ATOM   2414  S  SD    B MET A  1  337  ? -55.727 63.254  78.507  0.46 21.34 ? 335  MET A SD    1 
ATOM   2415  C  CE    A MET A  1  337  ? -55.629 64.280  76.990  0.54 23.74 ? 335  MET A CE    1 
ATOM   2416  C  CE    B MET A  1  337  ? -55.082 63.828  76.935  0.46 19.87 ? 335  MET A CE    1 
ATOM   2417  N  N     . GLY A  1  338  ? -53.989 58.940  76.849  1.00 15.95 ? 336  GLY A N     1 
ATOM   2418  C  CA    . GLY A  1  338  ? -53.321 57.818  77.468  1.00 16.96 ? 336  GLY A CA    1 
ATOM   2419  C  C     . GLY A  1  338  ? -52.385 58.300  78.561  1.00 17.21 ? 336  GLY A C     1 
ATOM   2420  O  O     . GLY A  1  338  ? -51.972 59.457  78.594  1.00 17.37 ? 336  GLY A O     1 
ATOM   2421  N  N     . PHE A  1  339  ? -52.062 57.383  79.473  1.00 15.54 ? 337  PHE A N     1 
ATOM   2422  C  CA    . PHE A  1  339  ? -51.276 57.752  80.643  1.00 16.80 ? 337  PHE A CA    1 
ATOM   2423  C  C     . PHE A  1  339  ? -50.492 56.536  81.120  1.00 17.01 ? 337  PHE A C     1 
ATOM   2424  O  O     . PHE A  1  339  ? -51.051 55.448  81.278  1.00 17.66 ? 337  PHE A O     1 
ATOM   2425  C  CB    . PHE A  1  339  ? -52.219 58.281  81.734  1.00 16.82 ? 337  PHE A CB    1 
ATOM   2426  C  CG    . PHE A  1  339  ? -51.532 58.909  82.912  1.00 18.46 ? 337  PHE A CG    1 
ATOM   2427  C  CD1   . PHE A  1  339  ? -51.212 60.270  82.903  1.00 18.14 ? 337  PHE A CD1   1 
ATOM   2428  C  CD2   . PHE A  1  339  ? -51.259 58.165  84.042  1.00 18.40 ? 337  PHE A CD2   1 
ATOM   2429  C  CE1   . PHE A  1  339  ? -50.601 60.857  84.009  1.00 18.44 ? 337  PHE A CE1   1 
ATOM   2430  C  CE2   . PHE A  1  339  ? -50.651 58.743  85.141  1.00 19.88 ? 337  PHE A CE2   1 
ATOM   2431  C  CZ    . PHE A  1  339  ? -50.317 60.089  85.121  1.00 20.71 ? 337  PHE A CZ    1 
ATOM   2432  N  N     . VAL A  1  340  ? -49.197 56.721  81.346  1.00 17.19 ? 338  VAL A N     1 
ATOM   2433  C  CA    . VAL A  1  340  ? -48.328 55.656  81.821  1.00 16.41 ? 338  VAL A CA    1 
ATOM   2434  C  C     . VAL A  1  340  ? -48.333 55.599  83.340  1.00 17.36 ? 338  VAL A C     1 
ATOM   2435  O  O     . VAL A  1  340  ? -48.289 56.629  84.020  1.00 17.60 ? 338  VAL A O     1 
ATOM   2436  C  CB    . VAL A  1  340  ? -46.898 55.873  81.311  1.00 16.24 ? 338  VAL A CB    1 
ATOM   2437  C  CG1   . VAL A  1  340  ? -45.973 54.777  81.821  1.00 16.62 ? 338  VAL A CG1   1 
ATOM   2438  C  CG2   . VAL A  1  340  ? -46.884 55.963  79.796  1.00 18.41 ? 338  VAL A CG2   1 
ATOM   2439  N  N     . VAL A  1  341  ? -48.343 54.384  83.875  1.00 16.25 ? 339  VAL A N     1 
ATOM   2440  C  CA    A VAL A  1  341  ? -48.114 54.156  85.295  0.55 15.96 ? 339  VAL A CA    1 
ATOM   2441  C  CA    B VAL A  1  341  ? -48.114 54.155  85.296  0.45 15.98 ? 339  VAL A CA    1 
ATOM   2442  C  C     . VAL A  1  341  ? -46.980 53.150  85.438  1.00 16.92 ? 339  VAL A C     1 
ATOM   2443  O  O     . VAL A  1  341  ? -46.917 52.159  84.701  1.00 18.85 ? 339  VAL A O     1 
ATOM   2444  C  CB    A VAL A  1  341  ? -49.375 53.664  86.030  0.55 17.92 ? 339  VAL A CB    1 
ATOM   2445  C  CB    B VAL A  1  341  ? -49.385 53.671  86.026  0.45 17.92 ? 339  VAL A CB    1 
ATOM   2446  C  CG1   A VAL A  1  341  ? -49.194 53.886  87.508  0.55 18.53 ? 339  VAL A CG1   1 
ATOM   2447  C  CG1   B VAL A  1  341  ? -50.436 54.765  86.021  0.45 19.04 ? 339  VAL A CG1   1 
ATOM   2448  C  CG2   A VAL A  1  341  ? -50.622 54.389  85.527  0.55 18.79 ? 339  VAL A CG2   1 
ATOM   2449  C  CG2   B VAL A  1  341  ? -49.925 52.411  85.385  0.45 19.42 ? 339  VAL A CG2   1 
ATOM   2450  N  N     . GLN A  1  342  ? -46.068 53.424  86.370  1.00 17.10 ? 340  GLN A N     1 
ATOM   2451  C  CA    . GLN A  1  342  ? -44.842 52.654  86.530  1.00 17.71 ? 340  GLN A CA    1 
ATOM   2452  C  C     . GLN A  1  342  ? -45.008 51.663  87.674  1.00 17.22 ? 340  GLN A C     1 
ATOM   2453  O  O     . GLN A  1  342  ? -45.114 52.060  88.842  1.00 18.60 ? 340  GLN A O     1 
ATOM   2454  C  CB    . GLN A  1  342  ? -43.663 53.586  86.777  1.00 16.06 ? 340  GLN A CB    1 
ATOM   2455  C  CG    . GLN A  1  342  ? -43.432 54.585  85.647  1.00 17.36 ? 340  GLN A CG    1 
ATOM   2456  C  CD    . GLN A  1  342  ? -42.864 55.876  86.158  1.00 17.15 ? 340  GLN A CD    1 
ATOM   2457  O  OE1   . GLN A  1  342  ? -43.384 56.448  87.108  1.00 17.63 ? 340  GLN A OE1   1 
ATOM   2458  N  NE2   . GLN A  1  342  ? -41.788 56.357  85.525  1.00 17.41 ? 340  GLN A NE2   1 
ATOM   2459  N  N     . ALA A  1  343  ? -44.994 50.372  87.328  1.00 15.36 ? 341  ALA A N     1 
ATOM   2460  C  CA    . ALA A  1  343  ? -45.162 49.311  88.314  1.00 19.00 ? 341  ALA A CA    1 
ATOM   2461  C  C     . ALA A  1  343  ? -43.991 49.209  89.285  1.00 20.46 ? 341  ALA A C     1 
ATOM   2462  O  O     . ALA A  1  343  ? -44.135 48.578  90.342  1.00 18.79 ? 341  ALA A O     1 
ATOM   2463  C  CB    . ALA A  1  343  ? -45.372 47.983  87.596  1.00 20.27 ? 341  ALA A CB    1 
ATOM   2464  N  N     . TYR A  1  344  ? -42.843 49.807  88.981  1.00 17.72 ? 342  TYR A N     1 
ATOM   2465  C  CA    . TYR A  1  344  ? -41.802 49.784  90.002  1.00 17.92 ? 342  TYR A CA    1 
ATOM   2466  C  C     . TYR A  1  344  ? -42.079 50.767  91.123  1.00 17.98 ? 342  TYR A C     1 
ATOM   2467  O  O     . TYR A  1  344  ? -41.339 50.784  92.109  1.00 18.86 ? 342  TYR A O     1 
ATOM   2468  C  CB    . TYR A  1  344  ? -40.403 50.020  89.401  1.00 17.94 ? 342  TYR A CB    1 
ATOM   2469  C  CG    . TYR A  1  344  ? -39.992 51.393  88.890  1.00 16.75 ? 342  TYR A CG    1 
ATOM   2470  C  CD1   . TYR A  1  344  ? -40.850 52.486  88.862  1.00 15.68 ? 342  TYR A CD1   1 
ATOM   2471  C  CD2   . TYR A  1  344  ? -38.687 51.570  88.427  1.00 16.21 ? 342  TYR A CD2   1 
ATOM   2472  C  CE1   . TYR A  1  344  ? -40.411 53.722  88.364  1.00 16.39 ? 342  TYR A CE1   1 
ATOM   2473  C  CE2   . TYR A  1  344  ? -38.250 52.770  87.932  1.00 17.25 ? 342  TYR A CE2   1 
ATOM   2474  C  CZ    . TYR A  1  344  ? -39.100 53.843  87.906  1.00 17.72 ? 342  TYR A CZ    1 
ATOM   2475  O  OH    . TYR A  1  344  ? -38.613 55.027  87.417  1.00 17.95 ? 342  TYR A OH    1 
ATOM   2476  N  N     . GLY A  1  345  ? -43.137 51.564  90.996  1.00 17.52 ? 343  GLY A N     1 
ATOM   2477  C  CA    . GLY A  1  345  ? -43.466 52.553  91.999  1.00 18.55 ? 343  GLY A CA    1 
ATOM   2478  C  C     . GLY A  1  345  ? -44.466 52.014  93.008  1.00 18.36 ? 343  GLY A C     1 
ATOM   2479  O  O     . GLY A  1  345  ? -45.407 51.296  92.660  1.00 19.01 ? 343  GLY A O     1 
ATOM   2480  N  N     . LYS A  1  346  ? -44.242 52.380  94.270  1.00 18.28 ? 344  LYS A N     1 
ATOM   2481  C  CA    . LYS A  1  346  ? -45.084 51.911  95.360  1.00 19.35 ? 344  LYS A CA    1 
ATOM   2482  C  C     . LYS A  1  346  ? -46.506 52.439  95.277  1.00 21.12 ? 344  LYS A C     1 
ATOM   2483  O  O     . LYS A  1  346  ? -47.414 51.843  95.867  1.00 19.63 ? 344  LYS A O     1 
ATOM   2484  C  CB    . LYS A  1  346  ? -44.462 52.316  96.686  1.00 18.65 ? 344  LYS A CB    1 
ATOM   2485  C  CG    . LYS A  1  346  ? -43.105 51.686  96.890  1.00 19.83 ? 344  LYS A CG    1 
ATOM   2486  C  CD    . LYS A  1  346  ? -42.490 52.148  98.176  1.00 21.50 ? 344  LYS A CD    1 
ATOM   2487  C  CE    . LYS A  1  346  ? -41.236 51.353  98.457  1.00 20.11 ? 344  LYS A CE    1 
ATOM   2488  N  NZ    . LYS A  1  346  ? -40.501 51.919  99.626  1.00 21.90 ? 344  LYS A NZ    1 
ATOM   2489  N  N     . ARG A  1  347  ? -46.724 53.539  94.572  1.00 19.29 ? 345  ARG A N     1 
ATOM   2490  C  CA    . ARG A  1  347  ? -48.060 54.110  94.465  1.00 18.53 ? 345  ARG A CA    1 
ATOM   2491  C  C     . ARG A  1  347  ? -48.883 53.512  93.336  1.00 19.29 ? 345  ARG A C     1 
ATOM   2492  O  O     . ARG A  1  347  ? -50.084 53.801  93.253  1.00 19.92 ? 345  ARG A O     1 
ATOM   2493  C  CB    . ARG A  1  347  ? -47.953 55.628  94.283  1.00 18.35 ? 345  ARG A CB    1 
ATOM   2494  C  CG    . ARG A  1  347  ? -47.440 56.303  95.547  1.00 17.98 ? 345  ARG A CG    1 
ATOM   2495  C  CD    . ARG A  1  347  ? -47.034 57.722  95.282  1.00 17.20 ? 345  ARG A CD    1 
ATOM   2496  N  NE    . ARG A  1  347  ? -45.794 57.778  94.513  1.00 18.96 ? 345  ARG A NE    1 
ATOM   2497  C  CZ    . ARG A  1  347  ? -45.332 58.879  93.933  1.00 18.08 ? 345  ARG A CZ    1 
ATOM   2498  N  NH1   . ARG A  1  347  ? -45.962 60.041  94.047  1.00 17.74 ? 345  ARG A NH1   1 
ATOM   2499  N  NH2   . ARG A  1  347  ? -44.220 58.813  93.208  1.00 17.95 ? 345  ARG A NH2   1 
ATOM   2500  N  N     . CYS A  1  348  ? -48.283 52.668  92.493  1.00 19.14 ? 346  CYS A N     1 
ATOM   2501  C  CA    . CYS A  1  348  ? -48.895 52.219  91.243  1.00 19.34 ? 346  CYS A CA    1 
ATOM   2502  C  C     . CYS A  1  348  ? -50.333 51.722  91.389  1.00 19.61 ? 346  CYS A C     1 
ATOM   2503  O  O     . CYS A  1  348  ? -51.207 52.216  90.669  1.00 19.21 ? 346  CYS A O     1 
ATOM   2504  C  CB    . CYS A  1  348  ? -48.043 51.125  90.594  1.00 20.08 ? 346  CYS A CB    1 
ATOM   2505  S  SG    . CYS A  1  348  ? -48.512 50.850  88.862  1.00 23.83 ? 346  CYS A SG    1 
ATOM   2506  N  N     . PRO A  1  349  ? -50.640 50.762  92.268  1.00 19.74 ? 347  PRO A N     1 
ATOM   2507  C  CA    . PRO A  1  349  ? -52.039 50.305  92.340  1.00 20.52 ? 347  PRO A CA    1 
ATOM   2508  C  C     . PRO A  1  349  ? -52.991 51.406  92.761  1.00 18.06 ? 347  PRO A C     1 
ATOM   2509  O  O     . PRO A  1  349  ? -54.133 51.438  92.288  1.00 20.09 ? 347  PRO A O     1 
ATOM   2510  C  CB    . PRO A  1  349  ? -51.996 49.162  93.365  1.00 20.66 ? 347  PRO A CB    1 
ATOM   2511  C  CG    . PRO A  1  349  ? -50.767 49.400  94.158  1.00 21.55 ? 347  PRO A CG    1 
ATOM   2512  C  CD    . PRO A  1  349  ? -49.786 50.085  93.262  1.00 20.97 ? 347  PRO A CD    1 
ATOM   2513  N  N     . PHE A  1  350  ? -52.540 52.324  93.613  1.00 19.70 ? 348  PHE A N     1 
ATOM   2514  C  CA    . PHE A  1  350  ? -53.395 53.422  94.061  1.00 19.69 ? 348  PHE A CA    1 
ATOM   2515  C  C     . PHE A  1  350  ? -53.571 54.467  92.975  1.00 19.18 ? 348  PHE A C     1 
ATOM   2516  O  O     . PHE A  1  350  ? -54.645 55.070  92.856  1.00 19.18 ? 348  PHE A O     1 
ATOM   2517  C  CB    . PHE A  1  350  ? -52.800 54.028  95.332  1.00 20.17 ? 348  PHE A CB    1 
ATOM   2518  C  CG    . PHE A  1  350  ? -52.467 52.994  96.365  1.00 22.41 ? 348  PHE A CG    1 
ATOM   2519  C  CD1   . PHE A  1  350  ? -53.471 52.451  97.146  1.00 26.10 ? 348  PHE A CD1   1 
ATOM   2520  C  CD2   . PHE A  1  350  ? -51.169 52.534  96.522  1.00 21.04 ? 348  PHE A CD2   1 
ATOM   2521  C  CE1   . PHE A  1  350  ? -53.185 51.480  98.082  1.00 27.74 ? 348  PHE A CE1   1 
ATOM   2522  C  CE2   . PHE A  1  350  ? -50.871 51.549  97.462  1.00 24.11 ? 348  PHE A CE2   1 
ATOM   2523  C  CZ    . PHE A  1  350  ? -51.874 51.026  98.237  1.00 29.28 ? 348  PHE A CZ    1 
ATOM   2524  N  N     . VAL A  1  351  ? -52.527 54.687  92.177  1.00 17.73 ? 349  VAL A N     1 
ATOM   2525  C  CA    . VAL A  1  351  ? -52.653 55.532  90.995  1.00 17.38 ? 349  VAL A CA    1 
ATOM   2526  C  C     . VAL A  1  351  ? -53.669 54.934  90.036  1.00 17.21 ? 349  VAL A C     1 
ATOM   2527  O  O     . VAL A  1  351  ? -54.505 55.643  89.467  1.00 19.31 ? 349  VAL A O     1 
ATOM   2528  C  CB    . VAL A  1  351  ? -51.279 55.710  90.334  1.00 18.27 ? 349  VAL A CB    1 
ATOM   2529  C  CG1   . VAL A  1  351  ? -51.426 56.521  89.063  1.00 17.18 ? 349  VAL A CG1   1 
ATOM   2530  C  CG2   . VAL A  1  351  ? -50.327 56.428  91.306  1.00 19.01 ? 349  VAL A CG2   1 
ATOM   2531  N  N     . LEU A  1  352  ? -53.615 53.612  89.845  1.00 20.25 ? 350  LEU A N     1 
ATOM   2532  C  CA    . LEU A  1  352  ? -54.576 52.955  88.970  1.00 17.21 ? 350  LEU A CA    1 
ATOM   2533  C  C     . LEU A  1  352  ? -56.000 53.092  89.500  1.00 19.11 ? 350  LEU A C     1 
ATOM   2534  O  O     . LEU A  1  352  ? -56.927 53.346  88.726  1.00 19.48 ? 350  LEU A O     1 
ATOM   2535  C  CB    . LEU A  1  352  ? -54.195 51.486  88.796  1.00 18.76 ? 350  LEU A CB    1 
ATOM   2536  C  CG    . LEU A  1  352  ? -52.956 51.267  87.928  1.00 18.93 ? 350  LEU A CG    1 
ATOM   2537  C  CD1   . LEU A  1  352  ? -52.577 49.797  87.928  1.00 22.36 ? 350  LEU A CD1   1 
ATOM   2538  C  CD2   . LEU A  1  352  ? -53.185 51.762  86.507  1.00 21.58 ? 350  LEU A CD2   1 
ATOM   2539  N  N     . ASP A  1  353  ? -56.203 52.911  90.813  1.00 22.01 ? 351  ASP A N     1 
ATOM   2540  C  CA    . ASP A  1  353  ? -57.532 53.157  91.370  1.00 23.07 ? 351  ASP A CA    1 
ATOM   2541  C  C     . ASP A  1  353  ? -58.007 54.562  91.044  1.00 19.00 ? 351  ASP A C     1 
ATOM   2542  O  O     . ASP A  1  353  ? -59.177 54.767  90.693  1.00 21.10 ? 351  ASP A O     1 
ATOM   2543  C  CB    . ASP A  1  353  ? -57.538 52.962  92.885  1.00 21.32 ? 351  ASP A CB    1 
ATOM   2544  C  CG    . ASP A  1  353  ? -57.331 51.528  93.298  1.00 23.19 ? 351  ASP A CG    1 
ATOM   2545  O  OD1   . ASP A  1  353  ? -57.585 50.614  92.495  1.00 24.46 ? 351  ASP A OD1   1 
ATOM   2546  O  OD2   . ASP A  1  353  ? -56.927 51.323  94.455  1.00 28.66 ? 351  ASP A OD2   1 
ATOM   2547  N  N     . PHE A  1  354  ? -57.116 55.545  91.171  1.00 18.67 ? 352  PHE A N     1 
ATOM   2548  C  CA    . PHE A  1  354  ? -57.490 56.921  90.862  1.00 19.20 ? 352  PHE A CA    1 
ATOM   2549  C  C     . PHE A  1  354  ? -57.843 57.074  89.387  1.00 19.54 ? 352  PHE A C     1 
ATOM   2550  O  O     . PHE A  1  354  ? -58.846 57.712  89.046  1.00 18.90 ? 352  PHE A O     1 
ATOM   2551  C  CB    . PHE A  1  354  ? -56.359 57.880  91.254  1.00 19.75 ? 352  PHE A CB    1 
ATOM   2552  C  CG    . PHE A  1  354  ? -56.530 59.254  90.691  1.00 18.32 ? 352  PHE A CG    1 
ATOM   2553  C  CD1   . PHE A  1  354  ? -57.316 60.190  91.345  1.00 19.27 ? 352  PHE A CD1   1 
ATOM   2554  C  CD2   . PHE A  1  354  ? -55.916 59.606  89.496  1.00 20.37 ? 352  PHE A CD2   1 
ATOM   2555  C  CE1   . PHE A  1  354  ? -57.495 61.471  90.805  1.00 21.28 ? 352  PHE A CE1   1 
ATOM   2556  C  CE2   . PHE A  1  354  ? -56.090 60.870  88.949  1.00 23.47 ? 352  PHE A CE2   1 
ATOM   2557  C  CZ    . PHE A  1  354  ? -56.874 61.805  89.607  1.00 21.36 ? 352  PHE A CZ    1 
ATOM   2558  N  N     . ILE A  1  355  ? -57.041 56.477  88.499  1.00 18.49 ? 353  ILE A N     1 
ATOM   2559  C  CA    . ILE A  1  355  ? -57.270 56.624  87.062  1.00 17.46 ? 353  ILE A CA    1 
ATOM   2560  C  C     . ILE A  1  355  ? -58.553 55.930  86.641  1.00 20.60 ? 353  ILE A C     1 
ATOM   2561  O  O     . ILE A  1  355  ? -59.320 56.457  85.831  1.00 18.69 ? 353  ILE A O     1 
ATOM   2562  C  CB    . ILE A  1  355  ? -56.070 56.083  86.274  1.00 17.54 ? 353  ILE A CB    1 
ATOM   2563  C  CG1   . ILE A  1  355  ? -54.864 56.996  86.480  1.00 19.31 ? 353  ILE A CG1   1 
ATOM   2564  C  CG2   . ILE A  1  355  ? -56.402 55.966  84.787  1.00 19.49 ? 353  ILE A CG2   1 
ATOM   2565  C  CD1   . ILE A  1  355  ? -53.616 56.406  85.883  1.00 19.71 ? 353  ILE A CD1   1 
ATOM   2566  N  N     . ILE A  1  356  ? -58.783 54.717  87.144  1.00 19.27 ? 354  ILE A N     1 
ATOM   2567  C  CA    . ILE A  1  356  ? -60.012 54.007  86.809  1.00 16.64 ? 354  ILE A CA    1 
ATOM   2568  C  C     . ILE A  1  356  ? -61.218 54.812  87.262  1.00 16.53 ? 354  ILE A C     1 
ATOM   2569  O  O     . ILE A  1  356  ? -62.208 54.941  86.533  1.00 19.81 ? 354  ILE A O     1 
ATOM   2570  C  CB    . ILE A  1  356  ? -59.986 52.595  87.429  1.00 18.78 ? 354  ILE A CB    1 
ATOM   2571  C  CG1   . ILE A  1  356  ? -58.908 51.763  86.729  1.00 19.77 ? 354  ILE A CG1   1 
ATOM   2572  C  CG2   . ILE A  1  356  ? -61.354 51.931  87.340  1.00 21.90 ? 354  ILE A CG2   1 
ATOM   2573  C  CD1   . ILE A  1  356  ? -58.491 50.505  87.508  1.00 21.36 ? 354  ILE A CD1   1 
ATOM   2574  N  N     . ASP A  1  357  ? -61.137 55.406  88.449  1.00 18.16 ? 355  ASP A N     1 
ATOM   2575  C  CA    . ASP A  1  357  ? -62.254 56.213  88.919  1.00 20.82 ? 355  ASP A CA    1 
ATOM   2576  C  C     . ASP A  1  357  ? -62.416 57.462  88.064  1.00 21.95 ? 355  ASP A C     1 
ATOM   2577  O  O     . ASP A  1  357  ? -63.539 57.844  87.725  1.00 19.59 ? 355  ASP A O     1 
ATOM   2578  C  CB    . ASP A  1  357  ? -62.060 56.583  90.385  1.00 18.65 ? 355  ASP A CB    1 
ATOM   2579  C  CG    . ASP A  1  357  ? -63.110 57.560  90.871  1.00 22.03 ? 355  ASP A CG    1 
ATOM   2580  O  OD1   . ASP A  1  357  ? -64.241 57.113  91.159  1.00 27.35 ? 355  ASP A OD1   1 
ATOM   2581  O  OD2   . ASP A  1  357  ? -62.800 58.770  90.939  1.00 22.92 ? 355  ASP A OD2   1 
ATOM   2582  N  N     . LEU A  1  358  ? -61.306 58.082  87.665  1.00 18.38 ? 356  LEU A N     1 
ATOM   2583  C  CA    . LEU A  1  358  ? -61.401 59.248  86.794  1.00 18.20 ? 356  LEU A CA    1 
ATOM   2584  C  C     . LEU A  1  358  ? -62.019 58.878  85.453  1.00 19.06 ? 356  LEU A C     1 
ATOM   2585  O  O     . LEU A  1  358  ? -62.818 59.638  84.895  1.00 19.94 ? 356  LEU A O     1 
ATOM   2586  C  CB    . LEU A  1  358  ? -60.017 59.857  86.602  1.00 16.70 ? 356  LEU A CB    1 
ATOM   2587  C  CG    . LEU A  1  358  ? -59.913 60.973  85.572  1.00 17.13 ? 356  LEU A CG    1 
ATOM   2588  C  CD1   . LEU A  1  358  ? -60.785 62.147  85.978  1.00 21.27 ? 356  LEU A CD1   1 
ATOM   2589  C  CD2   . LEU A  1  358  ? -58.439 61.402  85.444  1.00 18.64 ? 356  LEU A CD2   1 
ATOM   2590  N  N     . ALA A  1  359  ? -61.664 57.708  84.923  1.00 20.37 ? 357  ALA A N     1 
ATOM   2591  C  CA    . ALA A  1  359  ? -62.282 57.226  83.693  1.00 20.98 ? 357  ALA A CA    1 
ATOM   2592  C  C     . ALA A  1  359  ? -63.787 57.049  83.872  1.00 20.31 ? 357  ALA A C     1 
ATOM   2593  O  O     . ALA A  1  359  ? -64.567 57.398  82.981  1.00 21.20 ? 357  ALA A O     1 
ATOM   2594  C  CB    . ALA A  1  359  ? -61.628 55.906  83.270  1.00 21.42 ? 357  ALA A CB    1 
ATOM   2595  N  N     . ARG A  1  360  ? -64.217 56.509  85.021  1.00 19.72 ? 358  ARG A N     1 
ATOM   2596  C  CA    . ARG A  1  360  ? -65.646 56.375  85.274  1.00 21.11 ? 358  ARG A CA    1 
ATOM   2597  C  C     . ARG A  1  360  ? -66.320 57.740  85.358  1.00 24.38 ? 358  ARG A C     1 
ATOM   2598  O  O     . ARG A  1  360  ? -67.371 57.961  84.743  1.00 24.98 ? 358  ARG A O     1 
ATOM   2599  C  CB    . ARG A  1  360  ? -65.889 55.580  86.559  1.00 23.81 ? 358  ARG A CB    1 
ATOM   2600  C  CG    . ARG A  1  360  ? -65.448 54.127  86.501  1.00 30.92 ? 358  ARG A CG    1 
ATOM   2601  C  CD    . ARG A  1  360  ? -65.957 53.365  87.728  1.00 30.21 ? 358  ARG A CD    1 
ATOM   2602  N  NE    . ARG A  1  360  ? -65.263 52.093  87.887  1.00 33.06 ? 358  ARG A NE    1 
ATOM   2603  C  CZ    . ARG A  1  360  ? -65.571 50.990  87.220  1.00 39.03 ? 358  ARG A CZ    1 
ATOM   2604  N  NH1   . ARG A  1  360  ? -66.595 50.954  86.381  1.00 39.00 ? 358  ARG A NH1   1 
ATOM   2605  N  NH2   . ARG A  1  360  ? -64.834 49.898  87.399  1.00 40.91 ? 358  ARG A NH2   1 
ATOM   2606  N  N     . ARG A  1  361  ? -65.726 58.673  86.108  1.00 21.90 ? 359  ARG A N     1 
ATOM   2607  C  CA    . ARG A  1  361  ? -66.338 59.993  86.272  1.00 21.91 ? 359  ARG A CA    1 
ATOM   2608  C  C     . ARG A  1  361  ? -66.407 60.750  84.954  1.00 22.83 ? 359  ARG A C     1 
ATOM   2609  O  O     . ARG A  1  361  ? -67.415 61.399  84.644  1.00 24.16 ? 359  ARG A O     1 
ATOM   2610  C  CB    . ARG A  1  361  ? -65.540 60.818  87.282  1.00 24.07 ? 359  ARG A CB    1 
ATOM   2611  C  CG    . ARG A  1  361  ? -65.621 60.318  88.703  1.00 25.59 ? 359  ARG A CG    1 
ATOM   2612  C  CD    . ARG A  1  361  ? -64.935 61.292  89.637  1.00 28.29 ? 359  ARG A CD    1 
ATOM   2613  N  NE    . ARG A  1  361  ? -63.479 61.195  89.605  1.00 27.21 ? 359  ARG A NE    1 
ATOM   2614  C  CZ    . ARG A  1  361  ? -62.657 62.196  89.317  1.00 26.34 ? 359  ARG A CZ    1 
ATOM   2615  N  NH1   . ARG A  1  361  ? -63.111 63.381  88.934  1.00 24.71 ? 359  ARG A NH1   1 
ATOM   2616  N  NH2   . ARG A  1  361  ? -61.343 62.009  89.426  1.00 23.65 ? 359  ARG A NH2   1 
ATOM   2617  N  N     . SER A  1  362  ? -65.327 60.718  84.186  1.00 21.14 ? 360  SER A N     1 
ATOM   2618  C  CA    . SER A  1  362  ? -65.258 61.492  82.957  1.00 21.00 ? 360  SER A CA    1 
ATOM   2619  C  C     . SER A  1  362  ? -65.941 60.801  81.794  1.00 21.60 ? 360  SER A C     1 
ATOM   2620  O  O     . SER A  1  362  ? -66.243 61.452  80.788  1.00 23.51 ? 360  SER A O     1 
ATOM   2621  C  CB    . SER A  1  362  ? -63.798 61.746  82.592  1.00 20.91 ? 360  SER A CB    1 
ATOM   2622  O  OG    . SER A  1  362  ? -63.152 60.511  82.287  1.00 19.53 ? 360  SER A OG    1 
ATOM   2623  N  N     . GLY A  1  363  ? -66.171 59.498  81.900  1.00 22.18 ? 361  GLY A N     1 
ATOM   2624  C  CA    . GLY A  1  363  ? -66.677 58.755  80.774  1.00 20.21 ? 361  GLY A CA    1 
ATOM   2625  C  C     . GLY A  1  363  ? -65.669 58.534  79.674  1.00 25.08 ? 361  GLY A C     1 
ATOM   2626  O  O     . GLY A  1  363  ? -66.060 58.121  78.580  1.00 23.99 ? 361  GLY A O     1 
ATOM   2627  N  N     . ARG A  1  364  ? -64.392 58.820  79.929  1.00 21.50 ? 362  ARG A N     1 
ATOM   2628  C  CA    . ARG A  1  364  ? -63.319 58.634  78.956  1.00 21.48 ? 362  ARG A CA    1 
ATOM   2629  C  C     . ARG A  1  364  ? -62.639 57.309  79.227  1.00 21.61 ? 362  ARG A C     1 
ATOM   2630  O  O     . ARG A  1  364  ? -62.260 57.028  80.368  1.00 21.98 ? 362  ARG A O     1 
ATOM   2631  C  CB    . ARG A  1  364  ? -62.263 59.734  79.048  1.00 24.60 ? 362  ARG A CB    1 
ATOM   2632  C  CG    . ARG A  1  364  ? -62.799 61.138  79.161  1.00 30.33 ? 362  ARG A CG    1 
ATOM   2633  C  CD    . ARG A  1  364  ? -62.643 61.896  77.876  1.00 22.48 ? 362  ARG A CD    1 
ATOM   2634  N  NE    . ARG A  1  364  ? -63.457 63.099  77.947  1.00 19.32 ? 362  ARG A NE    1 
ATOM   2635  C  CZ    . ARG A  1  364  ? -62.979 64.329  78.076  1.00 20.43 ? 362  ARG A CZ    1 
ATOM   2636  N  NH1   . ARG A  1  364  ? -61.677 64.574  78.050  1.00 19.40 ? 362  ARG A NH1   1 
ATOM   2637  N  NH2   . ARG A  1  364  ? -63.834 65.339  78.224  1.00 18.33 ? 362  ARG A NH2   1 
ATOM   2638  N  N     . ARG A  1  365  ? -62.461 56.512  78.182  1.00 20.09 ? 363  ARG A N     1 
ATOM   2639  C  CA    . ARG A  1  365  ? -61.802 55.221  78.338  1.00 18.90 ? 363  ARG A CA    1 
ATOM   2640  C  C     . ARG A  1  365  ? -60.298 55.468  78.291  1.00 20.78 ? 363  ARG A C     1 
ATOM   2641  O  O     . ARG A  1  365  ? -59.664 55.391  77.241  1.00 21.29 ? 363  ARG A O     1 
ATOM   2642  C  CB    . ARG A  1  365  ? -62.263 54.252  77.262  1.00 18.68 ? 363  ARG A CB    1 
ATOM   2643  C  CG    . ARG A  1  365  ? -61.707 52.861  77.464  1.00 20.36 ? 363  ARG A CG    1 
ATOM   2644  C  CD    . ARG A  1  365  ? -62.585 51.836  76.809  1.00 25.29 ? 363  ARG A CD    1 
ATOM   2645  N  NE    . ARG A  1  365  ? -62.099 50.506  77.136  1.00 23.06 ? 363  ARG A NE    1 
ATOM   2646  C  CZ    . ARG A  1  365  ? -61.398 49.753  76.306  1.00 21.95 ? 363  ARG A CZ    1 
ATOM   2647  N  NH1   . ARG A  1  365  ? -61.172 50.127  75.057  1.00 22.97 ? 363  ARG A NH1   1 
ATOM   2648  N  NH2   . ARG A  1  365  ? -60.899 48.604  76.744  1.00 22.16 ? 363  ARG A NH2   1 
ATOM   2649  N  N     . ILE A  1  366  ? -59.720 55.789  79.447  1.00 19.42 ? 364  ILE A N     1 
ATOM   2650  C  CA    . ILE A  1  366  ? -58.318 56.190  79.475  1.00 17.46 ? 364  ILE A CA    1 
ATOM   2651  C  C     . ILE A  1  366  ? -57.440 55.033  79.036  1.00 18.76 ? 364  ILE A C     1 
ATOM   2652  O  O     . ILE A  1  366  ? -57.603 53.897  79.494  1.00 19.40 ? 364  ILE A O     1 
ATOM   2653  C  CB    . ILE A  1  366  ? -57.935 56.697  80.872  1.00 17.45 ? 364  ILE A CB    1 
ATOM   2654  C  CG1   . ILE A  1  366  ? -58.796 57.914  81.204  1.00 20.24 ? 364  ILE A CG1   1 
ATOM   2655  C  CG2   . ILE A  1  366  ? -56.456 57.071  80.927  1.00 18.80 ? 364  ILE A CG2   1 
ATOM   2656  C  CD1   . ILE A  1  366  ? -58.643 58.431  82.621  1.00 21.43 ? 364  ILE A CD1   1 
ATOM   2657  N  N     . MET A  1  367  ? -56.503 55.318  78.138  1.00 17.48 ? 365  MET A N     1 
ATOM   2658  C  CA    . MET A  1  367  ? -55.546 54.308  77.709  1.00 18.42 ? 365  MET A CA    1 
ATOM   2659  C  C     . MET A  1  367  ? -54.443 54.271  78.746  1.00 18.76 ? 365  MET A C     1 
ATOM   2660  O  O     . MET A  1  367  ? -53.753 55.268  78.953  1.00 21.14 ? 365  MET A O     1 
ATOM   2661  C  CB    . MET A  1  367  ? -54.983 54.627  76.325  1.00 18.88 ? 365  MET A CB    1 
ATOM   2662  C  CG    . MET A  1  367  ? -56.082 54.942  75.318  1.00 18.31 ? 365  MET A CG    1 
ATOM   2663  S  SD    . MET A  1  367  ? -55.527 55.308  73.633  1.00 20.64 ? 365  MET A SD    1 
ATOM   2664  C  CE    . MET A  1  367  ? -55.312 53.677  72.905  1.00 23.14 ? 365  MET A CE    1 
ATOM   2665  N  N     . VAL A  1  368  ? -54.288 53.153  79.429  1.00 16.21 ? 366  VAL A N     1 
ATOM   2666  C  CA    . VAL A  1  368  ? -53.353 53.098  80.540  1.00 17.08 ? 366  VAL A CA    1 
ATOM   2667  C  C     . VAL A  1  368  ? -52.202 52.200  80.122  1.00 18.80 ? 366  VAL A C     1 
ATOM   2668  O  O     . VAL A  1  368  ? -52.393 50.990  79.928  1.00 18.71 ? 366  VAL A O     1 
ATOM   2669  C  CB    . VAL A  1  368  ? -54.021 52.590  81.824  1.00 17.61 ? 366  VAL A CB    1 
ATOM   2670  C  CG1   . VAL A  1  368  ? -52.990 52.521  82.952  1.00 20.94 ? 366  VAL A CG1   1 
ATOM   2671  C  CG2   . VAL A  1  368  ? -55.189 53.476  82.212  1.00 20.38 ? 366  VAL A CG2   1 
ATOM   2672  N  N     . ARG A  1  369  ? -51.016 52.787  79.936  1.00 16.45 ? 367  ARG A N     1 
ATOM   2673  C  CA    . ARG A  1  369  ? -49.836 51.988  79.628  1.00 17.47 ? 367  ARG A CA    1 
ATOM   2674  C  C     . ARG A  1  369  ? -49.164 51.596  80.934  1.00 20.31 ? 367  ARG A C     1 
ATOM   2675  O  O     . ARG A  1  369  ? -48.667 52.456  81.670  1.00 18.63 ? 367  ARG A O     1 
ATOM   2676  C  CB    . ARG A  1  369  ? -48.851 52.738  78.736  1.00 17.57 ? 367  ARG A CB    1 
ATOM   2677  C  CG    . ARG A  1  369  ? -47.639 51.878  78.422  1.00 19.19 ? 367  ARG A CG    1 
ATOM   2678  C  CD    . ARG A  1  369  ? -46.469 52.713  77.945  1.00 20.22 ? 367  ARG A CD    1 
ATOM   2679  N  NE    . ARG A  1  369  ? -46.767 53.369  76.683  1.00 18.66 ? 367  ARG A NE    1 
ATOM   2680  C  CZ    . ARG A  1  369  ? -46.229 54.517  76.289  1.00 20.51 ? 367  ARG A CZ    1 
ATOM   2681  N  NH1   . ARG A  1  369  ? -45.335 55.156  77.035  1.00 21.08 ? 367  ARG A NH1   1 
ATOM   2682  N  NH2   . ARG A  1  369  ? -46.611 55.046  75.125  1.00 20.99 ? 367  ARG A NH2   1 
ATOM   2683  N  N     . LEU A  1  370  ? -49.144 50.304  81.216  1.00 18.56 ? 368  LEU A N     1 
ATOM   2684  C  CA    . LEU A  1  370  ? -48.458 49.795  82.392  1.00 16.21 ? 368  LEU A CA    1 
ATOM   2685  C  C     . LEU A  1  370  ? -47.027 49.450  82.009  1.00 18.32 ? 368  LEU A C     1 
ATOM   2686  O  O     . LEU A  1  370  ? -46.797 48.627  81.123  1.00 18.55 ? 368  LEU A O     1 
ATOM   2687  C  CB    . LEU A  1  370  ? -49.181 48.572  82.953  1.00 18.52 ? 368  LEU A CB    1 
ATOM   2688  C  CG    . LEU A  1  370  ? -48.603 48.042  84.257  1.00 18.04 ? 368  LEU A CG    1 
ATOM   2689  C  CD1   . LEU A  1  370  ? -48.815 49.038  85.391  1.00 20.58 ? 368  LEU A CD1   1 
ATOM   2690  C  CD2   . LEU A  1  370  ? -49.270 46.706  84.593  1.00 20.00 ? 368  LEU A CD2   1 
ATOM   2691  N  N     . VAL A  1  371  ? -46.070 50.084  82.670  1.00 16.49 ? 369  VAL A N     1 
ATOM   2692  C  CA    . VAL A  1  371  ? -44.663 49.826  82.431  1.00 15.99 ? 369  VAL A CA    1 
ATOM   2693  C  C     . VAL A  1  371  ? -44.056 49.443  83.758  1.00 16.57 ? 369  VAL A C     1 
ATOM   2694  O  O     . VAL A  1  371  ? -44.667 49.611  84.807  1.00 18.64 ? 369  VAL A O     1 
ATOM   2695  C  CB    . VAL A  1  371  ? -43.933 51.042  81.836  1.00 18.04 ? 369  VAL A CB    1 
ATOM   2696  C  CG1   . VAL A  1  371  ? -44.653 51.553  80.609  1.00 18.00 ? 369  VAL A CG1   1 
ATOM   2697  C  CG2   . VAL A  1  371  ? -43.801 52.152  82.879  1.00 17.85 ? 369  VAL A CG2   1 
ATOM   2698  N  N     . LYS A  1  372  ? -42.822 48.965  83.716  1.00 18.51 ? 370  LYS A N     1 
ATOM   2699  C  CA    . LYS A  1  372  ? -42.156 48.770  84.996  1.00 18.34 ? 370  LYS A CA    1 
ATOM   2700  C  C     . LYS A  1  372  ? -41.525 50.076  85.479  1.00 17.57 ? 370  LYS A C     1 
ATOM   2701  O  O     . LYS A  1  372  ? -41.866 50.562  86.561  1.00 22.05 ? 370  LYS A O     1 
ATOM   2702  C  CB    . LYS A  1  372  ? -41.167 47.603  84.897  1.00 20.04 ? 370  LYS A CB    1 
ATOM   2703  C  CG    . LYS A  1  372  ? -41.953 46.296  84.767  1.00 20.38 ? 370  LYS A CG    1 
ATOM   2704  C  CD    . LYS A  1  372  ? -41.101 45.039  84.686  1.00 21.53 ? 370  LYS A CD    1 
ATOM   2705  C  CE    . LYS A  1  372  ? -42.033 43.851  84.405  1.00 22.66 ? 370  LYS A CE    1 
ATOM   2706  N  NZ    . LYS A  1  372  ? -41.299 42.591  84.108  1.00 21.00 ? 370  LYS A NZ    1 
ATOM   2707  N  N     . GLY A  1  373  ? -40.686 50.718  84.665  1.00 18.50 ? 371  GLY A N     1 
ATOM   2708  C  CA    . GLY A  1  373  ? -40.183 52.045  85.008  1.00 17.43 ? 371  GLY A CA    1 
ATOM   2709  C  C     . GLY A  1  373  ? -38.757 52.269  84.546  1.00 16.28 ? 371  GLY A C     1 
ATOM   2710  O  O     . GLY A  1  373  ? -37.932 51.356  84.633  1.00 17.54 ? 371  GLY A O     1 
ATOM   2711  N  N     . ALA A  1  374  ? -38.434 53.473  84.071  1.00 17.26 ? 372  ALA A N     1 
ATOM   2712  C  CA    . ALA A  1  374  ? -37.166 53.701  83.384  1.00 18.38 ? 372  ALA A CA    1 
ATOM   2713  C  C     . ALA A  1  374  ? -36.121 54.444  84.208  1.00 20.62 ? 372  ALA A C     1 
ATOM   2714  O  O     . ALA A  1  374  ? -35.001 54.623  83.718  1.00 21.44 ? 372  ALA A O     1 
ATOM   2715  C  CB    . ALA A  1  374  ? -37.398 54.480  82.086  1.00 20.01 ? 372  ALA A CB    1 
ATOM   2716  N  N     . TYR A  1  375  ? -36.440 54.881  85.428  1.00 18.28 ? 373  TYR A N     1 
ATOM   2717  C  CA    . TYR A  1  375  ? -35.572 55.796  86.171  1.00 16.48 ? 373  TYR A CA    1 
ATOM   2718  C  C     . TYR A  1  375  ? -35.069 55.189  87.476  1.00 15.67 ? 373  TYR A C     1 
ATOM   2719  O  O     . TYR A  1  375  ? -34.798 55.919  88.431  1.00 17.23 ? 373  TYR A O     1 
ATOM   2720  C  CB    . TYR A  1  375  ? -36.300 57.112  86.473  1.00 18.46 ? 373  TYR A CB    1 
ATOM   2721  C  CG    . TYR A  1  375  ? -36.866 57.791  85.246  1.00 15.60 ? 373  TYR A CG    1 
ATOM   2722  C  CD1   . TYR A  1  375  ? -38.078 57.369  84.694  1.00 17.45 ? 373  TYR A CD1   1 
ATOM   2723  C  CD2   . TYR A  1  375  ? -36.184 58.826  84.629  1.00 20.39 ? 373  TYR A CD2   1 
ATOM   2724  C  CE1   . TYR A  1  375  ? -38.589 57.964  83.560  1.00 18.25 ? 373  TYR A CE1   1 
ATOM   2725  C  CE2   . TYR A  1  375  ? -36.695 59.435  83.500  1.00 22.83 ? 373  TYR A CE2   1 
ATOM   2726  C  CZ    . TYR A  1  375  ? -37.890 58.994  82.969  1.00 24.20 ? 373  TYR A CZ    1 
ATOM   2727  O  OH    . TYR A  1  375  ? -38.402 59.606  81.846  1.00 25.61 ? 373  TYR A OH    1 
ATOM   2728  N  N     . TRP A  1  376  ? -34.912 53.868  87.524  1.00 16.78 ? 374  TRP A N     1 
ATOM   2729  C  CA    . TRP A  1  376  ? -34.739 53.206  88.813  1.00 18.75 ? 374  TRP A CA    1 
ATOM   2730  C  C     . TRP A  1  376  ? -33.488 53.694  89.539  1.00 20.66 ? 374  TRP A C     1 
ATOM   2731  O  O     . TRP A  1  376  ? -33.572 54.127  90.698  1.00 17.49 ? 374  TRP A O     1 
ATOM   2732  C  CB    . TRP A  1  376  ? -34.715 51.688  88.644  1.00 18.45 ? 374  TRP A CB    1 
ATOM   2733  C  CG    . TRP A  1  376  ? -34.553 50.995  89.961  1.00 18.57 ? 374  TRP A CG    1 
ATOM   2734  C  CD1   . TRP A  1  376  ? -35.522 50.780  90.905  1.00 19.01 ? 374  TRP A CD1   1 
ATOM   2735  C  CD2   . TRP A  1  376  ? -33.338 50.478  90.508  1.00 20.54 ? 374  TRP A CD2   1 
ATOM   2736  N  NE1   . TRP A  1  376  ? -34.985 50.136  91.994  1.00 18.99 ? 374  TRP A NE1   1 
ATOM   2737  C  CE2   . TRP A  1  376  ? -33.642 49.948  91.777  1.00 19.80 ? 374  TRP A CE2   1 
ATOM   2738  C  CE3   . TRP A  1  376  ? -32.024 50.405  90.045  1.00 21.60 ? 374  TRP A CE3   1 
ATOM   2739  C  CZ2   . TRP A  1  376  ? -32.676 49.347  92.587  1.00 21.63 ? 374  TRP A CZ2   1 
ATOM   2740  C  CZ3   . TRP A  1  376  ? -31.062 49.809  90.854  1.00 23.66 ? 374  TRP A CZ3   1 
ATOM   2741  C  CH2   . TRP A  1  376  ? -31.398 49.286  92.106  1.00 23.75 ? 374  TRP A CH2   1 
ATOM   2742  N  N     . ASP A  1  377  ? -32.311 53.627  88.884  1.00 19.20 ? 375  ASP A N     1 
ATOM   2743  C  CA    A ASP A  1  377  ? -31.118 54.005  89.627  0.46 19.34 ? 375  ASP A CA    1 
ATOM   2744  C  CA    B ASP A  1  377  ? -31.055 54.057  89.512  0.54 19.37 ? 375  ASP A CA    1 
ATOM   2745  C  C     . ASP A  1  377  ? -31.163 55.469  90.045  1.00 18.67 ? 375  ASP A C     1 
ATOM   2746  O  O     . ASP A  1  377  ? -30.659 55.796  91.126  1.00 19.34 ? 375  ASP A O     1 
ATOM   2747  C  CB    A ASP A  1  377  ? -29.834 53.678  88.852  0.46 22.44 ? 375  ASP A CB    1 
ATOM   2748  C  CB    B ASP A  1  377  ? -29.897 54.038  88.507  0.54 22.23 ? 375  ASP A CB    1 
ATOM   2749  C  CG    A ASP A  1  377  ? -29.811 54.248  87.453  0.46 24.55 ? 375  ASP A CG    1 
ATOM   2750  C  CG    B ASP A  1  377  ? -29.532 52.660  88.031  0.54 27.94 ? 375  ASP A CG    1 
ATOM   2751  O  OD1   A ASP A  1  377  ? -30.207 55.409  87.261  0.46 26.87 ? 375  ASP A OD1   1 
ATOM   2752  O  OD1   B ASP A  1  377  ? -29.665 51.700  88.804  0.54 34.72 ? 375  ASP A OD1   1 
ATOM   2753  O  OD2   A ASP A  1  377  ? -29.346 53.527  86.542  0.46 26.34 ? 375  ASP A OD2   1 
ATOM   2754  O  OD2   B ASP A  1  377  ? -29.084 52.549  86.871  0.54 33.39 ? 375  ASP A OD2   1 
ATOM   2755  N  N     . ALA A  1  378  ? -31.776 56.345  89.242  1.00 18.25 ? 376  ALA A N     1 
ATOM   2756  C  CA    . ALA A  1  378  ? -31.864 57.745  89.615  1.00 17.50 ? 376  ALA A CA    1 
ATOM   2757  C  C     . ALA A  1  378  ? -32.765 57.929  90.817  1.00 16.48 ? 376  ALA A C     1 
ATOM   2758  O  O     . ALA A  1  378  ? -32.514 58.812  91.648  1.00 18.56 ? 376  ALA A O     1 
ATOM   2759  C  CB    . ALA A  1  378  ? -32.373 58.580  88.439  1.00 18.57 ? 376  ALA A CB    1 
ATOM   2760  N  N     . GLU A  1  379  ? -33.811 57.107  90.930  1.00 16.26 ? 377  GLU A N     1 
ATOM   2761  C  CA    . GLU A  1  379  ? -34.692 57.240  92.084  1.00 14.84 ? 377  GLU A CA    1 
ATOM   2762  C  C     . GLU A  1  379  ? -33.980 56.809  93.355  1.00 17.02 ? 377  GLU A C     1 
ATOM   2763  O  O     . GLU A  1  379  ? -34.213 57.385  94.420  1.00 18.74 ? 377  GLU A O     1 
ATOM   2764  C  CB    . GLU A  1  379  ? -35.965 56.419  91.896  1.00 16.93 ? 377  GLU A CB    1 
ATOM   2765  C  CG    . GLU A  1  379  ? -36.855 56.838  90.705  1.00 17.47 ? 377  GLU A CG    1 
ATOM   2766  C  CD    . GLU A  1  379  ? -37.446 58.233  90.801  1.00 18.78 ? 377  GLU A CD    1 
ATOM   2767  O  OE1   . GLU A  1  379  ? -37.314 58.916  91.840  1.00 19.10 ? 377  GLU A OE1   1 
ATOM   2768  O  OE2   . GLU A  1  379  ? -38.066 58.640  89.801  1.00 18.69 ? 377  GLU A OE2   1 
ATOM   2769  N  N     . ILE A  1  380  ? -33.125 55.785  93.266  1.00 16.10 ? 378  ILE A N     1 
ATOM   2770  C  CA    . ILE A  1  380  ? -32.368 55.354  94.441  1.00 17.89 ? 378  ILE A CA    1 
ATOM   2771  C  C     . ILE A  1  380  ? -31.439 56.467  94.889  1.00 19.35 ? 378  ILE A C     1 
ATOM   2772  O  O     . ILE A  1  380  ? -31.399 56.837  96.068  1.00 17.78 ? 378  ILE A O     1 
ATOM   2773  C  CB    . ILE A  1  380  ? -31.586 54.067  94.135  1.00 17.14 ? 378  ILE A CB    1 
ATOM   2774  C  CG1   . ILE A  1  380  ? -32.526 52.933  93.719  1.00 17.42 ? 378  ILE A CG1   1 
ATOM   2775  C  CG2   . ILE A  1  380  ? -30.752 53.632  95.358  1.00 18.77 ? 378  ILE A CG2   1 
ATOM   2776  C  CD1   . ILE A  1  380  ? -33.657 52.593  94.714  1.00 18.97 ? 378  ILE A CD1   1 
ATOM   2777  N  N     . LYS A  1  381  ? -30.698 57.038  93.937  1.00 15.99 ? 379  LYS A N     1 
ATOM   2778  C  CA    . LYS A  1  381  ? -29.761 58.104  94.254  1.00 17.18 ? 379  LYS A CA    1 
ATOM   2779  C  C     . LYS A  1  381  ? -30.479 59.305  94.856  1.00 18.91 ? 379  LYS A C     1 
ATOM   2780  O  O     . LYS A  1  381  ? -30.034 59.860  95.865  1.00 17.44 ? 379  LYS A O     1 
ATOM   2781  C  CB    . LYS A  1  381  ? -28.981 58.502  92.998  1.00 16.79 ? 379  LYS A CB    1 
ATOM   2782  C  CG    . LYS A  1  381  ? -28.038 59.677  93.240  1.00 18.07 ? 379  LYS A CG    1 
ATOM   2783  C  CD    . LYS A  1  381  ? -27.149 59.939  92.031  1.00 17.89 ? 379  LYS A CD    1 
ATOM   2784  C  CE    . LYS A  1  381  ? -26.157 61.045  92.331  1.00 17.77 ? 379  LYS A CE    1 
ATOM   2785  N  NZ    . LYS A  1  381  ? -25.261 61.338  91.148  1.00 18.22 ? 379  LYS A NZ    1 
ATOM   2786  N  N     . ARG A  1  382  ? -31.608 59.709  94.261  1.00 16.51 ? 380  ARG A N     1 
ATOM   2787  C  CA    . ARG A  1  382  ? -32.296 60.911  94.721  1.00 17.84 ? 380  ARG A CA    1 
ATOM   2788  C  C     . ARG A  1  382  ? -32.774 60.762  96.158  1.00 18.11 ? 380  ARG A C     1 
ATOM   2789  O  O     . ARG A  1  382  ? -32.613 61.676  96.976  1.00 19.40 ? 380  ARG A O     1 
ATOM   2790  C  CB    . ARG A  1  382  ? -33.478 61.216  93.791  1.00 21.04 ? 380  ARG A CB    1 
ATOM   2791  C  CG    . ARG A  1  382  ? -34.139 62.557  94.025  1.00 25.77 ? 380  ARG A CG    1 
ATOM   2792  C  CD    . ARG A  1  382  ? -33.281 63.675  93.453  1.00 41.00 ? 380  ARG A CD    1 
ATOM   2793  N  NE    . ARG A  1  382  ? -32.588 64.404  94.507  1.00 45.09 ? 380  ARG A NE    1 
ATOM   2794  C  CZ    . ARG A  1  382  ? -31.566 65.226  94.315  1.00 42.07 ? 380  ARG A CZ    1 
ATOM   2795  N  NH1   . ARG A  1  382  ? -31.043 65.412  93.113  1.00 50.45 ? 380  ARG A NH1   1 
ATOM   2796  N  NH2   . ARG A  1  382  ? -31.056 65.881  95.356  1.00 34.01 ? 380  ARG A NH2   1 
ATOM   2797  N  N     . ALA A  1  383  ? -33.378 59.617  96.483  1.00 17.45 ? 381  ALA A N     1 
ATOM   2798  C  CA    . ALA A  1  383  ? -33.889 59.423  97.837  1.00 15.60 ? 381  ALA A CA    1 
ATOM   2799  C  C     . ALA A  1  383  ? -32.751 59.418  98.847  1.00 18.13 ? 381  ALA A C     1 
ATOM   2800  O  O     . ALA A  1  383  ? -32.900 59.929  99.965  1.00 18.71 ? 381  ALA A O     1 
ATOM   2801  C  CB    . ALA A  1  383  ? -34.694 58.123  97.918  1.00 18.45 ? 381  ALA A CB    1 
ATOM   2802  N  N     . GLN A  1  384  ? -31.603 58.854  98.466  1.00 17.92 ? 382  GLN A N     1 
ATOM   2803  C  CA    . GLN A  1  384  ? -30.454 58.859  99.362  1.00 18.19 ? 382  GLN A CA    1 
ATOM   2804  C  C     . GLN A  1  384  ? -29.922 60.269  99.553  1.00 18.50 ? 382  GLN A C     1 
ATOM   2805  O  O     . GLN A  1  384  ? -29.679 60.698  100.685 1.00 21.31 ? 382  GLN A O     1 
ATOM   2806  C  CB    . GLN A  1  384  ? -29.363 57.935  98.824  1.00 17.97 ? 382  GLN A CB    1 
ATOM   2807  C  CG    . GLN A  1  384  ? -29.711 56.458  98.961  1.00 17.26 ? 382  GLN A CG    1 
ATOM   2808  C  CD    . GLN A  1  384  ? -28.571 55.554  98.529  1.00 17.74 ? 382  GLN A CD    1 
ATOM   2809  O  OE1   . GLN A  1  384  ? -27.657 55.984  97.830  1.00 20.21 ? 382  GLN A OE1   1 
ATOM   2810  N  NE2   . GLN A  1  384  ? -28.627 54.293  98.938  1.00 19.82 ? 382  GLN A NE2   1 
ATOM   2811  N  N     . LEU A  1  385  ? -29.753 61.016  98.456  1.00 17.94 ? 383  LEU A N     1 
ATOM   2812  C  CA    . LEU A  1  385  ? -29.282 62.394  98.562  1.00 18.80 ? 383  LEU A CA    1 
ATOM   2813  C  C     . LEU A  1  385  ? -30.191 63.227  99.451  1.00 19.35 ? 383  LEU A C     1 
ATOM   2814  O  O     . LEU A  1  385  ? -29.718 64.051  100.240 1.00 20.37 ? 383  LEU A O     1 
ATOM   2815  C  CB    . LEU A  1  385  ? -29.207 63.038  97.176  1.00 18.18 ? 383  LEU A CB    1 
ATOM   2816  C  CG    . LEU A  1  385  ? -28.049 62.612  96.283  1.00 20.92 ? 383  LEU A CG    1 
ATOM   2817  C  CD1   . LEU A  1  385  ? -28.209 63.255  94.926  1.00 21.02 ? 383  LEU A CD1   1 
ATOM   2818  C  CD2   . LEU A  1  385  ? -26.749 63.047  96.913  1.00 22.37 ? 383  LEU A CD2   1 
ATOM   2819  N  N     . ASP A  1  386  ? -31.504 63.047  99.314  1.00 19.18 ? 384  ASP A N     1 
ATOM   2820  C  CA    . ASP A  1  386  ? -32.460 63.880  100.017 1.00 19.19 ? 384  ASP A CA    1 
ATOM   2821  C  C     . ASP A  1  386  ? -32.738 63.381  101.423 1.00 19.57 ? 384  ASP A C     1 
ATOM   2822  O  O     . ASP A  1  386  ? -33.509 64.022  102.144 1.00 20.34 ? 384  ASP A O     1 
ATOM   2823  C  CB    . ASP A  1  386  ? -33.758 63.966  99.209  1.00 19.60 ? 384  ASP A CB    1 
ATOM   2824  C  CG    . ASP A  1  386  ? -33.602 64.805  97.953  1.00 26.90 ? 384  ASP A CG    1 
ATOM   2825  O  OD1   . ASP A  1  386  ? -32.552 65.467  97.802  1.00 28.10 ? 384  ASP A OD1   1 
ATOM   2826  O  OD2   . ASP A  1  386  ? -34.523 64.802  97.113  1.00 25.94 ? 384  ASP A OD2   1 
ATOM   2827  N  N     . GLY A  1  387  ? -32.138 62.262  101.827 1.00 19.96 ? 385  GLY A N     1 
ATOM   2828  C  CA    . GLY A  1  387  ? -32.321 61.771  103.187 1.00 19.88 ? 385  GLY A CA    1 
ATOM   2829  C  C     . GLY A  1  387  ? -33.755 61.429  103.529 1.00 22.28 ? 385  GLY A C     1 
ATOM   2830  O  O     . GLY A  1  387  ? -34.214 61.702  104.645 1.00 22.87 ? 385  GLY A O     1 
ATOM   2831  N  N     . LEU A  1  388  ? -34.474 60.824  102.597 1.00 20.13 ? 386  LEU A N     1 
ATOM   2832  C  CA    . LEU A  1  388  ? -35.890 60.591  102.817 1.00 21.78 ? 386  LEU A CA    1 
ATOM   2833  C  C     . LEU A  1  388  ? -36.114 59.236  103.468 1.00 20.99 ? 386  LEU A C     1 
ATOM   2834  O  O     . LEU A  1  388  ? -35.200 58.425  103.623 1.00 22.12 ? 386  LEU A O     1 
ATOM   2835  C  CB    . LEU A  1  388  ? -36.657 60.736  101.499 1.00 20.94 ? 386  LEU A CB    1 
ATOM   2836  C  CG    . LEU A  1  388  ? -36.474 62.146  100.915 1.00 22.84 ? 386  LEU A CG    1 
ATOM   2837  C  CD1   . LEU A  1  388  ? -37.189 62.309  99.580  1.00 22.68 ? 386  LEU A CD1   1 
ATOM   2838  C  CD2   . LEU A  1  388  ? -36.930 63.241  101.871 1.00 21.74 ? 386  LEU A CD2   1 
ATOM   2839  N  N     . ALA A  1  389  ? -37.353 59.023  103.921 1.00 24.42 ? 387  ALA A N     1 
ATOM   2840  C  CA    . ALA A  1  389  ? -37.642 57.879  104.772 1.00 25.77 ? 387  ALA A CA    1 
ATOM   2841  C  C     . ALA A  1  389  ? -37.386 56.564  104.049 1.00 21.68 ? 387  ALA A C     1 
ATOM   2842  O  O     . ALA A  1  389  ? -36.920 55.592  104.652 1.00 26.10 ? 387  ALA A O     1 
ATOM   2843  C  CB    . ALA A  1  389  ? -39.089 57.955  105.255 1.00 24.10 ? 387  ALA A CB    1 
ATOM   2844  N  N     . ASP A  1  390  ? -37.678 56.516  102.754 1.00 20.10 ? 388  ASP A N     1 
ATOM   2845  C  CA    . ASP A  1  390  ? -37.605 55.272  102.004 1.00 22.78 ? 388  ASP A CA    1 
ATOM   2846  C  C     . ASP A  1  390  ? -37.610 55.637  100.530 1.00 22.95 ? 388  ASP A C     1 
ATOM   2847  O  O     . ASP A  1  390  ? -37.659 56.815  100.167 1.00 19.74 ? 388  ASP A O     1 
ATOM   2848  C  CB    . ASP A  1  390  ? -38.778 54.350  102.357 1.00 22.46 ? 388  ASP A CB    1 
ATOM   2849  C  CG    . ASP A  1  390  ? -38.459 52.875  102.157 1.00 23.93 ? 388  ASP A CG    1 
ATOM   2850  O  OD1   . ASP A  1  390  ? -37.770 52.513  101.179 1.00 24.39 ? 388  ASP A OD1   1 
ATOM   2851  O  OD2   . ASP A  1  390  ? -38.910 52.062  102.998 1.00 27.55 ? 388  ASP A OD2   1 
ATOM   2852  N  N     . PHE A  1  391  ? -37.580 54.614  99.684  1.00 20.54 ? 389  PHE A N     1 
ATOM   2853  C  CA    . PHE A  1  391  ? -37.601 54.872  98.256  1.00 20.81 ? 389  PHE A CA    1 
ATOM   2854  C  C     . PHE A  1  391  ? -39.033 54.906  97.746  1.00 19.35 ? 389  PHE A C     1 
ATOM   2855  O  O     . PHE A  1  391  ? -39.930 54.332  98.363  1.00 19.72 ? 389  PHE A O     1 
ATOM   2856  C  CB    . PHE A  1  391  ? -36.804 53.799  97.524  1.00 18.75 ? 389  PHE A CB    1 
ATOM   2857  C  CG    . PHE A  1  391  ? -35.388 53.717  98.006  1.00 16.46 ? 389  PHE A CG    1 
ATOM   2858  C  CD1   . PHE A  1  391  ? -34.475 54.663  97.618  1.00 20.68 ? 389  PHE A CD1   1 
ATOM   2859  C  CD2   . PHE A  1  391  ? -35.008 52.746  98.918  1.00 18.26 ? 389  PHE A CD2   1 
ATOM   2860  C  CE1   . PHE A  1  391  ? -33.170 54.625  98.074  1.00 21.14 ? 389  PHE A CE1   1 
ATOM   2861  C  CE2   . PHE A  1  391  ? -33.700 52.707  99.390  1.00 19.57 ? 389  PHE A CE2   1 
ATOM   2862  C  CZ    . PHE A  1  391  ? -32.787 53.643  98.970  1.00 20.84 ? 389  PHE A CZ    1 
ATOM   2863  N  N     . PRO A  1  392  ? -39.274 55.630  96.653  1.00 17.57 ? 390  PRO A N     1 
ATOM   2864  C  CA    . PRO A  1  392  ? -40.595 55.618  96.011  1.00 18.78 ? 390  PRO A CA    1 
ATOM   2865  C  C     . PRO A  1  392  ? -40.755 54.502  94.991  1.00 19.59 ? 390  PRO A C     1 
ATOM   2866  O  O     . PRO A  1  392  ? -41.795 54.422  94.318  1.00 19.62 ? 390  PRO A O     1 
ATOM   2867  C  CB    . PRO A  1  392  ? -40.633 56.988  95.332  1.00 16.75 ? 390  PRO A CB    1 
ATOM   2868  C  CG    . PRO A  1  392  ? -39.180 57.184  94.894  1.00 18.42 ? 390  PRO A CG    1 
ATOM   2869  C  CD    . PRO A  1  392  ? -38.343 56.582  96.016  1.00 16.71 ? 390  PRO A CD    1 
ATOM   2870  N  N     . VAL A  1  393  ? -39.733 53.660  94.867  1.00 19.10 ? 391  VAL A N     1 
ATOM   2871  C  CA    . VAL A  1  393  ? -39.720 52.511  93.981  1.00 17.39 ? 391  VAL A CA    1 
ATOM   2872  C  C     . VAL A  1  393  ? -39.260 51.309  94.782  1.00 18.75 ? 391  VAL A C     1 
ATOM   2873  O  O     . VAL A  1  393  ? -38.632 51.438  95.833  1.00 19.24 ? 391  VAL A O     1 
ATOM   2874  C  CB    . VAL A  1  393  ? -38.788 52.699  92.774  1.00 16.46 ? 391  VAL A CB    1 
ATOM   2875  C  CG1   . VAL A  1  393  ? -39.336 53.768  91.850  1.00 18.13 ? 391  VAL A CG1   1 
ATOM   2876  C  CG2   . VAL A  1  393  ? -37.366 53.044  93.248  1.00 17.48 ? 391  VAL A CG2   1 
ATOM   2877  N  N     . PHE A  1  394  ? -39.560 50.132  94.252  1.00 16.86 ? 392  PHE A N     1 
ATOM   2878  C  CA    . PHE A  1  394  ? -39.045 48.914  94.856  1.00 18.16 ? 392  PHE A CA    1 
ATOM   2879  C  C     . PHE A  1  394  ? -37.531 48.837  94.666  1.00 19.62 ? 392  PHE A C     1 
ATOM   2880  O  O     . PHE A  1  394  ? -36.946 49.521  93.824  1.00 19.97 ? 392  PHE A O     1 
ATOM   2881  C  CB    . PHE A  1  394  ? -39.766 47.705  94.260  1.00 19.79 ? 392  PHE A CB    1 
ATOM   2882  C  CG    . PHE A  1  394  ? -41.244 47.756  94.475  1.00 19.89 ? 392  PHE A CG    1 
ATOM   2883  C  CD1   . PHE A  1  394  ? -41.757 47.656  95.759  1.00 22.84 ? 392  PHE A CD1   1 
ATOM   2884  C  CD2   . PHE A  1  394  ? -42.118 47.962  93.426  1.00 20.61 ? 392  PHE A CD2   1 
ATOM   2885  C  CE1   . PHE A  1  394  ? -43.106 47.741  95.993  1.00 20.72 ? 392  PHE A CE1   1 
ATOM   2886  C  CE2   . PHE A  1  394  ? -43.487 48.050  93.655  1.00 18.75 ? 392  PHE A CE2   1 
ATOM   2887  C  CZ    . PHE A  1  394  ? -43.978 47.933  94.943  1.00 22.28 ? 392  PHE A CZ    1 
ATOM   2888  N  N     . THR A  1  395  ? -36.891 48.011  95.498  1.00 19.99 ? 393  THR A N     1 
ATOM   2889  C  CA    . THR A  1  395  ? -35.451 47.827  95.435  1.00 21.98 ? 393  THR A CA    1 
ATOM   2890  C  C     . THR A  1  395  ? -35.047 46.435  94.990  1.00 22.31 ? 393  THR A C     1 
ATOM   2891  O  O     . THR A  1  395  ? -33.865 46.220  94.702  1.00 21.07 ? 393  THR A O     1 
ATOM   2892  C  CB    . THR A  1  395  ? -34.796 48.108  96.788  1.00 19.75 ? 393  THR A CB    1 
ATOM   2893  O  OG1   . THR A  1  395  ? -35.363 47.239  97.776  1.00 21.61 ? 393  THR A OG1   1 
ATOM   2894  C  CG2   . THR A  1  395  ? -34.978 49.567  97.187  1.00 23.32 ? 393  THR A CG2   1 
ATOM   2895  N  N     . ARG A  1  396  ? -35.978 45.493  94.926  1.00 21.30 ? 394  ARG A N     1 
ATOM   2896  C  CA    . ARG A  1  396  ? -35.730 44.193  94.320  1.00 21.51 ? 394  ARG A CA    1 
ATOM   2897  C  C     . ARG A  1  396  ? -36.513 44.106  93.024  1.00 21.83 ? 394  ARG A C     1 
ATOM   2898  O  O     . ARG A  1  396  ? -37.703 44.430  92.993  1.00 21.74 ? 394  ARG A O     1 
ATOM   2899  C  CB    . ARG A  1  396  ? -36.136 43.053  95.243  1.00 25.34 ? 394  ARG A CB    1 
ATOM   2900  C  CG    . ARG A  1  396  ? -35.306 42.965  96.490  1.00 23.95 ? 394  ARG A CG    1 
ATOM   2901  C  CD    . ARG A  1  396  ? -35.634 41.690  97.246  1.00 26.73 ? 394  ARG A CD    1 
ATOM   2902  N  NE    . ARG A  1  396  ? -35.089 41.747  98.593  1.00 30.00 ? 394  ARG A NE    1 
ATOM   2903  C  CZ    . ARG A  1  396  ? -34.275 40.836  99.105  1.00 36.48 ? 394  ARG A CZ    1 
ATOM   2904  N  NH1   . ARG A  1  396  ? -33.956 39.744  98.432  1.00 38.04 ? 394  ARG A NH1   1 
ATOM   2905  N  NH2   . ARG A  1  396  ? -33.765 41.033  100.318 1.00 32.16 ? 394  ARG A NH2   1 
ATOM   2906  N  N     . LYS A  1  397  ? -35.836 43.682  91.958  1.00 22.62 ? 395  LYS A N     1 
ATOM   2907  C  CA    . LYS A  1  397  ? -36.478 43.617  90.652  1.00 21.59 ? 395  LYS A CA    1 
ATOM   2908  C  C     . LYS A  1  397  ? -37.710 42.725  90.688  1.00 22.50 ? 395  LYS A C     1 
ATOM   2909  O  O     . LYS A  1  397  ? -38.725 43.024  90.046  1.00 22.01 ? 395  LYS A O     1 
ATOM   2910  C  CB    . LYS A  1  397  ? -35.469 43.133  89.608  1.00 26.44 ? 395  LYS A CB    1 
ATOM   2911  C  CG    . LYS A  1  397  ? -35.879 43.396  88.171  1.00 26.88 ? 395  LYS A CG    1 
ATOM   2912  C  CD    . LYS A  1  397  ? -36.591 42.212  87.581  1.00 28.02 ? 395  LYS A CD    1 
ATOM   2913  C  CE    . LYS A  1  397  ? -36.966 42.481  86.134  1.00 27.33 ? 395  LYS A CE    1 
ATOM   2914  N  NZ    . LYS A  1  397  ? -37.609 41.275  85.544  1.00 27.58 ? 395  LYS A NZ    1 
ATOM   2915  N  N     . ILE A  1  398  ? -37.660 41.643  91.468  1.00 21.89 ? 396  ILE A N     1 
ATOM   2916  C  CA    . ILE A  1  398  ? -38.785 40.722  91.497  1.00 22.79 ? 396  ILE A CA    1 
ATOM   2917  C  C     . ILE A  1  398  ? -40.014 41.391  92.106  1.00 20.16 ? 396  ILE A C     1 
ATOM   2918  O  O     . ILE A  1  398  ? -41.153 41.012  91.801  1.00 23.59 ? 396  ILE A O     1 
ATOM   2919  C  CB    . ILE A  1  398  ? -38.372 39.441  92.250  1.00 27.86 ? 396  ILE A CB    1 
ATOM   2920  C  CG1   . ILE A  1  398  ? -39.368 38.322  91.990  1.00 30.22 ? 396  ILE A CG1   1 
ATOM   2921  C  CG2   . ILE A  1  398  ? -38.228 39.725  93.718  1.00 23.19 ? 396  ILE A CG2   1 
ATOM   2922  C  CD1   . ILE A  1  398  ? -38.755 36.942  92.130  1.00 34.56 ? 396  ILE A CD1   1 
ATOM   2923  N  N     . HIS A  1  399  ? -39.813 42.394  92.963  1.00 21.25 ? 397  HIS A N     1 
ATOM   2924  C  CA    . HIS A  1  399  ? -40.944 43.126  93.523  1.00 24.91 ? 397  HIS A CA    1 
ATOM   2925  C  C     . HIS A  1  399  ? -41.668 43.918  92.445  1.00 20.23 ? 397  HIS A C     1 
ATOM   2926  O  O     . HIS A  1  399  ? -42.902 43.926  92.390  1.00 21.50 ? 397  HIS A O     1 
ATOM   2927  C  CB    . HIS A  1  399  ? -40.466 44.056  94.638  1.00 22.62 ? 397  HIS A CB    1 
ATOM   2928  C  CG    . HIS A  1  399  ? -39.958 43.329  95.847  1.00 22.43 ? 397  HIS A CG    1 
ATOM   2929  N  ND1   . HIS A  1  399  ? -39.325 43.968  96.888  1.00 22.48 ? 397  HIS A ND1   1 
ATOM   2930  C  CD2   . HIS A  1  399  ? -39.992 42.015  96.174  1.00 28.49 ? 397  HIS A CD2   1 
ATOM   2931  C  CE1   . HIS A  1  399  ? -38.983 43.077  97.805  1.00 23.86 ? 397  HIS A CE1   1 
ATOM   2932  N  NE2   . HIS A  1  399  ? -39.381 41.885  97.398  1.00 25.77 ? 397  HIS A NE2   1 
ATOM   2933  N  N     . THR A  1  400  ? -40.907 44.586  91.578  1.00 18.93 ? 398  THR A N     1 
ATOM   2934  C  CA    . THR A  1  400  ? -41.506 45.247  90.424  1.00 16.94 ? 398  THR A CA    1 
ATOM   2935  C  C     . THR A  1  400  ? -42.274 44.259  89.552  1.00 19.05 ? 398  THR A C     1 
ATOM   2936  O  O     . THR A  1  400  ? -43.354 44.580  89.044  1.00 19.75 ? 398  THR A O     1 
ATOM   2937  C  CB    . THR A  1  400  ? -40.406 45.954  89.638  1.00 20.67 ? 398  THR A CB    1 
ATOM   2938  O  OG1   . THR A  1  400  ? -39.863 46.991  90.466  1.00 20.57 ? 398  THR A OG1   1 
ATOM   2939  C  CG2   . THR A  1  400  ? -40.941 46.545  88.334  1.00 19.33 ? 398  THR A CG2   1 
ATOM   2940  N  N     . ASP A  1  401  ? -41.749 43.043  89.374  1.00 20.22 ? 399  ASP A N     1 
ATOM   2941  C  CA    . ASP A  1  401  ? -42.463 42.079  88.544  1.00 19.82 ? 399  ASP A CA    1 
ATOM   2942  C  C     . ASP A  1  401  ? -43.800 41.701  89.175  1.00 19.54 ? 399  ASP A C     1 
ATOM   2943  O  O     . ASP A  1  401  ? -44.821 41.647  88.483  1.00 22.19 ? 399  ASP A O     1 
ATOM   2944  C  CB    . ASP A  1  401  ? -41.610 40.830  88.303  1.00 20.39 ? 399  ASP A CB    1 
ATOM   2945  C  CG    . ASP A  1  401  ? -40.417 41.103  87.397  1.00 23.17 ? 399  ASP A CG    1 
ATOM   2946  O  OD1   . ASP A  1  401  ? -40.487 42.055  86.585  1.00 23.83 ? 399  ASP A OD1   1 
ATOM   2947  O  OD2   . ASP A  1  401  ? -39.414 40.373  87.498  1.00 26.82 ? 399  ASP A OD2   1 
ATOM   2948  N  N     . VAL A  1  402  ? -43.816 41.457  90.488  1.00 20.54 ? 400  VAL A N     1 
ATOM   2949  C  CA    . VAL A  1  402  ? -45.073 41.138  91.159  1.00 21.16 ? 400  VAL A CA    1 
ATOM   2950  C  C     . VAL A  1  402  ? -46.013 42.330  91.115  1.00 19.21 ? 400  VAL A C     1 
ATOM   2951  O  O     . VAL A  1  402  ? -47.214 42.179  90.861  1.00 21.68 ? 400  VAL A O     1 
ATOM   2952  C  CB    . VAL A  1  402  ? -44.824 40.687  92.605  1.00 23.87 ? 400  VAL A CB    1 
ATOM   2953  C  CG1   . VAL A  1  402  ? -46.162 40.505  93.350  1.00 21.14 ? 400  VAL A CG1   1 
ATOM   2954  C  CG2   . VAL A  1  402  ? -44.032 39.382  92.618  1.00 25.09 ? 400  VAL A CG2   1 
ATOM   2955  N  N     . SER A  1  403  ? -45.484 43.529  91.368  1.00 22.57 ? 401  SER A N     1 
ATOM   2956  C  CA    . SER A  1  403  ? -46.305 44.727  91.270  1.00 19.99 ? 401  SER A CA    1 
ATOM   2957  C  C     . SER A  1  403  ? -46.954 44.827  89.901  1.00 22.76 ? 401  SER A C     1 
ATOM   2958  O  O     . SER A  1  403  ? -48.152 45.114  89.790  1.00 20.79 ? 401  SER A O     1 
ATOM   2959  C  CB    . SER A  1  403  ? -45.450 45.960  91.545  1.00 20.95 ? 401  SER A CB    1 
ATOM   2960  O  OG    . SER A  1  403  ? -46.206 47.139  91.365  1.00 20.69 ? 401  SER A OG    1 
ATOM   2961  N  N     . TYR A  1  404  ? -46.171 44.586  88.846  1.00 19.74 ? 402  TYR A N     1 
ATOM   2962  C  CA    . TYR A  1  404  ? -46.694 44.664  87.491  1.00 20.83 ? 402  TYR A CA    1 
ATOM   2963  C  C     . TYR A  1  404  ? -47.846 43.688  87.293  1.00 20.78 ? 402  TYR A C     1 
ATOM   2964  O  O     . TYR A  1  404  ? -48.906 44.057  86.778  1.00 20.15 ? 402  TYR A O     1 
ATOM   2965  C  CB    . TYR A  1  404  ? -45.562 44.396  86.504  1.00 19.28 ? 402  TYR A CB    1 
ATOM   2966  C  CG    . TYR A  1  404  ? -45.887 44.737  85.080  1.00 19.06 ? 402  TYR A CG    1 
ATOM   2967  C  CD1   . TYR A  1  404  ? -46.649 43.873  84.298  1.00 19.98 ? 402  TYR A CD1   1 
ATOM   2968  C  CD2   . TYR A  1  404  ? -45.410 45.905  84.503  1.00 18.94 ? 402  TYR A CD2   1 
ATOM   2969  C  CE1   . TYR A  1  404  ? -46.942 44.172  82.988  1.00 21.65 ? 402  TYR A CE1   1 
ATOM   2970  C  CE2   . TYR A  1  404  ? -45.702 46.210  83.178  1.00 17.91 ? 402  TYR A CE2   1 
ATOM   2971  C  CZ    . TYR A  1  404  ? -46.458 45.338  82.433  1.00 19.10 ? 402  TYR A CZ    1 
ATOM   2972  O  OH    . TYR A  1  404  ? -46.754 45.639  81.127  1.00 21.69 ? 402  TYR A OH    1 
ATOM   2973  N  N     . ILE A  1  405  ? -47.660 42.434  87.711  1.00 21.27 ? 403  ILE A N     1 
ATOM   2974  C  CA    . ILE A  1  405  ? -48.701 41.444  87.491  1.00 22.80 ? 403  ILE A CA    1 
ATOM   2975  C  C     . ILE A  1  405  ? -49.936 41.774  88.324  1.00 22.02 ? 403  ILE A C     1 
ATOM   2976  O  O     . ILE A  1  405  ? -51.069 41.648  87.850  1.00 22.15 ? 403  ILE A O     1 
ATOM   2977  C  CB    . ILE A  1  405  ? -48.147 40.038  87.773  1.00 23.32 ? 403  ILE A CB    1 
ATOM   2978  C  CG1   . ILE A  1  405  ? -47.053 39.725  86.746  1.00 24.07 ? 403  ILE A CG1   1 
ATOM   2979  C  CG2   . ILE A  1  405  ? -49.263 39.006  87.663  1.00 23.61 ? 403  ILE A CG2   1 
ATOM   2980  C  CD1   . ILE A  1  405  ? -46.022 38.678  87.177  1.00 29.37 ? 403  ILE A CD1   1 
ATOM   2981  N  N     . ALA A  1  406  ? -49.735 42.255  89.554  1.00 22.45 ? 404  ALA A N     1 
ATOM   2982  C  CA    . ALA A  1  406  ? -50.867 42.643  90.396  1.00 21.86 ? 404  ALA A CA    1 
ATOM   2983  C  C     . ALA A  1  406  ? -51.636 43.800  89.784  1.00 22.96 ? 404  ALA A C     1 
ATOM   2984  O  O     . ALA A  1  406  ? -52.872 43.835  89.829  1.00 24.25 ? 404  ALA A O     1 
ATOM   2985  C  CB    . ALA A  1  406  ? -50.377 43.027  91.790  1.00 24.72 ? 404  ALA A CB    1 
ATOM   2986  N  N     . CYS A  1  407  ? -50.918 44.770  89.223  1.00 21.94 ? 405  CYS A N     1 
ATOM   2987  C  CA    . CYS A  1  407  ? -51.579 45.907  88.602  1.00 20.86 ? 405  CYS A CA    1 
ATOM   2988  C  C     . CYS A  1  407  ? -52.262 45.514  87.300  1.00 23.57 ? 405  CYS A C     1 
ATOM   2989  O  O     . CYS A  1  407  ? -53.290 46.100  86.938  1.00 20.82 ? 405  CYS A O     1 
ATOM   2990  C  CB    . CYS A  1  407  ? -50.560 47.024  88.391  1.00 19.03 ? 405  CYS A CB    1 
ATOM   2991  S  SG    . CYS A  1  407  ? -50.101 47.779  89.977  1.00 24.83 ? 405  CYS A SG    1 
ATOM   2992  N  N     . ALA A  1  408  ? -51.725 44.516  86.593  1.00 21.66 ? 406  ALA A N     1 
ATOM   2993  C  CA    . ALA A  1  408  ? -52.407 44.014  85.410  1.00 19.36 ? 406  ALA A CA    1 
ATOM   2994  C  C     . ALA A  1  408  ? -53.726 43.357  85.782  1.00 19.78 ? 406  ALA A C     1 
ATOM   2995  O  O     . ALA A  1  408  ? -54.715 43.480  85.052  1.00 23.19 ? 406  ALA A O     1 
ATOM   2996  C  CB    . ALA A  1  408  ? -51.507 43.035  84.652  1.00 23.46 ? 406  ALA A CB    1 
ATOM   2997  N  N     . ALA A  1  409  ? -53.760 42.650  86.914  1.00 22.23 ? 407  ALA A N     1 
ATOM   2998  C  CA    . ALA A  1  409  ? -55.018 42.069  87.367  1.00 23.98 ? 407  ALA A CA    1 
ATOM   2999  C  C     . ALA A  1  409  ? -56.055 43.152  87.627  1.00 23.36 ? 407  ALA A C     1 
ATOM   3000  O  O     . ALA A  1  409  ? -57.230 42.993  87.277  1.00 23.07 ? 407  ALA A O     1 
ATOM   3001  C  CB    . ALA A  1  409  ? -54.789 41.224  88.624  1.00 23.44 ? 407  ALA A CB    1 
ATOM   3002  N  N     . LYS A  1  410  ? -55.632 44.266  88.230  1.00 21.08 ? 408  LYS A N     1 
ATOM   3003  C  CA    . LYS A  1  410  ? -56.546 45.377  88.467  1.00 19.75 ? 408  LYS A CA    1 
ATOM   3004  C  C     . LYS A  1  410  ? -57.038 45.963  87.152  1.00 20.67 ? 408  LYS A C     1 
ATOM   3005  O  O     . LYS A  1  410  ? -58.234 46.234  86.981  1.00 22.10 ? 408  LYS A O     1 
ATOM   3006  C  CB    . LYS A  1  410  ? -55.843 46.442  89.316  1.00 21.88 ? 408  LYS A CB    1 
ATOM   3007  C  CG    . LYS A  1  410  ? -56.700 47.654  89.655  1.00 23.54 ? 408  LYS A CG    1 
ATOM   3008  C  CD    . LYS A  1  410  ? -55.893 48.698  90.412  1.00 24.01 ? 408  LYS A CD    1 
ATOM   3009  C  CE    . LYS A  1  410  ? -55.442 48.209  91.780  1.00 25.00 ? 408  LYS A CE    1 
ATOM   3010  N  NZ    . LYS A  1  410  ? -56.624 48.007  92.675  1.00 26.06 ? 408  LYS A NZ    1 
ATOM   3011  N  N     . LEU A  1  411  ? -56.118 46.183  86.208  1.00 19.82 ? 409  LEU A N     1 
ATOM   3012  C  CA    . LEU A  1  411  ? -56.501 46.747  84.919  1.00 19.45 ? 409  LEU A CA    1 
ATOM   3013  C  C     . LEU A  1  411  ? -57.432 45.818  84.146  1.00 19.11 ? 409  LEU A C     1 
ATOM   3014  O  O     . LEU A  1  411  ? -58.396 46.275  83.520  1.00 20.04 ? 409  LEU A O     1 
ATOM   3015  C  CB    . LEU A  1  411  ? -55.252 47.058  84.095  1.00 19.88 ? 409  LEU A CB    1 
ATOM   3016  C  CG    . LEU A  1  411  ? -54.564 48.366  84.486  1.00 18.26 ? 409  LEU A CG    1 
ATOM   3017  C  CD1   . LEU A  1  411  ? -53.139 48.399  83.930  1.00 21.36 ? 409  LEU A CD1   1 
ATOM   3018  C  CD2   . LEU A  1  411  ? -55.340 49.585  84.005  1.00 20.56 ? 409  LEU A CD2   1 
ATOM   3019  N  N     . LEU A  1  412  ? -57.154 44.511  84.163  1.00 19.13 ? 410  LEU A N     1 
ATOM   3020  C  CA    . LEU A  1  412  ? -57.983 43.584  83.403  1.00 19.25 ? 410  LEU A CA    1 
ATOM   3021  C  C     . LEU A  1  412  ? -59.379 43.453  83.979  1.00 22.01 ? 410  LEU A C     1 
ATOM   3022  O  O     . LEU A  1  412  ? -60.283 43.008  83.265  1.00 27.16 ? 410  LEU A O     1 
ATOM   3023  C  CB    . LEU A  1  412  ? -57.313 42.210  83.319  1.00 22.85 ? 410  LEU A CB    1 
ATOM   3024  C  CG    . LEU A  1  412  ? -56.132 42.186  82.336  1.00 21.64 ? 410  LEU A CG    1 
ATOM   3025  C  CD1   . LEU A  1  412  ? -55.352 40.891  82.470  1.00 26.17 ? 410  LEU A CD1   1 
ATOM   3026  C  CD2   . LEU A  1  412  ? -56.637 42.363  80.915  1.00 26.61 ? 410  LEU A CD2   1 
ATOM   3027  N  N     . ALA A  1  413  ? -59.585 43.841  85.238  1.00 22.21 ? 411  ALA A N     1 
ATOM   3028  C  CA    . ALA A  1  413  ? -60.935 43.866  85.787  1.00 22.91 ? 411  ALA A CA    1 
ATOM   3029  C  C     . ALA A  1  413  ? -61.713 45.111  85.393  1.00 24.91 ? 411  ALA A C     1 
ATOM   3030  O  O     . ALA A  1  413  ? -62.902 45.208  85.712  1.00 26.05 ? 411  ALA A O     1 
ATOM   3031  C  CB    . ALA A  1  413  ? -60.891 43.763  87.315  1.00 28.08 ? 411  ALA A CB    1 
ATOM   3032  N  N     . ALA A  1  414  ? -61.082 46.061  84.703  1.00 23.72 ? 412  ALA A N     1 
ATOM   3033  C  CA    . ALA A  1  414  ? -61.718 47.335  84.409  1.00 26.49 ? 412  ALA A CA    1 
ATOM   3034  C  C     . ALA A  1  414  ? -61.614 47.680  82.928  1.00 25.05 ? 412  ALA A C     1 
ATOM   3035  O  O     . ALA A  1  414  ? -61.572 48.855  82.569  1.00 21.53 ? 412  ALA A O     1 
ATOM   3036  C  CB    . ALA A  1  414  ? -61.108 48.449  85.265  1.00 27.12 ? 412  ALA A CB    1 
ATOM   3037  N  N     . THR A  1  415  ? -61.581 46.669  82.051  1.00 23.28 ? 413  THR A N     1 
ATOM   3038  C  CA    . THR A  1  415  ? -61.445 46.944  80.622  1.00 24.72 ? 413  THR A CA    1 
ATOM   3039  C  C     . THR A  1  415  ? -62.677 47.625  80.041  1.00 23.89 ? 413  THR A C     1 
ATOM   3040  O  O     . THR A  1  415  ? -62.599 48.178  78.936  1.00 25.12 ? 413  THR A O     1 
ATOM   3041  C  CB    . THR A  1  415  ? -61.144 45.658  79.840  1.00 25.62 ? 413  THR A CB    1 
ATOM   3042  O  OG1   . THR A  1  415  ? -62.233 44.736  79.980  1.00 26.67 ? 413  THR A OG1   1 
ATOM   3043  C  CG2   . THR A  1  415  ? -59.862 44.996  80.353  1.00 26.98 ? 413  THR A CG2   1 
ATOM   3044  N  N     . ASP A  1  416  ? -63.813 47.614  80.752  1.00 24.04 ? 414  ASP A N     1 
ATOM   3045  C  CA    . ASP A  1  416  ? -64.953 48.386  80.274  1.00 26.13 ? 414  ASP A CA    1 
ATOM   3046  C  C     . ASP A  1  416  ? -64.709 49.886  80.377  1.00 25.04 ? 414  ASP A C     1 
ATOM   3047  O  O     . ASP A  1  416  ? -65.291 50.656  79.608  1.00 30.93 ? 414  ASP A O     1 
ATOM   3048  C  CB    . ASP A  1  416  ? -66.217 48.005  81.048  1.00 27.75 ? 414  ASP A CB    1 
ATOM   3049  C  CG    . ASP A  1  416  ? -66.104 48.308  82.522  1.00 35.09 ? 414  ASP A CG    1 
ATOM   3050  O  OD1   . ASP A  1  416  ? -65.059 47.977  83.115  1.00 34.34 ? 414  ASP A OD1   1 
ATOM   3051  O  OD2   . ASP A  1  416  ? -67.058 48.885  83.091  1.00 46.51 ? 414  ASP A OD2   1 
ATOM   3052  N  N     . VAL A  1  417  ? -63.842 50.327  81.285  1.00 22.25 ? 415  VAL A N     1 
ATOM   3053  C  CA    . VAL A  1  417  ? -63.664 51.754  81.514  1.00 27.97 ? 415  VAL A CA    1 
ATOM   3054  C  C     . VAL A  1  417  ? -62.256 52.252  81.219  1.00 24.25 ? 415  VAL A C     1 
ATOM   3055  O  O     . VAL A  1  417  ? -62.078 53.468  81.074  1.00 22.52 ? 415  VAL A O     1 
ATOM   3056  C  CB    . VAL A  1  417  ? -64.068 52.148  82.947  1.00 28.83 ? 415  VAL A CB    1 
ATOM   3057  C  CG1   . VAL A  1  417  ? -65.531 51.812  83.193  1.00 35.79 ? 415  VAL A CG1   1 
ATOM   3058  C  CG2   . VAL A  1  417  ? -63.183 51.474  83.939  1.00 28.23 ? 415  VAL A CG2   1 
ATOM   3059  N  N     . VAL A  1  418  ? -61.241 51.387  81.142  1.00 21.09 ? 416  VAL A N     1 
ATOM   3060  C  CA    . VAL A  1  418  ? -59.917 51.790  80.679  1.00 18.36 ? 416  VAL A CA    1 
ATOM   3061  C  C     . VAL A  1  418  ? -59.456 50.793  79.628  1.00 18.04 ? 416  VAL A C     1 
ATOM   3062  O  O     . VAL A  1  418  ? -59.973 49.682  79.520  1.00 20.25 ? 416  VAL A O     1 
ATOM   3063  C  CB    . VAL A  1  418  ? -58.865 51.894  81.813  1.00 17.08 ? 416  VAL A CB    1 
ATOM   3064  C  CG1   . VAL A  1  418  ? -59.246 53.006  82.795  1.00 23.15 ? 416  VAL A CG1   1 
ATOM   3065  C  CG2   . VAL A  1  418  ? -58.674 50.558  82.544  1.00 20.71 ? 416  VAL A CG2   1 
ATOM   3066  N  N     . PHE A  1  419  ? -58.453 51.204  78.869  1.00 18.05 ? 417  PHE A N     1 
ATOM   3067  C  CA    . PHE A  1  419  ? -57.827 50.363  77.859  1.00 19.39 ? 417  PHE A CA    1 
ATOM   3068  C  C     . PHE A  1  419  ? -56.426 50.007  78.338  1.00 17.29 ? 417  PHE A C     1 
ATOM   3069  O  O     . PHE A  1  419  ? -55.502 50.826  78.220  1.00 19.71 ? 417  PHE A O     1 
ATOM   3070  C  CB    . PHE A  1  419  ? -57.778 51.096  76.516  1.00 18.20 ? 417  PHE A CB    1 
ATOM   3071  C  CG    . PHE A  1  419  ? -57.071 50.339  75.432  1.00 20.44 ? 417  PHE A CG    1 
ATOM   3072  C  CD1   . PHE A  1  419  ? -57.519 49.089  75.039  1.00 22.35 ? 417  PHE A CD1   1 
ATOM   3073  C  CD2   . PHE A  1  419  ? -55.974 50.894  74.785  1.00 19.49 ? 417  PHE A CD2   1 
ATOM   3074  C  CE1   . PHE A  1  419  ? -56.879 48.391  74.026  1.00 19.28 ? 417  PHE A CE1   1 
ATOM   3075  C  CE2   . PHE A  1  419  ? -55.333 50.201  73.784  1.00 17.61 ? 417  PHE A CE2   1 
ATOM   3076  C  CZ    . PHE A  1  419  ? -55.791 48.958  73.395  1.00 19.48 ? 417  PHE A CZ    1 
ATOM   3077  N  N     . PRO A  1  420  ? -56.217 48.814  78.887  1.00 18.39 ? 418  PRO A N     1 
ATOM   3078  C  CA    . PRO A  1  420  ? -54.887 48.460  79.394  1.00 19.14 ? 418  PRO A CA    1 
ATOM   3079  C  C     . PRO A  1  420  ? -53.913 48.172  78.268  1.00 19.57 ? 418  PRO A C     1 
ATOM   3080  O  O     . PRO A  1  420  ? -54.254 47.549  77.258  1.00 20.06 ? 418  PRO A O     1 
ATOM   3081  C  CB    . PRO A  1  420  ? -55.148 47.202  80.229  1.00 18.39 ? 418  PRO A CB    1 
ATOM   3082  C  CG    . PRO A  1  420  ? -56.626 47.221  80.500  1.00 20.45 ? 418  PRO A CG    1 
ATOM   3083  C  CD    . PRO A  1  420  ? -57.217 47.795  79.244  1.00 20.41 ? 418  PRO A CD    1 
ATOM   3084  N  N     . GLN A  1  421  ? -52.687 48.644  78.457  1.00 17.42 ? 419  GLN A N     1 
ATOM   3085  C  CA    . GLN A  1  421  ? -51.623 48.503  77.473  1.00 19.24 ? 419  GLN A CA    1 
ATOM   3086  C  C     . GLN A  1  421  ? -50.412 47.981  78.223  1.00 18.83 ? 419  GLN A C     1 
ATOM   3087  O  O     . GLN A  1  421  ? -49.810 48.709  79.014  1.00 19.62 ? 419  GLN A O     1 
ATOM   3088  C  CB    . GLN A  1  421  ? -51.320 49.837  76.798  1.00 16.53 ? 419  GLN A CB    1 
ATOM   3089  C  CG    . GLN A  1  421  ? -52.559 50.469  76.144  1.00 17.81 ? 419  GLN A CG    1 
ATOM   3090  C  CD    . GLN A  1  421  ? -52.327 51.928  75.801  1.00 19.55 ? 419  GLN A CD    1 
ATOM   3091  O  OE1   . GLN A  1  421  ? -52.055 52.745  76.686  1.00 20.35 ? 419  GLN A OE1   1 
ATOM   3092  N  NE2   . GLN A  1  421  ? -52.409 52.257  74.518  1.00 20.12 ? 419  GLN A NE2   1 
ATOM   3093  N  N     . PHE A  1  422  ? -50.074 46.724  78.002  1.00 17.22 ? 420  PHE A N     1 
ATOM   3094  C  CA    . PHE A  1  422  ? -49.064 46.058  78.814  1.00 19.33 ? 420  PHE A CA    1 
ATOM   3095  C  C     . PHE A  1  422  ? -47.730 46.129  78.088  1.00 17.57 ? 420  PHE A C     1 
ATOM   3096  O  O     . PHE A  1  422  ? -47.427 45.301  77.225  1.00 19.48 ? 420  PHE A O     1 
ATOM   3097  C  CB    . PHE A  1  422  ? -49.497 44.635  79.113  1.00 19.34 ? 420  PHE A CB    1 
ATOM   3098  C  CG    . PHE A  1  422  ? -50.784 44.577  79.875  1.00 21.55 ? 420  PHE A CG    1 
ATOM   3099  C  CD1   . PHE A  1  422  ? -50.868 45.108  81.149  1.00 21.35 ? 420  PHE A CD1   1 
ATOM   3100  C  CD2   . PHE A  1  422  ? -51.914 44.018  79.302  1.00 20.27 ? 420  PHE A CD2   1 
ATOM   3101  C  CE1   . PHE A  1  422  ? -52.061 45.061  81.851  1.00 20.09 ? 420  PHE A CE1   1 
ATOM   3102  C  CE2   . PHE A  1  422  ? -53.104 43.971  79.995  1.00 21.48 ? 420  PHE A CE2   1 
ATOM   3103  C  CZ    . PHE A  1  422  ? -53.177 44.491  81.267  1.00 21.43 ? 420  PHE A CZ    1 
ATOM   3104  N  N     . ALA A  1  423  ? -46.939 47.129  78.460  1.00 18.18 ? 421  ALA A N     1 
ATOM   3105  C  CA    . ALA A  1  423  ? -45.628 47.367  77.873  1.00 18.69 ? 421  ALA A CA    1 
ATOM   3106  C  C     . ALA A  1  423  ? -44.619 46.502  78.613  1.00 21.62 ? 421  ALA A C     1 
ATOM   3107  O  O     . ALA A  1  423  ? -44.369 46.710  79.805  1.00 24.66 ? 421  ALA A O     1 
ATOM   3108  C  CB    . ALA A  1  423  ? -45.275 48.847  77.971  1.00 18.61 ? 421  ALA A CB    1 
ATOM   3109  N  N     . THR A  1  424  ? -44.040 45.528  77.916  1.00 18.03 ? 422  THR A N     1 
ATOM   3110  C  CA    . THR A  1  424  ? -43.019 44.700  78.546  1.00 19.57 ? 422  THR A CA    1 
ATOM   3111  C  C     . THR A  1  424  ? -42.324 43.877  77.480  1.00 21.52 ? 422  THR A C     1 
ATOM   3112  O  O     . THR A  1  424  ? -42.951 43.457  76.500  1.00 22.15 ? 422  THR A O     1 
ATOM   3113  C  CB    . THR A  1  424  ? -43.604 43.771  79.622  1.00 22.07 ? 422  THR A CB    1 
ATOM   3114  O  OG1   . THR A  1  424  ? -42.532 43.083  80.288  1.00 22.61 ? 422  THR A OG1   1 
ATOM   3115  C  CG2   . THR A  1  424  ? -44.565 42.754  79.022  1.00 24.64 ? 422  THR A CG2   1 
ATOM   3116  N  N     . HIS A  1  425  ? -41.032 43.654  77.682  1.00 20.96 ? 423  HIS A N     1 
ATOM   3117  C  CA    . HIS A  1  425  ? -40.269 42.724  76.866  1.00 19.99 ? 423  HIS A CA    1 
ATOM   3118  C  C     . HIS A  1  425  ? -40.041 41.398  77.559  1.00 21.66 ? 423  HIS A C     1 
ATOM   3119  O  O     . HIS A  1  425  ? -39.363 40.530  77.002  1.00 24.81 ? 423  HIS A O     1 
ATOM   3120  C  CB    . HIS A  1  425  ? -38.927 43.346  76.489  1.00 23.05 ? 423  HIS A CB    1 
ATOM   3121  C  CG    . HIS A  1  425  ? -39.069 44.598  75.697  1.00 21.68 ? 423  HIS A CG    1 
ATOM   3122  N  ND1   . HIS A  1  425  ? -38.325 45.730  75.952  1.00 25.60 ? 423  HIS A ND1   1 
ATOM   3123  C  CD2   . HIS A  1  425  ? -39.893 44.907  74.668  1.00 24.07 ? 423  HIS A CD2   1 
ATOM   3124  C  CE1   . HIS A  1  425  ? -38.684 46.681  75.106  1.00 24.69 ? 423  HIS A CE1   1 
ATOM   3125  N  NE2   . HIS A  1  425  ? -39.632 46.207  74.319  1.00 24.57 ? 423  HIS A NE2   1 
ATOM   3126  N  N     . ASN A  1  426  ? -40.582 41.227  78.755  1.00 21.61 ? 424  ASN A N     1 
ATOM   3127  C  CA    . ASN A  1  426  ? -40.353 40.034  79.567  1.00 22.25 ? 424  ASN A CA    1 
ATOM   3128  C  C     . ASN A  1  426  ? -41.379 38.968  79.187  1.00 28.47 ? 424  ASN A C     1 
ATOM   3129  O  O     . ASN A  1  426  ? -42.575 39.123  79.453  1.00 24.89 ? 424  ASN A O     1 
ATOM   3130  C  CB    . ASN A  1  426  ? -40.443 40.422  81.039  1.00 24.10 ? 424  ASN A CB    1 
ATOM   3131  C  CG    . ASN A  1  426  ? -40.074 39.300  81.972  1.00 23.34 ? 424  ASN A CG    1 
ATOM   3132  O  OD1   . ASN A  1  426  ? -40.478 38.155  81.781  1.00 27.73 ? 424  ASN A OD1   1 
ATOM   3133  N  ND2   . ASN A  1  426  ? -39.314 39.634  83.012  1.00 24.25 ? 424  ASN A ND2   1 
ATOM   3134  N  N     . ALA A  1  427  ? -40.911 37.872  78.580  1.00 21.97 ? 425  ALA A N     1 
ATOM   3135  C  CA    . ALA A  1  427  ? -41.829 36.833  78.123  1.00 22.88 ? 425  ALA A CA    1 
ATOM   3136  C  C     . ALA A  1  427  ? -42.606 36.204  79.274  1.00 23.04 ? 425  ALA A C     1 
ATOM   3137  O  O     . ALA A  1  427  ? -43.720 35.711  79.068  1.00 24.22 ? 425  ALA A O     1 
ATOM   3138  C  CB    . ALA A  1  427  ? -41.060 35.749  77.362  1.00 26.06 ? 425  ALA A CB    1 
ATOM   3139  N  N     . GLN A  1  428  ? -42.027 36.174  80.477  1.00 25.81 ? 426  GLN A N     1 
ATOM   3140  C  CA    . GLN A  1  428  ? -42.742 35.609  81.618  1.00 26.93 ? 426  GLN A CA    1 
ATOM   3141  C  C     . GLN A  1  428  ? -43.890 36.520  82.028  1.00 25.66 ? 426  GLN A C     1 
ATOM   3142  O  O     . GLN A  1  428  ? -45.021 36.056  82.230  1.00 25.63 ? 426  GLN A O     1 
ATOM   3143  C  CB    . GLN A  1  428  ? -41.780 35.381  82.787  1.00 26.16 ? 426  GLN A CB    1 
ATOM   3144  C  CG    . GLN A  1  428  ? -42.327 34.478  83.902  1.00 27.92 ? 426  GLN A CG    1 
ATOM   3145  C  CD    . GLN A  1  428  ? -43.411 35.128  84.761  1.00 32.17 ? 426  GLN A CD    1 
ATOM   3146  O  OE1   . GLN A  1  428  ? -43.368 36.328  85.042  1.00 32.69 ? 426  GLN A OE1   1 
ATOM   3147  N  NE2   . GLN A  1  428  ? -44.389 34.329  85.181  1.00 27.63 ? 426  GLN A NE2   1 
ATOM   3148  N  N     . THR A  1  429  ? -43.606 37.822  82.159  1.00 25.46 ? 427  THR A N     1 
ATOM   3149  C  CA    . THR A  1  429  ? -44.650 38.807  82.424  1.00 23.56 ? 427  THR A CA    1 
ATOM   3150  C  C     . THR A  1  429  ? -45.751 38.727  81.375  1.00 26.34 ? 427  THR A C     1 
ATOM   3151  O  O     . THR A  1  429  ? -46.943 38.685  81.702  1.00 24.61 ? 427  THR A O     1 
ATOM   3152  C  CB    . THR A  1  429  ? -44.048 40.213  82.442  1.00 25.90 ? 427  THR A CB    1 
ATOM   3153  O  OG1   . THR A  1  429  ? -42.881 40.235  83.270  1.00 25.13 ? 427  THR A OG1   1 
ATOM   3154  C  CG2   . THR A  1  429  ? -45.055 41.193  83.003  1.00 24.22 ? 427  THR A CG2   1 
ATOM   3155  N  N     . LEU A  1  430  ? -45.358 38.709  80.100  1.00 21.92 ? 428  LEU A N     1 
ATOM   3156  C  CA    . LEU A  1  430  ? -46.317 38.634  79.003  1.00 23.49 ? 428  LEU A CA    1 
ATOM   3157  C  C     . LEU A  1  430  ? -47.220 37.418  79.140  1.00 27.80 ? 428  LEU A C     1 
ATOM   3158  O  O     . LEU A  1  430  ? -48.451 37.528  79.065  1.00 25.05 ? 428  LEU A O     1 
ATOM   3159  C  CB    . LEU A  1  430  ? -45.557 38.597  77.673  1.00 22.16 ? 428  LEU A CB    1 
ATOM   3160  C  CG    . LEU A  1  430  ? -46.261 38.807  76.325  1.00 28.22 ? 428  LEU A CG    1 
ATOM   3161  C  CD1   . LEU A  1  430  ? -45.176 38.931  75.271  1.00 30.32 ? 428  LEU A CD1   1 
ATOM   3162  C  CD2   . LEU A  1  430  ? -47.198 37.670  75.955  1.00 29.00 ? 428  LEU A CD2   1 
ATOM   3163  N  N     . ALA A  1  431  ? -46.617 36.240  79.303  1.00 25.20 ? 429  ALA A N     1 
ATOM   3164  C  CA    . ALA A  1  431  ? -47.392 35.010  79.372  1.00 26.84 ? 429  ALA A CA    1 
ATOM   3165  C  C     . ALA A  1  431  ? -48.360 35.029  80.547  1.00 24.51 ? 429  ALA A C     1 
ATOM   3166  O  O     . ALA A  1  431  ? -49.507 34.584  80.421  1.00 25.86 ? 429  ALA A O     1 
ATOM   3167  C  CB    . ALA A  1  431  ? -46.450 33.814  79.481  1.00 25.88 ? 429  ALA A CB    1 
ATOM   3168  N  N     . ALA A  1  432  ? -47.912 35.540  81.697  1.00 24.37 ? 430  ALA A N     1 
ATOM   3169  C  CA    . ALA A  1  432  ? -48.782 35.608  82.867  1.00 26.25 ? 430  ALA A CA    1 
ATOM   3170  C  C     . ALA A  1  432  ? -50.026 36.434  82.578  1.00 24.07 ? 430  ALA A C     1 
ATOM   3171  O  O     . ALA A  1  432  ? -51.142 36.050  82.953  1.00 26.26 ? 430  ALA A O     1 
ATOM   3172  C  CB    . ALA A  1  432  ? -48.018 36.193  84.056  1.00 25.52 ? 430  ALA A CB    1 
ATOM   3173  N  N     . ILE A  1  433  ? -49.859 37.556  81.885  1.00 26.05 ? 431  ILE A N     1 
ATOM   3174  C  CA    . ILE A  1  433  ? -50.987 38.430  81.606  1.00 25.45 ? 431  ILE A CA    1 
ATOM   3175  C  C     . ILE A  1  433  ? -51.840 37.870  80.484  1.00 24.68 ? 431  ILE A C     1 
ATOM   3176  O  O     . ILE A  1  433  ? -53.068 37.983  80.509  1.00 25.50 ? 431  ILE A O     1 
ATOM   3177  C  CB    . ILE A  1  433  ? -50.464 39.837  81.286  1.00 25.20 ? 431  ILE A CB    1 
ATOM   3178  C  CG1   . ILE A  1  433  ? -49.804 40.415  82.531  1.00 28.23 ? 431  ILE A CG1   1 
ATOM   3179  C  CG2   . ILE A  1  433  ? -51.586 40.720  80.777  1.00 26.64 ? 431  ILE A CG2   1 
ATOM   3180  C  CD1   . ILE A  1  433  ? -49.123 41.692  82.275  1.00 26.78 ? 431  ILE A CD1   1 
ATOM   3181  N  N     . TYR A  1  434  ? -51.203 37.265  79.483  1.00 23.96 ? 432  TYR A N     1 
ATOM   3182  C  CA    . TYR A  1  434  ? -51.947 36.625  78.404  1.00 26.49 ? 432  TYR A CA    1 
ATOM   3183  C  C     . TYR A  1  434  ? -52.944 35.608  78.950  1.00 29.15 ? 432  TYR A C     1 
ATOM   3184  O  O     . TYR A  1  434  ? -54.114 35.583  78.548  1.00 28.47 ? 432  TYR A O     1 
ATOM   3185  C  CB    . TYR A  1  434  ? -50.962 35.968  77.440  1.00 26.52 ? 432  TYR A CB    1 
ATOM   3186  C  CG    . TYR A  1  434  ? -51.593 35.060  76.425  1.00 26.78 ? 432  TYR A CG    1 
ATOM   3187  C  CD1   . TYR A  1  434  ? -52.388 35.566  75.411  1.00 30.54 ? 432  TYR A CD1   1 
ATOM   3188  C  CD2   . TYR A  1  434  ? -51.381 33.689  76.475  1.00 29.88 ? 432  TYR A CD2   1 
ATOM   3189  C  CE1   . TYR A  1  434  ? -52.961 34.735  74.474  1.00 28.52 ? 432  TYR A CE1   1 
ATOM   3190  C  CE2   . TYR A  1  434  ? -51.948 32.847  75.545  1.00 30.14 ? 432  TYR A CE2   1 
ATOM   3191  C  CZ    . TYR A  1  434  ? -52.736 33.369  74.547  1.00 35.73 ? 432  TYR A CZ    1 
ATOM   3192  O  OH    . TYR A  1  434  ? -53.300 32.519  73.623  1.00 40.85 ? 432  TYR A OH    1 
ATOM   3193  N  N     . HIS A  1  435  ? -52.503 34.769  79.882  1.00 26.25 ? 433  HIS A N     1 
ATOM   3194  C  CA    . HIS A  1  435  ? -53.422 33.792  80.454  1.00 28.39 ? 433  HIS A CA    1 
ATOM   3195  C  C     . HIS A  1  435  ? -54.353 34.420  81.480  1.00 27.42 ? 433  HIS A C     1 
ATOM   3196  O  O     . HIS A  1  435  ? -55.515 34.008  81.590  1.00 28.95 ? 433  HIS A O     1 
ATOM   3197  C  CB    . HIS A  1  435  ? -52.634 32.634  81.055  1.00 29.42 ? 433  HIS A CB    1 
ATOM   3198  C  CG    . HIS A  1  435  ? -51.985 31.773  80.018  1.00 33.58 ? 433  HIS A CG    1 
ATOM   3199  N  ND1   . HIS A  1  435  ? -52.660 30.765  79.368  1.00 36.43 ? 433  HIS A ND1   1 
ATOM   3200  C  CD2   . HIS A  1  435  ? -50.748 31.811  79.471  1.00 28.30 ? 433  HIS A CD2   1 
ATOM   3201  C  CE1   . HIS A  1  435  ? -51.856 30.196  78.488  1.00 33.29 ? 433  HIS A CE1   1 
ATOM   3202  N  NE2   . HIS A  1  435  ? -50.690 30.815  78.528  1.00 30.25 ? 433  HIS A NE2   1 
ATOM   3203  N  N     . MET A  1  436  ? -53.877 35.423  82.218  1.00 28.67 ? 434  MET A N     1 
ATOM   3204  C  CA    . MET A  1  436  ? -54.762 36.138  83.130  1.00 26.21 ? 434  MET A CA    1 
ATOM   3205  C  C     . MET A  1  436  ? -55.940 36.753  82.388  1.00 28.10 ? 434  MET A C     1 
ATOM   3206  O  O     . MET A  1  436  ? -57.064 36.764  82.899  1.00 32.56 ? 434  MET A O     1 
ATOM   3207  C  CB    . MET A  1  436  ? -53.981 37.215  83.873  1.00 26.74 ? 434  MET A CB    1 
ATOM   3208  C  CG    . MET A  1  436  ? -54.823 37.977  84.857  1.00 27.90 ? 434  MET A CG    1 
ATOM   3209  S  SD    . MET A  1  436  ? -53.895 39.348  85.540  1.00 29.51 ? 434  MET A SD    1 
ATOM   3210  C  CE    . MET A  1  436  ? -52.725 38.505  86.601  1.00 30.46 ? 434  MET A CE    1 
ATOM   3211  N  N     . ALA A  1  437  ? -55.704 37.265  81.178  1.00 25.41 ? 435  ALA A N     1 
ATOM   3212  C  CA    . ALA A  1  437  ? -56.752 37.948  80.431  1.00 26.19 ? 435  ALA A CA    1 
ATOM   3213  C  C     . ALA A  1  437  ? -57.798 36.986  79.895  1.00 32.58 ? 435  ALA A C     1 
ATOM   3214  O  O     . ALA A  1  437  ? -58.935 37.399  79.645  1.00 31.22 ? 435  ALA A O     1 
ATOM   3215  C  CB    . ALA A  1  437  ? -56.138 38.740  79.278  1.00 26.81 ? 435  ALA A CB    1 
ATOM   3216  N  N     . GLY A  1  438  ? -57.436 35.722  79.711  1.00 34.28 ? 436  GLY A N     1 
ATOM   3217  C  CA    . GLY A  1  438  ? -58.391 34.711  79.316  1.00 36.81 ? 436  GLY A CA    1 
ATOM   3218  C  C     . GLY A  1  438  ? -58.621 34.678  77.823  1.00 34.57 ? 436  GLY A C     1 
ATOM   3219  O  O     . GLY A  1  438  ? -58.026 35.421  77.037  1.00 33.31 ? 436  GLY A O     1 
ATOM   3220  N  N     . LYS A  1  439  ? -59.559 33.808  77.435  1.00 42.82 ? 437  LYS A N     1 
ATOM   3221  C  CA    . LYS A  1  439  ? -59.737 33.450  76.034  1.00 44.30 ? 437  LYS A CA    1 
ATOM   3222  C  C     . LYS A  1  439  ? -60.570 34.467  75.267  1.00 41.46 ? 437  LYS A C     1 
ATOM   3223  O  O     . LYS A  1  439  ? -60.399 34.603  74.051  1.00 52.09 ? 437  LYS A O     1 
ATOM   3224  C  CB    . LYS A  1  439  ? -60.386 32.068  75.925  1.00 51.64 ? 437  LYS A CB    1 
ATOM   3225  N  N     . ASP A  1  440  ? -61.473 35.175  75.939  1.00 41.04 ? 438  ASP A N     1 
ATOM   3226  C  CA    . ASP A  1  440  ? -62.299 36.165  75.262  1.00 42.53 ? 438  ASP A CA    1 
ATOM   3227  C  C     . ASP A  1  440  ? -61.456 37.388  74.941  1.00 41.89 ? 438  ASP A C     1 
ATOM   3228  O  O     . ASP A  1  440  ? -60.921 38.034  75.848  1.00 43.63 ? 438  ASP A O     1 
ATOM   3229  C  CB    . ASP A  1  440  ? -63.492 36.555  76.130  1.00 48.85 ? 438  ASP A CB    1 
ATOM   3230  C  CG    . ASP A  1  440  ? -64.539 35.459  76.211  1.00 54.59 ? 438  ASP A CG    1 
ATOM   3231  O  OD1   . ASP A  1  440  ? -64.366 34.417  75.543  1.00 54.47 ? 438  ASP A OD1   1 
ATOM   3232  O  OD2   . ASP A  1  440  ? -65.534 35.644  76.943  1.00 57.22 ? 438  ASP A OD2   1 
ATOM   3233  N  N     . PHE A  1  441  ? -61.328 37.706  73.656  1.00 36.52 ? 439  PHE A N     1 
ATOM   3234  C  CA    . PHE A  1  441  ? -60.573 38.882  73.263  1.00 35.40 ? 439  PHE A CA    1 
ATOM   3235  C  C     . PHE A  1  441  ? -61.229 39.550  72.069  1.00 37.51 ? 439  PHE A C     1 
ATOM   3236  O  O     . PHE A  1  441  ? -61.829 38.895  71.216  1.00 32.70 ? 439  PHE A O     1 
ATOM   3237  C  CB    . PHE A  1  441  ? -59.113 38.564  72.910  1.00 30.27 ? 439  PHE A CB    1 
ATOM   3238  C  CG    . PHE A  1  441  ? -58.299 39.796  72.618  1.00 31.45 ? 439  PHE A CG    1 
ATOM   3239  C  CD1   . PHE A  1  441  ? -57.813 40.575  73.652  1.00 30.06 ? 439  PHE A CD1   1 
ATOM   3240  C  CD2   . PHE A  1  441  ? -58.063 40.200  71.317  1.00 31.21 ? 439  PHE A CD2   1 
ATOM   3241  C  CE1   . PHE A  1  441  ? -57.088 41.722  73.393  1.00 23.18 ? 439  PHE A CE1   1 
ATOM   3242  C  CE2   . PHE A  1  441  ? -57.340 41.350  71.057  1.00 28.93 ? 439  PHE A CE2   1 
ATOM   3243  C  CZ    . PHE A  1  441  ? -56.857 42.107  72.102  1.00 25.16 ? 439  PHE A CZ    1 
ATOM   3244  N  N     . HIS A  1  442  ? -61.095 40.871  72.022  1.00 32.23 ? 440  HIS A N     1 
ATOM   3245  C  CA    . HIS A  1  442  ? -61.432 41.656  70.848  1.00 31.87 ? 440  HIS A CA    1 
ATOM   3246  C  C     . HIS A  1  442  ? -60.468 42.825  70.798  1.00 33.64 ? 440  HIS A C     1 
ATOM   3247  O  O     . HIS A  1  442  ? -60.016 43.308  71.841  1.00 27.89 ? 440  HIS A O     1 
ATOM   3248  C  CB    . HIS A  1  442  ? -62.875 42.160  70.886  1.00 31.37 ? 440  HIS A CB    1 
ATOM   3249  C  CG    . HIS A  1  442  ? -63.156 43.117  72.001  1.00 29.82 ? 440  HIS A CG    1 
ATOM   3250  N  ND1   . HIS A  1  442  ? -63.590 42.705  73.244  1.00 30.62 ? 440  HIS A ND1   1 
ATOM   3251  C  CD2   . HIS A  1  442  ? -63.083 44.469  72.056  1.00 30.79 ? 440  HIS A CD2   1 
ATOM   3252  C  CE1   . HIS A  1  442  ? -63.762 43.762  74.019  1.00 29.97 ? 440  HIS A CE1   1 
ATOM   3253  N  NE2   . HIS A  1  442  ? -63.464 44.844  73.321  1.00 32.23 ? 440  HIS A NE2   1 
ATOM   3254  N  N     . VAL A  1  443  ? -60.141 43.269  69.582  1.00 31.57 ? 441  VAL A N     1 
ATOM   3255  C  CA    . VAL A  1  443  ? -59.299 44.451  69.455  1.00 32.26 ? 441  VAL A CA    1 
ATOM   3256  C  C     . VAL A  1  443  ? -59.997 45.616  70.138  1.00 29.79 ? 441  VAL A C     1 
ATOM   3257  O  O     . VAL A  1  443  ? -61.186 45.874  69.910  1.00 28.96 ? 441  VAL A O     1 
ATOM   3258  C  CB    . VAL A  1  443  ? -58.986 44.750  67.982  1.00 34.33 ? 441  VAL A CB    1 
ATOM   3259  C  CG1   . VAL A  1  443  ? -58.456 46.163  67.839  1.00 30.71 ? 441  VAL A CG1   1 
ATOM   3260  C  CG2   . VAL A  1  443  ? -57.952 43.763  67.460  1.00 38.05 ? 441  VAL A CG2   1 
ATOM   3261  N  N     . GLY A  1  444  ? -59.267 46.309  71.003  1.00 24.54 ? 442  GLY A N     1 
ATOM   3262  C  CA    . GLY A  1  444  ? -59.828 47.336  71.853  1.00 22.22 ? 442  GLY A CA    1 
ATOM   3263  C  C     . GLY A  1  444  ? -59.984 46.921  73.297  1.00 22.75 ? 442  GLY A C     1 
ATOM   3264  O  O     . GLY A  1  444  ? -60.174 47.788  74.157  1.00 23.86 ? 442  GLY A O     1 
ATOM   3265  N  N     . LYS A  1  445  ? -59.904 45.629  73.598  1.00 22.92 ? 443  LYS A N     1 
ATOM   3266  C  CA    . LYS A  1  445  ? -60.038 45.209  74.986  1.00 22.24 ? 443  LYS A CA    1 
ATOM   3267  C  C     . LYS A  1  445  ? -58.791 45.558  75.779  1.00 21.24 ? 443  LYS A C     1 
ATOM   3268  O  O     . LYS A  1  445  ? -58.867 46.215  76.823  1.00 22.78 ? 443  LYS A O     1 
ATOM   3269  C  CB    . LYS A  1  445  ? -60.311 43.715  75.069  1.00 25.99 ? 443  LYS A CB    1 
ATOM   3270  C  CG    . LYS A  1  445  ? -60.607 43.280  76.486  1.00 27.57 ? 443  LYS A CG    1 
ATOM   3271  C  CD    . LYS A  1  445  ? -61.026 41.839  76.555  1.00 32.30 ? 443  LYS A CD    1 
ATOM   3272  C  CE    . LYS A  1  445  ? -61.457 41.485  77.970  1.00 39.84 ? 443  LYS A CE    1 
ATOM   3273  N  NZ    . LYS A  1  445  ? -61.993 40.094  78.050  1.00 46.65 ? 443  LYS A NZ    1 
ATOM   3274  N  N     . TYR A  1  446  ? -57.634 45.117  75.294  1.00 21.13 ? 444  TYR A N     1 
ATOM   3275  C  CA    . TYR A  1  446  ? -56.333 45.513  75.819  1.00 21.38 ? 444  TYR A CA    1 
ATOM   3276  C  C     . TYR A  1  446  ? -55.319 45.279  74.709  1.00 20.84 ? 444  TYR A C     1 
ATOM   3277  O  O     . TYR A  1  446  ? -55.638 44.710  73.663  1.00 20.74 ? 444  TYR A O     1 
ATOM   3278  C  CB    . TYR A  1  446  ? -55.964 44.727  77.087  1.00 18.96 ? 444  TYR A CB    1 
ATOM   3279  C  CG    . TYR A  1  446  ? -55.650 43.264  76.849  1.00 24.23 ? 444  TYR A CG    1 
ATOM   3280  C  CD1   . TYR A  1  446  ? -54.361 42.851  76.568  1.00 25.14 ? 444  TYR A CD1   1 
ATOM   3281  C  CD2   . TYR A  1  446  ? -56.652 42.303  76.910  1.00 29.93 ? 444  TYR A CD2   1 
ATOM   3282  C  CE1   . TYR A  1  446  ? -54.074 41.516  76.346  1.00 33.16 ? 444  TYR A CE1   1 
ATOM   3283  C  CE2   . TYR A  1  446  ? -56.372 40.976  76.695  1.00 28.53 ? 444  TYR A CE2   1 
ATOM   3284  C  CZ    . TYR A  1  446  ? -55.087 40.593  76.407  1.00 30.71 ? 444  TYR A CZ    1 
ATOM   3285  O  OH    . TYR A  1  446  ? -54.820 39.260  76.194  1.00 46.36 ? 444  TYR A OH    1 
ATOM   3286  N  N     . GLU A  1  447  ? -54.080 45.704  74.946  1.00 19.16 ? 445  GLU A N     1 
ATOM   3287  C  CA    . GLU A  1  447  ? -53.017 45.388  74.001  1.00 21.17 ? 445  GLU A CA    1 
ATOM   3288  C  C     . GLU A  1  447  ? -51.724 45.220  74.772  1.00 20.49 ? 445  GLU A C     1 
ATOM   3289  O  O     . GLU A  1  447  ? -51.624 45.579  75.943  1.00 20.90 ? 445  GLU A O     1 
ATOM   3290  C  CB    . GLU A  1  447  ? -52.855 46.474  72.928  1.00 18.03 ? 445  GLU A CB    1 
ATOM   3291  C  CG    . GLU A  1  447  ? -52.378 47.794  73.512  1.00 19.56 ? 445  GLU A CG    1 
ATOM   3292  C  CD    . GLU A  1  447  ? -52.296 48.914  72.504  1.00 20.91 ? 445  GLU A CD    1 
ATOM   3293  O  OE1   . GLU A  1  447  ? -52.851 48.777  71.393  1.00 22.00 ? 445  GLU A OE1   1 
ATOM   3294  O  OE2   . GLU A  1  447  ? -51.675 49.950  72.836  1.00 19.84 ? 445  GLU A OE2   1 
ATOM   3295  N  N     . PHE A  1  448  ? -50.730 44.665  74.099  1.00 20.77 ? 446  PHE A N     1 
ATOM   3296  C  CA    . PHE A  1  448  ? -49.365 44.701  74.587  1.00 20.43 ? 446  PHE A CA    1 
ATOM   3297  C  C     . PHE A  1  448  ? -48.633 45.858  73.922  1.00 17.52 ? 446  PHE A C     1 
ATOM   3298  O  O     . PHE A  1  448  ? -49.124 46.460  72.959  1.00 20.65 ? 446  PHE A O     1 
ATOM   3299  C  CB    . PHE A  1  448  ? -48.658 43.378  74.302  1.00 21.28 ? 446  PHE A CB    1 
ATOM   3300  C  CG    . PHE A  1  448  ? -49.220 42.233  75.061  1.00 20.99 ? 446  PHE A CG    1 
ATOM   3301  C  CD1   . PHE A  1  448  ? -48.909 42.059  76.400  1.00 22.80 ? 446  PHE A CD1   1 
ATOM   3302  C  CD2   . PHE A  1  448  ? -50.075 41.342  74.445  1.00 22.22 ? 446  PHE A CD2   1 
ATOM   3303  C  CE1   . PHE A  1  448  ? -49.438 40.999  77.118  1.00 26.18 ? 446  PHE A CE1   1 
ATOM   3304  C  CE2   . PHE A  1  448  ? -50.610 40.276  75.148  1.00 25.44 ? 446  PHE A CE2   1 
ATOM   3305  C  CZ    . PHE A  1  448  ? -50.289 40.105  76.488  1.00 25.44 ? 446  PHE A CZ    1 
ATOM   3306  N  N     . GLN A  1  449  ? -47.460 46.192  74.462  1.00 19.01 ? 447  GLN A N     1 
ATOM   3307  C  CA    . GLN A  1  449  ? -46.610 47.200  73.841  1.00 18.60 ? 447  GLN A CA    1 
ATOM   3308  C  C     . GLN A  1  449  ? -45.157 46.796  73.981  1.00 22.09 ? 447  GLN A C     1 
ATOM   3309  O  O     . GLN A  1  449  ? -44.774 46.071  74.902  1.00 20.56 ? 447  GLN A O     1 
ATOM   3310  C  CB    . GLN A  1  449  ? -46.795 48.596  74.451  1.00 18.56 ? 447  GLN A CB    1 
ATOM   3311  C  CG    . GLN A  1  449  ? -48.190 49.130  74.296  1.00 18.39 ? 447  GLN A CG    1 
ATOM   3312  C  CD    . GLN A  1  449  ? -48.273 50.614  74.534  1.00 19.02 ? 447  GLN A CD    1 
ATOM   3313  O  OE1   . GLN A  1  449  ? -47.336 51.223  75.050  1.00 22.44 ? 447  GLN A OE1   1 
ATOM   3314  N  NE2   . GLN A  1  449  ? -49.389 51.213  74.141  1.00 19.30 ? 447  GLN A NE2   1 
ATOM   3315  N  N     . CYS A  1  450  ? -44.344 47.288  73.054  1.00 19.74 ? 448  CYS A N     1 
ATOM   3316  C  CA    . CYS A  1  450  ? -42.924 46.989  73.076  1.00 20.19 ? 448  CYS A CA    1 
ATOM   3317  C  C     . CYS A  1  450  ? -42.180 48.156  72.457  1.00 21.74 ? 448  CYS A C     1 
ATOM   3318  O  O     . CYS A  1  450  ? -42.771 49.049  71.844  1.00 21.11 ? 448  CYS A O     1 
ATOM   3319  C  CB    . CYS A  1  450  ? -42.599 45.693  72.330  1.00 21.56 ? 448  CYS A CB    1 
ATOM   3320  S  SG    . CYS A  1  450  ? -42.737 45.801  70.521  1.00 23.94 ? 448  CYS A SG    1 
ATOM   3321  N  N     . LEU A  1  451  ? -40.865 48.129  72.616  1.00 19.53 ? 449  LEU A N     1 
ATOM   3322  C  CA    . LEU A  1  451  ? -40.010 49.154  72.054  1.00 20.31 ? 449  LEU A CA    1 
ATOM   3323  C  C     . LEU A  1  451  ? -39.550 48.739  70.666  1.00 20.22 ? 449  LEU A C     1 
ATOM   3324  O  O     . LEU A  1  451  ? -39.196 47.581  70.432  1.00 22.64 ? 449  LEU A O     1 
ATOM   3325  C  CB    . LEU A  1  451  ? -38.807 49.395  72.967  1.00 21.34 ? 449  LEU A CB    1 
ATOM   3326  C  CG    . LEU A  1  451  ? -37.759 50.404  72.508  1.00 28.87 ? 449  LEU A CG    1 
ATOM   3327  C  CD1   . LEU A  1  451  ? -38.336 51.829  72.418  1.00 25.88 ? 449  LEU A CD1   1 
ATOM   3328  C  CD2   . LEU A  1  451  ? -36.592 50.333  73.481  1.00 28.58 ? 449  LEU A CD2   1 
ATOM   3329  N  N     . HIS A  1  452  ? -39.577 49.695  69.744  1.00 20.14 ? 450  HIS A N     1 
ATOM   3330  C  CA    . HIS A  1  452  ? -39.002 49.490  68.424  1.00 21.83 ? 450  HIS A CA    1 
ATOM   3331  C  C     . HIS A  1  452  ? -37.583 48.946  68.504  1.00 21.35 ? 450  HIS A C     1 
ATOM   3332  O  O     . HIS A  1  452  ? -36.772 49.397  69.316  1.00 24.96 ? 450  HIS A O     1 
ATOM   3333  C  CB    . HIS A  1  452  ? -38.981 50.812  67.664  1.00 21.48 ? 450  HIS A CB    1 
ATOM   3334  C  CG    . HIS A  1  452  ? -38.220 50.742  66.381  1.00 20.79 ? 450  HIS A CG    1 
ATOM   3335  N  ND1   . HIS A  1  452  ? -38.790 50.310  65.201  1.00 24.19 ? 450  HIS A ND1   1 
ATOM   3336  C  CD2   . HIS A  1  452  ? -36.929 51.031  66.097  1.00 23.83 ? 450  HIS A CD2   1 
ATOM   3337  C  CE1   . HIS A  1  452  ? -37.883 50.351  64.241  1.00 25.85 ? 450  HIS A CE1   1 
ATOM   3338  N  NE2   . HIS A  1  452  ? -36.746 50.782  64.759  1.00 25.54 ? 450  HIS A NE2   1 
ATOM   3339  N  N     . GLY A  1  453  ? -37.279 48.001  67.617  1.00 28.72 ? 451  GLY A N     1 
ATOM   3340  C  CA    . GLY A  1  453  ? -35.919 47.499  67.513  1.00 30.58 ? 451  GLY A CA    1 
ATOM   3341  C  C     . GLY A  1  453  ? -35.439 46.768  68.741  1.00 38.34 ? 451  GLY A C     1 
ATOM   3342  O  O     . GLY A  1  453  ? -34.228 46.634  68.949  1.00 40.15 ? 451  GLY A O     1 
ATOM   3343  N  N     . MET A  1  454  ? -36.364 46.299  69.570  1.00 28.63 ? 452  MET A N     1 
ATOM   3344  C  CA    . MET A  1  454  ? -36.036 45.584  70.793  1.00 26.15 ? 452  MET A CA    1 
ATOM   3345  C  C     . MET A  1  454  ? -37.087 44.511  71.045  1.00 31.35 ? 452  MET A C     1 
ATOM   3346  O  O     . MET A  1  454  ? -36.757 43.340  71.257  1.00 28.57 ? 452  MET A O     1 
ATOM   3347  C  CB    . MET A  1  454  ? -35.948 46.559  71.967  1.00 30.20 ? 452  MET A CB    1 
ATOM   3348  C  CG    . MET A  1  454  ? -35.853 45.891  73.319  1.00 29.85 ? 452  MET A CG    1 
ATOM   3349  S  SD    . MET A  1  454  ? -34.362 44.906  73.446  1.00 41.05 ? 452  MET A SD    1 
ATOM   3350  C  CE    . MET A  1  454  ? -33.121 46.196  73.304  1.00 38.68 ? 452  MET A CE    1 
ATOM   3351  N  N     . GLY A  1  455  ? -38.359 44.887  70.976  1.00 26.75 ? 453  GLY A N     1 
ATOM   3352  C  CA    . GLY A  1  455  ? -39.418 43.944  71.274  1.00 25.08 ? 453  GLY A CA    1 
ATOM   3353  C  C     . GLY A  1  455  ? -39.995 43.162  70.111  1.00 29.84 ? 453  GLY A C     1 
ATOM   3354  O  O     . GLY A  1  455  ? -40.792 42.251  70.342  1.00 27.33 ? 453  GLY A O     1 
ATOM   3355  N  N     . GLU A  1  456  ? -39.640 43.482  68.865  1.00 28.19 ? 454  GLU A N     1 
ATOM   3356  C  CA    . GLU A  1  456  ? -40.249 42.774  67.741  1.00 28.62 ? 454  GLU A CA    1 
ATOM   3357  C  C     . GLU A  1  456  ? -39.954 41.282  67.719  1.00 31.03 ? 454  GLU A C     1 
ATOM   3358  O  O     . GLU A  1  456  ? -40.856 40.519  67.333  1.00 30.70 ? 454  GLU A O     1 
ATOM   3359  C  CB    . GLU A  1  456  ? -39.823 43.394  66.405  1.00 33.59 ? 454  GLU A CB    1 
ATOM   3360  C  CG    . GLU A  1  456  ? -40.383 44.770  66.163  1.00 41.11 ? 454  GLU A CG    1 
ATOM   3361  C  CD    . GLU A  1  456  ? -39.393 45.836  66.526  1.00 34.41 ? 454  GLU A CD    1 
ATOM   3362  O  OE1   . GLU A  1  456  ? -38.476 45.535  67.325  1.00 35.67 ? 454  GLU A OE1   1 
ATOM   3363  O  OE2   . GLU A  1  456  ? -39.518 46.961  66.001  1.00 35.37 ? 454  GLU A OE2   1 
ATOM   3364  N  N     . PRO A  1  457  ? -38.755 40.799  68.063  1.00 35.02 ? 455  PRO A N     1 
ATOM   3365  C  CA    . PRO A  1  457  ? -38.575 39.340  68.093  1.00 35.21 ? 455  PRO A CA    1 
ATOM   3366  C  C     . PRO A  1  457  ? -39.571 38.650  69.003  1.00 31.38 ? 455  PRO A C     1 
ATOM   3367  O  O     . PRO A  1  457  ? -40.149 37.621  68.627  1.00 32.88 ? 455  PRO A O     1 
ATOM   3368  C  CB    . PRO A  1  457  ? -37.130 39.178  68.585  1.00 30.00 ? 455  PRO A CB    1 
ATOM   3369  C  CG    . PRO A  1  457  ? -36.454 40.397  68.131  1.00 34.12 ? 455  PRO A CG    1 
ATOM   3370  C  CD    . PRO A  1  457  ? -37.478 41.495  68.314  1.00 32.57 ? 455  PRO A CD    1 
ATOM   3371  N  N     . LEU A  1  458  ? -39.807 39.207  70.189  1.00 31.80 ? 456  LEU A N     1 
ATOM   3372  C  CA    . LEU A  1  458  ? -40.778 38.601  71.091  1.00 25.49 ? 456  LEU A CA    1 
ATOM   3373  C  C     . LEU A  1  458  ? -42.185 38.714  70.524  1.00 26.36 ? 456  LEU A C     1 
ATOM   3374  O  O     . LEU A  1  458  ? -42.920 37.728  70.458  1.00 26.65 ? 456  LEU A O     1 
ATOM   3375  C  CB    . LEU A  1  458  ? -40.699 39.259  72.466  1.00 27.76 ? 456  LEU A CB    1 
ATOM   3376  C  CG    . LEU A  1  458  ? -41.782 38.823  73.458  1.00 25.82 ? 456  LEU A CG    1 
ATOM   3377  C  CD1   . LEU A  1  458  ? -41.775 37.299  73.631  1.00 25.80 ? 456  LEU A CD1   1 
ATOM   3378  C  CD2   . LEU A  1  458  ? -41.563 39.529  74.792  1.00 29.00 ? 456  LEU A CD2   1 
ATOM   3379  N  N     . TYR A  1  459  ? -42.580 39.909  70.098  1.00 26.37 ? 457  TYR A N     1 
ATOM   3380  C  CA    . TYR A  1  459  ? -43.981 40.081  69.747  1.00 27.58 ? 457  TYR A CA    1 
ATOM   3381  C  C     . TYR A  1  459  ? -44.336 39.554  68.364  1.00 27.85 ? 457  TYR A C     1 
ATOM   3382  O  O     . TYR A  1  459  ? -45.525 39.379  68.077  1.00 28.62 ? 457  TYR A O     1 
ATOM   3383  C  CB    . TYR A  1  459  ? -44.367 41.546  69.920  1.00 25.28 ? 457  TYR A CB    1 
ATOM   3384  C  CG    . TYR A  1  459  ? -44.587 41.821  71.383  1.00 24.30 ? 457  TYR A CG    1 
ATOM   3385  C  CD1   . TYR A  1  459  ? -45.764 41.421  71.996  1.00 27.01 ? 457  TYR A CD1   1 
ATOM   3386  C  CD2   . TYR A  1  459  ? -43.598 42.405  72.167  1.00 23.30 ? 457  TYR A CD2   1 
ATOM   3387  C  CE1   . TYR A  1  459  ? -45.976 41.632  73.330  1.00 22.82 ? 457  TYR A CE1   1 
ATOM   3388  C  CE2   . TYR A  1  459  ? -43.803 42.626  73.519  1.00 20.40 ? 457  TYR A CE2   1 
ATOM   3389  C  CZ    . TYR A  1  459  ? -44.999 42.235  74.091  1.00 22.03 ? 457  TYR A CZ    1 
ATOM   3390  O  OH    . TYR A  1  459  ? -45.228 42.433  75.434  1.00 24.77 ? 457  TYR A OH    1 
ATOM   3391  N  N     . GLU A  1  460  ? -43.353 39.242  67.521  1.00 28.85 ? 458  GLU A N     1 
ATOM   3392  C  CA    . GLU A  1  460  ? -43.692 38.461  66.340  1.00 29.45 ? 458  GLU A CA    1 
ATOM   3393  C  C     . GLU A  1  460  ? -44.082 37.032  66.689  1.00 33.66 ? 458  GLU A C     1 
ATOM   3394  O  O     . GLU A  1  460  ? -44.623 36.328  65.833  1.00 35.48 ? 458  GLU A O     1 
ATOM   3395  C  CB    . GLU A  1  460  ? -42.538 38.492  65.348  1.00 36.49 ? 458  GLU A CB    1 
ATOM   3396  C  CG    . GLU A  1  460  ? -42.523 39.793  64.560  1.00 43.10 ? 458  GLU A CG    1 
ATOM   3397  C  CD    . GLU A  1  460  ? -41.330 39.916  63.645  1.00 56.41 ? 458  GLU A CD    1 
ATOM   3398  O  OE1   . GLU A  1  460  ? -40.270 39.346  63.975  1.00 56.03 ? 458  GLU A OE1   1 
ATOM   3399  O  OE2   . GLU A  1  460  ? -41.458 40.584  62.597  1.00 53.89 ? 458  GLU A OE2   1 
ATOM   3400  N  N     . GLU A  1  461  ? -43.837 36.597  67.920  1.00 30.69 ? 459  GLU A N     1 
ATOM   3401  C  CA    . GLU A  1  461  ? -44.383 35.348  68.428  1.00 33.99 ? 459  GLU A CA    1 
ATOM   3402  C  C     . GLU A  1  461  ? -45.729 35.535  69.117  1.00 33.14 ? 459  GLU A C     1 
ATOM   3403  O  O     . GLU A  1  461  ? -46.267 34.571  69.669  1.00 32.23 ? 459  GLU A O     1 
ATOM   3404  C  CB    . GLU A  1  461  ? -43.391 34.699  69.399  1.00 29.87 ? 459  GLU A CB    1 
ATOM   3405  C  CG    . GLU A  1  461  ? -42.010 34.496  68.821  1.00 33.88 ? 459  GLU A CG    1 
ATOM   3406  C  CD    . GLU A  1  461  ? -42.006 33.570  67.611  1.00 39.16 ? 459  GLU A CD    1 
ATOM   3407  O  OE1   . GLU A  1  461  ? -42.939 32.743  67.467  1.00 39.76 ? 459  GLU A OE1   1 
ATOM   3408  O  OE2   . GLU A  1  461  ? -41.059 33.675  66.800  1.00 42.87 ? 459  GLU A OE2   1 
ATOM   3409  N  N     . VAL A  1  462  ? -46.281 36.750  69.088  1.00 31.90 ? 460  VAL A N     1 
ATOM   3410  C  CA    . VAL A  1  462  ? -47.503 37.099  69.803  1.00 28.99 ? 460  VAL A CA    1 
ATOM   3411  C  C     . VAL A  1  462  ? -48.588 37.580  68.847  1.00 32.10 ? 460  VAL A C     1 
ATOM   3412  O  O     . VAL A  1  462  ? -49.721 37.082  68.867  1.00 31.69 ? 460  VAL A O     1 
ATOM   3413  C  CB    . VAL A  1  462  ? -47.227 38.166  70.888  1.00 30.70 ? 460  VAL A CB    1 
ATOM   3414  C  CG1   . VAL A  1  462  ? -48.534 38.633  71.536  1.00 27.27 ? 460  VAL A CG1   1 
ATOM   3415  C  CG2   . VAL A  1  462  ? -46.247 37.631  71.928  1.00 28.88 ? 460  VAL A CG2   1 
ATOM   3416  N  N     . VAL A  1  463  ? -48.254 38.548  67.992  1.00 28.45 ? 461  VAL A N     1 
ATOM   3417  C  CA    . VAL A  1  463  ? -49.232 39.143  67.092  1.00 29.94 ? 461  VAL A CA    1 
ATOM   3418  C  C     . VAL A  1  463  ? -49.611 38.150  66.002  1.00 36.28 ? 461  VAL A C     1 
ATOM   3419  O  O     . VAL A  1  463  ? -48.775 37.371  65.530  1.00 36.63 ? 461  VAL A O     1 
ATOM   3420  C  CB    . VAL A  1  463  ? -48.659 40.438  66.493  1.00 31.27 ? 461  VAL A CB    1 
ATOM   3421  C  CG1   . VAL A  1  463  ? -49.648 41.067  65.522  1.00 31.53 ? 461  VAL A CG1   1 
ATOM   3422  C  CG2   . VAL A  1  463  ? -48.300 41.407  67.612  1.00 27.90 ? 461  VAL A CG2   1 
ATOM   3423  N  N     . GLY A  1  464  ? -50.874 38.170  65.603  1.00 35.63 ? 462  GLY A N     1 
ATOM   3424  C  CA    . GLY A  1  464  ? -51.297 37.401  64.453  1.00 40.13 ? 462  GLY A CA    1 
ATOM   3425  C  C     . GLY A  1  464  ? -52.057 36.147  64.838  1.00 42.07 ? 462  GLY A C     1 
ATOM   3426  O  O     . GLY A  1  464  ? -51.845 35.554  65.902  1.00 34.50 ? 462  GLY A O     1 
ATOM   3427  N  N     . ARG A  1  465  ? -52.958 35.729  63.946  1.00 39.49 ? 463  ARG A N     1 
ATOM   3428  C  CA    . ARG A  1  465  ? -53.774 34.549  64.206  1.00 40.55 ? 463  ARG A CA    1 
ATOM   3429  C  C     . ARG A  1  465  ? -52.923 33.294  64.350  1.00 44.33 ? 463  ARG A C     1 
ATOM   3430  O  O     . ARG A  1  465  ? -53.305 32.362  65.067  1.00 50.02 ? 463  ARG A O     1 
ATOM   3431  C  CB    . ARG A  1  465  ? -54.814 34.383  63.093  1.00 38.74 ? 463  ARG A CB    1 
ATOM   3432  N  N     . GLY A  1  466  ? -51.767 33.251  63.693  1.00 38.61 ? 464  GLY A N     1 
ATOM   3433  C  CA    . GLY A  1  466  ? -50.893 32.093  63.811  1.00 39.29 ? 464  GLY A CA    1 
ATOM   3434  C  C     . GLY A  1  466  ? -50.095 32.035  65.090  1.00 42.39 ? 464  GLY A C     1 
ATOM   3435  O  O     . GLY A  1  466  ? -49.369 31.059  65.306  1.00 42.83 ? 464  GLY A O     1 
ATOM   3436  N  N     . LYS A  1  467  ? -50.205 33.055  65.946  1.00 40.17 ? 465  LYS A N     1 
ATOM   3437  C  CA    . LYS A  1  467  ? -49.456 33.101  67.196  1.00 34.04 ? 465  LYS A CA    1 
ATOM   3438  C  C     . LYS A  1  467  ? -50.475 33.164  68.327  1.00 35.43 ? 465  LYS A C     1 
ATOM   3439  O  O     . LYS A  1  467  ? -51.342 32.298  68.397  1.00 37.37 ? 465  LYS A O     1 
ATOM   3440  C  CB    . LYS A  1  467  ? -48.448 34.241  67.182  1.00 33.20 ? 465  LYS A CB    1 
ATOM   3441  C  CG    . LYS A  1  467  ? -47.419 34.131  66.074  1.00 38.65 ? 465  LYS A CG    1 
ATOM   3442  C  CD    . LYS A  1  467  ? -46.455 32.981  66.321  1.00 37.53 ? 465  LYS A CD    1 
ATOM   3443  C  CE    . LYS A  1  467  ? -45.476 32.859  65.180  1.00 44.16 ? 465  LYS A CE    1 
ATOM   3444  N  NZ    . LYS A  1  467  ? -44.408 31.882  65.489  1.00 40.56 ? 465  LYS A NZ    1 
ATOM   3445  N  N     . LEU A  1  468  ? -50.394 34.163  69.212  1.00 35.39 ? 466  LEU A N     1 
ATOM   3446  C  CA    . LEU A  1  468  ? -51.347 34.320  70.303  1.00 31.41 ? 466  LEU A CA    1 
ATOM   3447  C  C     . LEU A  1  468  ? -52.502 35.242  69.944  1.00 32.87 ? 466  LEU A C     1 
ATOM   3448  O  O     . LEU A  1  468  ? -53.432 35.384  70.745  1.00 34.42 ? 466  LEU A O     1 
ATOM   3449  C  CB    . LEU A  1  468  ? -50.637 34.842  71.553  1.00 34.15 ? 466  LEU A CB    1 
ATOM   3450  C  CG    . LEU A  1  468  ? -49.394 34.076  72.025  1.00 32.25 ? 466  LEU A CG    1 
ATOM   3451  C  CD1   . LEU A  1  468  ? -48.886 34.623  73.347  1.00 35.36 ? 466  LEU A CD1   1 
ATOM   3452  C  CD2   . LEU A  1  468  ? -49.703 32.593  72.146  1.00 34.07 ? 466  LEU A CD2   1 
ATOM   3453  N  N     . ASP A  1  469  ? -52.458 35.861  68.765  1.00 34.04 ? 467  ASP A N     1 
ATOM   3454  C  CA    . ASP A  1  469  ? -53.528 36.718  68.260  1.00 30.32 ? 467  ASP A CA    1 
ATOM   3455  C  C     . ASP A  1  469  ? -53.856 37.823  69.254  1.00 28.17 ? 467  ASP A C     1 
ATOM   3456  O  O     . ASP A  1  469  ? -55.015 38.096  69.571  1.00 27.29 ? 467  ASP A O     1 
ATOM   3457  C  CB    . ASP A  1  469  ? -54.776 35.908  67.914  1.00 31.66 ? 467  ASP A CB    1 
ATOM   3458  C  CG    . ASP A  1  469  ? -55.669 36.624  66.920  1.00 40.02 ? 467  ASP A CG    1 
ATOM   3459  O  OD1   . ASP A  1  469  ? -55.160 37.502  66.192  1.00 37.44 ? 467  ASP A OD1   1 
ATOM   3460  O  OD2   . ASP A  1  469  ? -56.877 36.323  66.874  1.00 50.34 ? 467  ASP A OD2   1 
ATOM   3461  N  N     . ARG A  1  470  ? -52.805 38.457  69.757  1.00 27.68 ? 468  ARG A N     1 
ATOM   3462  C  CA    . ARG A  1  470  ? -52.946 39.641  70.571  1.00 28.41 ? 468  ARG A CA    1 
ATOM   3463  C  C     . ARG A  1  470  ? -52.152 40.769  69.935  1.00 26.89 ? 468  ARG A C     1 
ATOM   3464  O  O     . ARG A  1  470  ? -51.051 40.540  69.427  1.00 27.74 ? 468  ARG A O     1 
ATOM   3465  C  CB    . ARG A  1  470  ? -52.450 39.407  72.004  1.00 24.60 ? 468  ARG A CB    1 
ATOM   3466  C  CG    . ARG A  1  470  ? -53.229 38.337  72.750  1.00 25.09 ? 468  ARG A CG    1 
ATOM   3467  C  CD    . ARG A  1  470  ? -54.690 38.716  72.948  1.00 27.74 ? 468  ARG A CD    1 
ATOM   3468  N  NE    . ARG A  1  470  ? -55.427 37.625  73.575  1.00 28.28 ? 468  ARG A NE    1 
ATOM   3469  C  CZ    . ARG A  1  470  ? -56.161 36.738  72.914  1.00 28.77 ? 468  ARG A CZ    1 
ATOM   3470  N  NH1   . ARG A  1  470  ? -56.277 36.781  71.595  1.00 29.79 ? 468  ARG A NH1   1 
ATOM   3471  N  NH2   . ARG A  1  470  ? -56.816 35.799  73.595  1.00 32.36 ? 468  ARG A NH2   1 
ATOM   3472  N  N     . PRO A  1  471  ? -52.686 41.979  69.930  1.00 26.58 ? 469  PRO A N     1 
ATOM   3473  C  CA    . PRO A  1  471  ? -52.006 43.094  69.272  1.00 21.48 ? 469  PRO A CA    1 
ATOM   3474  C  C     . PRO A  1  471  ? -50.891 43.659  70.130  1.00 23.07 ? 469  PRO A C     1 
ATOM   3475  O  O     . PRO A  1  471  ? -50.883 43.545  71.358  1.00 22.73 ? 469  PRO A O     1 
ATOM   3476  C  CB    . PRO A  1  471  ? -53.122 44.126  69.101  1.00 22.56 ? 469  PRO A CB    1 
ATOM   3477  C  CG    . PRO A  1  471  ? -54.014 43.864  70.278  1.00 25.02 ? 469  PRO A CG    1 
ATOM   3478  C  CD    . PRO A  1  471  ? -54.008 42.363  70.449  1.00 25.84 ? 469  PRO A CD    1 
ATOM   3479  N  N     . CYS A  1  472  ? -49.945 44.299  69.450  1.00 22.82 ? 470  CYS A N     1 
ATOM   3480  C  CA    . CYS A  1  472  ? -48.818 44.946  70.102  1.00 22.26 ? 470  CYS A CA    1 
ATOM   3481  C  C     . CYS A  1  472  ? -48.612 46.313  69.479  1.00 21.73 ? 470  CYS A C     1 
ATOM   3482  O  O     . CYS A  1  472  ? -48.556 46.436  68.250  1.00 23.87 ? 470  CYS A O     1 
ATOM   3483  C  CB    . CYS A  1  472  ? -47.545 44.116  69.977  1.00 22.50 ? 470  CYS A CB    1 
ATOM   3484  S  SG    . CYS A  1  472  ? -46.164 44.830  70.869  1.00 23.95 ? 470  CYS A SG    1 
ATOM   3485  N  N     . ARG A  1  473  ? -48.500 47.329  70.322  1.00 19.64 ? 471  ARG A N     1 
ATOM   3486  C  CA    . ARG A  1  473  ? -48.174 48.678  69.880  1.00 19.09 ? 471  ARG A CA    1 
ATOM   3487  C  C     . ARG A  1  473  ? -46.686 48.932  70.075  1.00 21.29 ? 471  ARG A C     1 
ATOM   3488  O  O     . ARG A  1  473  ? -46.168 48.803  71.187  1.00 21.47 ? 471  ARG A O     1 
ATOM   3489  C  CB    . ARG A  1  473  ? -48.983 49.732  70.630  1.00 17.99 ? 471  ARG A CB    1 
ATOM   3490  C  CG    . ARG A  1  473  ? -48.822 51.121  70.009  1.00 19.03 ? 471  ARG A CG    1 
ATOM   3491  C  CD    . ARG A  1  473  ? -49.719 52.136  70.684  1.00 19.57 ? 471  ARG A CD    1 
ATOM   3492  N  NE    . ARG A  1  473  ? -51.092 51.652  70.676  1.00 20.53 ? 471  ARG A NE    1 
ATOM   3493  C  CZ    . ARG A  1  473  ? -51.938 51.807  69.667  1.00 22.75 ? 471  ARG A CZ    1 
ATOM   3494  N  NH1   . ARG A  1  473  ? -51.640 52.565  68.619  1.00 21.20 ? 471  ARG A NH1   1 
ATOM   3495  N  NH2   . ARG A  1  473  ? -53.112 51.187  69.708  1.00 21.88 ? 471  ARG A NH2   1 
ATOM   3496  N  N     . ILE A  1  474  ? -46.015 49.328  69.000  1.00 20.79 ? 472  ILE A N     1 
ATOM   3497  C  CA    . ILE A  1  474  ? -44.581 49.581  69.020  1.00 19.63 ? 472  ILE A CA    1 
ATOM   3498  C  C     . ILE A  1  474  ? -44.338 51.037  69.391  1.00 20.55 ? 472  ILE A C     1 
ATOM   3499  O  O     . ILE A  1  474  ? -44.778 51.948  68.684  1.00 21.29 ? 472  ILE A O     1 
ATOM   3500  C  CB    . ILE A  1  474  ? -43.952 49.245  67.660  1.00 19.97 ? 472  ILE A CB    1 
ATOM   3501  C  CG1   . ILE A  1  474  ? -44.231 47.780  67.308  1.00 24.90 ? 472  ILE A CG1   1 
ATOM   3502  C  CG2   . ILE A  1  474  ? -42.466 49.570  67.665  1.00 21.88 ? 472  ILE A CG2   1 
ATOM   3503  C  CD1   . ILE A  1  474  ? -43.787 47.391  65.905  1.00 25.88 ? 472  ILE A CD1   1 
ATOM   3504  N  N     . TYR A  1  475  ? -43.634 51.255  70.502  1.00 19.85 ? 473  TYR A N     1 
ATOM   3505  C  CA    . TYR A  1  475  ? -43.172 52.579  70.900  1.00 21.37 ? 473  TYR A CA    1 
ATOM   3506  C  C     . TYR A  1  475  ? -41.977 52.930  70.020  1.00 22.39 ? 473  TYR A C     1 
ATOM   3507  O  O     . TYR A  1  475  ? -40.918 52.289  70.099  1.00 20.13 ? 473  TYR A O     1 
ATOM   3508  C  CB    . TYR A  1  475  ? -42.826 52.559  72.384  1.00 21.92 ? 473  TYR A CB    1 
ATOM   3509  C  CG    . TYR A  1  475  ? -42.489 53.855  73.084  1.00 23.11 ? 473  TYR A CG    1 
ATOM   3510  C  CD1   . TYR A  1  475  ? -43.480 54.743  73.467  1.00 22.87 ? 473  TYR A CD1   1 
ATOM   3511  C  CD2   . TYR A  1  475  ? -41.184 54.147  73.437  1.00 35.29 ? 473  TYR A CD2   1 
ATOM   3512  C  CE1   . TYR A  1  475  ? -43.168 55.919  74.143  1.00 22.61 ? 473  TYR A CE1   1 
ATOM   3513  C  CE2   . TYR A  1  475  ? -40.864 55.313  74.108  1.00 40.32 ? 473  TYR A CE2   1 
ATOM   3514  C  CZ    . TYR A  1  475  ? -41.860 56.190  74.461  1.00 33.97 ? 473  TYR A CZ    1 
ATOM   3515  O  OH    . TYR A  1  475  ? -41.539 57.352  75.126  1.00 39.67 ? 473  TYR A OH    1 
ATOM   3516  N  N     . ALA A  1  476  ? -42.159 53.924  69.152  1.00 20.85 ? 474  ALA A N     1 
ATOM   3517  C  CA    . ALA A  1  476  ? -41.245 54.152  68.037  1.00 21.02 ? 474  ALA A CA    1 
ATOM   3518  C  C     . ALA A  1  476  ? -40.525 55.477  68.207  1.00 18.87 ? 474  ALA A C     1 
ATOM   3519  O  O     . ALA A  1  476  ? -41.117 56.542  67.964  1.00 20.60 ? 474  ALA A O     1 
ATOM   3520  C  CB    . ALA A  1  476  ? -42.013 54.128  66.713  1.00 22.71 ? 474  ALA A CB    1 
ATOM   3521  N  N     . PRO A  1  477  ? -39.265 55.474  68.640  1.00 19.66 ? 475  PRO A N     1 
ATOM   3522  C  CA    . PRO A  1  477  ? -38.526 56.731  68.748  1.00 19.64 ? 475  PRO A CA    1 
ATOM   3523  C  C     . PRO A  1  477  ? -38.322 57.341  67.376  1.00 19.36 ? 475  PRO A C     1 
ATOM   3524  O  O     . PRO A  1  477  ? -38.133 56.638  66.380  1.00 21.29 ? 475  PRO A O     1 
ATOM   3525  C  CB    . PRO A  1  477  ? -37.190 56.309  69.376  1.00 18.93 ? 475  PRO A CB    1 
ATOM   3526  C  CG    . PRO A  1  477  ? -37.462 54.937  69.970  1.00 25.84 ? 475  PRO A CG    1 
ATOM   3527  C  CD    . PRO A  1  477  ? -38.437 54.318  69.020  1.00 21.48 ? 475  PRO A CD    1 
ATOM   3528  N  N     . VAL A  1  478  ? -38.372 58.666  67.330  1.00 19.49 ? 476  VAL A N     1 
ATOM   3529  C  CA    . VAL A  1  478  ? -38.217 59.405  66.088  1.00 21.51 ? 476  VAL A CA    1 
ATOM   3530  C  C     . VAL A  1  478  ? -37.287 60.570  66.369  1.00 24.32 ? 476  VAL A C     1 
ATOM   3531  O  O     . VAL A  1  478  ? -37.540 61.359  67.289  1.00 25.16 ? 476  VAL A O     1 
ATOM   3532  C  CB    . VAL A  1  478  ? -39.566 59.916  65.556  1.00 20.63 ? 476  VAL A CB    1 
ATOM   3533  C  CG1   . VAL A  1  478  ? -39.372 60.716  64.274  1.00 22.98 ? 476  VAL A CG1   1 
ATOM   3534  C  CG2   . VAL A  1  478  ? -40.512 58.752  65.314  1.00 21.58 ? 476  VAL A CG2   1 
ATOM   3535  N  N     . GLY A  1  479  ? -36.212 60.681  65.604  1.00 21.83 ? 477  GLY A N     1 
ATOM   3536  C  CA    . GLY A  1  479  ? -35.315 61.789  65.848  1.00 24.52 ? 477  GLY A CA    1 
ATOM   3537  C  C     . GLY A  1  479  ? -33.996 61.626  65.134  1.00 25.31 ? 477  GLY A C     1 
ATOM   3538  O  O     . GLY A  1  479  ? -33.653 60.556  64.614  1.00 23.69 ? 477  GLY A O     1 
ATOM   3539  N  N     . THR A  1  480  ? -33.263 62.733  65.113  1.00 26.15 ? 478  THR A N     1 
ATOM   3540  C  CA    . THR A  1  480  ? -31.932 62.769  64.535  1.00 28.43 ? 478  THR A CA    1 
ATOM   3541  C  C     . THR A  1  480  ? -30.941 62.051  65.445  1.00 30.99 ? 478  THR A C     1 
ATOM   3542  O  O     . THR A  1  480  ? -31.247 61.686  66.583  1.00 30.96 ? 478  THR A O     1 
ATOM   3543  C  CB    . THR A  1  480  ? -31.476 64.210  64.342  1.00 31.05 ? 478  THR A CB    1 
ATOM   3544  O  OG1   . THR A  1  480  ? -31.465 64.858  65.621  1.00 37.34 ? 478  THR A OG1   1 
ATOM   3545  C  CG2   . THR A  1  480  ? -32.422 64.939  63.419  1.00 30.22 ? 478  THR A CG2   1 
ATOM   3546  N  N     . HIS A  1  481  ? -29.725 61.878  64.925  1.00 31.23 ? 479  HIS A N     1 
ATOM   3547  C  CA    . HIS A  1  481  ? -28.646 61.280  65.707  1.00 34.67 ? 479  HIS A CA    1 
ATOM   3548  C  C     . HIS A  1  481  ? -28.427 62.029  67.015  1.00 36.23 ? 479  HIS A C     1 
ATOM   3549  O  O     . HIS A  1  481  ? -28.306 61.414  68.082  1.00 35.12 ? 479  HIS A O     1 
ATOM   3550  C  CB    . HIS A  1  481  ? -27.361 61.263  64.882  1.00 30.60 ? 479  HIS A CB    1 
ATOM   3551  C  CG    . HIS A  1  481  ? -27.430 60.376  63.682  1.00 36.64 ? 479  HIS A CG    1 
ATOM   3552  N  ND1   . HIS A  1  481  ? -26.350 60.158  62.855  1.00 37.04 ? 479  HIS A ND1   1 
ATOM   3553  C  CD2   . HIS A  1  481  ? -28.449 59.643  63.172  1.00 36.15 ? 479  HIS A CD2   1 
ATOM   3554  C  CE1   . HIS A  1  481  ? -26.701 59.332  61.886  1.00 37.74 ? 479  HIS A CE1   1 
ATOM   3555  N  NE2   . HIS A  1  481  ? -27.969 59.003  62.057  1.00 36.91 ? 479  HIS A NE2   1 
ATOM   3556  N  N     . GLU A  1  482  ? -28.375 63.363  66.950  1.00 36.09 ? 480  GLU A N     1 
ATOM   3557  C  CA    . GLU A  1  482  ? -28.166 64.167  68.152  1.00 41.04 ? 480  GLU A CA    1 
ATOM   3558  C  C     . GLU A  1  482  ? -29.253 63.904  69.183  1.00 42.08 ? 480  GLU A C     1 
ATOM   3559  O  O     . GLU A  1  482  ? -28.969 63.712  70.371  1.00 38.14 ? 480  GLU A O     1 
ATOM   3560  C  CB    . GLU A  1  482  ? -28.127 65.652  67.787  1.00 41.61 ? 480  GLU A CB    1 
ATOM   3561  N  N     . THR A  1  483  ? -30.511 63.880  68.739  1.00 34.04 ? 481  THR A N     1 
ATOM   3562  C  CA    . THR A  1  483  ? -31.624 63.723  69.665  1.00 38.92 ? 481  THR A CA    1 
ATOM   3563  C  C     . THR A  1  483  ? -31.624 62.342  70.306  1.00 35.55 ? 481  THR A C     1 
ATOM   3564  O  O     . THR A  1  483  ? -31.899 62.209  71.502  1.00 36.21 ? 481  THR A O     1 
ATOM   3565  C  CB    . THR A  1  483  ? -32.944 63.970  68.937  1.00 38.25 ? 481  THR A CB    1 
ATOM   3566  O  OG1   . THR A  1  483  ? -32.901 65.246  68.289  1.00 42.28 ? 481  THR A OG1   1 
ATOM   3567  C  CG2   . THR A  1  483  ? -34.099 63.956  69.914  1.00 43.55 ? 481  THR A CG2   1 
ATOM   3568  N  N     . LEU A  1  484  ? -31.335 61.298  69.525  1.00 33.20 ? 482  LEU A N     1 
ATOM   3569  C  CA    . LEU A  1  484  ? -31.434 59.948  70.069  1.00 31.83 ? 482  LEU A CA    1 
ATOM   3570  C  C     . LEU A  1  484  ? -30.313 59.666  71.063  1.00 32.19 ? 482  LEU A C     1 
ATOM   3571  O  O     . LEU A  1  484  ? -30.534 58.994  72.077  1.00 38.30 ? 482  LEU A O     1 
ATOM   3572  C  CB    . LEU A  1  484  ? -31.447 58.923  68.933  1.00 31.32 ? 482  LEU A CB    1 
ATOM   3573  C  CG    . LEU A  1  484  ? -30.175 58.623  68.141  1.00 34.88 ? 482  LEU A CG    1 
ATOM   3574  C  CD1   . LEU A  1  484  ? -29.421 57.453  68.748  1.00 35.78 ? 482  LEU A CD1   1 
ATOM   3575  C  CD2   . LEU A  1  484  ? -30.521 58.323  66.688  1.00 36.89 ? 482  LEU A CD2   1 
ATOM   3576  N  N     . LEU A  1  485  ? -29.109 60.179  70.796  1.00 35.72 ? 483  LEU A N     1 
ATOM   3577  C  CA    . LEU A  1  485  ? -27.968 59.898  71.659  1.00 33.39 ? 483  LEU A CA    1 
ATOM   3578  C  C     . LEU A  1  485  ? -28.108 60.527  73.040  1.00 37.29 ? 483  LEU A C     1 
ATOM   3579  O  O     . LEU A  1  485  ? -27.488 60.037  73.992  1.00 36.22 ? 483  LEU A O     1 
ATOM   3580  C  CB    . LEU A  1  485  ? -26.681 60.386  70.990  1.00 30.53 ? 483  LEU A CB    1 
ATOM   3581  C  CG    . LEU A  1  485  ? -26.233 59.596  69.755  1.00 36.83 ? 483  LEU A CG    1 
ATOM   3582  C  CD1   . LEU A  1  485  ? -25.129 60.331  69.018  1.00 38.92 ? 483  LEU A CD1   1 
ATOM   3583  C  CD2   . LEU A  1  485  ? -25.790 58.193  70.137  1.00 31.38 ? 483  LEU A CD2   1 
ATOM   3584  N  N     . ALA A  1  486  ? -28.926 61.578  73.171  1.00 36.13 ? 484  ALA A N     1 
ATOM   3585  C  CA    . ALA A  1  486  ? -28.945 62.371  74.398  1.00 30.06 ? 484  ALA A CA    1 
ATOM   3586  C  C     . ALA A  1  486  ? -29.292 61.529  75.618  1.00 37.12 ? 484  ALA A C     1 
ATOM   3587  O  O     . ALA A  1  486  ? -28.659 61.665  76.671  1.00 36.91 ? 484  ALA A O     1 
ATOM   3588  C  CB    . ALA A  1  486  ? -29.930 63.532  74.255  1.00 35.25 ? 484  ALA A CB    1 
ATOM   3589  N  N     . TYR A  1  487  ? -30.301 60.662  75.509  1.00 36.36 ? 485  TYR A N     1 
ATOM   3590  C  CA    . TYR A  1  487  ? -30.683 59.820  76.637  1.00 35.51 ? 485  TYR A CA    1 
ATOM   3591  C  C     . TYR A  1  487  ? -30.738 58.356  76.226  1.00 36.49 ? 485  TYR A C     1 
ATOM   3592  O  O     . TYR A  1  487  ? -31.511 57.573  76.784  1.00 36.11 ? 485  TYR A O     1 
ATOM   3593  C  CB    . TYR A  1  487  ? -32.016 60.279  77.238  1.00 37.42 ? 485  TYR A CB    1 
ATOM   3594  C  CG    . TYR A  1  487  ? -31.979 61.731  77.677  1.00 35.89 ? 485  TYR A CG    1 
ATOM   3595  C  CD1   . TYR A  1  487  ? -31.366 62.100  78.871  1.00 42.62 ? 485  TYR A CD1   1 
ATOM   3596  C  CD2   . TYR A  1  487  ? -32.525 62.734  76.886  1.00 31.97 ? 485  TYR A CD2   1 
ATOM   3597  C  CE1   . TYR A  1  487  ? -31.311 63.427  79.271  1.00 45.16 ? 485  TYR A CE1   1 
ATOM   3598  C  CE2   . TYR A  1  487  ? -32.475 64.065  77.277  1.00 41.97 ? 485  TYR A CE2   1 
ATOM   3599  C  CZ    . TYR A  1  487  ? -31.869 64.407  78.471  1.00 45.79 ? 485  TYR A CZ    1 
ATOM   3600  O  OH    . TYR A  1  487  ? -31.817 65.730  78.867  1.00 45.69 ? 485  TYR A OH    1 
ATOM   3601  N  N     . LEU A  1  488  ? -29.907 57.967  75.254  1.00 35.20 ? 486  LEU A N     1 
ATOM   3602  C  CA    . LEU A  1  488  ? -29.909 56.578  74.807  1.00 35.02 ? 486  LEU A CA    1 
ATOM   3603  C  C     . LEU A  1  488  ? -29.393 55.639  75.892  1.00 34.81 ? 486  LEU A C     1 
ATOM   3604  O  O     . LEU A  1  488  ? -29.805 54.474  75.951  1.00 30.96 ? 486  LEU A O     1 
ATOM   3605  C  CB    . LEU A  1  488  ? -29.074 56.430  73.532  1.00 32.29 ? 486  LEU A CB    1 
ATOM   3606  C  CG    . LEU A  1  488  ? -29.148 55.046  72.883  1.00 37.73 ? 486  LEU A CG    1 
ATOM   3607  C  CD1   . LEU A  1  488  ? -30.603 54.656  72.621  1.00 33.37 ? 486  LEU A CD1   1 
ATOM   3608  C  CD2   . LEU A  1  488  ? -28.338 55.007  71.598  1.00 31.31 ? 486  LEU A CD2   1 
ATOM   3609  N  N     . VAL A  1  489  ? -28.509 56.130  76.762  1.00 31.09 ? 487  VAL A N     1 
ATOM   3610  C  CA    . VAL A  1  489  ? -27.976 55.285  77.829  1.00 29.33 ? 487  VAL A CA    1 
ATOM   3611  C  C     . VAL A  1  489  ? -29.101 54.787  78.730  1.00 30.89 ? 487  VAL A C     1 
ATOM   3612  O  O     . VAL A  1  489  ? -29.175 53.597  79.054  1.00 28.81 ? 487  VAL A O     1 
ATOM   3613  C  CB    . VAL A  1  489  ? -26.904 56.044  78.627  1.00 32.33 ? 487  VAL A CB    1 
ATOM   3614  C  CG1   . VAL A  1  489  ? -26.620 55.327  79.940  1.00 33.19 ? 487  VAL A CG1   1 
ATOM   3615  C  CG2   . VAL A  1  489  ? -25.630 56.178  77.796  1.00 33.69 ? 487  VAL A CG2   1 
ATOM   3616  N  N     . ARG A  1  490  ? -29.995 55.688  79.152  1.00 30.90 ? 488  ARG A N     1 
ATOM   3617  C  CA    . ARG A  1  490  ? -31.105 55.265  80.005  1.00 28.10 ? 488  ARG A CA    1 
ATOM   3618  C  C     . ARG A  1  490  ? -31.963 54.220  79.302  1.00 35.59 ? 488  ARG A C     1 
ATOM   3619  O  O     . ARG A  1  490  ? -32.419 53.253  79.924  1.00 32.15 ? 488  ARG A O     1 
ATOM   3620  C  CB    . ARG A  1  490  ? -31.960 56.472  80.414  1.00 34.64 ? 488  ARG A CB    1 
ATOM   3621  C  CG    . ARG A  1  490  ? -33.126 56.112  81.344  1.00 30.26 ? 488  ARG A CG    1 
ATOM   3622  C  CD    . ARG A  1  490  ? -34.109 57.284  81.579  1.00 31.95 ? 488  ARG A CD    1 
ATOM   3623  N  NE    . ARG A  1  490  ? -34.831 57.670  80.368  1.00 34.55 ? 488  ARG A NE    1 
ATOM   3624  C  CZ    . ARG A  1  490  ? -34.920 58.912  79.902  1.00 36.82 ? 488  ARG A CZ    1 
ATOM   3625  N  NH1   . ARG A  1  490  ? -34.332 59.926  80.514  1.00 29.36 ? 488  ARG A NH1   1 
ATOM   3626  N  NH2   . ARG A  1  490  ? -35.620 59.141  78.794  1.00 39.18 ? 488  ARG A NH2   1 
ATOM   3627  N  N     . ARG A  1  491  ? -32.168 54.385  77.996  1.00 32.97 ? 489  ARG A N     1 
ATOM   3628  C  CA    . ARG A  1  491  ? -33.036 53.475  77.262  1.00 34.07 ? 489  ARG A CA    1 
ATOM   3629  C  C     . ARG A  1  491  ? -32.388 52.111  77.087  1.00 44.01 ? 489  ARG A C     1 
ATOM   3630  O  O     . ARG A  1  491  ? -33.088 51.092  77.091  1.00 36.68 ? 489  ARG A O     1 
ATOM   3631  C  CB    . ARG A  1  491  ? -33.404 54.104  75.917  1.00 39.95 ? 489  ARG A CB    1 
ATOM   3632  C  CG    . ARG A  1  491  ? -33.313 53.182  74.724  1.00 49.24 ? 489  ARG A CG    1 
ATOM   3633  C  CD    . ARG A  1  491  ? -34.619 53.145  73.950  1.00 51.86 ? 489  ARG A CD    1 
ATOM   3634  N  NE    . ARG A  1  491  ? -35.137 54.467  73.610  1.00 55.43 ? 489  ARG A NE    1 
ATOM   3635  C  CZ    . ARG A  1  491  ? -36.260 54.981  74.099  1.00 55.89 ? 489  ARG A CZ    1 
ATOM   3636  N  NH1   . ARG A  1  491  ? -36.999 54.321  74.976  1.00 52.59 ? 489  ARG A NH1   1 
ATOM   3637  N  NH2   . ARG A  1  491  ? -36.656 56.183  73.688  1.00 53.80 ? 489  ARG A NH2   1 
ATOM   3638  N  N     . LEU A  1  492  ? -31.055 52.069  76.969  1.00 37.62 ? 490  LEU A N     1 
ATOM   3639  C  CA    . LEU A  1  492  ? -30.358 50.791  76.855  1.00 37.31 ? 490  LEU A CA    1 
ATOM   3640  C  C     . LEU A  1  492  ? -30.365 50.034  78.181  1.00 43.83 ? 490  LEU A C     1 
ATOM   3641  O  O     . LEU A  1  492  ? -30.528 48.806  78.200  1.00 42.02 ? 490  LEU A O     1 
ATOM   3642  C  CB    . LEU A  1  492  ? -28.923 51.020  76.375  1.00 32.70 ? 490  LEU A CB    1 
ATOM   3643  C  CG    . LEU A  1  492  ? -28.761 51.634  74.979  1.00 36.94 ? 490  LEU A CG    1 
ATOM   3644  C  CD1   . LEU A  1  492  ? -27.315 52.080  74.741  1.00 37.59 ? 490  LEU A CD1   1 
ATOM   3645  C  CD2   . LEU A  1  492  ? -29.215 50.658  73.899  1.00 42.32 ? 490  LEU A CD2   1 
ATOM   3646  N  N     . LEU A  1  493  ? -30.191 50.748  79.299  1.00 32.45 ? 491  LEU A N     1 
ATOM   3647  C  CA    . LEU A  1  493  ? -30.161 50.081  80.599  1.00 34.35 ? 491  LEU A CA    1 
ATOM   3648  C  C     . LEU A  1  493  ? -31.478 49.385  80.909  1.00 40.44 ? 491  LEU A C     1 
ATOM   3649  O  O     . LEU A  1  493  ? -31.499 48.424  81.686  1.00 43.01 ? 491  LEU A O     1 
ATOM   3650  C  CB    . LEU A  1  493  ? -29.838 51.082  81.710  1.00 35.12 ? 491  LEU A CB    1 
ATOM   3651  C  CG    . LEU A  1  493  ? -28.473 51.755  81.637  1.00 42.99 ? 491  LEU A CG    1 
ATOM   3652  C  CD1   . LEU A  1  493  ? -28.096 52.375  82.979  1.00 41.43 ? 491  LEU A CD1   1 
ATOM   3653  C  CD2   . LEU A  1  493  ? -27.447 50.749  81.199  1.00 45.24 ? 491  LEU A CD2   1 
ATOM   3654  N  N     . GLU A  1  494  ? -32.581 49.867  80.328  1.00 44.54 ? 492  GLU A N     1 
ATOM   3655  C  CA    . GLU A  1  494  ? -33.892 49.288  80.611  1.00 45.72 ? 492  GLU A CA    1 
ATOM   3656  C  C     . GLU A  1  494  ? -33.908 47.796  80.318  1.00 46.29 ? 492  GLU A C     1 
ATOM   3657  O  O     . GLU A  1  494  ? -34.446 47.005  81.102  1.00 42.93 ? 492  GLU A O     1 
ATOM   3658  C  CB    . GLU A  1  494  ? -34.968 50.001  79.792  1.00 40.47 ? 492  GLU A CB    1 
ATOM   3659  N  N     . ASN A  1  495  ? -33.304 47.393  79.201  1.00 45.23 ? 493  ASN A N     1 
ATOM   3660  C  CA    . ASN A  1  495  ? -33.251 45.997  78.794  1.00 49.85 ? 493  ASN A CA    1 
ATOM   3661  C  C     . ASN A  1  495  ? -31.831 45.435  78.806  1.00 48.60 ? 493  ASN A C     1 
ATOM   3662  O  O     . ASN A  1  495  ? -31.610 44.343  78.276  1.00 39.56 ? 493  ASN A O     1 
ATOM   3663  C  CB    . ASN A  1  495  ? -33.877 45.837  77.404  1.00 42.71 ? 493  ASN A CB    1 
ATOM   3664  C  CG    . ASN A  1  495  ? -35.320 46.338  77.346  1.00 39.47 ? 493  ASN A CG    1 
ATOM   3665  O  OD1   . ASN A  1  495  ? -36.235 45.719  77.913  1.00 35.28 ? 493  ASN A OD1   1 
ATOM   3666  N  ND2   . ASN A  1  495  ? -35.531 47.462  76.653  1.00 32.28 ? 493  ASN A ND2   1 
ATOM   3667  N  N     . GLY A  1  496  ? -30.873 46.135  79.420  1.00 47.49 ? 494  GLY A N     1 
ATOM   3668  C  CA    . GLY A  1  496  ? -29.481 45.724  79.336  1.00 48.34 ? 494  GLY A CA    1 
ATOM   3669  C  C     . GLY A  1  496  ? -28.748 45.469  80.642  1.00 53.01 ? 494  GLY A C     1 
ATOM   3670  O  O     . GLY A  1  496  ? -27.578 45.067  80.621  1.00 50.30 ? 494  GLY A O     1 
ATOM   3671  N  N     . ALA A  1  497  ? -29.404 45.701  81.780  1.00 45.38 ? 495  ALA A N     1 
ATOM   3672  C  CA    . ALA A  1  497  ? -28.795 45.418  83.074  1.00 43.64 ? 495  ALA A CA    1 
ATOM   3673  C  C     . ALA A  1  497  ? -28.830 43.920  83.366  1.00 37.95 ? 495  ALA A C     1 
ATOM   3674  O  O     . ALA A  1  497  ? -29.601 43.163  82.767  1.00 39.87 ? 495  ALA A O     1 
ATOM   3675  C  CB    . ALA A  1  497  ? -29.508 46.187  84.189  1.00 38.00 ? 495  ALA A CB    1 
ATOM   3676  N  N     . ASN A  1  498  ? -27.991 43.493  84.317  1.00 40.54 ? 496  ASN A N     1 
ATOM   3677  C  CA    . ASN A  1  498  ? -27.850 42.062  84.592  1.00 38.46 ? 496  ASN A CA    1 
ATOM   3678  C  C     . ASN A  1  498  ? -29.172 41.420  85.001  1.00 42.10 ? 496  ASN A C     1 
ATOM   3679  O  O     . ASN A  1  498  ? -29.376 40.221  84.778  1.00 40.04 ? 496  ASN A O     1 
ATOM   3680  C  CB    . ASN A  1  498  ? -26.793 41.835  85.676  1.00 43.59 ? 496  ASN A CB    1 
ATOM   3681  N  N     . SER A  1  499  ? -30.076 42.192  85.602  1.00 37.93 ? 497  SER A N     1 
ATOM   3682  C  CA    . SER A  1  499  ? -31.387 41.693  85.989  1.00 38.15 ? 497  SER A CA    1 
ATOM   3683  C  C     . SER A  1  499  ? -32.421 41.800  84.874  1.00 33.87 ? 497  SER A C     1 
ATOM   3684  O  O     . SER A  1  499  ? -33.527 41.267  85.026  1.00 32.74 ? 497  SER A O     1 
ATOM   3685  C  CB    . SER A  1  499  ? -31.886 42.452  87.225  1.00 42.79 ? 497  SER A CB    1 
ATOM   3686  O  OG    . SER A  1  499  ? -31.702 43.849  87.057  1.00 42.12 ? 497  SER A OG    1 
ATOM   3687  N  N     . SER A  1  500  ? -32.090 42.470  83.771  1.00 33.81 ? 498  SER A N     1 
ATOM   3688  C  CA    . SER A  1  500  ? -33.045 42.684  82.692  1.00 30.66 ? 498  SER A CA    1 
ATOM   3689  C  C     . SER A  1  500  ? -33.307 41.399  81.917  1.00 34.11 ? 498  SER A C     1 
ATOM   3690  O  O     . SER A  1  500  ? -32.385 40.630  81.632  1.00 33.17 ? 498  SER A O     1 
ATOM   3691  C  CB    . SER A  1  500  ? -32.537 43.758  81.734  1.00 34.47 ? 498  SER A CB    1 
ATOM   3692  O  OG    . SER A  1  500  ? -32.579 45.035  82.332  1.00 40.53 ? 498  SER A OG    1 
ATOM   3693  N  N     . PHE A  1  501  ? -34.579 41.182  81.558  1.00 29.19 ? 499  PHE A N     1 
ATOM   3694  C  CA    . PHE A  1  501  ? -34.946 40.003  80.780  1.00 30.27 ? 499  PHE A CA    1 
ATOM   3695  C  C     . PHE A  1  501  ? -34.150 39.922  79.484  1.00 36.82 ? 499  PHE A C     1 
ATOM   3696  O  O     . PHE A  1  501  ? -33.642 38.855  79.119  1.00 36.22 ? 499  PHE A O     1 
ATOM   3697  C  CB    . PHE A  1  501  ? -36.445 40.011  80.469  1.00 26.27 ? 499  PHE A CB    1 
ATOM   3698  C  CG    . PHE A  1  501  ? -36.876 38.887  79.570  1.00 29.16 ? 499  PHE A CG    1 
ATOM   3699  C  CD1   . PHE A  1  501  ? -37.207 37.660  80.101  1.00 28.37 ? 499  PHE A CD1   1 
ATOM   3700  C  CD2   . PHE A  1  501  ? -36.931 39.053  78.192  1.00 32.16 ? 499  PHE A CD2   1 
ATOM   3701  C  CE1   . PHE A  1  501  ? -37.598 36.612  79.285  1.00 31.26 ? 499  PHE A CE1   1 
ATOM   3702  C  CE2   . PHE A  1  501  ? -37.321 38.007  77.365  1.00 29.65 ? 499  PHE A CE2   1 
ATOM   3703  C  CZ    . PHE A  1  501  ? -37.656 36.787  77.916  1.00 33.35 ? 499  PHE A CZ    1 
ATOM   3704  N  N     . VAL A  1  502  ? -34.064 41.035  78.752  1.00 33.92 ? 500  VAL A N     1 
ATOM   3705  C  CA    . VAL A  1  502  ? -33.420 41.000  77.443  1.00 37.24 ? 500  VAL A CA    1 
ATOM   3706  C  C     . VAL A  1  502  ? -31.946 40.647  77.586  1.00 40.93 ? 500  VAL A C     1 
ATOM   3707  O  O     . VAL A  1  502  ? -31.385 39.912  76.764  1.00 42.99 ? 500  VAL A O     1 
ATOM   3708  C  CB    . VAL A  1  502  ? -33.620 42.337  76.710  1.00 37.89 ? 500  VAL A CB    1 
ATOM   3709  N  N     . HIS A  1  503  ? -31.300 41.143  78.641  1.00 34.66 ? 501  HIS A N     1 
ATOM   3710  C  CA    . HIS A  1  503  ? -29.930 40.727  78.920  1.00 38.80 ? 501  HIS A CA    1 
ATOM   3711  C  C     . HIS A  1  503  ? -29.865 39.246  79.273  1.00 40.39 ? 501  HIS A C     1 
ATOM   3712  O  O     . HIS A  1  503  ? -28.956 38.533  78.831  1.00 38.18 ? 501  HIS A O     1 
ATOM   3713  C  CB    . HIS A  1  503  ? -29.346 41.573  80.052  1.00 38.55 ? 501  HIS A CB    1 
ATOM   3714  C  CG    . HIS A  1  503  ? -27.927 41.233  80.391  1.00 44.89 ? 501  HIS A CG    1 
ATOM   3715  N  ND1   . HIS A  1  503  ? -27.592 40.309  81.359  1.00 46.48 ? 501  HIS A ND1   1 
ATOM   3716  C  CD2   . HIS A  1  503  ? -26.756 41.690  79.887  1.00 44.35 ? 501  HIS A CD2   1 
ATOM   3717  C  CE1   . HIS A  1  503  ? -26.276 40.212  81.437  1.00 42.36 ? 501  HIS A CE1   1 
ATOM   3718  N  NE2   . HIS A  1  503  ? -25.746 41.038  80.552  1.00 46.57 ? 501  HIS A NE2   1 
ATOM   3719  N  N     . ARG A  1  504  ? -30.827 38.760  80.056  1.00 34.03 ? 502  ARG A N     1 
ATOM   3720  C  CA    . ARG A  1  504  ? -30.761 37.382  80.524  1.00 34.00 ? 502  ARG A CA    1 
ATOM   3721  C  C     . ARG A  1  504  ? -31.098 36.393  79.415  1.00 39.34 ? 502  ARG A C     1 
ATOM   3722  O  O     . ARG A  1  504  ? -30.501 35.312  79.345  1.00 34.34 ? 502  ARG A O     1 
ATOM   3723  C  CB    . ARG A  1  504  ? -31.685 37.198  81.728  1.00 36.65 ? 502  ARG A CB    1 
ATOM   3724  C  CG    . ARG A  1  504  ? -31.168 37.905  82.971  1.00 36.26 ? 502  ARG A CG    1 
ATOM   3725  C  CD    . ARG A  1  504  ? -32.280 38.178  83.970  1.00 39.68 ? 502  ARG A CD    1 
ATOM   3726  N  NE    . ARG A  1  504  ? -33.058 36.981  84.264  1.00 39.28 ? 502  ARG A NE    1 
ATOM   3727  C  CZ    . ARG A  1  504  ? -32.653 35.999  85.058  1.00 46.35 ? 502  ARG A CZ    1 
ATOM   3728  N  NH1   . ARG A  1  504  ? -31.456 36.018  85.626  1.00 45.61 ? 502  ARG A NH1   1 
ATOM   3729  N  NH2   . ARG A  1  504  ? -33.465 34.971  85.285  1.00 45.75 ? 502  ARG A NH2   1 
ATOM   3730  N  N     . ILE A  1  505  ? -32.043 36.734  78.533  1.00 40.29 ? 503  ILE A N     1 
ATOM   3731  C  CA    . ILE A  1  505  ? -32.361 35.809  77.446  1.00 38.92 ? 503  ILE A CA    1 
ATOM   3732  C  C     . ILE A  1  505  ? -31.137 35.591  76.562  1.00 42.84 ? 503  ILE A C     1 
ATOM   3733  O  O     . ILE A  1  505  ? -30.948 34.501  76.006  1.00 42.28 ? 503  ILE A O     1 
ATOM   3734  C  CB    . ILE A  1  505  ? -33.575 36.302  76.632  1.00 40.50 ? 503  ILE A CB    1 
ATOM   3735  C  CG1   . ILE A  1  505  ? -33.882 35.329  75.494  1.00 44.91 ? 503  ILE A CG1   1 
ATOM   3736  C  CG2   . ILE A  1  505  ? -33.313 37.655  76.036  1.00 43.41 ? 503  ILE A CG2   1 
ATOM   3737  C  CD1   . ILE A  1  505  ? -35.237 34.701  75.580  1.00 35.00 ? 503  ILE A CD1   1 
ATOM   3738  N  N     . ASN A  1  506  ? -30.273 36.604  76.442  1.00 38.67 ? 504  ASN A N     1 
ATOM   3739  C  CA    . ASN A  1  506  ? -29.035 36.471  75.683  1.00 43.21 ? 504  ASN A CA    1 
ATOM   3740  C  C     . ASN A  1  506  ? -27.916 35.803  76.471  1.00 48.26 ? 504  ASN A C     1 
ATOM   3741  O  O     . ASN A  1  506  ? -26.878 35.481  75.882  1.00 53.48 ? 504  ASN A O     1 
ATOM   3742  C  CB    . ASN A  1  506  ? -28.554 37.841  75.200  1.00 43.42 ? 504  ASN A CB    1 
ATOM   3743  C  CG    . ASN A  1  506  ? -29.397 38.388  74.068  1.00 47.90 ? 504  ASN A CG    1 
ATOM   3744  O  OD1   . ASN A  1  506  ? -30.015 37.633  73.319  1.00 56.51 ? 504  ASN A OD1   1 
ATOM   3745  N  ND2   . ASN A  1  506  ? -29.424 39.708  73.935  1.00 56.85 ? 504  ASN A ND2   1 
ATOM   3746  N  N     . ASP A  1  507  ? -28.091 35.592  77.775  1.00 39.69 ? 505  ASP A N     1 
ATOM   3747  C  CA    . ASP A  1  507  ? -27.049 34.995  78.599  1.00 42.28 ? 505  ASP A CA    1 
ATOM   3748  C  C     . ASP A  1  507  ? -27.169 33.479  78.525  1.00 50.94 ? 505  ASP A C     1 
ATOM   3749  O  O     . ASP A  1  507  ? -28.144 32.920  79.051  1.00 43.27 ? 505  ASP A O     1 
ATOM   3750  C  CB    . ASP A  1  507  ? -27.168 35.472  80.040  1.00 40.16 ? 505  ASP A CB    1 
ATOM   3751  C  CG    . ASP A  1  507  ? -25.986 35.050  80.903  1.00 47.44 ? 505  ASP A CG    1 
ATOM   3752  O  OD1   . ASP A  1  507  ? -25.284 34.079  80.544  1.00 49.99 ? 505  ASP A OD1   1 
ATOM   3753  O  OD2   . ASP A  1  507  ? -25.766 35.687  81.952  1.00 43.74 ? 505  ASP A OD2   1 
ATOM   3754  N  N     . PRO A  1  508  ? -26.214 32.774  77.908  1.00 51.13 ? 506  PRO A N     1 
ATOM   3755  C  CA    . PRO A  1  508  ? -26.333 31.310  77.809  1.00 48.79 ? 506  PRO A CA    1 
ATOM   3756  C  C     . PRO A  1  508  ? -26.272 30.605  79.150  1.00 43.01 ? 506  PRO A C     1 
ATOM   3757  O  O     . PRO A  1  508  ? -26.707 29.450  79.240  1.00 54.05 ? 506  PRO A O     1 
ATOM   3758  C  CB    . PRO A  1  508  ? -25.144 30.914  76.919  1.00 49.53 ? 506  PRO A CB    1 
ATOM   3759  C  CG    . PRO A  1  508  ? -24.699 32.193  76.258  1.00 56.08 ? 506  PRO A CG    1 
ATOM   3760  C  CD    . PRO A  1  508  ? -25.005 33.279  77.238  1.00 50.43 ? 506  PRO A CD    1 
ATOM   3761  N  N     . LYS A  1  509  ? -25.754 31.255  80.189  1.00 43.78 ? 507  LYS A N     1 
ATOM   3762  C  CA    . LYS A  1  509  ? -25.717 30.671  81.523  1.00 46.61 ? 507  LYS A CA    1 
ATOM   3763  C  C     . LYS A  1  509  ? -27.037 30.814  82.274  1.00 48.72 ? 507  LYS A C     1 
ATOM   3764  O  O     . LYS A  1  509  ? -27.125 30.370  83.423  1.00 54.04 ? 507  LYS A O     1 
ATOM   3765  C  CB    . LYS A  1  509  ? -24.585 31.302  82.338  1.00 50.13 ? 507  LYS A CB    1 
ATOM   3766  N  N     . VAL A  1  510  ? -28.054 31.423  81.668  1.00 45.02 ? 508  VAL A N     1 
ATOM   3767  C  CA    . VAL A  1  510  ? -29.382 31.539  82.265  1.00 41.39 ? 508  VAL A CA    1 
ATOM   3768  C  C     . VAL A  1  510  ? -30.300 30.558  81.549  1.00 39.96 ? 508  VAL A C     1 
ATOM   3769  O  O     . VAL A  1  510  ? -30.495 30.656  80.332  1.00 41.16 ? 508  VAL A O     1 
ATOM   3770  C  CB    . VAL A  1  510  ? -29.923 32.975  82.179  1.00 41.84 ? 508  VAL A CB    1 
ATOM   3771  C  CG1   . VAL A  1  510  ? -31.307 33.070  82.829  1.00 38.91 ? 508  VAL A CG1   1 
ATOM   3772  C  CG2   . VAL A  1  510  ? -28.952 33.953  82.826  1.00 41.21 ? 508  VAL A CG2   1 
ATOM   3773  N  N     . SER A  1  511  ? -30.858 29.608  82.299  1.00 36.12 ? 509  SER A N     1 
ATOM   3774  C  CA    . SER A  1  511  ? -31.719 28.586  81.723  1.00 43.18 ? 509  SER A CA    1 
ATOM   3775  C  C     . SER A  1  511  ? -33.125 29.129  81.487  1.00 39.50 ? 509  SER A C     1 
ATOM   3776  O  O     . SER A  1  511  ? -33.528 30.155  82.046  1.00 37.20 ? 509  SER A O     1 
ATOM   3777  C  CB    . SER A  1  511  ? -31.798 27.361  82.634  1.00 44.07 ? 509  SER A CB    1 
ATOM   3778  O  OG    . SER A  1  511  ? -32.517 27.663  83.817  1.00 43.14 ? 509  SER A OG    1 
ATOM   3779  N  N     . ILE A  1  512  ? -33.873 28.418  80.641  1.00 41.01 ? 510  ILE A N     1 
ATOM   3780  C  CA    . ILE A  1  512  ? -35.256 28.800  80.373  1.00 43.10 ? 510  ILE A CA    1 
ATOM   3781  C  C     . ILE A  1  512  ? -36.108 28.615  81.621  1.00 45.51 ? 510  ILE A C     1 
ATOM   3782  O  O     . ILE A  1  512  ? -37.005 29.421  81.900  1.00 39.85 ? 510  ILE A O     1 
ATOM   3783  C  CB    . ILE A  1  512  ? -35.806 28.009  79.173  1.00 37.64 ? 510  ILE A CB    1 
ATOM   3784  C  CG1   . ILE A  1  512  ? -34.971 28.315  77.929  1.00 40.28 ? 510  ILE A CG1   1 
ATOM   3785  C  CG2   . ILE A  1  512  ? -37.279 28.335  78.930  1.00 38.48 ? 510  ILE A CG2   1 
ATOM   3786  C  CD1   . ILE A  1  512  ? -35.529 27.745  76.659  1.00 42.50 ? 510  ILE A CD1   1 
ATOM   3787  N  N     . ASP A  1  513  ? -35.831 27.565  82.400  1.00 41.46 ? 511  ASP A N     1 
ATOM   3788  C  CA    . ASP A  1  513  ? -36.514 27.387  83.677  1.00 36.72 ? 511  ASP A CA    1 
ATOM   3789  C  C     . ASP A  1  513  ? -36.297 28.586  84.589  1.00 39.72 ? 511  ASP A C     1 
ATOM   3790  O  O     . ASP A  1  513  ? -37.205 28.986  85.326  1.00 37.41 ? 511  ASP A O     1 
ATOM   3791  C  CB    . ASP A  1  513  ? -36.031 26.108  84.362  1.00 46.65 ? 511  ASP A CB    1 
ATOM   3792  C  CG    . ASP A  1  513  ? -36.519 24.851  83.668  1.00 52.89 ? 511  ASP A CG    1 
ATOM   3793  O  OD1   . ASP A  1  513  ? -37.678 24.837  83.200  1.00 53.23 ? 511  ASP A OD1   1 
ATOM   3794  O  OD2   . ASP A  1  513  ? -35.743 23.873  83.594  1.00 59.31 ? 511  ASP A OD2   1 
ATOM   3795  N  N     . GLU A  1  514  ? -35.099 29.171  84.557  1.00 38.47 ? 512  GLU A N     1 
ATOM   3796  C  CA    . GLU A  1  514  ? -34.862 30.389  85.323  1.00 36.38 ? 512  GLU A CA    1 
ATOM   3797  C  C     . GLU A  1  514  ? -35.679 31.548  84.769  1.00 33.43 ? 512  GLU A C     1 
ATOM   3798  O  O     . GLU A  1  514  ? -36.221 32.354  85.532  1.00 38.05 ? 512  GLU A O     1 
ATOM   3799  C  CB    . GLU A  1  514  ? -33.370 30.734  85.322  1.00 41.69 ? 512  GLU A CB    1 
ATOM   3800  C  CG    . GLU A  1  514  ? -32.530 29.881  86.269  1.00 48.21 ? 512  GLU A CG    1 
ATOM   3801  C  CD    . GLU A  1  514  ? -31.038 29.976  85.986  1.00 55.55 ? 512  GLU A CD    1 
ATOM   3802  O  OE1   . GLU A  1  514  ? -30.663 30.123  84.805  1.00 55.01 ? 512  GLU A OE1   1 
ATOM   3803  O  OE2   . GLU A  1  514  ? -30.237 29.902  86.941  1.00 64.08 ? 512  GLU A OE2   1 
ATOM   3804  N  N     . LEU A  1  515  ? -35.786 31.640  83.444  1.00 37.54 ? 513  LEU A N     1 
ATOM   3805  C  CA    . LEU A  1  515  ? -36.485 32.764  82.833  1.00 38.13 ? 513  LEU A CA    1 
ATOM   3806  C  C     . LEU A  1  515  ? -37.995 32.664  83.001  1.00 32.53 ? 513  LEU A C     1 
ATOM   3807  O  O     . LEU A  1  515  ? -38.686 33.686  82.937  1.00 32.77 ? 513  LEU A O     1 
ATOM   3808  C  CB    . LEU A  1  515  ? -36.130 32.858  81.352  1.00 35.40 ? 513  LEU A CB    1 
ATOM   3809  C  CG    . LEU A  1  515  ? -34.703 33.290  81.016  1.00 35.62 ? 513  LEU A CG    1 
ATOM   3810  C  CD1   . LEU A  1  515  ? -34.457 33.163  79.521  1.00 36.65 ? 513  LEU A CD1   1 
ATOM   3811  C  CD2   . LEU A  1  515  ? -34.442 34.717  81.499  1.00 33.69 ? 513  LEU A CD2   1 
ATOM   3812  N  N     . ILE A  1  516  ? -38.532 31.458  83.188  1.00 32.55 ? 514  ILE A N     1 
ATOM   3813  C  CA    . ILE A  1  516  ? -39.969 31.286  83.362  1.00 30.65 ? 514  ILE A CA    1 
ATOM   3814  C  C     . ILE A  1  516  ? -40.347 31.142  84.829  1.00 31.62 ? 514  ILE A C     1 
ATOM   3815  O  O     . ILE A  1  516  ? -41.507 30.848  85.141  1.00 32.51 ? 514  ILE A O     1 
ATOM   3816  C  CB    . ILE A  1  516  ? -40.499 30.099  82.541  1.00 34.22 ? 514  ILE A CB    1 
ATOM   3817  C  CG1   . ILE A  1  516  ? -39.976 28.774  83.102  1.00 38.91 ? 514  ILE A CG1   1 
ATOM   3818  C  CG2   . ILE A  1  516  ? -40.123 30.270  81.076  1.00 34.37 ? 514  ILE A CG2   1 
ATOM   3819  C  CD1   . ILE A  1  516  ? -40.631 27.551  82.494  1.00 37.23 ? 514  ILE A CD1   1 
ATOM   3820  N  N     . ALA A  1  517  ? -39.396 31.355  85.738  1.00 30.52 ? 515  ALA A N     1 
ATOM   3821  C  CA    . ALA A  1  517  ? -39.708 31.373  87.160  1.00 33.10 ? 515  ALA A CA    1 
ATOM   3822  C  C     . ALA A  1  517  ? -40.802 32.394  87.439  1.00 33.06 ? 515  ALA A C     1 
ATOM   3823  O  O     . ALA A  1  517  ? -40.796 33.498  86.892  1.00 30.33 ? 515  ALA A O     1 
ATOM   3824  C  CB    . ALA A  1  517  ? -38.459 31.704  87.977  1.00 34.47 ? 515  ALA A CB    1 
ATOM   3825  N  N     . ASP A  1  518  ? -41.755 32.004  88.278  1.00 31.71 ? 516  ASP A N     1 
ATOM   3826  C  CA    . ASP A  1  518  ? -42.904 32.822  88.630  1.00 31.02 ? 516  ASP A CA    1 
ATOM   3827  C  C     . ASP A  1  518  ? -42.540 33.779  89.758  1.00 30.49 ? 516  ASP A C     1 
ATOM   3828  O  O     . ASP A  1  518  ? -42.411 33.358  90.914  1.00 30.32 ? 516  ASP A O     1 
ATOM   3829  C  CB    . ASP A  1  518  ? -44.067 31.926  89.043  1.00 35.27 ? 516  ASP A CB    1 
ATOM   3830  C  CG    . ASP A  1  518  ? -45.334 32.699  89.305  1.00 33.10 ? 516  ASP A CG    1 
ATOM   3831  O  OD1   . ASP A  1  518  ? -45.334 33.940  89.165  1.00 31.32 ? 516  ASP A OD1   1 
ATOM   3832  O  OD2   . ASP A  1  518  ? -46.341 32.051  89.647  1.00 36.94 ? 516  ASP A OD2   1 
ATOM   3833  N  N     . PRO A  1  519  ? -42.393 35.072  89.473  1.00 29.21 ? 517  PRO A N     1 
ATOM   3834  C  CA    . PRO A  1  519  ? -42.013 36.002  90.543  1.00 29.49 ? 517  PRO A CA    1 
ATOM   3835  C  C     . PRO A  1  519  ? -43.018 36.049  91.680  1.00 27.41 ? 517  PRO A C     1 
ATOM   3836  O  O     . PRO A  1  519  ? -42.621 36.298  92.825  1.00 28.53 ? 517  PRO A O     1 
ATOM   3837  C  CB    . PRO A  1  519  ? -41.913 37.353  89.815  1.00 27.81 ? 517  PRO A CB    1 
ATOM   3838  C  CG    . PRO A  1  519  ? -42.755 37.193  88.597  1.00 30.14 ? 517  PRO A CG    1 
ATOM   3839  C  CD    . PRO A  1  519  ? -42.645 35.758  88.193  1.00 29.87 ? 517  PRO A CD    1 
ATOM   3840  N  N     . VAL A  1  520  ? -44.304 35.810  91.395  1.00 28.88 ? 518  VAL A N     1 
ATOM   3841  C  CA    . VAL A  1  520  ? -45.326 35.860  92.438  1.00 27.00 ? 518  VAL A CA    1 
ATOM   3842  C  C     . VAL A  1  520  ? -45.080 34.763  93.463  1.00 31.00 ? 518  VAL A C     1 
ATOM   3843  O  O     . VAL A  1  520  ? -45.104 35.004  94.675  1.00 30.86 ? 518  VAL A O     1 
ATOM   3844  C  CB    . VAL A  1  520  ? -46.731 35.744  91.824  1.00 28.27 ? 518  VAL A CB    1 
ATOM   3845  C  CG1   . VAL A  1  520  ? -47.795 35.837  92.909  1.00 29.83 ? 518  VAL A CG1   1 
ATOM   3846  C  CG2   . VAL A  1  520  ? -46.933 36.831  90.776  1.00 30.83 ? 518  VAL A CG2   1 
ATOM   3847  N  N     . GLU A  1  521  ? -44.806 33.551  92.987  1.00 32.73 ? 519  GLU A N     1 
ATOM   3848  C  CA    . GLU A  1  521  ? -44.565 32.440  93.901  1.00 32.50 ? 519  GLU A CA    1 
ATOM   3849  C  C     . GLU A  1  521  ? -43.194 32.521  94.554  1.00 38.31 ? 519  GLU A C     1 
ATOM   3850  O  O     . GLU A  1  521  ? -43.029 32.048  95.683  1.00 35.16 ? 519  GLU A O     1 
ATOM   3851  C  CB    . GLU A  1  521  ? -44.729 31.113  93.164  1.00 33.94 ? 519  GLU A CB    1 
ATOM   3852  C  CG    . GLU A  1  521  ? -46.161 30.861  92.719  1.00 39.56 ? 519  GLU A CG    1 
ATOM   3853  C  CD    . GLU A  1  521  ? -47.155 31.022  93.857  1.00 48.15 ? 519  GLU A CD    1 
ATOM   3854  O  OE1   . GLU A  1  521  ? -46.836 30.609  94.994  1.00 48.47 ? 519  GLU A OE1   1 
ATOM   3855  O  OE2   . GLU A  1  521  ? -48.256 31.566  93.620  1.00 49.41 ? 519  GLU A OE2   1 
ATOM   3856  N  N     . VAL A  1  522  ? -42.205 33.110  93.876  1.00 32.90 ? 520  VAL A N     1 
ATOM   3857  C  CA    . VAL A  1  522  ? -40.893 33.275  94.492  1.00 27.01 ? 520  VAL A CA    1 
ATOM   3858  C  C     . VAL A  1  522  ? -40.973 34.261  95.650  1.00 37.36 ? 520  VAL A C     1 
ATOM   3859  O  O     . VAL A  1  522  ? -40.453 34.006  96.741  1.00 34.49 ? 520  VAL A O     1 
ATOM   3860  C  CB    . VAL A  1  522  ? -39.848 33.709  93.448  1.00 31.95 ? 520  VAL A CB    1 
ATOM   3861  C  CG1   . VAL A  1  522  ? -38.520 34.031  94.127  1.00 34.50 ? 520  VAL A CG1   1 
ATOM   3862  C  CG2   . VAL A  1  522  ? -39.665 32.630  92.389  1.00 37.82 ? 520  VAL A CG2   1 
ATOM   3863  N  N     . VAL A  1  523  ? -41.631 35.403  95.435  1.00 29.12 ? 521  VAL A N     1 
ATOM   3864  C  CA    . VAL A  1  523  ? -41.790 36.361  96.523  1.00 29.56 ? 521  VAL A CA    1 
ATOM   3865  C  C     . VAL A  1  523  ? -42.615 35.753  97.649  1.00 32.74 ? 521  VAL A C     1 
ATOM   3866  O  O     . VAL A  1  523  ? -42.275 35.902  98.829  1.00 32.25 ? 521  VAL A O     1 
ATOM   3867  C  CB    . VAL A  1  523  ? -42.415 37.668  96.004  1.00 23.63 ? 521  VAL A CB    1 
ATOM   3868  C  CG1   . VAL A  1  523  ? -42.810 38.563  97.168  1.00 29.69 ? 521  VAL A CG1   1 
ATOM   3869  C  CG2   . VAL A  1  523  ? -41.433 38.373  95.091  1.00 28.32 ? 521  VAL A CG2   1 
ATOM   3870  N  N     . ARG A  1  524  ? -43.708 35.055  97.303  1.00 31.19 ? 522  ARG A N     1 
ATOM   3871  C  CA    . ARG A  1  524  ? -44.575 34.463  98.318  1.00 33.33 ? 522  ARG A CA    1 
ATOM   3872  C  C     . ARG A  1  524  ? -43.800 33.559  99.264  1.00 37.95 ? 522  ARG A C     1 
ATOM   3873  O  O     . ARG A  1  524  ? -44.140 33.468  100.449 1.00 41.01 ? 522  ARG A O     1 
ATOM   3874  C  CB    . ARG A  1  524  ? -45.704 33.665  97.665  1.00 38.99 ? 522  ARG A CB    1 
ATOM   3875  C  CG    . ARG A  1  524  ? -46.575 32.917  98.674  1.00 40.23 ? 522  ARG A CG    1 
ATOM   3876  C  CD    . ARG A  1  524  ? -47.446 31.873  98.024  1.00 43.38 ? 522  ARG A CD    1 
ATOM   3877  N  NE    . ARG A  1  524  ? -48.112 32.392  96.837  1.00 44.06 ? 522  ARG A NE    1 
ATOM   3878  C  CZ    . ARG A  1  524  ? -49.161 33.202  96.860  1.00 40.05 ? 522  ARG A CZ    1 
ATOM   3879  N  NH1   . ARG A  1  524  ? -49.665 33.650  97.999  1.00 39.25 ? 522  ARG A NH1   1 
ATOM   3880  N  NH2   . ARG A  1  524  ? -49.718 33.571  95.712  1.00 40.11 ? 522  ARG A NH2   1 
ATOM   3881  N  N     . ALA A  1  525  ? -42.746 32.907  98.768  1.00 36.64 ? 523  ALA A N     1 
ATOM   3882  C  CA    . ALA A  1  525  ? -42.007 31.915  99.533  1.00 43.75 ? 523  ALA A CA    1 
ATOM   3883  C  C     . ALA A  1  525  ? -40.792 32.477  100.260 1.00 41.50 ? 523  ALA A C     1 
ATOM   3884  O  O     . ALA A  1  525  ? -40.166 31.742  101.030 1.00 45.94 ? 523  ALA A O     1 
ATOM   3885  C  CB    . ALA A  1  525  ? -41.561 30.773  98.615  1.00 35.80 ? 523  ALA A CB    1 
ATOM   3886  N  N     . MET A  1  526  ? -40.438 33.743  100.050 1.00 36.18 ? 524  MET A N     1 
ATOM   3887  C  CA    . MET A  1  526  ? -39.268 34.283  100.721 1.00 40.20 ? 524  MET A CA    1 
ATOM   3888  C  C     . MET A  1  526  ? -39.520 34.390  102.226 1.00 39.68 ? 524  MET A C     1 
ATOM   3889  O  O     . MET A  1  526  ? -40.672 34.467  102.666 1.00 38.02 ? 524  MET A O     1 
ATOM   3890  C  CB    . MET A  1  526  ? -38.896 35.644  100.138 1.00 43.35 ? 524  MET A CB    1 
ATOM   3891  C  CG    . MET A  1  526  ? -38.174 35.538  98.807  1.00 40.31 ? 524  MET A CG    1 
ATOM   3892  S  SD    . MET A  1  526  ? -37.816 37.149  98.083  1.00 63.58 ? 524  MET A SD    1 
ATOM   3893  C  CE    . MET A  1  526  ? -37.246 36.666  96.451  1.00 52.19 ? 524  MET A CE    1 
ATOM   3894  N  N     . PRO A  1  527  ? -38.459 34.362  103.043 1.00 48.06 ? 525  PRO A N     1 
ATOM   3895  C  CA    . PRO A  1  527  ? -38.675 34.390  104.503 1.00 49.47 ? 525  PRO A CA    1 
ATOM   3896  C  C     . PRO A  1  527  ? -39.392 35.644  104.969 1.00 46.62 ? 525  PRO A C     1 
ATOM   3897  O  O     . PRO A  1  527  ? -40.346 35.565  105.754 1.00 45.95 ? 525  PRO A O     1 
ATOM   3898  C  CB    . PRO A  1  527  ? -37.249 34.286  105.066 1.00 43.71 ? 525  PRO A CB    1 
ATOM   3899  C  CG    . PRO A  1  527  ? -36.363 34.744  103.961 1.00 48.77 ? 525  PRO A CG    1 
ATOM   3900  C  CD    . PRO A  1  527  ? -37.029 34.282  102.702 1.00 46.81 ? 525  PRO A CD    1 
ATOM   3901  N  N     . VAL A  1  528  ? -38.964 36.804  104.492 1.00 44.14 ? 526  VAL A N     1 
ATOM   3902  C  CA    . VAL A  1  528  ? -39.632 38.068  104.764 1.00 34.13 ? 526  VAL A CA    1 
ATOM   3903  C  C     . VAL A  1  528  ? -40.166 38.579  103.436 1.00 34.15 ? 526  VAL A C     1 
ATOM   3904  O  O     . VAL A  1  528  ? -39.388 39.004  102.572 1.00 40.88 ? 526  VAL A O     1 
ATOM   3905  C  CB    . VAL A  1  528  ? -38.684 39.086  105.407 1.00 39.87 ? 526  VAL A CB    1 
ATOM   3906  C  CG1   . VAL A  1  528  ? -39.381 40.430  105.557 1.00 37.28 ? 526  VAL A CG1   1 
ATOM   3907  C  CG2   . VAL A  1  528  ? -38.187 38.574  106.749 1.00 39.72 ? 526  VAL A CG2   1 
ATOM   3908  N  N     . VAL A  1  529  ? -41.488 38.537  103.262 1.00 33.42 ? 527  VAL A N     1 
ATOM   3909  C  CA    . VAL A  1  529  ? -42.075 39.004  102.014 1.00 30.52 ? 527  VAL A CA    1 
ATOM   3910  C  C     . VAL A  1  529  ? -41.823 40.496  101.867 1.00 32.08 ? 527  VAL A C     1 
ATOM   3911  O  O     . VAL A  1  529  ? -42.092 41.284  102.782 1.00 32.94 ? 527  VAL A O     1 
ATOM   3912  C  CB    . VAL A  1  529  ? -43.573 38.677  101.964 1.00 30.90 ? 527  VAL A CB    1 
ATOM   3913  C  CG1   . VAL A  1  529  ? -44.193 39.295  100.735 1.00 28.81 ? 527  VAL A CG1   1 
ATOM   3914  C  CG2   . VAL A  1  529  ? -43.774 37.166  101.947 1.00 35.71 ? 527  VAL A CG2   1 
ATOM   3915  N  N     . GLY A  1  530  ? -41.265 40.886  100.724 1.00 27.97 ? 528  GLY A N     1 
ATOM   3916  C  CA    . GLY A  1  530  ? -41.061 42.292  100.444 1.00 28.39 ? 528  GLY A CA    1 
ATOM   3917  C  C     . GLY A  1  530  ? -39.872 42.950  101.107 1.00 23.96 ? 528  GLY A C     1 
ATOM   3918  O  O     . GLY A  1  530  ? -39.815 44.180  101.152 1.00 27.80 ? 528  GLY A O     1 
ATOM   3919  N  N     . ALA A  1  531  ? -38.910 42.181  101.621 1.00 28.46 ? 529  ALA A N     1 
ATOM   3920  C  CA    . ALA A  1  531  ? -37.736 42.788  102.237 1.00 25.46 ? 529  ALA A CA    1 
ATOM   3921  C  C     . ALA A  1  531  ? -36.958 43.643  101.238 1.00 24.96 ? 529  ALA A C     1 
ATOM   3922  O  O     . ALA A  1  531  ? -36.812 43.286  100.066 1.00 26.96 ? 529  ALA A O     1 
ATOM   3923  C  CB    . ALA A  1  531  ? -36.819 41.708  102.815 1.00 27.72 ? 529  ALA A CB    1 
ATOM   3924  N  N     . LYS A  1  532  ? -36.443 44.772  101.729 1.00 24.22 ? 530  LYS A N     1 
ATOM   3925  C  CA    . LYS A  1  532  ? -35.561 45.640  100.957 1.00 25.79 ? 530  LYS A CA    1 
ATOM   3926  C  C     . LYS A  1  532  ? -34.361 44.858  100.439 1.00 25.43 ? 530  LYS A C     1 
ATOM   3927  O  O     . LYS A  1  532  ? -33.909 43.890  101.053 1.00 25.38 ? 530  LYS A O     1 
ATOM   3928  C  CB    . LYS A  1  532  ? -35.084 46.807  101.835 1.00 28.14 ? 530  LYS A CB    1 
ATOM   3929  C  CG    . LYS A  1  532  ? -34.120 47.788  101.158 1.00 32.51 ? 530  LYS A CG    1 
ATOM   3930  C  CD    . LYS A  1  532  ? -33.597 48.847  102.130 1.00 28.10 ? 530  LYS A CD    1 
ATOM   3931  C  CE    . LYS A  1  532  ? -32.836 48.224  103.297 1.00 30.49 ? 530  LYS A CE    1 
ATOM   3932  N  NZ    . LYS A  1  532  ? -31.574 47.571  102.856 1.00 28.01 ? 530  LYS A NZ    1 
ATOM   3933  N  N     . HIS A  1  533  ? -33.845 45.275  99.290  1.00 23.15 ? 531  HIS A N     1 
ATOM   3934  C  CA    . HIS A  1  533  ? -32.604 44.699  98.796  1.00 22.93 ? 531  HIS A CA    1 
ATOM   3935  C  C     . HIS A  1  533  ? -31.497 44.844  99.836  1.00 26.52 ? 531  HIS A C     1 
ATOM   3936  O  O     . HIS A  1  533  ? -31.307 45.920  100.409 1.00 26.87 ? 531  HIS A O     1 
ATOM   3937  C  CB    . HIS A  1  533  ? -32.195 45.385  97.497  1.00 24.15 ? 531  HIS A CB    1 
ATOM   3938  C  CG    . HIS A  1  533  ? -31.188 44.612  96.712  1.00 28.13 ? 531  HIS A CG    1 
ATOM   3939  N  ND1   . HIS A  1  533  ? -29.891 44.428  97.145  1.00 26.30 ? 531  HIS A ND1   1 
ATOM   3940  C  CD2   . HIS A  1  533  ? -31.292 43.950  95.536  1.00 33.03 ? 531  HIS A CD2   1 
ATOM   3941  C  CE1   . HIS A  1  533  ? -29.235 43.700  96.259  1.00 34.18 ? 531  HIS A CE1   1 
ATOM   3942  N  NE2   . HIS A  1  533  ? -30.064 43.389  95.279  1.00 36.81 ? 531  HIS A NE2   1 
ATOM   3943  N  N     . ASP A  1  534  ? -30.770 43.744  100.077 1.00 25.49 ? 532  ASP A N     1 
ATOM   3944  C  CA    . ASP A  1  534  ? -29.699 43.745  101.073 1.00 28.17 ? 532  ASP A CA    1 
ATOM   3945  C  C     . ASP A  1  534  ? -28.614 44.766  100.766 1.00 29.34 ? 532  ASP A C     1 
ATOM   3946  O  O     . ASP A  1  534  ? -27.986 45.297  101.689 1.00 32.98 ? 532  ASP A O     1 
ATOM   3947  C  CB    . ASP A  1  534  ? -29.057 42.357  101.159 1.00 28.69 ? 532  ASP A CB    1 
ATOM   3948  C  CG    . ASP A  1  534  ? -29.960 41.333  101.798 1.00 46.06 ? 532  ASP A CG    1 
ATOM   3949  O  OD1   . ASP A  1  534  ? -30.851 41.731  102.581 1.00 51.39 ? 532  ASP A OD1   1 
ATOM   3950  O  OD2   . ASP A  1  534  ? -29.771 40.127  101.526 1.00 57.46 ? 532  ASP A OD2   1 
ATOM   3951  N  N     . ARG A  1  535  ? -28.354 45.032  99.491  1.00 24.12 ? 533  ARG A N     1 
ATOM   3952  C  CA    . ARG A  1  535  ? -27.217 45.852  99.100  1.00 24.35 ? 533  ARG A CA    1 
ATOM   3953  C  C     . ARG A  1  535  ? -27.588 47.300  98.804  1.00 27.06 ? 533  ARG A C     1 
ATOM   3954  O  O     . ARG A  1  535  ? -26.757 48.047  98.286  1.00 28.11 ? 533  ARG A O     1 
ATOM   3955  C  CB    . ARG A  1  535  ? -26.520 45.239  97.881  1.00 30.47 ? 533  ARG A CB    1 
ATOM   3956  N  N     . ILE A  1  536  ? -28.804 47.726  99.118  1.00 23.47 ? 534  ILE A N     1 
ATOM   3957  C  CA    . ILE A  1  536  ? -29.192 49.114  98.919  1.00 24.93 ? 534  ILE A CA    1 
ATOM   3958  C  C     . ILE A  1  536  ? -29.491 49.700  100.287 1.00 26.24 ? 534  ILE A C     1 
ATOM   3959  O  O     . ILE A  1  536  ? -30.349 49.187  101.014 1.00 26.45 ? 534  ILE A O     1 
ATOM   3960  C  CB    . ILE A  1  536  ? -30.391 49.243  97.973  1.00 23.21 ? 534  ILE A CB    1 
ATOM   3961  C  CG1   . ILE A  1  536  ? -29.997 48.722  96.592  1.00 30.63 ? 534  ILE A CG1   1 
ATOM   3962  C  CG2   . ILE A  1  536  ? -30.885 50.696  97.903  1.00 25.18 ? 534  ILE A CG2   1 
ATOM   3963  C  CD1   . ILE A  1  536  ? -31.125 48.740  95.627  1.00 28.23 ? 534  ILE A CD1   1 
ATOM   3964  N  N     . ALA A  1  537  ? -28.773 50.752  100.646 1.00 21.68 ? 535  ALA A N     1 
ATOM   3965  C  CA    . ALA A  1  537  ? -28.970 51.359  101.952 1.00 22.83 ? 535  ALA A CA    1 
ATOM   3966  C  C     . ALA A  1  537  ? -30.160 52.302  101.924 1.00 21.41 ? 535  ALA A C     1 
ATOM   3967  O  O     . ALA A  1  537  ? -30.304 53.109  100.999 1.00 22.06 ? 535  ALA A O     1 
ATOM   3968  C  CB    . ALA A  1  537  ? -27.719 52.115  102.390 1.00 23.85 ? 535  ALA A CB    1 
ATOM   3969  N  N     . LEU A  1  538  ? -31.010 52.205  102.941 1.00 20.64 ? 536  LEU A N     1 
ATOM   3970  C  CA    . LEU A  1  538  ? -31.970 53.270  103.159 1.00 20.86 ? 536  LEU A CA    1 
ATOM   3971  C  C     . LEU A  1  538  ? -31.201 54.569  103.387 1.00 23.57 ? 536  LEU A C     1 
ATOM   3972  O  O     . LEU A  1  538  ? -30.071 54.546  103.882 1.00 22.17 ? 536  LEU A O     1 
ATOM   3973  C  CB    . LEU A  1  538  ? -32.859 52.973  104.368 1.00 21.12 ? 536  LEU A CB    1 
ATOM   3974  C  CG    . LEU A  1  538  ? -33.890 51.854  104.219 1.00 23.40 ? 536  LEU A CG    1 
ATOM   3975  C  CD1   . LEU A  1  538  ? -34.516 51.532  105.560 1.00 30.27 ? 536  LEU A CD1   1 
ATOM   3976  C  CD2   . LEU A  1  538  ? -34.971 52.281  103.237 1.00 23.31 ? 536  LEU A CD2   1 
ATOM   3977  N  N     . PRO A  1  539  ? -31.782 55.713  103.034 1.00 20.33 ? 537  PRO A N     1 
ATOM   3978  C  CA    . PRO A  1  539  ? -31.044 56.972  103.202 1.00 19.67 ? 537  PRO A CA    1 
ATOM   3979  C  C     . PRO A  1  539  ? -30.532 57.188  104.618 1.00 19.27 ? 537  PRO A C     1 
ATOM   3980  O  O     . PRO A  1  539  ? -29.400 57.659  104.777 1.00 20.43 ? 537  PRO A O     1 
ATOM   3981  C  CB    . PRO A  1  539  ? -32.068 58.031  102.767 1.00 19.92 ? 537  PRO A CB    1 
ATOM   3982  C  CG    . PRO A  1  539  ? -32.918 57.295  101.755 1.00 20.11 ? 537  PRO A CG    1 
ATOM   3983  C  CD    . PRO A  1  539  ? -33.054 55.906  102.315 1.00 19.93 ? 537  PRO A CD    1 
ATOM   3984  N  N     . ALA A  1  540  ? -31.304 56.800  105.640 1.00 20.72 ? 538  ALA A N     1 
ATOM   3985  C  CA    . ALA A  1  540  ? -30.860 56.945  107.024 1.00 21.66 ? 538  ALA A CA    1 
ATOM   3986  C  C     . ALA A  1  540  ? -29.615 56.125  107.326 1.00 26.57 ? 538  ALA A C     1 
ATOM   3987  O  O     . ALA A  1  540  ? -28.905 56.437  108.286 1.00 26.09 ? 538  ALA A O     1 
ATOM   3988  C  CB    . ALA A  1  540  ? -31.974 56.539  107.995 1.00 24.84 ? 538  ALA A CB    1 
ATOM   3989  N  N     . GLU A  1  541  ? -29.338 55.085  106.543 1.00 22.38 ? 539  GLU A N     1 
ATOM   3990  C  CA    . GLU A  1  541  ? -28.264 54.148  106.853 1.00 25.06 ? 539  GLU A CA    1 
ATOM   3991  C  C     . GLU A  1  541  ? -27.070 54.296  105.916 1.00 23.09 ? 539  GLU A C     1 
ATOM   3992  O  O     . GLU A  1  541  ? -26.223 53.397  105.850 1.00 23.28 ? 539  GLU A O     1 
ATOM   3993  C  CB    . GLU A  1  541  ? -28.802 52.714  106.837 1.00 28.24 ? 539  GLU A CB    1 
ATOM   3994  C  CG    . GLU A  1  541  ? -29.980 52.540  107.783 1.00 32.67 ? 539  GLU A CG    1 
ATOM   3995  C  CD    . GLU A  1  541  ? -30.483 51.114  107.869 1.00 43.15 ? 539  GLU A CD    1 
ATOM   3996  O  OE1   . GLU A  1  541  ? -29.651 50.182  107.840 1.00 54.12 ? 539  GLU A OE1   1 
ATOM   3997  O  OE2   . GLU A  1  541  ? -31.713 50.925  107.968 1.00 50.55 ? 539  GLU A OE2   1 
ATOM   3998  N  N     . LEU A  1  542  ? -26.963 55.439  105.228 1.00 21.61 ? 540  LEU A N     1 
ATOM   3999  C  CA    . LEU A  1  542  ? -25.882 55.657  104.273 1.00 24.09 ? 540  LEU A CA    1 
ATOM   4000  C  C     . LEU A  1  542  ? -24.512 55.470  104.898 1.00 24.36 ? 540  LEU A C     1 
ATOM   4001  O  O     . LEU A  1  542  ? -23.572 55.057  104.215 1.00 26.10 ? 540  LEU A O     1 
ATOM   4002  C  CB    . LEU A  1  542  ? -25.958 57.070  103.691 1.00 24.43 ? 540  LEU A CB    1 
ATOM   4003  C  CG    . LEU A  1  542  ? -26.744 57.335  102.417 1.00 31.02 ? 540  LEU A CG    1 
ATOM   4004  C  CD1   . LEU A  1  542  ? -26.316 58.688  101.847 1.00 21.96 ? 540  LEU A CD1   1 
ATOM   4005  C  CD2   . LEU A  1  542  ? -26.558 56.221  101.397 1.00 25.88 ? 540  LEU A CD2   1 
ATOM   4006  N  N     . PHE A  1  543  ? -24.365 55.796  106.178 1.00 21.30 ? 541  PHE A N     1 
ATOM   4007  C  CA    . PHE A  1  543  ? -23.072 55.720  106.833 1.00 22.71 ? 541  PHE A CA    1 
ATOM   4008  C  C     . PHE A  1  543  ? -22.956 54.511  107.745 1.00 24.69 ? 541  PHE A C     1 
ATOM   4009  O  O     . PHE A  1  543  ? -21.975 54.397  108.489 1.00 25.44 ? 541  PHE A O     1 
ATOM   4010  C  CB    . PHE A  1  543  ? -22.811 57.020  107.596 1.00 24.94 ? 541  PHE A CB    1 
ATOM   4011  C  CG    . PHE A  1  543  ? -23.025 58.239  106.752 1.00 23.57 ? 541  PHE A CG    1 
ATOM   4012  C  CD1   . PHE A  1  543  ? -22.323 58.389  105.570 1.00 26.36 ? 541  PHE A CD1   1 
ATOM   4013  C  CD2   . PHE A  1  543  ? -23.954 59.208  107.106 1.00 21.94 ? 541  PHE A CD2   1 
ATOM   4014  C  CE1   . PHE A  1  543  ? -22.517 59.478  104.767 1.00 25.07 ? 541  PHE A CE1   1 
ATOM   4015  C  CE2   . PHE A  1  543  ? -24.152 60.319  106.295 1.00 21.24 ? 541  PHE A CE2   1 
ATOM   4016  C  CZ    . PHE A  1  543  ? -23.442 60.451  105.129 1.00 24.24 ? 541  PHE A CZ    1 
ATOM   4017  N  N     . GLY A  1  544  ? -23.936 53.611  107.707 1.00 21.55 ? 542  GLY A N     1 
ATOM   4018  C  CA    . GLY A  1  544  ? -23.834 52.377  108.472 1.00 24.39 ? 542  GLY A CA    1 
ATOM   4019  C  C     . GLY A  1  544  ? -23.686 52.644  109.956 1.00 23.56 ? 542  GLY A C     1 
ATOM   4020  O  O     . GLY A  1  544  ? -24.384 53.484  110.537 1.00 24.65 ? 542  GLY A O     1 
ATOM   4021  N  N     . ASP A  1  545  ? -22.741 51.936  110.577 1.00 27.20 ? 543  ASP A N     1 
ATOM   4022  C  CA    . ASP A  1  545  ? -22.561 52.003  112.020 1.00 30.34 ? 543  ASP A CA    1 
ATOM   4023  C  C     . ASP A  1  545  ? -21.863 53.274  112.482 1.00 28.79 ? 543  ASP A C     1 
ATOM   4024  O  O     . ASP A  1  545  ? -21.845 53.537  113.691 1.00 33.17 ? 543  ASP A O     1 
ATOM   4025  C  CB    . ASP A  1  545  ? -21.766 50.786  112.505 1.00 32.86 ? 543  ASP A CB    1 
ATOM   4026  C  CG    . ASP A  1  545  ? -22.504 49.483  112.275 1.00 47.13 ? 543  ASP A CG    1 
ATOM   4027  O  OD1   . ASP A  1  545  ? -23.754 49.504  112.231 1.00 49.47 ? 543  ASP A OD1   1 
ATOM   4028  O  OD2   . ASP A  1  545  ? -21.834 48.436  112.146 1.00 65.29 ? 543  ASP A OD2   1 
ATOM   4029  N  N     . ALA A  1  546  ? -21.299 54.059  111.565 1.00 25.91 ? 544  ALA A N     1 
ATOM   4030  C  CA    . ALA A  1  546  ? -20.561 55.256  111.960 1.00 25.90 ? 544  ALA A CA    1 
ATOM   4031  C  C     . ALA A  1  546  ? -21.488 56.287  112.583 1.00 30.58 ? 544  ALA A C     1 
ATOM   4032  O  O     . ALA A  1  546  ? -21.198 56.832  113.653 1.00 29.95 ? 544  ALA A O     1 
ATOM   4033  C  CB    . ALA A  1  546  ? -19.834 55.854  110.757 1.00 25.66 ? 544  ALA A CB    1 
ATOM   4034  N  N     . ARG A  1  547  ? -22.607 56.573  111.926 1.00 25.05 ? 545  ARG A N     1 
ATOM   4035  C  CA    . ARG A  1  547  ? -23.543 57.560  112.442 1.00 24.69 ? 545  ARG A CA    1 
ATOM   4036  C  C     . ARG A  1  547  ? -24.820 57.472  111.629 1.00 20.07 ? 545  ARG A C     1 
ATOM   4037  O  O     . ARG A  1  547  ? -24.862 56.877  110.548 1.00 24.80 ? 545  ARG A O     1 
ATOM   4038  C  CB    . ARG A  1  547  ? -22.979 58.976  112.388 1.00 30.13 ? 545  ARG A CB    1 
ATOM   4039  C  CG    . ARG A  1  547  ? -22.744 59.462  111.006 1.00 27.86 ? 545  ARG A CG    1 
ATOM   4040  C  CD    . ARG A  1  547  ? -21.991 60.768  111.024 1.00 31.31 ? 545  ARG A CD    1 
ATOM   4041  N  NE    . ARG A  1  547  ? -21.292 60.951  109.764 1.00 28.18 ? 545  ARG A NE    1 
ATOM   4042  C  CZ    . ARG A  1  547  ? -21.759 61.648  108.735 1.00 24.60 ? 545  ARG A CZ    1 
ATOM   4043  N  NH1   . ARG A  1  547  ? -22.894 62.323  108.817 1.00 24.72 ? 545  ARG A NH1   1 
ATOM   4044  N  NH2   . ARG A  1  547  ? -21.065 61.674  107.605 1.00 25.43 ? 545  ARG A NH2   1 
ATOM   4045  N  N     . THR A  1  548  ? -25.865 58.073  112.179 1.00 21.07 ? 546  THR A N     1 
ATOM   4046  C  CA    . THR A  1  548  ? -27.171 58.112  111.540 1.00 20.18 ? 546  THR A CA    1 
ATOM   4047  C  C     . THR A  1  548  ? -27.237 59.320  110.626 1.00 21.18 ? 546  THR A C     1 
ATOM   4048  O  O     . THR A  1  548  ? -26.956 60.440  111.052 1.00 21.75 ? 546  THR A O     1 
ATOM   4049  C  CB    . THR A  1  548  ? -28.274 58.200  112.590 1.00 24.71 ? 546  THR A CB    1 
ATOM   4050  O  OG1   . THR A  1  548  ? -28.168 57.088  113.483 1.00 29.27 ? 546  THR A OG1   1 
ATOM   4051  C  CG2   . THR A  1  548  ? -29.631 58.191  111.931 1.00 24.58 ? 546  THR A CG2   1 
ATOM   4052  N  N     . ASN A  1  549  ? -27.596 59.091  109.367 1.00 20.13 ? 547  ASN A N     1 
ATOM   4053  C  CA    . ASN A  1  549  ? -27.741 60.200  108.435 1.00 18.46 ? 547  ASN A CA    1 
ATOM   4054  C  C     . ASN A  1  549  ? -28.879 61.106  108.888 1.00 21.13 ? 547  ASN A C     1 
ATOM   4055  O  O     . ASN A  1  549  ? -29.866 60.646  109.465 1.00 22.46 ? 547  ASN A O     1 
ATOM   4056  C  CB    . ASN A  1  549  ? -27.993 59.645  107.026 1.00 19.35 ? 547  ASN A CB    1 
ATOM   4057  C  CG    . ASN A  1  549  ? -27.838 60.693  105.933 1.00 18.35 ? 547  ASN A CG    1 
ATOM   4058  O  OD1   . ASN A  1  549  ? -27.321 61.795  106.156 1.00 20.13 ? 547  ASN A OD1   1 
ATOM   4059  N  ND2   . ASN A  1  549  ? -28.274 60.345  104.728 1.00 19.25 ? 547  ASN A ND2   1 
ATOM   4060  N  N     . SER A  1  550  ? -28.717 62.409  108.679 1.00 19.27 ? 548  SER A N     1 
ATOM   4061  C  CA    . SER A  1  550  ? -29.839 63.314  108.892 1.00 18.82 ? 548  SER A CA    1 
ATOM   4062  C  C     . SER A  1  550  ? -30.958 62.986  107.911 1.00 21.80 ? 548  SER A C     1 
ATOM   4063  O  O     . SER A  1  550  ? -30.719 62.463  106.821 1.00 21.77 ? 548  SER A O     1 
ATOM   4064  C  CB    . SER A  1  550  ? -29.392 64.764  108.706 1.00 19.28 ? 548  SER A CB    1 
ATOM   4065  O  OG    . SER A  1  550  ? -28.890 64.962  107.390 1.00 20.57 ? 548  SER A OG    1 
ATOM   4066  N  N     . ALA A  1  551  ? -32.187 63.314  108.298 1.00 20.65 ? 549  ALA A N     1 
ATOM   4067  C  CA    . ALA A  1  551  ? -33.358 63.104  107.456 1.00 22.21 ? 549  ALA A CA    1 
ATOM   4068  C  C     . ALA A  1  551  ? -33.831 64.430  106.888 1.00 21.34 ? 549  ALA A C     1 
ATOM   4069  O  O     . ALA A  1  551  ? -33.849 65.448  107.587 1.00 21.72 ? 549  ALA A O     1 
ATOM   4070  C  CB    . ALA A  1  551  ? -34.501 62.454  108.240 1.00 22.33 ? 549  ALA A CB    1 
ATOM   4071  N  N     . GLY A  1  552  ? -34.222 64.412  105.619 1.00 20.77 ? 550  GLY A N     1 
ATOM   4072  C  CA    . GLY A  1  552  ? -34.808 65.560  104.979 1.00 21.66 ? 550  GLY A CA    1 
ATOM   4073  C  C     . GLY A  1  552  ? -36.319 65.495  104.978 1.00 19.69 ? 550  GLY A C     1 
ATOM   4074  O  O     . GLY A  1  552  ? -36.942 64.760  105.752 1.00 23.02 ? 550  GLY A O     1 
ATOM   4075  N  N     . LEU A  1  553  ? -36.917 66.275  104.076 1.00 21.31 ? 551  LEU A N     1 
ATOM   4076  C  CA    . LEU A  1  553  ? -38.363 66.344  103.924 1.00 21.36 ? 551  LEU A CA    1 
ATOM   4077  C  C     . LEU A  1  553  ? -38.675 66.337  102.441 1.00 21.22 ? 551  LEU A C     1 
ATOM   4078  O  O     . LEU A  1  553  ? -37.945 66.939  101.653 1.00 24.34 ? 551  LEU A O     1 
ATOM   4079  C  CB    . LEU A  1  553  ? -38.939 67.599  104.569 1.00 23.96 ? 551  LEU A CB    1 
ATOM   4080  C  CG    . LEU A  1  553  ? -38.868 67.681  106.092 1.00 23.06 ? 551  LEU A CG    1 
ATOM   4081  C  CD1   . LEU A  1  553  ? -39.352 69.054  106.554 1.00 27.27 ? 551  LEU A CD1   1 
ATOM   4082  C  CD2   . LEU A  1  553  ? -39.700 66.572  106.724 1.00 24.29 ? 551  LEU A CD2   1 
ATOM   4083  N  N     . ASP A  1  554  ? -39.750 65.650  102.058 1.00 19.28 ? 552  ASP A N     1 
ATOM   4084  C  CA    . ASP A  1  554  ? -40.101 65.521  100.642 1.00 21.68 ? 552  ASP A CA    1 
ATOM   4085  C  C     . ASP A  1  554  ? -41.063 66.643  100.281 1.00 21.41 ? 552  ASP A C     1 
ATOM   4086  O  O     . ASP A  1  554  ? -42.249 66.573  100.595 1.00 20.25 ? 552  ASP A O     1 
ATOM   4087  C  CB    . ASP A  1  554  ? -40.722 64.159  100.372 1.00 20.29 ? 552  ASP A CB    1 
ATOM   4088  C  CG    . ASP A  1  554  ? -41.007 63.931  98.905  1.00 22.74 ? 552  ASP A CG    1 
ATOM   4089  O  OD1   . ASP A  1  554  ? -40.727 64.833  98.080  1.00 24.12 ? 552  ASP A OD1   1 
ATOM   4090  O  OD2   . ASP A  1  554  ? -41.493 62.831  98.577  1.00 23.81 ? 552  ASP A OD2   1 
ATOM   4091  N  N     . LEU A  1  555  ? -40.562 67.672  99.596  1.00 20.49 ? 553  LEU A N     1 
ATOM   4092  C  CA    . LEU A  1  555  ? -41.419 68.801  99.237  1.00 20.33 ? 553  LEU A CA    1 
ATOM   4093  C  C     . LEU A  1  555  ? -42.276 68.517  98.018  1.00 21.17 ? 553  LEU A C     1 
ATOM   4094  O  O     . LEU A  1  555  ? -42.917 69.434  97.489  1.00 22.65 ? 553  LEU A O     1 
ATOM   4095  C  CB    . LEU A  1  555  ? -40.581 70.057  99.008  1.00 19.33 ? 553  LEU A CB    1 
ATOM   4096  C  CG    . LEU A  1  555  ? -39.767 70.469  100.236 1.00 23.44 ? 553  LEU A CG    1 
ATOM   4097  C  CD1   . LEU A  1  555  ? -38.979 71.714  99.961  1.00 24.07 ? 553  LEU A CD1   1 
ATOM   4098  C  CD2   . LEU A  1  555  ? -40.715 70.672  101.411 1.00 25.80 ? 553  LEU A CD2   1 
ATOM   4099  N  N     . SER A  1  556  ? -42.285 67.277  97.552  1.00 19.99 ? 554  SER A N     1 
ATOM   4100  C  CA    . SER A  1  556  ? -43.251 66.844  96.556  1.00 20.38 ? 554  SER A CA    1 
ATOM   4101  C  C     . SER A  1  556  ? -44.387 66.056  97.180  1.00 21.84 ? 554  SER A C     1 
ATOM   4102  O  O     . SER A  1  556  ? -45.316 65.653  96.474  1.00 21.32 ? 554  SER A O     1 
ATOM   4103  C  CB    . SER A  1  556  ? -42.560 66.001  95.479  1.00 22.26 ? 554  SER A CB    1 
ATOM   4104  O  OG    . SER A  1  556  ? -42.335 64.676  95.942  1.00 23.03 ? 554  SER A OG    1 
ATOM   4105  N  N     . ASN A  1  557  ? -44.348 65.845  98.488  1.00 21.02 ? 555  ASN A N     1 
ATOM   4106  C  CA    . ASN A  1  557  ? -45.346 65.051  99.184  1.00 19.90 ? 555  ASN A CA    1 
ATOM   4107  C  C     . ASN A  1  557  ? -46.397 65.992  99.765  1.00 21.27 ? 555  ASN A C     1 
ATOM   4108  O  O     . ASN A  1  557  ? -46.066 66.847  100.590 1.00 19.99 ? 555  ASN A O     1 
ATOM   4109  C  CB    . ASN A  1  557  ? -44.653 64.225  100.270 1.00 20.25 ? 555  ASN A CB    1 
ATOM   4110  C  CG    . ASN A  1  557  ? -45.607 63.335  101.042 1.00 20.97 ? 555  ASN A CG    1 
ATOM   4111  O  OD1   . ASN A  1  557  ? -46.630 63.789  101.554 1.00 23.83 ? 555  ASN A OD1   1 
ATOM   4112  N  ND2   . ASN A  1  557  ? -45.271 62.051  101.129 1.00 22.88 ? 555  ASN A ND2   1 
ATOM   4113  N  N     . GLU A  1  558  ? -47.663 65.839  99.333  1.00 22.20 ? 556  GLU A N     1 
ATOM   4114  C  CA    . GLU A  1  558  ? -48.709 66.766  99.774  1.00 22.92 ? 556  GLU A CA    1 
ATOM   4115  C  C     . GLU A  1  558  ? -48.942 66.703  101.274 1.00 21.82 ? 556  GLU A C     1 
ATOM   4116  O  O     . GLU A  1  558  ? -49.296 67.721  101.882 1.00 23.98 ? 556  GLU A O     1 
ATOM   4117  C  CB    . GLU A  1  558  ? -50.038 66.505  99.055  1.00 25.19 ? 556  GLU A CB    1 
ATOM   4118  C  CG    . GLU A  1  558  ? -50.056 66.834  97.568  1.00 24.32 ? 556  GLU A CG    1 
ATOM   4119  C  CD    . GLU A  1  558  ? -49.803 68.300  97.207  1.00 23.43 ? 556  GLU A CD    1 
ATOM   4120  O  OE1   . GLU A  1  558  ? -49.829 69.214  98.062  1.00 23.44 ? 556  GLU A OE1   1 
ATOM   4121  O  OE2   . GLU A  1  558  ? -49.579 68.536  96.005  1.00 23.11 ? 556  GLU A OE2   1 
ATOM   4122  N  N     . GLU A  1  559  ? -48.796 65.526  101.888 1.00 20.38 ? 557  GLU A N     1 
ATOM   4123  C  CA    . GLU A  1  559  ? -48.909 65.459  103.345 1.00 23.26 ? 557  GLU A CA    1 
ATOM   4124  C  C     . GLU A  1  559  ? -47.800 66.272  103.996 1.00 21.52 ? 557  GLU A C     1 
ATOM   4125  O  O     . GLU A  1  559  ? -48.037 67.035  104.940 1.00 22.68 ? 557  GLU A O     1 
ATOM   4126  C  CB    . GLU A  1  559  ? -48.841 64.012  103.836 1.00 27.18 ? 557  GLU A CB    1 
ATOM   4127  C  CG    . GLU A  1  559  ? -49.946 63.093  103.378 1.00 26.73 ? 557  GLU A CG    1 
ATOM   4128  C  CD    . GLU A  1  559  ? -49.690 61.641  103.789 1.00 35.99 ? 557  GLU A CD    1 
ATOM   4129  O  OE1   . GLU A  1  559  ? -48.712 61.388  104.529 1.00 43.64 ? 557  GLU A OE1   1 
ATOM   4130  O  OE2   . GLU A  1  559  ? -50.456 60.749  103.370 1.00 36.40 ? 557  GLU A OE2   1 
ATOM   4131  N  N     . THR A  1  560  ? -46.571 66.115  103.496 1.00 22.54 ? 558  THR A N     1 
ATOM   4132  C  CA    . THR A  1  560  ? -45.458 66.890  104.032 1.00 22.95 ? 558  THR A CA    1 
ATOM   4133  C  C     . THR A  1  560  ? -45.686 68.379  103.834 1.00 21.04 ? 558  THR A C     1 
ATOM   4134  O  O     . THR A  1  560  ? -45.472 69.173  104.751 1.00 24.80 ? 558  THR A O     1 
ATOM   4135  C  CB    . THR A  1  560  ? -44.157 66.466  103.359 1.00 23.51 ? 558  THR A CB    1 
ATOM   4136  O  OG1   . THR A  1  560  ? -43.988 65.057  103.528 1.00 23.22 ? 558  THR A OG1   1 
ATOM   4137  C  CG2   . THR A  1  560  ? -42.977 67.211  103.965 1.00 26.43 ? 558  THR A CG2   1 
ATOM   4138  N  N     . LEU A  1  561  ? -46.138 68.780  102.643 1.00 19.84 ? 559  LEU A N     1 
ATOM   4139  C  CA    . LEU A  1  561  ? -46.359 70.201  102.403 1.00 18.73 ? 559  LEU A CA    1 
ATOM   4140  C  C     . LEU A  1  561  ? -47.445 70.751  103.314 1.00 21.32 ? 559  LEU A C     1 
ATOM   4141  O  O     . LEU A  1  561  ? -47.362 71.897  103.768 1.00 22.62 ? 559  LEU A O     1 
ATOM   4142  C  CB    . LEU A  1  561  ? -46.715 70.438  100.935 1.00 19.26 ? 559  LEU A CB    1 
ATOM   4143  C  CG    . LEU A  1  561  ? -45.554 70.152  99.985  1.00 19.38 ? 559  LEU A CG    1 
ATOM   4144  C  CD1   . LEU A  1  561  ? -46.038 70.247  98.534  1.00 22.29 ? 559  LEU A CD1   1 
ATOM   4145  C  CD2   . LEU A  1  561  ? -44.393 71.132  100.244 1.00 19.72 ? 559  LEU A CD2   1 
ATOM   4146  N  N     . ALA A  1  562  ? -48.475 69.950  103.592 1.00 20.33 ? 560  ALA A N     1 
ATOM   4147  C  CA    . ALA A  1  562  ? -49.571 70.449  104.414 1.00 22.02 ? 560  ALA A CA    1 
ATOM   4148  C  C     . ALA A  1  562  ? -49.144 70.577  105.867 1.00 24.27 ? 560  ALA A C     1 
ATOM   4149  O  O     . ALA A  1  562  ? -49.468 71.566  106.534 1.00 24.72 ? 560  ALA A O     1 
ATOM   4150  C  CB    . ALA A  1  562  ? -50.790 69.536  104.285 1.00 25.40 ? 560  ALA A CB    1 
ATOM   4151  N  N     . SER A  1  563  ? -48.416 69.588  106.374 1.00 24.60 ? 561  SER A N     1 
ATOM   4152  C  CA    A SER A  1  563  ? -47.899 69.675  107.735 0.50 25.21 ? 561  SER A CA    1 
ATOM   4153  C  CA    B SER A  1  563  ? -47.924 69.695  107.740 0.50 25.20 ? 561  SER A CA    1 
ATOM   4154  C  C     . SER A  1  563  ? -46.864 70.784  107.856 1.00 22.97 ? 561  SER A C     1 
ATOM   4155  O  O     . SER A  1  563  ? -46.850 71.533  108.840 1.00 26.14 ? 561  SER A O     1 
ATOM   4156  C  CB    A SER A  1  563  ? -47.294 68.332  108.144 0.50 27.49 ? 561  SER A CB    1 
ATOM   4157  C  CB    B SER A  1  563  ? -47.385 68.346  108.216 0.50 27.63 ? 561  SER A CB    1 
ATOM   4158  O  OG    A SER A  1  563  ? -46.650 68.439  109.399 0.50 28.21 ? 561  SER A OG    1 
ATOM   4159  O  OG    B SER A  1  563  ? -46.267 67.948  107.457 0.50 28.91 ? 561  SER A OG    1 
ATOM   4160  N  N     . LEU A  1  564  ? -45.978 70.897  106.861 1.00 24.55 ? 562  LEU A N     1 
ATOM   4161  C  CA    A LEU A  1  564  ? -44.970 71.949  106.893 0.56 24.04 ? 562  LEU A CA    1 
ATOM   4162  C  CA    B LEU A  1  564  ? -44.971 71.953  106.881 0.44 24.05 ? 562  LEU A CA    1 
ATOM   4163  C  C     . LEU A  1  564  ? -45.618 73.329  106.851 1.00 24.23 ? 562  LEU A C     1 
ATOM   4164  O  O     . LEU A  1  564  ? -45.186 74.246  107.556 1.00 25.35 ? 562  LEU A O     1 
ATOM   4165  C  CB    A LEU A  1  564  ? -43.990 71.767  105.733 0.56 23.73 ? 562  LEU A CB    1 
ATOM   4166  C  CB    B LEU A  1  564  ? -44.016 71.797  105.698 0.44 23.75 ? 562  LEU A CB    1 
ATOM   4167  C  CG    A LEU A  1  564  ? -42.687 72.550  105.796 0.56 24.40 ? 562  LEU A CG    1 
ATOM   4168  C  CG    B LEU A  1  564  ? -42.635 71.228  105.980 0.44 26.14 ? 562  LEU A CG    1 
ATOM   4169  C  CD1   A LEU A  1  564  ? -41.951 72.206  107.073 0.56 27.40 ? 562  LEU A CD1   1 
ATOM   4170  C  CD1   B LEU A  1  564  ? -41.824 71.245  104.706 0.44 22.03 ? 562  LEU A CD1   1 
ATOM   4171  C  CD2   A LEU A  1  564  ? -41.834 72.221  104.589 0.56 22.98 ? 562  LEU A CD2   1 
ATOM   4172  C  CD2   B LEU A  1  564  ? -41.952 72.042  107.063 0.44 27.30 ? 562  LEU A CD2   1 
ATOM   4173  N  N     . THR A  1  565  ? -46.660 73.494  106.038 1.00 22.53 ? 563  THR A N     1 
ATOM   4174  C  CA    . THR A  1  565  ? -47.357 74.771  105.999 1.00 24.25 ? 563  THR A CA    1 
ATOM   4175  C  C     . THR A  1  565  ? -47.770 75.203  107.399 1.00 22.64 ? 563  THR A C     1 
ATOM   4176  O  O     . THR A  1  565  ? -47.555 76.351  107.798 1.00 24.81 ? 563  THR A O     1 
ATOM   4177  C  CB    . THR A  1  565  ? -48.578 74.671  105.090 1.00 24.21 ? 563  THR A CB    1 
ATOM   4178  O  OG1   . THR A  1  565  ? -48.146 74.487  103.737 1.00 23.01 ? 563  THR A OG1   1 
ATOM   4179  C  CG2   . THR A  1  565  ? -49.423 75.935  105.189 1.00 26.71 ? 563  THR A CG2   1 
ATOM   4180  N  N     . GLU A  1  566  ? -48.337 74.274  108.171 1.00 24.30 ? 564  GLU A N     1 
ATOM   4181  C  CA    . GLU A  1  566  ? -48.816 74.625  109.503 1.00 24.73 ? 564  GLU A CA    1 
ATOM   4182  C  C     . GLU A  1  566  ? -47.656 74.887  110.452 1.00 24.73 ? 564  GLU A C     1 
ATOM   4183  O  O     . GLU A  1  566  ? -47.691 75.841  111.237 1.00 27.96 ? 564  GLU A O     1 
ATOM   4184  C  CB    . GLU A  1  566  ? -49.728 73.519  110.031 1.00 29.58 ? 564  GLU A CB    1 
ATOM   4185  C  CG    . GLU A  1  566  ? -50.935 73.291  109.137 1.00 34.31 ? 564  GLU A CG    1 
ATOM   4186  C  CD    . GLU A  1  566  ? -51.745 74.563  108.924 1.00 46.05 ? 564  GLU A CD    1 
ATOM   4187  O  OE1   . GLU A  1  566  ? -51.927 75.324  109.900 1.00 48.81 ? 564  GLU A OE1   1 
ATOM   4188  O  OE2   . GLU A  1  566  ? -52.188 74.808  107.778 1.00 43.47 ? 564  GLU A OE2   1 
ATOM   4189  N  N     . ALA A  1  567  ? -46.604 74.071  110.375 1.00 24.49 ? 565  ALA A N     1 
ATOM   4190  C  CA    . ALA A  1  567  ? -45.451 74.297  111.238 1.00 25.09 ? 565  ALA A CA    1 
ATOM   4191  C  C     . ALA A  1  567  ? -44.773 75.616  110.903 1.00 20.92 ? 565  ALA A C     1 
ATOM   4192  O  O     . ALA A  1  567  ? -44.325 76.343  111.803 1.00 27.06 ? 565  ALA A O     1 
ATOM   4193  C  CB    . ALA A  1  567  ? -44.469 73.137  111.115 1.00 25.46 ? 565  ALA A CB    1 
ATOM   4194  N  N     . LEU A  1  568  ? -44.671 75.936  109.611 1.00 22.93 ? 566  LEU A N     1 
ATOM   4195  C  CA    . LEU A  1  568  ? -44.045 77.193  109.220 1.00 20.86 ? 566  LEU A CA    1 
ATOM   4196  C  C     . LEU A  1  568  ? -44.870 78.382  109.692 1.00 23.03 ? 566  LEU A C     1 
ATOM   4197  O  O     . LEU A  1  568  ? -44.319 79.352  110.225 1.00 24.24 ? 566  LEU A O     1 
ATOM   4198  C  CB    . LEU A  1  568  ? -43.841 77.234  107.702 1.00 22.27 ? 566  LEU A CB    1 
ATOM   4199  C  CG    . LEU A  1  568  ? -42.888 76.179  107.143 1.00 23.07 ? 566  LEU A CG    1 
ATOM   4200  C  CD1   . LEU A  1  568  ? -42.918 76.189  105.628 1.00 22.13 ? 566  LEU A CD1   1 
ATOM   4201  C  CD2   . LEU A  1  568  ? -41.472 76.407  107.635 1.00 26.91 ? 566  LEU A CD2   1 
ATOM   4202  N  N     . ARG A  1  569  ? -46.195 78.319  109.523 1.00 22.23 ? 567  ARG A N     1 
ATOM   4203  C  CA    . ARG A  1  569  ? -47.047 79.386  110.034 1.00 23.89 ? 567  ARG A CA    1 
ATOM   4204  C  C     . ARG A  1  569  ? -46.889 79.537  111.536 1.00 27.45 ? 567  ARG A C     1 
ATOM   4205  O  O     . ARG A  1  569  ? -46.768 80.658  112.047 1.00 28.94 ? 567  ARG A O     1 
ATOM   4206  C  CB    . ARG A  1  569  ? -48.508 79.112  109.677 1.00 27.36 ? 567  ARG A CB    1 
ATOM   4207  C  CG    . ARG A  1  569  ? -48.825 79.338  108.211 1.00 32.26 ? 567  ARG A CG    1 
ATOM   4208  C  CD    . ARG A  1  569  ? -50.267 78.973  107.916 1.00 36.51 ? 567  ARG A CD    1 
ATOM   4209  N  NE    . ARG A  1  569  ? -50.535 78.928  106.485 1.00 34.72 ? 567  ARG A NE    1 
ATOM   4210  C  CZ    . ARG A  1  569  ? -51.659 78.462  105.957 1.00 43.69 ? 567  ARG A CZ    1 
ATOM   4211  N  NH1   . ARG A  1  569  ? -52.618 77.954  106.714 1.00 47.18 ? 567  ARG A NH1   1 
ATOM   4212  N  NH2   . ARG A  1  569  ? -51.826 78.507  104.638 1.00 48.42 ? 567  ARG A NH2   1 
ATOM   4213  N  N     . GLU A  1  570  ? -46.865 78.418  112.259 1.00 25.89 ? 568  GLU A N     1 
ATOM   4214  C  CA    . GLU A  1  570  ? -46.700 78.485  113.706 1.00 25.78 ? 568  GLU A CA    1 
ATOM   4215  C  C     . GLU A  1  570  ? -45.351 79.086  114.082 1.00 34.30 ? 568  GLU A C     1 
ATOM   4216  O  O     . GLU A  1  570  ? -45.254 79.841  115.054 1.00 30.71 ? 568  GLU A O     1 
ATOM   4217  C  CB    . GLU A  1  570  ? -46.878 77.093  114.317 1.00 28.18 ? 568  GLU A CB    1 
ATOM   4218  C  CG    . GLU A  1  570  ? -48.316 76.597  114.225 1.00 40.67 ? 568  GLU A CG    1 
ATOM   4219  C  CD    . GLU A  1  570  ? -48.477 75.133  114.586 1.00 46.27 ? 568  GLU A CD    1 
ATOM   4220  O  OE1   . GLU A  1  570  ? -47.452 74.444  114.776 1.00 56.58 ? 568  GLU A OE1   1 
ATOM   4221  O  OE2   . GLU A  1  570  ? -49.637 74.673  114.675 1.00 57.67 ? 568  GLU A OE2   1 
ATOM   4222  N  N     . SER A  1  571  ? -44.303 78.791  113.308 1.00 26.97 ? 569  SER A N     1 
ATOM   4223  C  CA    . SER A  1  571  ? -42.990 79.363  113.605 1.00 26.90 ? 569  SER A CA    1 
ATOM   4224  C  C     . SER A  1  571  ? -42.988 80.876  113.446 1.00 28.93 ? 569  SER A C     1 
ATOM   4225  O  O     . SER A  1  571  ? -42.249 81.572  114.150 1.00 27.29 ? 569  SER A O     1 
ATOM   4226  C  CB    . SER A  1  571  ? -41.922 78.754  112.701 1.00 24.05 ? 569  SER A CB    1 
ATOM   4227  O  OG    . SER A  1  571  ? -41.920 79.381  111.424 1.00 26.77 ? 569  SER A OG    1 
ATOM   4228  N  N     . ALA A  1  572  ? -43.798 81.405  112.535 1.00 28.76 ? 570  ALA A N     1 
ATOM   4229  C  CA    . ALA A  1  572  ? -43.846 82.847  112.337 1.00 27.56 ? 570  ALA A CA    1 
ATOM   4230  C  C     . ALA A  1  572  ? -44.622 83.558  113.432 1.00 32.69 ? 570  ALA A C     1 
ATOM   4231  O  O     . ALA A  1  572  ? -44.524 84.783  113.544 1.00 36.60 ? 570  ALA A O     1 
ATOM   4232  C  CB    . ALA A  1  572  ? -44.457 83.180  110.978 1.00 33.41 ? 570  ALA A CB    1 
ATOM   4233  N  N     . ALA A  1  573  ? -45.388 82.821  114.227 1.00 33.97 ? 571  ALA A N     1 
ATOM   4234  C  CA    . ALA A  1  573  ? -46.113 83.381  115.358 1.00 33.17 ? 571  ALA A CA    1 
ATOM   4235  C  C     . ALA A  1  573  ? -45.273 83.419  116.626 1.00 40.64 ? 571  ALA A C     1 
ATOM   4236  O  O     . ALA A  1  573  ? -45.742 83.923  117.651 1.00 39.90 ? 571  ALA A O     1 
ATOM   4237  C  CB    . ALA A  1  573  ? -47.394 82.579  115.611 1.00 35.60 ? 571  ALA A CB    1 
ATOM   4238  N  N     . MET A  1  574  ? -44.050 82.910  116.584 1.00 32.35 ? 572  MET A N     1 
ATOM   4239  C  CA    . MET A  1  574  ? -43.233 82.800  117.781 1.00 40.00 ? 572  MET A CA    1 
ATOM   4240  C  C     . MET A  1  574  ? -42.444 84.080  118.007 1.00 37.76 ? 572  MET A C     1 
ATOM   4241  O  O     . MET A  1  574  ? -42.038 84.760  117.059 1.00 32.90 ? 572  MET A O     1 
ATOM   4242  C  CB    . MET A  1  574  ? -42.290 81.603  117.675 1.00 34.42 ? 572  MET A CB    1 
ATOM   4243  C  CG    . MET A  1  574  ? -43.022 80.273  117.592 1.00 34.95 ? 572  MET A CG    1 
ATOM   4244  S  SD    . MET A  1  574  ? -41.931 78.861  117.412 1.00 38.92 ? 572  MET A SD    1 
ATOM   4245  C  CE    . MET A  1  574  ? -40.989 78.973  118.933 1.00 49.56 ? 572  MET A CE    1 
ATOM   4246  N  N     . LYS A  1  575  ? -42.241 84.410  119.283 1.00 35.30 ? 573  LYS A N     1 
ATOM   4247  C  CA    . LYS A  1  575  ? -41.506 85.615  119.669 1.00 40.04 ? 573  LYS A CA    1 
ATOM   4248  C  C     . LYS A  1  575  ? -40.024 85.277  119.822 1.00 31.90 ? 573  LYS A C     1 
ATOM   4249  O  O     . LYS A  1  575  ? -39.463 85.229  120.920 1.00 33.94 ? 573  LYS A O     1 
ATOM   4250  C  CB    . LYS A  1  575  ? -42.085 86.208  120.948 1.00 40.83 ? 573  LYS A CB    1 
ATOM   4251  C  CG    . LYS A  1  575  ? -43.451 86.846  120.771 1.00 47.99 ? 573  LYS A CG    1 
ATOM   4252  C  CD    . LYS A  1  575  ? -43.411 87.940  119.715 1.00 51.58 ? 573  LYS A CD    1 
ATOM   4253  C  CE    . LYS A  1  575  ? -44.735 88.676  119.624 1.00 57.90 ? 573  LYS A CE    1 
ATOM   4254  N  NZ    . LYS A  1  575  ? -44.738 89.666  118.512 1.00 57.76 ? 573  LYS A NZ    1 
ATOM   4255  N  N     . TRP A  1  576  ? -39.392 85.047  118.672 1.00 28.75 ? 574  TRP A N     1 
ATOM   4256  C  CA    . TRP A  1  576  ? -37.974 84.706  118.631 1.00 28.08 ? 574  TRP A CA    1 
ATOM   4257  C  C     . TRP A  1  576  ? -37.124 85.824  119.221 1.00 26.84 ? 574  TRP A C     1 
ATOM   4258  O  O     . TRP A  1  576  ? -37.325 87.006  118.921 1.00 28.87 ? 574  TRP A O     1 
ATOM   4259  C  CB    . TRP A  1  576  ? -37.543 84.445  117.192 1.00 25.85 ? 574  TRP A CB    1 
ATOM   4260  C  CG    . TRP A  1  576  ? -38.228 83.291  116.536 1.00 27.86 ? 574  TRP A CG    1 
ATOM   4261  C  CD1   . TRP A  1  576  ? -39.202 83.346  115.577 1.00 27.73 ? 574  TRP A CD1   1 
ATOM   4262  C  CD2   . TRP A  1  576  ? -37.982 81.907  116.781 1.00 22.80 ? 574  TRP A CD2   1 
ATOM   4263  N  NE1   . TRP A  1  576  ? -39.576 82.079  115.211 1.00 24.46 ? 574  TRP A NE1   1 
ATOM   4264  C  CE2   . TRP A  1  576  ? -38.843 81.175  115.937 1.00 24.89 ? 574  TRP A CE2   1 
ATOM   4265  C  CE3   . TRP A  1  576  ? -37.118 81.211  117.635 1.00 24.95 ? 574  TRP A CE3   1 
ATOM   4266  C  CZ2   . TRP A  1  576  ? -38.858 79.781  115.914 1.00 28.25 ? 574  TRP A CZ2   1 
ATOM   4267  C  CZ3   . TRP A  1  576  ? -37.132 79.828  117.613 1.00 27.84 ? 574  TRP A CZ3   1 
ATOM   4268  C  CH2   . TRP A  1  576  ? -38.001 79.125  116.759 1.00 27.13 ? 574  TRP A CH2   1 
ATOM   4269  N  N     . THR A  1  577  ? -36.186 85.455  120.084 1.00 27.47 ? 575  THR A N     1 
ATOM   4270  C  CA    . THR A  1  577  ? -35.263 86.428  120.644 1.00 25.60 ? 575  THR A CA    1 
ATOM   4271  C  C     . THR A  1  577  ? -33.866 85.834  120.685 1.00 28.60 ? 575  THR A C     1 
ATOM   4272  O  O     . THR A  1  577  ? -33.679 84.616  120.648 1.00 29.91 ? 575  THR A O     1 
ATOM   4273  C  CB    . THR A  1  577  ? -35.648 86.876  122.063 1.00 28.98 ? 575  THR A CB    1 
ATOM   4274  O  OG1   . THR A  1  577  ? -35.542 85.761  122.951 1.00 31.90 ? 575  THR A OG1   1 
ATOM   4275  C  CG2   . THR A  1  577  ? -37.065 87.440  122.109 1.00 33.15 ? 575  THR A CG2   1 
ATOM   4276  N  N     . ALA A  1  578  ? -32.881 86.720  120.759 1.00 27.05 ? 576  ALA A N     1 
ATOM   4277  C  CA    . ALA A  1  578  ? -31.496 86.337  120.969 1.00 24.39 ? 576  ALA A CA    1 
ATOM   4278  C  C     . ALA A  1  578  ? -30.934 87.299  121.995 1.00 30.79 ? 576  ALA A C     1 
ATOM   4279  O  O     . ALA A  1  578  ? -31.094 88.512  121.853 1.00 30.37 ? 576  ALA A O     1 
ATOM   4280  C  CB    . ALA A  1  578  ? -30.682 86.398  119.676 1.00 25.94 ? 576  ALA A CB    1 
ATOM   4281  N  N     . LEU A  1  579  ? -30.310 86.760  123.028 1.00 28.43 ? 577  LEU A N     1 
ATOM   4282  C  CA    . LEU A  1  579  ? -29.818 87.535  124.153 1.00 29.81 ? 577  LEU A CA    1 
ATOM   4283  C  C     . LEU A  1  579  ? -28.370 87.160  124.394 1.00 25.04 ? 577  LEU A C     1 
ATOM   4284  O  O     . LEU A  1  579  ? -27.934 86.072  124.007 1.00 27.06 ? 577  LEU A O     1 
ATOM   4285  C  CB    . LEU A  1  579  ? -30.631 87.258  125.426 1.00 29.04 ? 577  LEU A CB    1 
ATOM   4286  C  CG    . LEU A  1  579  ? -32.153 87.317  125.343 1.00 35.42 ? 577  LEU A CG    1 
ATOM   4287  C  CD1   . LEU A  1  579  ? -32.742 87.064  126.723 1.00 37.85 ? 577  LEU A CD1   1 
ATOM   4288  C  CD2   . LEU A  1  579  ? -32.600 88.660  124.798 1.00 38.40 ? 577  LEU A CD2   1 
ATOM   4289  N  N     . PRO A  1  580  ? -27.591 88.041  125.028 1.00 27.09 ? 578  PRO A N     1 
ATOM   4290  C  CA    . PRO A  1  580  ? -26.272 87.631  125.515 1.00 26.72 ? 578  PRO A CA    1 
ATOM   4291  C  C     . PRO A  1  580  ? -26.452 86.619  126.629 1.00 31.35 ? 578  PRO A C     1 
ATOM   4292  O  O     . PRO A  1  580  ? -26.899 86.975  127.723 1.00 33.63 ? 578  PRO A O     1 
ATOM   4293  C  CB    . PRO A  1  580  ? -25.654 88.937  126.034 1.00 27.35 ? 578  PRO A CB    1 
ATOM   4294  C  CG    . PRO A  1  580  ? -26.546 90.037  125.515 1.00 31.30 ? 578  PRO A CG    1 
ATOM   4295  C  CD    . PRO A  1  580  ? -27.896 89.434  125.383 1.00 30.38 ? 578  PRO A CD    1 
ATOM   4296  N  N     . GLN A  1  581  ? -26.161 85.355  126.350 1.00 25.98 ? 579  GLN A N     1 
ATOM   4297  C  CA    . GLN A  1  581  ? -26.381 84.269  127.299 1.00 30.12 ? 579  GLN A CA    1 
ATOM   4298  C  C     . GLN A  1  581  ? -25.035 83.967  127.933 1.00 30.67 ? 579  GLN A C     1 
ATOM   4299  O  O     . GLN A  1  581  ? -24.284 83.119  127.457 1.00 29.80 ? 579  GLN A O     1 
ATOM   4300  C  CB    . GLN A  1  581  ? -26.961 83.040  126.605 1.00 27.90 ? 579  GLN A CB    1 
ATOM   4301  C  CG    . GLN A  1  581  ? -28.333 83.252  125.998 1.00 27.01 ? 579  GLN A CG    1 
ATOM   4302  C  CD    . GLN A  1  581  ? -29.419 83.445  127.043 1.00 31.53 ? 579  GLN A CD    1 
ATOM   4303  O  OE1   . GLN A  1  581  ? -29.185 83.283  128.240 1.00 32.57 ? 579  GLN A OE1   1 
ATOM   4304  N  NE2   . GLN A  1  581  ? -30.615 83.797  126.591 1.00 33.09 ? 579  GLN A NE2   1 
ATOM   4305  N  N     . LEU A  1  582  ? -24.724 84.683  129.008 1.00 32.04 ? 580  LEU A N     1 
ATOM   4306  C  CA    . LEU A  1  582  ? -23.483 84.451  129.716 1.00 32.73 ? 580  LEU A CA    1 
ATOM   4307  C  C     . LEU A  1  582  ? -23.620 83.236  130.628 1.00 32.67 ? 580  LEU A C     1 
ATOM   4308  O  O     . LEU A  1  582  ? -24.715 82.706  130.844 1.00 33.60 ? 580  LEU A O     1 
ATOM   4309  C  CB    . LEU A  1  582  ? -23.085 85.691  130.511 1.00 30.16 ? 580  LEU A CB    1 
ATOM   4310  C  CG    . LEU A  1  582  ? -22.144 86.678  129.804 1.00 41.18 ? 580  LEU A CG    1 
ATOM   4311  C  CD1   . LEU A  1  582  ? -22.795 87.308  128.600 1.00 36.70 ? 580  LEU A CD1   1 
ATOM   4312  C  CD2   . LEU A  1  582  ? -21.692 87.754  130.768 1.00 40.24 ? 580  LEU A CD2   1 
ATOM   4313  N  N     . ALA A  1  583  ? -22.482 82.784  131.159 1.00 31.54 ? 581  ALA A N     1 
ATOM   4314  C  CA    . ALA A  1  583  ? -22.501 81.652  132.078 1.00 31.95 ? 581  ALA A CA    1 
ATOM   4315  C  C     . ALA A  1  583  ? -23.410 81.923  133.265 1.00 38.17 ? 581  ALA A C     1 
ATOM   4316  O  O     . ALA A  1  583  ? -24.020 80.995  133.808 1.00 43.69 ? 581  ALA A O     1 
ATOM   4317  C  CB    . ALA A  1  583  ? -21.087 81.346  132.564 1.00 33.49 ? 581  ALA A CB    1 
ATOM   4318  N  N     . THR A  1  584  ? -23.524 83.188  133.661 1.00 32.10 ? 582  THR A N     1 
ATOM   4319  C  CA    . THR A  1  584  ? -24.279 83.613  134.830 1.00 39.00 ? 582  THR A CA    1 
ATOM   4320  C  C     . THR A  1  584  ? -25.755 83.860  134.536 1.00 39.23 ? 582  THR A C     1 
ATOM   4321  O  O     . THR A  1  584  ? -26.528 84.084  135.475 1.00 42.90 ? 582  THR A O     1 
ATOM   4322  C  CB    . THR A  1  584  ? -23.663 84.894  135.401 1.00 43.89 ? 582  THR A CB    1 
ATOM   4323  O  OG1   . THR A  1  584  ? -23.553 85.872  134.357 1.00 43.06 ? 582  THR A OG1   1 
ATOM   4324  C  CG2   . THR A  1  584  ? -22.284 84.619  135.979 1.00 41.21 ? 582  THR A CG2   1 
ATOM   4325  N  N     . GLY A  1  585  ? -26.158 83.833  133.268 1.00 36.92 ? 583  GLY A N     1 
ATOM   4326  C  CA    . GLY A  1  585  ? -27.520 84.114  132.886 1.00 34.07 ? 583  GLY A CA    1 
ATOM   4327  C  C     . GLY A  1  585  ? -27.586 85.122  131.757 1.00 40.12 ? 583  GLY A C     1 
ATOM   4328  O  O     . GLY A  1  585  ? -26.561 85.633  131.294 1.00 37.99 ? 583  GLY A O     1 
ATOM   4329  N  N     . PRO A  1  586  ? -28.796 85.426  131.287 1.00 40.24 ? 584  PRO A N     1 
ATOM   4330  C  CA    . PRO A  1  586  ? -28.940 86.439  130.237 1.00 30.89 ? 584  PRO A CA    1 
ATOM   4331  C  C     . PRO A  1  586  ? -28.463 87.792  130.741 1.00 40.59 ? 584  PRO A C     1 
ATOM   4332  O  O     . PRO A  1  586  ? -28.631 88.130  131.914 1.00 40.83 ? 584  PRO A O     1 
ATOM   4333  C  CB    . PRO A  1  586  ? -30.448 86.449  129.947 1.00 42.29 ? 584  PRO A CB    1 
ATOM   4334  C  CG    . PRO A  1  586  ? -31.016 85.260  130.674 1.00 40.18 ? 584  PRO A CG    1 
ATOM   4335  C  CD    . PRO A  1  586  ? -30.095 84.957  131.795 1.00 42.66 ? 584  PRO A CD    1 
ATOM   4336  N  N     . ALA A  1  587  ? -27.856 88.565  129.849 1.00 36.73 ? 585  ALA A N     1 
ATOM   4337  C  CA    . ALA A  1  587  ? -27.363 89.891  130.192 1.00 37.32 ? 585  ALA A CA    1 
ATOM   4338  C  C     . ALA A  1  587  ? -28.180 90.960  129.481 1.00 38.64 ? 585  ALA A C     1 
ATOM   4339  O  O     . ALA A  1  587  ? -28.791 90.709  128.439 1.00 40.93 ? 585  ALA A O     1 
ATOM   4340  C  CB    . ALA A  1  587  ? -25.883 90.045  129.831 1.00 38.49 ? 585  ALA A CB    1 
ATOM   4341  N  N     . ALA A  1  588  ? -28.200 92.156  130.068 1.00 36.41 ? 586  ALA A N     1 
ATOM   4342  C  CA    . ALA A  1  588  ? -28.874 93.281  129.443 1.00 38.47 ? 586  ALA A CA    1 
ATOM   4343  C  C     . ALA A  1  588  ? -28.007 93.867  128.336 1.00 38.15 ? 586  ALA A C     1 
ATOM   4344  O  O     . ALA A  1  588  ? -26.784 93.706  128.314 1.00 40.90 ? 586  ALA A O     1 
ATOM   4345  C  CB    . ALA A  1  588  ? -29.194 94.364  130.474 1.00 40.50 ? 586  ALA A CB    1 
ATOM   4346  N  N     . GLY A  1  589  ? -28.656 94.559  127.411 1.00 35.93 ? 587  GLY A N     1 
ATOM   4347  C  CA    . GLY A  1  589  ? -27.928 95.203  126.335 1.00 34.29 ? 587  GLY A CA    1 
ATOM   4348  C  C     . GLY A  1  589  ? -28.877 95.967  125.442 1.00 40.66 ? 587  GLY A C     1 
ATOM   4349  O  O     . GLY A  1  589  ? -30.075 96.087  125.721 1.00 41.80 ? 587  GLY A O     1 
ATOM   4350  N  N     . GLU A  1  590  ? -28.312 96.496  124.359 1.00 39.81 ? 588  GLU A N     1 
ATOM   4351  C  CA    . GLU A  1  590  ? -29.100 97.225  123.373 1.00 42.96 ? 588  GLU A CA    1 
ATOM   4352  C  C     . GLU A  1  590  ? -29.924 96.241  122.553 1.00 37.40 ? 588  GLU A C     1 
ATOM   4353  O  O     . GLU A  1  590  ? -29.375 95.308  121.956 1.00 38.29 ? 588  GLU A O     1 
ATOM   4354  C  CB    . GLU A  1  590  ? -28.184 98.047  122.468 1.00 43.68 ? 588  GLU A CB    1 
ATOM   4355  N  N     . THR A  1  591  ? -31.237 96.455  122.514 1.00 33.97 ? 589  THR A N     1 
ATOM   4356  C  CA    . THR A  1  591  ? -32.172 95.547  121.858 1.00 34.55 ? 589  THR A CA    1 
ATOM   4357  C  C     . THR A  1  591  ? -32.709 96.177  120.578 1.00 33.13 ? 589  THR A C     1 
ATOM   4358  O  O     . THR A  1  591  ? -33.096 97.350  120.571 1.00 37.67 ? 589  THR A O     1 
ATOM   4359  C  CB    . THR A  1  591  ? -33.330 95.193  122.798 1.00 33.59 ? 589  THR A CB    1 
ATOM   4360  O  OG1   . THR A  1  591  ? -32.812 94.643  124.018 1.00 34.61 ? 589  THR A OG1   1 
ATOM   4361  C  CG2   . THR A  1  591  ? -34.261 94.181  122.145 1.00 35.00 ? 589  THR A CG2   1 
ATOM   4362  N  N     . ARG A  1  592  ? -32.746 95.394  119.499 1.00 31.12 ? 590  ARG A N     1 
ATOM   4363  C  CA    . ARG A  1  592  ? -33.317 95.855  118.245 1.00 30.98 ? 590  ARG A CA    1 
ATOM   4364  C  C     . ARG A  1  592  ? -34.054 94.703  117.575 1.00 30.22 ? 590  ARG A C     1 
ATOM   4365  O  O     . ARG A  1  592  ? -33.881 93.534  117.931 1.00 30.95 ? 590  ARG A O     1 
ATOM   4366  C  CB    . ARG A  1  592  ? -32.245 96.421  117.310 1.00 34.25 ? 590  ARG A CB    1 
ATOM   4367  C  CG    . ARG A  1  592  ? -31.264 95.374  116.826 1.00 35.89 ? 590  ARG A CG    1 
ATOM   4368  C  CD    . ARG A  1  592  ? -30.552 95.811  115.556 1.00 41.30 ? 590  ARG A CD    1 
ATOM   4369  N  NE    . ARG A  1  592  ? -29.492 94.877  115.198 1.00 42.18 ? 590  ARG A NE    1 
ATOM   4370  C  CZ    . ARG A  1  592  ? -29.667 93.791  114.458 1.00 39.47 ? 590  ARG A CZ    1 
ATOM   4371  N  NH1   . ARG A  1  592  ? -30.847 93.486  113.946 1.00 35.52 ? 590  ARG A NH1   1 
ATOM   4372  N  NH2   . ARG A  1  592  ? -28.632 92.987  114.232 1.00 39.82 ? 590  ARG A NH2   1 
ATOM   4373  N  N     . THR A  1  593  ? -34.886 95.044  116.596 1.00 30.40 ? 591  THR A N     1 
ATOM   4374  C  CA    . THR A  1  593  ? -35.626 94.020  115.882 1.00 30.17 ? 591  THR A CA    1 
ATOM   4375  C  C     . THR A  1  593  ? -34.754 93.369  114.810 1.00 32.40 ? 591  THR A C     1 
ATOM   4376  O  O     . THR A  1  593  ? -33.757 93.930  114.344 1.00 31.46 ? 591  THR A O     1 
ATOM   4377  C  CB    . THR A  1  593  ? -36.884 94.593  115.229 1.00 34.81 ? 591  THR A CB    1 
ATOM   4378  O  OG1   . THR A  1  593  ? -36.525 95.690  114.381 1.00 35.01 ? 591  THR A OG1   1 
ATOM   4379  C  CG2   . THR A  1  593  ? -37.882 95.060  116.286 1.00 36.30 ? 591  THR A CG2   1 
ATOM   4380  N  N     . VAL A  1  594  ? -35.143 92.157  114.435 1.00 24.52 ? 592  VAL A N     1 
ATOM   4381  C  CA    . VAL A  1  594  ? -34.555 91.435  113.313 1.00 26.32 ? 592  VAL A CA    1 
ATOM   4382  C  C     . VAL A  1  594  ? -35.620 91.352  112.233 1.00 26.69 ? 592  VAL A C     1 
ATOM   4383  O  O     . VAL A  1  594  ? -36.730 90.872  112.489 1.00 27.84 ? 592  VAL A O     1 
ATOM   4384  C  CB    . VAL A  1  594  ? -34.070 90.032  113.723 1.00 24.76 ? 592  VAL A CB    1 
ATOM   4385  C  CG1   . VAL A  1  594  ? -33.574 89.260  112.503 1.00 26.96 ? 592  VAL A CG1   1 
ATOM   4386  C  CG2   . VAL A  1  594  ? -32.968 90.126  114.774 1.00 26.80 ? 592  VAL A CG2   1 
ATOM   4387  N  N     . LEU A  1  595  ? -35.298 91.833  111.036 1.00 27.14 ? 593  LEU A N     1 
ATOM   4388  C  CA    . LEU A  1  595  ? -36.276 91.923  109.962 1.00 25.25 ? 593  LEU A CA    1 
ATOM   4389  C  C     . LEU A  1  595  ? -36.003 90.877  108.891 1.00 25.24 ? 593  LEU A C     1 
ATOM   4390  O  O     . LEU A  1  595  ? -34.853 90.501  108.640 1.00 26.84 ? 593  LEU A O     1 
ATOM   4391  C  CB    . LEU A  1  595  ? -36.270 93.322  109.331 1.00 26.53 ? 593  LEU A CB    1 
ATOM   4392  C  CG    . LEU A  1  595  ? -36.450 94.482  110.307 1.00 32.29 ? 593  LEU A CG    1 
ATOM   4393  C  CD1   . LEU A  1  595  ? -36.465 95.817  109.568 1.00 32.81 ? 593  LEU A CD1   1 
ATOM   4394  C  CD2   . LEU A  1  595  ? -37.722 94.288  111.116 1.00 27.75 ? 593  LEU A CD2   1 
ATOM   4395  N  N     . ASN A  1  596  ? -37.080 90.405  108.271 1.00 24.96 ? 594  ASN A N     1 
ATOM   4396  C  CA    . ASN A  1  596  ? -36.990 89.485  107.143 1.00 23.90 ? 594  ASN A CA    1 
ATOM   4397  C  C     . ASN A  1  596  ? -36.316 90.197  105.979 1.00 23.96 ? 594  ASN A C     1 
ATOM   4398  O  O     . ASN A  1  596  ? -36.833 91.225  105.515 1.00 23.39 ? 594  ASN A O     1 
ATOM   4399  C  CB    . ASN A  1  596  ? -38.407 89.021  106.772 1.00 22.85 ? 594  ASN A CB    1 
ATOM   4400  C  CG    . ASN A  1  596  ? -38.438 87.974  105.670 1.00 23.16 ? 594  ASN A CG    1 
ATOM   4401  O  OD1   . ASN A  1  596  ? -37.545 87.890  104.830 1.00 23.76 ? 594  ASN A OD1   1 
ATOM   4402  N  ND2   . ASN A  1  596  ? -39.493 87.165  105.672 1.00 25.87 ? 594  ASN A ND2   1 
ATOM   4403  N  N     . PRO A  1  597  ? -35.179 89.705  105.479 1.00 23.73 ? 595  PRO A N     1 
ATOM   4404  C  CA    . PRO A  1  597  ? -34.510 90.404  104.370 1.00 20.24 ? 595  PRO A CA    1 
ATOM   4405  C  C     . PRO A  1  597  ? -35.355 90.479  103.113 1.00 22.54 ? 595  PRO A C     1 
ATOM   4406  O  O     . PRO A  1  597  ? -35.126 91.363  102.279 1.00 22.55 ? 595  PRO A O     1 
ATOM   4407  C  CB    . PRO A  1  597  ? -33.228 89.584  104.147 1.00 24.39 ? 595  PRO A CB    1 
ATOM   4408  C  CG    . PRO A  1  597  ? -33.499 88.264  104.770 1.00 26.89 ? 595  PRO A CG    1 
ATOM   4409  C  CD    . PRO A  1  597  ? -34.421 88.520  105.922 1.00 20.52 ? 595  PRO A CD    1 
ATOM   4410  N  N     . GLY A  1  598  ? -36.345 89.607  102.966 1.00 20.53 ? 596  GLY A N     1 
ATOM   4411  C  CA    . GLY A  1  598  ? -37.209 89.655  101.804 1.00 21.48 ? 596  GLY A CA    1 
ATOM   4412  C  C     . GLY A  1  598  ? -38.400 90.566  101.937 1.00 23.88 ? 596  GLY A C     1 
ATOM   4413  O  O     . GLY A  1  598  ? -39.139 90.757  100.967 1.00 25.18 ? 596  GLY A O     1 
ATOM   4414  N  N     . ASP A  1  599  ? -38.591 91.146  103.118 1.00 24.21 ? 597  ASP A N     1 
ATOM   4415  C  CA    . ASP A  1  599  ? -39.722 92.019  103.405 1.00 22.48 ? 597  ASP A CA    1 
ATOM   4416  C  C     . ASP A  1  599  ? -39.512 92.604  104.787 1.00 25.42 ? 597  ASP A C     1 
ATOM   4417  O  O     . ASP A  1  599  ? -39.830 91.957  105.791 1.00 24.03 ? 597  ASP A O     1 
ATOM   4418  C  CB    . ASP A  1  599  ? -41.036 91.250  103.342 1.00 22.05 ? 597  ASP A CB    1 
ATOM   4419  C  CG    . ASP A  1  599  ? -42.261 92.149  103.463 1.00 27.48 ? 597  ASP A CG    1 
ATOM   4420  O  OD1   . ASP A  1  599  ? -42.132 93.316  103.898 1.00 28.77 ? 597  ASP A OD1   1 
ATOM   4421  O  OD2   . ASP A  1  599  ? -43.359 91.664  103.118 1.00 32.43 ? 597  ASP A OD2   1 
ATOM   4422  N  N     . HIS A  1  600  ? -38.966 93.820  104.838 1.00 24.09 ? 598  HIS A N     1 
ATOM   4423  C  CA    . HIS A  1  600  ? -38.597 94.438  106.104 1.00 30.04 ? 598  HIS A CA    1 
ATOM   4424  C  C     . HIS A  1  600  ? -39.799 94.737  106.988 1.00 28.82 ? 598  HIS A C     1 
ATOM   4425  O  O     . HIS A  1  600  ? -39.617 95.004  108.182 1.00 31.29 ? 598  HIS A O     1 
ATOM   4426  C  CB    . HIS A  1  600  ? -37.801 95.708  105.833 1.00 30.52 ? 598  HIS A CB    1 
ATOM   4427  C  CG    . HIS A  1  600  ? -36.413 95.443  105.344 1.00 29.42 ? 598  HIS A CG    1 
ATOM   4428  N  ND1   . HIS A  1  600  ? -35.540 96.447  104.983 1.00 29.83 ? 598  HIS A ND1   1 
ATOM   4429  C  CD2   . HIS A  1  600  ? -35.744 94.278  105.159 1.00 26.83 ? 598  HIS A CD2   1 
ATOM   4430  C  CE1   . HIS A  1  600  ? -34.393 95.914  104.600 1.00 32.34 ? 598  HIS A CE1   1 
ATOM   4431  N  NE2   . HIS A  1  600  ? -34.488 94.599  104.701 1.00 30.59 ? 598  HIS A NE2   1 
ATOM   4432  N  N     . ARG A  1  601  ? -41.010 94.682  106.438 1.00 26.74 ? 599  ARG A N     1 
ATOM   4433  C  CA    . ARG A  1  601  ? -42.209 94.812  107.255 1.00 28.43 ? 599  ARG A CA    1 
ATOM   4434  C  C     . ARG A  1  601  ? -42.426 93.596  108.146 1.00 30.97 ? 599  ARG A C     1 
ATOM   4435  O  O     . ARG A  1  601  ? -43.157 93.690  109.137 1.00 31.64 ? 599  ARG A O     1 
ATOM   4436  C  CB    . ARG A  1  601  ? -43.424 95.022  106.354 1.00 29.51 ? 599  ARG A CB    1 
ATOM   4437  C  CG    . ARG A  1  601  ? -43.278 96.183  105.395 1.00 30.31 ? 599  ARG A CG    1 
ATOM   4438  C  CD    . ARG A  1  601  ? -44.375 96.168  104.358 1.00 31.35 ? 599  ARG A CD    1 
ATOM   4439  N  NE    . ARG A  1  601  ? -44.393 94.911  103.620 1.00 29.44 ? 599  ARG A NE    1 
ATOM   4440  C  CZ    . ARG A  1  601  ? -45.294 94.601  102.699 1.00 32.48 ? 599  ARG A CZ    1 
ATOM   4441  N  NH1   . ARG A  1  601  ? -46.270 95.440  102.372 1.00 35.52 ? 599  ARG A NH1   1 
ATOM   4442  N  NH2   . ARG A  1  601  ? -45.223 93.421  102.094 1.00 30.47 ? 599  ARG A NH2   1 
ATOM   4443  N  N     . ASP A  1  602  ? -41.807 92.466  107.816 1.00 27.49 ? 600  ASP A N     1 
ATOM   4444  C  CA    . ASP A  1  602  ? -41.985 91.226  108.557 1.00 30.56 ? 600  ASP A CA    1 
ATOM   4445  C  C     . ASP A  1  602  ? -40.926 91.191  109.648 1.00 32.62 ? 600  ASP A C     1 
ATOM   4446  O  O     . ASP A  1  602  ? -39.745 90.964  109.380 1.00 29.01 ? 600  ASP A O     1 
ATOM   4447  C  CB    . ASP A  1  602  ? -41.878 90.026  107.619 1.00 27.93 ? 600  ASP A CB    1 
ATOM   4448  C  CG    . ASP A  1  602  ? -42.010 88.705  108.342 1.00 33.78 ? 600  ASP A CG    1 
ATOM   4449  O  OD1   . ASP A  1  602  ? -42.571 88.699  109.453 1.00 31.18 ? 600  ASP A OD1   1 
ATOM   4450  O  OD2   . ASP A  1  602  ? -41.539 87.675  107.801 1.00 28.46 ? 600  ASP A OD2   1 
ATOM   4451  N  N     . VAL A  1  603  ? -41.343 91.436  110.882 1.00 28.42 ? 601  VAL A N     1 
ATOM   4452  C  CA    . VAL A  1  603  ? -40.423 91.401  112.010 1.00 28.08 ? 601  VAL A CA    1 
ATOM   4453  C  C     . VAL A  1  603  ? -40.308 89.958  112.474 1.00 30.42 ? 601  VAL A C     1 
ATOM   4454  O  O     . VAL A  1  603  ? -41.313 89.320  112.805 1.00 30.28 ? 601  VAL A O     1 
ATOM   4455  C  CB    . VAL A  1  603  ? -40.905 92.317  113.143 1.00 29.82 ? 601  VAL A CB    1 
ATOM   4456  C  CG1   . VAL A  1  603  ? -39.904 92.314  114.293 1.00 31.24 ? 601  VAL A CG1   1 
ATOM   4457  C  CG2   . VAL A  1  603  ? -41.104 93.723  112.617 1.00 36.88 ? 601  VAL A CG2   1 
ATOM   4458  N  N     . VAL A  1  604  ? -39.089 89.435  112.482 1.00 26.13 ? 602  VAL A N     1 
ATOM   4459  C  CA    . VAL A  1  604  ? -38.889 88.033  112.826 1.00 23.86 ? 602  VAL A CA    1 
ATOM   4460  C  C     . VAL A  1  604  ? -38.636 87.860  114.315 1.00 26.33 ? 602  VAL A C     1 
ATOM   4461  O  O     . VAL A  1  604  ? -39.086 86.878  114.910 1.00 27.33 ? 602  VAL A O     1 
ATOM   4462  C  CB    . VAL A  1  604  ? -37.741 87.442  111.991 1.00 25.00 ? 602  VAL A CB    1 
ATOM   4463  C  CG1   . VAL A  1  604  ? -37.564 85.972  112.313 1.00 25.26 ? 602  VAL A CG1   1 
ATOM   4464  C  CG2   . VAL A  1  604  ? -38.029 87.649  110.498 1.00 24.74 ? 602  VAL A CG2   1 
ATOM   4465  N  N     . GLY A  1  605  ? -37.948 88.802  114.937 1.00 27.53 ? 603  GLY A N     1 
ATOM   4466  C  CA    . GLY A  1  605  ? -37.715 88.714  116.359 1.00 26.44 ? 603  GLY A CA    1 
ATOM   4467  C  C     . GLY A  1  605  ? -36.919 89.896  116.844 1.00 29.19 ? 603  GLY A C     1 
ATOM   4468  O  O     . GLY A  1  605  ? -36.839 90.928  116.178 1.00 28.94 ? 603  GLY A O     1 
ATOM   4469  N  N     . SER A  1  606  ? -36.321 89.730  118.015 1.00 27.27 ? 604  SER A N     1 
ATOM   4470  C  CA    . SER A  1  606  ? -35.573 90.796  118.658 1.00 27.91 ? 604  SER A CA    1 
ATOM   4471  C  C     . SER A  1  606  ? -34.253 90.241  119.151 1.00 28.94 ? 604  SER A C     1 
ATOM   4472  O  O     . SER A  1  606  ? -34.192 89.118  119.660 1.00 30.71 ? 604  SER A O     1 
ATOM   4473  C  CB    . SER A  1  606  ? -36.344 91.396  119.831 1.00 32.11 ? 604  SER A CB    1 
ATOM   4474  O  OG    . SER A  1  606  ? -37.467 92.128  119.372 1.00 45.52 ? 604  SER A OG    1 
ATOM   4475  N  N     . VAL A  1  607  ? -33.194 91.023  118.995 1.00 26.88 ? 605  VAL A N     1 
ATOM   4476  C  CA    . VAL A  1  607  ? -31.878 90.626  119.467 1.00 27.22 ? 605  VAL A CA    1 
ATOM   4477  C  C     . VAL A  1  607  ? -31.389 91.657  120.469 1.00 27.12 ? 605  VAL A C     1 
ATOM   4478  O  O     . VAL A  1  607  ? -31.477 92.866  120.224 1.00 29.91 ? 605  VAL A O     1 
ATOM   4479  C  CB    . VAL A  1  607  ? -30.870 90.465  118.315 1.00 27.94 ? 605  VAL A CB    1 
ATOM   4480  C  CG1   . VAL A  1  607  ? -30.822 91.715  117.434 1.00 27.41 ? 605  VAL A CG1   1 
ATOM   4481  C  CG2   . VAL A  1  607  ? -29.499 90.150  118.877 1.00 26.93 ? 605  VAL A CG2   1 
ATOM   4482  N  N     . THR A  1  608  ? -30.895 91.175  121.602 1.00 28.38 ? 606  THR A N     1 
ATOM   4483  C  CA    . THR A  1  608  ? -30.196 92.006  122.568 1.00 30.64 ? 606  THR A CA    1 
ATOM   4484  C  C     . THR A  1  608  ? -28.711 91.755  122.372 1.00 30.24 ? 606  THR A C     1 
ATOM   4485  O  O     . THR A  1  608  ? -28.252 90.615  122.490 1.00 29.53 ? 606  THR A O     1 
ATOM   4486  C  CB    . THR A  1  608  ? -30.628 91.668  123.993 1.00 30.68 ? 606  THR A CB    1 
ATOM   4487  O  OG1   . THR A  1  608  ? -32.037 91.889  124.118 1.00 32.89 ? 606  THR A OG1   1 
ATOM   4488  C  CG2   . THR A  1  608  ? -29.895 92.539  124.991 1.00 30.87 ? 606  THR A CG2   1 
ATOM   4489  N  N     . GLU A  1  609  ? -27.972 92.805  122.047 1.00 33.64 ? 607  GLU A N     1 
ATOM   4490  C  CA    . GLU A  1  609  ? -26.582 92.650  121.659 1.00 33.83 ? 607  GLU A CA    1 
ATOM   4491  C  C     . GLU A  1  609  ? -25.660 92.846  122.854 1.00 31.98 ? 607  GLU A C     1 
ATOM   4492  O  O     . GLU A  1  609  ? -26.005 93.510  123.835 1.00 32.07 ? 607  GLU A O     1 
ATOM   4493  C  CB    . GLU A  1  609  ? -26.246 93.608  120.514 1.00 35.31 ? 607  GLU A CB    1 
ATOM   4494  C  CG    . GLU A  1  609  ? -27.020 93.214  119.249 1.00 40.69 ? 607  GLU A CG    1 
ATOM   4495  C  CD    . GLU A  1  609  ? -26.551 93.922  117.995 1.00 50.39 ? 607  GLU A CD    1 
ATOM   4496  O  OE1   . GLU A  1  609  ? -26.248 95.133  118.076 1.00 51.57 ? 607  GLU A OE1   1 
ATOM   4497  O  OE2   . GLU A  1  609  ? -26.494 93.259  116.929 1.00 39.48 ? 607  GLU A OE2   1 
ATOM   4498  N  N     . THR A  1  610  ? -24.491 92.226  122.765 1.00 28.80 ? 608  THR A N     1 
ATOM   4499  C  CA    . THR A  1  610  ? -23.564 92.141  123.885 1.00 30.75 ? 608  THR A CA    1 
ATOM   4500  C  C     . THR A  1  610  ? -22.704 93.393  123.954 1.00 33.40 ? 608  THR A C     1 
ATOM   4501  O  O     . THR A  1  610  ? -22.177 93.846  122.936 1.00 34.12 ? 608  THR A O     1 
ATOM   4502  C  CB    . THR A  1  610  ? -22.670 90.913  123.714 1.00 28.92 ? 608  THR A CB    1 
ATOM   4503  O  OG1   . THR A  1  610  ? -23.473 89.782  123.350 1.00 28.03 ? 608  THR A OG1   1 
ATOM   4504  C  CG2   . THR A  1  610  ? -21.892 90.607  124.986 1.00 34.75 ? 608  THR A CG2   1 
ATOM   4505  N  N     . SER A  1  611  ? -22.547 93.938  125.157 1.00 34.38 ? 609  SER A N     1 
ATOM   4506  C  CA    . SER A  1  611  ? -21.574 94.997  125.367 1.00 37.33 ? 609  SER A CA    1 
ATOM   4507  C  C     . SER A  1  611  ? -20.160 94.430  125.305 1.00 36.18 ? 609  SER A C     1 
ATOM   4508  O  O     . SER A  1  611  ? -19.927 93.245  125.563 1.00 33.81 ? 609  SER A O     1 
ATOM   4509  C  CB    . SER A  1  611  ? -21.796 95.666  126.718 1.00 36.47 ? 609  SER A CB    1 
ATOM   4510  O  OG    . SER A  1  611  ? -21.343 94.813  127.752 1.00 36.61 ? 609  SER A OG    1 
ATOM   4511  N  N     . GLU A  1  612  ? -19.204 95.296  124.961 1.00 38.77 ? 610  GLU A N     1 
ATOM   4512  C  CA    . GLU A  1  612  ? -17.811 94.863  124.946 1.00 39.77 ? 610  GLU A CA    1 
ATOM   4513  C  C     . GLU A  1  612  ? -17.372 94.404  126.328 1.00 35.44 ? 610  GLU A C     1 
ATOM   4514  O  O     . GLU A  1  612  ? -16.616 93.434  126.455 1.00 34.40 ? 610  GLU A O     1 
ATOM   4515  C  CB    . GLU A  1  612  ? -16.909 95.986  124.432 1.00 45.76 ? 610  GLU A CB    1 
ATOM   4516  C  CG    . GLU A  1  612  ? -17.075 96.252  122.940 1.00 55.07 ? 610  GLU A CG    1 
ATOM   4517  C  CD    . GLU A  1  612  ? -15.978 97.125  122.360 1.00 61.89 ? 610  GLU A CD    1 
ATOM   4518  O  OE1   . GLU A  1  612  ? -14.972 97.378  123.062 1.00 64.23 ? 610  GLU A OE1   1 
ATOM   4519  O  OE2   . GLU A  1  612  ? -16.123 97.556  121.195 1.00 59.49 ? 610  GLU A OE2   1 
ATOM   4520  N  N     . GLU A  1  613  ? -17.861 95.071  127.378 1.00 34.61 ? 611  GLU A N     1 
ATOM   4521  C  CA    . GLU A  1  613  ? -17.545 94.641  128.736 1.00 36.83 ? 611  GLU A CA    1 
ATOM   4522  C  C     . GLU A  1  613  ? -18.027 93.217  128.981 1.00 33.17 ? 611  GLU A C     1 
ATOM   4523  O  O     . GLU A  1  613  ? -17.289 92.392  129.529 1.00 32.41 ? 611  GLU A O     1 
ATOM   4524  C  CB    . GLU A  1  613  ? -18.160 95.603  129.758 1.00 40.75 ? 611  GLU A CB    1 
ATOM   4525  N  N     . ASP A  1  614  ? -19.257 92.903  128.559 1.00 36.41 ? 612  ASP A N     1 
ATOM   4526  C  CA    . ASP A  1  614  ? -19.794 91.569  128.809 1.00 30.81 ? 612  ASP A CA    1 
ATOM   4527  C  C     . ASP A  1  614  ? -19.120 90.512  127.947 1.00 32.75 ? 612  ASP A C     1 
ATOM   4528  O  O     . ASP A  1  614  ? -18.992 89.361  128.375 1.00 30.95 ? 612  ASP A O     1 
ATOM   4529  C  CB    . ASP A  1  614  ? -21.307 91.552  128.594 1.00 31.11 ? 612  ASP A CB    1 
ATOM   4530  C  CG    . ASP A  1  614  ? -22.058 92.151  129.770 1.00 36.23 ? 612  ASP A CG    1 
ATOM   4531  O  OD1   . ASP A  1  614  ? -21.461 92.241  130.860 1.00 39.47 ? 612  ASP A OD1   1 
ATOM   4532  O  OD2   . ASP A  1  614  ? -23.237 92.521  129.604 1.00 39.33 ? 612  ASP A OD2   1 
ATOM   4533  N  N     . ALA A  1  615  ? -18.680 90.871  126.741 1.00 28.65 ? 613  ALA A N     1 
ATOM   4534  C  CA    . ALA A  1  615  ? -17.924 89.915  125.938 1.00 31.75 ? 613  ALA A CA    1 
ATOM   4535  C  C     . ALA A  1  615  ? -16.629 89.526  126.640 1.00 33.25 ? 613  ALA A C     1 
ATOM   4536  O  O     . ALA A  1  615  ? -16.286 88.343  126.713 1.00 30.99 ? 613  ALA A O     1 
ATOM   4537  C  CB    . ALA A  1  615  ? -17.635 90.490  124.554 1.00 29.68 ? 613  ALA A CB    1 
ATOM   4538  N  N     . ARG A  1  616  ? -15.910 90.510  127.185 1.00 34.25 ? 614  ARG A N     1 
ATOM   4539  C  CA    . ARG A  1  616  ? -14.699 90.200  127.937 1.00 35.90 ? 614  ARG A CA    1 
ATOM   4540  C  C     . ARG A  1  616  ? -15.019 89.416  129.205 1.00 31.43 ? 614  ARG A C     1 
ATOM   4541  O  O     . ARG A  1  616  ? -14.282 88.491  129.568 1.00 31.13 ? 614  ARG A O     1 
ATOM   4542  C  CB    . ARG A  1  616  ? -13.945 91.490  128.260 1.00 37.26 ? 614  ARG A CB    1 
ATOM   4543  C  CG    . ARG A  1  616  ? -13.508 92.251  127.011 1.00 43.78 ? 614  ARG A CG    1 
ATOM   4544  C  CD    . ARG A  1  616  ? -12.587 93.406  127.342 1.00 46.37 ? 614  ARG A CD    1 
ATOM   4545  N  NE    . ARG A  1  616  ? -13.158 94.260  128.373 1.00 51.28 ? 614  ARG A NE    1 
ATOM   4546  C  CZ    . ARG A  1  616  ? -13.806 95.392  128.139 1.00 53.75 ? 614  ARG A CZ    1 
ATOM   4547  N  NH1   . ARG A  1  616  ? -13.977 95.848  126.908 1.00 45.67 ? 614  ARG A NH1   1 
ATOM   4548  N  NH2   . ARG A  1  616  ? -14.288 96.088  129.166 1.00 52.40 ? 614  ARG A NH2   1 
ATOM   4549  N  N     . ARG A  1  617  ? -16.120 89.758  129.887 1.00 29.12 ? 615  ARG A N     1 
ATOM   4550  C  CA    . ARG A  1  617  ? -16.523 88.974  131.049 1.00 30.77 ? 615  ARG A CA    1 
ATOM   4551  C  C     . ARG A  1  617  ? -16.833 87.533  130.658 1.00 30.76 ? 615  ARG A C     1 
ATOM   4552  O  O     . ARG A  1  617  ? -16.517 86.597  131.400 1.00 30.37 ? 615  ARG A O     1 
ATOM   4553  C  CB    . ARG A  1  617  ? -17.730 89.618  131.733 1.00 33.21 ? 615  ARG A CB    1 
ATOM   4554  C  CG    . ARG A  1  617  ? -18.188 88.878  132.976 1.00 41.67 ? 615  ARG A CG    1 
ATOM   4555  C  CD    . ARG A  1  617  ? -18.912 89.801  133.943 1.00 47.73 ? 615  ARG A CD    1 
ATOM   4556  N  NE    . ARG A  1  617  ? -20.192 90.255  133.415 1.00 47.60 ? 615  ARG A NE    1 
ATOM   4557  C  CZ    . ARG A  1  617  ? -21.347 89.633  133.618 1.00 56.37 ? 615  ARG A CZ    1 
ATOM   4558  N  NH1   . ARG A  1  617  ? -21.413 88.511  134.321 1.00 49.45 ? 615  ARG A NH1   1 
ATOM   4559  N  NH2   . ARG A  1  617  ? -22.463 90.150  133.107 1.00 47.73 ? 615  ARG A NH2   1 
ATOM   4560  N  N     . ALA A  1  618  ? -17.448 87.334  129.491 1.00 30.46 ? 616  ALA A N     1 
ATOM   4561  C  CA    . ALA A  1  618  ? -17.806 85.983  129.072 1.00 27.96 ? 616  ALA A CA    1 
ATOM   4562  C  C     . ALA A  1  618  ? -16.568 85.115  128.881 1.00 27.26 ? 616  ALA A C     1 
ATOM   4563  O  O     . ALA A  1  618  ? -16.567 83.935  129.252 1.00 27.07 ? 616  ALA A O     1 
ATOM   4564  C  CB    . ALA A  1  618  ? -18.640 86.035  127.791 1.00 25.48 ? 616  ALA A CB    1 
ATOM   4565  N  N     . VAL A  1  619  ? -15.500 85.679  128.306 1.00 26.96 ? 617  VAL A N     1 
ATOM   4566  C  CA    . VAL A  1  619  ? -14.267 84.911  128.150 1.00 26.53 ? 617  VAL A CA    1 
ATOM   4567  C  C     . VAL A  1  619  ? -13.719 84.504  129.511 1.00 28.85 ? 617  VAL A C     1 
ATOM   4568  O  O     . VAL A  1  619  ? -13.298 83.356  129.706 1.00 28.33 ? 617  VAL A O     1 
ATOM   4569  C  CB    . VAL A  1  619  ? -13.229 85.702  127.333 1.00 29.88 ? 617  VAL A CB    1 
ATOM   4570  C  CG1   . VAL A  1  619  ? -11.942 84.892  127.198 1.00 31.29 ? 617  VAL A CG1   1 
ATOM   4571  C  CG2   . VAL A  1  619  ? -13.790 86.049  125.953 1.00 30.35 ? 617  VAL A CG2   1 
ATOM   4572  N  N     . ARG A  1  620  ? -13.714 85.430  130.475 1.00 29.43 ? 618  ARG A N     1 
ATOM   4573  C  CA    . ARG A  1  620  ? -13.215 85.087  131.803 1.00 30.20 ? 618  ARG A CA    1 
ATOM   4574  C  C     . ARG A  1  620  ? -14.059 83.988  132.437 1.00 29.97 ? 618  ARG A C     1 
ATOM   4575  O  O     . ARG A  1  620  ? -13.521 83.075  133.074 1.00 33.63 ? 618  ARG A O     1 
ATOM   4576  C  CB    . ARG A  1  620  ? -13.174 86.326  132.701 1.00 31.26 ? 618  ARG A CB    1 
ATOM   4577  N  N     . LEU A  1  621  ? -15.379 84.038  132.246 1.00 27.10 ? 619  LEU A N     1 
ATOM   4578  C  CA    . LEU A  1  621  ? -16.241 82.982  132.772 1.00 31.49 ? 619  LEU A CA    1 
ATOM   4579  C  C     . LEU A  1  621  ? -15.969 81.653  132.074 1.00 29.80 ? 619  LEU A C     1 
ATOM   4580  O  O     . LEU A  1  621  ? -15.973 80.597  132.719 1.00 31.92 ? 619  LEU A O     1 
ATOM   4581  C  CB    . LEU A  1  621  ? -17.709 83.370  132.618 1.00 28.09 ? 619  LEU A CB    1 
ATOM   4582  C  CG    . LEU A  1  621  ? -18.228 84.556  133.430 1.00 31.03 ? 619  LEU A CG    1 
ATOM   4583  C  CD1   . LEU A  1  621  ? -19.602 84.953  132.931 1.00 32.12 ? 619  LEU A CD1   1 
ATOM   4584  C  CD2   . LEU A  1  621  ? -18.278 84.174  134.893 1.00 32.12 ? 619  LEU A CD2   1 
ATOM   4585  N  N     . ALA A  1  622  ? -15.732 81.687  130.759 1.00 28.18 ? 620  ALA A N     1 
ATOM   4586  C  CA    . ALA A  1  622  ? -15.378 80.468  130.035 1.00 28.35 ? 620  ALA A CA    1 
ATOM   4587  C  C     . ALA A  1  622  ? -14.067 79.891  130.549 1.00 28.27 ? 620  ALA A C     1 
ATOM   4588  O  O     . ALA A  1  622  ? -13.932 78.671  130.702 1.00 28.52 ? 620  ALA A O     1 
ATOM   4589  C  CB    . ALA A  1  622  ? -15.286 80.747  128.530 1.00 24.66 ? 620  ALA A CB    1 
ATOM   4590  N  N     . ALA A  1  623  ? -13.088 80.758  130.821 1.00 25.88 ? 621  ALA A N     1 
ATOM   4591  C  CA    . ALA A  1  623  ? -11.817 80.299  131.360 1.00 28.71 ? 621  ALA A CA    1 
ATOM   4592  C  C     . ALA A  1  623  ? -12.007 79.638  132.717 1.00 29.20 ? 621  ALA A C     1 
ATOM   4593  O  O     . ALA A  1  623  ? -11.424 78.582  132.985 1.00 30.03 ? 621  ALA A O     1 
ATOM   4594  C  CB    . ALA A  1  623  ? -10.842 81.470  131.456 1.00 31.12 ? 621  ALA A CB    1 
ATOM   4595  N  N     . ASP A  1  624  ? -12.837 80.237  133.578 1.00 31.65 ? 622  ASP A N     1 
ATOM   4596  C  CA    . ASP A  1  624  ? -13.090 79.661  134.897 1.00 37.78 ? 622  ASP A CA    1 
ATOM   4597  C  C     . ASP A  1  624  ? -13.752 78.295  134.782 1.00 36.08 ? 622  ASP A C     1 
ATOM   4598  O  O     . ASP A  1  624  ? -13.460 77.383  135.565 1.00 39.78 ? 622  ASP A O     1 
ATOM   4599  C  CB    . ASP A  1  624  ? -13.973 80.595  135.729 1.00 40.57 ? 622  ASP A CB    1 
ATOM   4600  C  CG    . ASP A  1  624  ? -13.260 81.869  136.141 1.00 51.47 ? 622  ASP A CG    1 
ATOM   4601  O  OD1   . ASP A  1  624  ? -12.013 81.912  136.068 1.00 51.11 ? 622  ASP A OD1   1 
ATOM   4602  O  OD2   . ASP A  1  624  ? -13.957 82.825  136.551 1.00 59.42 ? 622  ASP A OD2   1 
ATOM   4603  N  N     . ALA A  1  625  ? -14.639 78.136  133.802 1.00 37.08 ? 623  ALA A N     1 
ATOM   4604  C  CA    . ALA A  1  625  ? -15.376 76.902  133.582 1.00 38.19 ? 623  ALA A CA    1 
ATOM   4605  C  C     . ALA A  1  625  ? -14.614 75.874  132.762 1.00 37.07 ? 623  ALA A C     1 
ATOM   4606  O  O     . ALA A  1  625  ? -15.112 74.755  132.596 1.00 39.71 ? 623  ALA A O     1 
ATOM   4607  C  CB    . ALA A  1  625  ? -16.689 77.208  132.868 1.00 41.52 ? 623  ALA A CB    1 
ATOM   4608  N  N     . ALA A  1  626  ? -13.449 76.224  132.222 1.00 34.46 ? 624  ALA A N     1 
ATOM   4609  C  CA    . ALA A  1  626  ? -12.764 75.308  131.312 1.00 31.08 ? 624  ALA A CA    1 
ATOM   4610  C  C     . ALA A  1  626  ? -12.414 73.973  131.961 1.00 34.63 ? 624  ALA A C     1 
ATOM   4611  O  O     . ALA A  1  626  ? -12.664 72.928  131.336 1.00 33.49 ? 624  ALA A O     1 
ATOM   4612  C  CB    . ALA A  1  626  ? -11.532 75.997  130.718 1.00 32.20 ? 624  ALA A CB    1 
ATOM   4613  N  N     . PRO A  1  627  ? -11.857 73.914  133.181 1.00 33.51 ? 625  PRO A N     1 
ATOM   4614  C  CA    . PRO A  1  627  ? -11.584 72.592  133.775 1.00 36.38 ? 625  PRO A CA    1 
ATOM   4615  C  C     . PRO A  1  627  ? -12.815 71.713  133.906 1.00 32.97 ? 625  PRO A C     1 
ATOM   4616  O  O     . PRO A  1  627  ? -12.737 70.508  133.638 1.00 34.69 ? 625  PRO A O     1 
ATOM   4617  C  CB    . PRO A  1  627  ? -11.000 72.944  135.152 1.00 39.80 ? 625  PRO A CB    1 
ATOM   4618  C  CG    . PRO A  1  627  ? -10.433 74.303  134.979 1.00 35.44 ? 625  PRO A CG    1 
ATOM   4619  C  CD    . PRO A  1  627  ? -11.367 75.006  134.046 1.00 37.45 ? 625  PRO A CD    1 
ATOM   4620  N  N     . ASP A  1  628  ? -13.947 72.279  134.321 1.00 34.26 ? 626  ASP A N     1 
ATOM   4621  C  CA    . ASP A  1  628  ? -15.136 71.463  134.542 1.00 33.28 ? 626  ASP A CA    1 
ATOM   4622  C  C     . ASP A  1  628  ? -15.626 70.846  133.240 1.00 34.96 ? 626  ASP A C     1 
ATOM   4623  O  O     . ASP A  1  628  ? -16.071 69.692  133.220 1.00 34.58 ? 626  ASP A O     1 
ATOM   4624  C  CB    . ASP A  1  628  ? -16.245 72.296  135.186 1.00 33.76 ? 626  ASP A CB    1 
ATOM   4625  C  CG    . ASP A  1  628  ? -15.892 72.758  136.593 1.00 42.11 ? 626  ASP A CG    1 
ATOM   4626  O  OD1   . ASP A  1  628  ? -15.004 72.142  137.221 1.00 50.06 ? 626  ASP A OD1   1 
ATOM   4627  O  OD2   . ASP A  1  628  ? -16.507 73.732  137.072 1.00 50.05 ? 626  ASP A OD2   1 
ATOM   4628  N  N     . TRP A  1  629  ? -15.548 71.593  132.142 1.00 29.82 ? 627  TRP A N     1 
ATOM   4629  C  CA    . TRP A  1  629  ? -16.020 71.051  130.876 1.00 27.59 ? 627  TRP A CA    1 
ATOM   4630  C  C     . TRP A  1  629  ? -15.022 70.061  130.292 1.00 27.94 ? 627  TRP A C     1 
ATOM   4631  O  O     . TRP A  1  629  ? -15.422 69.039  129.725 1.00 29.55 ? 627  TRP A O     1 
ATOM   4632  C  CB    . TRP A  1  629  ? -16.294 72.179  129.883 1.00 27.94 ? 627  TRP A CB    1 
ATOM   4633  C  CG    . TRP A  1  629  ? -16.759 71.670  128.566 1.00 26.05 ? 627  TRP A CG    1 
ATOM   4634  C  CD1   . TRP A  1  629  ? -16.157 71.857  127.351 1.00 23.98 ? 627  TRP A CD1   1 
ATOM   4635  C  CD2   . TRP A  1  629  ? -17.911 70.855  128.323 1.00 27.40 ? 627  TRP A CD2   1 
ATOM   4636  N  NE1   . TRP A  1  629  ? -16.873 71.223  126.373 1.00 24.40 ? 627  TRP A NE1   1 
ATOM   4637  C  CE2   . TRP A  1  629  ? -17.956 70.603  126.939 1.00 22.69 ? 627  TRP A CE2   1 
ATOM   4638  C  CE3   . TRP A  1  629  ? -18.913 70.325  129.136 1.00 25.56 ? 627  TRP A CE3   1 
ATOM   4639  C  CZ2   . TRP A  1  629  ? -18.965 69.836  126.348 1.00 25.73 ? 627  TRP A CZ2   1 
ATOM   4640  C  CZ3   . TRP A  1  629  ? -19.915 69.560  128.548 1.00 29.02 ? 627  TRP A CZ3   1 
ATOM   4641  C  CH2   . TRP A  1  629  ? -19.930 69.322  127.170 1.00 28.51 ? 627  TRP A CH2   1 
ATOM   4642  N  N     . ALA A  1  630  ? -13.722 70.351  130.412 1.00 26.57 ? 628  ALA A N     1 
ATOM   4643  C  CA    . ALA A  1  630  ? -12.715 69.404  129.947 1.00 29.79 ? 628  ALA A CA    1 
ATOM   4644  C  C     . ALA A  1  630  ? -12.816 68.082  130.694 1.00 32.10 ? 628  ALA A C     1 
ATOM   4645  O  O     . ALA A  1  630  ? -12.468 67.030  130.142 1.00 31.71 ? 628  ALA A O     1 
ATOM   4646  C  CB    . ALA A  1  630  ? -11.317 69.998  130.105 1.00 29.57 ? 628  ALA A CB    1 
ATOM   4647  N  N     . ALA A  1  631  ? -13.308 68.114  131.936 1.00 28.90 ? 629  ALA A N     1 
ATOM   4648  C  CA    . ALA A  1  631  ? -13.409 66.913  132.754 1.00 34.01 ? 629  ALA A CA    1 
ATOM   4649  C  C     . ALA A  1  631  ? -14.598 66.039  132.387 1.00 31.52 ? 629  ALA A C     1 
ATOM   4650  O  O     . ALA A  1  631  ? -14.651 64.883  132.817 1.00 34.32 ? 629  ALA A O     1 
ATOM   4651  C  CB    . ALA A  1  631  ? -13.486 67.287  134.237 1.00 33.56 ? 629  ALA A CB    1 
ATOM   4652  N  N     . VAL A  1  632  ? -15.547 66.551  131.610 1.00 27.16 ? 630  VAL A N     1 
ATOM   4653  C  CA    . VAL A  1  632  ? -16.628 65.718  131.095 1.00 29.49 ? 630  VAL A CA    1 
ATOM   4654  C  C     . VAL A  1  632  ? -15.986 64.786  130.076 1.00 29.03 ? 630  VAL A C     1 
ATOM   4655  O  O     . VAL A  1  632  ? -15.327 65.267  129.144 1.00 28.50 ? 630  VAL A O     1 
ATOM   4656  C  CB    . VAL A  1  632  ? -17.756 66.571  130.493 1.00 31.06 ? 630  VAL A CB    1 
ATOM   4657  C  CG1   . VAL A  1  632  ? -18.820 65.696  129.849 1.00 27.84 ? 630  VAL A CG1   1 
ATOM   4658  C  CG2   . VAL A  1  632  ? -18.368 67.461  131.585 1.00 28.62 ? 630  VAL A CG2   1 
ATOM   4659  N  N     . PRO A  1  633  ? -16.103 63.468  130.236 1.00 28.17 ? 631  PRO A N     1 
ATOM   4660  C  CA    . PRO A  1  633  ? -15.390 62.559  129.339 1.00 25.76 ? 631  PRO A CA    1 
ATOM   4661  C  C     . PRO A  1  633  ? -15.806 62.785  127.902 1.00 27.05 ? 631  PRO A C     1 
ATOM   4662  O  O     . PRO A  1  633  ? -16.960 63.160  127.622 1.00 27.40 ? 631  PRO A O     1 
ATOM   4663  C  CB    . PRO A  1  633  ? -15.814 61.169  129.835 1.00 30.64 ? 631  PRO A CB    1 
ATOM   4664  C  CG    . PRO A  1  633  ? -16.253 61.376  131.233 1.00 30.63 ? 631  PRO A CG    1 
ATOM   4665  C  CD    . PRO A  1  633  ? -16.841 62.749  131.290 1.00 29.59 ? 631  PRO A CD    1 
ATOM   4666  N  N     . PRO A  1  634  ? -14.896 62.565  126.945 1.00 23.45 ? 632  PRO A N     1 
ATOM   4667  C  CA    . PRO A  1  634  ? -15.235 62.823  125.532 1.00 23.85 ? 632  PRO A CA    1 
ATOM   4668  C  C     . PRO A  1  634  ? -16.494 62.108  125.076 1.00 23.97 ? 632  PRO A C     1 
ATOM   4669  O  O     . PRO A  1  634  ? -17.296 62.692  124.345 1.00 23.89 ? 632  PRO A O     1 
ATOM   4670  C  CB    . PRO A  1  634  ? -13.998 62.323  124.772 1.00 28.10 ? 632  PRO A CB    1 
ATOM   4671  C  CG    . PRO A  1  634  ? -12.882 62.361  125.777 1.00 29.89 ? 632  PRO A CG    1 
ATOM   4672  C  CD    . PRO A  1  634  ? -13.502 62.115  127.129 1.00 26.42 ? 632  PRO A CD    1 
ATOM   4673  N  N     . SER A  1  635  ? -16.696 60.859  125.502 1.00 27.80 ? 633  SER A N     1 
ATOM   4674  C  CA    . SER A  1  635  ? -17.882 60.116  125.086 1.00 29.33 ? 633  SER A CA    1 
ATOM   4675  C  C     . SER A  1  635  ? -19.163 60.809  125.538 1.00 27.35 ? 633  SER A C     1 
ATOM   4676  O  O     . SER A  1  635  ? -20.165 60.807  124.811 1.00 26.95 ? 633  SER A O     1 
ATOM   4677  C  CB    . SER A  1  635  ? -17.828 58.695  125.638 1.00 34.35 ? 633  SER A CB    1 
ATOM   4678  O  OG    . SER A  1  635  ? -18.028 58.710  127.038 1.00 47.25 ? 633  SER A OG    1 
ATOM   4679  N  N     . GLU A  1  636  ? -19.149 61.411  126.732 1.00 24.86 ? 634  GLU A N     1 
ATOM   4680  C  CA    . GLU A  1  636  ? -20.333 62.112  127.216 1.00 28.26 ? 634  GLU A CA    1 
ATOM   4681  C  C     . GLU A  1  636  ? -20.511 63.455  126.512 1.00 26.97 ? 634  GLU A C     1 
ATOM   4682  O  O     . GLU A  1  636  ? -21.643 63.866  126.232 1.00 27.46 ? 634  GLU A O     1 
ATOM   4683  C  CB    . GLU A  1  636  ? -20.265 62.288  128.737 1.00 27.33 ? 634  GLU A CB    1 
ATOM   4684  C  CG    . GLU A  1  636  ? -21.452 63.041  129.317 1.00 38.67 ? 634  GLU A CG    1 
ATOM   4685  C  CD    . GLU A  1  636  ? -22.794 62.498  128.831 1.00 48.12 ? 634  GLU A CD    1 
ATOM   4686  O  OE1   . GLU A  1  636  ? -22.977 61.262  128.852 1.00 40.20 ? 634  GLU A OE1   1 
ATOM   4687  O  OE2   . GLU A  1  636  ? -23.661 63.303  128.413 1.00 39.15 ? 634  GLU A OE2   1 
ATOM   4688  N  N     . ARG A  1  637  ? -19.414 64.151  126.199 1.00 24.63 ? 635  ARG A N     1 
ATOM   4689  C  CA    . ARG A  1  637  ? -19.540 65.344  125.372 1.00 22.15 ? 635  ARG A CA    1 
ATOM   4690  C  C     . ARG A  1  637  ? -20.141 64.987  124.017 1.00 24.37 ? 635  ARG A C     1 
ATOM   4691  O  O     . ARG A  1  637  ? -21.039 65.678  123.519 1.00 23.45 ? 635  ARG A O     1 
ATOM   4692  C  CB    . ARG A  1  637  ? -18.179 66.026  125.203 1.00 22.80 ? 635  ARG A CB    1 
ATOM   4693  C  CG    . ARG A  1  637  ? -17.501 66.318  126.536 1.00 25.16 ? 635  ARG A CG    1 
ATOM   4694  C  CD    . ARG A  1  637  ? -16.347 67.310  126.422 1.00 26.01 ? 635  ARG A CD    1 
ATOM   4695  N  NE    . ARG A  1  637  ? -15.284 66.833  125.550 1.00 24.34 ? 635  ARG A NE    1 
ATOM   4696  C  CZ    . ARG A  1  637  ? -14.093 66.406  125.952 1.00 29.23 ? 635  ARG A CZ    1 
ATOM   4697  N  NH1   . ARG A  1  637  ? -13.786 66.313  127.237 1.00 28.71 ? 635  ARG A NH1   1 
ATOM   4698  N  NH2   . ARG A  1  637  ? -13.183 66.078  125.040 1.00 26.73 ? 635  ARG A NH2   1 
ATOM   4699  N  N     . ALA A  1  638  ? -19.667 63.895  123.413 1.00 25.79 ? 636  ALA A N     1 
ATOM   4700  C  CA    . ALA A  1  638  ? -20.229 63.450  122.142 1.00 23.56 ? 636  ALA A CA    1 
ATOM   4701  C  C     . ALA A  1  638  ? -21.703 63.096  122.282 1.00 25.65 ? 636  ALA A C     1 
ATOM   4702  O  O     . ALA A  1  638  ? -22.493 63.324  121.356 1.00 21.76 ? 636  ALA A O     1 
ATOM   4703  C  CB    . ALA A  1  638  ? -19.437 62.253  121.614 1.00 22.28 ? 636  ALA A CB    1 
ATOM   4704  N  N     . ALA A  1  639  ? -22.091 62.528  123.429 1.00 24.94 ? 637  ALA A N     1 
ATOM   4705  C  CA    . ALA A  1  639  ? -23.501 62.222  123.652 1.00 24.49 ? 637  ALA A CA    1 
ATOM   4706  C  C     . ALA A  1  639  ? -24.347 63.487  123.690 1.00 23.83 ? 637  ALA A C     1 
ATOM   4707  O  O     . ALA A  1  639  ? -25.496 63.473  123.232 1.00 25.41 ? 637  ALA A O     1 
ATOM   4708  C  CB    . ALA A  1  639  ? -23.678 61.404  124.932 1.00 23.59 ? 637  ALA A CB    1 
ATOM   4709  N  N     . CYS A  1  640  ? -23.801 64.592  124.210 1.00 22.38 ? 638  CYS A N     1 
ATOM   4710  C  CA    . CYS A  1  640  ? -24.507 65.866  124.117 1.00 24.59 ? 638  CYS A CA    1 
ATOM   4711  C  C     . CYS A  1  640  ? -24.741 66.250  122.666 1.00 24.67 ? 638  CYS A C     1 
ATOM   4712  O  O     . CYS A  1  640  ? -25.836 66.696  122.302 1.00 25.37 ? 638  CYS A O     1 
ATOM   4713  C  CB    . CYS A  1  640  ? -23.728 66.977  124.809 1.00 24.15 ? 638  CYS A CB    1 
ATOM   4714  S  SG    . CYS A  1  640  ? -23.602 66.806  126.577 1.00 27.49 ? 638  CYS A SG    1 
ATOM   4715  N  N     . LEU A  1  641  ? -23.715 66.109  121.826 1.00 22.76 ? 639  LEU A N     1 
ATOM   4716  C  CA    . LEU A  1  641  ? -23.883 66.456  120.422 1.00 21.45 ? 639  LEU A CA    1 
ATOM   4717  C  C     . LEU A  1  641  ? -24.934 65.574  119.773 1.00 22.03 ? 639  LEU A C     1 
ATOM   4718  O  O     . LEU A  1  641  ? -25.772 66.059  119.009 1.00 22.97 ? 639  LEU A O     1 
ATOM   4719  C  CB    . LEU A  1  641  ? -22.552 66.338  119.679 1.00 21.38 ? 639  LEU A CB    1 
ATOM   4720  C  CG    . LEU A  1  641  ? -21.634 67.567  119.663 1.00 23.75 ? 639  LEU A CG    1 
ATOM   4721  C  CD1   . LEU A  1  641  ? -21.191 67.973  121.054 1.00 25.38 ? 639  LEU A CD1   1 
ATOM   4722  C  CD2   . LEU A  1  641  ? -20.427 67.324  118.774 1.00 22.38 ? 639  LEU A CD2   1 
ATOM   4723  N  N     . ASP A  1  642  ? -24.916 64.273  120.071 1.00 23.60 ? 640  ASP A N     1 
ATOM   4724  C  CA    . ASP A  1  642  ? -25.919 63.396  119.475 1.00 22.20 ? 640  ASP A CA    1 
ATOM   4725  C  C     . ASP A  1  642  ? -27.321 63.759  119.949 1.00 21.48 ? 640  ASP A C     1 
ATOM   4726  O  O     . ASP A  1  642  ? -28.271 63.719  119.163 1.00 21.80 ? 640  ASP A O     1 
ATOM   4727  C  CB    . ASP A  1  642  ? -25.603 61.932  119.783 1.00 23.47 ? 640  ASP A CB    1 
ATOM   4728  C  CG    . ASP A  1  642  ? -24.500 61.377  118.896 1.00 24.14 ? 640  ASP A CG    1 
ATOM   4729  O  OD1   . ASP A  1  642  ? -24.283 61.918  117.782 1.00 27.02 ? 640  ASP A OD1   1 
ATOM   4730  O  OD2   . ASP A  1  642  ? -23.859 60.389  119.314 1.00 25.28 ? 640  ASP A OD2   1 
ATOM   4731  N  N     . ARG A  1  643  ? -27.474 64.119  121.230 1.00 23.65 ? 641  ARG A N     1 
ATOM   4732  C  CA    . ARG A  1  643  ? -28.782 64.557  121.712 1.00 23.96 ? 641  ARG A CA    1 
ATOM   4733  C  C     . ARG A  1  643  ? -29.210 65.840  121.020 1.00 21.91 ? 641  ARG A C     1 
ATOM   4734  O  O     . ARG A  1  643  ? -30.380 65.996  120.660 1.00 25.78 ? 641  ARG A O     1 
ATOM   4735  C  CB    . ARG A  1  643  ? -28.768 64.744  123.233 1.00 25.50 ? 641  ARG A CB    1 
ATOM   4736  C  CG    . ARG A  1  643  ? -28.881 63.436  124.003 1.00 26.53 ? 641  ARG A CG    1 
ATOM   4737  C  CD    . ARG A  1  643  ? -29.083 63.667  125.488 1.00 26.97 ? 641  ARG A CD    1 
ATOM   4738  N  NE    . ARG A  1  643  ? -27.955 64.360  126.097 1.00 28.14 ? 641  ARG A NE    1 
ATOM   4739  C  CZ    . ARG A  1  643  ? -26.936 63.751  126.688 1.00 28.50 ? 641  ARG A CZ    1 
ATOM   4740  N  NH1   . ARG A  1  643  ? -26.857 62.432  126.738 1.00 31.54 ? 641  ARG A NH1   1 
ATOM   4741  N  NH2   . ARG A  1  643  ? -25.980 64.482  127.252 1.00 31.45 ? 641  ARG A NH2   1 
ATOM   4742  N  N     . ALA A  1  644  ? -28.274 66.768  120.810 1.00 22.19 ? 642  ALA A N     1 
ATOM   4743  C  CA    . ALA A  1  644  ? -28.624 67.999  120.108 1.00 23.02 ? 642  ALA A CA    1 
ATOM   4744  C  C     . ALA A  1  644  ? -29.048 67.713  118.679 1.00 23.26 ? 642  ALA A C     1 
ATOM   4745  O  O     . ALA A  1  644  ? -29.934 68.393  118.145 1.00 22.35 ? 642  ALA A O     1 
ATOM   4746  C  CB    . ALA A  1  644  ? -27.454 68.977  120.123 1.00 24.16 ? 642  ALA A CB    1 
ATOM   4747  N  N     . ALA A  1  645  ? -28.433 66.712  118.048 1.00 22.20 ? 643  ALA A N     1 
ATOM   4748  C  CA    . ALA A  1  645  ? -28.816 66.361  116.686 1.00 19.21 ? 643  ALA A CA    1 
ATOM   4749  C  C     . ALA A  1  645  ? -30.233 65.818  116.647 1.00 21.72 ? 643  ALA A C     1 
ATOM   4750  O  O     . ALA A  1  645  ? -31.004 66.146  115.739 1.00 22.57 ? 643  ALA A O     1 
ATOM   4751  C  CB    . ALA A  1  645  ? -27.836 65.340  116.111 1.00 22.02 ? 643  ALA A CB    1 
ATOM   4752  N  N     . GLU A  1  646  ? -30.589 64.980  117.620 1.00 23.53 ? 644  GLU A N     1 
ATOM   4753  C  CA    . GLU A  1  646  ? -31.959 64.495  117.702 1.00 26.06 ? 644  GLU A CA    1 
ATOM   4754  C  C     . GLU A  1  646  ? -32.929 65.648  117.888 1.00 23.80 ? 644  GLU A C     1 
ATOM   4755  O  O     . GLU A  1  646  ? -33.990 65.679  117.260 1.00 25.46 ? 644  GLU A O     1 
ATOM   4756  C  CB    . GLU A  1  646  ? -32.112 63.503  118.851 1.00 26.48 ? 644  GLU A CB    1 
ATOM   4757  C  CG    . GLU A  1  646  ? -31.301 62.241  118.691 1.00 33.65 ? 644  GLU A CG    1 
ATOM   4758  C  CD    . GLU A  1  646  ? -31.762 61.396  117.523 1.00 45.33 ? 644  GLU A CD    1 
ATOM   4759  O  OE1   . GLU A  1  646  ? -32.971 61.426  117.210 1.00 49.72 ? 644  GLU A OE1   1 
ATOM   4760  O  OE2   . GLU A  1  646  ? -30.913 60.707  116.915 1.00 42.08 ? 644  GLU A OE2   1 
ATOM   4761  N  N     . LEU A  1  647  ? -32.582 66.602  118.755 1.00 24.77 ? 645  LEU A N     1 
ATOM   4762  C  CA    . LEU A  1  647  ? -33.475 67.731  118.991 1.00 24.52 ? 645  LEU A CA    1 
ATOM   4763  C  C     . LEU A  1  647  ? -33.639 68.564  117.728 1.00 26.35 ? 645  LEU A C     1 
ATOM   4764  O  O     . LEU A  1  647  ? -34.748 69.010  117.408 1.00 26.65 ? 645  LEU A O     1 
ATOM   4765  C  CB    . LEU A  1  647  ? -32.955 68.590  120.143 1.00 24.10 ? 645  LEU A CB    1 
ATOM   4766  C  CG    . LEU A  1  647  ? -32.995 67.926  121.518 1.00 26.62 ? 645  LEU A CG    1 
ATOM   4767  C  CD1   . LEU A  1  647  ? -32.304 68.807  122.549 1.00 26.25 ? 645  LEU A CD1   1 
ATOM   4768  C  CD2   . LEU A  1  647  ? -34.438 67.621  121.935 1.00 30.62 ? 645  LEU A CD2   1 
ATOM   4769  N  N     . MET A  1  648  ? -32.550 68.769  116.985 1.00 21.83 ? 646  MET A N     1 
ATOM   4770  C  CA    . MET A  1  648  ? -32.664 69.553  115.764 1.00 23.39 ? 646  MET A CA    1 
ATOM   4771  C  C     . MET A  1  648  ? -33.480 68.817  114.720 1.00 23.37 ? 646  MET A C     1 
ATOM   4772  O  O     . MET A  1  648  ? -34.271 69.435  114.004 1.00 24.17 ? 646  MET A O     1 
ATOM   4773  C  CB    . MET A  1  648  ? -31.286 69.909  115.209 1.00 19.39 ? 646  MET A CB    1 
ATOM   4774  C  CG    . MET A  1  648  ? -30.584 70.963  116.032 1.00 24.11 ? 646  MET A CG    1 
ATOM   4775  S  SD    . MET A  1  648  ? -29.236 71.667  115.077 1.00 25.93 ? 646  MET A SD    1 
ATOM   4776  C  CE    . MET A  1  648  ? -28.569 72.808  116.281 1.00 27.44 ? 646  MET A CE    1 
ATOM   4777  N  N     . GLN A  1  649  ? -33.306 67.496  114.620 1.00 21.78 ? 647  GLN A N     1 
ATOM   4778  C  CA    . GLN A  1  649  ? -34.110 66.721  113.682 1.00 21.08 ? 647  GLN A CA    1 
ATOM   4779  C  C     . GLN A  1  649  ? -35.595 66.844  114.006 1.00 22.49 ? 647  GLN A C     1 
ATOM   4780  O  O     . GLN A  1  649  ? -36.424 67.063  113.116 1.00 24.17 ? 647  GLN A O     1 
ATOM   4781  C  CB    . GLN A  1  649  ? -33.676 65.255  113.702 1.00 23.50 ? 647  GLN A CB    1 
ATOM   4782  C  CG    . GLN A  1  649  ? -34.382 64.421  112.651 1.00 22.07 ? 647  GLN A CG    1 
ATOM   4783  C  CD    . GLN A  1  649  ? -33.814 64.663  111.272 1.00 23.33 ? 647  GLN A CD    1 
ATOM   4784  O  OE1   . GLN A  1  649  ? -32.736 64.175  110.941 1.00 23.00 ? 647  GLN A OE1   1 
ATOM   4785  N  NE2   . GLN A  1  649  ? -34.537 65.428  110.456 1.00 24.44 ? 647  GLN A NE2   1 
ATOM   4786  N  N     . ALA A  1  650  ? -35.946 66.706  115.281 1.00 23.66 ? 648  ALA A N     1 
ATOM   4787  C  CA    . ALA A  1  650  ? -37.349 66.788  115.672 1.00 24.48 ? 648  ALA A CA    1 
ATOM   4788  C  C     . ALA A  1  650  ? -37.903 68.186  115.457 1.00 29.13 ? 648  ALA A C     1 
ATOM   4789  O  O     . ALA A  1  650  ? -39.081 68.341  115.105 1.00 30.96 ? 648  ALA A O     1 
ATOM   4790  C  CB    . ALA A  1  650  ? -37.512 66.366  117.131 1.00 28.33 ? 648  ALA A CB    1 
ATOM   4791  N  N     . ARG A  1  651  ? -37.074 69.204  115.643 1.00 24.69 ? 649  ARG A N     1 
ATOM   4792  C  CA    . ARG A  1  651  ? -37.490 70.592  115.533 1.00 24.49 ? 649  ARG A CA    1 
ATOM   4793  C  C     . ARG A  1  651  ? -37.326 71.145  114.127 1.00 23.63 ? 649  ARG A C     1 
ATOM   4794  O  O     . ARG A  1  651  ? -37.591 72.333  113.916 1.00 24.03 ? 649  ARG A O     1 
ATOM   4795  C  CB    . ARG A  1  651  ? -36.692 71.451  116.525 1.00 27.21 ? 649  ARG A CB    1 
ATOM   4796  C  CG    . ARG A  1  651  ? -37.285 72.815  116.834 1.00 32.66 ? 649  ARG A CG    1 
ATOM   4797  C  CD    . ARG A  1  651  ? -37.214 73.130  118.323 1.00 30.69 ? 649  ARG A CD    1 
ATOM   4798  N  NE    . ARG A  1  651  ? -37.627 74.498  118.617 1.00 34.51 ? 649  ARG A NE    1 
ATOM   4799  C  CZ    . ARG A  1  651  ? -38.884 74.885  118.776 1.00 36.56 ? 649  ARG A CZ    1 
ATOM   4800  N  NH1   . ARG A  1  651  ? -39.892 74.045  118.607 1.00 35.98 ? 649  ARG A NH1   1 
ATOM   4801  N  NH2   . ARG A  1  651  ? -39.137 76.148  119.109 1.00 38.62 ? 649  ARG A NH2   1 
ATOM   4802  N  N     . MET A  1  652  ? -36.909 70.319  113.162 1.00 23.09 ? 650  MET A N     1 
ATOM   4803  C  CA    . MET A  1  652  ? -36.573 70.833  111.835 1.00 21.29 ? 650  MET A CA    1 
ATOM   4804  C  C     . MET A  1  652  ? -37.650 71.721  111.234 1.00 22.69 ? 650  MET A C     1 
ATOM   4805  O  O     . MET A  1  652  ? -37.303 72.797  110.728 1.00 23.71 ? 650  MET A O     1 
ATOM   4806  C  CB    . MET A  1  652  ? -36.236 69.684  110.874 1.00 23.51 ? 650  MET A CB    1 
ATOM   4807  C  CG    . MET A  1  652  ? -36.047 70.154  109.429 1.00 22.99 ? 650  MET A CG    1 
ATOM   4808  S  SD    . MET A  1  652  ? -35.612 68.816  108.293 1.00 26.17 ? 650  MET A SD    1 
ATOM   4809  C  CE    . MET A  1  652  ? -33.922 68.522  108.798 1.00 24.27 ? 650  MET A CE    1 
ATOM   4810  N  N     . PRO A  1  653  ? -38.943 71.368  111.258 1.00 23.96 ? 651  PRO A N     1 
ATOM   4811  C  CA    . PRO A  1  653  ? -39.929 72.255  110.609 1.00 23.50 ? 651  PRO A CA    1 
ATOM   4812  C  C     . PRO A  1  653  ? -39.943 73.656  111.189 1.00 25.54 ? 651  PRO A C     1 
ATOM   4813  O  O     . PRO A  1  653  ? -39.993 74.635  110.431 1.00 23.72 ? 651  PRO A O     1 
ATOM   4814  C  CB    . PRO A  1  653  ? -41.264 71.533  110.838 1.00 21.72 ? 651  PRO A CB    1 
ATOM   4815  C  CG    . PRO A  1  653  ? -40.882 70.097  110.996 1.00 26.07 ? 651  PRO A CG    1 
ATOM   4816  C  CD    . PRO A  1  653  ? -39.579 70.140  111.768 1.00 24.41 ? 651  PRO A CD    1 
ATOM   4817  N  N     . THR A  1  654  ? -39.873 73.776  112.518 1.00 22.97 ? 652  THR A N     1 
ATOM   4818  C  CA    . THR A  1  654  ? -39.813 75.092  113.141 1.00 25.09 ? 652  THR A CA    1 
ATOM   4819  C  C     . THR A  1  654  ? -38.515 75.808  112.797 1.00 26.51 ? 652  THR A C     1 
ATOM   4820  O  O     . THR A  1  654  ? -38.524 77.007  112.493 1.00 25.73 ? 652  THR A O     1 
ATOM   4821  C  CB    . THR A  1  654  ? -39.969 74.964  114.656 1.00 24.12 ? 652  THR A CB    1 
ATOM   4822  O  OG1   . THR A  1  654  ? -41.212 74.313  114.951 1.00 25.22 ? 652  THR A OG1   1 
ATOM   4823  C  CG2   . THR A  1  654  ? -39.959 76.330  115.306 1.00 25.29 ? 652  THR A CG2   1 
ATOM   4824  N  N     . LEU A  1  655  ? -37.385 75.094  112.851 1.00 21.88 ? 653  LEU A N     1 
ATOM   4825  C  CA    . LEU A  1  655  ? -36.114 75.693  112.446 1.00 21.28 ? 653  LEU A CA    1 
ATOM   4826  C  C     . LEU A  1  655  ? -36.155 76.176  111.000 1.00 24.68 ? 653  LEU A C     1 
ATOM   4827  O  O     . LEU A  1  655  ? -35.609 77.241  110.684 1.00 24.17 ? 653  LEU A O     1 
ATOM   4828  C  CB    . LEU A  1  655  ? -34.974 74.691  112.632 1.00 21.90 ? 653  LEU A CB    1 
ATOM   4829  C  CG    . LEU A  1  655  ? -34.802 74.222  114.073 1.00 25.78 ? 653  LEU A CG    1 
ATOM   4830  C  CD1   . LEU A  1  655  ? -33.697 73.182  114.186 1.00 25.56 ? 653  LEU A CD1   1 
ATOM   4831  C  CD2   . LEU A  1  655  ? -34.495 75.405  114.957 1.00 28.87 ? 653  LEU A CD2   1 
ATOM   4832  N  N     . LEU A  1  656  ? -36.780 75.401  110.104 1.00 22.52 ? 654  LEU A N     1 
ATOM   4833  C  CA    . LEU A  1  656  ? -36.915 75.841  108.714 1.00 24.41 ? 654  LEU A CA    1 
ATOM   4834  C  C     . LEU A  1  656  ? -37.561 77.207  108.641 1.00 26.52 ? 654  LEU A C     1 
ATOM   4835  O  O     . LEU A  1  656  ? -37.094 78.097  107.920 1.00 24.93 ? 654  LEU A O     1 
ATOM   4836  C  CB    . LEU A  1  656  ? -37.766 74.863  107.903 1.00 27.15 ? 654  LEU A CB    1 
ATOM   4837  C  CG    . LEU A  1  656  ? -37.308 73.422  107.795 1.00 28.57 ? 654  LEU A CG    1 
ATOM   4838  C  CD1   . LEU A  1  656  ? -38.239 72.640  106.902 1.00 25.42 ? 654  LEU A CD1   1 
ATOM   4839  C  CD2   . LEU A  1  656  ? -35.897 73.381  107.301 1.00 27.28 ? 654  LEU A CD2   1 
ATOM   4840  N  N     . GLY A  1  657  ? -38.677 77.363  109.350 1.00 25.46 ? 655  GLY A N     1 
ATOM   4841  C  CA    . GLY A  1  657  ? -39.402 78.615  109.303 1.00 26.27 ? 655  GLY A CA    1 
ATOM   4842  C  C     . GLY A  1  657  ? -38.553 79.784  109.740 1.00 25.47 ? 655  GLY A C     1 
ATOM   4843  O  O     . GLY A  1  657  ? -38.612 80.861  109.147 1.00 23.50 ? 655  GLY A O     1 
ATOM   4844  N  N     . LEU A  1  658  ? -37.747 79.588  110.783 1.00 22.65 ? 656  LEU A N     1 
ATOM   4845  C  CA    . LEU A  1  658  ? -36.912 80.682  111.254 1.00 22.26 ? 656  LEU A CA    1 
ATOM   4846  C  C     . LEU A  1  658  ? -35.827 81.005  110.234 1.00 22.38 ? 656  LEU A C     1 
ATOM   4847  O  O     . LEU A  1  658  ? -35.570 82.176  109.931 1.00 24.50 ? 656  LEU A O     1 
ATOM   4848  C  CB    . LEU A  1  658  ? -36.310 80.323  112.611 1.00 22.12 ? 656  LEU A CB    1 
ATOM   4849  C  CG    . LEU A  1  658  ? -35.440 81.392  113.262 1.00 23.50 ? 656  LEU A CG    1 
ATOM   4850  C  CD1   . LEU A  1  658  ? -36.200 82.717  113.341 1.00 25.67 ? 656  LEU A CD1   1 
ATOM   4851  C  CD2   . LEU A  1  658  ? -35.034 80.929  114.650 1.00 23.81 ? 656  LEU A CD2   1 
ATOM   4852  N  N     . ILE A  1  659  ? -35.175 79.978  109.695 1.00 21.82 ? 657  ILE A N     1 
ATOM   4853  C  CA    . ILE A  1  659  ? -34.129 80.206  108.699 1.00 19.68 ? 657  ILE A CA    1 
ATOM   4854  C  C     . ILE A  1  659  ? -34.702 80.891  107.462 1.00 23.43 ? 657  ILE A C     1 
ATOM   4855  O  O     . ILE A  1  659  ? -34.087 81.807  106.896 1.00 21.00 ? 657  ILE A O     1 
ATOM   4856  C  CB    . ILE A  1  659  ? -33.447 78.875  108.347 1.00 20.89 ? 657  ILE A CB    1 
ATOM   4857  C  CG1   . ILE A  1  659  ? -32.685 78.355  109.569 1.00 21.87 ? 657  ILE A CG1   1 
ATOM   4858  C  CG2   . ILE A  1  659  ? -32.511 79.059  107.179 1.00 20.92 ? 657  ILE A CG2   1 
ATOM   4859  C  CD1   . ILE A  1  659  ? -32.170 76.952  109.428 1.00 24.68 ? 657  ILE A CD1   1 
ATOM   4860  N  N     . ILE A  1  660  ? -35.895 80.467  107.034 1.00 22.29 ? 658  ILE A N     1 
ATOM   4861  C  CA    . ILE A  1  660  ? -36.532 81.067  105.860 1.00 21.12 ? 658  ILE A CA    1 
ATOM   4862  C  C     . ILE A  1  660  ? -36.728 82.562  106.072 1.00 23.74 ? 658  ILE A C     1 
ATOM   4863  O  O     . ILE A  1  660  ? -36.414 83.381  105.200 1.00 25.07 ? 658  ILE A O     1 
ATOM   4864  C  CB    . ILE A  1  660  ? -37.867 80.357  105.559 1.00 20.22 ? 658  ILE A CB    1 
ATOM   4865  C  CG1   . ILE A  1  660  ? -37.618 78.984  104.940 1.00 22.22 ? 658  ILE A CG1   1 
ATOM   4866  C  CG2   . ILE A  1  660  ? -38.771 81.215  104.657 1.00 23.07 ? 658  ILE A CG2   1 
ATOM   4867  C  CD1   . ILE A  1  660  ? -38.876 78.149  104.820 1.00 27.32 ? 658  ILE A CD1   1 
ATOM   4868  N  N     . ARG A  1  661  ? -37.250 82.940  107.240 1.00 22.55 ? 659  ARG A N     1 
ATOM   4869  C  CA    . ARG A  1  661  ? -37.630 84.329  107.457 1.00 24.58 ? 659  ARG A CA    1 
ATOM   4870  C  C     . ARG A  1  661  ? -36.452 85.181  107.906 1.00 25.75 ? 659  ARG A C     1 
ATOM   4871  O  O     . ARG A  1  661  ? -36.363 86.352  107.529 1.00 23.74 ? 659  ARG A O     1 
ATOM   4872  C  CB    . ARG A  1  661  ? -38.780 84.410  108.464 1.00 25.11 ? 659  ARG A CB    1 
ATOM   4873  C  CG    . ARG A  1  661  ? -40.103 84.034  107.831 1.00 26.44 ? 659  ARG A CG    1 
ATOM   4874  C  CD    . ARG A  1  661  ? -41.260 84.020  108.817 1.00 26.93 ? 659  ARG A CD    1 
ATOM   4875  N  NE    . ARG A  1  661  ? -41.480 85.311  109.454 1.00 28.26 ? 659  ARG A NE    1 
ATOM   4876  C  CZ    . ARG A  1  661  ? -41.405 85.525  110.761 1.00 25.00 ? 659  ARG A CZ    1 
ATOM   4877  N  NH1   . ARG A  1  661  ? -41.094 84.554  111.604 1.00 27.99 ? 659  ARG A NH1   1 
ATOM   4878  N  NH2   . ARG A  1  661  ? -41.666 86.739  111.237 1.00 27.69 ? 659  ARG A NH2   1 
ATOM   4879  N  N     . GLU A  1  662  ? -35.537 84.623  108.705 1.00 23.66 ? 660  GLU A N     1 
ATOM   4880  C  CA    . GLU A  1  662  ? -34.439 85.443  109.206 1.00 24.19 ? 660  GLU A CA    1 
ATOM   4881  C  C     . GLU A  1  662  ? -33.321 85.586  108.182 1.00 22.90 ? 660  GLU A C     1 
ATOM   4882  O  O     . GLU A  1  662  ? -32.716 86.656  108.061 1.00 26.30 ? 660  GLU A O     1 
ATOM   4883  C  CB    . GLU A  1  662  ? -33.875 84.857  110.499 1.00 26.73 ? 660  GLU A CB    1 
ATOM   4884  C  CG    . GLU A  1  662  ? -32.689 85.641  111.023 1.00 25.12 ? 660  GLU A CG    1 
ATOM   4885  C  CD    . GLU A  1  662  ? -32.160 85.115  112.340 1.00 29.91 ? 660  GLU A CD    1 
ATOM   4886  O  OE1   . GLU A  1  662  ? -32.174 83.886  112.550 1.00 27.58 ? 660  GLU A OE1   1 
ATOM   4887  O  OE2   . GLU A  1  662  ? -31.732 85.943  113.167 1.00 28.40 ? 660  GLU A OE2   1 
ATOM   4888  N  N     . ALA A  1  663  ? -33.023 84.523  107.448 1.00 24.66 ? 661  ALA A N     1 
ATOM   4889  C  CA    . ALA A  1  663  ? -31.849 84.496  106.594 1.00 24.43 ? 661  ALA A CA    1 
ATOM   4890  C  C     . ALA A  1  663  ? -32.187 84.598  105.121 1.00 25.12 ? 661  ALA A C     1 
ATOM   4891  O  O     . ALA A  1  663  ? -31.276 84.598  104.292 1.00 31.77 ? 661  ALA A O     1 
ATOM   4892  C  CB    . ALA A  1  663  ? -31.034 83.222  106.855 1.00 22.78 ? 661  ALA A CB    1 
ATOM   4893  N  N     . GLY A  1  664  ? -33.467 84.671  104.771 1.00 25.54 ? 662  GLY A N     1 
ATOM   4894  C  CA    . GLY A  1  664  ? -33.842 84.808  103.377 1.00 25.37 ? 662  GLY A CA    1 
ATOM   4895  C  C     . GLY A  1  664  ? -33.684 83.552  102.552 1.00 25.94 ? 662  GLY A C     1 
ATOM   4896  O  O     . GLY A  1  664  ? -33.506 83.636  101.335 1.00 32.43 ? 662  GLY A O     1 
ATOM   4897  N  N     . LYS A  1  665  ? -33.748 82.381  103.179 1.00 24.88 ? 663  LYS A N     1 
ATOM   4898  C  CA    . LYS A  1  665  ? -33.527 81.122  102.487 1.00 23.50 ? 663  LYS A CA    1 
ATOM   4899  C  C     . LYS A  1  665  ? -34.831 80.494  102.026 1.00 19.33 ? 663  LYS A C     1 
ATOM   4900  O  O     . LYS A  1  665  ? -35.875 80.656  102.652 1.00 20.47 ? 663  LYS A O     1 
ATOM   4901  C  CB    . LYS A  1  665  ? -32.806 80.136  103.392 1.00 22.64 ? 663  LYS A CB    1 
ATOM   4902  C  CG    . LYS A  1  665  ? -31.479 80.667  103.828 1.00 26.74 ? 663  LYS A CG    1 
ATOM   4903  C  CD    . LYS A  1  665  ? -30.509 79.544  103.937 1.00 35.92 ? 663  LYS A CD    1 
ATOM   4904  C  CE    . LYS A  1  665  ? -29.130 80.089  104.099 1.00 32.31 ? 663  LYS A CE    1 
ATOM   4905  N  NZ    . LYS A  1  665  ? -28.150 78.967  104.129 1.00 34.79 ? 663  LYS A NZ    1 
ATOM   4906  N  N     . SER A  1  666  ? -34.742 79.743  100.936 1.00 22.74 ? 664  SER A N     1 
ATOM   4907  C  CA    . SER A  1  666  ? -35.852 78.916  100.496 1.00 22.42 ? 664  SER A CA    1 
ATOM   4908  C  C     . SER A  1  666  ? -36.016 77.720  101.428 1.00 24.45 ? 664  SER A C     1 
ATOM   4909  O  O     . SER A  1  666  ? -35.100 77.350  102.173 1.00 23.32 ? 664  SER A O     1 
ATOM   4910  C  CB    . SER A  1  666  ? -35.611 78.426  99.073  1.00 24.51 ? 664  SER A CB    1 
ATOM   4911  O  OG    . SER A  1  666  ? -34.620 77.412  99.082  1.00 26.66 ? 664  SER A OG    1 
ATOM   4912  N  N     . ALA A  1  667  ? -37.205 77.111  101.379 1.00 22.20 ? 665  ALA A N     1 
ATOM   4913  C  CA    . ALA A  1  667  ? -37.461 75.925  102.194 1.00 23.42 ? 665  ALA A CA    1 
ATOM   4914  C  C     . ALA A  1  667  ? -36.469 74.813  101.877 1.00 24.35 ? 665  ALA A C     1 
ATOM   4915  O  O     . ALA A  1  667  ? -35.916 74.184  102.786 1.00 21.01 ? 665  ALA A O     1 
ATOM   4916  C  CB    . ALA A  1  667  ? -38.895 75.440  101.981 1.00 23.91 ? 665  ALA A CB    1 
ATOM   4917  N  N     . LEU A  1  668  ? -36.241 74.553  100.586 1.00 22.87 ? 666  LEU A N     1 
ATOM   4918  C  CA    . LEU A  1  668  ? -35.274 73.544  100.174 1.00 22.54 ? 666  LEU A CA    1 
ATOM   4919  C  C     . LEU A  1  668  ? -33.917 73.791  100.812 1.00 23.73 ? 666  LEU A C     1 
ATOM   4920  O  O     . LEU A  1  668  ? -33.311 72.881  101.389 1.00 22.18 ? 666  LEU A O     1 
ATOM   4921  C  CB    . LEU A  1  668  ? -35.162 73.550  98.646  1.00 29.01 ? 666  LEU A CB    1 
ATOM   4922  C  CG    . LEU A  1  668  ? -34.786 72.278  97.907  1.00 44.83 ? 666  LEU A CG    1 
ATOM   4923  C  CD1   . LEU A  1  668  ? -35.475 71.100  98.558  1.00 37.62 ? 666  LEU A CD1   1 
ATOM   4924  C  CD2   . LEU A  1  668  ? -35.225 72.429  96.448  1.00 38.62 ? 666  LEU A CD2   1 
ATOM   4925  N  N     . ASN A  1  669  ? -33.432 75.032  100.734 1.00 21.42 ? 667  ASN A N     1 
ATOM   4926  C  CA    . ASN A  1  669  ? -32.125 75.350  101.298 1.00 22.76 ? 667  ASN A CA    1 
ATOM   4927  C  C     . ASN A  1  669  ? -32.134 75.306  102.821 1.00 20.57 ? 667  ASN A C     1 
ATOM   4928  O  O     . ASN A  1  669  ? -31.126 74.923  103.430 1.00 22.30 ? 667  ASN A O     1 
ATOM   4929  C  CB    . ASN A  1  669  ? -31.669 76.722  100.811 1.00 23.30 ? 667  ASN A CB    1 
ATOM   4930  C  CG    . ASN A  1  669  ? -31.397 76.748  99.307  1.00 25.97 ? 667  ASN A CG    1 
ATOM   4931  O  OD1   . ASN A  1  669  ? -31.033 75.731  98.714  1.00 30.13 ? 667  ASN A OD1   1 
ATOM   4932  N  ND2   . ASN A  1  669  ? -31.561 77.910  98.696  1.00 28.81 ? 667  ASN A ND2   1 
ATOM   4933  N  N     . ALA A  1  670  ? -33.253 75.672  103.452 1.00 20.03 ? 668  ALA A N     1 
ATOM   4934  C  CA    . ALA A  1  670  ? -33.330 75.594  104.908 1.00 21.29 ? 668  ALA A CA    1 
ATOM   4935  C  C     . ALA A  1  670  ? -33.286 74.148  105.379 1.00 21.81 ? 668  ALA A C     1 
ATOM   4936  O  O     . ALA A  1  670  ? -32.665 73.843  106.406 1.00 20.53 ? 668  ALA A O     1 
ATOM   4937  C  CB    . ALA A  1  670  ? -34.598 76.290  105.409 1.00 22.69 ? 668  ALA A CB    1 
ATOM   4938  N  N     . ILE A  1  671  ? -33.946 73.242  104.651 1.00 20.06 ? 669  ILE A N     1 
ATOM   4939  C  CA    . ILE A  1  671  ? -33.875 71.826  105.004 1.00 18.88 ? 669  ILE A CA    1 
ATOM   4940  C  C     . ILE A  1  671  ? -32.430 71.353  104.983 1.00 21.82 ? 669  ILE A C     1 
ATOM   4941  O  O     . ILE A  1  671  ? -31.951 70.702  105.922 1.00 21.43 ? 669  ILE A O     1 
ATOM   4942  C  CB    . ILE A  1  671  ? -34.740 70.979  104.055 1.00 20.19 ? 669  ILE A CB    1 
ATOM   4943  C  CG1   . ILE A  1  671  ? -36.223 71.254  104.280 1.00 22.13 ? 669  ILE A CG1   1 
ATOM   4944  C  CG2   . ILE A  1  671  ? -34.453 69.511  104.285 1.00 23.34 ? 669  ILE A CG2   1 
ATOM   4945  C  CD1   . ILE A  1  671  ? -37.126 70.687  103.162 1.00 24.63 ? 669  ILE A CD1   1 
ATOM   4946  N  N     . ALA A  1  672  ? -31.714 71.671  103.904 1.00 21.85 ? 670  ALA A N     1 
ATOM   4947  C  CA    . ALA A  1  672  ? -30.340 71.219  103.779 1.00 20.52 ? 670  ALA A CA    1 
ATOM   4948  C  C     . ALA A  1  672  ? -29.466 71.851  104.848 1.00 21.75 ? 670  ALA A C     1 
ATOM   4949  O  O     . ALA A  1  672  ? -28.551 71.201  105.362 1.00 21.65 ? 670  ALA A O     1 
ATOM   4950  C  CB    . ALA A  1  672  ? -29.813 71.530  102.378 1.00 23.76 ? 670  ALA A CB    1 
ATOM   4951  N  N     . GLU A  1  673  ? -29.773 73.091  105.229 1.00 19.79 ? 671  GLU A N     1 
ATOM   4952  C  CA    A GLU A  1  673  ? -29.039 73.760  106.298 0.54 18.89 ? 671  GLU A CA    1 
ATOM   4953  C  CA    B GLU A  1  673  ? -29.011 73.736  106.291 0.46 18.91 ? 671  GLU A CA    1 
ATOM   4954  C  C     . GLU A  1  673  ? -29.216 73.034  107.628 1.00 20.43 ? 671  GLU A C     1 
ATOM   4955  O  O     . GLU A  1  673  ? -28.246 72.787  108.356 1.00 19.82 ? 671  GLU A O     1 
ATOM   4956  C  CB    A GLU A  1  673  ? -29.518 75.206  106.399 0.54 20.78 ? 671  GLU A CB    1 
ATOM   4957  C  CB    B GLU A  1  673  ? -29.385 75.210  106.405 0.46 20.85 ? 671  GLU A CB    1 
ATOM   4958  C  CG    A GLU A  1  673  ? -28.916 75.974  107.543 0.54 25.78 ? 671  GLU A CG    1 
ATOM   4959  C  CG    B GLU A  1  673  ? -28.916 75.809  107.720 0.46 25.82 ? 671  GLU A CG    1 
ATOM   4960  C  CD    A GLU A  1  673  ? -27.664 76.709  107.150 0.54 23.19 ? 671  GLU A CD    1 
ATOM   4961  C  CD    B GLU A  1  673  ? -28.333 77.192  107.575 0.46 24.39 ? 671  GLU A CD    1 
ATOM   4962  O  OE1   A GLU A  1  673  ? -27.336 76.747  105.941 0.54 25.72 ? 671  GLU A OE1   1 
ATOM   4963  O  OE1   B GLU A  1  673  ? -28.778 77.938  106.683 0.46 22.91 ? 671  GLU A OE1   1 
ATOM   4964  O  OE2   A GLU A  1  673  ? -27.008 77.260  108.054 0.54 23.20 ? 671  GLU A OE2   1 
ATOM   4965  O  OE2   B GLU A  1  673  ? -27.428 77.533  108.364 0.46 22.84 ? 671  GLU A OE2   1 
ATOM   4966  N  N     . VAL A  1  674  ? -30.461 72.691  107.970 1.00 19.02 ? 672  VAL A N     1 
ATOM   4967  C  CA    . VAL A  1  674  ? -30.684 71.985  109.230 1.00 19.00 ? 672  VAL A CA    1 
ATOM   4968  C  C     . VAL A  1  674  ? -30.064 70.596  109.169 1.00 21.48 ? 672  VAL A C     1 
ATOM   4969  O  O     . VAL A  1  674  ? -29.458 70.130  110.144 1.00 19.65 ? 672  VAL A O     1 
ATOM   4970  C  CB    . VAL A  1  674  ? -32.184 71.921  109.572 1.00 21.16 ? 672  VAL A CB    1 
ATOM   4971  C  CG1   . VAL A  1  674  ? -32.387 71.147  110.873 1.00 19.48 ? 672  VAL A CG1   1 
ATOM   4972  C  CG2   . VAL A  1  674  ? -32.780 73.340  109.695 1.00 20.09 ? 672  VAL A CG2   1 
ATOM   4973  N  N     . ARG A  1  675  ? -30.183 69.920  108.018 1.00 20.72 ? 673  ARG A N     1 
ATOM   4974  C  CA    . ARG A  1  675  ? -29.523 68.626  107.863 1.00 16.79 ? 673  ARG A CA    1 
ATOM   4975  C  C     . ARG A  1  675  ? -28.029 68.744  108.099 1.00 17.50 ? 673  ARG A C     1 
ATOM   4976  O  O     . ARG A  1  675  ? -27.435 67.889  108.759 1.00 19.62 ? 673  ARG A O     1 
ATOM   4977  C  CB    . ARG A  1  675  ? -29.782 68.050  106.476 1.00 16.79 ? 673  ARG A CB    1 
ATOM   4978  C  CG    . ARG A  1  675  ? -31.183 67.532  106.284 1.00 20.24 ? 673  ARG A CG    1 
ATOM   4979  C  CD    . ARG A  1  675  ? -31.237 66.790  104.972 1.00 21.24 ? 673  ARG A CD    1 
ATOM   4980  N  NE    . ARG A  1  675  ? -30.516 65.529  105.074 1.00 20.44 ? 673  ARG A NE    1 
ATOM   4981  C  CZ    . ARG A  1  675  ? -30.143 64.809  104.027 1.00 22.16 ? 673  ARG A CZ    1 
ATOM   4982  N  NH1   . ARG A  1  675  ? -30.395 65.210  102.792 1.00 20.32 ? 673  ARG A NH1   1 
ATOM   4983  N  NH2   . ARG A  1  675  ? -29.503 63.662  104.226 1.00 18.89 ? 673  ARG A NH2   1 
ATOM   4984  N  N     . GLU A  1  676  ? -27.404 69.791  107.554 1.00 18.71 ? 674  GLU A N     1 
ATOM   4985  C  CA    . GLU A  1  676  ? -25.967 69.962  107.730 1.00 19.97 ? 674  GLU A CA    1 
ATOM   4986  C  C     . GLU A  1  676  ? -25.614 70.139  109.198 1.00 18.06 ? 674  GLU A C     1 
ATOM   4987  O  O     . GLU A  1  676  ? -24.613 69.598  109.674 1.00 18.62 ? 674  GLU A O     1 
ATOM   4988  C  CB    . GLU A  1  676  ? -25.469 71.162  106.932 1.00 17.90 ? 674  GLU A CB    1 
ATOM   4989  C  CG    . GLU A  1  676  ? -23.958 71.203  106.798 1.00 23.26 ? 674  GLU A CG    1 
ATOM   4990  C  CD    . GLU A  1  676  ? -23.494 70.657  105.456 1.00 39.87 ? 674  GLU A CD    1 
ATOM   4991  O  OE1   . GLU A  1  676  ? -24.321 70.028  104.755 1.00 48.51 ? 674  GLU A OE1   1 
ATOM   4992  O  OE2   . GLU A  1  676  ? -22.317 70.865  105.095 1.00 33.61 ? 674  GLU A OE2   1 
ATOM   4993  N  N     . ALA A  1  677  ? -26.423 70.903  109.931 1.00 19.33 ? 675  ALA A N     1 
ATOM   4994  C  CA    . ALA A  1  677  ? -26.152 71.075  111.350 1.00 17.59 ? 675  ALA A CA    1 
ATOM   4995  C  C     . ALA A  1  677  ? -26.247 69.747  112.077 1.00 19.80 ? 675  ALA A C     1 
ATOM   4996  O  O     . ALA A  1  677  ? -25.389 69.419  112.906 1.00 19.87 ? 675  ALA A O     1 
ATOM   4997  C  CB    . ALA A  1  677  ? -27.120 72.097  111.946 1.00 17.93 ? 675  ALA A CB    1 
ATOM   4998  N  N     . ILE A  1  678  ? -27.274 68.960  111.759 1.00 18.92 ? 676  ILE A N     1 
ATOM   4999  C  CA    . ILE A  1  678  ? -27.438 67.644  112.361 1.00 19.57 ? 676  ILE A CA    1 
ATOM   5000  C  C     . ILE A  1  678  ? -26.245 66.767  112.020 1.00 18.37 ? 676  ILE A C     1 
ATOM   5001  O  O     . ILE A  1  678  ? -25.716 66.042  112.878 1.00 19.45 ? 676  ILE A O     1 
ATOM   5002  C  CB    . ILE A  1  678  ? -28.758 67.018  111.874 1.00 19.22 ? 676  ILE A CB    1 
ATOM   5003  C  CG1   . ILE A  1  678  ? -29.951 67.807  112.429 1.00 20.66 ? 676  ILE A CG1   1 
ATOM   5004  C  CG2   . ILE A  1  678  ? -28.839 65.533  112.238 1.00 20.10 ? 676  ILE A CG2   1 
ATOM   5005  C  CD1   . ILE A  1  678  ? -31.250 67.509  111.678 1.00 18.88 ? 676  ILE A CD1   1 
ATOM   5006  N  N     . ASP A  1  679  ? -25.802 66.827  110.761 1.00 18.27 ? 677  ASP A N     1 
ATOM   5007  C  CA    . ASP A  1  679  ? -24.674 66.009  110.331 1.00 18.50 ? 677  ASP A CA    1 
ATOM   5008  C  C     . ASP A  1  679  ? -23.378 66.431  111.019 1.00 19.69 ? 677  ASP A C     1 
ATOM   5009  O  O     . ASP A  1  679  ? -22.591 65.569  111.419 1.00 19.33 ? 677  ASP A O     1 
ATOM   5010  C  CB    . ASP A  1  679  ? -24.551 66.079  108.810 1.00 18.73 ? 677  ASP A CB    1 
ATOM   5011  C  CG    . ASP A  1  679  ? -25.714 65.403  108.101 1.00 22.26 ? 677  ASP A CG    1 
ATOM   5012  O  OD1   . ASP A  1  679  ? -26.299 64.467  108.663 1.00 24.26 ? 677  ASP A OD1   1 
ATOM   5013  O  OD2   . ASP A  1  679  ? -26.019 65.789  106.956 1.00 27.47 ? 677  ASP A OD2   1 
ATOM   5014  N  N     . PHE A  1  680  ? -23.133 67.743  111.156 1.00 18.90 ? 678  PHE A N     1 
ATOM   5015  C  CA    . PHE A  1  680  ? -21.978 68.213  111.926 1.00 19.13 ? 678  PHE A CA    1 
ATOM   5016  C  C     . PHE A  1  680  ? -21.980 67.631  113.330 1.00 21.10 ? 678  PHE A C     1 
ATOM   5017  O  O     . PHE A  1  680  ? -20.962 67.110  113.802 1.00 19.20 ? 678  PHE A O     1 
ATOM   5018  C  CB    . PHE A  1  680  ? -21.965 69.736  112.027 1.00 18.68 ? 678  PHE A CB    1 
ATOM   5019  C  CG    . PHE A  1  680  ? -21.310 70.430  110.870 1.00 18.24 ? 678  PHE A CG    1 
ATOM   5020  C  CD1   . PHE A  1  680  ? -20.069 70.036  110.399 1.00 19.92 ? 678  PHE A CD1   1 
ATOM   5021  C  CD2   . PHE A  1  680  ? -21.950 71.492  110.251 1.00 18.11 ? 678  PHE A CD2   1 
ATOM   5022  C  CE1   . PHE A  1  680  ? -19.470 70.702  109.349 1.00 20.81 ? 678  PHE A CE1   1 
ATOM   5023  C  CE2   . PHE A  1  680  ? -21.368 72.154  109.190 1.00 19.97 ? 678  PHE A CE2   1 
ATOM   5024  C  CZ    . PHE A  1  680  ? -20.134 71.762  108.726 1.00 21.39 ? 678  PHE A CZ    1 
ATOM   5025  N  N     . LEU A  1  681  ? -23.112 67.753  114.028 1.00 19.57 ? 679  LEU A N     1 
ATOM   5026  C  CA    . LEU A  1  681  ? -23.202 67.256  115.391 1.00 18.20 ? 679  LEU A CA    1 
ATOM   5027  C  C     . LEU A  1  681  ? -22.864 65.773  115.443 1.00 21.18 ? 679  LEU A C     1 
ATOM   5028  O  O     . LEU A  1  681  ? -22.033 65.341  116.245 1.00 20.41 ? 679  LEU A O     1 
ATOM   5029  C  CB    . LEU A  1  681  ? -24.603 67.527  115.934 1.00 20.82 ? 679  LEU A CB    1 
ATOM   5030  C  CG    . LEU A  1  681  ? -24.904 69.011  116.178 1.00 21.31 ? 679  LEU A CG    1 
ATOM   5031  C  CD1   . LEU A  1  681  ? -26.406 69.275  116.239 1.00 20.14 ? 679  LEU A CD1   1 
ATOM   5032  C  CD2   . LEU A  1  681  ? -24.257 69.488  117.474 1.00 22.07 ? 679  LEU A CD2   1 
ATOM   5033  N  N     . ARG A  1  682  ? -23.474 64.979  114.564 1.00 19.39 ? 680  ARG A N     1 
ATOM   5034  C  CA    . ARG A  1  682  ? -23.265 63.540  114.617 1.00 18.89 ? 680  ARG A CA    1 
ATOM   5035  C  C     . ARG A  1  682  ? -21.890 63.150  114.120 1.00 21.14 ? 680  ARG A C     1 
ATOM   5036  O  O     . ARG A  1  682  ? -21.290 62.211  114.656 1.00 20.64 ? 680  ARG A O     1 
ATOM   5037  C  CB    . ARG A  1  682  ? -24.345 62.823  113.811 1.00 18.50 ? 680  ARG A CB    1 
ATOM   5038  C  CG    . ARG A  1  682  ? -25.667 62.844  114.510 1.00 21.31 ? 680  ARG A CG    1 
ATOM   5039  C  CD    . ARG A  1  682  ? -26.730 62.232  113.646 1.00 21.28 ? 680  ARG A CD    1 
ATOM   5040  N  NE    . ARG A  1  682  ? -28.023 62.274  114.308 1.00 21.46 ? 680  ARG A NE    1 
ATOM   5041  C  CZ    . ARG A  1  682  ? -29.177 62.088  113.685 1.00 26.04 ? 680  ARG A CZ    1 
ATOM   5042  N  NH1   . ARG A  1  682  ? -29.224 61.852  112.385 1.00 21.93 ? 680  ARG A NH1   1 
ATOM   5043  N  NH2   . ARG A  1  682  ? -30.306 62.135  114.385 1.00 25.27 ? 680  ARG A NH2   1 
ATOM   5044  N  N     . TYR A  1  683  ? -21.368 63.868  113.125 1.00 19.43 ? 681  TYR A N     1 
ATOM   5045  C  CA    . TYR A  1  683  ? -20.033 63.566  112.621 1.00 17.05 ? 681  TYR A CA    1 
ATOM   5046  C  C     . TYR A  1  683  ? -18.972 63.854  113.678 1.00 19.94 ? 681  TYR A C     1 
ATOM   5047  O  O     . TYR A  1  683  ? -18.116 63.003  113.957 1.00 18.90 ? 681  TYR A O     1 
ATOM   5048  C  CB    . TYR A  1  683  ? -19.769 64.368  111.348 1.00 18.24 ? 681  TYR A CB    1 
ATOM   5049  C  CG    . TYR A  1  683  ? -18.392 64.149  110.793 1.00 18.09 ? 681  TYR A CG    1 
ATOM   5050  C  CD1   . TYR A  1  683  ? -18.092 63.005  110.063 1.00 18.91 ? 681  TYR A CD1   1 
ATOM   5051  C  CD2   . TYR A  1  683  ? -17.387 65.083  111.013 1.00 17.44 ? 681  TYR A CD2   1 
ATOM   5052  C  CE1   . TYR A  1  683  ? -16.817 62.804  109.552 1.00 16.99 ? 681  TYR A CE1   1 
ATOM   5053  C  CE2   . TYR A  1  683  ? -16.120 64.890  110.526 1.00 19.11 ? 681  TYR A CE2   1 
ATOM   5054  C  CZ    . TYR A  1  683  ? -15.844 63.753  109.795 1.00 18.14 ? 681  TYR A CZ    1 
ATOM   5055  O  OH    . TYR A  1  683  ? -14.580 63.558  109.314 1.00 21.63 ? 681  TYR A OH    1 
ATOM   5056  N  N     . TYR A  1  684  ? -19.004 65.053  114.274 1.00 17.96 ? 682  TYR A N     1 
ATOM   5057  C  CA    . TYR A  1  684  ? -17.989 65.363  115.277 1.00 17.32 ? 682  TYR A CA    1 
ATOM   5058  C  C     . TYR A  1  684  ? -18.154 64.495  116.514 1.00 21.82 ? 682  TYR A C     1 
ATOM   5059  O  O     . TYR A  1  684  ? -17.159 64.179  117.171 1.00 19.14 ? 682  TYR A O     1 
ATOM   5060  C  CB    . TYR A  1  684  ? -18.021 66.844  115.655 1.00 19.40 ? 682  TYR A CB    1 
ATOM   5061  C  CG    . TYR A  1  684  ? -17.647 67.762  114.510 1.00 18.30 ? 682  TYR A CG    1 
ATOM   5062  C  CD1   . TYR A  1  684  ? -16.594 67.454  113.655 1.00 18.51 ? 682  TYR A CD1   1 
ATOM   5063  C  CD2   . TYR A  1  684  ? -18.361 68.928  114.277 1.00 18.78 ? 682  TYR A CD2   1 
ATOM   5064  C  CE1   . TYR A  1  684  ? -16.253 68.294  112.602 1.00 19.08 ? 682  TYR A CE1   1 
ATOM   5065  C  CE2   . TYR A  1  684  ? -18.034 69.768  113.236 1.00 16.50 ? 682  TYR A CE2   1 
ATOM   5066  C  CZ    . TYR A  1  684  ? -16.979 69.442  112.391 1.00 19.09 ? 682  TYR A CZ    1 
ATOM   5067  O  OH    . TYR A  1  684  ? -16.640 70.269  111.349 1.00 20.02 ? 682  TYR A OH    1 
ATOM   5068  N  N     . ALA A  1  685  ? -19.386 64.091  116.839 1.00 18.64 ? 683  ALA A N     1 
ATOM   5069  C  CA    . ALA A  1  685  ? -19.580 63.138  117.924 1.00 19.91 ? 683  ALA A CA    1 
ATOM   5070  C  C     . ALA A  1  685  ? -18.875 61.825  117.617 1.00 21.29 ? 683  ALA A C     1 
ATOM   5071  O  O     . ALA A  1  685  ? -18.165 61.277  118.464 1.00 19.98 ? 683  ALA A O     1 
ATOM   5072  C  CB    . ALA A  1  685  ? -21.070 62.891  118.167 1.00 20.76 ? 683  ALA A CB    1 
ATOM   5073  N  N     . GLU A  1  686  ? -19.075 61.294  116.415 1.00 19.21 ? 684  GLU A N     1 
ATOM   5074  C  CA    . GLU A  1  686  ? -18.448 60.022  116.071 1.00 19.79 ? 684  GLU A CA    1 
ATOM   5075  C  C     . GLU A  1  686  ? -16.935 60.167  115.983 1.00 22.73 ? 684  GLU A C     1 
ATOM   5076  O  O     . GLU A  1  686  ? -16.198 59.296  116.455 1.00 22.00 ? 684  GLU A O     1 
ATOM   5077  C  CB    . GLU A  1  686  ? -19.016 59.480  114.754 1.00 20.29 ? 684  GLU A CB    1 
ATOM   5078  C  CG    . GLU A  1  686  ? -18.290 58.229  114.227 1.00 26.45 ? 684  GLU A CG    1 
ATOM   5079  C  CD    . GLU A  1  686  ? -18.363 57.001  115.143 1.00 30.57 ? 684  GLU A CD    1 
ATOM   5080  O  OE1   . GLU A  1  686  ? -19.159 56.968  116.113 1.00 28.40 ? 684  GLU A OE1   1 
ATOM   5081  O  OE2   . GLU A  1  686  ? -17.616 56.034  114.877 1.00 30.99 ? 684  GLU A OE2   1 
ATOM   5082  N  N     . GLN A  1  687  ? -16.454 61.270  115.408 1.00 19.47 ? 685  GLN A N     1 
ATOM   5083  C  CA    . GLN A  1  687  ? -15.012 61.474  115.322 1.00 18.46 ? 685  GLN A CA    1 
ATOM   5084  C  C     . GLN A  1  687  ? -14.397 61.553  116.707 1.00 20.32 ? 685  GLN A C     1 
ATOM   5085  O  O     . GLN A  1  687  ? -13.285 61.063  116.935 1.00 20.87 ? 685  GLN A O     1 
ATOM   5086  C  CB    . GLN A  1  687  ? -14.696 62.739  114.527 1.00 17.33 ? 685  GLN A CB    1 
ATOM   5087  C  CG    . GLN A  1  687  ? -15.004 62.599  113.033 1.00 18.65 ? 685  GLN A CG    1 
ATOM   5088  C  CD    . GLN A  1  687  ? -14.234 61.450  112.399 1.00 21.73 ? 685  GLN A CD    1 
ATOM   5089  O  OE1   . GLN A  1  687  ? -13.002 61.395  112.478 1.00 22.72 ? 685  GLN A OE1   1 
ATOM   5090  N  NE2   . GLN A  1  687  ? -14.958 60.516  111.787 1.00 26.79 ? 685  GLN A NE2   1 
ATOM   5091  N  N     . THR A  1  688  ? -15.120 62.155  117.651 1.00 18.73 ? 686  THR A N     1 
ATOM   5092  C  CA    . THR A  1  688  ? -14.657 62.179  119.031 1.00 18.47 ? 686  THR A CA    1 
ATOM   5093  C  C     . THR A  1  688  ? -14.557 60.774  119.597 1.00 19.71 ? 686  THR A C     1 
ATOM   5094  O  O     . THR A  1  688  ? -13.541 60.405  120.199 1.00 22.29 ? 686  THR A O     1 
ATOM   5095  C  CB    . THR A  1  688  ? -15.602 63.019  119.881 1.00 20.60 ? 686  THR A CB    1 
ATOM   5096  O  OG1   . THR A  1  688  ? -15.471 64.383  119.488 1.00 21.07 ? 686  THR A OG1   1 
ATOM   5097  C  CG2   . THR A  1  688  ? -15.248 62.878  121.359 1.00 19.72 ? 686  THR A CG2   1 
ATOM   5098  N  N     . ARG A  1  689  ? -15.610 59.977  119.411 1.00 21.93 ? 687  ARG A N     1 
ATOM   5099  C  CA    . ARG A  1  689  ? -15.617 58.617  119.935 1.00 21.01 ? 687  ARG A CA    1 
ATOM   5100  C  C     . ARG A  1  689  ? -14.503 57.786  119.325 1.00 22.01 ? 687  ARG A C     1 
ATOM   5101  O  O     . ARG A  1  689  ? -14.032 56.828  119.951 1.00 24.14 ? 687  ARG A O     1 
ATOM   5102  C  CB    . ARG A  1  689  ? -16.972 57.957  119.677 1.00 22.35 ? 687  ARG A CB    1 
ATOM   5103  C  CG    . ARG A  1  689  ? -18.107 58.496  120.551 1.00 24.79 ? 687  ARG A CG    1 
ATOM   5104  C  CD    . ARG A  1  689  ? -19.345 57.644  120.378 1.00 24.57 ? 687  ARG A CD    1 
ATOM   5105  N  NE    . ARG A  1  689  ? -19.867 57.737  119.022 1.00 25.86 ? 687  ARG A NE    1 
ATOM   5106  C  CZ    . ARG A  1  689  ? -20.862 58.537  118.664 1.00 29.20 ? 687  ARG A CZ    1 
ATOM   5107  N  NH1   . ARG A  1  689  ? -21.471 59.314  119.546 1.00 28.92 ? 687  ARG A NH1   1 
ATOM   5108  N  NH2   . ARG A  1  689  ? -21.265 58.545  117.395 1.00 25.90 ? 687  ARG A NH2   1 
ATOM   5109  N  N     . ARG A  1  690  ? -14.068 58.142  118.116 1.00 21.34 ? 688  ARG A N     1 
ATOM   5110  C  CA    . ARG A  1  690  ? -12.968 57.441  117.476 1.00 21.51 ? 688  ARG A CA    1 
ATOM   5111  C  C     . ARG A  1  690  ? -11.598 57.886  117.969 1.00 24.21 ? 688  ARG A C     1 
ATOM   5112  O  O     . ARG A  1  690  ? -10.628 57.151  117.771 1.00 22.74 ? 688  ARG A O     1 
ATOM   5113  C  CB    . ARG A  1  690  ? -13.019 57.645  115.956 1.00 19.38 ? 688  ARG A CB    1 
ATOM   5114  C  CG    . ARG A  1  690  ? -14.234 57.044  115.267 1.00 23.92 ? 688  ARG A CG    1 
ATOM   5115  C  CD    . ARG A  1  690  ? -14.175 55.518  115.186 1.00 29.59 ? 688  ARG A CD    1 
ATOM   5116  N  NE    . ARG A  1  690  ? -13.032 55.058  114.402 1.00 27.66 ? 688  ARG A NE    1 
ATOM   5117  C  CZ    . ARG A  1  690  ? -11.985 54.432  114.918 1.00 29.20 ? 688  ARG A CZ    1 
ATOM   5118  N  NH1   . ARG A  1  690  ? -11.925 54.128  116.207 1.00 29.80 ? 688  ARG A NH1   1 
ATOM   5119  N  NH2   . ARG A  1  690  ? -10.970 54.106  114.125 1.00 26.50 ? 688  ARG A NH2   1 
ATOM   5120  N  N     . THR A  1  691  ? -11.473 59.073  118.570 1.00 20.65 ? 689  THR A N     1 
ATOM   5121  C  CA    . THR A  1  691  ? -10.126 59.614  118.726 1.00 19.44 ? 689  THR A CA    1 
ATOM   5122  C  C     . THR A  1  691  ? -9.755  60.102  120.120 1.00 26.27 ? 689  THR A C     1 
ATOM   5123  O  O     . THR A  1  691  ? -8.655  59.810  120.593 1.00 26.83 ? 689  THR A O     1 
ATOM   5124  C  CB    . THR A  1  691  ? -9.893  60.774  117.759 1.00 19.99 ? 689  THR A CB    1 
ATOM   5125  O  OG1   . THR A  1  691  ? -10.892 61.776  117.967 1.00 23.65 ? 689  THR A OG1   1 
ATOM   5126  C  CG2   . THR A  1  691  ? -9.940  60.293  116.296 1.00 23.68 ? 689  THR A CG2   1 
ATOM   5127  N  N     . LEU A  1  692  ? -10.611 60.886  120.769 1.00 22.95 ? 690  LEU A N     1 
ATOM   5128  C  CA    . LEU A  1  692  ? -10.128 61.732  121.857 1.00 22.46 ? 690  LEU A CA    1 
ATOM   5129  C  C     . LEU A  1  692  ? -9.915  60.949  123.144 1.00 26.24 ? 690  LEU A C     1 
ATOM   5130  O  O     . LEU A  1  692  ? -10.778 60.179  123.578 1.00 27.27 ? 690  LEU A O     1 
ATOM   5131  C  CB    . LEU A  1  692  ? -11.085 62.894  122.098 1.00 24.42 ? 690  LEU A CB    1 
ATOM   5132  C  CG    . LEU A  1  692  ? -11.089 63.911  120.952 1.00 24.91 ? 690  LEU A CG    1 
ATOM   5133  C  CD1   . LEU A  1  692  ? -11.896 65.141  121.353 1.00 24.67 ? 690  LEU A CD1   1 
ATOM   5134  C  CD2   . LEU A  1  692  ? -9.673  64.305  120.547 1.00 27.81 ? 690  LEU A CD2   1 
ATOM   5135  N  N     . GLY A  1  693  ? -8.760  61.173  123.753 1.00 22.62 ? 691  GLY A N     1 
ATOM   5136  C  CA    . GLY A  1  693  ? -8.381  60.526  124.982 1.00 25.83 ? 691  GLY A CA    1 
ATOM   5137  C  C     . GLY A  1  693  ? -7.788  61.537  125.934 1.00 29.62 ? 691  GLY A C     1 
ATOM   5138  O  O     . GLY A  1  693  ? -7.755  62.738  125.656 1.00 29.51 ? 691  GLY A O     1 
ATOM   5139  N  N     . PRO A  1  694  ? -7.289  61.058  127.073 1.00 29.09 ? 692  PRO A N     1 
ATOM   5140  C  CA    . PRO A  1  694  ? -6.830  61.988  128.121 1.00 30.95 ? 692  PRO A CA    1 
ATOM   5141  C  C     . PRO A  1  694  ? -5.668  62.870  127.702 1.00 29.85 ? 692  PRO A C     1 
ATOM   5142  O  O     . PRO A  1  694  ? -5.543  63.994  128.209 1.00 34.13 ? 692  PRO A O     1 
ATOM   5143  C  CB    . PRO A  1  694  ? -6.441  61.050  129.273 1.00 36.41 ? 692  PRO A CB    1 
ATOM   5144  C  CG    . PRO A  1  694  ? -7.214  59.796  129.027 1.00 34.60 ? 692  PRO A CG    1 
ATOM   5145  C  CD    . PRO A  1  694  ? -7.337  59.661  127.533 1.00 28.85 ? 692  PRO A CD    1 
ATOM   5146  N  N     . GLY A  1  695  ? -4.813  62.406  126.793 1.00 26.18 ? 693  GLY A N     1 
ATOM   5147  C  CA    . GLY A  1  695  ? -3.680  63.203  126.369 1.00 31.85 ? 693  GLY A CA    1 
ATOM   5148  C  C     . GLY A  1  695  ? -3.974  64.253  125.325 1.00 30.12 ? 693  GLY A C     1 
ATOM   5149  O  O     . GLY A  1  695  ? -3.067  65.000  124.949 1.00 31.30 ? 693  GLY A O     1 
ATOM   5150  N  N     . HIS A  1  696  ? -5.210  64.326  124.828 1.00 28.20 ? 694  HIS A N     1 
ATOM   5151  C  CA    . HIS A  1  696  ? -5.581  65.328  123.831 1.00 26.61 ? 694  HIS A CA    1 
ATOM   5152  C  C     . HIS A  1  696  ? -6.308  66.441  124.577 1.00 31.56 ? 694  HIS A C     1 
ATOM   5153  O  O     . HIS A  1  696  ? -7.532  66.561  124.551 1.00 28.94 ? 694  HIS A O     1 
ATOM   5154  C  CB    . HIS A  1  696  ? -6.426  64.701  122.719 1.00 27.88 ? 694  HIS A CB    1 
ATOM   5155  C  CG    . HIS A  1  696  ? -5.865  63.411  122.210 1.00 24.34 ? 694  HIS A CG    1 
ATOM   5156  N  ND1   . HIS A  1  696  ? -6.488  62.199  122.410 1.00 27.42 ? 694  HIS A ND1   1 
ATOM   5157  C  CD2   . HIS A  1  696  ? -4.715  63.139  121.546 1.00 25.41 ? 694  HIS A CD2   1 
ATOM   5158  C  CE1   . HIS A  1  696  ? -5.759  61.237  121.874 1.00 26.92 ? 694  HIS A CE1   1 
ATOM   5159  N  NE2   . HIS A  1  696  ? -4.678  61.781  121.341 1.00 27.00 ? 694  HIS A NE2   1 
ATOM   5160  N  N     . GLY A  1  697  ? -5.526  67.249  125.280 1.00 28.51 ? 695  GLY A N     1 
ATOM   5161  C  CA    . GLY A  1  697  ? -6.093  68.260  126.141 1.00 28.49 ? 695  GLY A CA    1 
ATOM   5162  C  C     . GLY A  1  697  ? -6.700  69.396  125.350 1.00 26.59 ? 695  GLY A C     1 
ATOM   5163  O  O     . GLY A  1  697  ? -6.214  69.772  124.281 1.00 26.91 ? 695  GLY A O     1 
ATOM   5164  N  N     . PRO A  1  698  ? -7.777  69.975  125.863 1.00 27.14 ? 696  PRO A N     1 
ATOM   5165  C  CA    . PRO A  1  698  ? -8.396  71.113  125.172 1.00 25.21 ? 696  PRO A CA    1 
ATOM   5166  C  C     . PRO A  1  698  ? -7.467  72.319  125.116 1.00 24.10 ? 696  PRO A C     1 
ATOM   5167  O  O     . PRO A  1  698  ? -6.565  72.484  125.943 1.00 27.84 ? 696  PRO A O     1 
ATOM   5168  C  CB    . PRO A  1  698  ? -9.635  71.414  126.023 1.00 31.39 ? 696  PRO A CB    1 
ATOM   5169  C  CG    . PRO A  1  698  ? -9.887  70.160  126.796 1.00 37.23 ? 696  PRO A CG    1 
ATOM   5170  C  CD    . PRO A  1  698  ? -8.546  69.551  127.044 1.00 36.38 ? 696  PRO A CD    1 
ATOM   5171  N  N     . LEU A  1  699  ? -7.695  73.168  124.113 1.00 23.52 ? 697  LEU A N     1 
ATOM   5172  C  CA    . LEU A  1  699  ? -7.008  74.455  124.060 1.00 25.06 ? 697  LEU A CA    1 
ATOM   5173  C  C     . LEU A  1  699  ? -7.428  75.354  125.207 1.00 24.08 ? 697  LEU A C     1 
ATOM   5174  O  O     . LEU A  1  699  ? -6.591  76.026  125.822 1.00 24.87 ? 697  LEU A O     1 
ATOM   5175  C  CB    . LEU A  1  699  ? -7.301  75.157  122.740 1.00 22.93 ? 697  LEU A CB    1 
ATOM   5176  C  CG    . LEU A  1  699  ? -6.824  74.445  121.490 1.00 25.12 ? 697  LEU A CG    1 
ATOM   5177  C  CD1   . LEU A  1  699  ? -7.263  75.273  120.307 1.00 24.73 ? 697  LEU A CD1   1 
ATOM   5178  C  CD2   . LEU A  1  699  ? -5.321  74.279  121.512 1.00 26.83 ? 697  LEU A CD2   1 
ATOM   5179  N  N     . GLY A  1  700  ? -8.728  75.395  125.501 1.00 22.46 ? 698  GLY A N     1 
ATOM   5180  C  CA    . GLY A  1  700  ? -9.267  76.385  126.400 1.00 23.32 ? 698  GLY A CA    1 
ATOM   5181  C  C     . GLY A  1  700  ? -10.410 77.109  125.728 1.00 23.53 ? 698  GLY A C     1 
ATOM   5182  O  O     . GLY A  1  700  ? -10.980 76.617  124.750 1.00 24.70 ? 698  GLY A O     1 
ATOM   5183  N  N     . PRO A  1  701  ? -10.767 78.295  126.218 1.00 24.25 ? 699  PRO A N     1 
ATOM   5184  C  CA    . PRO A  1  701  ? -11.905 79.015  125.621 1.00 23.15 ? 699  PRO A CA    1 
ATOM   5185  C  C     . PRO A  1  701  ? -11.672 79.269  124.138 1.00 23.40 ? 699  PRO A C     1 
ATOM   5186  O  O     . PRO A  1  701  ? -10.630 79.779  123.731 1.00 24.77 ? 699  PRO A O     1 
ATOM   5187  C  CB    . PRO A  1  701  ? -11.960 80.322  126.418 1.00 25.61 ? 699  PRO A CB    1 
ATOM   5188  C  CG    . PRO A  1  701  ? -11.294 79.990  127.737 1.00 29.00 ? 699  PRO A CG    1 
ATOM   5189  C  CD    . PRO A  1  701  ? -10.203 79.005  127.381 1.00 25.61 ? 699  PRO A CD    1 
ATOM   5190  N  N     . ILE A  1  702  ? -12.651 78.896  123.323 1.00 25.79 ? 700  ILE A N     1 
ATOM   5191  C  CA    A ILE A  1  702  ? -12.570 79.079  121.883 0.61 22.30 ? 700  ILE A CA    1 
ATOM   5192  C  CA    B ILE A  1  702  ? -12.585 79.060  121.876 0.39 22.33 ? 700  ILE A CA    1 
ATOM   5193  C  C     . ILE A  1  702  ? -13.652 80.060  121.466 1.00 22.92 ? 700  ILE A C     1 
ATOM   5194  O  O     . ILE A  1  702  ? -14.818 79.919  121.857 1.00 23.23 ? 700  ILE A O     1 
ATOM   5195  C  CB    A ILE A  1  702  ? -12.701 77.741  121.134 0.61 22.29 ? 700  ILE A CB    1 
ATOM   5196  C  CB    B ILE A  1  702  ? -12.790 77.721  121.146 0.39 22.30 ? 700  ILE A CB    1 
ATOM   5197  C  CG1   A ILE A  1  702  ? -11.414 76.930  121.311 0.61 23.82 ? 700  ILE A CG1   1 
ATOM   5198  C  CG1   B ILE A  1  702  ? -11.732 76.702  121.571 0.39 23.15 ? 700  ILE A CG1   1 
ATOM   5199  C  CG2   A ILE A  1  702  ? -13.009 77.966  119.653 0.61 23.21 ? 700  ILE A CG2   1 
ATOM   5200  C  CG2   B ILE A  1  702  ? -12.760 77.921  119.632 0.39 23.06 ? 700  ILE A CG2   1 
ATOM   5201  C  CD1   A ILE A  1  702  ? -11.421 75.595  120.626 0.61 23.76 ? 700  ILE A CD1   1 
ATOM   5202  C  CD1   B ILE A  1  702  ? -10.353 77.003  121.066 0.39 25.03 ? 700  ILE A CD1   1 
ATOM   5203  N  N     . VAL A  1  703  ? -13.260 81.057  120.678 1.00 22.03 ? 701  VAL A N     1 
ATOM   5204  C  CA    . VAL A  1  703  ? -14.198 82.028  120.131 1.00 19.81 ? 701  VAL A CA    1 
ATOM   5205  C  C     . VAL A  1  703  ? -14.641 81.525  118.763 1.00 21.82 ? 701  VAL A C     1 
ATOM   5206  O  O     . VAL A  1  703  ? -13.813 81.333  117.868 1.00 21.28 ? 701  VAL A O     1 
ATOM   5207  C  CB    . VAL A  1  703  ? -13.562 83.420  120.036 1.00 23.28 ? 701  VAL A CB    1 
ATOM   5208  C  CG1   . VAL A  1  703  ? -14.486 84.365  119.321 1.00 24.26 ? 701  VAL A CG1   1 
ATOM   5209  C  CG2   . VAL A  1  703  ? -13.271 83.947  121.435 1.00 25.97 ? 701  VAL A CG2   1 
ATOM   5210  N  N     . CYS A  1  704  ? -15.938 81.276  118.614 1.00 21.24 ? 702  CYS A N     1 
ATOM   5211  C  CA    . CYS A  1  704  ? -16.505 80.806  117.355 1.00 20.58 ? 702  CYS A CA    1 
ATOM   5212  C  C     . CYS A  1  704  ? -17.277 81.955  116.728 1.00 20.37 ? 702  CYS A C     1 
ATOM   5213  O  O     . CYS A  1  704  ? -18.271 82.423  117.291 1.00 21.90 ? 702  CYS A O     1 
ATOM   5214  C  CB    . CYS A  1  704  ? -17.417 79.601  117.571 1.00 20.08 ? 702  CYS A CB    1 
ATOM   5215  S  SG    . CYS A  1  704  ? -16.579 78.189  118.287 1.00 21.99 ? 702  CYS A SG    1 
ATOM   5216  N  N     . ILE A  1  705  ? -16.798 82.416  115.579 1.00 19.34 ? 703  ILE A N     1 
ATOM   5217  C  CA    . ILE A  1  705  ? -17.388 83.524  114.847 1.00 19.60 ? 703  ILE A CA    1 
ATOM   5218  C  C     . ILE A  1  705  ? -17.948 82.959  113.550 1.00 18.97 ? 703  ILE A C     1 
ATOM   5219  O  O     . ILE A  1  705  ? -17.210 82.362  112.759 1.00 22.12 ? 703  ILE A O     1 
ATOM   5220  C  CB    . ILE A  1  705  ? -16.344 84.621  114.597 1.00 22.98 ? 703  ILE A CB    1 
ATOM   5221  C  CG1   . ILE A  1  705  ? -15.878 85.193  115.938 1.00 26.66 ? 703  ILE A CG1   1 
ATOM   5222  C  CG2   . ILE A  1  705  ? -16.905 85.700  113.724 1.00 24.30 ? 703  ILE A CG2   1 
ATOM   5223  C  CD1   . ILE A  1  705  ? -14.632 86.045  115.839 1.00 27.82 ? 703  ILE A CD1   1 
ATOM   5224  N  N     . SER A  1  706  ? -19.248 83.135  113.335 1.00 22.41 ? 704  SER A N     1 
ATOM   5225  C  CA    . SER A  1  706  ? -19.934 82.455  112.249 1.00 22.98 ? 704  SER A CA    1 
ATOM   5226  C  C     . SER A  1  706  ? -20.597 83.447  111.305 1.00 24.55 ? 704  SER A C     1 
ATOM   5227  O  O     . SER A  1  706  ? -20.902 84.582  111.687 1.00 22.86 ? 704  SER A O     1 
ATOM   5228  C  CB    . SER A  1  706  ? -20.981 81.477  112.799 1.00 25.54 ? 704  SER A CB    1 
ATOM   5229  O  OG    . SER A  1  706  ? -21.816 82.133  113.720 1.00 24.88 ? 704  SER A OG    1 
ATOM   5230  N  N     . PRO A  1  707  ? -20.835 83.040  110.063 1.00 23.40 ? 705  PRO A N     1 
ATOM   5231  C  CA    . PRO A  1  707  ? -21.361 83.945  109.040 1.00 23.96 ? 705  PRO A CA    1 
ATOM   5232  C  C     . PRO A  1  707  ? -22.885 83.922  109.010 1.00 21.88 ? 705  PRO A C     1 
ATOM   5233  O  O     . PRO A  1  707  ? -23.535 83.078  109.627 1.00 23.14 ? 705  PRO A O     1 
ATOM   5234  C  CB    . PRO A  1  707  ? -20.778 83.347  107.752 1.00 20.83 ? 705  PRO A CB    1 
ATOM   5235  C  CG    . PRO A  1  707  ? -20.814 81.884  108.026 1.00 21.10 ? 705  PRO A CG    1 
ATOM   5236  C  CD    . PRO A  1  707  ? -20.417 81.752  109.484 1.00 23.98 ? 705  PRO A CD    1 
ATOM   5237  N  N     . TRP A  1  708  ? -23.454 84.875  108.266 1.00 23.91 ? 706  TRP A N     1 
ATOM   5238  C  CA    . TRP A  1  708  ? -24.907 84.948  108.173 1.00 21.28 ? 706  TRP A CA    1 
ATOM   5239  C  C     . TRP A  1  708  ? -25.473 84.008  107.121 1.00 21.00 ? 706  TRP A C     1 
ATOM   5240  O  O     . TRP A  1  708  ? -26.676 83.731  107.138 1.00 25.24 ? 706  TRP A O     1 
ATOM   5241  C  CB    . TRP A  1  708  ? -25.361 86.381  107.862 1.00 22.35 ? 706  TRP A CB    1 
ATOM   5242  C  CG    . TRP A  1  708  ? -24.607 86.998  106.737 1.00 25.98 ? 706  TRP A CG    1 
ATOM   5243  C  CD1   . TRP A  1  708  ? -23.531 87.820  106.847 1.00 35.26 ? 706  TRP A CD1   1 
ATOM   5244  C  CD2   . TRP A  1  708  ? -24.843 86.833  105.338 1.00 25.07 ? 706  TRP A CD2   1 
ATOM   5245  N  NE1   . TRP A  1  708  ? -23.079 88.177  105.607 1.00 32.46 ? 706  TRP A NE1   1 
ATOM   5246  C  CE2   . TRP A  1  708  ? -23.867 87.581  104.661 1.00 27.28 ? 706  TRP A CE2   1 
ATOM   5247  C  CE3   . TRP A  1  708  ? -25.795 86.140  104.593 1.00 20.40 ? 706  TRP A CE3   1 
ATOM   5248  C  CZ2   . TRP A  1  708  ? -23.803 87.646  103.273 1.00 32.32 ? 706  TRP A CZ2   1 
ATOM   5249  C  CZ3   . TRP A  1  708  ? -25.731 86.195  103.206 1.00 23.52 ? 706  TRP A CZ3   1 
ATOM   5250  C  CH2   . TRP A  1  708  ? -24.742 86.948  102.564 1.00 33.34 ? 706  TRP A CH2   1 
ATOM   5251  N  N     . ASN A  1  709  ? -24.640 83.507  106.214 1.00 20.80 ? 707  ASN A N     1 
ATOM   5252  C  CA    . ASN A  1  709  ? -25.198 82.811  105.065 1.00 21.78 ? 707  ASN A CA    1 
ATOM   5253  C  C     . ASN A  1  709  ? -25.490 81.351  105.348 1.00 22.02 ? 707  ASN A C     1 
ATOM   5254  O  O     . ASN A  1  709  ? -26.326 80.764  104.664 1.00 23.77 ? 707  ASN A O     1 
ATOM   5255  C  CB    . ASN A  1  709  ? -24.260 82.939  103.872 1.00 19.60 ? 707  ASN A CB    1 
ATOM   5256  C  CG    . ASN A  1  709  ? -22.987 82.159  104.051 1.00 24.55 ? 707  ASN A CG    1 
ATOM   5257  O  OD1   . ASN A  1  709  ? -22.389 82.146  105.124 1.00 26.90 ? 707  ASN A OD1   1 
ATOM   5258  N  ND2   . ASN A  1  709  ? -22.561 81.492  102.987 1.00 29.69 ? 707  ASN A ND2   1 
ATOM   5259  N  N     . PHE A  1  710  ? -24.830 80.755  106.332 1.00 22.93 ? 708  PHE A N     1 
ATOM   5260  C  CA    . PHE A  1  710  ? -25.194 79.439  106.846 1.00 21.80 ? 708  PHE A CA    1 
ATOM   5261  C  C     . PHE A  1  710  ? -25.385 79.610  108.344 1.00 22.21 ? 708  PHE A C     1 
ATOM   5262  O  O     . PHE A  1  710  ? -24.569 79.152  109.152 1.00 20.99 ? 708  PHE A O     1 
ATOM   5263  C  CB    . PHE A  1  710  ? -24.131 78.384  106.526 1.00 21.87 ? 708  PHE A CB    1 
ATOM   5264  C  CG    . PHE A  1  710  ? -23.917 78.151  105.045 1.00 29.04 ? 708  PHE A CG    1 
ATOM   5265  C  CD1   . PHE A  1  710  ? -24.988 78.008  104.186 1.00 35.05 ? 708  PHE A CD1   1 
ATOM   5266  C  CD2   . PHE A  1  710  ? -22.634 78.068  104.522 1.00 33.10 ? 708  PHE A CD2   1 
ATOM   5267  C  CE1   . PHE A  1  710  ? -24.790 77.786  102.830 1.00 32.63 ? 708  PHE A CE1   1 
ATOM   5268  C  CE2   . PHE A  1  710  ? -22.424 77.839  103.171 1.00 31.73 ? 708  PHE A CE2   1 
ATOM   5269  C  CZ    . PHE A  1  710  ? -23.509 77.708  102.323 1.00 30.22 ? 708  PHE A CZ    1 
ATOM   5270  N  N     . PRO A  1  711  ? -26.461 80.291  108.747 1.00 21.66 ? 709  PRO A N     1 
ATOM   5271  C  CA    . PRO A  1  711  ? -26.556 80.773  110.130 1.00 22.12 ? 709  PRO A CA    1 
ATOM   5272  C  C     . PRO A  1  711  ? -26.861 79.700  111.157 1.00 22.02 ? 709  PRO A C     1 
ATOM   5273  O  O     . PRO A  1  711  ? -26.756 79.978  112.356 1.00 21.28 ? 709  PRO A O     1 
ATOM   5274  C  CB    . PRO A  1  711  ? -27.692 81.795  110.052 1.00 24.05 ? 709  PRO A CB    1 
ATOM   5275  C  CG    . PRO A  1  711  ? -28.568 81.264  108.975 1.00 21.48 ? 709  PRO A CG    1 
ATOM   5276  C  CD    . PRO A  1  711  ? -27.621 80.706  107.937 1.00 20.45 ? 709  PRO A CD    1 
ATOM   5277  N  N     . LEU A  1  712  ? -27.252 78.500  110.746 1.00 23.60 ? 710  LEU A N     1 
ATOM   5278  C  CA    . LEU A  1  712  ? -27.346 77.381  111.675 1.00 20.93 ? 710  LEU A CA    1 
ATOM   5279  C  C     . LEU A  1  712  ? -26.250 76.352  111.462 1.00 19.26 ? 710  LEU A C     1 
ATOM   5280  O  O     . LEU A  1  712  ? -25.656 75.879  112.426 1.00 20.90 ? 710  LEU A O     1 
ATOM   5281  C  CB    . LEU A  1  712  ? -28.712 76.687  111.556 1.00 19.77 ? 710  LEU A CB    1 
ATOM   5282  C  CG    . LEU A  1  712  ? -28.876 75.560  112.579 1.00 21.05 ? 710  LEU A CG    1 
ATOM   5283  C  CD1   . LEU A  1  712  ? -28.818 76.132  114.001 1.00 20.26 ? 710  LEU A CD1   1 
ATOM   5284  C  CD2   . LEU A  1  712  ? -30.159 74.777  112.351 1.00 22.71 ? 710  LEU A CD2   1 
ATOM   5285  N  N     . ALA A  1  713  ? -25.929 76.027  110.215 1.00 19.30 ? 711  ALA A N     1 
ATOM   5286  C  CA    . ALA A  1  713  ? -25.053 74.892  109.975 1.00 19.22 ? 711  ALA A CA    1 
ATOM   5287  C  C     . ALA A  1  713  ? -23.612 75.208  110.360 1.00 21.88 ? 711  ALA A C     1 
ATOM   5288  O  O     . ALA A  1  713  ? -22.991 74.468  111.129 1.00 21.13 ? 711  ALA A O     1 
ATOM   5289  C  CB    . ALA A  1  713  ? -25.151 74.468  108.515 1.00 20.53 ? 711  ALA A CB    1 
ATOM   5290  N  N     . ILE A  1  714  ? -23.047 76.287  109.820 1.00 21.11 ? 712  ILE A N     1 
ATOM   5291  C  CA    . ILE A  1  714  ? -21.661 76.604  110.160 1.00 18.70 ? 712  ILE A CA    1 
ATOM   5292  C  C     . ILE A  1  714  ? -21.552 77.040  111.613 1.00 21.35 ? 712  ILE A C     1 
ATOM   5293  O  O     . ILE A  1  714  ? -20.594 76.687  112.316 1.00 20.95 ? 712  ILE A O     1 
ATOM   5294  C  CB    . ILE A  1  714  ? -21.109 77.658  109.194 1.00 20.39 ? 712  ILE A CB    1 
ATOM   5295  C  CG1   . ILE A  1  714  ? -20.958 76.997  107.820 1.00 24.07 ? 712  ILE A CG1   1 
ATOM   5296  C  CG2   . ILE A  1  714  ? -19.769 78.241  109.728 1.00 20.24 ? 712  ILE A CG2   1 
ATOM   5297  C  CD1   . ILE A  1  714  ? -20.152 77.782  106.865 1.00 32.00 ? 712  ILE A CD1   1 
ATOM   5298  N  N     . PHE A  1  715  ? -22.528 77.814  112.086 1.00 23.27 ? 713  PHE A N     1 
ATOM   5299  C  CA    . PHE A  1  715  ? -22.626 78.117  113.508 1.00 19.96 ? 713  PHE A CA    1 
ATOM   5300  C  C     . PHE A  1  715  ? -22.528 76.852  114.355 1.00 21.03 ? 713  PHE A C     1 
ATOM   5301  O  O     . PHE A  1  715  ? -21.699 76.762  115.269 1.00 20.64 ? 713  PHE A O     1 
ATOM   5302  C  CB    . PHE A  1  715  ? -23.946 78.845  113.768 1.00 19.66 ? 713  PHE A CB    1 
ATOM   5303  C  CG    . PHE A  1  715  ? -24.210 79.140  115.201 1.00 21.75 ? 713  PHE A CG    1 
ATOM   5304  C  CD1   . PHE A  1  715  ? -23.645 80.252  115.803 1.00 24.32 ? 713  PHE A CD1   1 
ATOM   5305  C  CD2   . PHE A  1  715  ? -25.045 78.322  115.954 1.00 22.94 ? 713  PHE A CD2   1 
ATOM   5306  C  CE1   . PHE A  1  715  ? -23.907 80.542  117.131 1.00 26.07 ? 713  PHE A CE1   1 
ATOM   5307  C  CE2   . PHE A  1  715  ? -25.299 78.603  117.290 1.00 23.64 ? 713  PHE A CE2   1 
ATOM   5308  C  CZ    . PHE A  1  715  ? -24.736 79.718  117.876 1.00 27.44 ? 713  PHE A CZ    1 
ATOM   5309  N  N     . THR A  1  716  ? -23.371 75.862  114.062 1.00 20.13 ? 714  THR A N     1 
ATOM   5310  C  CA    . THR A  1  716  ? -23.386 74.638  114.854 1.00 19.70 ? 714  THR A CA    1 
ATOM   5311  C  C     . THR A  1  716  ? -22.095 73.858  114.687 1.00 19.15 ? 714  THR A C     1 
ATOM   5312  O  O     . THR A  1  716  ? -21.540 73.352  115.669 1.00 20.51 ? 714  THR A O     1 
ATOM   5313  C  CB    . THR A  1  716  ? -24.597 73.788  114.462 1.00 21.86 ? 714  THR A CB    1 
ATOM   5314  O  OG1   . THR A  1  716  ? -25.791 74.522  114.751 1.00 21.22 ? 714  THR A OG1   1 
ATOM   5315  C  CG2   . THR A  1  716  ? -24.622 72.485  115.232 1.00 24.47 ? 714  THR A CG2   1 
ATOM   5316  N  N     . GLY A  1  717  ? -21.595 73.766  113.452 1.00 18.47 ? 715  GLY A N     1 
ATOM   5317  C  CA    . GLY A  1  717  ? -20.398 72.978  113.209 1.00 19.82 ? 715  GLY A CA    1 
ATOM   5318  C  C     . GLY A  1  717  ? -19.219 73.451  114.038 1.00 19.67 ? 715  GLY A C     1 
ATOM   5319  O  O     . GLY A  1  717  ? -18.564 72.660  114.714 1.00 21.13 ? 715  GLY A O     1 
ATOM   5320  N  N     . GLN A  1  718  ? -18.942 74.754  114.007 1.00 17.77 ? 716  GLN A N     1 
ATOM   5321  C  CA    . GLN A  1  718  ? -17.774 75.257  114.727 1.00 18.30 ? 716  GLN A CA    1 
ATOM   5322  C  C     . GLN A  1  718  ? -17.930 75.032  116.222 1.00 19.92 ? 716  GLN A C     1 
ATOM   5323  O  O     . GLN A  1  718  ? -17.016 74.541  116.893 1.00 19.99 ? 716  GLN A O     1 
ATOM   5324  C  CB    . GLN A  1  718  ? -17.567 76.742  114.437 1.00 19.73 ? 716  GLN A CB    1 
ATOM   5325  C  CG    . GLN A  1  718  ? -17.246 77.036  112.979 1.00 19.96 ? 716  GLN A CG    1 
ATOM   5326  C  CD    . GLN A  1  718  ? -16.876 78.490  112.737 1.00 21.89 ? 716  GLN A CD    1 
ATOM   5327  O  OE1   . GLN A  1  718  ? -15.944 78.779  111.992 1.00 22.91 ? 716  GLN A OE1   1 
ATOM   5328  N  NE2   . GLN A  1  718  ? -17.605 79.410  113.358 1.00 20.26 ? 716  GLN A NE2   1 
ATOM   5329  N  N     . ILE A  1  719  ? -19.094 75.388  116.760 1.00 21.44 ? 717  ILE A N     1 
ATOM   5330  C  CA    . ILE A  1  719  ? -19.317 75.275  118.195 1.00 19.11 ? 717  ILE A CA    1 
ATOM   5331  C  C     . ILE A  1  719  ? -19.277 73.823  118.633 1.00 21.94 ? 717  ILE A C     1 
ATOM   5332  O  O     . ILE A  1  719  ? -18.690 73.492  119.671 1.00 22.38 ? 717  ILE A O     1 
ATOM   5333  C  CB    . ILE A  1  719  ? -20.650 75.944  118.558 1.00 22.72 ? 717  ILE A CB    1 
ATOM   5334  C  CG1   . ILE A  1  719  ? -20.516 77.444  118.373 1.00 22.10 ? 717  ILE A CG1   1 
ATOM   5335  C  CG2   . ILE A  1  719  ? -21.067 75.590  119.959 1.00 29.29 ? 717  ILE A CG2   1 
ATOM   5336  C  CD1   . ILE A  1  719  ? -21.830 78.097  118.267 1.00 31.77 ? 717  ILE A CD1   1 
ATOM   5337  N  N     . ALA A  1  720  ? -19.899 72.936  117.856 1.00 20.31 ? 718  ALA A N     1 
ATOM   5338  C  CA    . ALA A  1  720  ? -19.962 71.532  118.240 1.00 23.89 ? 718  ALA A CA    1 
ATOM   5339  C  C     . ALA A  1  720  ? -18.572 70.927  118.283 1.00 19.21 ? 718  ALA A C     1 
ATOM   5340  O  O     . ALA A  1  720  ? -18.228 70.212  119.226 1.00 21.42 ? 718  ALA A O     1 
ATOM   5341  C  CB    . ALA A  1  720  ? -20.848 70.751  117.270 1.00 22.35 ? 718  ALA A CB    1 
ATOM   5342  N  N     . ALA A  1  721  ? -17.768 71.204  117.255 1.00 21.35 ? 719  ALA A N     1 
ATOM   5343  C  CA    . ALA A  1  721  ? -16.395 70.714  117.236 1.00 18.85 ? 719  ALA A CA    1 
ATOM   5344  C  C     . ALA A  1  721  ? -15.627 71.203  118.458 1.00 18.71 ? 719  ALA A C     1 
ATOM   5345  O  O     . ALA A  1  721  ? -14.999 70.411  119.167 1.00 20.79 ? 719  ALA A O     1 
ATOM   5346  C  CB    . ALA A  1  721  ? -15.697 71.168  115.957 1.00 18.87 ? 719  ALA A CB    1 
ATOM   5347  N  N     . ALA A  1  722  ? -15.664 72.512  118.715 1.00 19.68 ? 720  ALA A N     1 
ATOM   5348  C  CA    . ALA A  1  722  ? -14.893 73.049  119.829 1.00 21.32 ? 720  ALA A CA    1 
ATOM   5349  C  C     . ALA A  1  722  ? -15.368 72.460  121.152 1.00 22.88 ? 720  ALA A C     1 
ATOM   5350  O  O     . ALA A  1  722  ? -14.554 72.041  121.981 1.00 22.72 ? 720  ALA A O     1 
ATOM   5351  C  CB    . ALA A  1  722  ? -14.978 74.577  119.849 1.00 20.50 ? 720  ALA A CB    1 
ATOM   5352  N  N     . LEU A  1  723  ? -16.688 72.380  121.343 1.00 20.10 ? 721  LEU A N     1 
ATOM   5353  C  CA    . LEU A  1  723  ? -17.234 71.835  122.580 1.00 20.31 ? 721  LEU A CA    1 
ATOM   5354  C  C     . LEU A  1  723  ? -16.830 70.383  122.770 1.00 22.31 ? 721  LEU A C     1 
ATOM   5355  O  O     . LEU A  1  723  ? -16.432 69.970  123.864 1.00 21.48 ? 721  LEU A O     1 
ATOM   5356  C  CB    . LEU A  1  723  ? -18.752 71.945  122.568 1.00 22.18 ? 721  LEU A CB    1 
ATOM   5357  C  CG    . LEU A  1  723  ? -19.392 73.308  122.745 1.00 21.07 ? 721  LEU A CG    1 
ATOM   5358  C  CD1   . LEU A  1  723  ? -20.878 73.163  122.487 1.00 24.33 ? 721  LEU A CD1   1 
ATOM   5359  C  CD2   . LEU A  1  723  ? -19.131 73.803  124.154 1.00 23.04 ? 721  LEU A CD2   1 
ATOM   5360  N  N     . VAL A  1  724  ? -16.945 69.580  121.713 1.00 22.55 ? 722  VAL A N     1 
ATOM   5361  C  CA    . VAL A  1  724  ? -16.735 68.152  121.898 1.00 21.90 ? 722  VAL A CA    1 
ATOM   5362  C  C     . VAL A  1  724  ? -15.256 67.858  122.104 1.00 22.31 ? 722  VAL A C     1 
ATOM   5363  O  O     . VAL A  1  724  ? -14.904 66.850  122.719 1.00 21.93 ? 722  VAL A O     1 
ATOM   5364  C  CB    . VAL A  1  724  ? -17.336 67.369  120.714 1.00 20.17 ? 722  VAL A CB    1 
ATOM   5365  C  CG1   . VAL A  1  724  ? -16.399 67.381  119.500 1.00 22.63 ? 722  VAL A CG1   1 
ATOM   5366  C  CG2   . VAL A  1  724  ? -17.716 65.956  121.135 1.00 22.67 ? 722  VAL A CG2   1 
ATOM   5367  N  N     . ALA A  1  725  ? -14.374 68.729  121.606 1.00 22.30 ? 723  ALA A N     1 
ATOM   5368  C  CA    . ALA A  1  725  ? -12.947 68.629  121.894 1.00 23.44 ? 723  ALA A CA    1 
ATOM   5369  C  C     . ALA A  1  725  ? -12.601 69.069  123.315 1.00 22.60 ? 723  ALA A C     1 
ATOM   5370  O  O     . ALA A  1  725  ? -11.418 69.055  123.676 1.00 26.20 ? 723  ALA A O     1 
ATOM   5371  C  CB    . ALA A  1  725  ? -12.148 69.453  120.887 1.00 21.91 ? 723  ALA A CB    1 
ATOM   5372  N  N     . GLY A  1  726  ? -13.587 69.452  124.124 1.00 23.39 ? 724  GLY A N     1 
ATOM   5373  C  CA    . GLY A  1  726  ? -13.346 69.792  125.507 1.00 22.66 ? 724  GLY A CA    1 
ATOM   5374  C  C     . GLY A  1  726  ? -13.169 71.261  125.804 1.00 24.40 ? 724  GLY A C     1 
ATOM   5375  O  O     . GLY A  1  726  ? -12.758 71.601  126.919 1.00 26.03 ? 724  GLY A O     1 
ATOM   5376  N  N     . ASN A  1  727  ? -13.457 72.131  124.859 1.00 22.43 ? 725  ASN A N     1 
ATOM   5377  C  CA    . ASN A  1  727  ? -13.268 73.568  124.999 1.00 25.03 ? 725  ASN A CA    1 
ATOM   5378  C  C     . ASN A  1  727  ? -14.584 74.256  125.301 1.00 23.18 ? 725  ASN A C     1 
ATOM   5379  O  O     . ASN A  1  727  ? -15.579 74.009  124.610 1.00 23.20 ? 725  ASN A O     1 
ATOM   5380  C  CB    . ASN A  1  727  ? -12.701 74.155  123.717 1.00 23.53 ? 725  ASN A CB    1 
ATOM   5381  C  CG    . ASN A  1  727  ? -11.447 73.451  123.258 1.00 23.37 ? 725  ASN A CG    1 
ATOM   5382  O  OD1   . ASN A  1  727  ? -10.372 73.636  123.827 1.00 24.28 ? 725  ASN A OD1   1 
ATOM   5383  N  ND2   . ASN A  1  727  ? -11.578 72.645  122.215 1.00 22.12 ? 725  ASN A ND2   1 
ATOM   5384  N  N     . PRO A  1  728  ? -14.620 75.154  126.273 1.00 23.20 ? 726  PRO A N     1 
ATOM   5385  C  CA    . PRO A  1  728  ? -15.787 76.024  126.416 1.00 26.75 ? 726  PRO A CA    1 
ATOM   5386  C  C     . PRO A  1  728  ? -15.790 77.031  125.282 1.00 25.03 ? 726  PRO A C     1 
ATOM   5387  O  O     . PRO A  1  728  ? -14.736 77.427  124.777 1.00 25.15 ? 726  PRO A O     1 
ATOM   5388  C  CB    . PRO A  1  728  ? -15.566 76.692  127.778 1.00 24.88 ? 726  PRO A CB    1 
ATOM   5389  C  CG    . PRO A  1  728  ? -14.083 76.718  127.932 1.00 25.30 ? 726  PRO A CG    1 
ATOM   5390  C  CD    . PRO A  1  728  ? -13.552 75.487  127.232 1.00 24.11 ? 726  PRO A CD    1 
ATOM   5391  N  N     . VAL A  1  729  ? -16.990 77.434  124.866 1.00 23.64 ? 727  VAL A N     1 
ATOM   5392  C  CA    . VAL A  1  729  ? -17.168 78.199  123.641 1.00 21.77 ? 727  VAL A CA    1 
ATOM   5393  C  C     . VAL A  1  729  ? -17.834 79.537  123.927 1.00 24.12 ? 727  VAL A C     1 
ATOM   5394  O  O     . VAL A  1  729  ? -18.797 79.624  124.697 1.00 25.06 ? 727  VAL A O     1 
ATOM   5395  C  CB    . VAL A  1  729  ? -17.988 77.398  122.609 1.00 20.88 ? 727  VAL A CB    1 
ATOM   5396  C  CG1   . VAL A  1  729  ? -18.404 78.280  121.424 1.00 21.95 ? 727  VAL A CG1   1 
ATOM   5397  C  CG2   . VAL A  1  729  ? -17.181 76.216  122.130 1.00 22.50 ? 727  VAL A CG2   1 
ATOM   5398  N  N     . LEU A  1  730  ? -17.329 80.570  123.262 1.00 21.92 ? 728  LEU A N     1 
ATOM   5399  C  CA    . LEU A  1  730  ? -17.979 81.865  123.146 1.00 23.93 ? 728  LEU A CA    1 
ATOM   5400  C  C     . LEU A  1  730  ? -18.481 81.941  121.712 1.00 23.50 ? 728  LEU A C     1 
ATOM   5401  O  O     . LEU A  1  730  ? -17.678 82.013  120.779 1.00 23.47 ? 728  LEU A O     1 
ATOM   5402  C  CB    . LEU A  1  730  ? -17.013 83.007  123.448 1.00 25.16 ? 728  LEU A CB    1 
ATOM   5403  C  CG    . LEU A  1  730  ? -16.275 83.059  124.792 1.00 22.10 ? 728  LEU A CG    1 
ATOM   5404  C  CD1   . LEU A  1  730  ? -17.280 82.857  125.925 1.00 23.66 ? 728  LEU A CD1   1 
ATOM   5405  C  CD2   . LEU A  1  730  ? -15.159 82.047  124.869 1.00 24.51 ? 728  LEU A CD2   1 
ATOM   5406  N  N     . ALA A  1  731  ? -19.796 81.905  121.536 1.00 23.76 ? 729  ALA A N     1 
ATOM   5407  C  CA    . ALA A  1  731  ? -20.408 81.849  120.212 1.00 21.96 ? 729  ALA A CA    1 
ATOM   5408  C  C     . ALA A  1  731  ? -20.822 83.258  119.805 1.00 22.41 ? 729  ALA A C     1 
ATOM   5409  O  O     . ALA A  1  731  ? -21.707 83.860  120.426 1.00 27.21 ? 729  ALA A O     1 
ATOM   5410  C  CB    . ALA A  1  731  ? -21.604 80.903  120.208 1.00 23.46 ? 729  ALA A CB    1 
ATOM   5411  N  N     . LYS A  1  732  ? -20.181 83.788  118.766 1.00 22.25 ? 730  LYS A N     1 
ATOM   5412  C  CA    . LYS A  1  732  ? -20.515 85.119  118.268 1.00 23.59 ? 730  LYS A CA    1 
ATOM   5413  C  C     . LYS A  1  732  ? -21.162 84.960  116.902 1.00 23.27 ? 730  LYS A C     1 
ATOM   5414  O  O     . LYS A  1  732  ? -20.450 84.808  115.895 1.00 23.95 ? 730  LYS A O     1 
ATOM   5415  C  CB    . LYS A  1  732  ? -19.261 85.995  118.174 1.00 23.61 ? 730  LYS A CB    1 
ATOM   5416  C  CG    . LYS A  1  732  ? -19.481 87.462  118.518 1.00 29.64 ? 730  LYS A CG    1 
ATOM   5417  C  CD    . LYS A  1  732  ? -20.470 88.130  117.563 1.00 28.50 ? 730  LYS A CD    1 
ATOM   5418  C  CE    . LYS A  1  732  ? -19.888 88.252  116.168 1.00 32.97 ? 730  LYS A CE    1 
ATOM   5419  N  NZ    . LYS A  1  732  ? -20.870 88.906  115.262 1.00 30.26 ? 730  LYS A NZ    1 
ATOM   5420  N  N     . PRO A  1  733  ? -22.487 84.962  116.810 1.00 21.92 ? 731  PRO A N     1 
ATOM   5421  C  CA    . PRO A  1  733  ? -23.138 84.806  115.509 1.00 22.54 ? 731  PRO A CA    1 
ATOM   5422  C  C     . PRO A  1  733  ? -23.088 86.102  114.723 1.00 22.13 ? 731  PRO A C     1 
ATOM   5423  O  O     . PRO A  1  733  ? -22.929 87.193  115.274 1.00 24.57 ? 731  PRO A O     1 
ATOM   5424  C  CB    . PRO A  1  733  ? -24.582 84.452  115.875 1.00 25.37 ? 731  PRO A CB    1 
ATOM   5425  C  CG    . PRO A  1  733  ? -24.805 85.171  117.158 1.00 25.17 ? 731  PRO A CG    1 
ATOM   5426  C  CD    . PRO A  1  733  ? -23.467 85.124  117.897 1.00 25.53 ? 731  PRO A CD    1 
ATOM   5427  N  N     . ALA A  1  734  ? -23.239 85.960  113.410 1.00 21.53 ? 732  ALA A N     1 
ATOM   5428  C  CA    . ALA A  1  734  ? -23.367 87.126  112.550 1.00 24.03 ? 732  ALA A CA    1 
ATOM   5429  C  C     . ALA A  1  734  ? -24.442 88.072  113.065 1.00 25.36 ? 732  ALA A C     1 
ATOM   5430  O  O     . ALA A  1  734  ? -25.507 87.646  113.524 1.00 26.55 ? 732  ALA A O     1 
ATOM   5431  C  CB    . ALA A  1  734  ? -23.715 86.687  111.130 1.00 22.59 ? 732  ALA A CB    1 
ATOM   5432  N  N     . GLU A  1  735  ? -24.162 89.371  112.973 1.00 23.80 ? 733  GLU A N     1 
ATOM   5433  C  CA    . GLU A  1  735  ? -25.137 90.359  113.414 1.00 24.57 ? 733  GLU A CA    1 
ATOM   5434  C  C     . GLU A  1  735  ? -26.460 90.218  112.669 1.00 26.88 ? 733  GLU A C     1 
ATOM   5435  O  O     . GLU A  1  735  ? -27.519 90.526  113.224 1.00 25.17 ? 733  GLU A O     1 
ATOM   5436  C  CB    . GLU A  1  735  ? -24.569 91.769  113.243 1.00 29.69 ? 733  GLU A CB    1 
ATOM   5437  C  CG    . GLU A  1  735  ? -24.081 92.105  111.841 1.00 38.91 ? 733  GLU A CG    1 
ATOM   5438  C  CD    . GLU A  1  735  ? -22.589 91.831  111.651 1.00 43.66 ? 733  GLU A CD    1 
ATOM   5439  O  OE1   . GLU A  1  735  ? -22.053 90.902  112.300 1.00 41.03 ? 733  GLU A OE1   1 
ATOM   5440  O  OE2   . GLU A  1  735  ? -21.953 92.554  110.853 1.00 42.19 ? 733  GLU A OE2   1 
ATOM   5441  N  N     . GLU A  1  736  ? -26.428 89.721  111.433 1.00 26.43 ? 734  GLU A N     1 
ATOM   5442  C  CA    . GLU A  1  736  ? -27.653 89.629  110.646 1.00 25.47 ? 734  GLU A CA    1 
ATOM   5443  C  C     . GLU A  1  736  ? -28.569 88.497  111.093 1.00 26.17 ? 734  GLU A C     1 
ATOM   5444  O  O     . GLU A  1  736  ? -29.787 88.586  110.895 1.00 26.46 ? 734  GLU A O     1 
ATOM   5445  C  CB    . GLU A  1  736  ? -27.315 89.450  109.169 1.00 26.92 ? 734  GLU A CB    1 
ATOM   5446  C  CG    . GLU A  1  736  ? -26.565 90.614  108.568 1.00 29.11 ? 734  GLU A CG    1 
ATOM   5447  C  CD    . GLU A  1  736  ? -25.056 90.445  108.647 1.00 36.59 ? 734  GLU A CD    1 
ATOM   5448  O  OE1   . GLU A  1  736  ? -24.576 89.626  109.471 1.00 28.66 ? 734  GLU A OE1   1 
ATOM   5449  O  OE2   . GLU A  1  736  ? -24.354 91.121  107.864 1.00 37.82 ? 734  GLU A OE2   1 
ATOM   5450  N  N     . THR A  1  737  ? -28.028 87.427  111.677 1.00 25.45 ? 735  THR A N     1 
ATOM   5451  C  CA    . THR A  1  737  ? -28.795 86.200  111.916 1.00 23.80 ? 735  THR A CA    1 
ATOM   5452  C  C     . THR A  1  737  ? -28.606 85.659  113.334 1.00 25.00 ? 735  THR A C     1 
ATOM   5453  O  O     . THR A  1  737  ? -28.208 84.506  113.520 1.00 24.14 ? 735  THR A O     1 
ATOM   5454  C  CB    . THR A  1  737  ? -28.410 85.138  110.887 1.00 24.67 ? 735  THR A CB    1 
ATOM   5455  O  OG1   . THR A  1  737  ? -26.991 84.932  110.925 1.00 24.99 ? 735  THR A OG1   1 
ATOM   5456  C  CG2   . THR A  1  737  ? -28.811 85.568  109.480 1.00 23.96 ? 735  THR A CG2   1 
ATOM   5457  N  N     . PRO A  1  738  ? -28.943 86.447  114.366 1.00 22.65 ? 736  PRO A N     1 
ATOM   5458  C  CA    . PRO A  1  738  ? -28.754 85.964  115.744 1.00 24.35 ? 736  PRO A CA    1 
ATOM   5459  C  C     . PRO A  1  738  ? -29.838 85.025  116.236 1.00 25.24 ? 736  PRO A C     1 
ATOM   5460  O  O     . PRO A  1  738  ? -29.587 84.281  117.194 1.00 24.38 ? 736  PRO A O     1 
ATOM   5461  C  CB    . PRO A  1  738  ? -28.768 87.257  116.564 1.00 25.37 ? 736  PRO A CB    1 
ATOM   5462  C  CG    . PRO A  1  738  ? -29.769 88.101  115.826 1.00 24.74 ? 736  PRO A CG    1 
ATOM   5463  C  CD    . PRO A  1  738  ? -29.499 87.815  114.351 1.00 21.50 ? 736  PRO A CD    1 
ATOM   5464  N  N     . LEU A  1  739  ? -31.038 85.059  115.649 1.00 22.03 ? 737  LEU A N     1 
ATOM   5465  C  CA    . LEU A  1  739  ? -32.156 84.312  116.225 1.00 25.37 ? 737  LEU A CA    1 
ATOM   5466  C  C     . LEU A  1  739  ? -31.956 82.812  116.075 1.00 22.07 ? 737  LEU A C     1 
ATOM   5467  O  O     . LEU A  1  739  ? -32.160 82.057  117.030 1.00 24.15 ? 737  LEU A O     1 
ATOM   5468  C  CB    . LEU A  1  739  ? -33.470 84.735  115.578 1.00 27.45 ? 737  LEU A CB    1 
ATOM   5469  C  CG    . LEU A  1  739  ? -33.817 86.209  115.697 1.00 25.36 ? 737  LEU A CG    1 
ATOM   5470  C  CD1   . LEU A  1  739  ? -35.108 86.470  114.939 1.00 24.03 ? 737  LEU A CD1   1 
ATOM   5471  C  CD2   . LEU A  1  739  ? -33.948 86.629  117.163 1.00 25.70 ? 737  LEU A CD2   1 
ATOM   5472  N  N     . ILE A  1  740  ? -31.585 82.356  114.877 1.00 22.80 ? 738  ILE A N     1 
ATOM   5473  C  CA    . ILE A  1  740  ? -31.376 80.924  114.699 1.00 22.86 ? 738  ILE A CA    1 
ATOM   5474  C  C     . ILE A  1  740  ? -30.165 80.479  115.506 1.00 23.33 ? 738  ILE A C     1 
ATOM   5475  O  O     . ILE A  1  740  ? -30.127 79.352  116.014 1.00 23.93 ? 738  ILE A O     1 
ATOM   5476  C  CB    . ILE A  1  740  ? -31.258 80.566  113.203 1.00 25.81 ? 738  ILE A CB    1 
ATOM   5477  C  CG1   . ILE A  1  740  ? -31.208 79.045  113.008 1.00 23.59 ? 738  ILE A CG1   1 
ATOM   5478  C  CG2   . ILE A  1  740  ? -30.021 81.202  112.583 1.00 24.88 ? 738  ILE A CG2   1 
ATOM   5479  C  CD1   . ILE A  1  740  ? -32.448 78.319  113.518 1.00 25.27 ? 738  ILE A CD1   1 
ATOM   5480  N  N     . ALA A  1  741  ? -29.194 81.373  115.700 1.00 24.18 ? 739  ALA A N     1 
ATOM   5481  C  CA    . ALA A  1  741  ? -28.062 81.049  116.559 1.00 27.61 ? 739  ALA A CA    1 
ATOM   5482  C  C     . ALA A  1  741  ? -28.508 80.855  117.998 1.00 21.65 ? 739  ALA A C     1 
ATOM   5483  O  O     . ALA A  1  741  ? -28.080 79.901  118.658 1.00 25.51 ? 739  ALA A O     1 
ATOM   5484  C  CB    . ALA A  1  741  ? -27.002 82.145  116.482 1.00 26.85 ? 739  ALA A CB    1 
ATOM   5485  N  N     . ALA A  1  742  ? -29.365 81.751  118.502 1.00 22.07 ? 740  ALA A N     1 
ATOM   5486  C  CA    . ALA A  1  742  ? -29.859 81.608  119.865 1.00 23.36 ? 740  ALA A CA    1 
ATOM   5487  C  C     . ALA A  1  742  ? -30.634 80.312  120.024 1.00 24.31 ? 740  ALA A C     1 
ATOM   5488  O  O     . ALA A  1  742  ? -30.555 79.652  121.064 1.00 26.16 ? 740  ALA A O     1 
ATOM   5489  C  CB    . ALA A  1  742  ? -30.735 82.807  120.242 1.00 23.78 ? 740  ALA A CB    1 
ATOM   5490  N  N     . GLU A  1  743  ? -31.382 79.925  118.993 1.00 22.89 ? 741  GLU A N     1 
ATOM   5491  C  CA    . GLU A  1  743  ? -32.138 78.685  119.070 1.00 25.60 ? 741  GLU A CA    1 
ATOM   5492  C  C     . GLU A  1  743  ? -31.208 77.481  119.040 1.00 24.44 ? 741  GLU A C     1 
ATOM   5493  O  O     . GLU A  1  743  ? -31.445 76.493  119.748 1.00 23.54 ? 741  GLU A O     1 
ATOM   5494  C  CB    . GLU A  1  743  ? -33.159 78.638  117.934 1.00 24.55 ? 741  GLU A CB    1 
ATOM   5495  C  CG    . GLU A  1  743  ? -33.935 77.339  117.804 1.00 26.93 ? 741  GLU A CG    1 
ATOM   5496  C  CD    . GLU A  1  743  ? -34.875 77.054  118.968 1.00 25.98 ? 741  GLU A CD    1 
ATOM   5497  O  OE1   . GLU A  1  743  ? -35.037 77.903  119.875 1.00 28.54 ? 741  GLU A OE1   1 
ATOM   5498  O  OE2   . GLU A  1  743  ? -35.455 75.950  118.971 1.00 34.03 ? 741  GLU A OE2   1 
ATOM   5499  N  N     . GLY A  1  744  ? -30.124 77.566  118.260 1.00 22.81 ? 742  GLY A N     1 
ATOM   5500  C  CA    . GLY A  1  744  ? -29.125 76.511  118.276 1.00 22.23 ? 742  GLY A CA    1 
ATOM   5501  C  C     . GLY A  1  744  ? -28.472 76.358  119.638 1.00 24.17 ? 742  GLY A C     1 
ATOM   5502  O  O     . GLY A  1  744  ? -28.276 75.241  120.119 1.00 24.04 ? 742  GLY A O     1 
ATOM   5503  N  N     . VAL A  1  745  ? -28.136 77.479  120.281 1.00 23.80 ? 743  VAL A N     1 
ATOM   5504  C  CA    . VAL A  1  745  ? -27.553 77.424  121.621 1.00 26.16 ? 743  VAL A CA    1 
ATOM   5505  C  C     . VAL A  1  745  ? -28.559 76.871  122.623 1.00 23.62 ? 743  VAL A C     1 
ATOM   5506  O  O     . VAL A  1  745  ? -28.213 76.061  123.493 1.00 27.28 ? 743  VAL A O     1 
ATOM   5507  C  CB    . VAL A  1  745  ? -27.033 78.815  122.028 1.00 26.10 ? 743  VAL A CB    1 
ATOM   5508  C  CG1   . VAL A  1  745  ? -26.764 78.883  123.540 1.00 27.55 ? 743  VAL A CG1   1 
ATOM   5509  C  CG2   . VAL A  1  745  ? -25.763 79.131  121.225 1.00 25.74 ? 743  VAL A CG2   1 
ATOM   5510  N  N     . ARG A  1  746  ? -29.822 77.288  122.514 1.00 26.24 ? 744  ARG A N     1 
ATOM   5511  C  CA    . ARG A  1  746  ? -30.853 76.724  123.381 1.00 25.87 ? 744  ARG A CA    1 
ATOM   5512  C  C     . ARG A  1  746  ? -30.917 75.208  123.243 1.00 24.56 ? 744  ARG A C     1 
ATOM   5513  O  O     . ARG A  1  746  ? -31.008 74.488  124.243 1.00 27.59 ? 744  ARG A O     1 
ATOM   5514  C  CB    . ARG A  1  746  ? -32.210 77.341  123.047 1.00 28.68 ? 744  ARG A CB    1 
ATOM   5515  C  CG    . ARG A  1  746  ? -33.300 76.934  124.017 1.00 26.96 ? 744  ARG A CG    1 
ATOM   5516  C  CD    . ARG A  1  746  ? -34.699 77.226  123.488 1.00 30.48 ? 744  ARG A CD    1 
ATOM   5517  N  NE    . ARG A  1  746  ? -35.033 76.362  122.362 1.00 31.26 ? 744  ARG A NE    1 
ATOM   5518  C  CZ    . ARG A  1  746  ? -35.309 75.068  122.464 1.00 33.33 ? 744  ARG A CZ    1 
ATOM   5519  N  NH1   . ARG A  1  746  ? -35.291 74.445  123.634 1.00 33.33 ? 744  ARG A NH1   1 
ATOM   5520  N  NH2   . ARG A  1  746  ? -35.599 74.378  121.363 1.00 30.41 ? 744  ARG A NH2   1 
ATOM   5521  N  N     . ILE A  1  747  ? -30.863 74.709  122.006 1.00 24.13 ? 745  ILE A N     1 
ATOM   5522  C  CA    . ILE A  1  747  ? -30.915 73.270  121.764 1.00 24.80 ? 745  ILE A CA    1 
ATOM   5523  C  C     . ILE A  1  747  ? -29.682 72.576  122.331 1.00 24.63 ? 745  ILE A C     1 
ATOM   5524  O  O     . ILE A  1  747  ? -29.788 71.529  122.980 1.00 23.16 ? 745  ILE A O     1 
ATOM   5525  C  CB    . ILE A  1  747  ? -31.085 72.996  120.260 1.00 24.49 ? 745  ILE A CB    1 
ATOM   5526  C  CG1   . ILE A  1  747  ? -32.507 73.385  119.841 1.00 24.26 ? 745  ILE A CG1   1 
ATOM   5527  C  CG2   . ILE A  1  747  ? -30.740 71.532  119.933 1.00 24.95 ? 745  ILE A CG2   1 
ATOM   5528  C  CD1   . ILE A  1  747  ? -32.690 73.488  118.354 1.00 25.78 ? 745  ILE A CD1   1 
ATOM   5529  N  N     . LEU A  1  748  ? -28.489 73.137  122.091 1.00 24.62 ? 746  LEU A N     1 
ATOM   5530  C  CA    . LEU A  1  748  ? -27.272 72.528  122.627 1.00 22.85 ? 746  LEU A CA    1 
ATOM   5531  C  C     . LEU A  1  748  ? -27.294 72.498  124.146 1.00 24.99 ? 746  LEU A C     1 
ATOM   5532  O  O     . LEU A  1  748  ? -26.863 71.519  124.766 1.00 26.31 ? 746  LEU A O     1 
ATOM   5533  C  CB    . LEU A  1  748  ? -26.043 73.280  122.127 1.00 23.23 ? 746  LEU A CB    1 
ATOM   5534  C  CG    . LEU A  1  748  ? -25.554 72.849  120.754 1.00 26.89 ? 746  LEU A CG    1 
ATOM   5535  C  CD1   . LEU A  1  748  ? -24.672 73.928  120.136 1.00 27.94 ? 746  LEU A CD1   1 
ATOM   5536  C  CD2   . LEU A  1  748  ? -24.786 71.549  120.881 1.00 26.92 ? 746  LEU A CD2   1 
ATOM   5537  N  N     . ARG A  1  749  ? -27.800 73.562  124.766 1.00 24.92 ? 747  ARG A N     1 
ATOM   5538  C  CA    . ARG A  1  749  ? -27.919 73.564  126.218 1.00 24.52 ? 747  ARG A CA    1 
ATOM   5539  C  C     . ARG A  1  749  ? -28.965 72.557  126.684 1.00 25.70 ? 747  ARG A C     1 
ATOM   5540  O  O     . ARG A  1  749  ? -28.766 71.871  127.695 1.00 28.50 ? 747  ARG A O     1 
ATOM   5541  C  CB    . ARG A  1  749  ? -28.247 74.975  126.703 1.00 26.73 ? 747  ARG A CB    1 
ATOM   5542  C  CG    . ARG A  1  749  ? -27.025 75.899  126.753 1.00 28.49 ? 747  ARG A CG    1 
ATOM   5543  C  CD    . ARG A  1  749  ? -27.398 77.268  127.282 1.00 35.78 ? 747  ARG A CD    1 
ATOM   5544  N  NE    . ARG A  1  749  ? -26.258 78.167  127.433 1.00 35.28 ? 747  ARG A NE    1 
ATOM   5545  C  CZ    . ARG A  1  749  ? -26.313 79.301  128.120 1.00 33.85 ? 747  ARG A CZ    1 
ATOM   5546  N  NH1   . ARG A  1  749  ? -27.428 79.691  128.716 1.00 33.76 ? 747  ARG A NH1   1 
ATOM   5547  N  NH2   . ARG A  1  749  ? -25.223 80.057  128.224 1.00 32.87 ? 747  ARG A NH2   1 
ATOM   5548  N  N     . GLU A  1  750  ? -30.082 72.443  125.960 1.00 24.95 ? 748  GLU A N     1 
ATOM   5549  C  CA    . GLU A  1  750  ? -31.067 71.423  126.311 1.00 27.30 ? 748  GLU A CA    1 
ATOM   5550  C  C     . GLU A  1  750  ? -30.455 70.029  126.224 1.00 24.71 ? 748  GLU A C     1 
ATOM   5551  O  O     . GLU A  1  750  ? -30.737 69.157  127.058 1.00 27.02 ? 748  GLU A O     1 
ATOM   5552  C  CB    . GLU A  1  750  ? -32.292 71.521  125.401 1.00 26.09 ? 748  GLU A CB    1 
ATOM   5553  C  CG    . GLU A  1  750  ? -33.384 70.557  125.817 1.00 32.66 ? 748  GLU A CG    1 
ATOM   5554  C  CD    . GLU A  1  750  ? -34.546 70.512  124.852 1.00 31.22 ? 748  GLU A CD    1 
ATOM   5555  O  OE1   . GLU A  1  750  ? -34.739 71.477  124.085 1.00 41.33 ? 748  GLU A OE1   1 
ATOM   5556  O  OE2   . GLU A  1  750  ? -35.265 69.492  124.859 1.00 35.10 ? 748  GLU A OE2   1 
ATOM   5557  N  N     . ALA A  1  751  ? -29.580 69.818  125.243 1.00 24.47 ? 749  ALA A N     1 
ATOM   5558  C  CA    . ALA A  1  751  ? -28.930 68.533  125.044 1.00 25.96 ? 749  ALA A CA    1 
ATOM   5559  C  C     . ALA A  1  751  ? -27.903 68.229  126.120 1.00 26.19 ? 749  ALA A C     1 
ATOM   5560  O  O     . ALA A  1  751  ? -27.373 67.114  126.149 1.00 28.28 ? 749  ALA A O     1 
ATOM   5561  C  CB    . ALA A  1  751  ? -28.268 68.502  123.664 1.00 25.27 ? 749  ALA A CB    1 
ATOM   5562  N  N     . GLY A  1  752  ? -27.605 69.187  126.995 1.00 25.96 ? 750  GLY A N     1 
ATOM   5563  C  CA    . GLY A  1  752  ? -26.711 68.948  128.112 1.00 29.18 ? 750  GLY A CA    1 
ATOM   5564  C  C     . GLY A  1  752  ? -25.446 69.779  128.124 1.00 31.67 ? 750  GLY A C     1 
ATOM   5565  O  O     . GLY A  1  752  ? -24.654 69.639  129.067 1.00 30.55 ? 750  GLY A O     1 
ATOM   5566  N  N     . ILE A  1  753  ? -25.189 70.629  127.135 1.00 27.59 ? 751  ILE A N     1 
ATOM   5567  C  CA    . ILE A  1  753  ? -24.021 71.500  127.205 1.00 25.93 ? 751  ILE A CA    1 
ATOM   5568  C  C     . ILE A  1  753  ? -24.256 72.494  128.332 1.00 26.47 ? 751  ILE A C     1 
ATOM   5569  O  O     . ILE A  1  753  ? -25.257 73.220  128.307 1.00 28.78 ? 751  ILE A O     1 
ATOM   5570  C  CB    . ILE A  1  753  ? -23.765 72.235  125.883 1.00 24.94 ? 751  ILE A CB    1 
ATOM   5571  C  CG1   . ILE A  1  753  ? -23.609 71.241  124.730 1.00 22.57 ? 751  ILE A CG1   1 
ATOM   5572  C  CG2   . ILE A  1  753  ? -22.522 73.118  126.018 1.00 28.42 ? 751  ILE A CG2   1 
ATOM   5573  C  CD1   . ILE A  1  753  ? -22.317 70.422  124.773 1.00 23.36 ? 751  ILE A CD1   1 
ATOM   5574  N  N     . PRO A  1  754  ? -23.382 72.555  129.333 1.00 28.50 ? 752  PRO A N     1 
ATOM   5575  C  CA    . PRO A  1  754  ? -23.593 73.504  130.432 1.00 32.62 ? 752  PRO A CA    1 
ATOM   5576  C  C     . PRO A  1  754  ? -23.528 74.943  129.945 1.00 24.80 ? 752  PRO A C     1 
ATOM   5577  O  O     . PRO A  1  754  ? -22.812 75.268  128.991 1.00 26.53 ? 752  PRO A O     1 
ATOM   5578  C  CB    . PRO A  1  754  ? -22.440 73.199  131.396 1.00 33.41 ? 752  PRO A CB    1 
ATOM   5579  C  CG    . PRO A  1  754  ? -21.939 71.846  131.012 1.00 32.39 ? 752  PRO A CG    1 
ATOM   5580  C  CD    . PRO A  1  754  ? -22.186 71.725  129.534 1.00 27.44 ? 752  PRO A CD    1 
ATOM   5581  N  N     . ALA A  1  755  ? -24.283 75.810  130.629 1.00 30.33 ? 753  ALA A N     1 
ATOM   5582  C  CA    . ALA A  1  755  ? -24.282 77.232  130.293 1.00 30.65 ? 753  ALA A CA    1 
ATOM   5583  C  C     . ALA A  1  755  ? -22.881 77.824  130.350 1.00 30.30 ? 753  ALA A C     1 
ATOM   5584  O  O     . ALA A  1  755  ? -22.554 78.734  129.581 1.00 30.26 ? 753  ALA A O     1 
ATOM   5585  C  CB    . ALA A  1  755  ? -25.211 77.997  131.242 1.00 28.72 ? 753  ALA A CB    1 
ATOM   5586  N  N     . SER A  1  756  ? -22.040 77.328  131.252 1.00 26.76 ? 754  SER A N     1 
ATOM   5587  C  CA    . SER A  1  756  ? -20.699 77.871  131.335 1.00 27.63 ? 754  SER A CA    1 
ATOM   5588  C  C     . SER A  1  756  ? -19.833 77.434  130.162 1.00 28.11 ? 754  SER A C     1 
ATOM   5589  O  O     . SER A  1  756  ? -18.829 78.093  129.872 1.00 29.36 ? 754  SER A O     1 
ATOM   5590  C  CB    . SER A  1  756  ? -20.060 77.444  132.644 1.00 30.66 ? 754  SER A CB    1 
ATOM   5591  O  OG    . SER A  1  756  ? -19.938 76.037  132.691 1.00 31.28 ? 754  SER A OG    1 
ATOM   5592  N  N     . ALA A  1  757  ? -20.193 76.338  129.493 1.00 27.12 ? 755  ALA A N     1 
ATOM   5593  C  CA    . ALA A  1  757  ? -19.417 75.842  128.363 1.00 24.15 ? 755  ALA A CA    1 
ATOM   5594  C  C     . ALA A  1  757  ? -19.853 76.432  127.034 1.00 24.65 ? 755  ALA A C     1 
ATOM   5595  O  O     . ALA A  1  757  ? -19.098 76.347  126.064 1.00 24.25 ? 755  ALA A O     1 
ATOM   5596  C  CB    . ALA A  1  757  ? -19.509 74.312  128.270 1.00 25.66 ? 755  ALA A CB    1 
ATOM   5597  N  N     . LEU A  1  758  ? -21.037 77.035  126.966 1.00 22.87 ? 756  LEU A N     1 
ATOM   5598  C  CA    . LEU A  1  758  ? -21.545 77.577  125.707 1.00 21.57 ? 756  LEU A CA    1 
ATOM   5599  C  C     . LEU A  1  758  ? -22.267 78.881  126.013 1.00 25.60 ? 756  LEU A C     1 
ATOM   5600  O  O     . LEU A  1  758  ? -23.394 78.869  126.510 1.00 28.27 ? 756  LEU A O     1 
ATOM   5601  C  CB    . LEU A  1  758  ? -22.461 76.582  125.015 1.00 25.57 ? 756  LEU A CB    1 
ATOM   5602  C  CG    . LEU A  1  758  ? -23.088 77.078  123.719 1.00 23.44 ? 756  LEU A CG    1 
ATOM   5603  C  CD1   . LEU A  1  758  ? -22.013 77.613  122.757 1.00 22.37 ? 756  LEU A CD1   1 
ATOM   5604  C  CD2   . LEU A  1  758  ? -23.845 75.944  123.076 1.00 26.26 ? 756  LEU A CD2   1 
ATOM   5605  N  N     . GLN A  1  759  ? -21.610 79.994  125.719 1.00 23.60 ? 757  GLN A N     1 
ATOM   5606  C  CA    . GLN A  1  759  ? -22.173 81.317  125.914 1.00 25.50 ? 757  GLN A CA    1 
ATOM   5607  C  C     . GLN A  1  759  ? -22.419 81.965  124.560 1.00 26.98 ? 757  GLN A C     1 
ATOM   5608  O  O     . GLN A  1  759  ? -21.575 81.887  123.658 1.00 29.26 ? 757  GLN A O     1 
ATOM   5609  C  CB    . GLN A  1  759  ? -21.237 82.186  126.764 1.00 27.89 ? 757  GLN A CB    1 
ATOM   5610  C  CG    . GLN A  1  759  ? -21.042 81.685  128.182 1.00 27.56 ? 757  GLN A CG    1 
ATOM   5611  C  CD    . GLN A  1  759  ? -19.998 82.495  128.932 1.00 27.31 ? 757  GLN A CD    1 
ATOM   5612  O  OE1   . GLN A  1  759  ? -20.320 83.490  129.581 1.00 27.74 ? 757  GLN A OE1   1 
ATOM   5613  N  NE2   . GLN A  1  759  ? -18.740 82.085  128.826 1.00 27.20 ? 757  GLN A NE2   1 
ATOM   5614  N  N     . LEU A  1  760  ? -23.583 82.579  124.410 1.00 27.68 ? 758  LEU A N     1 
ATOM   5615  C  CA    . LEU A  1  760  ? -23.966 83.234  123.169 1.00 25.99 ? 758  LEU A CA    1 
ATOM   5616  C  C     . LEU A  1  760  ? -23.799 84.736  123.330 1.00 26.11 ? 758  LEU A C     1 
ATOM   5617  O  O     . LEU A  1  760  ? -24.325 85.317  124.277 1.00 26.86 ? 758  LEU A O     1 
ATOM   5618  C  CB    . LEU A  1  760  ? -25.409 82.898  122.804 1.00 28.10 ? 758  LEU A CB    1 
ATOM   5619  C  CG    . LEU A  1  760  ? -25.943 83.585  121.553 1.00 26.48 ? 758  LEU A CG    1 
ATOM   5620  C  CD1   . LEU A  1  760  ? -25.495 82.852  120.288 1.00 25.81 ? 758  LEU A CD1   1 
ATOM   5621  C  CD2   . LEU A  1  760  ? -27.448 83.675  121.632 1.00 26.37 ? 758  LEU A CD2   1 
ATOM   5622  N  N     . LEU A  1  761  ? -23.057 85.360  122.417 1.00 26.50 ? 759  LEU A N     1 
ATOM   5623  C  CA    . LEU A  1  761  ? -22.777 86.796  122.482 1.00 27.82 ? 759  LEU A CA    1 
ATOM   5624  C  C     . LEU A  1  761  ? -23.187 87.439  121.164 1.00 25.46 ? 759  LEU A C     1 
ATOM   5625  O  O     . LEU A  1  761  ? -22.352 87.639  120.274 1.00 27.80 ? 759  LEU A O     1 
ATOM   5626  C  CB    . LEU A  1  761  ? -21.300 87.073  122.766 1.00 27.52 ? 759  LEU A CB    1 
ATOM   5627  C  CG    . LEU A  1  761  ? -20.614 86.561  124.038 1.00 28.86 ? 759  LEU A CG    1 
ATOM   5628  C  CD1   . LEU A  1  761  ? -21.524 86.667  125.265 1.00 25.72 ? 759  LEU A CD1   1 
ATOM   5629  C  CD2   . LEU A  1  761  ? -20.067 85.144  123.857 1.00 33.25 ? 759  LEU A CD2   1 
ATOM   5630  N  N     . PRO A  1  762  ? -24.460 87.795  121.008 1.00 26.43 ? 760  PRO A N     1 
ATOM   5631  C  CA    . PRO A  1  762  ? -24.882 88.461  119.771 1.00 27.98 ? 760  PRO A CA    1 
ATOM   5632  C  C     . PRO A  1  762  ? -24.275 89.851  119.658 1.00 32.15 ? 760  PRO A C     1 
ATOM   5633  O  O     . PRO A  1  762  ? -23.965 90.507  120.656 1.00 28.66 ? 760  PRO A O     1 
ATOM   5634  C  CB    . PRO A  1  762  ? -26.410 88.536  119.900 1.00 25.17 ? 760  PRO A CB    1 
ATOM   5635  C  CG    . PRO A  1  762  ? -26.772 87.580  120.998 1.00 26.26 ? 760  PRO A CG    1 
ATOM   5636  C  CD    . PRO A  1  762  ? -25.588 87.557  121.923 1.00 25.74 ? 760  PRO A CD    1 
ATOM   5637  N  N     . GLY A  1  763  ? -24.112 90.298  118.423 1.00 26.18 ? 761  GLY A N     1 
ATOM   5638  C  CA    . GLY A  1  763  ? -23.615 91.629  118.161 1.00 32.78 ? 761  GLY A CA    1 
ATOM   5639  C  C     . GLY A  1  763  ? -22.804 91.646  116.882 1.00 36.62 ? 761  GLY A C     1 
ATOM   5640  O  O     . GLY A  1  763  ? -22.720 90.651  116.163 1.00 32.82 ? 761  GLY A O     1 
ATOM   5641  N  N     . ASP A  1  764  ? -22.187 92.797  116.631 1.00 38.47 ? 762  ASP A N     1 
ATOM   5642  C  CA    . ASP A  1  764  ? -21.467 93.046  115.389 1.00 44.97 ? 762  ASP A CA    1 
ATOM   5643  C  C     . ASP A  1  764  ? -20.003 92.618  115.539 1.00 43.25 ? 762  ASP A C     1 
ATOM   5644  O  O     . ASP A  1  764  ? -19.652 91.849  116.438 1.00 39.82 ? 762  ASP A O     1 
ATOM   5645  C  CB    . ASP A  1  764  ? -21.616 94.520  114.991 1.00 47.63 ? 762  ASP A CB    1 
ATOM   5646  C  CG    . ASP A  1  764  ? -21.145 95.480  116.079 1.00 49.46 ? 762  ASP A CG    1 
ATOM   5647  O  OD1   . ASP A  1  764  ? -20.332 95.081  116.940 1.00 53.14 ? 762  ASP A OD1   1 
ATOM   5648  O  OD2   . ASP A  1  764  ? -21.597 96.645  116.080 1.00 56.17 ? 762  ASP A OD2   1 
ATOM   5649  N  N     . GLY A  1  765  ? -19.133 93.113  114.656 1.00 43.96 ? 763  GLY A N     1 
ATOM   5650  C  CA    . GLY A  1  765  ? -17.726 92.757  114.711 1.00 39.95 ? 763  GLY A CA    1 
ATOM   5651  C  C     . GLY A  1  765  ? -17.005 93.269  115.941 1.00 40.11 ? 763  GLY A C     1 
ATOM   5652  O  O     . GLY A  1  765  ? -15.943 92.738  116.285 1.00 42.23 ? 763  GLY A O     1 
ATOM   5653  N  N     . ARG A  1  766  ? -17.554 94.288  116.607 1.00 38.54 ? 764  ARG A N     1 
ATOM   5654  C  CA    . ARG A  1  766  ? -16.950 94.778  117.842 1.00 41.90 ? 764  ARG A CA    1 
ATOM   5655  C  C     . ARG A  1  766  ? -17.004 93.717  118.935 1.00 43.85 ? 764  ARG A C     1 
ATOM   5656  O  O     . ARG A  1  766  ? -16.062 93.573  119.722 1.00 36.38 ? 764  ARG A O     1 
ATOM   5657  C  CB    . ARG A  1  766  ? -17.647 96.061  118.301 1.00 37.43 ? 764  ARG A CB    1 
ATOM   5658  N  N     . VAL A  1  767  ? -18.108 92.972  119.009 1.00 40.39 ? 765  VAL A N     1 
ATOM   5659  C  CA    . VAL A  1  767  ? -18.182 91.854  119.945 1.00 35.95 ? 765  VAL A CA    1 
ATOM   5660  C  C     . VAL A  1  767  ? -17.183 90.780  119.546 1.00 33.49 ? 765  VAL A C     1 
ATOM   5661  O  O     . VAL A  1  767  ? -16.471 90.219  120.387 1.00 34.91 ? 765  VAL A O     1 
ATOM   5662  C  CB    . VAL A  1  767  ? -19.614 91.298  120.005 1.00 29.19 ? 765  VAL A CB    1 
ATOM   5663  C  CG1   . VAL A  1  767  ? -19.696 90.140  120.991 1.00 30.61 ? 765  VAL A CG1   1 
ATOM   5664  C  CG2   . VAL A  1  767  ? -20.586 92.397  120.381 1.00 39.48 ? 765  VAL A CG2   1 
ATOM   5665  N  N     . GLY A  1  768  ? -17.120 90.477  118.248 1.00 34.34 ? 766  GLY A N     1 
ATOM   5666  C  CA    . GLY A  1  768  ? -16.155 89.499  117.776 1.00 29.18 ? 766  GLY A CA    1 
ATOM   5667  C  C     . GLY A  1  768  ? -14.732 89.887  118.123 1.00 28.68 ? 766  GLY A C     1 
ATOM   5668  O  O     . GLY A  1  768  ? -13.962 89.072  118.632 1.00 27.97 ? 766  GLY A O     1 
ATOM   5669  N  N     . ALA A  1  769  ? -14.379 91.150  117.882 1.00 31.79 ? 767  ALA A N     1 
ATOM   5670  C  CA    . ALA A  1  769  ? -13.011 91.597  118.121 1.00 36.23 ? 767  ALA A CA    1 
ATOM   5671  C  C     . ALA A  1  769  ? -12.678 91.588  119.606 1.00 33.41 ? 767  ALA A C     1 
ATOM   5672  O  O     . ALA A  1  769  ? -11.567 91.214  119.995 1.00 34.54 ? 767  ALA A O     1 
ATOM   5673  C  CB    . ALA A  1  769  ? -12.801 92.992  117.536 1.00 32.04 ? 767  ALA A CB    1 
ATOM   5674  N  N     . ALA A  1  770  ? -13.620 92.010  120.450 1.00 34.56 ? 768  ALA A N     1 
ATOM   5675  C  CA    . ALA A  1  770  ? -13.377 91.977  121.887 1.00 30.52 ? 768  ALA A CA    1 
ATOM   5676  C  C     . ALA A  1  770  ? -13.109 90.555  122.352 1.00 26.19 ? 768  ALA A C     1 
ATOM   5677  O  O     . ALA A  1  770  ? -12.250 90.324  123.212 1.00 29.67 ? 768  ALA A O     1 
ATOM   5678  C  CB    . ALA A  1  770  ? -14.567 92.575  122.636 1.00 33.82 ? 768  ALA A CB    1 
ATOM   5679  N  N     . LEU A  1  771  ? -13.832 89.587  121.782 1.00 27.50 ? 769  LEU A N     1 
ATOM   5680  C  CA    . LEU A  1  771  ? -13.611 88.187  122.125 1.00 26.09 ? 769  LEU A CA    1 
ATOM   5681  C  C     . LEU A  1  771  ? -12.243 87.718  121.656 1.00 25.27 ? 769  LEU A C     1 
ATOM   5682  O  O     . LEU A  1  771  ? -11.505 87.064  122.405 1.00 28.07 ? 769  LEU A O     1 
ATOM   5683  C  CB    . LEU A  1  771  ? -14.712 87.321  121.511 1.00 24.53 ? 769  LEU A CB    1 
ATOM   5684  C  CG    . LEU A  1  771  ? -16.129 87.572  122.033 1.00 25.43 ? 769  LEU A CG    1 
ATOM   5685  C  CD1   . LEU A  1  771  ? -17.136 86.794  121.181 1.00 27.37 ? 769  LEU A CD1   1 
ATOM   5686  C  CD2   . LEU A  1  771  ? -16.246 87.182  123.500 1.00 30.29 ? 769  LEU A CD2   1 
ATOM   5687  N  N     . VAL A  1  772  ? -11.888 88.048  120.411 1.00 27.57 ? 770  VAL A N     1 
ATOM   5688  C  CA    . VAL A  1  772  ? -10.612 87.614  119.849 1.00 25.70 ? 770  VAL A CA    1 
ATOM   5689  C  C     . VAL A  1  772  ? -9.457  88.169  120.669 1.00 28.40 ? 770  VAL A C     1 
ATOM   5690  O  O     . VAL A  1  772  ? -8.447  87.493  120.881 1.00 28.65 ? 770  VAL A O     1 
ATOM   5691  C  CB    . VAL A  1  772  ? -10.514 88.031  118.365 1.00 25.35 ? 770  VAL A CB    1 
ATOM   5692  C  CG1   . VAL A  1  772  ? -9.092  87.876  117.838 1.00 29.43 ? 770  VAL A CG1   1 
ATOM   5693  C  CG2   . VAL A  1  772  ? -11.469 87.189  117.514 1.00 27.94 ? 770  VAL A CG2   1 
ATOM   5694  N  N     . ALA A  1  773  ? -9.590  89.400  121.153 1.00 29.54 ? 771  ALA A N     1 
ATOM   5695  C  CA    . ALA A  1  773  ? -8.496  90.054  121.860 1.00 27.71 ? 771  ALA A CA    1 
ATOM   5696  C  C     . ALA A  1  773  ? -8.393  89.655  123.325 1.00 34.34 ? 771  ALA A C     1 
ATOM   5697  O  O     . ALA A  1  773  ? -7.397  90.002  123.973 1.00 36.12 ? 771  ALA A O     1 
ATOM   5698  C  CB    . ALA A  1  773  ? -8.652  91.570  121.769 1.00 29.77 ? 771  ALA A CB    1 
ATOM   5699  N  N     . ALA A  1  774  ? -9.385  88.956  123.869 1.00 32.25 ? 772  ALA A N     1 
ATOM   5700  C  CA    . ALA A  1  774  ? -9.382  88.663  125.298 1.00 31.03 ? 772  ALA A CA    1 
ATOM   5701  C  C     . ALA A  1  774  ? -8.253  87.697  125.638 1.00 31.81 ? 772  ALA A C     1 
ATOM   5702  O  O     . ALA A  1  774  ? -8.018  86.719  124.929 1.00 31.46 ? 772  ALA A O     1 
ATOM   5703  C  CB    . ALA A  1  774  ? -10.735 88.098  125.731 1.00 31.27 ? 772  ALA A CB    1 
ATOM   5704  N  N     . ALA A  1  775  ? -7.551  87.974  126.743 1.00 32.90 ? 773  ALA A N     1 
ATOM   5705  C  CA    . ALA A  1  775  ? -6.315  87.250  127.028 1.00 36.79 ? 773  ALA A CA    1 
ATOM   5706  C  C     . ALA A  1  775  ? -6.545  85.753  127.204 1.00 30.21 ? 773  ALA A C     1 
ATOM   5707  O  O     . ALA A  1  775  ? -5.656  84.953  126.893 1.00 33.64 ? 773  ALA A O     1 
ATOM   5708  C  CB    . ALA A  1  775  ? -5.639  87.837  128.269 1.00 39.65 ? 773  ALA A CB    1 
ATOM   5709  N  N     . GLU A  1  776  ? -7.721  85.348  127.677 1.00 29.69 ? 774  GLU A N     1 
ATOM   5710  C  CA    . GLU A  1  776  ? -7.975  83.931  127.917 1.00 26.72 ? 774  GLU A CA    1 
ATOM   5711  C  C     . GLU A  1  776  ? -8.459  83.187  126.678 1.00 24.11 ? 774  GLU A C     1 
ATOM   5712  O  O     . GLU A  1  776  ? -8.636  81.966  126.735 1.00 29.54 ? 774  GLU A O     1 
ATOM   5713  C  CB    . GLU A  1  776  ? -8.992  83.752  129.044 1.00 30.93 ? 774  GLU A CB    1 
ATOM   5714  C  CG    . GLU A  1  776  ? -8.564  84.395  130.351 1.00 39.46 ? 774  GLU A CG    1 
ATOM   5715  C  CD    . GLU A  1  776  ? -9.185  85.766  130.562 1.00 44.72 ? 774  GLU A CD    1 
ATOM   5716  O  OE1   . GLU A  1  776  ? -9.638  86.393  129.572 1.00 36.54 ? 774  GLU A OE1   1 
ATOM   5717  O  OE2   . GLU A  1  776  ? -9.221  86.218  131.726 1.00 51.51 ? 774  GLU A OE2   1 
ATOM   5718  N  N     . THR A  1  777  ? -8.668  83.883  125.570 1.00 26.19 ? 775  THR A N     1 
ATOM   5719  C  CA    . THR A  1  777  ? -9.083  83.222  124.341 1.00 28.31 ? 775  THR A CA    1 
ATOM   5720  C  C     . THR A  1  777  ? -7.958  82.333  123.830 1.00 24.88 ? 775  THR A C     1 
ATOM   5721  O  O     . THR A  1  777  ? -6.852  82.810  123.561 1.00 29.02 ? 775  THR A O     1 
ATOM   5722  C  CB    . THR A  1  777  ? -9.475  84.263  123.305 1.00 25.81 ? 775  THR A CB    1 
ATOM   5723  O  OG1   . THR A  1  777  ? -10.682 84.892  123.740 1.00 27.59 ? 775  THR A OG1   1 
ATOM   5724  C  CG2   . THR A  1  777  ? -9.681  83.599  121.932 1.00 24.78 ? 775  THR A CG2   1 
ATOM   5725  N  N     . ALA A  1  778  ? -8.232  81.036  123.733 1.00 23.83 ? 776  ALA A N     1 
ATOM   5726  C  CA    . ALA A  1  778  ? -7.206  80.047  123.450 1.00 21.90 ? 776  ALA A CA    1 
ATOM   5727  C  C     . ALA A  1  778  ? -7.219  79.581  122.007 1.00 24.51 ? 776  ALA A C     1 
ATOM   5728  O  O     . ALA A  1  778  ? -6.316  78.846  121.601 1.00 24.74 ? 776  ALA A O     1 
ATOM   5729  C  CB    . ALA A  1  778  ? -7.372  78.842  124.386 1.00 25.61 ? 776  ALA A CB    1 
ATOM   5730  N  N     . GLY A  1  779  ? -8.212  79.994  121.230 1.00 24.09 ? 777  GLY A N     1 
ATOM   5731  C  CA    . GLY A  1  779  ? -8.318  79.599  119.843 1.00 20.83 ? 777  GLY A CA    1 
ATOM   5732  C  C     . GLY A  1  779  ? -9.505  80.302  119.234 1.00 20.64 ? 777  GLY A C     1 
ATOM   5733  O  O     . GLY A  1  779  ? -10.439 80.688  119.946 1.00 22.14 ? 777  GLY A O     1 
ATOM   5734  N  N     . VAL A  1  780  ? -9.476  80.492  117.921 1.00 22.40 ? 778  VAL A N     1 
ATOM   5735  C  CA    . VAL A  1  780  ? -10.536 81.181  117.204 1.00 21.94 ? 778  VAL A CA    1 
ATOM   5736  C  C     . VAL A  1  780  ? -10.929 80.328  116.010 1.00 21.40 ? 778  VAL A C     1 
ATOM   5737  O  O     . VAL A  1  780  ? -10.061 79.841  115.278 1.00 20.38 ? 778  VAL A O     1 
ATOM   5738  C  CB    . VAL A  1  780  ? -10.098 82.589  116.756 1.00 21.79 ? 778  VAL A CB    1 
ATOM   5739  C  CG1   . VAL A  1  780  ? -11.202 83.274  115.990 1.00 23.36 ? 778  VAL A CG1   1 
ATOM   5740  C  CG2   . VAL A  1  780  ? -9.670  83.425  117.984 1.00 24.22 ? 778  VAL A CG2   1 
ATOM   5741  N  N     . MET A  1  781  ? -12.226 80.113  115.846 1.00 21.12 ? 779  MET A N     1 
ATOM   5742  C  CA    . MET A  1  781  ? -12.788 79.494  114.658 1.00 19.31 ? 779  MET A CA    1 
ATOM   5743  C  C     . MET A  1  781  ? -13.597 80.567  113.953 1.00 19.36 ? 779  MET A C     1 
ATOM   5744  O  O     . MET A  1  781  ? -14.597 81.057  114.493 1.00 22.24 ? 779  MET A O     1 
ATOM   5745  C  CB    . MET A  1  781  ? -13.649 78.291  115.024 1.00 20.90 ? 779  MET A CB    1 
ATOM   5746  C  CG    . MET A  1  781  ? -12.859 77.278  115.809 1.00 19.14 ? 779  MET A CG    1 
ATOM   5747  S  SD    . MET A  1  781  ? -13.890 75.992  116.495 1.00 22.04 ? 779  MET A SD    1 
ATOM   5748  C  CE    . MET A  1  781  ? -14.133 74.990  115.037 1.00 20.12 ? 779  MET A CE    1 
ATOM   5749  N  N     . PHE A  1  782  ? -13.142 80.954  112.768 1.00 20.16 ? 780  PHE A N     1 
ATOM   5750  C  CA    . PHE A  1  782  ? -13.775 82.011  112.004 1.00 21.77 ? 780  PHE A CA    1 
ATOM   5751  C  C     . PHE A  1  782  ? -14.201 81.484  110.648 1.00 23.38 ? 780  PHE A C     1 
ATOM   5752  O  O     . PHE A  1  782  ? -13.414 80.836  109.951 1.00 21.99 ? 780  PHE A O     1 
ATOM   5753  C  CB    . PHE A  1  782  ? -12.837 83.202  111.808 1.00 21.42 ? 780  PHE A CB    1 
ATOM   5754  C  CG    . PHE A  1  782  ? -13.395 84.251  110.892 1.00 22.96 ? 780  PHE A CG    1 
ATOM   5755  C  CD1   . PHE A  1  782  ? -14.288 85.187  111.367 1.00 23.25 ? 780  PHE A CD1   1 
ATOM   5756  C  CD2   . PHE A  1  782  ? -13.029 84.289  109.552 1.00 22.72 ? 780  PHE A CD2   1 
ATOM   5757  C  CE1   . PHE A  1  782  ? -14.808 86.151  110.549 1.00 26.57 ? 780  PHE A CE1   1 
ATOM   5758  C  CE2   . PHE A  1  782  ? -13.550 85.261  108.726 1.00 20.34 ? 780  PHE A CE2   1 
ATOM   5759  C  CZ    . PHE A  1  782  ? -14.438 86.185  109.219 1.00 23.55 ? 780  PHE A CZ    1 
ATOM   5760  N  N     . THR A  1  783  ? -15.430 81.789  110.275 1.00 19.30 ? 781  THR A N     1 
ATOM   5761  C  CA    . THR A  1  783  ? -15.895 81.591  108.913 1.00 22.06 ? 781  THR A CA    1 
ATOM   5762  C  C     . THR A  1  783  ? -16.523 82.901  108.471 1.00 22.84 ? 781  THR A C     1 
ATOM   5763  O  O     . THR A  1  783  ? -17.400 83.434  109.158 1.00 23.96 ? 781  THR A O     1 
ATOM   5764  C  CB    . THR A  1  783  ? -16.889 80.427  108.820 1.00 20.25 ? 781  THR A CB    1 
ATOM   5765  O  OG1   . THR A  1  783  ? -16.268 79.230  109.303 1.00 23.24 ? 781  THR A OG1   1 
ATOM   5766  C  CG2   . THR A  1  783  ? -17.263 80.214  107.396 1.00 22.91 ? 781  THR A CG2   1 
ATOM   5767  N  N     . GLY A  1  784  ? -16.041 83.436  107.355 1.00 23.53 ? 782  GLY A N     1 
ATOM   5768  C  CA    . GLY A  1  784  ? -16.459 84.756  106.928 1.00 21.59 ? 782  GLY A CA    1 
ATOM   5769  C  C     . GLY A  1  784  ? -15.543 85.265  105.835 1.00 22.01 ? 782  GLY A C     1 
ATOM   5770  O  O     . GLY A  1  784  ? -14.873 84.485  105.162 1.00 24.50 ? 782  GLY A O     1 
ATOM   5771  N  N     . SER A  1  785  ? -15.529 86.577  105.665 1.00 24.31 ? 783  SER A N     1 
ATOM   5772  C  CA    . SER A  1  785  ? -14.765 87.160  104.569 1.00 27.65 ? 783  SER A CA    1 
ATOM   5773  C  C     . SER A  1  785  ? -13.261 87.083  104.832 1.00 30.15 ? 783  SER A C     1 
ATOM   5774  O  O     . SER A  1  785  ? -12.800 87.106  105.980 1.00 24.98 ? 783  SER A O     1 
ATOM   5775  C  CB    . SER A  1  785  ? -15.184 88.609  104.355 1.00 29.52 ? 783  SER A CB    1 
ATOM   5776  O  OG    . SER A  1  785  ? -14.823 89.396  105.464 1.00 29.86 ? 783  SER A OG    1 
ATOM   5777  N  N     . THR A  1  786  ? -12.488 86.984  103.742 1.00 27.59 ? 784  THR A N     1 
ATOM   5778  C  CA    . THR A  1  786  ? -11.031 86.968  103.857 1.00 28.64 ? 784  THR A CA    1 
ATOM   5779  C  C     . THR A  1  786  ? -10.504 88.235  104.525 1.00 23.68 ? 784  THR A C     1 
ATOM   5780  O  O     . THR A  1  786  ? -9.532  88.185  105.291 1.00 26.57 ? 784  THR A O     1 
ATOM   5781  C  CB    . THR A  1  786  ? -10.395 86.789  102.474 1.00 30.22 ? 784  THR A CB    1 
ATOM   5782  O  OG1   . THR A  1  786  ? -10.958 85.639  101.839 1.00 31.37 ? 784  THR A OG1   1 
ATOM   5783  C  CG2   . THR A  1  786  ? -8.893  86.595  102.600 1.00 31.85 ? 784  THR A CG2   1 
ATOM   5784  N  N     . GLU A  1  787  ? -11.138 89.382  104.262 1.00 30.98 ? 785  GLU A N     1 
ATOM   5785  C  CA    . GLU A  1  787  ? -10.670 90.637  104.840 1.00 27.95 ? 785  GLU A CA    1 
ATOM   5786  C  C     . GLU A  1  787  ? -10.833 90.654  106.356 1.00 24.32 ? 785  GLU A C     1 
ATOM   5787  O  O     . GLU A  1  787  ? -9.954  91.139  107.075 1.00 25.11 ? 785  GLU A O     1 
ATOM   5788  C  CB    . GLU A  1  787  ? -11.411 91.821  104.213 1.00 33.29 ? 785  GLU A CB    1 
ATOM   5789  N  N     . VAL A  1  788  ? -11.944 90.123  106.863 1.00 26.93 ? 786  VAL A N     1 
ATOM   5790  C  CA    . VAL A  1  788  ? -12.127 90.105  108.310 1.00 24.37 ? 786  VAL A CA    1 
ATOM   5791  C  C     . VAL A  1  788  ? -11.205 89.072  108.949 1.00 23.66 ? 786  VAL A C     1 
ATOM   5792  O  O     . VAL A  1  788  ? -10.623 89.312  110.013 1.00 25.89 ? 786  VAL A O     1 
ATOM   5793  C  CB    . VAL A  1  788  ? -13.603 89.854  108.655 1.00 24.70 ? 786  VAL A CB    1 
ATOM   5794  C  CG1   . VAL A  1  788  ? -13.740 89.493  110.121 1.00 25.61 ? 786  VAL A CG1   1 
ATOM   5795  C  CG2   . VAL A  1  788  ? -14.417 91.113  108.349 1.00 29.43 ? 786  VAL A CG2   1 
ATOM   5796  N  N     . ALA A  1  789  ? -11.041 87.915  108.304 1.00 22.56 ? 787  ALA A N     1 
ATOM   5797  C  CA    . ALA A  1  789  ? -10.077 86.937  108.806 1.00 19.98 ? 787  ALA A CA    1 
ATOM   5798  C  C     . ALA A  1  789  ? -8.691  87.546  108.931 1.00 20.54 ? 787  ALA A C     1 
ATOM   5799  O  O     . ALA A  1  789  ? -7.956  87.253  109.882 1.00 21.86 ? 787  ALA A O     1 
ATOM   5800  C  CB    . ALA A  1  789  ? -10.037 85.715  107.887 1.00 18.31 ? 787  ALA A CB    1 
ATOM   5801  N  N     . ARG A  1  790  ? -8.311  88.393  107.975 1.00 20.94 ? 788  ARG A N     1 
ATOM   5802  C  CA    . ARG A  1  790  ? -6.987  89.000  108.025 1.00 21.89 ? 788  ARG A CA    1 
ATOM   5803  C  C     . ARG A  1  790  ? -6.870  89.937  109.223 1.00 23.29 ? 788  ARG A C     1 
ATOM   5804  O  O     . ARG A  1  790  ? -5.822  90.003  109.875 1.00 24.23 ? 788  ARG A O     1 
ATOM   5805  C  CB    . ARG A  1  790  ? -6.723  89.723  106.701 1.00 25.56 ? 788  ARG A CB    1 
ATOM   5806  C  CG    . ARG A  1  790  ? -5.321  90.271  106.499 1.00 26.43 ? 788  ARG A CG    1 
ATOM   5807  C  CD    . ARG A  1  790  ? -5.165  90.829  105.060 1.00 29.05 ? 788  ARG A CD    1 
ATOM   5808  N  NE    . ARG A  1  790  ? -5.104  89.770  104.053 1.00 29.80 ? 788  ARG A NE    1 
ATOM   5809  C  CZ    . ARG A  1  790  ? -5.941  89.626  103.034 1.00 33.42 ? 788  ARG A CZ    1 
ATOM   5810  N  NH1   . ARG A  1  790  ? -6.952  90.458  102.839 1.00 34.24 ? 788  ARG A NH1   1 
ATOM   5811  N  NH2   . ARG A  1  790  ? -5.754  88.623  102.180 1.00 31.52 ? 788  ARG A NH2   1 
ATOM   5812  N  N     . LEU A  1  791  ? -7.959  90.634  109.558 1.00 24.22 ? 789  LEU A N     1 
ATOM   5813  C  CA    . LEU A  1  791  ? -7.957  91.474  110.747 1.00 25.60 ? 789  LEU A CA    1 
ATOM   5814  C  C     . LEU A  1  791  ? -7.846  90.634  112.012 1.00 24.12 ? 789  LEU A C     1 
ATOM   5815  O  O     . LEU A  1  791  ? -7.135  91.007  112.948 1.00 25.08 ? 789  LEU A O     1 
ATOM   5816  C  CB    . LEU A  1  791  ? -9.219  92.331  110.784 1.00 24.81 ? 789  LEU A CB    1 
ATOM   5817  C  CG    . LEU A  1  791  ? -9.362  93.390  109.690 1.00 29.06 ? 789  LEU A CG    1 
ATOM   5818  C  CD1   . LEU A  1  791  ? -10.757 93.974  109.713 1.00 32.43 ? 789  LEU A CD1   1 
ATOM   5819  C  CD2   . LEU A  1  791  ? -8.325  94.474  109.884 1.00 30.58 ? 789  LEU A CD2   1 
ATOM   5820  N  N     . ILE A  1  792  ? -8.531  89.488  112.054 1.00 22.96 ? 790  ILE A N     1 
ATOM   5821  C  CA    . ILE A  1  792  ? -8.405  88.614  113.217 1.00 25.34 ? 790  ILE A CA    1 
ATOM   5822  C  C     . ILE A  1  792  ? -6.991  88.060  113.317 1.00 23.10 ? 790  ILE A C     1 
ATOM   5823  O  O     . ILE A  1  792  ? -6.401  88.017  114.408 1.00 25.00 ? 790  ILE A O     1 
ATOM   5824  C  CB    . ILE A  1  792  ? -9.462  87.498  113.159 1.00 22.73 ? 790  ILE A CB    1 
ATOM   5825  C  CG1   . ILE A  1  792  ? -10.853 88.095  113.355 1.00 24.68 ? 790  ILE A CG1   1 
ATOM   5826  C  CG2   . ILE A  1  792  ? -9.158  86.393  114.190 1.00 23.01 ? 790  ILE A CG2   1 
ATOM   5827  C  CD1   . ILE A  1  792  ? -11.977 87.137  113.038 1.00 25.00 ? 790  ILE A CD1   1 
ATOM   5828  N  N     . GLN A  1  793  ? -6.424  87.633  112.185 1.00 20.95 ? 791  GLN A N     1 
ATOM   5829  C  CA    . GLN A  1  793  ? -5.044  87.158  112.150 1.00 19.97 ? 791  GLN A CA    1 
ATOM   5830  C  C     . GLN A  1  793  ? -4.083  88.184  112.741 1.00 22.37 ? 791  GLN A C     1 
ATOM   5831  O  O     . GLN A  1  793  ? -3.200  87.840  113.535 1.00 23.25 ? 791  GLN A O     1 
ATOM   5832  C  CB    . GLN A  1  793  ? -4.669  86.821  110.702 1.00 24.48 ? 791  GLN A CB    1 
ATOM   5833  C  CG    . GLN A  1  793  ? -3.224  86.369  110.488 1.00 25.69 ? 791  GLN A CG    1 
ATOM   5834  C  CD    . GLN A  1  793  ? -2.788  86.426  109.019 1.00 30.69 ? 791  GLN A CD    1 
ATOM   5835  O  OE1   . GLN A  1  793  ? -3.077  87.388  108.299 1.00 34.30 ? 791  GLN A OE1   1 
ATOM   5836  N  NE2   . GLN A  1  793  ? -2.094  85.386  108.571 1.00 32.47 ? 791  GLN A NE2   1 
ATOM   5837  N  N     . ALA A  1  794  ? -4.252  89.455  112.372 1.00 26.18 ? 792  ALA A N     1 
ATOM   5838  C  CA    . ALA A  1  794  ? -3.365  90.488  112.890 1.00 27.81 ? 792  ALA A CA    1 
ATOM   5839  C  C     . ALA A  1  794  ? -3.530  90.649  114.396 1.00 26.54 ? 792  ALA A C     1 
ATOM   5840  O  O     . ALA A  1  794  ? -2.542  90.826  115.119 1.00 30.45 ? 792  ALA A O     1 
ATOM   5841  C  CB    . ALA A  1  794  ? -3.631  91.811  112.172 1.00 28.43 ? 792  ALA A CB    1 
ATOM   5842  N  N     . GLN A  1  795  ? -4.770  90.586  114.889 1.00 27.98 ? 793  GLN A N     1 
ATOM   5843  C  CA    . GLN A  1  795  ? -4.988  90.687  116.329 1.00 29.45 ? 793  GLN A CA    1 
ATOM   5844  C  C     . GLN A  1  795  ? -4.362  89.508  117.064 1.00 27.30 ? 793  GLN A C     1 
ATOM   5845  O  O     . GLN A  1  795  ? -3.716  89.684  118.105 1.00 28.93 ? 793  GLN A O     1 
ATOM   5846  C  CB    . GLN A  1  795  ? -6.483  90.780  116.631 1.00 33.69 ? 793  GLN A CB    1 
ATOM   5847  N  N     . LEU A  1  796  ? -4.507  88.300  116.518 1.00 24.58 ? 794  LEU A N     1 
ATOM   5848  C  CA    . LEU A  1  796  ? -3.977  87.131  117.209 1.00 27.54 ? 794  LEU A CA    1 
ATOM   5849  C  C     . LEU A  1  796  ? -2.457  87.103  117.209 1.00 26.21 ? 794  LEU A C     1 
ATOM   5850  O  O     . LEU A  1  796  ? -1.855  86.513  118.114 1.00 31.68 ? 794  LEU A O     1 
ATOM   5851  C  CB    . LEU A  1  796  ? -4.512  85.851  116.577 1.00 22.01 ? 794  LEU A CB    1 
ATOM   5852  C  CG    . LEU A  1  796  ? -5.980  85.535  116.831 1.00 24.58 ? 794  LEU A CG    1 
ATOM   5853  C  CD1   . LEU A  1  796  ? -6.342  84.214  116.178 1.00 23.27 ? 794  LEU A CD1   1 
ATOM   5854  C  CD2   . LEU A  1  796  ? -6.246  85.521  118.352 1.00 25.65 ? 794  LEU A CD2   1 
ATOM   5855  N  N     . ALA A  1  797  ? -1.821  87.719  116.215 1.00 27.55 ? 795  ALA A N     1 
ATOM   5856  C  CA    . ALA A  1  797  ? -0.366  87.697  116.155 1.00 29.27 ? 795  ALA A CA    1 
ATOM   5857  C  C     . ALA A  1  797  ? 0.258   88.453  117.316 1.00 29.47 ? 795  ALA A C     1 
ATOM   5858  O  O     . ALA A  1  797  ? 1.428   88.224  117.637 1.00 39.39 ? 795  ALA A O     1 
ATOM   5859  C  CB    . ALA A  1  797  ? 0.119   88.272  114.824 1.00 33.42 ? 795  ALA A CB    1 
ATOM   5860  N  N     . ASP A  1  798  ? -0.514  89.325  117.968 1.00 31.04 ? 796  ASP A N     1 
ATOM   5861  C  CA    . ASP A  1  798  ? -0.047  90.005  119.167 1.00 36.67 ? 796  ASP A CA    1 
ATOM   5862  C  C     . ASP A  1  798  ? 0.079   89.067  120.355 1.00 41.43 ? 796  ASP A C     1 
ATOM   5863  O  O     . ASP A  1  798  ? 0.769   89.411  121.322 1.00 34.90 ? 796  ASP A O     1 
ATOM   5864  C  CB    . ASP A  1  798  ? -0.995  91.149  119.533 1.00 29.23 ? 796  ASP A CB    1 
ATOM   5865  C  CG    . ASP A  1  798  ? -0.830  92.358  118.630 1.00 50.46 ? 796  ASP A CG    1 
ATOM   5866  O  OD1   . ASP A  1  798  ? 0.288   92.566  118.113 1.00 55.46 ? 796  ASP A OD1   1 
ATOM   5867  O  OD2   . ASP A  1  798  ? -1.815  93.108  118.444 1.00 47.71 ? 796  ASP A OD2   1 
ATOM   5868  N  N     . ARG A  1  799  ? -0.558  87.896  120.305 1.00 32.62 ? 797  ARG A N     1 
ATOM   5869  C  CA    . ARG A  1  799  ? -0.771  87.088  121.493 1.00 35.85 ? 797  ARG A CA    1 
ATOM   5870  C  C     . ARG A  1  799  ? -0.071  85.740  121.392 1.00 30.93 ? 797  ARG A C     1 
ATOM   5871  O  O     . ARG A  1  799  ? 0.170   85.204  120.302 1.00 27.23 ? 797  ARG A O     1 
ATOM   5872  C  CB    . ARG A  1  799  ? -2.276  86.874  121.756 1.00 38.20 ? 797  ARG A CB    1 
ATOM   5873  C  CG    . ARG A  1  799  ? -3.028  88.164  122.055 1.00 38.65 ? 797  ARG A CG    1 
ATOM   5874  C  CD    . ARG A  1  799  ? -4.201  87.951  123.004 1.00 35.08 ? 797  ARG A CD    1 
ATOM   5875  N  NE    . ARG A  1  799  ? -5.311  87.254  122.371 1.00 42.46 ? 797  ARG A NE    1 
ATOM   5876  C  CZ    . ARG A  1  799  ? -5.658  86.001  122.635 1.00 41.05 ? 797  ARG A CZ    1 
ATOM   5877  N  NH1   . ARG A  1  799  ? -5.026  85.288  123.555 1.00 39.85 ? 797  ARG A NH1   1 
ATOM   5878  N  NH2   . ARG A  1  799  ? -6.667  85.451  121.964 1.00 32.95 ? 797  ARG A NH2   1 
ATOM   5879  N  N     . LEU A  1  800  ? 0.266   85.210  122.560 1.00 29.61 ? 798  LEU A N     1 
ATOM   5880  C  CA    . LEU A  1  800  ? 0.751   83.851  122.710 1.00 29.50 ? 798  LEU A CA    1 
ATOM   5881  C  C     . LEU A  1  800  ? -0.067  83.177  123.799 1.00 29.66 ? 798  LEU A C     1 
ATOM   5882  O  O     . LEU A  1  800  ? -0.611  83.838  124.684 1.00 33.13 ? 798  LEU A O     1 
ATOM   5883  C  CB    . LEU A  1  800  ? 2.237   83.807  123.075 1.00 31.93 ? 798  LEU A CB    1 
ATOM   5884  C  CG    . LEU A  1  800  ? 3.248   84.285  122.030 1.00 34.22 ? 798  LEU A CG    1 
ATOM   5885  C  CD1   . LEU A  1  800  ? 4.622   84.417  122.669 1.00 37.11 ? 798  LEU A CD1   1 
ATOM   5886  C  CD2   . LEU A  1  800  ? 3.290   83.343  120.838 1.00 31.50 ? 798  LEU A CD2   1 
ATOM   5887  N  N     . SER A  1  801  ? -0.163  81.859  123.711 1.00 32.23 ? 799  SER A N     1 
ATOM   5888  C  CA    . SER A  1  801  ? -0.758  81.052  124.768 1.00 33.39 ? 799  SER A CA    1 
ATOM   5889  C  C     . SER A  1  801  ? 0.092   81.163  126.033 1.00 38.77 ? 799  SER A C     1 
ATOM   5890  O  O     . SER A  1  801  ? 1.225   81.661  125.973 1.00 35.95 ? 799  SER A O     1 
ATOM   5891  C  CB    . SER A  1  801  ? -0.862  79.595  124.312 1.00 36.93 ? 799  SER A CB    1 
ATOM   5892  O  OG    . SER A  1  801  ? 0.428   79.005  124.227 1.00 38.49 ? 799  SER A OG    1 
ATOM   5893  N  N     . PRO A  1  802  ? -0.413  80.734  127.196 1.00 36.96 ? 800  PRO A N     1 
ATOM   5894  C  CA    . PRO A  1  802  ? 0.446   80.721  128.395 1.00 39.40 ? 800  PRO A CA    1 
ATOM   5895  C  C     . PRO A  1  802  ? 1.716   79.909  128.212 1.00 41.67 ? 800  PRO A C     1 
ATOM   5896  O  O     . PRO A  1  802  ? 2.742   80.210  128.843 1.00 43.82 ? 800  PRO A O     1 
ATOM   5897  C  CB    . PRO A  1  802  ? -0.462  80.113  129.471 1.00 46.61 ? 800  PRO A CB    1 
ATOM   5898  C  CG    . PRO A  1  802  ? -1.847  80.422  129.010 1.00 45.56 ? 800  PRO A CG    1 
ATOM   5899  C  CD    . PRO A  1  802  ? -1.800  80.346  127.508 1.00 39.12 ? 800  PRO A CD    1 
ATOM   5900  N  N     . ALA A  1  803  ? 1.678   78.881  127.370 1.00 38.67 ? 801  ALA A N     1 
ATOM   5901  C  CA    . ALA A  1  803  ? 2.871   78.135  127.005 1.00 45.15 ? 801  ALA A CA    1 
ATOM   5902  C  C     . ALA A  1  803  ? 3.767   78.887  126.028 1.00 43.35 ? 801  ALA A C     1 
ATOM   5903  O  O     . ALA A  1  803  ? 4.867   78.411  125.737 1.00 39.68 ? 801  ALA A O     1 
ATOM   5904  C  CB    . ALA A  1  803  ? 2.479   76.786  126.399 1.00 40.61 ? 801  ALA A CB    1 
ATOM   5905  N  N     . GLY A  1  804  ? 3.328   80.031  125.515 1.00 43.40 ? 802  GLY A N     1 
ATOM   5906  C  CA    . GLY A  1  804  ? 4.147   80.807  124.600 1.00 35.31 ? 802  GLY A CA    1 
ATOM   5907  C  C     . GLY A  1  804  ? 4.099   80.360  123.155 1.00 36.20 ? 802  GLY A C     1 
ATOM   5908  O  O     . GLY A  1  804  ? 5.112   80.447  122.450 1.00 34.79 ? 802  GLY A O     1 
ATOM   5909  N  N     . ARG A  1  805  ? 2.947   79.899  122.682 1.00 33.78 ? 803  ARG A N     1 
ATOM   5910  C  CA    . ARG A  1  805  ? 2.781   79.422  121.319 1.00 35.53 ? 803  ARG A CA    1 
ATOM   5911  C  C     . ARG A  1  805  ? 1.616   80.147  120.659 1.00 25.84 ? 803  ARG A C     1 
ATOM   5912  O  O     . ARG A  1  805  ? 0.778   80.739  121.348 1.00 27.16 ? 803  ARG A O     1 
ATOM   5913  C  CB    . ARG A  1  805  ? 2.557   77.903  121.299 1.00 32.91 ? 803  ARG A CB    1 
ATOM   5914  C  CG    . ARG A  1  805  ? 3.706   77.122  121.946 1.00 34.88 ? 803  ARG A CG    1 
ATOM   5915  C  CD    . ARG A  1  805  ? 5.052   77.414  121.264 1.00 36.77 ? 803  ARG A CD    1 
ATOM   5916  N  NE    . ARG A  1  805  ? 6.155   76.677  121.878 1.00 30.78 ? 803  ARG A NE    1 
ATOM   5917  C  CZ    . ARG A  1  805  ? 7.048   77.194  122.713 1.00 36.50 ? 803  ARG A CZ    1 
ATOM   5918  N  NH1   . ARG A  1  805  ? 7.029   78.475  123.046 1.00 34.75 ? 803  ARG A NH1   1 
ATOM   5919  N  NH2   . ARG A  1  805  ? 7.986   76.404  123.229 1.00 46.84 ? 803  ARG A NH2   1 
ATOM   5920  N  N     . PRO A  1  806  ? 1.569   80.174  119.323 1.00 27.32 ? 804  PRO A N     1 
ATOM   5921  C  CA    . PRO A  1  806  ? 0.512   80.936  118.645 1.00 25.76 ? 804  PRO A CA    1 
ATOM   5922  C  C     . PRO A  1  806  ? -0.871  80.402  118.975 1.00 26.76 ? 804  PRO A C     1 
ATOM   5923  O  O     . PRO A  1  806  ? -1.074  79.197  119.155 1.00 27.93 ? 804  PRO A O     1 
ATOM   5924  C  CB    . PRO A  1  806  ? 0.837   80.748  117.159 1.00 27.36 ? 804  PRO A CB    1 
ATOM   5925  C  CG    . PRO A  1  806  ? 2.305   80.457  117.132 1.00 29.42 ? 804  PRO A CG    1 
ATOM   5926  C  CD    . PRO A  1  806  ? 2.547   79.635  118.366 1.00 26.79 ? 804  PRO A CD    1 
ATOM   5927  N  N     . ILE A  1  807  ? -1.826  81.322  119.041 1.00 24.35 ? 805  ILE A N     1 
ATOM   5928  C  CA    . ILE A  1  807  ? -3.228  80.978  119.258 1.00 26.02 ? 805  ILE A CA    1 
ATOM   5929  C  C     . ILE A  1  807  ? -3.773  80.404  117.956 1.00 24.22 ? 805  ILE A C     1 
ATOM   5930  O  O     . ILE A  1  807  ? -3.754  81.091  116.926 1.00 23.33 ? 805  ILE A O     1 
ATOM   5931  C  CB    . ILE A  1  807  ? -4.037  82.201  119.715 1.00 24.26 ? 805  ILE A CB    1 
ATOM   5932  C  CG1   . ILE A  1  807  ? -3.443  82.792  120.999 1.00 27.30 ? 805  ILE A CG1   1 
ATOM   5933  C  CG2   . ILE A  1  807  ? -5.518  81.842  119.886 1.00 24.01 ? 805  ILE A CG2   1 
ATOM   5934  C  CD1   . ILE A  1  807  ? -3.546  81.896  122.209 1.00 28.30 ? 805  ILE A CD1   1 
ATOM   5935  N  N     . PRO A  1  808  ? -4.241  79.157  117.943 1.00 22.50 ? 806  PRO A N     1 
ATOM   5936  C  CA    . PRO A  1  808  ? -4.723  78.565  116.690 1.00 23.23 ? 806  PRO A CA    1 
ATOM   5937  C  C     . PRO A  1  808  ? -5.903  79.333  116.120 1.00 20.85 ? 806  PRO A C     1 
ATOM   5938  O  O     . PRO A  1  808  ? -6.819  79.733  116.840 1.00 22.31 ? 806  PRO A O     1 
ATOM   5939  C  CB    . PRO A  1  808  ? -5.131  77.149  117.107 1.00 24.63 ? 806  PRO A CB    1 
ATOM   5940  C  CG    . PRO A  1  808  ? -4.298  76.859  118.298 1.00 27.55 ? 806  PRO A CG    1 
ATOM   5941  C  CD    . PRO A  1  808  ? -4.209  78.178  119.040 1.00 23.10 ? 806  PRO A CD    1 
ATOM   5942  N  N     . LEU A  1  809  ? -5.868  79.536  114.805 1.00 22.79 ? 807  LEU A N     1 
ATOM   5943  C  CA    . LEU A  1  809  ? -6.954  80.166  114.069 1.00 21.26 ? 807  LEU A CA    1 
ATOM   5944  C  C     . LEU A  1  809  ? -7.359  79.248  112.925 1.00 21.98 ? 807  LEU A C     1 
ATOM   5945  O  O     . LEU A  1  809  ? -6.516  78.873  112.099 1.00 23.52 ? 807  LEU A O     1 
ATOM   5946  C  CB    . LEU A  1  809  ? -6.533  81.530  113.517 1.00 24.42 ? 807  LEU A CB    1 
ATOM   5947  C  CG    . LEU A  1  809  ? -7.495  82.156  112.509 1.00 23.07 ? 807  LEU A CG    1 
ATOM   5948  C  CD1   . LEU A  1  809  ? -8.794  82.566  113.182 1.00 24.39 ? 807  LEU A CD1   1 
ATOM   5949  C  CD2   . LEU A  1  809  ? -6.857  83.355  111.826 1.00 27.21 ? 807  LEU A CD2   1 
ATOM   5950  N  N     . ILE A  1  810  ? -8.631  78.856  112.896 1.00 19.52 ? 808  ILE A N     1 
ATOM   5951  C  CA    . ILE A  1  810  ? -9.213  78.208  111.731 1.00 20.62 ? 808  ILE A CA    1 
ATOM   5952  C  C     . ILE A  1  810  ? -10.032 79.270  111.037 1.00 22.54 ? 808  ILE A C     1 
ATOM   5953  O  O     . ILE A  1  810  ? -11.005 79.774  111.606 1.00 22.31 ? 808  ILE A O     1 
ATOM   5954  C  CB    . ILE A  1  810  ? -10.085 76.999  112.103 1.00 18.70 ? 808  ILE A CB    1 
ATOM   5955  C  CG1   . ILE A  1  810  ? -9.304  76.000  112.943 1.00 21.67 ? 808  ILE A CG1   1 
ATOM   5956  C  CG2   . ILE A  1  810  ? -10.594 76.310  110.820 1.00 20.94 ? 808  ILE A CG2   1 
ATOM   5957  C  CD1   . ILE A  1  810  ? -10.126 74.760  113.291 1.00 26.86 ? 808  ILE A CD1   1 
ATOM   5958  N  N     . ALA A  1  811  ? -9.637  79.625  109.818 1.00 20.43 ? 809  ALA A N     1 
ATOM   5959  C  CA    . ALA A  1  811  ? -10.246 80.743  109.108 1.00 20.43 ? 809  ALA A CA    1 
ATOM   5960  C  C     . ALA A  1  811  ? -10.669 80.240  107.743 1.00 22.35 ? 809  ALA A C     1 
ATOM   5961  O  O     . ALA A  1  811  ? -9.823  79.970  106.883 1.00 23.25 ? 809  ALA A O     1 
ATOM   5962  C  CB    . ALA A  1  811  ? -9.278  81.922  108.979 1.00 24.29 ? 809  ALA A CB    1 
ATOM   5963  N  N     . GLU A  1  812  ? -11.968 80.092  107.558 1.00 20.65 ? 810  GLU A N     1 
ATOM   5964  C  CA    . GLU A  1  812  ? -12.511 79.580  106.310 1.00 19.42 ? 810  GLU A CA    1 
ATOM   5965  C  C     . GLU A  1  812  ? -13.202 80.742  105.611 1.00 22.53 ? 810  GLU A C     1 
ATOM   5966  O  O     . GLU A  1  812  ? -14.125 81.351  106.165 1.00 22.87 ? 810  GLU A O     1 
ATOM   5967  C  CB    . GLU A  1  812  ? -13.435 78.399  106.586 1.00 24.71 ? 810  GLU A CB    1 
ATOM   5968  C  CG    . GLU A  1  812  ? -12.693 77.276  107.339 1.00 24.69 ? 810  GLU A CG    1 
ATOM   5969  C  CD    . GLU A  1  812  ? -11.532 76.663  106.532 1.00 33.73 ? 810  GLU A CD    1 
ATOM   5970  O  OE1   . GLU A  1  812  ? -11.807 75.863  105.617 1.00 31.97 ? 810  GLU A OE1   1 
ATOM   5971  O  OE2   . GLU A  1  812  ? -10.349 76.976  106.800 1.00 25.68 ? 810  GLU A OE2   1 
ATOM   5972  N  N     . THR A  1  813  ? -12.699 81.099  104.436 1.00 21.94 ? 811  THR A N     1 
ATOM   5973  C  CA    . THR A  1  813  ? -13.002 82.391  103.842 1.00 19.75 ? 811  THR A CA    1 
ATOM   5974  C  C     . THR A  1  813  ? -13.535 82.173  102.430 1.00 23.59 ? 811  THR A C     1 
ATOM   5975  O  O     . THR A  1  813  ? -14.072 81.116  102.089 1.00 24.39 ? 811  THR A O     1 
ATOM   5976  C  CB    . THR A  1  813  ? -11.771 83.302  103.938 1.00 22.06 ? 811  THR A CB    1 
ATOM   5977  O  OG1   . THR A  1  813  ? -10.603 82.607  103.482 1.00 23.37 ? 811  THR A OG1   1 
ATOM   5978  C  CG2   . THR A  1  813  ? -11.559 83.695  105.388 1.00 21.75 ? 811  THR A CG2   1 
ATOM   5979  N  N     . GLY A  1  814  ? -13.441 83.199  101.598 1.00 24.99 ? 812  GLY A N     1 
ATOM   5980  C  CA    . GLY A  1  814  ? -14.218 83.225  100.377 1.00 29.09 ? 812  GLY A CA    1 
ATOM   5981  C  C     . GLY A  1  814  ? -13.646 82.358  99.272  1.00 28.11 ? 812  GLY A C     1 
ATOM   5982  O  O     . GLY A  1  814  ? -12.643 81.665  99.419  1.00 26.05 ? 812  GLY A O     1 
ATOM   5983  N  N     . GLY A  1  815  ? -14.321 82.398  98.128  1.00 23.60 ? 813  GLY A N     1 
ATOM   5984  C  CA    . GLY A  1  815  ? -13.827 81.724  96.950  1.00 22.15 ? 813  GLY A CA    1 
ATOM   5985  C  C     . GLY A  1  815  ? -14.136 82.547  95.718  1.00 21.73 ? 813  GLY A C     1 
ATOM   5986  O  O     . GLY A  1  815  ? -14.943 83.476  95.749  1.00 30.07 ? 813  GLY A O     1 
ATOM   5987  N  N     . GLN A  1  816  ? -13.422 82.235  94.653  1.00 21.56 ? 814  GLN A N     1 
ATOM   5988  C  CA    . GLN A  1  816  ? -13.701 82.774  93.327  1.00 19.04 ? 814  GLN A CA    1 
ATOM   5989  C  C     . GLN A  1  816  ? -13.888 81.569  92.425  1.00 17.16 ? 814  GLN A C     1 
ATOM   5990  O  O     . GLN A  1  816  ? -13.054 81.274  91.569  1.00 20.11 ? 814  GLN A O     1 
ATOM   5991  C  CB    . GLN A  1  816  ? -12.576 83.683  92.846  1.00 21.62 ? 814  GLN A CB    1 
ATOM   5992  C  CG    . GLN A  1  816  ? -12.931 84.502  91.623  1.00 23.69 ? 814  GLN A CG    1 
ATOM   5993  C  CD    . GLN A  1  816  ? -13.989 85.548  91.932  1.00 30.38 ? 814  GLN A CD    1 
ATOM   5994  O  OE1   . GLN A  1  816  ? -15.173 85.238  92.014  1.00 27.41 ? 814  GLN A OE1   1 
ATOM   5995  N  NE2   . GLN A  1  816  ? -13.559 86.792  92.121  1.00 28.06 ? 814  GLN A NE2   1 
ATOM   5996  N  N     . ASN A  1  817  ? -14.968 80.845  92.678  1.00 17.95 ? 815  ASN A N     1 
ATOM   5997  C  CA    . ASN A  1  817  ? -15.074 79.460  92.250  1.00 16.12 ? 815  ASN A CA    1 
ATOM   5998  C  C     . ASN A  1  817  ? -15.433 79.375  90.780  1.00 15.95 ? 815  ASN A C     1 
ATOM   5999  O  O     . ASN A  1  817  ? -16.350 80.061  90.308  1.00 18.95 ? 815  ASN A O     1 
ATOM   6000  C  CB    . ASN A  1  817  ? -16.123 78.749  93.099  1.00 18.28 ? 815  ASN A CB    1 
ATOM   6001  C  CG    . ASN A  1  817  ? -15.910 78.998  94.575  1.00 17.94 ? 815  ASN A CG    1 
ATOM   6002  O  OD1   . ASN A  1  817  ? -14.824 78.732  95.100  1.00 17.28 ? 815  ASN A OD1   1 
ATOM   6003  N  ND2   . ASN A  1  817  ? -16.923 79.529  95.251  1.00 17.24 ? 815  ASN A ND2   1 
ATOM   6004  N  N     . ALA A  1  818  ? -14.727 78.508  90.068  1.00 15.99 ? 816  ALA A N     1 
ATOM   6005  C  CA    . ALA A  1  818  ? -14.895 78.359  88.637  1.00 17.28 ? 816  ALA A CA    1 
ATOM   6006  C  C     . ALA A  1  818  ? -15.471 76.995  88.305  1.00 16.01 ? 816  ALA A C     1 
ATOM   6007  O  O     . ALA A  1  818  ? -15.324 76.028  89.052  1.00 17.08 ? 816  ALA A O     1 
ATOM   6008  C  CB    . ALA A  1  818  ? -13.560 78.533  87.907  1.00 19.92 ? 816  ALA A CB    1 
ATOM   6009  N  N     . MET A  1  819  ? -16.121 76.934  87.153  1.00 18.64 ? 817  MET A N     1 
ATOM   6010  C  CA    . MET A  1  819  ? -16.492 75.670  86.538  1.00 16.28 ? 817  MET A CA    1 
ATOM   6011  C  C     . MET A  1  819  ? -16.016 75.709  85.099  1.00 16.06 ? 817  MET A C     1 
ATOM   6012  O  O     . MET A  1  819  ? -16.238 76.704  84.408  1.00 17.99 ? 817  MET A O     1 
ATOM   6013  C  CB    . MET A  1  819  ? -17.997 75.436  86.583  1.00 18.40 ? 817  MET A CB    1 
ATOM   6014  C  CG    . MET A  1  819  ? -18.427 74.174  85.849  1.00 19.21 ? 817  MET A CG    1 
ATOM   6015  S  SD    . MET A  1  819  ? -20.224 74.005  85.775  1.00 19.92 ? 817  MET A SD    1 
ATOM   6016  C  CE    . MET A  1  819  ? -20.596 73.679  87.508  1.00 19.65 ? 817  MET A CE    1 
ATOM   6017  N  N     . ILE A  1  820  ? -15.339 74.647  84.666  1.00 16.24 ? 818  ILE A N     1 
ATOM   6018  C  CA    . ILE A  1  820  ? -14.869 74.512  83.294  1.00 16.90 ? 818  ILE A CA    1 
ATOM   6019  C  C     . ILE A  1  820  ? -15.751 73.496  82.592  1.00 14.70 ? 818  ILE A C     1 
ATOM   6020  O  O     . ILE A  1  820  ? -16.021 72.417  83.135  1.00 16.34 ? 818  ILE A O     1 
ATOM   6021  C  CB    . ILE A  1  820  ? -13.392 74.088  83.238  1.00 17.76 ? 818  ILE A CB    1 
ATOM   6022  C  CG1   . ILE A  1  820  ? -12.528 75.170  83.864  1.00 18.51 ? 818  ILE A CG1   1 
ATOM   6023  C  CG2   . ILE A  1  820  ? -12.966 73.822  81.783  1.00 19.35 ? 818  ILE A CG2   1 
ATOM   6024  C  CD1   . ILE A  1  820  ? -11.046 74.823  83.890  1.00 18.89 ? 818  ILE A CD1   1 
ATOM   6025  N  N     . VAL A  1  821  ? -16.233 73.863  81.405  1.00 15.84 ? 819  VAL A N     1 
ATOM   6026  C  CA    . VAL A  1  821  ? -17.153 73.040  80.635  1.00 17.18 ? 819  VAL A CA    1 
ATOM   6027  C  C     . VAL A  1  821  ? -16.547 72.862  79.258  1.00 18.26 ? 819  VAL A C     1 
ATOM   6028  O  O     . VAL A  1  821  ? -16.247 73.854  78.584  1.00 19.81 ? 819  VAL A O     1 
ATOM   6029  C  CB    . VAL A  1  821  ? -18.535 73.706  80.523  1.00 16.05 ? 819  VAL A CB    1 
ATOM   6030  C  CG1   . VAL A  1  821  ? -19.447 72.902  79.612  1.00 18.07 ? 819  VAL A CG1   1 
ATOM   6031  C  CG2   . VAL A  1  821  ? -19.134 73.878  81.906  1.00 17.36 ? 819  VAL A CG2   1 
ATOM   6032  N  N     . ASP A  1  822  ? -16.379 71.619  78.825  1.00 16.77 ? 820  ASP A N     1 
ATOM   6033  C  CA    . ASP A  1  822  ? -15.849 71.422  77.483  1.00 19.18 ? 820  ASP A CA    1 
ATOM   6034  C  C     . ASP A  1  822  ? -16.964 70.950  76.562  1.00 17.20 ? 820  ASP A C     1 
ATOM   6035  O  O     . ASP A  1  822  ? -18.122 70.835  76.959  1.00 19.02 ? 820  ASP A O     1 
ATOM   6036  C  CB    . ASP A  1  822  ? -14.634 70.484  77.486  1.00 21.25 ? 820  ASP A CB    1 
ATOM   6037  C  CG    . ASP A  1  822  ? -14.971 69.012  77.740  1.00 19.39 ? 820  ASP A CG    1 
ATOM   6038  O  OD1   . ASP A  1  822  ? -16.152 68.576  77.703  1.00 20.21 ? 820  ASP A OD1   1 
ATOM   6039  O  OD2   . ASP A  1  822  ? -13.980 68.276  77.988  1.00 20.51 ? 820  ASP A OD2   1 
ATOM   6040  N  N     . SER A  1  823  ? -16.605 70.726  75.296  1.00 20.16 ? 821  SER A N     1 
ATOM   6041  C  CA    . SER A  1  823  ? -17.599 70.413  74.283  1.00 20.99 ? 821  SER A CA    1 
ATOM   6042  C  C     . SER A  1  823  ? -18.160 69.010  74.396  1.00 21.88 ? 821  SER A C     1 
ATOM   6043  O  O     . SER A  1  823  ? -19.047 68.661  73.606  1.00 25.34 ? 821  SER A O     1 
ATOM   6044  C  CB    . SER A  1  823  ? -17.001 70.611  72.885  1.00 21.35 ? 821  SER A CB    1 
ATOM   6045  O  OG    . SER A  1  823  ? -15.843 69.819  72.719  1.00 25.29 ? 821  SER A OG    1 
ATOM   6046  N  N     . SER A  1  824  ? -17.663 68.187  75.321  1.00 19.46 ? 822  SER A N     1 
ATOM   6047  C  CA    . SER A  1  824  ? -18.226 66.865  75.530  1.00 17.49 ? 822  SER A CA    1 
ATOM   6048  C  C     . SER A  1  824  ? -19.345 66.853  76.562  1.00 20.68 ? 822  SER A C     1 
ATOM   6049  O  O     . SER A  1  824  ? -20.061 65.854  76.668  1.00 21.44 ? 822  SER A O     1 
ATOM   6050  C  CB    . SER A  1  824  ? -17.131 65.882  75.959  1.00 20.70 ? 822  SER A CB    1 
ATOM   6051  O  OG    . SER A  1  824  ? -16.760 66.097  77.313  1.00 19.95 ? 822  SER A OG    1 
ATOM   6052  N  N     . ALA A  1  825  ? -19.519 67.941  77.314  1.00 19.23 ? 823  ALA A N     1 
ATOM   6053  C  CA    . ALA A  1  825  ? -20.545 67.992  78.340  1.00 20.78 ? 823  ALA A CA    1 
ATOM   6054  C  C     . ALA A  1  825  ? -21.937 68.107  77.722  1.00 20.74 ? 823  ALA A C     1 
ATOM   6055  O  O     . ALA A  1  825  ? -22.107 68.622  76.618  1.00 24.27 ? 823  ALA A O     1 
ATOM   6056  C  CB    . ALA A  1  825  ? -20.276 69.176  79.267  1.00 20.42 ? 823  ALA A CB    1 
ATOM   6057  N  N     . LEU A  1  826  ? -22.938 67.615  78.444  1.00 22.18 ? 824  LEU A N     1 
ATOM   6058  C  CA    . LEU A  1  826  ? -24.327 67.717  78.006  1.00 21.85 ? 824  LEU A CA    1 
ATOM   6059  C  C     . LEU A  1  826  ? -24.878 69.065  78.452  1.00 25.04 ? 824  LEU A C     1 
ATOM   6060  O  O     . LEU A  1  826  ? -24.961 69.341  79.657  1.00 24.19 ? 824  LEU A O     1 
ATOM   6061  C  CB    . LEU A  1  826  ? -25.167 66.571  78.568  1.00 28.16 ? 824  LEU A CB    1 
ATOM   6062  C  CG    . LEU A  1  826  ? -26.586 66.443  78.008  1.00 36.40 ? 824  LEU A CG    1 
ATOM   6063  C  CD1   . LEU A  1  826  ? -26.549 66.281  76.487  1.00 36.21 ? 824  LEU A CD1   1 
ATOM   6064  C  CD2   . LEU A  1  826  ? -27.312 65.277  78.649  1.00 36.17 ? 824  LEU A CD2   1 
ATOM   6065  N  N     . ALA A  1  827  ? -25.260 69.897  77.482  1.00 23.88 ? 825  ALA A N     1 
ATOM   6066  C  CA    . ALA A  1  827  ? -25.599 71.285  77.788  1.00 22.23 ? 825  ALA A CA    1 
ATOM   6067  C  C     . ALA A  1  827  ? -26.713 71.383  78.824  1.00 21.98 ? 825  ALA A C     1 
ATOM   6068  O  O     . ALA A  1  827  ? -26.625 72.194  79.754  1.00 20.76 ? 825  ALA A O     1 
ATOM   6069  C  CB    . ALA A  1  827  ? -25.983 72.024  76.507  1.00 23.90 ? 825  ALA A CB    1 
ATOM   6070  N  N     . GLU A  1  828  ? -27.751 70.547  78.704  1.00 21.21 ? 826  GLU A N     1 
ATOM   6071  C  CA    . GLU A  1  828  ? -28.860 70.599  79.654  1.00 22.11 ? 826  GLU A CA    1 
ATOM   6072  C  C     . GLU A  1  828  ? -28.397 70.319  81.083  1.00 21.06 ? 826  GLU A C     1 
ATOM   6073  O  O     . GLU A  1  828  ? -28.855 70.974  82.030  1.00 23.18 ? 826  GLU A O     1 
ATOM   6074  C  CB    . GLU A  1  828  ? -29.948 69.603  79.245  1.00 29.30 ? 826  GLU A CB    1 
ATOM   6075  C  CG    . GLU A  1  828  ? -30.812 70.059  78.070  1.00 31.70 ? 826  GLU A CG    1 
ATOM   6076  C  CD    . GLU A  1  828  ? -30.193 69.760  76.711  1.00 38.71 ? 826  GLU A CD    1 
ATOM   6077  O  OE1   . GLU A  1  828  ? -29.041 69.278  76.653  1.00 32.86 ? 826  GLU A OE1   1 
ATOM   6078  O  OE2   . GLU A  1  828  ? -30.873 70.011  75.691  1.00 46.38 ? 826  GLU A OE2   1 
ATOM   6079  N  N     . GLN A  1  829  ? -27.521 69.327  81.262  1.00 22.86 ? 827  GLN A N     1 
ATOM   6080  C  CA    . GLN A  1  829  ? -26.951 69.047  82.579  1.00 22.66 ? 827  GLN A CA    1 
ATOM   6081  C  C     . GLN A  1  829  ? -26.140 70.228  83.084  1.00 20.07 ? 827  GLN A C     1 
ATOM   6082  O  O     . GLN A  1  829  ? -26.241 70.621  84.257  1.00 20.10 ? 827  GLN A O     1 
ATOM   6083  C  CB    . GLN A  1  829  ? -26.043 67.820  82.522  1.00 29.37 ? 827  GLN A CB    1 
ATOM   6084  C  CG    . GLN A  1  829  ? -26.709 66.478  82.477  1.00 37.22 ? 827  GLN A CG    1 
ATOM   6085  C  CD    . GLN A  1  829  ? -25.682 65.368  82.580  1.00 45.55 ? 827  GLN A CD    1 
ATOM   6086  O  OE1   . GLN A  1  829  ? -24.485 65.603  82.393  1.00 31.99 ? 827  GLN A OE1   1 
ATOM   6087  N  NE2   . GLN A  1  829  ? -26.137 64.160  82.895  1.00 46.11 ? 827  GLN A NE2   1 
ATOM   6088  N  N     . VAL A  1  830  ? -25.288 70.769  82.215  1.00 18.01 ? 828  VAL A N     1 
ATOM   6089  C  CA    . VAL A  1  830  ? -24.444 71.904  82.576  1.00 17.68 ? 828  VAL A CA    1 
ATOM   6090  C  C     . VAL A  1  830  ? -25.301 73.061  83.052  1.00 21.76 ? 828  VAL A C     1 
ATOM   6091  O  O     . VAL A  1  830  ? -25.047 73.659  84.105  1.00 18.69 ? 828  VAL A O     1 
ATOM   6092  C  CB    . VAL A  1  830  ? -23.568 72.328  81.384  1.00 16.60 ? 828  VAL A CB    1 
ATOM   6093  C  CG1   . VAL A  1  830  ? -22.913 73.677  81.653  1.00 18.96 ? 828  VAL A CG1   1 
ATOM   6094  C  CG2   . VAL A  1  830  ? -22.509 71.273  81.091  1.00 19.69 ? 828  VAL A CG2   1 
ATOM   6095  N  N     . VAL A  1  831  ? -26.332 73.397  82.277  1.00 18.54 ? 829  VAL A N     1 
ATOM   6096  C  CA    . VAL A  1  831  ? -27.116 74.579  82.603  1.00 17.05 ? 829  VAL A CA    1 
ATOM   6097  C  C     . VAL A  1  831  ? -27.796 74.417  83.953  1.00 17.57 ? 829  VAL A C     1 
ATOM   6098  O  O     . VAL A  1  831  ? -27.816 75.349  84.763  1.00 17.60 ? 829  VAL A O     1 
ATOM   6099  C  CB    . VAL A  1  831  ? -28.117 74.870  81.474  1.00 16.35 ? 829  VAL A CB    1 
ATOM   6100  C  CG1   . VAL A  1  831  ? -29.104 75.929  81.910  1.00 20.55 ? 829  VAL A CG1   1 
ATOM   6101  C  CG2   . VAL A  1  831  ? -27.357 75.337  80.252  1.00 21.71 ? 829  VAL A CG2   1 
ATOM   6102  N  N     . GLY A  1  832  ? -28.366 73.241  84.222  1.00 17.41 ? 830  GLY A N     1 
ATOM   6103  C  CA    . GLY A  1  832  ? -29.000 73.036  85.510  1.00 17.85 ? 830  GLY A CA    1 
ATOM   6104  C  C     . GLY A  1  832  ? -28.004 73.178  86.644  1.00 18.90 ? 830  GLY A C     1 
ATOM   6105  O  O     . GLY A  1  832  ? -28.294 73.795  87.672  1.00 18.06 ? 830  GLY A O     1 
ATOM   6106  N  N     . ASP A  1  833  ? -26.812 72.628  86.460  1.00 17.10 ? 831  ASP A N     1 
ATOM   6107  C  CA    . ASP A  1  833  ? -25.815 72.714  87.520  1.00 16.85 ? 831  ASP A CA    1 
ATOM   6108  C  C     . ASP A  1  833  ? -25.288 74.127  87.687  1.00 17.61 ? 831  ASP A C     1 
ATOM   6109  O  O     . ASP A  1  833  ? -24.926 74.518  88.803  1.00 19.09 ? 831  ASP A O     1 
ATOM   6110  C  CB    . ASP A  1  833  ? -24.664 71.747  87.237  1.00 17.11 ? 831  ASP A CB    1 
ATOM   6111  C  CG    . ASP A  1  833  ? -25.072 70.305  87.412  1.00 19.83 ? 831  ASP A CG    1 
ATOM   6112  O  OD1   . ASP A  1  833  ? -26.153 70.058  87.999  1.00 20.43 ? 831  ASP A OD1   1 
ATOM   6113  O  OD2   . ASP A  1  833  ? -24.326 69.422  86.937  1.00 19.20 ? 831  ASP A OD2   1 
ATOM   6114  N  N     . VAL A  1  834  ? -25.208 74.891  86.597  1.00 16.57 ? 832  VAL A N     1 
ATOM   6115  C  CA    . VAL A  1  834  ? -24.749 76.276  86.661  1.00 17.07 ? 832  VAL A CA    1 
ATOM   6116  C  C     . VAL A  1  834  ? -25.802 77.164  87.325  1.00 17.57 ? 832  VAL A C     1 
ATOM   6117  O  O     . VAL A  1  834  ? -25.496 77.958  88.224  1.00 17.38 ? 832  VAL A O     1 
ATOM   6118  C  CB    . VAL A  1  834  ? -24.413 76.769  85.242  1.00 16.94 ? 832  VAL A CB    1 
ATOM   6119  C  CG1   . VAL A  1  834  ? -24.240 78.262  85.221  1.00 18.36 ? 832  VAL A CG1   1 
ATOM   6120  C  CG2   . VAL A  1  834  ? -23.152 76.067  84.731  1.00 18.22 ? 832  VAL A CG2   1 
ATOM   6121  N  N     . ILE A  1  835  ? -27.064 77.031  86.902  1.00 15.94 ? 833  ILE A N     1 
ATOM   6122  C  CA    . ILE A  1  835  ? -28.137 77.829  87.492  1.00 16.56 ? 833  ILE A CA    1 
ATOM   6123  C  C     . ILE A  1  835  ? -28.215 77.576  88.993  1.00 18.28 ? 833  ILE A C     1 
ATOM   6124  O  O     . ILE A  1  835  ? -28.322 78.514  89.797  1.00 18.36 ? 833  ILE A O     1 
ATOM   6125  C  CB    . ILE A  1  835  ? -29.480 77.533  86.789  1.00 18.06 ? 833  ILE A CB    1 
ATOM   6126  C  CG1   . ILE A  1  835  ? -29.483 78.065  85.351  1.00 19.55 ? 833  ILE A CG1   1 
ATOM   6127  C  CG2   . ILE A  1  835  ? -30.643 78.159  87.549  1.00 21.15 ? 833  ILE A CG2   1 
ATOM   6128  C  CD1   . ILE A  1  835  ? -29.565 79.575  85.270  1.00 22.51 ? 833  ILE A CD1   1 
ATOM   6129  N  N     . THR A  1  836  ? -28.118 76.314  89.395  1.00 16.56 ? 834  THR A N     1 
ATOM   6130  C  CA    . THR A  1  836  ? -28.129 75.996  90.820  1.00 16.73 ? 834  THR A CA    1 
ATOM   6131  C  C     . THR A  1  836  ? -26.880 76.537  91.513  1.00 17.38 ? 834  THR A C     1 
ATOM   6132  O  O     . THR A  1  836  ? -26.974 77.228  92.531  1.00 20.00 ? 834  THR A O     1 
ATOM   6133  C  CB    . THR A  1  836  ? -28.234 74.484  91.003  1.00 21.77 ? 834  THR A CB    1 
ATOM   6134  O  OG1   . THR A  1  836  ? -29.495 74.048  90.485  1.00 24.07 ? 834  THR A OG1   1 
ATOM   6135  C  CG2   . THR A  1  836  ? -28.150 74.109  92.462  1.00 21.53 ? 834  THR A CG2   1 
ATOM   6136  N  N     . SER A  1  837  ? -25.701 76.264  90.955  1.00 17.23 ? 835  SER A N     1 
ATOM   6137  C  CA    . SER A  1  837  ? -24.468 76.649  91.641  1.00 16.72 ? 835  SER A CA    1 
ATOM   6138  C  C     . SER A  1  837  ? -24.333 78.155  91.763  1.00 18.17 ? 835  SER A C     1 
ATOM   6139  O  O     . SER A  1  837  ? -23.786 78.650  92.750  1.00 17.86 ? 835  SER A O     1 
ATOM   6140  C  CB    . SER A  1  837  ? -23.251 76.091  90.917  1.00 16.26 ? 835  SER A CB    1 
ATOM   6141  O  OG    . SER A  1  837  ? -23.296 74.671  90.910  1.00 18.60 ? 835  SER A OG    1 
ATOM   6142  N  N     . ALA A  1  838  ? -24.776 78.902  90.754  1.00 17.42 ? 836  ALA A N     1 
ATOM   6143  C  CA    . ALA A  1  838  ? -24.542 80.338  90.766  1.00 17.99 ? 836  ALA A CA    1 
ATOM   6144  C  C     . ALA A  1  838  ? -25.610 81.090  91.549  1.00 17.99 ? 836  ALA A C     1 
ATOM   6145  O  O     . ALA A  1  838  ? -25.306 82.108  92.177  1.00 19.12 ? 836  ALA A O     1 
ATOM   6146  C  CB    . ALA A  1  838  ? -24.478 80.876  89.329  1.00 17.32 ? 836  ALA A CB    1 
ATOM   6147  N  N     . PHE A  1  839  ? -26.864 80.646  91.486  1.00 18.61 ? 837  PHE A N     1 
ATOM   6148  C  CA    . PHE A  1  839  ? -27.964 81.474  91.959  1.00 17.65 ? 837  PHE A CA    1 
ATOM   6149  C  C     . PHE A  1  839  ? -28.731 80.892  93.128  1.00 18.41 ? 837  PHE A C     1 
ATOM   6150  O  O     . PHE A  1  839  ? -29.539 81.614  93.727  1.00 18.86 ? 837  PHE A O     1 
ATOM   6151  C  CB    . PHE A  1  839  ? -28.930 81.779  90.806  1.00 16.28 ? 837  PHE A CB    1 
ATOM   6152  C  CG    . PHE A  1  839  ? -28.237 82.367  89.613  1.00 16.27 ? 837  PHE A CG    1 
ATOM   6153  C  CD1   . PHE A  1  839  ? -27.478 83.520  89.736  1.00 18.95 ? 837  PHE A CD1   1 
ATOM   6154  C  CD2   . PHE A  1  839  ? -28.318 81.746  88.375  1.00 18.09 ? 837  PHE A CD2   1 
ATOM   6155  C  CE1   . PHE A  1  839  ? -26.826 84.061  88.643  1.00 19.50 ? 837  PHE A CE1   1 
ATOM   6156  C  CE2   . PHE A  1  839  ? -27.651 82.279  87.275  1.00 19.73 ? 837  PHE A CE2   1 
ATOM   6157  C  CZ    . PHE A  1  839  ? -26.902 83.433  87.409  1.00 18.96 ? 837  PHE A CZ    1 
ATOM   6158  N  N     . ASP A  1  840  ? -28.499 79.631  93.489  1.00 17.40 ? 838  ASP A N     1 
ATOM   6159  C  CA    . ASP A  1  840  ? -29.083 79.100  94.706  1.00 17.38 ? 838  ASP A CA    1 
ATOM   6160  C  C     . ASP A  1  840  ? -28.681 79.989  95.873  1.00 17.66 ? 838  ASP A C     1 
ATOM   6161  O  O     . ASP A  1  840  ? -27.541 80.456  95.941  1.00 19.46 ? 838  ASP A O     1 
ATOM   6162  C  CB    . ASP A  1  840  ? -28.597 77.667  94.930  1.00 20.50 ? 838  ASP A CB    1 
ATOM   6163  C  CG    . ASP A  1  840  ? -29.135 77.054  96.187  1.00 23.04 ? 838  ASP A CG    1 
ATOM   6164  O  OD1   . ASP A  1  840  ? -28.646 77.419  97.274  1.00 24.18 ? 838  ASP A OD1   1 
ATOM   6165  O  OD2   . ASP A  1  840  ? -30.046 76.205  96.082  1.00 28.32 ? 838  ASP A OD2   1 
ATOM   6166  N  N     . SER A  1  841  ? -29.631 80.242  96.777  1.00 19.68 ? 839  SER A N     1 
ATOM   6167  C  CA    . SER A  1  841  ? -29.391 81.106  97.935  1.00 18.20 ? 839  SER A CA    1 
ATOM   6168  C  C     . SER A  1  841  ? -28.910 82.488  97.509  1.00 19.52 ? 839  SER A C     1 
ATOM   6169  O  O     . SER A  1  841  ? -28.163 83.154  98.232  1.00 20.85 ? 839  SER A O     1 
ATOM   6170  C  CB    . SER A  1  841  ? -28.396 80.456  98.901  1.00 21.31 ? 839  SER A CB    1 
ATOM   6171  O  OG    . SER A  1  841  ? -28.859 79.170  99.285  1.00 24.15 ? 839  SER A OG    1 
ATOM   6172  N  N     . ALA A  1  842  ? -29.333 82.920  96.322  1.00 19.39 ? 840  ALA A N     1 
ATOM   6173  C  CA    . ALA A  1  842  ? -28.928 84.203  95.748  1.00 15.75 ? 840  ALA A CA    1 
ATOM   6174  C  C     . ALA A  1  842  ? -27.408 84.322  95.666  1.00 18.67 ? 840  ALA A C     1 
ATOM   6175  O  O     . ALA A  1  842  ? -26.838 85.395  95.849  1.00 20.33 ? 840  ALA A O     1 
ATOM   6176  C  CB    . ALA A  1  842  ? -29.535 85.380  96.526  1.00 20.98 ? 840  ALA A CB    1 
ATOM   6177  N  N     . GLY A  1  843  ? -26.739 83.206  95.375  1.00 19.04 ? 841  GLY A N     1 
ATOM   6178  C  CA    . GLY A  1  843  ? -25.293 83.203  95.277  1.00 18.04 ? 841  GLY A CA    1 
ATOM   6179  C  C     . GLY A  1  843  ? -24.577 83.459  96.579  1.00 19.59 ? 841  GLY A C     1 
ATOM   6180  O  O     . GLY A  1  843  ? -23.374 83.736  96.573  1.00 20.61 ? 841  GLY A O     1 
ATOM   6181  N  N     . GLN A  1  844  ? -25.285 83.390  97.701  1.00 18.92 ? 842  GLN A N     1 
ATOM   6182  C  CA    . GLN A  1  844  ? -24.682 83.648  99.004  1.00 18.89 ? 842  GLN A CA    1 
ATOM   6183  C  C     . GLN A  1  844  ? -24.234 82.361  99.673  1.00 25.07 ? 842  GLN A C     1 
ATOM   6184  O  O     . GLN A  1  844  ? -24.557 82.069  100.822 1.00 26.64 ? 842  GLN A O     1 
ATOM   6185  C  CB    . GLN A  1  844  ? -25.663 84.413  99.876  1.00 19.34 ? 842  GLN A CB    1 
ATOM   6186  C  CG    . GLN A  1  844  ? -25.999 85.774  99.313  1.00 19.57 ? 842  GLN A CG    1 
ATOM   6187  C  CD    . GLN A  1  844  ? -27.120 86.445  100.091 1.00 24.58 ? 842  GLN A CD    1 
ATOM   6188  O  OE1   . GLN A  1  844  ? -27.032 87.616  100.435 1.00 20.45 ? 842  GLN A OE1   1 
ATOM   6189  N  NE2   . GLN A  1  844  ? -28.171 85.693  100.386 1.00 33.31 ? 842  GLN A NE2   1 
ATOM   6190  N  N     . ARG A  1  845  ? -23.528 81.550  98.904  1.00 19.82 ? 843  ARG A N     1 
ATOM   6191  C  CA    . ARG A  1  845  ? -22.777 80.423  99.414  1.00 18.75 ? 843  ARG A CA    1 
ATOM   6192  C  C     . ARG A  1  845  ? -21.313 80.703  99.157  1.00 19.66 ? 843  ARG A C     1 
ATOM   6193  O  O     . ARG A  1  845  ? -20.961 81.253  98.115  1.00 20.37 ? 843  ARG A O     1 
ATOM   6194  C  CB    . ARG A  1  845  ? -23.171 79.133  98.701  1.00 19.81 ? 843  ARG A CB    1 
ATOM   6195  C  CG    . ARG A  1  845  ? -24.598 78.711  98.935  1.00 19.62 ? 843  ARG A CG    1 
ATOM   6196  C  CD    . ARG A  1  845  ? -24.814 77.383  98.247  1.00 22.71 ? 843  ARG A CD    1 
ATOM   6197  N  NE    . ARG A  1  845  ? -26.175 76.904  98.397  1.00 27.92 ? 843  ARG A NE    1 
ATOM   6198  C  CZ    . ARG A  1  845  ? -26.533 75.910  99.195  1.00 24.30 ? 843  ARG A CZ    1 
ATOM   6199  N  NH1   . ARG A  1  845  ? -25.647 75.266  99.948  1.00 24.76 ? 843  ARG A NH1   1 
ATOM   6200  N  NH2   . ARG A  1  845  ? -27.806 75.533  99.221  1.00 25.94 ? 843  ARG A NH2   1 
ATOM   6201  N  N     . CYS A  1  846  ? -20.448 80.304  100.089 1.00 20.30 ? 844  CYS A N     1 
ATOM   6202  C  CA    . CYS A  1  846  ? -19.028 80.452  99.814  1.00 21.50 ? 844  CYS A CA    1 
ATOM   6203  C  C     . CYS A  1  846  ? -18.624 79.614  98.614  1.00 16.63 ? 844  CYS A C     1 
ATOM   6204  O  O     . CYS A  1  846  ? -17.695 79.974  97.892  1.00 18.74 ? 844  CYS A O     1 
ATOM   6205  C  CB    . CYS A  1  846  ? -18.217 80.023  101.022 1.00 22.62 ? 844  CYS A CB    1 
ATOM   6206  S  SG    . CYS A  1  846  ? -18.801 78.447  101.663 1.00 32.48 ? 844  CYS A SG    1 
ATOM   6207  N  N     . SER A  1  847  ? -19.345 78.521  98.386  1.00 19.65 ? 845  SER A N     1 
ATOM   6208  C  CA    . SER A  1  847  ? -19.110 77.555  97.324  1.00 18.49 ? 845  SER A CA    1 
ATOM   6209  C  C     . SER A  1  847  ? -19.699 77.968  95.987  1.00 18.94 ? 845  SER A C     1 
ATOM   6210  O  O     . SER A  1  847  ? -19.508 77.243  95.010  1.00 18.20 ? 845  SER A O     1 
ATOM   6211  C  CB    . SER A  1  847  ? -19.727 76.220  97.729  1.00 19.57 ? 845  SER A CB    1 
ATOM   6212  O  OG    . SER A  1  847  ? -21.088 76.438  98.072  1.00 22.60 ? 845  SER A OG    1 
ATOM   6213  N  N     . ALA A  1  848  ? -20.437 79.074  95.933  1.00 18.38 ? 846  ALA A N     1 
ATOM   6214  C  CA    . ALA A  1  848  ? -21.210 79.408  94.739  1.00 16.82 ? 846  ALA A CA    1 
ATOM   6215  C  C     . ALA A  1  848  ? -20.318 79.565  93.516  1.00 17.78 ? 846  ALA A C     1 
ATOM   6216  O  O     . ALA A  1  848  ? -19.175 80.015  93.593  1.00 17.83 ? 846  ALA A O     1 
ATOM   6217  C  CB    . ALA A  1  848  ? -21.995 80.706  94.970  1.00 15.98 ? 846  ALA A CB    1 
ATOM   6218  N  N     . LEU A  1  849  ? -20.875 79.202  92.363  1.00 15.84 ? 847  LEU A N     1 
ATOM   6219  C  CA    . LEU A  1  849  ? -20.181 79.366  91.098  1.00 15.92 ? 847  LEU A CA    1 
ATOM   6220  C  C     . LEU A  1  849  ? -20.106 80.840  90.726  1.00 18.48 ? 847  LEU A C     1 
ATOM   6221  O  O     . LEU A  1  849  ? -21.138 81.512  90.597  1.00 18.09 ? 847  LEU A O     1 
ATOM   6222  C  CB    . LEU A  1  849  ? -20.913 78.589  90.019  1.00 13.87 ? 847  LEU A CB    1 
ATOM   6223  C  CG    . LEU A  1  849  ? -20.342 78.757  88.618  1.00 16.88 ? 847  LEU A CG    1 
ATOM   6224  C  CD1   . LEU A  1  849  ? -18.903 78.295  88.563  1.00 17.60 ? 847  LEU A CD1   1 
ATOM   6225  C  CD2   . LEU A  1  849  ? -21.218 77.985  87.638  1.00 16.58 ? 847  LEU A CD2   1 
ATOM   6226  N  N     . ARG A  1  850  ? -18.884 81.344  90.576  1.00 16.85 ? 848  ARG A N     1 
ATOM   6227  C  CA    . ARG A  1  850  ? -18.659 82.732  90.214  1.00 18.51 ? 848  ARG A CA    1 
ATOM   6228  C  C     . ARG A  1  850  ? -18.222 82.911  88.778  1.00 17.18 ? 848  ARG A C     1 
ATOM   6229  O  O     . ARG A  1  850  ? -18.522 83.944  88.181  1.00 18.64 ? 848  ARG A O     1 
ATOM   6230  C  CB    . ARG A  1  850  ? -17.593 83.362  91.121  1.00 18.83 ? 848  ARG A CB    1 
ATOM   6231  C  CG    . ARG A  1  850  ? -17.842 83.134  92.594  1.00 20.10 ? 848  ARG A CG    1 
ATOM   6232  C  CD    . ARG A  1  850  ? -19.223 83.618  92.994  1.00 19.30 ? 848  ARG A CD    1 
ATOM   6233  N  NE    . ARG A  1  850  ? -19.389 83.566  94.438  1.00 21.02 ? 848  ARG A NE    1 
ATOM   6234  C  CZ    . ARG A  1  850  ? -20.512 83.874  95.072  1.00 21.48 ? 848  ARG A CZ    1 
ATOM   6235  N  NH1   . ARG A  1  850  ? -21.610 84.209  94.407  1.00 19.87 ? 848  ARG A NH1   1 
ATOM   6236  N  NH2   . ARG A  1  850  ? -20.529 83.859  96.403  1.00 21.06 ? 848  ARG A NH2   1 
ATOM   6237  N  N     . VAL A  1  851  ? -17.485 81.950  88.224  1.00 17.27 ? 849  VAL A N     1 
ATOM   6238  C  CA    . VAL A  1  851  ? -16.912 82.085  86.890  1.00 16.62 ? 849  VAL A CA    1 
ATOM   6239  C  C     . VAL A  1  851  ? -17.154 80.793  86.136  1.00 17.10 ? 849  VAL A C     1 
ATOM   6240  O  O     . VAL A  1  851  ? -16.570 79.756  86.479  1.00 18.50 ? 849  VAL A O     1 
ATOM   6241  C  CB    . VAL A  1  851  ? -15.411 82.382  86.910  1.00 22.87 ? 849  VAL A CB    1 
ATOM   6242  C  CG1   . VAL A  1  851  ? -14.962 82.632  85.468  1.00 23.58 ? 849  VAL A CG1   1 
ATOM   6243  C  CG2   . VAL A  1  851  ? -15.093 83.566  87.796  1.00 28.22 ? 849  VAL A CG2   1 
ATOM   6244  N  N     . LEU A  1  852  ? -17.995 80.852  85.108  1.00 16.46 ? 850  LEU A N     1 
ATOM   6245  C  CA    . LEU A  1  852  ? -18.236 79.724  84.221  1.00 18.32 ? 850  LEU A CA    1 
ATOM   6246  C  C     . LEU A  1  852  ? -17.326 79.864  83.010  1.00 17.41 ? 850  LEU A C     1 
ATOM   6247  O  O     . LEU A  1  852  ? -17.298 80.921  82.378  1.00 17.45 ? 850  LEU A O     1 
ATOM   6248  C  CB    . LEU A  1  852  ? -19.701 79.695  83.783  1.00 16.21 ? 850  LEU A CB    1 
ATOM   6249  C  CG    . LEU A  1  852  ? -20.085 78.612  82.770  1.00 17.60 ? 850  LEU A CG    1 
ATOM   6250  C  CD1   . LEU A  1  852  ? -19.915 77.210  83.368  1.00 17.84 ? 850  LEU A CD1   1 
ATOM   6251  C  CD2   . LEU A  1  852  ? -21.536 78.842  82.306  1.00 19.17 ? 850  LEU A CD2   1 
ATOM   6252  N  N     . CYS A  1  853  ? -16.592 78.799  82.685  1.00 17.92 ? 851  CYS A N     1 
ATOM   6253  C  CA    . CYS A  1  853  ? -15.630 78.819  81.588  1.00 17.43 ? 851  CYS A CA    1 
ATOM   6254  C  C     . CYS A  1  853  ? -16.101 77.830  80.533  1.00 18.05 ? 851  CYS A C     1 
ATOM   6255  O  O     . CYS A  1  853  ? -16.126 76.625  80.781  1.00 19.45 ? 851  CYS A O     1 
ATOM   6256  C  CB    . CYS A  1  853  ? -14.226 78.464  82.067  1.00 18.65 ? 851  CYS A CB    1 
ATOM   6257  S  SG    . CYS A  1  853  ? -13.695 79.359  83.529  1.00 21.04 ? 851  CYS A SG    1 
ATOM   6258  N  N     . LEU A  1  854  ? -16.472 78.343  79.364  1.00 18.17 ? 852  LEU A N     1 
ATOM   6259  C  CA    . LEU A  1  854  ? -17.088 77.554  78.310  1.00 17.50 ? 852  LEU A CA    1 
ATOM   6260  C  C     . LEU A  1  854  ? -16.115 77.404  77.156  1.00 17.96 ? 852  LEU A C     1 
ATOM   6261  O  O     . LEU A  1  854  ? -15.586 78.400  76.655  1.00 18.26 ? 852  LEU A O     1 
ATOM   6262  C  CB    . LEU A  1  854  ? -18.363 78.228  77.808  1.00 18.66 ? 852  LEU A CB    1 
ATOM   6263  C  CG    . LEU A  1  854  ? -19.435 78.429  78.882  1.00 19.31 ? 852  LEU A CG    1 
ATOM   6264  C  CD1   . LEU A  1  854  ? -20.633 79.203  78.304  1.00 18.46 ? 852  LEU A CD1   1 
ATOM   6265  C  CD2   . LEU A  1  854  ? -19.906 77.087  79.430  1.00 19.29 ? 852  LEU A CD2   1 
ATOM   6266  N  N     . GLN A  1  855  ? -15.889 76.166  76.738  1.00 18.04 ? 853  GLN A N     1 
ATOM   6267  C  CA    . GLN A  1  855  ? -15.096 75.958  75.538  1.00 16.73 ? 853  GLN A CA    1 
ATOM   6268  C  C     . GLN A  1  855  ? -15.768 76.654  74.356  1.00 20.23 ? 853  GLN A C     1 
ATOM   6269  O  O     . GLN A  1  855  ? -16.989 76.590  74.186  1.00 20.72 ? 853  GLN A O     1 
ATOM   6270  C  CB    . GLN A  1  855  ? -14.919 74.472  75.269  1.00 18.61 ? 853  GLN A CB    1 
ATOM   6271  C  CG    . GLN A  1  855  ? -13.832 74.231  74.239  1.00 19.44 ? 853  GLN A CG    1 
ATOM   6272  C  CD    . GLN A  1  855  ? -13.788 72.798  73.781  1.00 23.39 ? 853  GLN A CD    1 
ATOM   6273  O  OE1   . GLN A  1  855  ? -13.867 71.871  74.591  1.00 23.79 ? 853  GLN A OE1   1 
ATOM   6274  N  NE2   . GLN A  1  855  ? -13.674 72.604  72.466  1.00 25.75 ? 853  GLN A NE2   1 
ATOM   6275  N  N     . GLU A  1  856  ? -14.950 77.319  73.540  1.00 19.60 ? 854  GLU A N     1 
ATOM   6276  C  CA    . GLU A  1  856  ? -15.474 78.263  72.551  1.00 20.97 ? 854  GLU A CA    1 
ATOM   6277  C  C     . GLU A  1  856  ? -16.507 77.623  71.627  1.00 26.58 ? 854  GLU A C     1 
ATOM   6278  O  O     . GLU A  1  856  ? -17.529 78.245  71.309  1.00 24.03 ? 854  GLU A O     1 
ATOM   6279  C  CB    . GLU A  1  856  ? -14.317 78.854  71.748  1.00 23.05 ? 854  GLU A CB    1 
ATOM   6280  C  CG    . GLU A  1  856  ? -14.765 79.752  70.595  1.00 28.80 ? 854  GLU A CG    1 
ATOM   6281  C  CD    . GLU A  1  856  ? -15.521 80.987  71.060  1.00 35.12 ? 854  GLU A CD    1 
ATOM   6282  O  OE1   . GLU A  1  856  ? -15.198 81.518  72.142  1.00 29.57 ? 854  GLU A OE1   1 
ATOM   6283  O  OE2   . GLU A  1  856  ? -16.441 81.427  70.341  1.00 33.97 ? 854  GLU A OE2   1 
ATOM   6284  N  N     . ASP A  1  857  ? -16.278 76.373  71.211  1.00 24.96 ? 855  ASP A N     1 
ATOM   6285  C  CA    . ASP A  1  857  ? -17.145 75.727  70.227  1.00 25.99 ? 855  ASP A CA    1 
ATOM   6286  C  C     . ASP A  1  857  ? -18.563 75.490  70.732  1.00 27.60 ? 855  ASP A C     1 
ATOM   6287  O  O     . ASP A  1  857  ? -19.480 75.352  69.915  1.00 31.37 ? 855  ASP A O     1 
ATOM   6288  C  CB    . ASP A  1  857  ? -16.535 74.395  69.781  1.00 30.26 ? 855  ASP A CB    1 
ATOM   6289  N  N     . VAL A  1  858  ? -18.771 75.415  72.044  1.00 21.10 ? 856  VAL A N     1 
ATOM   6290  C  CA    . VAL A  1  858  ? -20.105 75.215  72.593  1.00 22.80 ? 856  VAL A CA    1 
ATOM   6291  C  C     . VAL A  1  858  ? -20.600 76.419  73.367  1.00 20.48 ? 856  VAL A C     1 
ATOM   6292  O  O     . VAL A  1  858  ? -21.702 76.362  73.928  1.00 21.57 ? 856  VAL A O     1 
ATOM   6293  C  CB    . VAL A  1  858  ? -20.163 73.958  73.477  1.00 20.78 ? 856  VAL A CB    1 
ATOM   6294  C  CG1   . VAL A  1  858  ? -19.959 72.711  72.620  1.00 26.04 ? 856  VAL A CG1   1 
ATOM   6295  C  CG2   . VAL A  1  858  ? -19.104 74.032  74.593  1.00 19.87 ? 856  VAL A CG2   1 
ATOM   6296  N  N     . ALA A  1  859  ? -19.826 77.505  73.419  1.00 19.92 ? 857  ALA A N     1 
ATOM   6297  C  CA    . ALA A  1  859  ? -20.137 78.590  74.344  1.00 19.74 ? 857  ALA A CA    1 
ATOM   6298  C  C     . ALA A  1  859  ? -21.427 79.304  73.964  1.00 21.52 ? 857  ALA A C     1 
ATOM   6299  O  O     . ALA A  1  859  ? -22.228 79.643  74.839  1.00 20.79 ? 857  ALA A O     1 
ATOM   6300  C  CB    . ALA A  1  859  ? -18.987 79.589  74.400  1.00 20.23 ? 857  ALA A CB    1 
ATOM   6301  N  N     . ASP A  1  860  ? -21.645 79.565  72.674  1.00 22.32 ? 858  ASP A N     1 
ATOM   6302  C  CA    . ASP A  1  860  ? -22.856 80.284  72.302  1.00 25.27 ? 858  ASP A CA    1 
ATOM   6303  C  C     . ASP A  1  860  ? -24.104 79.461  72.597  1.00 21.93 ? 858  ASP A C     1 
ATOM   6304  O  O     . ASP A  1  860  ? -25.091 79.997  73.112  1.00 23.35 ? 858  ASP A O     1 
ATOM   6305  C  CB    . ASP A  1  860  ? -22.800 80.695  70.829  1.00 25.46 ? 858  ASP A CB    1 
ATOM   6306  C  CG    . ASP A  1  860  ? -21.778 81.780  70.570  1.00 30.41 ? 858  ASP A CG    1 
ATOM   6307  O  OD1   . ASP A  1  860  ? -21.574 82.635  71.459  1.00 39.27 ? 858  ASP A OD1   1 
ATOM   6308  O  OD2   . ASP A  1  860  ? -21.180 81.778  69.479  1.00 41.92 ? 858  ASP A OD2   1 
ATOM   6309  N  N     . ARG A  1  861  ? -24.085 78.159  72.295  1.00 20.73 ? 859  ARG A N     1 
ATOM   6310  C  CA    . ARG A  1  861  ? -25.255 77.332  72.551  1.00 22.05 ? 859  ARG A CA    1 
ATOM   6311  C  C     . ARG A  1  861  ? -25.562 77.254  74.041  1.00 18.73 ? 859  ARG A C     1 
ATOM   6312  O  O     . ARG A  1  861  ? -26.715 77.394  74.459  1.00 22.53 ? 859  ARG A O     1 
ATOM   6313  C  CB    . ARG A  1  861  ? -25.060 75.927  71.982  1.00 28.46 ? 859  ARG A CB    1 
ATOM   6314  C  CG    . ARG A  1  861  ? -26.224 75.008  72.303  1.00 34.17 ? 859  ARG A CG    1 
ATOM   6315  C  CD    . ARG A  1  861  ? -26.228 73.758  71.450  1.00 48.38 ? 859  ARG A CD    1 
ATOM   6316  N  NE    . ARG A  1  861  ? -27.338 72.893  71.831  1.00 60.70 ? 859  ARG A NE    1 
ATOM   6317  C  CZ    . ARG A  1  861  ? -27.242 71.886  72.687  1.00 51.74 ? 859  ARG A CZ    1 
ATOM   6318  N  NH1   . ARG A  1  861  ? -26.083 71.553  73.232  1.00 55.35 ? 859  ARG A NH1   1 
ATOM   6319  N  NH2   . ARG A  1  861  ? -28.333 71.194  73.001  1.00 48.84 ? 859  ARG A NH2   1 
ATOM   6320  N  N     . ILE A  1  862  ? -24.534 77.034  74.864  1.00 18.90 ? 860  ILE A N     1 
ATOM   6321  C  CA    . ILE A  1  862  ? -24.754 76.926  76.305  1.00 19.71 ? 860  ILE A CA    1 
ATOM   6322  C  C     . ILE A  1  862  ? -25.184 78.266  76.890  1.00 19.05 ? 860  ILE A C     1 
ATOM   6323  O  O     . ILE A  1  862  ? -26.088 78.331  77.734  1.00 20.08 ? 860  ILE A O     1 
ATOM   6324  C  CB    . ILE A  1  862  ? -23.483 76.379  76.978  1.00 19.74 ? 860  ILE A CB    1 
ATOM   6325  C  CG1   . ILE A  1  862  ? -23.361 74.891  76.634  1.00 21.96 ? 860  ILE A CG1   1 
ATOM   6326  C  CG2   . ILE A  1  862  ? -23.554 76.563  78.487  1.00 20.92 ? 860  ILE A CG2   1 
ATOM   6327  C  CD1   . ILE A  1  862  ? -22.031 74.272  77.029  1.00 26.20 ? 860  ILE A CD1   1 
ATOM   6328  N  N     . LEU A  1  863  ? -24.553 79.352  76.453  1.00 19.73 ? 861  LEU A N     1 
ATOM   6329  C  CA    A LEU A  1  863  ? -24.935 80.669  76.949  0.60 20.22 ? 861  LEU A CA    1 
ATOM   6330  C  CA    B LEU A  1  863  ? -24.935 80.674  76.946  0.40 20.24 ? 861  LEU A CA    1 
ATOM   6331  C  C     . LEU A  1  863  ? -26.387 80.988  76.616  1.00 19.08 ? 861  LEU A C     1 
ATOM   6332  O  O     . LEU A  1  863  ? -27.121 81.510  77.459  1.00 18.30 ? 861  LEU A O     1 
ATOM   6333  C  CB    A LEU A  1  863  ? -23.998 81.721  76.371  0.60 22.18 ? 861  LEU A CB    1 
ATOM   6334  C  CB    B LEU A  1  863  ? -24.010 81.744  76.369  0.40 22.19 ? 861  LEU A CB    1 
ATOM   6335  C  CG    A LEU A  1  863  ? -24.063 83.099  77.003  0.60 21.52 ? 861  LEU A CG    1 
ATOM   6336  C  CG    B LEU A  1  863  ? -23.034 82.407  77.342  0.40 23.14 ? 861  LEU A CG    1 
ATOM   6337  C  CD1   A LEU A  1  863  ? -23.865 83.008  78.516  0.60 23.65 ? 861  LEU A CD1   1 
ATOM   6338  C  CD1   B LEU A  1  863  ? -22.149 83.398  76.612  0.40 26.04 ? 861  LEU A CD1   1 
ATOM   6339  C  CD2   A LEU A  1  863  ? -23.003 83.967  76.358  0.60 25.80 ? 861  LEU A CD2   1 
ATOM   6340  C  CD2   B LEU A  1  863  ? -23.790 83.080  78.485  0.40 23.67 ? 861  LEU A CD2   1 
ATOM   6341  N  N     . THR A  1  864  ? -26.821 80.688  75.387  1.00 20.82 ? 862  THR A N     1 
ATOM   6342  C  CA    . THR A  1  864  ? -28.231 80.878  75.047  1.00 21.74 ? 862  THR A CA    1 
ATOM   6343  C  C     . THR A  1  864  ? -29.129 80.097  75.999  1.00 17.20 ? 862  THR A C     1 
ATOM   6344  O  O     . THR A  1  864  ? -30.119 80.622  76.522  1.00 19.41 ? 862  THR A O     1 
ATOM   6345  C  CB    . THR A  1  864  ? -28.485 80.444  73.606  1.00 21.83 ? 862  THR A CB    1 
ATOM   6346  O  OG1   . THR A  1  864  ? -27.784 81.330  72.734  1.00 22.57 ? 862  THR A OG1   1 
ATOM   6347  C  CG2   . THR A  1  864  ? -29.986 80.467  73.278  1.00 21.72 ? 862  THR A CG2   1 
ATOM   6348  N  N     . MET A  1  865  ? -28.802 78.826  76.226  1.00 17.28 ? 863  MET A N     1 
ATOM   6349  C  CA    . MET A  1  865  ? -29.609 78.020  77.128  1.00 17.36 ? 863  MET A CA    1 
ATOM   6350  C  C     . MET A  1  865  ? -29.560 78.572  78.546  1.00 17.68 ? 863  MET A C     1 
ATOM   6351  O  O     . MET A  1  865  ? -30.580 78.599  79.250  1.00 17.61 ? 863  MET A O     1 
ATOM   6352  C  CB    . MET A  1  865  ? -29.124 76.571  77.082  1.00 18.96 ? 863  MET A CB    1 
ATOM   6353  C  CG    . MET A  1  865  ? -29.994 75.583  77.845  1.00 24.70 ? 863  MET A CG    1 
ATOM   6354  S  SD    . MET A  1  865  ? -29.402 73.893  77.560  1.00 30.46 ? 863  MET A SD    1 
ATOM   6355  C  CE    . MET A  1  865  ? -28.717 74.171  75.905  1.00 17.94 ? 863  MET A CE    1 
ATOM   6356  N  N     . LEU A  1  866  ? -28.378 79.029  78.978  1.00 18.63 ? 864  LEU A N     1 
ATOM   6357  C  CA    . LEU A  1  866  ? -28.237 79.578  80.321  1.00 16.84 ? 864  LEU A CA    1 
ATOM   6358  C  C     . LEU A  1  866  ? -29.106 80.816  80.516  1.00 17.88 ? 864  LEU A C     1 
ATOM   6359  O  O     . LEU A  1  866  ? -29.757 80.972  81.557  1.00 18.67 ? 864  LEU A O     1 
ATOM   6360  C  CB    . LEU A  1  866  ? -26.770 79.911  80.571  1.00 19.30 ? 864  LEU A CB    1 
ATOM   6361  C  CG    . LEU A  1  866  ? -26.413 80.362  81.971  1.00 26.12 ? 864  LEU A CG    1 
ATOM   6362  C  CD1   . LEU A  1  866  ? -26.838 79.280  82.959  1.00 22.22 ? 864  LEU A CD1   1 
ATOM   6363  C  CD2   . LEU A  1  866  ? -24.916 80.606  82.041  1.00 23.71 ? 864  LEU A CD2   1 
ATOM   6364  N  N     . LYS A  1  867  ? -29.101 81.728  79.540  1.00 17.75 ? 865  LYS A N     1 
ATOM   6365  C  CA    . LYS A  1  867  ? -29.922 82.924  79.669  1.00 16.77 ? 865  LYS A CA    1 
ATOM   6366  C  C     . LYS A  1  867  ? -31.396 82.563  79.690  1.00 18.60 ? 865  LYS A C     1 
ATOM   6367  O  O     . LYS A  1  867  ? -32.167 83.122  80.475  1.00 18.63 ? 865  LYS A O     1 
ATOM   6368  C  CB    . LYS A  1  867  ? -29.620 83.905  78.536  1.00 18.55 ? 865  LYS A CB    1 
ATOM   6369  C  CG    . LYS A  1  867  ? -28.202 84.490  78.612  1.00 19.14 ? 865  LYS A CG    1 
ATOM   6370  C  CD    . LYS A  1  867  ? -27.855 85.273  77.350  1.00 20.98 ? 865  LYS A CD    1 
ATOM   6371  C  CE    . LYS A  1  867  ? -26.422 85.776  77.412  1.00 28.83 ? 865  LYS A CE    1 
ATOM   6372  N  NZ    . LYS A  1  867  ? -26.002 86.516  76.183  1.00 30.13 ? 865  LYS A NZ    1 
ATOM   6373  N  N     . GLY A  1  868  ? -31.800 81.601  78.857  1.00 18.84 ? 866  GLY A N     1 
ATOM   6374  C  CA    . GLY A  1  868  ? -33.185 81.178  78.868  1.00 19.62 ? 866  GLY A CA    1 
ATOM   6375  C  C     . GLY A  1  868  ? -33.584 80.568  80.197  1.00 17.24 ? 866  GLY A C     1 
ATOM   6376  O  O     . GLY A  1  868  ? -34.687 80.805  80.698  1.00 19.10 ? 866  GLY A O     1 
ATOM   6377  N  N     . ALA A  1  869  ? -32.682 79.796  80.797  1.00 16.55 ? 867  ALA A N     1 
ATOM   6378  C  CA    . ALA A  1  869  ? -32.972 79.199  82.093  1.00 15.98 ? 867  ALA A CA    1 
ATOM   6379  C  C     . ALA A  1  869  ? -33.009 80.256  83.186  1.00 17.16 ? 867  ALA A C     1 
ATOM   6380  O  O     . ALA A  1  869  ? -33.774 80.139  84.147  1.00 17.31 ? 867  ALA A O     1 
ATOM   6381  C  CB    . ALA A  1  869  ? -31.916 78.147  82.427  1.00 16.63 ? 867  ALA A CB    1 
ATOM   6382  N  N     . LEU A  1  870  ? -32.138 81.255  83.076  1.00 17.07 ? 868  LEU A N     1 
ATOM   6383  C  CA    . LEU A  1  870  ? -32.129 82.347  84.037  1.00 17.16 ? 868  LEU A CA    1 
ATOM   6384  C  C     . LEU A  1  870  ? -33.506 82.976  84.158  1.00 18.69 ? 868  LEU A C     1 
ATOM   6385  O  O     . LEU A  1  870  ? -33.964 83.288  85.263  1.00 18.47 ? 868  LEU A O     1 
ATOM   6386  C  CB    . LEU A  1  870  ? -31.101 83.393  83.592  1.00 17.45 ? 868  LEU A CB    1 
ATOM   6387  C  CG    . LEU A  1  870  ? -30.846 84.565  84.526  1.00 20.84 ? 868  LEU A CG    1 
ATOM   6388  C  CD1   . LEU A  1  870  ? -29.853 84.147  85.578  1.00 25.31 ? 868  LEU A CD1   1 
ATOM   6389  C  CD2   . LEU A  1  870  ? -30.332 85.785  83.760  1.00 23.66 ? 868  LEU A CD2   1 
ATOM   6390  N  N     . HIS A  1  871  ? -34.181 83.185  83.030  1.00 18.19 ? 869  HIS A N     1 
ATOM   6391  C  CA    . HIS A  1  871  ? -35.449 83.899  83.065  1.00 20.70 ? 869  HIS A CA    1 
ATOM   6392  C  C     . HIS A  1  871  ? -36.608 83.052  83.569  1.00 20.29 ? 869  HIS A C     1 
ATOM   6393  O  O     . HIS A  1  871  ? -37.712 83.580  83.720  1.00 23.61 ? 869  HIS A O     1 
ATOM   6394  C  CB    . HIS A  1  871  ? -35.755 84.468  81.685  1.00 21.71 ? 869  HIS A CB    1 
ATOM   6395  C  CG    . HIS A  1  871  ? -34.853 85.601  81.325  1.00 21.49 ? 869  HIS A CG    1 
ATOM   6396  N  ND1   . HIS A  1  871  ? -34.977 86.852  81.892  1.00 25.94 ? 869  HIS A ND1   1 
ATOM   6397  C  CD2   . HIS A  1  871  ? -33.765 85.657  80.523  1.00 20.25 ? 869  HIS A CD2   1 
ATOM   6398  C  CE1   . HIS A  1  871  ? -34.026 87.639  81.424  1.00 26.27 ? 869  HIS A CE1   1 
ATOM   6399  N  NE2   . HIS A  1  871  ? -33.275 86.938  80.595  1.00 22.86 ? 869  HIS A NE2   1 
ATOM   6400  N  N     . GLU A  1  872  ? -36.385 81.773  83.852  1.00 17.26 ? 870  GLU A N     1 
ATOM   6401  C  CA    . GLU A  1  872  ? -37.407 80.925  84.443  1.00 17.93 ? 870  GLU A CA    1 
ATOM   6402  C  C     . GLU A  1  872  ? -37.361 80.911  85.961  1.00 19.41 ? 870  GLU A C     1 
ATOM   6403  O  O     . GLU A  1  872  ? -38.188 80.234  86.588  1.00 20.09 ? 870  GLU A O     1 
ATOM   6404  C  CB    . GLU A  1  872  ? -37.275 79.493  83.917  1.00 18.37 ? 870  GLU A CB    1 
ATOM   6405  C  CG    . GLU A  1  872  ? -37.460 79.402  82.420  1.00 19.62 ? 870  GLU A CG    1 
ATOM   6406  C  CD    . GLU A  1  872  ? -38.853 79.817  81.985  1.00 22.22 ? 870  GLU A CD    1 
ATOM   6407  O  OE1   . GLU A  1  872  ? -39.784 79.763  82.825  1.00 23.82 ? 870  GLU A OE1   1 
ATOM   6408  O  OE2   . GLU A  1  872  ? -39.017 80.199  80.799  1.00 23.87 ? 870  GLU A OE2   1 
ATOM   6409  N  N     . LEU A  1  873  ? -36.418 81.636  86.562  1.00 18.94 ? 871  LEU A N     1 
ATOM   6410  C  CA    . LEU A  1  873  ? -36.312 81.695  88.009  1.00 19.51 ? 871  LEU A CA    1 
ATOM   6411  C  C     . LEU A  1  873  ? -37.331 82.658  88.606  1.00 18.85 ? 871  LEU A C     1 
ATOM   6412  O  O     . LEU A  1  873  ? -37.588 83.738  88.062  1.00 22.36 ? 871  LEU A O     1 
ATOM   6413  C  CB    . LEU A  1  873  ? -34.906 82.131  88.417  1.00 18.81 ? 871  LEU A CB    1 
ATOM   6414  C  CG    . LEU A  1  873  ? -33.798 81.219  87.897  1.00 18.31 ? 871  LEU A CG    1 
ATOM   6415  C  CD1   . LEU A  1  873  ? -32.418 81.827  88.249  1.00 19.19 ? 871  LEU A CD1   1 
ATOM   6416  C  CD2   . LEU A  1  873  ? -33.951 79.844  88.516  1.00 21.11 ? 871  LEU A CD2   1 
ATOM   6417  N  N     . HIS A  1  874  ? -37.888 82.262  89.748  1.00 18.79 ? 872  HIS A N     1 
ATOM   6418  C  CA    . HIS A  1  874  ? -38.845 83.071  90.488  1.00 18.87 ? 872  HIS A CA    1 
ATOM   6419  C  C     . HIS A  1  874  ? -38.111 83.657  91.686  1.00 20.11 ? 872  HIS A C     1 
ATOM   6420  O  O     . HIS A  1  874  ? -37.597 82.914  92.527  1.00 19.41 ? 872  HIS A O     1 
ATOM   6421  C  CB    . HIS A  1  874  ? -40.031 82.209  90.925  1.00 20.45 ? 872  HIS A CB    1 
ATOM   6422  C  CG    . HIS A  1  874  ? -41.075 82.939  91.718  1.00 23.29 ? 872  HIS A CG    1 
ATOM   6423  N  ND1   . HIS A  1  874  ? -42.285 82.362  92.046  1.00 28.71 ? 872  HIS A ND1   1 
ATOM   6424  C  CD2   . HIS A  1  874  ? -41.100 84.186  92.247  1.00 34.70 ? 872  HIS A CD2   1 
ATOM   6425  C  CE1   . HIS A  1  874  ? -43.005 83.220  92.747  1.00 29.37 ? 872  HIS A CE1   1 
ATOM   6426  N  NE2   . HIS A  1  874  ? -42.310 84.335  92.882  1.00 28.27 ? 872  HIS A NE2   1 
ATOM   6427  N  N     . ILE A  1  875  ? -38.054 84.980  91.754  1.00 19.94 ? 873  ILE A N     1 
ATOM   6428  C  CA    . ILE A  1  875  ? -37.361 85.685  92.823  1.00 20.49 ? 873  ILE A CA    1 
ATOM   6429  C  C     . ILE A  1  875  ? -38.413 86.346  93.698  1.00 23.63 ? 873  ILE A C     1 
ATOM   6430  O  O     . ILE A  1  875  ? -39.315 87.021  93.191  1.00 22.68 ? 873  ILE A O     1 
ATOM   6431  C  CB    . ILE A  1  875  ? -36.362 86.719  92.274  1.00 20.90 ? 873  ILE A CB    1 
ATOM   6432  C  CG1   . ILE A  1  875  ? -35.094 86.051  91.740  1.00 28.07 ? 873  ILE A CG1   1 
ATOM   6433  C  CG2   . ILE A  1  875  ? -35.917 87.662  93.373  1.00 23.41 ? 873  ILE A CG2   1 
ATOM   6434  C  CD1   . ILE A  1  875  ? -35.258 85.150  90.533  1.00 28.84 ? 873  ILE A CD1   1 
ATOM   6435  N  N     . GLY A  1  876  ? -38.302 86.161  95.007  1.00 19.40 ? 874  GLY A N     1 
ATOM   6436  C  CA    . GLY A  1  876  ? -39.232 86.813  95.906  1.00 20.55 ? 874  GLY A CA    1 
ATOM   6437  C  C     . GLY A  1  876  ? -38.999 86.392  97.342  1.00 23.78 ? 874  GLY A C     1 
ATOM   6438  O  O     . GLY A  1  876  ? -38.043 85.675  97.659  1.00 20.67 ? 874  GLY A O     1 
ATOM   6439  N  N     . ARG A  1  877  ? -39.887 86.878  98.209  1.00 22.36 ? 875  ARG A N     1 
ATOM   6440  C  CA    . ARG A  1  877  ? -39.886 86.453  99.600  1.00 23.20 ? 875  ARG A CA    1 
ATOM   6441  C  C     . ARG A  1  877  ? -40.019 84.936  99.676  1.00 22.12 ? 875  ARG A C     1 
ATOM   6442  O  O     . ARG A  1  877  ? -40.846 84.337  98.983  1.00 20.17 ? 875  ARG A O     1 
ATOM   6443  C  CB    . ARG A  1  877  ? -41.027 87.140  100.356 1.00 26.03 ? 875  ARG A CB    1 
ATOM   6444  C  CG    . ARG A  1  877  ? -40.804 87.186  101.845 1.00 26.12 ? 875  ARG A CG    1 
ATOM   6445  C  CD    . ARG A  1  877  ? -41.881 88.013  102.518 1.00 27.71 ? 875  ARG A CD    1 
ATOM   6446  N  NE    . ARG A  1  877  ? -43.107 87.256  102.705 1.00 27.57 ? 875  ARG A NE    1 
ATOM   6447  C  CZ    . ARG A  1  877  ? -44.164 87.713  103.364 1.00 36.74 ? 875  ARG A CZ    1 
ATOM   6448  N  NH1   . ARG A  1  877  ? -44.180 88.933  103.876 1.00 32.10 ? 875  ARG A NH1   1 
ATOM   6449  N  NH2   . ARG A  1  877  ? -45.226 86.925  103.516 1.00 34.28 ? 875  ARG A NH2   1 
ATOM   6450  N  N     . THR A  1  878  ? -39.199 84.311  100.517 1.00 20.33 ? 876  THR A N     1 
ATOM   6451  C  CA    . THR A  1  878  ? -38.974 82.877  100.429 1.00 22.38 ? 876  THR A CA    1 
ATOM   6452  C  C     . THR A  1  878  ? -39.995 82.045  101.196 1.00 21.12 ? 876  THR A C     1 
ATOM   6453  O  O     . THR A  1  878  ? -39.804 80.832  101.328 1.00 23.33 ? 876  THR A O     1 
ATOM   6454  C  CB    . THR A  1  878  ? -37.567 82.541  100.912 1.00 19.93 ? 876  THR A CB    1 
ATOM   6455  O  OG1   . THR A  1  878  ? -37.339 83.169  102.179 1.00 24.27 ? 876  THR A OG1   1 
ATOM   6456  C  CG2   . THR A  1  878  ? -36.549 83.062  99.924  1.00 24.06 ? 876  THR A CG2   1 
ATOM   6457  N  N     . ASP A  1  879  ? -41.072 82.643  101.691 1.00 21.60 ? 877  ASP A N     1 
ATOM   6458  C  CA    . ASP A  1  879  ? -42.104 81.848  102.343 1.00 26.15 ? 877  ASP A CA    1 
ATOM   6459  C  C     . ASP A  1  879  ? -43.133 81.306  101.350 1.00 23.99 ? 877  ASP A C     1 
ATOM   6460  O  O     . ASP A  1  879  ? -44.278 81.022  101.732 1.00 22.06 ? 877  ASP A O     1 
ATOM   6461  C  CB    . ASP A  1  879  ? -42.765 82.653  103.463 1.00 23.22 ? 877  ASP A CB    1 
ATOM   6462  C  CG    . ASP A  1  879  ? -43.546 83.848  102.951 1.00 28.54 ? 877  ASP A CG    1 
ATOM   6463  O  OD1   . ASP A  1  879  ? -43.178 84.407  101.891 1.00 30.50 ? 877  ASP A OD1   1 
ATOM   6464  O  OD2   . ASP A  1  879  ? -44.533 84.228  103.619 1.00 28.56 ? 877  ASP A OD2   1 
ATOM   6465  N  N     . ARG A  1  880  ? -42.736 81.133  100.085 1.00 22.53 ? 878  ARG A N     1 
ATOM   6466  C  CA    . ARG A  1  880  ? -43.520 80.436  99.069  1.00 20.34 ? 878  ARG A CA    1 
ATOM   6467  C  C     . ARG A  1  880  ? -42.634 79.375  98.441  1.00 19.94 ? 878  ARG A C     1 
ATOM   6468  O  O     . ARG A  1  880  ? -41.500 79.669  98.058  1.00 21.24 ? 878  ARG A O     1 
ATOM   6469  C  CB    . ARG A  1  880  ? -44.021 81.375  97.962  1.00 24.08 ? 878  ARG A CB    1 
ATOM   6470  C  CG    . ARG A  1  880  ? -45.160 82.306  98.343  1.00 29.34 ? 878  ARG A CG    1 
ATOM   6471  C  CD    . ARG A  1  880  ? -45.460 83.224  97.148  1.00 30.89 ? 878  ARG A CD    1 
ATOM   6472  N  NE    . ARG A  1  880  ? -46.871 83.568  97.015  1.00 49.47 ? 878  ARG A NE    1 
ATOM   6473  C  CZ    . ARG A  1  880  ? -47.479 84.516  97.715  1.00 49.24 ? 878  ARG A CZ    1 
ATOM   6474  N  NH1   . ARG A  1  880  ? -46.847 85.187  98.662  1.00 53.03 ? 878  ARG A NH1   1 
ATOM   6475  N  NH2   . ARG A  1  880  ? -48.756 84.794  97.460  1.00 52.40 ? 878  ARG A NH2   1 
ATOM   6476  N  N     . LEU A  1  881  ? -43.160 78.152  98.321  1.00 19.32 ? 879  LEU A N     1 
ATOM   6477  C  CA    . LEU A  1  881  ? -42.415 77.061  97.704  1.00 19.45 ? 879  LEU A CA    1 
ATOM   6478  C  C     . LEU A  1  881  ? -41.987 77.402  96.277  1.00 19.11 ? 879  LEU A C     1 
ATOM   6479  O  O     . LEU A  1  881  ? -40.941 76.932  95.807  1.00 19.86 ? 879  LEU A O     1 
ATOM   6480  C  CB    . LEU A  1  881  ? -43.272 75.801  97.717  1.00 20.79 ? 879  LEU A CB    1 
ATOM   6481  C  CG    . LEU A  1  881  ? -42.644 74.523  97.182  1.00 21.85 ? 879  LEU A CG    1 
ATOM   6482  C  CD1   . LEU A  1  881  ? -41.475 74.091  98.077  1.00 24.13 ? 879  LEU A CD1   1 
ATOM   6483  C  CD2   . LEU A  1  881  ? -43.713 73.443  97.080  1.00 21.95 ? 879  LEU A CD2   1 
ATOM   6484  N  N     . SER A  1  882  ? -42.761 78.243  95.588  1.00 18.18 ? 880  SER A N     1 
ATOM   6485  C  CA    . SER A  1  882  ? -42.450 78.548  94.198  1.00 18.60 ? 880  SER A CA    1 
ATOM   6486  C  C     . SER A  1  882  ? -41.267 79.488  94.042  1.00 20.90 ? 880  SER A C     1 
ATOM   6487  O  O     . SER A  1  882  ? -40.805 79.689  92.917  1.00 22.10 ? 880  SER A O     1 
ATOM   6488  C  CB    . SER A  1  882  ? -43.671 79.159  93.506  1.00 20.98 ? 880  SER A CB    1 
ATOM   6489  O  OG    . SER A  1  882  ? -44.066 80.347  94.166  1.00 25.62 ? 880  SER A OG    1 
ATOM   6490  N  N     . VAL A  1  883  ? -40.747 80.049  95.126  1.00 21.24 ? 881  VAL A N     1 
ATOM   6491  C  CA    . VAL A  1  883  ? -39.616 80.962  95.018  1.00 19.55 ? 881  VAL A CA    1 
ATOM   6492  C  C     . VAL A  1  883  ? -38.325 80.163  94.887  1.00 20.28 ? 881  VAL A C     1 
ATOM   6493  O  O     . VAL A  1  883  ? -38.053 79.260  95.684  1.00 22.84 ? 881  VAL A O     1 
ATOM   6494  C  CB    . VAL A  1  883  ? -39.569 81.912  96.225  1.00 21.63 ? 881  VAL A CB    1 
ATOM   6495  C  CG1   . VAL A  1  883  ? -38.217 82.632  96.268  1.00 21.75 ? 881  VAL A CG1   1 
ATOM   6496  C  CG2   . VAL A  1  883  ? -40.709 82.908  96.122  1.00 23.30 ? 881  VAL A CG2   1 
ATOM   6497  N  N     . ASP A  1  884  ? -37.543 80.482  93.858  1.00 17.95 ? 882  ASP A N     1 
ATOM   6498  C  CA    . ASP A  1  884  ? -36.246 79.857  93.627  1.00 19.03 ? 882  ASP A CA    1 
ATOM   6499  C  C     . ASP A  1  884  ? -35.107 80.618  94.272  1.00 20.83 ? 882  ASP A C     1 
ATOM   6500  O  O     . ASP A  1  884  ? -34.147 80.010  94.760  1.00 23.94 ? 882  ASP A O     1 
ATOM   6501  C  CB    . ASP A  1  884  ? -35.965 79.765  92.132  1.00 19.23 ? 882  ASP A CB    1 
ATOM   6502  C  CG    . ASP A  1  884  ? -37.015 78.987  91.420  1.00 18.90 ? 882  ASP A CG    1 
ATOM   6503  O  OD1   . ASP A  1  884  ? -37.205 77.819  91.801  1.00 22.65 ? 882  ASP A OD1   1 
ATOM   6504  O  OD2   . ASP A  1  884  ? -37.664 79.554  90.516  1.00 18.95 ? 882  ASP A OD2   1 
ATOM   6505  N  N     . VAL A  1  885  ? -35.169 81.938  94.214  1.00 19.08 ? 883  VAL A N     1 
ATOM   6506  C  CA    . VAL A  1  885  ? -34.073 82.789  94.642  1.00 20.34 ? 883  VAL A CA    1 
ATOM   6507  C  C     . VAL A  1  885  ? -34.656 83.834  95.573  1.00 18.45 ? 883  VAL A C     1 
ATOM   6508  O  O     . VAL A  1  885  ? -35.587 84.555  95.195  1.00 18.74 ? 883  VAL A O     1 
ATOM   6509  C  CB    . VAL A  1  885  ? -33.368 83.455  93.453  1.00 20.24 ? 883  VAL A CB    1 
ATOM   6510  C  CG1   . VAL A  1  885  ? -32.265 84.375  93.946  1.00 22.34 ? 883  VAL A CG1   1 
ATOM   6511  C  CG2   . VAL A  1  885  ? -32.804 82.399  92.513  1.00 21.36 ? 883  VAL A CG2   1 
ATOM   6512  N  N     . GLY A  1  886  ? -34.120 83.908  96.783  1.00 19.32 ? 884  GLY A N     1 
ATOM   6513  C  CA    . GLY A  1  886  ? -34.570 84.882  97.744  1.00 17.73 ? 884  GLY A CA    1 
ATOM   6514  C  C     . GLY A  1  886  ? -33.747 86.147  97.730  1.00 19.66 ? 884  GLY A C     1 
ATOM   6515  O  O     . GLY A  1  886  ? -33.013 86.444  96.783  1.00 19.82 ? 884  GLY A O     1 
ATOM   6516  N  N     . PRO A  1  887  ? -33.869 86.922  98.796  1.00 19.40 ? 885  PRO A N     1 
ATOM   6517  C  CA    . PRO A  1  887  ? -33.178 88.206  98.873  1.00 17.44 ? 885  PRO A CA    1 
ATOM   6518  C  C     . PRO A  1  887  ? -31.717 88.027  99.243  1.00 19.20 ? 885  PRO A C     1 
ATOM   6519  O  O     . PRO A  1  887  ? -31.282 86.978  99.720  1.00 19.87 ? 885  PRO A O     1 
ATOM   6520  C  CB    . PRO A  1  887  ? -33.935 88.927  99.990  1.00 18.64 ? 885  PRO A CB    1 
ATOM   6521  C  CG    . PRO A  1  887  ? -34.305 87.805  100.923 1.00 19.70 ? 885  PRO A CG    1 
ATOM   6522  C  CD    . PRO A  1  887  ? -34.644 86.638  100.016 1.00 22.07 ? 885  PRO A CD    1 
ATOM   6523  N  N     . VAL A  1  888  ? -30.958 89.088  99.023  1.00 22.00 ? 886  VAL A N     1 
ATOM   6524  C  CA    . VAL A  1  888  ? -29.662 89.169  99.669  1.00 19.80 ? 886  VAL A CA    1 
ATOM   6525  C  C     . VAL A  1  888  ? -29.848 89.713  101.083 1.00 19.97 ? 886  VAL A C     1 
ATOM   6526  O  O     . VAL A  1  888  ? -30.890 90.276  101.437 1.00 22.48 ? 886  VAL A O     1 
ATOM   6527  C  CB    . VAL A  1  888  ? -28.663 90.004  98.846  1.00 20.13 ? 886  VAL A CB    1 
ATOM   6528  C  CG1   . VAL A  1  888  ? -28.436 89.332  97.488  1.00 21.99 ? 886  VAL A CG1   1 
ATOM   6529  C  CG2   . VAL A  1  888  ? -29.125 91.433  98.679  1.00 22.85 ? 886  VAL A CG2   1 
ATOM   6530  N  N     . ILE A  1  889  ? -28.832 89.493  101.920 1.00 20.01 ? 887  ILE A N     1 
ATOM   6531  C  CA    . ILE A  1  889  ? -29.053 89.568  103.364 1.00 22.66 ? 887  ILE A CA    1 
ATOM   6532  C  C     . ILE A  1  889  ? -29.342 90.987  103.834 1.00 24.76 ? 887  ILE A C     1 
ATOM   6533  O  O     . ILE A  1  889  ? -30.148 91.176  104.751 1.00 23.20 ? 887  ILE A O     1 
ATOM   6534  C  CB    . ILE A  1  889  ? -27.864 88.944  104.121 1.00 21.51 ? 887  ILE A CB    1 
ATOM   6535  C  CG1   . ILE A  1  889  ? -28.181 88.822  105.617 1.00 22.75 ? 887  ILE A CG1   1 
ATOM   6536  C  CG2   . ILE A  1  889  ? -26.554 89.707  103.882 1.00 20.53 ? 887  ILE A CG2   1 
ATOM   6537  C  CD1   . ILE A  1  889  ? -29.338 87.878  105.900 1.00 22.10 ? 887  ILE A CD1   1 
ATOM   6538  N  N     . THR A  1  890  ? -28.725 92.002  103.226 1.00 19.52 ? 888  THR A N     1 
ATOM   6539  C  CA    . THR A  1  890  ? -28.872 93.376  103.700 1.00 21.29 ? 888  THR A CA    1 
ATOM   6540  C  C     . THR A  1  890  ? -28.858 94.334  102.523 1.00 19.61 ? 888  THR A C     1 
ATOM   6541  O  O     . THR A  1  890  ? -28.419 93.996  101.420 1.00 22.53 ? 888  THR A O     1 
ATOM   6542  C  CB    . THR A  1  890  ? -27.736 93.810  104.641 1.00 23.54 ? 888  THR A CB    1 
ATOM   6543  O  OG1   . THR A  1  890  ? -26.495 93.720  103.930 1.00 23.40 ? 888  THR A OG1   1 
ATOM   6544  C  CG2   . THR A  1  890  ? -27.660 92.959  105.899 1.00 25.01 ? 888  THR A CG2   1 
ATOM   6545  N  N     . SER A  1  891  ? -29.308 95.567  102.796 1.00 22.32 ? 889  SER A N     1 
ATOM   6546  C  CA    A SER A  1  891  ? -29.205 96.639  101.809 0.46 23.86 ? 889  SER A CA    1 
ATOM   6547  C  CA    B SER A  1  891  ? -29.207 96.617  101.790 0.54 23.83 ? 889  SER A CA    1 
ATOM   6548  C  C     . SER A  1  891  ? -27.756 96.910  101.435 1.00 24.32 ? 889  SER A C     1 
ATOM   6549  O  O     . SER A  1  891  ? -27.460 97.258  100.290 1.00 24.47 ? 889  SER A O     1 
ATOM   6550  C  CB    A SER A  1  891  ? -29.847 97.919  102.345 0.46 25.27 ? 889  SER A CB    1 
ATOM   6551  C  CB    B SER A  1  891  ? -29.897 97.888  102.285 0.54 25.27 ? 889  SER A CB    1 
ATOM   6552  O  OG    A SER A  1  891  ? -31.246 97.787  102.468 0.46 25.05 ? 889  SER A OG    1 
ATOM   6553  O  OG    B SER A  1  891  ? -29.203 98.426  103.393 0.54 29.25 ? 889  SER A OG    1 
ATOM   6554  N  N     . GLU A  1  892  ? -26.837 96.789  102.401 1.00 25.29 ? 890  GLU A N     1 
ATOM   6555  C  CA    . GLU A  1  892  ? -25.431 97.033  102.099 1.00 25.14 ? 890  GLU A CA    1 
ATOM   6556  C  C     . GLU A  1  892  ? -24.885 95.959  101.174 1.00 26.15 ? 890  GLU A C     1 
ATOM   6557  O  O     . GLU A  1  892  ? -24.105 96.251  100.261 1.00 25.16 ? 890  GLU A O     1 
ATOM   6558  C  CB    . GLU A  1  892  ? -24.612 97.093  103.385 1.00 28.57 ? 890  GLU A CB    1 
ATOM   6559  C  CG    . GLU A  1  892  ? -25.209 98.007  104.438 1.00 37.91 ? 890  GLU A CG    1 
ATOM   6560  C  CD    . GLU A  1  892  ? -26.141 97.267  105.385 1.00 35.58 ? 890  GLU A CD    1 
ATOM   6561  O  OE1   . GLU A  1  892  ? -25.634 96.616  106.326 1.00 57.38 ? 890  GLU A OE1   1 
ATOM   6562  O  OE2   . GLU A  1  892  ? -27.373 97.334  105.191 1.00 33.45 ? 890  GLU A OE2   1 
ATOM   6563  N  N     . ALA A  1  893  ? -25.267 94.706  101.412 1.00 23.30 ? 891  ALA A N     1 
ATOM   6564  C  CA    . ALA A  1  893  ? -24.901 93.644  100.484 1.00 22.52 ? 891  ALA A CA    1 
ATOM   6565  C  C     . ALA A  1  893  ? -25.460 93.929  99.101  1.00 25.42 ? 891  ALA A C     1 
ATOM   6566  O  O     . ALA A  1  893  ? -24.740 93.843  98.100  1.00 25.27 ? 891  ALA A O     1 
ATOM   6567  C  CB    . ALA A  1  893  ? -25.394 92.295  101.005 1.00 22.51 ? 891  ALA A CB    1 
ATOM   6568  N  N     . LYS A  1  894  ? -26.747 94.290  99.032  1.00 22.42 ? 892  LYS A N     1 
ATOM   6569  C  CA    . LYS A  1  894  ? -27.364 94.648  97.760  1.00 21.38 ? 892  LYS A CA    1 
ATOM   6570  C  C     . LYS A  1  894  ? -26.590 95.760  97.070  1.00 23.99 ? 892  LYS A C     1 
ATOM   6571  O  O     . LYS A  1  894  ? -26.272 95.663  95.882  1.00 25.77 ? 892  LYS A O     1 
ATOM   6572  C  CB    . LYS A  1  894  ? -28.822 95.059  97.976  1.00 20.30 ? 892  LYS A CB    1 
ATOM   6573  C  CG    . LYS A  1  894  ? -29.547 95.510  96.719  1.00 22.92 ? 892  LYS A CG    1 
ATOM   6574  C  CD    . LYS A  1  894  ? -30.997 95.841  97.001  1.00 26.59 ? 892  LYS A CD    1 
ATOM   6575  C  CE    . LYS A  1  894  ? -31.671 96.416  95.755  1.00 28.41 ? 892  LYS A CE    1 
ATOM   6576  N  NZ    . LYS A  1  894  ? -32.937 97.109  96.099  1.00 42.35 ? 892  LYS A NZ    1 
ATOM   6577  N  N     . ASP A  1  895  ? -26.260 96.822  97.807  1.00 24.07 ? 893  ASP A N     1 
ATOM   6578  C  CA    . ASP A  1  895  ? -25.558 97.944  97.193  1.00 28.36 ? 893  ASP A CA    1 
ATOM   6579  C  C     . ASP A  1  895  ? -24.195 97.523  96.658  1.00 23.81 ? 893  ASP A C     1 
ATOM   6580  O  O     . ASP A  1  895  ? -23.783 97.956  95.573  1.00 26.42 ? 893  ASP A O     1 
ATOM   6581  C  CB    . ASP A  1  895  ? -25.393 99.085  98.198  1.00 26.36 ? 893  ASP A CB    1 
ATOM   6582  C  CG    . ASP A  1  895  ? -26.710 99.750  98.563  1.00 37.45 ? 893  ASP A CG    1 
ATOM   6583  O  OD1   . ASP A  1  895  ? -27.694 99.631  97.797  1.00 40.99 ? 893  ASP A OD1   1 
ATOM   6584  O  OD2   . ASP A  1  895  ? -26.748 100.408 99.627  1.00 40.29 ? 893  ASP A OD2   1 
ATOM   6585  N  N     . ASN A  1  896  ? -23.475 96.692  97.413  1.00 24.42 ? 894  ASN A N     1 
ATOM   6586  C  CA    . ASN A  1  896  ? -22.146 96.275  96.989  1.00 24.03 ? 894  ASN A CA    1 
ATOM   6587  C  C     . ASN A  1  896  ? -22.214 95.449  95.715  1.00 26.24 ? 894  ASN A C     1 
ATOM   6588  O  O     . ASN A  1  896  ? -21.427 95.662  94.785  1.00 26.52 ? 894  ASN A O     1 
ATOM   6589  C  CB    . ASN A  1  896  ? -21.465 95.488  98.106  1.00 30.59 ? 894  ASN A CB    1 
ATOM   6590  C  CG    . ASN A  1  896  ? -20.103 94.955  97.696  1.00 41.28 ? 894  ASN A CG    1 
ATOM   6591  O  OD1   . ASN A  1  896  ? -19.970 93.799  97.290  1.00 44.74 ? 894  ASN A OD1   1 
ATOM   6592  N  ND2   . ASN A  1  896  ? -19.086 95.803  97.789  1.00 44.72 ? 894  ASN A ND2   1 
ATOM   6593  N  N     . ILE A  1  897  ? -23.158 94.508  95.656  1.00 23.69 ? 895  ILE A N     1 
ATOM   6594  C  CA    . ILE A  1  897  ? -23.309 93.670  94.469  1.00 22.99 ? 895  ILE A CA    1 
ATOM   6595  C  C     . ILE A  1  897  ? -23.699 94.521  93.269  1.00 25.86 ? 895  ILE A C     1 
ATOM   6596  O  O     . ILE A  1  897  ? -23.144 94.372  92.172  1.00 24.57 ? 895  ILE A O     1 
ATOM   6597  C  CB    . ILE A  1  897  ? -24.340 92.562  94.744  1.00 21.79 ? 895  ILE A CB    1 
ATOM   6598  C  CG1   . ILE A  1  897  ? -23.895 91.701  95.932  1.00 21.89 ? 895  ILE A CG1   1 
ATOM   6599  C  CG2   . ILE A  1  897  ? -24.579 91.719  93.500  1.00 23.76 ? 895  ILE A CG2   1 
ATOM   6600  C  CD1   . ILE A  1  897  ? -25.066 90.989  96.606  1.00 21.78 ? 895  ILE A CD1   1 
ATOM   6601  N  N     . GLU A  1  898  ? -24.653 95.437  93.463  1.00 24.55 ? 896  GLU A N     1 
ATOM   6602  C  CA    . GLU A  1  898  ? -25.132 96.265  92.361  1.00 22.98 ? 896  GLU A CA    1 
ATOM   6603  C  C     . GLU A  1  898  ? -24.029 97.156  91.816  1.00 24.92 ? 896  GLU A C     1 
ATOM   6604  O  O     . GLU A  1  898  ? -23.955 97.395  90.606  1.00 26.35 ? 896  GLU A O     1 
ATOM   6605  C  CB    . GLU A  1  898  ? -26.309 97.122  92.818  1.00 27.30 ? 896  GLU A CB    1 
ATOM   6606  C  CG    . GLU A  1  898  ? -27.579 96.350  93.084  1.00 32.09 ? 896  GLU A CG    1 
ATOM   6607  C  CD    . GLU A  1  898  ? -28.727 97.265  93.494  1.00 27.10 ? 896  GLU A CD    1 
ATOM   6608  O  OE1   . GLU A  1  898  ? -28.465 98.329  94.104  1.00 39.68 ? 896  GLU A OE1   1 
ATOM   6609  O  OE2   . GLU A  1  898  ? -29.886 96.930  93.190  1.00 38.74 ? 896  GLU A OE2   1 
ATOM   6610  N  N     . LYS A  1  899  ? -23.180 97.682  92.699  1.00 23.47 ? 897  LYS A N     1 
ATOM   6611  C  CA    . LYS A  1  899  ? -22.062 98.494  92.244  1.00 23.71 ? 897  LYS A CA    1 
ATOM   6612  C  C     . LYS A  1  899  ? -21.164 97.695  91.309  1.00 27.35 ? 897  LYS A C     1 
ATOM   6613  O  O     . LYS A  1  899  ? -20.700 98.209  90.286  1.00 27.94 ? 897  LYS A O     1 
ATOM   6614  C  CB    . LYS A  1  899  ? -21.265 99.011  93.445  1.00 28.27 ? 897  LYS A CB    1 
ATOM   6615  N  N     . HIS A  1  900  ? -20.929 96.427  91.633  1.00 24.11 ? 898  HIS A N     1 
ATOM   6616  C  CA    . HIS A  1  900  ? -20.110 95.590  90.765  1.00 24.99 ? 898  HIS A CA    1 
ATOM   6617  C  C     . HIS A  1  900  ? -20.770 95.405  89.408  1.00 24.03 ? 898  HIS A C     1 
ATOM   6618  O  O     . HIS A  1  900  ? -20.128 95.566  88.367  1.00 25.42 ? 898  HIS A O     1 
ATOM   6619  C  CB    . HIS A  1  900  ? -19.873 94.233  91.413  1.00 23.09 ? 898  HIS A CB    1 
ATOM   6620  C  CG    . HIS A  1  900  ? -19.258 93.236  90.487  1.00 23.76 ? 898  HIS A CG    1 
ATOM   6621  N  ND1   . HIS A  1  900  ? -17.918 93.246  90.168  1.00 26.70 ? 898  HIS A ND1   1 
ATOM   6622  C  CD2   . HIS A  1  900  ? -19.802 92.203  89.801  1.00 24.79 ? 898  HIS A CD2   1 
ATOM   6623  C  CE1   . HIS A  1  900  ? -17.660 92.254  89.334  1.00 24.35 ? 898  HIS A CE1   1 
ATOM   6624  N  NE2   . HIS A  1  900  ? -18.785 91.603  89.100  1.00 23.13 ? 898  HIS A NE2   1 
ATOM   6625  N  N     . ILE A  1  901  ? -22.062 95.068  89.405  1.00 21.99 ? 899  ILE A N     1 
ATOM   6626  C  CA    . ILE A  1  901  ? -22.778 94.860  88.149  1.00 22.73 ? 899  ILE A CA    1 
ATOM   6627  C  C     . ILE A  1  901  ? -22.694 96.104  87.278  1.00 25.29 ? 899  ILE A C     1 
ATOM   6628  O  O     . ILE A  1  901  ? -22.446 96.024  86.068  1.00 27.20 ? 899  ILE A O     1 
ATOM   6629  C  CB    . ILE A  1  901  ? -24.238 94.472  88.430  1.00 21.16 ? 899  ILE A CB    1 
ATOM   6630  C  CG1   . ILE A  1  901  ? -24.276 93.148  89.199  1.00 22.06 ? 899  ILE A CG1   1 
ATOM   6631  C  CG2   . ILE A  1  901  ? -25.040 94.417  87.122  1.00 22.57 ? 899  ILE A CG2   1 
ATOM   6632  C  CD1   . ILE A  1  901  ? -25.667 92.761  89.722  1.00 22.51 ? 899  ILE A CD1   1 
ATOM   6633  N  N     . GLU A  1  902  ? -22.919 97.278  87.875  1.00 26.94 ? 900  GLU A N     1 
ATOM   6634  C  CA    . GLU A  1  902  ? -22.927 98.493  87.065  1.00 29.17 ? 900  GLU A CA    1 
ATOM   6635  C  C     . GLU A  1  902  ? -21.533 98.856  86.581  1.00 26.99 ? 900  GLU A C     1 
ATOM   6636  O  O     . GLU A  1  902  ? -21.393 99.426  85.493  1.00 31.31 ? 900  GLU A O     1 
ATOM   6637  C  CB    . GLU A  1  902  ? -23.552 99.648  87.846  1.00 30.93 ? 900  GLU A CB    1 
ATOM   6638  C  CG    . GLU A  1  902  ? -25.038 99.458  88.073  1.00 34.58 ? 900  GLU A CG    1 
ATOM   6639  C  CD    . GLU A  1  902  ? -25.769 99.060  86.801  1.00 43.05 ? 900  GLU A CD    1 
ATOM   6640  O  OE1   . GLU A  1  902  ? -25.599 99.753  85.774  1.00 44.86 ? 900  GLU A OE1   1 
ATOM   6641  O  OE2   . GLU A  1  902  ? -26.509 98.050  86.828  1.00 41.09 ? 900  GLU A OE2   1 
ATOM   6642  N  N     . ARG A  1  903  ? -20.499 98.542  87.363  1.00 28.52 ? 901  ARG A N     1 
ATOM   6643  C  CA    . ARG A  1  903  ? -19.133 98.711  86.880  1.00 30.29 ? 901  ARG A CA    1 
ATOM   6644  C  C     . ARG A  1  903  ? -18.887 97.851  85.646  1.00 34.03 ? 901  ARG A C     1 
ATOM   6645  O  O     . ARG A  1  903  ? -18.369 98.334  84.634  1.00 31.57 ? 901  ARG A O     1 
ATOM   6646  C  CB    . ARG A  1  903  ? -18.132 98.374  87.983  1.00 35.01 ? 901  ARG A CB    1 
ATOM   6647  N  N     . MET A  1  904  ? -19.271 96.572  85.710  1.00 29.86 ? 902  MET A N     1 
ATOM   6648  C  CA    A MET A  1  904  ? -19.144 95.691  84.551  0.41 29.07 ? 902  MET A CA    1 
ATOM   6649  C  CA    B MET A  1  904  ? -19.131 95.698  84.548  0.59 29.06 ? 902  MET A CA    1 
ATOM   6650  C  C     . MET A  1  904  ? -19.932 96.227  83.365  1.00 29.21 ? 902  MET A C     1 
ATOM   6651  O  O     . MET A  1  904  ? -19.440 96.248  82.231  1.00 30.97 ? 902  MET A O     1 
ATOM   6652  C  CB    A MET A  1  904  ? -19.625 94.284  84.906  0.41 26.50 ? 902  MET A CB    1 
ATOM   6653  C  CB    B MET A  1  904  ? -19.575 94.276  84.899  0.59 26.46 ? 902  MET A CB    1 
ATOM   6654  C  CG    A MET A  1  904  ? -18.682 93.526  85.791  0.41 27.12 ? 902  MET A CG    1 
ATOM   6655  C  CG    B MET A  1  904  ? -18.829 93.634  86.055  0.59 26.63 ? 902  MET A CG    1 
ATOM   6656  S  SD    A MET A  1  904  ? -17.037 93.538  85.068  0.41 32.50 ? 902  MET A SD    1 
ATOM   6657  S  SD    B MET A  1  904  ? -17.078 93.327  85.728  0.59 34.45 ? 902  MET A SD    1 
ATOM   6658  C  CE    A MET A  1  904  ? -16.138 92.550  86.259  0.41 28.56 ? 902  MET A CE    1 
ATOM   6659  C  CE    B MET A  1  904  ? -16.334 94.781  86.472  0.59 28.80 ? 902  MET A CE    1 
ATOM   6660  N  N     . ARG A  1  905  ? -21.170 96.657  83.612  1.00 26.20 ? 903  ARG A N     1 
ATOM   6661  C  CA    . ARG A  1  905  ? -22.004 97.170  82.534  1.00 28.78 ? 903  ARG A CA    1 
ATOM   6662  C  C     . ARG A  1  905  ? -21.387 98.417  81.917  1.00 36.59 ? 903  ARG A C     1 
ATOM   6663  O  O     . ARG A  1  905  ? -21.410 98.587  80.693  1.00 33.35 ? 903  ARG A O     1 
ATOM   6664  C  CB    . ARG A  1  905  ? -23.412 97.464  83.051  1.00 29.99 ? 903  ARG A CB    1 
ATOM   6665  C  CG    . ARG A  1  905  ? -24.434 97.659  81.957  1.00 34.93 ? 903  ARG A CG    1 
ATOM   6666  C  CD    . ARG A  1  905  ? -25.729 98.235  82.500  1.00 38.98 ? 903  ARG A CD    1 
ATOM   6667  N  NE    . ARG A  1  905  ? -26.180 97.574  83.720  1.00 35.30 ? 903  ARG A NE    1 
ATOM   6668  C  CZ    . ARG A  1  905  ? -27.013 96.542  83.752  1.00 32.56 ? 903  ARG A CZ    1 
ATOM   6669  N  NH1   . ARG A  1  905  ? -27.450 95.968  82.642  1.00 37.51 ? 903  ARG A NH1   1 
ATOM   6670  N  NH2   . ARG A  1  905  ? -27.424 96.078  84.929  1.00 39.50 ? 903  ARG A NH2   1 
ATOM   6671  N  N     . GLY A  1  906  ? -20.813 99.289  82.753  1.00 30.85 ? 904  GLY A N     1 
ATOM   6672  C  CA    . GLY A  1  906  ? -20.160 100.492 82.270  1.00 33.50 ? 904  GLY A CA    1 
ATOM   6673  C  C     . GLY A  1  906  ? -18.903 100.231 81.469  1.00 40.05 ? 904  GLY A C     1 
ATOM   6674  O  O     . GLY A  1  906  ? -18.524 101.072 80.648  1.00 39.89 ? 904  GLY A O     1 
ATOM   6675  N  N     . LEU A  1  907  ? -18.247 99.090  81.687  1.00 38.24 ? 905  LEU A N     1 
ATOM   6676  C  CA    . LEU A  1  907  ? -17.108 98.673  80.874  1.00 36.36 ? 905  LEU A CA    1 
ATOM   6677  C  C     . LEU A  1  907  ? -17.525 98.033  79.559  1.00 35.21 ? 905  LEU A C     1 
ATOM   6678  O  O     . LEU A  1  907  ? -16.652 97.589  78.806  1.00 39.71 ? 905  LEU A O     1 
ATOM   6679  C  CB    . LEU A  1  907  ? -16.235 97.693  81.654  1.00 34.12 ? 905  LEU A CB    1 
ATOM   6680  C  CG    . LEU A  1  907  ? -15.597 98.286  82.903  1.00 38.73 ? 905  LEU A CG    1 
ATOM   6681  C  CD1   . LEU A  1  907  ? -14.791 97.229  83.625  1.00 37.66 ? 905  LEU A CD1   1 
ATOM   6682  C  CD2   . LEU A  1  907  ? -14.736 99.489  82.528  1.00 39.59 ? 905  LEU A CD2   1 
ATOM   6683  N  N     . GLY A  1  908  ? -18.819 97.971  79.272  1.00 31.27 ? 906  GLY A N     1 
ATOM   6684  C  CA    . GLY A  1  908  ? -19.297 97.401  78.037  1.00 35.02 ? 906  GLY A CA    1 
ATOM   6685  C  C     . GLY A  1  908  ? -19.493 95.905  78.054  1.00 32.23 ? 906  GLY A C     1 
ATOM   6686  O  O     . GLY A  1  908  ? -19.772 95.327  77.002  1.00 31.26 ? 906  GLY A O     1 
ATOM   6687  N  N     . ARG A  1  909  ? -19.363 95.260  79.207  1.00 28.61 ? 907  ARG A N     1 
ATOM   6688  C  CA    . ARG A  1  909  ? -19.608 93.825  79.284  1.00 25.25 ? 907  ARG A CA    1 
ATOM   6689  C  C     . ARG A  1  909  ? -21.099 93.536  79.143  1.00 30.89 ? 907  ARG A C     1 
ATOM   6690  O  O     . ARG A  1  909  ? -21.942 94.274  79.661  1.00 30.52 ? 907  ARG A O     1 
ATOM   6691  C  CB    . ARG A  1  909  ? -19.083 93.272  80.609  1.00 25.31 ? 907  ARG A CB    1 
ATOM   6692  C  CG    . ARG A  1  909  ? -17.630 93.600  80.895  1.00 30.02 ? 907  ARG A CG    1 
ATOM   6693  C  CD    . ARG A  1  909  ? -16.688 92.859  79.961  1.00 32.54 ? 907  ARG A CD    1 
ATOM   6694  N  NE    . ARG A  1  909  ? -15.298 92.977  80.396  1.00 41.22 ? 907  ARG A NE    1 
ATOM   6695  C  CZ    . ARG A  1  909  ? -14.404 93.795  79.855  1.00 55.17 ? 907  ARG A CZ    1 
ATOM   6696  N  NH1   . ARG A  1  909  ? -14.718 94.592  78.846  1.00 49.46 ? 907  ARG A NH1   1 
ATOM   6697  N  NH2   . ARG A  1  909  ? -13.163 93.811  80.337  1.00 48.22 ? 907  ARG A NH2   1 
ATOM   6698  N  N     . LYS A  1  910  ? -21.429 92.459  78.429  1.00 23.04 ? 908  LYS A N     1 
ATOM   6699  C  CA    . LYS A  1  910  ? -22.825 92.085  78.276  1.00 24.92 ? 908  LYS A CA    1 
ATOM   6700  C  C     . LYS A  1  910  ? -23.371 91.562  79.596  1.00 23.06 ? 908  LYS A C     1 
ATOM   6701  O  O     . LYS A  1  910  ? -22.795 90.651  80.201  1.00 23.64 ? 908  LYS A O     1 
ATOM   6702  C  CB    . LYS A  1  910  ? -22.990 91.025  77.194  1.00 26.10 ? 908  LYS A CB    1 
ATOM   6703  C  CG    . LYS A  1  910  ? -22.842 91.543  75.779  1.00 35.85 ? 908  LYS A CG    1 
ATOM   6704  C  CD    . LYS A  1  910  ? -23.210 90.452  74.790  1.00 38.11 ? 908  LYS A CD    1 
ATOM   6705  C  CE    . LYS A  1  910  ? -24.607 89.913  75.056  1.00 39.59 ? 908  LYS A CE    1 
ATOM   6706  N  NZ    . LYS A  1  910  ? -25.071 89.042  73.933  1.00 55.04 ? 908  LYS A NZ    1 
ATOM   6707  N  N     . VAL A  1  911  ? -24.493 92.132  80.028  1.00 22.26 ? 909  VAL A N     1 
ATOM   6708  C  CA    . VAL A  1  911  ? -25.124 91.810  81.306  1.00 22.84 ? 909  VAL A CA    1 
ATOM   6709  C  C     . VAL A  1  911  ? -26.554 91.358  81.033  1.00 24.29 ? 909  VAL A C     1 
ATOM   6710  O  O     . VAL A  1  911  ? -27.345 92.096  80.419  1.00 22.98 ? 909  VAL A O     1 
ATOM   6711  C  CB    . VAL A  1  911  ? -25.100 93.011  82.267  1.00 23.54 ? 909  VAL A CB    1 
ATOM   6712  C  CG1   . VAL A  1  911  ? -25.807 92.672  83.583  1.00 24.51 ? 909  VAL A CG1   1 
ATOM   6713  C  CG2   . VAL A  1  911  ? -23.666 93.463  82.526  1.00 26.65 ? 909  VAL A CG2   1 
ATOM   6714  N  N     . GLU A  1  912  ? -26.879 90.144  81.477  1.00 20.83 ? 910  GLU A N     1 
ATOM   6715  C  CA    . GLU A  1  912  ? -28.222 89.584  81.426  1.00 21.80 ? 910  GLU A CA    1 
ATOM   6716  C  C     . GLU A  1  912  ? -28.793 89.588  82.838  1.00 21.75 ? 910  GLU A C     1 
ATOM   6717  O  O     . GLU A  1  912  ? -28.144 89.092  83.763  1.00 20.89 ? 910  GLU A O     1 
ATOM   6718  C  CB    . GLU A  1  912  ? -28.189 88.153  80.877  1.00 24.33 ? 910  GLU A CB    1 
ATOM   6719  C  CG    . GLU A  1  912  ? -29.554 87.564  80.536  1.00 22.82 ? 910  GLU A CG    1 
ATOM   6720  C  CD    . GLU A  1  912  ? -30.134 88.152  79.266  1.00 26.16 ? 910  GLU A CD    1 
ATOM   6721  O  OE1   . GLU A  1  912  ? -29.387 88.830  78.533  1.00 24.86 ? 910  GLU A OE1   1 
ATOM   6722  O  OE2   . GLU A  1  912  ? -31.335 87.938  78.998  1.00 29.25 ? 910  GLU A OE2   1 
ATOM   6723  N  N     . GLN A  1  913  ? -29.987 90.158  83.016  1.00 20.83 ? 911  GLN A N     1 
ATOM   6724  C  CA    . GLN A  1  913  ? -30.626 90.137  84.328  1.00 22.43 ? 911  GLN A CA    1 
ATOM   6725  C  C     . GLN A  1  913  ? -32.103 89.820  84.211  1.00 24.29 ? 911  GLN A C     1 
ATOM   6726  O  O     . GLN A  1  913  ? -32.774 90.307  83.299  1.00 25.90 ? 911  GLN A O     1 
ATOM   6727  C  CB    . GLN A  1  913  ? -30.499 91.481  85.054  1.00 23.11 ? 911  GLN A CB    1 
ATOM   6728  C  CG    . GLN A  1  913  ? -29.092 91.883  85.385  1.00 26.51 ? 911  GLN A CG    1 
ATOM   6729  C  CD    . GLN A  1  913  ? -29.055 93.097  86.278  1.00 27.24 ? 911  GLN A CD    1 
ATOM   6730  O  OE1   . GLN A  1  913  ? -29.529 94.173  85.906  1.00 30.16 ? 911  GLN A OE1   1 
ATOM   6731  N  NE2   . GLN A  1  913  ? -28.518 92.929  87.472  1.00 25.62 ? 911  GLN A NE2   1 
ATOM   6732  N  N     . ILE A  1  914  ? -32.615 89.046  85.162  1.00 24.78 ? 912  ILE A N     1 
ATOM   6733  C  CA    . ILE A  1  914  ? -34.052 88.804  85.210  1.00 22.30 ? 912  ILE A CA    1 
ATOM   6734  C  C     . ILE A  1  914  ? -34.738 90.041  85.774  1.00 29.51 ? 912  ILE A C     1 
ATOM   6735  O  O     . ILE A  1  914  ? -34.177 90.786  86.588  1.00 27.15 ? 912  ILE A O     1 
ATOM   6736  C  CB    . ILE A  1  914  ? -34.392 87.533  86.020  1.00 32.63 ? 912  ILE A CB    1 
ATOM   6737  C  CG1   . ILE A  1  914  ? -34.497 87.819  87.513  1.00 34.52 ? 912  ILE A CG1   1 
ATOM   6738  C  CG2   . ILE A  1  914  ? -33.372 86.457  85.805  1.00 34.94 ? 912  ILE A CG2   1 
ATOM   6739  C  CD1   . ILE A  1  914  ? -35.888 87.553  88.043  1.00 46.32 ? 912  ILE A CD1   1 
ATOM   6740  N  N     . GLY A  1  915  ? -35.949 90.307  85.296  1.00 31.72 ? 913  GLY A N     1 
ATOM   6741  C  CA    . GLY A  1  915  ? -36.712 91.417  85.836  1.00 30.01 ? 913  GLY A CA    1 
ATOM   6742  C  C     . GLY A  1  915  ? -37.384 91.004  87.133  1.00 28.75 ? 913  GLY A C     1 
ATOM   6743  O  O     . GLY A  1  915  ? -37.936 89.910  87.249  1.00 37.07 ? 913  GLY A O     1 
ATOM   6744  N  N     . LEU A  1  916  ? -37.314 91.890  88.123  1.00 29.82 ? 914  LEU A N     1 
ATOM   6745  C  CA    . LEU A  1  916  ? -37.864 91.616  89.444  1.00 29.10 ? 914  LEU A CA    1 
ATOM   6746  C  C     . LEU A  1  916  ? -39.291 92.127  89.564  1.00 32.95 ? 914  LEU A C     1 
ATOM   6747  O  O     . LEU A  1  916  ? -39.634 93.180  89.020  1.00 31.43 ? 914  LEU A O     1 
ATOM   6748  C  CB    . LEU A  1  916  ? -37.006 92.260  90.528  1.00 30.27 ? 914  LEU A CB    1 
ATOM   6749  C  CG    . LEU A  1  916  ? -35.595 91.696  90.623  1.00 29.10 ? 914  LEU A CG    1 
ATOM   6750  C  CD1   . LEU A  1  916  ? -34.948 92.201  91.891  1.00 33.57 ? 914  LEU A CD1   1 
ATOM   6751  C  CD2   . LEU A  1  916  ? -35.635 90.174  90.587  1.00 33.66 ? 914  LEU A CD2   1 
ATOM   6752  N  N     . ALA A  1  917  ? -40.114 91.377  90.293  1.00 29.74 ? 915  ALA A N     1 
ATOM   6753  C  CA    . ALA A  1  917  ? -41.478 91.808  90.557  1.00 29.03 ? 915  ALA A CA    1 
ATOM   6754  C  C     . ALA A  1  917  ? -41.487 92.992  91.517  1.00 29.50 ? 915  ALA A C     1 
ATOM   6755  O  O     . ALA A  1  917  ? -40.566 93.194  92.316  1.00 31.49 ? 915  ALA A O     1 
ATOM   6756  C  CB    . ALA A  1  917  ? -42.309 90.661  91.135  1.00 33.11 ? 915  ALA A CB    1 
ATOM   6757  N  N     . SER A  1  918  ? -42.564 93.780  91.436  1.00 33.29 ? 916  SER A N     1 
ATOM   6758  C  CA    . SER A  1  918  ? -42.681 94.969  92.273  1.00 33.63 ? 916  SER A CA    1 
ATOM   6759  C  C     . SER A  1  918  ? -42.666 94.620  93.754  1.00 29.33 ? 916  SER A C     1 
ATOM   6760  O  O     . SER A  1  918  ? -42.190 95.416  94.570  1.00 28.98 ? 916  SER A O     1 
ATOM   6761  C  CB    . SER A  1  918  ? -43.963 95.728  91.924  1.00 35.93 ? 916  SER A CB    1 
ATOM   6762  O  OG    . SER A  1  918  ? -45.086 94.871  92.046  1.00 45.06 ? 916  SER A OG    1 
ATOM   6763  N  N     . GLU A  1  919  ? -43.167 93.435  94.115  1.00 33.42 ? 917  GLU A N     1 
ATOM   6764  C  CA    . GLU A  1  919  ? -43.202 93.014  95.511  1.00 32.85 ? 917  GLU A CA    1 
ATOM   6765  C  C     . GLU A  1  919  ? -41.817 92.902  96.128  1.00 35.81 ? 917  GLU A C     1 
ATOM   6766  O  O     . GLU A  1  919  ? -41.705 92.866  97.357  1.00 33.01 ? 917  GLU A O     1 
ATOM   6767  C  CB    . GLU A  1  919  ? -43.915 91.665  95.652  1.00 34.42 ? 917  GLU A CB    1 
ATOM   6768  C  CG    . GLU A  1  919  ? -45.418 91.721  95.451  1.00 46.72 ? 917  GLU A CG    1 
ATOM   6769  C  CD    . GLU A  1  919  ? -45.833 91.494  94.008  1.00 52.33 ? 917  GLU A CD    1 
ATOM   6770  O  OE1   . GLU A  1  919  ? -44.968 91.565  93.109  1.00 43.80 ? 917  GLU A OE1   1 
ATOM   6771  O  OE2   . GLU A  1  919  ? -47.032 91.238  93.776  1.00 59.41 ? 917  GLU A OE2   1 
ATOM   6772  N  N     . THR A  1  920  ? -40.761 92.829  95.316  1.00 29.19 ? 918  THR A N     1 
ATOM   6773  C  CA    . THR A  1  920  ? -39.423 92.740  95.889  1.00 27.14 ? 918  THR A CA    1 
ATOM   6774  C  C     . THR A  1  920  ? -38.971 94.051  96.516  1.00 25.45 ? 918  THR A C     1 
ATOM   6775  O  O     . THR A  1  920  ? -38.013 94.048  97.290  1.00 25.23 ? 918  THR A O     1 
ATOM   6776  C  CB    . THR A  1  920  ? -38.407 92.292  94.830  1.00 26.91 ? 918  THR A CB    1 
ATOM   6777  O  OG1   . THR A  1  920  ? -38.362 93.242  93.757  1.00 28.51 ? 918  THR A OG1   1 
ATOM   6778  C  CG2   . THR A  1  920  ? -38.769 90.908  94.287  1.00 23.83 ? 918  THR A CG2   1 
ATOM   6779  N  N     . GLY A  1  921  ? -39.660 95.159  96.240  1.00 28.15 ? 919  GLY A N     1 
ATOM   6780  C  CA    . GLY A  1  921  ? -39.245 96.447  96.767  1.00 28.94 ? 919  GLY A CA    1 
ATOM   6781  C  C     . GLY A  1  921  ? -39.253 96.548  98.279  1.00 26.48 ? 919  GLY A C     1 
ATOM   6782  O  O     . GLY A  1  921  ? -38.510 97.362  98.829  1.00 32.02 ? 919  GLY A O     1 
ATOM   6783  N  N     . VAL A  1  922  ? -40.069 95.742  98.967  1.00 29.31 ? 920  VAL A N     1 
ATOM   6784  C  CA    . VAL A  1  922  ? -40.100 95.793  100.432 1.00 25.21 ? 920  VAL A CA    1 
ATOM   6785  C  C     . VAL A  1  922  ? -38.921 95.072  101.061 1.00 27.43 ? 920  VAL A C     1 
ATOM   6786  O  O     . VAL A  1  922  ? -38.727 95.169  102.280 1.00 25.81 ? 920  VAL A O     1 
ATOM   6787  C  CB    . VAL A  1  922  ? -41.398 95.192  101.009 1.00 25.06 ? 920  VAL A CB    1 
ATOM   6788  C  CG1   . VAL A  1  922  ? -42.589 96.090  100.709 1.00 28.30 ? 920  VAL A CG1   1 
ATOM   6789  C  CG2   . VAL A  1  922  ? -41.635 93.804  100.459 1.00 26.84 ? 920  VAL A CG2   1 
ATOM   6790  N  N     . GLY A  1  923  ? -38.131 94.347  100.270 1.00 24.20 ? 921  GLY A N     1 
ATOM   6791  C  CA    . GLY A  1  923  ? -36.937 93.706  100.784 1.00 24.53 ? 921  GLY A CA    1 
ATOM   6792  C  C     . GLY A  1  923  ? -35.693 94.108  100.017 1.00 26.58 ? 921  GLY A C     1 
ATOM   6793  O  O     . GLY A  1  923  ? -35.706 95.092  99.273  1.00 26.57 ? 921  GLY A O     1 
ATOM   6794  N  N     . THR A  1  924  ? -34.606 93.357  100.178 1.00 23.19 ? 922  THR A N     1 
ATOM   6795  C  CA    . THR A  1  924  ? -33.337 93.684  99.531  1.00 22.70 ? 922  THR A CA    1 
ATOM   6796  C  C     . THR A  1  924  ? -32.984 92.566  98.555  1.00 23.07 ? 922  THR A C     1 
ATOM   6797  O  O     . THR A  1  924  ? -32.381 91.563  98.943  1.00 22.34 ? 922  THR A O     1 
ATOM   6798  C  CB    . THR A  1  924  ? -32.238 93.903  100.569 1.00 23.74 ? 922  THR A CB    1 
ATOM   6799  O  OG1   . THR A  1  924  ? -32.134 92.761  101.426 1.00 21.16 ? 922  THR A OG1   1 
ATOM   6800  C  CG2   . THR A  1  924  ? -32.579 95.108  101.425 1.00 25.21 ? 922  THR A CG2   1 
ATOM   6801  N  N     . PHE A  1  925  ? -33.335 92.751  97.287  1.00 21.66 ? 923  PHE A N     1 
ATOM   6802  C  CA    . PHE A  1  925  ? -33.137 91.728  96.272  1.00 19.64 ? 923  PHE A CA    1 
ATOM   6803  C  C     . PHE A  1  925  ? -32.180 92.203  95.189  1.00 23.72 ? 923  PHE A C     1 
ATOM   6804  O  O     . PHE A  1  925  ? -32.196 93.375  94.790  1.00 24.44 ? 923  PHE A O     1 
ATOM   6805  C  CB    . PHE A  1  925  ? -34.460 91.340  95.610  1.00 20.23 ? 923  PHE A CB    1 
ATOM   6806  C  CG    . PHE A  1  925  ? -35.412 90.621  96.514  1.00 22.14 ? 923  PHE A CG    1 
ATOM   6807  C  CD1   . PHE A  1  925  ? -36.248 91.325  97.363  1.00 21.53 ? 923  PHE A CD1   1 
ATOM   6808  C  CD2   . PHE A  1  925  ? -35.494 89.243  96.487  1.00 21.34 ? 923  PHE A CD2   1 
ATOM   6809  C  CE1   . PHE A  1  925  ? -37.143 90.656  98.181  1.00 23.21 ? 923  PHE A CE1   1 
ATOM   6810  C  CE2   . PHE A  1  925  ? -36.380 88.569  97.300  1.00 19.43 ? 923  PHE A CE2   1 
ATOM   6811  C  CZ    . PHE A  1  925  ? -37.206 89.279  98.150  1.00 18.97 ? 923  PHE A CZ    1 
ATOM   6812  N  N     . VAL A  1  926  ? -31.376 91.269  94.694  1.00 22.97 ? 924  VAL A N     1 
ATOM   6813  C  CA    . VAL A  1  926  ? -30.559 91.459  93.505  1.00 22.19 ? 924  VAL A CA    1 
ATOM   6814  C  C     . VAL A  1  926  ? -31.006 90.417  92.491  1.00 20.67 ? 924  VAL A C     1 
ATOM   6815  O  O     . VAL A  1  926  ? -31.064 89.233  92.825  1.00 21.13 ? 924  VAL A O     1 
ATOM   6816  C  CB    . VAL A  1  926  ? -29.053 91.318  93.796  1.00 22.56 ? 924  VAL A CB    1 
ATOM   6817  C  CG1   . VAL A  1  926  ? -28.256 91.424  92.502  1.00 23.21 ? 924  VAL A CG1   1 
ATOM   6818  C  CG2   . VAL A  1  926  ? -28.615 92.394  94.770  1.00 24.98 ? 924  VAL A CG2   1 
ATOM   6819  N  N     . PRO A  1  927  ? -31.369 90.797  91.272  1.00 21.50 ? 925  PRO A N     1 
ATOM   6820  C  CA    . PRO A  1  927  ? -31.768 89.797  90.296  1.00 22.32 ? 925  PRO A CA    1 
ATOM   6821  C  C     . PRO A  1  927  ? -30.585 88.931  89.911  1.00 20.64 ? 925  PRO A C     1 
ATOM   6822  O  O     . PRO A  1  927  ? -29.458 89.427  89.785  1.00 21.36 ? 925  PRO A O     1 
ATOM   6823  C  CB    . PRO A  1  927  ? -32.250 90.634  89.107  1.00 24.77 ? 925  PRO A CB    1 
ATOM   6824  C  CG    . PRO A  1  927  ? -31.543 91.919  89.241  1.00 28.11 ? 925  PRO A CG    1 
ATOM   6825  C  CD    . PRO A  1  927  ? -31.398 92.158  90.713  1.00 24.49 ? 925  PRO A CD    1 
ATOM   6826  N  N     . PRO A  1  928  ? -30.798 87.632  89.750  1.00 19.77 ? 926  PRO A N     1 
ATOM   6827  C  CA    . PRO A  1  928  ? -29.767 86.788  89.142  1.00 17.98 ? 926  PRO A CA    1 
ATOM   6828  C  C     . PRO A  1  928  ? -29.254 87.415  87.853  1.00 17.76 ? 926  PRO A C     1 
ATOM   6829  O  O     . PRO A  1  928  ? -30.021 87.901  87.017  1.00 18.82 ? 926  PRO A O     1 
ATOM   6830  C  CB    . PRO A  1  928  ? -30.502 85.470  88.890  1.00 19.14 ? 926  PRO A CB    1 
ATOM   6831  C  CG    . PRO A  1  928  ? -31.486 85.418  90.015  1.00 22.71 ? 926  PRO A CG    1 
ATOM   6832  C  CD    . PRO A  1  928  ? -31.956 86.844  90.204  1.00 21.38 ? 926  PRO A CD    1 
ATOM   6833  N  N     . THR A  1  929  ? -27.939 87.400  87.704  1.00 17.97 ? 927  THR A N     1 
ATOM   6834  C  CA    . THR A  1  929  ? -27.250 88.210  86.716  1.00 18.26 ? 927  THR A CA    1 
ATOM   6835  C  C     . THR A  1  929  ? -26.171 87.365  86.061  1.00 18.95 ? 927  THR A C     1 
ATOM   6836  O  O     . THR A  1  929  ? -25.472 86.618  86.744  1.00 18.76 ? 927  THR A O     1 
ATOM   6837  C  CB    . THR A  1  929  ? -26.627 89.446  87.383  1.00 19.78 ? 927  THR A CB    1 
ATOM   6838  O  OG1   . THR A  1  929  ? -27.678 90.232  87.952  1.00 21.58 ? 927  THR A OG1   1 
ATOM   6839  C  CG2   . THR A  1  929  ? -25.840 90.299  86.376  1.00 23.16 ? 927  THR A CG2   1 
ATOM   6840  N  N     . ILE A  1  930  ? -26.043 87.486  84.740  1.00 18.66 ? 928  ILE A N     1 
ATOM   6841  C  CA    . ILE A  1  930  ? -24.971 86.842  83.990  1.00 18.39 ? 928  ILE A CA    1 
ATOM   6842  C  C     . ILE A  1  930  ? -24.165 87.942  83.326  1.00 19.69 ? 928  ILE A C     1 
ATOM   6843  O  O     . ILE A  1  930  ? -24.734 88.779  82.616  1.00 21.48 ? 928  ILE A O     1 
ATOM   6844  C  CB    . ILE A  1  930  ? -25.505 85.857  82.935  1.00 17.74 ? 928  ILE A CB    1 
ATOM   6845  C  CG1   . ILE A  1  930  ? -26.296 84.729  83.591  1.00 18.97 ? 928  ILE A CG1   1 
ATOM   6846  C  CG2   . ILE A  1  930  ? -24.336 85.310  82.089  1.00 20.81 ? 928  ILE A CG2   1 
ATOM   6847  C  CD1   . ILE A  1  930  ? -27.066 83.853  82.581  1.00 22.56 ? 928  ILE A CD1   1 
ATOM   6848  N  N     . ILE A  1  931  ? -22.852 87.945  83.559  1.00 18.64 ? 929  ILE A N     1 
ATOM   6849  C  CA    . ILE A  1  931  ? -21.951 88.957  83.017  1.00 20.23 ? 929  ILE A CA    1 
ATOM   6850  C  C     . ILE A  1  931  ? -20.899 88.250  82.175  1.00 21.86 ? 929  ILE A C     1 
ATOM   6851  O  O     . ILE A  1  931  ? -20.192 87.366  82.668  1.00 20.46 ? 929  ILE A O     1 
ATOM   6852  C  CB    . ILE A  1  931  ? -21.272 89.777  84.128  1.00 22.06 ? 929  ILE A CB    1 
ATOM   6853  C  CG1   . ILE A  1  931  ? -22.312 90.461  85.031  1.00 21.43 ? 929  ILE A CG1   1 
ATOM   6854  C  CG2   . ILE A  1  931  ? -20.318 90.788  83.518  1.00 23.72 ? 929  ILE A CG2   1 
ATOM   6855  C  CD1   . ILE A  1  931  ? -21.670 91.251  86.184  1.00 21.50 ? 929  ILE A CD1   1 
ATOM   6856  N  N     . GLU A  1  932  ? -20.767 88.651  80.922  1.00 21.30 ? 930  GLU A N     1 
ATOM   6857  C  CA    . GLU A  1  932  ? -19.803 88.019  80.032  1.00 20.98 ? 930  GLU A CA    1 
ATOM   6858  C  C     . GLU A  1  932  ? -18.490 88.782  80.097  1.00 21.10 ? 930  GLU A C     1 
ATOM   6859  O  O     . GLU A  1  932  ? -18.442 89.979  79.784  1.00 23.71 ? 930  GLU A O     1 
ATOM   6860  C  CB    . GLU A  1  932  ? -20.352 87.971  78.611  1.00 21.74 ? 930  GLU A CB    1 
ATOM   6861  C  CG    . GLU A  1  932  ? -21.522 87.011  78.516  1.00 21.37 ? 930  GLU A CG    1 
ATOM   6862  C  CD    . GLU A  1  932  ? -22.293 87.133  77.226  1.00 25.03 ? 930  GLU A CD    1 
ATOM   6863  O  OE1   . GLU A  1  932  ? -21.665 87.065  76.154  1.00 29.52 ? 930  GLU A OE1   1 
ATOM   6864  O  OE2   . GLU A  1  932  ? -23.529 87.291  77.296  1.00 26.09 ? 930  GLU A OE2   1 
ATOM   6865  N  N     . LEU A  1  933  ? -17.440 88.109  80.538  1.00 21.34 ? 931  LEU A N     1 
ATOM   6866  C  CA    . LEU A  1  933  ? -16.134 88.733  80.656  1.00 23.79 ? 931  LEU A CA    1 
ATOM   6867  C  C     . LEU A  1  933  ? -15.238 88.330  79.494  1.00 26.44 ? 931  LEU A C     1 
ATOM   6868  O  O     . LEU A  1  933  ? -15.416 87.279  78.874  1.00 27.01 ? 931  LEU A O     1 
ATOM   6869  C  CB    . LEU A  1  933  ? -15.466 88.357  81.983  1.00 24.14 ? 931  LEU A CB    1 
ATOM   6870  C  CG    . LEU A  1  933  ? -16.211 88.833  83.236  1.00 28.56 ? 931  LEU A CG    1 
ATOM   6871  C  CD1   . LEU A  1  933  ? -15.477 88.411  84.489  1.00 30.73 ? 931  LEU A CD1   1 
ATOM   6872  C  CD2   . LEU A  1  933  ? -16.368 90.337  83.192  1.00 31.66 ? 931  LEU A CD2   1 
ATOM   6873  N  N     . GLU A  1  934  ? -14.256 89.193  79.211  1.00 26.26 ? 932  GLU A N     1 
ATOM   6874  C  CA    . GLU A  1  934  ? -13.246 88.871  78.211  1.00 39.19 ? 932  GLU A CA    1 
ATOM   6875  C  C     . GLU A  1  934  ? -12.201 87.925  78.786  1.00 38.53 ? 932  GLU A C     1 
ATOM   6876  O  O     . GLU A  1  934  ? -11.835 86.929  78.152  1.00 39.51 ? 932  GLU A O     1 
ATOM   6877  C  CB    . GLU A  1  934  ? -12.588 90.153  77.695  1.00 42.09 ? 932  GLU A CB    1 
ATOM   6878  C  CG    . GLU A  1  934  ? -13.574 91.146  77.099  1.00 50.13 ? 932  GLU A CG    1 
ATOM   6879  C  CD    . GLU A  1  934  ? -14.230 90.626  75.830  1.00 58.69 ? 932  GLU A CD    1 
ATOM   6880  O  OE1   . GLU A  1  934  ? -13.587 90.696  74.759  1.00 62.90 ? 932  GLU A OE1   1 
ATOM   6881  O  OE2   . GLU A  1  934  ? -15.382 90.139  75.906  1.00 55.34 ? 932  GLU A OE2   1 
ATOM   6882  N  N     . LYS A  1  935  ? -11.731 88.211  79.996  1.00 32.22 ? 933  LYS A N     1 
ATOM   6883  C  CA    . LYS A  1  935  ? -10.678 87.434  80.628  1.00 41.82 ? 933  LYS A CA    1 
ATOM   6884  C  C     . LYS A  1  935  ? -11.019 87.246  82.094  1.00 34.07 ? 933  LYS A C     1 
ATOM   6885  O  O     . LYS A  1  935  ? -11.700 88.077  82.697  1.00 34.61 ? 933  LYS A O     1 
ATOM   6886  C  CB    . LYS A  1  935  ? -9.311  88.121  80.497  1.00 43.87 ? 933  LYS A CB    1 
ATOM   6887  N  N     . LEU A  1  936  ? -10.533 86.142  82.663  1.00 37.84 ? 934  LEU A N     1 
ATOM   6888  C  CA    . LEU A  1  936  ? -10.753 85.879  84.080  1.00 41.29 ? 934  LEU A CA    1 
ATOM   6889  C  C     . LEU A  1  936  ? -10.233 87.019  84.948  1.00 39.12 ? 934  LEU A C     1 
ATOM   6890  O  O     . LEU A  1  936  ? -10.811 87.309  86.001  1.00 37.67 ? 934  LEU A O     1 
ATOM   6891  C  CB    . LEU A  1  936  ? -10.091 84.556  84.463  1.00 41.89 ? 934  LEU A CB    1 
ATOM   6892  C  CG    . LEU A  1  936  ? -10.385 83.942  85.829  1.00 49.92 ? 934  LEU A CG    1 
ATOM   6893  C  CD1   . LEU A  1  936  ? -11.803 84.226  86.258  1.00 40.90 ? 934  LEU A CD1   1 
ATOM   6894  C  CD2   . LEU A  1  936  ? -10.156 82.441  85.760  1.00 43.10 ? 934  LEU A CD2   1 
ATOM   6895  N  N     . SER A  1  937  ? -9.168  87.692  84.511  1.00 42.91 ? 935  SER A N     1 
ATOM   6896  C  CA    . SER A  1  937  ? -8.592  88.790  85.280  1.00 39.05 ? 935  SER A CA    1 
ATOM   6897  C  C     . SER A  1  937  ? -9.475  90.032  85.303  1.00 37.24 ? 935  SER A C     1 
ATOM   6898  O  O     . SER A  1  937  ? -9.177  90.962  86.059  1.00 39.90 ? 935  SER A O     1 
ATOM   6899  C  CB    . SER A  1  937  ? -7.207  89.142  84.733  1.00 46.23 ? 935  SER A CB    1 
ATOM   6900  O  OG    . SER A  1  937  ? -7.268  89.485  83.362  1.00 46.78 ? 935  SER A OG    1 
ATOM   6901  N  N     . ASP A  1  938  ? -10.540 90.079  84.496  1.00 38.13 ? 936  ASP A N     1 
ATOM   6902  C  CA    . ASP A  1  938  ? -11.523 91.150  84.623  1.00 36.31 ? 936  ASP A CA    1 
ATOM   6903  C  C     . ASP A  1  938  ? -12.232 91.115  85.969  1.00 32.97 ? 936  ASP A C     1 
ATOM   6904  O  O     . ASP A  1  938  ? -12.807 92.123  86.389  1.00 35.60 ? 936  ASP A O     1 
ATOM   6905  C  CB    . ASP A  1  938  ? -12.570 91.059  83.504  1.00 39.71 ? 936  ASP A CB    1 
ATOM   6906  C  CG    . ASP A  1  938  ? -11.962 91.151  82.120  1.00 44.63 ? 936  ASP A CG    1 
ATOM   6907  O  OD1   . ASP A  1  938  ? -10.828 91.658  82.003  1.00 46.75 ? 936  ASP A OD1   1 
ATOM   6908  O  OD2   . ASP A  1  938  ? -12.620 90.718  81.147  1.00 47.76 ? 936  ASP A OD2   1 
ATOM   6909  N  N     . LEU A  1  939  ? -12.219 89.977  86.646  1.00 37.40 ? 937  LEU A N     1 
ATOM   6910  C  CA    . LEU A  1  939  ? -12.863 89.823  87.938  1.00 38.24 ? 937  LEU A CA    1 
ATOM   6911  C  C     . LEU A  1  939  ? -11.786 89.865  89.014  1.00 44.24 ? 937  LEU A C     1 
ATOM   6912  O  O     . LEU A  1  939  ? -10.855 89.053  88.993  1.00 51.65 ? 937  LEU A O     1 
ATOM   6913  C  CB    . LEU A  1  939  ? -13.640 88.510  87.976  1.00 35.01 ? 937  LEU A CB    1 
ATOM   6914  C  CG    . LEU A  1  939  ? -14.571 88.276  89.155  1.00 42.56 ? 937  LEU A CG    1 
ATOM   6915  C  CD1   . LEU A  1  939  ? -15.571 89.417  89.260  1.00 37.15 ? 937  LEU A CD1   1 
ATOM   6916  C  CD2   . LEU A  1  939  ? -15.281 86.948  88.975  1.00 38.46 ? 937  LEU A CD2   1 
ATOM   6917  N  N     . GLN A  1  940  ? -11.903 90.812  89.949  1.00 41.58 ? 938  GLN A N     1 
ATOM   6918  C  CA    . GLN A  1  940  ? -10.810 91.093  90.871  1.00 45.58 ? 938  GLN A CA    1 
ATOM   6919  C  C     . GLN A  1  940  ? -11.198 91.002  92.345  1.00 49.44 ? 938  GLN A C     1 
ATOM   6920  O  O     . GLN A  1  940  ? -10.388 91.371  93.202  1.00 60.56 ? 938  GLN A O     1 
ATOM   6921  C  CB    . GLN A  1  940  ? -10.221 92.481  90.582  1.00 51.74 ? 938  GLN A CB    1 
ATOM   6922  N  N     . ARG A  1  941  ? -12.395 90.519  92.668  1.00 48.45 ? 939  ARG A N     1 
ATOM   6923  C  CA    . ARG A  1  941  ? -12.846 90.423  94.052  1.00 45.22 ? 939  ARG A CA    1 
ATOM   6924  C  C     . ARG A  1  941  ? -14.068 89.517  94.104  1.00 29.94 ? 939  ARG A C     1 
ATOM   6925  O  O     . ARG A  1  941  ? -14.860 89.487  93.159  1.00 42.60 ? 939  ARG A O     1 
ATOM   6926  C  CB    . ARG A  1  941  ? -13.183 91.805  94.629  1.00 46.97 ? 939  ARG A CB    1 
ATOM   6927  N  N     . GLU A  1  942  ? -14.199 88.765  95.203  1.00 34.20 ? 940  GLU A N     1 
ATOM   6928  C  CA    . GLU A  1  942  ? -15.379 87.927  95.410  1.00 35.13 ? 940  GLU A CA    1 
ATOM   6929  C  C     . GLU A  1  942  ? -16.620 88.804  95.516  1.00 33.71 ? 940  GLU A C     1 
ATOM   6930  O  O     . GLU A  1  942  ? -16.689 89.700  96.366  1.00 33.91 ? 940  GLU A O     1 
ATOM   6931  C  CB    . GLU A  1  942  ? -15.222 87.067  96.671  1.00 32.83 ? 940  GLU A CB    1 
ATOM   6932  C  CG    . GLU A  1  942  ? -16.450 86.182  96.987  1.00 33.44 ? 940  GLU A CG    1 
ATOM   6933  C  CD    . GLU A  1  942  ? -16.428 85.559  98.386  1.00 39.72 ? 940  GLU A CD    1 
ATOM   6934  O  OE1   . GLU A  1  942  ? -16.206 86.294  99.376  1.00 39.31 ? 940  GLU A OE1   1 
ATOM   6935  O  OE2   . GLU A  1  942  ? -16.647 84.329  98.501  1.00 32.38 ? 940  GLU A OE2   1 
ATOM   6936  N  N     . VAL A  1  943  ? -17.587 88.564  94.634  1.00 26.53 ? 941  VAL A N     1 
ATOM   6937  C  CA    . VAL A  1  943  ? -18.863 89.274  94.636  1.00 23.86 ? 941  VAL A CA    1 
ATOM   6938  C  C     . VAL A  1  943  ? -19.897 88.310  95.194  1.00 26.59 ? 941  VAL A C     1 
ATOM   6939  O  O     . VAL A  1  943  ? -20.303 87.354  94.523  1.00 24.01 ? 941  VAL A O     1 
ATOM   6940  C  CB    . VAL A  1  943  ? -19.245 89.771  93.235  1.00 23.88 ? 941  VAL A CB    1 
ATOM   6941  C  CG1   . VAL A  1  943  ? -20.591 90.490  93.261  1.00 25.52 ? 941  VAL A CG1   1 
ATOM   6942  C  CG2   . VAL A  1  943  ? -18.165 90.695  92.694  1.00 28.79 ? 941  VAL A CG2   1 
ATOM   6943  N  N     . PHE A  1  944  ? -20.317 88.554  96.431  1.00 23.77 ? 942  PHE A N     1 
ATOM   6944  C  CA    . PHE A  1  944  ? -21.060 87.560  97.203  1.00 21.90 ? 942  PHE A CA    1 
ATOM   6945  C  C     . PHE A  1  944  ? -22.556 87.737  96.963  1.00 23.13 ? 942  PHE A C     1 
ATOM   6946  O  O     . PHE A  1  944  ? -23.323 88.158  97.830  1.00 22.89 ? 942  PHE A O     1 
ATOM   6947  C  CB    . PHE A  1  944  ? -20.713 87.676  98.683  1.00 21.38 ? 942  PHE A CB    1 
ATOM   6948  C  CG    . PHE A  1  944  ? -20.969 86.417  99.457  1.00 24.55 ? 942  PHE A CG    1 
ATOM   6949  C  CD1   . PHE A  1  944  ? -20.176 85.293  99.253  1.00 25.13 ? 942  PHE A CD1   1 
ATOM   6950  C  CD2   . PHE A  1  944  ? -22.002 86.347  100.387 1.00 23.84 ? 942  PHE A CD2   1 
ATOM   6951  C  CE1   . PHE A  1  944  ? -20.425 84.126  99.951  1.00 27.24 ? 942  PHE A CE1   1 
ATOM   6952  C  CE2   . PHE A  1  944  ? -22.236 85.184  101.107 1.00 26.59 ? 942  PHE A CE2   1 
ATOM   6953  C  CZ    . PHE A  1  944  ? -21.454 84.068  100.877 1.00 27.09 ? 942  PHE A CZ    1 
ATOM   6954  N  N     . GLY A  1  945  ? -22.967 87.401  95.743  1.00 20.98 ? 943  GLY A N     1 
ATOM   6955  C  CA    . GLY A  1  945  ? -24.327 87.626  95.322  1.00 20.72 ? 943  GLY A CA    1 
ATOM   6956  C  C     . GLY A  1  945  ? -24.640 86.785  94.106  1.00 21.54 ? 943  GLY A C     1 
ATOM   6957  O  O     . GLY A  1  945  ? -23.833 85.960  93.675  1.00 19.71 ? 943  GLY A O     1 
ATOM   6958  N  N     . PRO A  1  946  ? -25.821 86.976  93.532  1.00 19.98 ? 944  PRO A N     1 
ATOM   6959  C  CA    . PRO A  1  946  ? -26.279 86.101  92.432  1.00 18.76 ? 944  PRO A CA    1 
ATOM   6960  C  C     . PRO A  1  946  ? -25.755 86.598  91.091  1.00 18.00 ? 944  PRO A C     1 
ATOM   6961  O  O     . PRO A  1  946  ? -26.504 87.051  90.213  1.00 18.37 ? 944  PRO A O     1 
ATOM   6962  C  CB    . PRO A  1  946  ? -27.803 86.191  92.557  1.00 18.48 ? 944  PRO A CB    1 
ATOM   6963  C  CG    . PRO A  1  946  ? -28.060 87.564  93.112  1.00 21.63 ? 944  PRO A CG    1 
ATOM   6964  C  CD    . PRO A  1  946  ? -26.864 87.904  94.007  1.00 19.04 ? 944  PRO A CD    1 
ATOM   6965  N  N     . VAL A  1  947  ? -24.432 86.538  90.933  1.00 18.03 ? 945  VAL A N     1 
ATOM   6966  C  CA    . VAL A  1  947  ? -23.760 87.130  89.785  1.00 17.78 ? 945  VAL A CA    1 
ATOM   6967  C  C     . VAL A  1  947  ? -22.795 86.111  89.205  1.00 19.49 ? 945  VAL A C     1 
ATOM   6968  O  O     . VAL A  1  947  ? -21.739 85.838  89.787  1.00 20.98 ? 945  VAL A O     1 
ATOM   6969  C  CB    . VAL A  1  947  ? -23.030 88.431  90.137  1.00 21.76 ? 945  VAL A CB    1 
ATOM   6970  C  CG1   . VAL A  1  947  ? -22.459 89.051  88.886  1.00 22.23 ? 945  VAL A CG1   1 
ATOM   6971  C  CG2   . VAL A  1  947  ? -23.982 89.399  90.823  1.00 20.20 ? 945  VAL A CG2   1 
ATOM   6972  N  N     . LEU A  1  948  ? -23.139 85.583  88.043  1.00 18.68 ? 946  LEU A N     1 
ATOM   6973  C  CA    . LEU A  1  948  ? -22.321 84.619  87.332  1.00 17.09 ? 946  LEU A CA    1 
ATOM   6974  C  C     . LEU A  1  948  ? -21.540 85.333  86.245  1.00 19.53 ? 946  LEU A C     1 
ATOM   6975  O  O     . LEU A  1  948  ? -22.115 86.076  85.444  1.00 21.98 ? 946  LEU A O     1 
ATOM   6976  C  CB    . LEU A  1  948  ? -23.200 83.545  86.706  1.00 18.40 ? 946  LEU A CB    1 
ATOM   6977  C  CG    . LEU A  1  948  ? -22.399 82.542  85.884  1.00 17.18 ? 946  LEU A CG    1 
ATOM   6978  C  CD1   . LEU A  1  948  ? -21.489 81.744  86.799  1.00 19.18 ? 946  LEU A CD1   1 
ATOM   6979  C  CD2   . LEU A  1  948  ? -23.381 81.647  85.155  1.00 20.61 ? 946  LEU A CD2   1 
ATOM   6980  N  N     . HIS A  1  949  ? -20.243 85.105  86.216  1.00 18.63 ? 947  HIS A N     1 
ATOM   6981  C  CA    . HIS A  1  949  ? -19.407 85.620  85.149  1.00 16.63 ? 947  HIS A CA    1 
ATOM   6982  C  C     . HIS A  1  949  ? -19.085 84.483  84.203  1.00 18.43 ? 947  HIS A C     1 
ATOM   6983  O  O     . HIS A  1  949  ? -18.898 83.346  84.636  1.00 20.22 ? 947  HIS A O     1 
ATOM   6984  C  CB    . HIS A  1  949  ? -18.132 86.225  85.712  1.00 16.79 ? 947  HIS A CB    1 
ATOM   6985  C  CG    . HIS A  1  949  ? -18.397 87.259  86.754  1.00 20.16 ? 947  HIS A CG    1 
ATOM   6986  N  ND1   . HIS A  1  949  ? -18.643 86.932  88.072  1.00 21.01 ? 947  HIS A ND1   1 
ATOM   6987  C  CD2   . HIS A  1  949  ? -18.524 88.603  86.663  1.00 23.20 ? 947  HIS A CD2   1 
ATOM   6988  C  CE1   . HIS A  1  949  ? -18.877 88.040  88.754  1.00 21.03 ? 947  HIS A CE1   1 
ATOM   6989  N  NE2   . HIS A  1  949  ? -18.814 89.065  87.922  1.00 22.82 ? 947  HIS A NE2   1 
ATOM   6990  N  N     . VAL A  1  950  ? -19.066 84.782  82.909  1.00 18.38 ? 948  VAL A N     1 
ATOM   6991  C  CA    . VAL A  1  950  ? -18.858 83.754  81.896  1.00 18.17 ? 948  VAL A CA    1 
ATOM   6992  C  C     . VAL A  1  950  ? -17.663 84.150  81.052  1.00 21.29 ? 948  VAL A C     1 
ATOM   6993  O  O     . VAL A  1  950  ? -17.607 85.269  80.527  1.00 21.59 ? 948  VAL A O     1 
ATOM   6994  C  CB    . VAL A  1  950  ? -20.105 83.557  81.017  1.00 20.43 ? 948  VAL A CB    1 
ATOM   6995  C  CG1   . VAL A  1  950  ? -19.814 82.536  79.898  1.00 22.48 ? 948  VAL A CG1   1 
ATOM   6996  C  CG2   . VAL A  1  950  ? -21.303 83.126  81.852  1.00 20.93 ? 948  VAL A CG2   1 
ATOM   6997  N  N     . ILE A  1  951  ? -16.713 83.231  80.909  1.00 20.44 ? 949  ILE A N     1 
ATOM   6998  C  CA    . ILE A  1  951  ? -15.609 83.436  79.988  1.00 23.75 ? 949  ILE A CA    1 
ATOM   6999  C  C     . ILE A  1  951  ? -15.579 82.263  79.026  1.00 25.05 ? 949  ILE A C     1 
ATOM   7000  O  O     . ILE A  1  951  ? -16.098 81.185  79.309  1.00 20.89 ? 949  ILE A O     1 
ATOM   7001  C  CB    . ILE A  1  951  ? -14.260 83.598  80.705  1.00 20.33 ? 949  ILE A CB    1 
ATOM   7002  C  CG1   . ILE A  1  951  ? -13.925 82.371  81.534  1.00 26.45 ? 949  ILE A CG1   1 
ATOM   7003  C  CG2   . ILE A  1  951  ? -14.266 84.847  81.596  1.00 23.40 ? 949  ILE A CG2   1 
ATOM   7004  C  CD1   . ILE A  1  951  ? -12.611 82.528  82.234  1.00 31.90 ? 949  ILE A CD1   1 
ATOM   7005  N  N     . ARG A  1  952  ? -14.967 82.490  77.871  1.00 22.59 ? 950  ARG A N     1 
ATOM   7006  C  CA    . ARG A  1  952  ? -14.833 81.471  76.843  1.00 22.56 ? 950  ARG A CA    1 
ATOM   7007  C  C     . ARG A  1  952  ? -13.361 81.122  76.679  1.00 20.24 ? 950  ARG A C     1 
ATOM   7008  O  O     . ARG A  1  952  ? -12.483 81.963  76.896  1.00 23.83 ? 950  ARG A O     1 
ATOM   7009  C  CB    . ARG A  1  952  ? -15.412 81.966  75.513  1.00 22.96 ? 950  ARG A CB    1 
ATOM   7010  C  CG    . ARG A  1  952  ? -16.812 82.554  75.636  1.00 25.40 ? 950  ARG A CG    1 
ATOM   7011  C  CD    . ARG A  1  952  ? -17.063 83.558  74.538  1.00 30.95 ? 950  ARG A CD    1 
ATOM   7012  N  NE    . ARG A  1  952  ? -17.365 82.896  73.277  1.00 31.31 ? 950  ARG A NE    1 
ATOM   7013  C  CZ    . ARG A  1  952  ? -18.588 82.753  72.786  1.00 29.31 ? 950  ARG A CZ    1 
ATOM   7014  N  NH1   . ARG A  1  952  ? -19.647 83.240  73.413  1.00 28.70 ? 950  ARG A NH1   1 
ATOM   7015  N  NH2   . ARG A  1  952  ? -18.754 82.099  71.643  1.00 27.73 ? 950  ARG A NH2   1 
ATOM   7016  N  N     . TYR A  1  953  ? -13.082 79.874  76.305  1.00 19.53 ? 951  TYR A N     1 
ATOM   7017  C  CA    . TYR A  1  953  ? -11.695 79.467  76.124  1.00 20.62 ? 951  TYR A CA    1 
ATOM   7018  C  C     . TYR A  1  953  ? -11.568 78.516  74.945  1.00 21.16 ? 951  TYR A C     1 
ATOM   7019  O  O     . TYR A  1  953  ? -12.463 77.715  74.667  1.00 22.03 ? 951  TYR A O     1 
ATOM   7020  C  CB    . TYR A  1  953  ? -11.124 78.803  77.395  1.00 21.09 ? 951  TYR A CB    1 
ATOM   7021  C  CG    . TYR A  1  953  ? -11.649 77.414  77.657  1.00 19.77 ? 951  TYR A CG    1 
ATOM   7022  C  CD1   . TYR A  1  953  ? -12.877 77.219  78.277  1.00 17.33 ? 951  TYR A CD1   1 
ATOM   7023  C  CD2   . TYR A  1  953  ? -10.914 76.294  77.277  1.00 21.28 ? 951  TYR A CD2   1 
ATOM   7024  C  CE1   . TYR A  1  953  ? -13.355 75.950  78.529  1.00 18.03 ? 951  TYR A CE1   1 
ATOM   7025  C  CE2   . TYR A  1  953  ? -11.384 75.025  77.511  1.00 17.95 ? 951  TYR A CE2   1 
ATOM   7026  C  CZ    . TYR A  1  953  ? -12.602 74.858  78.132  1.00 20.12 ? 951  TYR A CZ    1 
ATOM   7027  O  OH    . TYR A  1  953  ? -13.069 73.597  78.355  1.00 19.76 ? 951  TYR A OH    1 
ATOM   7028  N  N     . ARG A  1  954  ? -10.426 78.613  74.264  1.00 22.87 ? 952  ARG A N     1 
ATOM   7029  C  CA    . ARG A  1  954  ? -10.065 77.667  73.216  1.00 26.04 ? 952  ARG A CA    1 
ATOM   7030  C  C     . ARG A  1  954  ? -9.534  76.379  73.833  1.00 20.61 ? 952  ARG A C     1 
ATOM   7031  O  O     . ARG A  1  954  ? -8.823  76.412  74.839  1.00 22.42 ? 952  ARG A O     1 
ATOM   7032  C  CB    . ARG A  1  954  ? -9.007  78.279  72.299  1.00 26.86 ? 952  ARG A CB    1 
ATOM   7033  C  CG    . ARG A  1  954  ? -9.390  79.636  71.743  1.00 34.69 ? 952  ARG A CG    1 
ATOM   7034  C  CD    . ARG A  1  954  ? -10.675 79.528  70.954  1.00 41.28 ? 952  ARG A CD    1 
ATOM   7035  N  NE    . ARG A  1  954  ? -10.567 78.490  69.939  1.00 49.45 ? 952  ARG A NE    1 
ATOM   7036  C  CZ    . ARG A  1  954  ? -10.220 78.714  68.680  1.00 58.34 ? 952  ARG A CZ    1 
ATOM   7037  N  NH1   . ARG A  1  954  ? -10.013 79.941  68.229  1.00 61.61 ? 952  ARG A NH1   1 
ATOM   7038  N  NH2   . ARG A  1  954  ? -10.074 77.682  67.854  1.00 62.24 ? 952  ARG A NH2   1 
ATOM   7039  N  N     . ARG A  1  955  ? -9.884  75.238  73.225  1.00 25.94 ? 953  ARG A N     1 
ATOM   7040  C  CA    . ARG A  1  955  ? -9.520  73.945  73.812  1.00 24.84 ? 953  ARG A CA    1 
ATOM   7041  C  C     . ARG A  1  955  ? -8.027  73.854  74.118  1.00 21.51 ? 953  ARG A C     1 
ATOM   7042  O  O     . ARG A  1  955  ? -7.633  73.379  75.190  1.00 24.23 ? 953  ARG A O     1 
ATOM   7043  C  CB    . ARG A  1  955  ? -9.935  72.799  72.882  1.00 31.25 ? 953  ARG A CB    1 
ATOM   7044  C  CG    . ARG A  1  955  ? -9.408  71.418  73.323  1.00 45.42 ? 953  ARG A CG    1 
ATOM   7045  C  CD    . ARG A  1  955  ? -9.775  71.165  74.778  1.00 41.67 ? 953  ARG A CD    1 
ATOM   7046  N  NE    . ARG A  1  955  ? -9.382  69.880  75.348  1.00 54.57 ? 953  ARG A NE    1 
ATOM   7047  C  CZ    . ARG A  1  955  ? -8.297  69.676  76.087  1.00 46.40 ? 953  ARG A CZ    1 
ATOM   7048  N  NH1   . ARG A  1  955  ? -7.378  70.617  76.246  1.00 34.11 ? 953  ARG A NH1   1 
ATOM   7049  N  NH2   . ARG A  1  955  ? -8.132  68.500  76.688  1.00 42.21 ? 953  ARG A NH2   1 
ATOM   7050  N  N     . ASP A  1  956  ? -7.180  74.311  73.195  1.00 25.31 ? 954  ASP A N     1 
ATOM   7051  C  CA    . ASP A  1  956  ? -5.737  74.228  73.421  1.00 24.33 ? 954  ASP A CA    1 
ATOM   7052  C  C     . ASP A  1  956  ? -5.279  75.103  74.576  1.00 22.14 ? 954  ASP A C     1 
ATOM   7053  O  O     . ASP A  1  956  ? -4.175  74.901  75.089  1.00 27.01 ? 954  ASP A O     1 
ATOM   7054  C  CB    . ASP A  1  956  ? -4.965  74.636  72.170  1.00 24.93 ? 954  ASP A CB    1 
ATOM   7055  C  CG    . ASP A  1  956  ? -5.133  73.654  71.027  1.00 30.83 ? 954  ASP A CG    1 
ATOM   7056  O  OD1   . ASP A  1  956  ? -5.540  72.504  71.277  1.00 33.90 ? 954  ASP A OD1   1 
ATOM   7057  O  OD2   . ASP A  1  956  ? -4.843  74.049  69.876  1.00 36.61 ? 954  ASP A OD2   1 
ATOM   7058  N  N     . ASP A  1  957  ? -6.093  76.073  74.989  1.00 22.59 ? 955  ASP A N     1 
ATOM   7059  C  CA    . ASP A  1  957  ? -5.742  76.950  76.096  1.00 23.63 ? 955  ASP A CA    1 
ATOM   7060  C  C     . ASP A  1  957  ? -6.293  76.464  77.430  1.00 23.14 ? 955  ASP A C     1 
ATOM   7061  O  O     . ASP A  1  957  ? -6.319  77.237  78.393  1.00 25.12 ? 955  ASP A O     1 
ATOM   7062  C  CB    . ASP A  1  957  ? -6.239  78.371  75.829  1.00 26.63 ? 955  ASP A CB    1 
ATOM   7063  C  CG    . ASP A  1  957  ? -5.536  79.024  74.669  1.00 35.97 ? 955  ASP A CG    1 
ATOM   7064  O  OD1   . ASP A  1  957  ? -4.340  78.729  74.448  1.00 35.32 ? 955  ASP A OD1   1 
ATOM   7065  O  OD2   . ASP A  1  957  ? -6.185  79.835  73.983  1.00 31.97 ? 955  ASP A OD2   1 
ATOM   7066  N  N     . LEU A  1  958  ? -6.727  75.205  77.513  1.00 20.37 ? 956  LEU A N     1 
ATOM   7067  C  CA    . LEU A  1  958  ? -7.281  74.701  78.769  1.00 18.85 ? 956  LEU A CA    1 
ATOM   7068  C  C     . LEU A  1  958  ? -6.273  74.813  79.907  1.00 21.41 ? 956  LEU A C     1 
ATOM   7069  O  O     . LEU A  1  958  ? -6.617  75.244  81.015  1.00 20.90 ? 956  LEU A O     1 
ATOM   7070  C  CB    . LEU A  1  958  ? -7.737  73.254  78.598  1.00 20.02 ? 956  LEU A CB    1 
ATOM   7071  C  CG    . LEU A  1  958  ? -8.237  72.536  79.853  1.00 21.41 ? 956  LEU A CG    1 
ATOM   7072  C  CD1   . LEU A  1  958  ? -9.448  73.242  80.458  1.00 22.18 ? 956  LEU A CD1   1 
ATOM   7073  C  CD2   . LEU A  1  958  ? -8.563  71.084  79.538  1.00 22.07 ? 956  LEU A CD2   1 
ATOM   7074  N  N     . ASP A  1  959  ? -5.015  74.425  79.658  1.00 19.81 ? 957  ASP A N     1 
ATOM   7075  C  CA    . ASP A  1  959  ? -4.038  74.455  80.737  1.00 21.64 ? 957  ASP A CA    1 
ATOM   7076  C  C     . ASP A  1  959  ? -3.795  75.878  81.203  1.00 21.84 ? 957  ASP A C     1 
ATOM   7077  O  O     . ASP A  1  959  ? -3.694  76.128  82.406  1.00 22.41 ? 957  ASP A O     1 
ATOM   7078  C  CB    . ASP A  1  959  ? -2.720  73.816  80.301  1.00 23.30 ? 957  ASP A CB    1 
ATOM   7079  C  CG    . ASP A  1  959  ? -1.827  73.498  81.481  1.00 24.69 ? 957  ASP A CG    1 
ATOM   7080  O  OD1   . ASP A  1  959  ? -2.295  72.810  82.411  1.00 23.92 ? 957  ASP A OD1   1 
ATOM   7081  O  OD2   . ASP A  1  959  ? -0.666  73.943  81.494  1.00 30.43 ? 957  ASP A OD2   1 
ATOM   7082  N  N     . ARG A  1  960  ? -3.703  76.820  80.265  1.00 20.45 ? 958  ARG A N     1 
ATOM   7083  C  CA    . ARG A  1  960  ? -3.554  78.220  80.647  1.00 21.61 ? 958  ARG A CA    1 
ATOM   7084  C  C     . ARG A  1  960  ? -4.762  78.691  81.447  1.00 22.86 ? 958  ARG A C     1 
ATOM   7085  O  O     . ARG A  1  960  ? -4.621  79.455  82.410  1.00 24.36 ? 958  ARG A O     1 
ATOM   7086  C  CB    . ARG A  1  960  ? -3.358  79.088  79.400  1.00 22.56 ? 958  ARG A CB    1 
ATOM   7087  C  CG    . ARG A  1  960  ? -3.159  80.567  79.702  1.00 25.54 ? 958  ARG A CG    1 
ATOM   7088  C  CD    . ARG A  1  960  ? -4.122  81.419  78.876  1.00 50.30 ? 958  ARG A CD    1 
ATOM   7089  N  NE    . ARG A  1  960  ? -5.510  81.050  79.138  1.00 46.10 ? 958  ARG A NE    1 
ATOM   7090  C  CZ    . ARG A  1  960  ? -6.542  81.409  78.387  1.00 46.58 ? 958  ARG A CZ    1 
ATOM   7091  N  NH1   . ARG A  1  960  ? -6.385  82.159  77.308  1.00 57.58 ? 958  ARG A NH1   1 
ATOM   7092  N  NH2   . ARG A  1  960  ? -7.763  80.998  78.722  1.00 46.91 ? 958  ARG A NH2   1 
ATOM   7093  N  N     . LEU A  1  961  ? -5.957  78.231  81.069  1.00 20.69 ? 959  LEU A N     1 
ATOM   7094  C  CA    . LEU A  1  961  ? -7.165  78.611  81.800  1.00 20.96 ? 959  LEU A CA    1 
ATOM   7095  C  C     . LEU A  1  961  ? -7.114  78.124  83.241  1.00 23.13 ? 959  LEU A C     1 
ATOM   7096  O  O     . LEU A  1  961  ? -7.475  78.859  84.164  1.00 21.19 ? 959  LEU A O     1 
ATOM   7097  C  CB    . LEU A  1  961  ? -8.401  78.054  81.100  1.00 21.80 ? 959  LEU A CB    1 
ATOM   7098  C  CG    . LEU A  1  961  ? -9.698  78.196  81.899  1.00 22.09 ? 959  LEU A CG    1 
ATOM   7099  C  CD1   . LEU A  1  961  ? -10.033 79.678  82.069  1.00 29.41 ? 959  LEU A CD1   1 
ATOM   7100  C  CD2   . LEU A  1  961  ? -10.831 77.448  81.223  1.00 25.23 ? 959  LEU A CD2   1 
ATOM   7101  N  N     . VAL A  1  962  ? -6.691  76.877  83.456  1.00 21.33 ? 960  VAL A N     1 
ATOM   7102  C  CA    . VAL A  1  962  ? -6.534  76.396  84.824  1.00 18.42 ? 960  VAL A CA    1 
ATOM   7103  C  C     . VAL A  1  962  ? -5.537  77.266  85.581  1.00 25.22 ? 960  VAL A C     1 
ATOM   7104  O  O     . VAL A  1  962  ? -5.751  77.594  86.755  1.00 23.14 ? 960  VAL A O     1 
ATOM   7105  C  CB    . VAL A  1  962  ? -6.122  74.913  84.823  1.00 20.18 ? 960  VAL A CB    1 
ATOM   7106  C  CG1   . VAL A  1  962  ? -5.816  74.433  86.242  1.00 24.46 ? 960  VAL A CG1   1 
ATOM   7107  C  CG2   . VAL A  1  962  ? -7.229  74.079  84.209  1.00 20.96 ? 960  VAL A CG2   1 
ATOM   7108  N  N     . ASP A  1  963  ? -4.444  77.666  84.920  1.00 23.89 ? 961  ASP A N     1 
ATOM   7109  C  CA    . ASP A  1  963  ? -3.517  78.628  85.516  1.00 25.29 ? 961  ASP A CA    1 
ATOM   7110  C  C     . ASP A  1  963  ? -4.247  79.895  85.934  1.00 24.93 ? 961  ASP A C     1 
ATOM   7111  O  O     . ASP A  1  963  ? -4.043  80.407  87.040  1.00 27.13 ? 961  ASP A O     1 
ATOM   7112  C  CB    . ASP A  1  963  ? -2.403  79.002  84.535  1.00 27.89 ? 961  ASP A CB    1 
ATOM   7113  C  CG    . ASP A  1  963  ? -1.377  77.917  84.352  1.00 32.44 ? 961  ASP A CG    1 
ATOM   7114  O  OD1   . ASP A  1  963  ? -1.306  77.001  85.191  1.00 37.48 ? 961  ASP A OD1   1 
ATOM   7115  O  OD2   . ASP A  1  963  ? -0.624  78.000  83.353  1.00 36.68 ? 961  ASP A OD2   1 
ATOM   7116  N  N     . ASP A  1  964  ? -5.095  80.416  85.042  1.00 24.15 ? 962  ASP A N     1 
ATOM   7117  C  CA    . ASP A  1  964  ? -5.834  81.645  85.318  1.00 28.61 ? 962  ASP A CA    1 
ATOM   7118  C  C     . ASP A  1  964  ? -6.766  81.482  86.514  1.00 30.13 ? 962  ASP A C     1 
ATOM   7119  O  O     . ASP A  1  964  ? -6.914  82.402  87.329  1.00 28.03 ? 962  ASP A O     1 
ATOM   7120  C  CB    . ASP A  1  964  ? -6.636  82.061  84.084  1.00 28.69 ? 962  ASP A CB    1 
ATOM   7121  C  CG    . ASP A  1  964  ? -5.756  82.539  82.939  1.00 31.26 ? 962  ASP A CG    1 
ATOM   7122  O  OD1   . ASP A  1  964  ? -4.552  82.778  83.164  1.00 36.80 ? 962  ASP A OD1   1 
ATOM   7123  O  OD2   . ASP A  1  964  ? -6.284  82.668  81.815  1.00 42.74 ? 962  ASP A OD2   1 
ATOM   7124  N  N     . VAL A  1  965  ? -7.430  80.333  86.622  1.00 24.59 ? 963  VAL A N     1 
ATOM   7125  C  CA    . VAL A  1  965  ? -8.286  80.096  87.780  1.00 23.62 ? 963  VAL A CA    1 
ATOM   7126  C  C     . VAL A  1  965  ? -7.446  80.091  89.048  1.00 27.02 ? 963  VAL A C     1 
ATOM   7127  O  O     . VAL A  1  965  ? -7.788  80.739  90.044  1.00 26.18 ? 963  VAL A O     1 
ATOM   7128  C  CB    . VAL A  1  965  ? -9.069  78.781  87.622  1.00 22.58 ? 963  VAL A CB    1 
ATOM   7129  C  CG1   . VAL A  1  965  ? -9.834  78.473  88.905  1.00 21.67 ? 963  VAL A CG1   1 
ATOM   7130  C  CG2   . VAL A  1  965  ? -10.024 78.860  86.430  1.00 23.09 ? 963  VAL A CG2   1 
ATOM   7131  N  N     . ASN A  1  966  ? -6.327  79.359  89.021  1.00 21.50 ? 964  ASN A N     1 
ATOM   7132  C  CA    . ASN A  1  966  ? -5.447  79.295  90.183  1.00 23.62 ? 964  ASN A CA    1 
ATOM   7133  C  C     . ASN A  1  966  ? -4.889  80.665  90.523  1.00 26.74 ? 964  ASN A C     1 
ATOM   7134  O  O     . ASN A  1  966  ? -4.614  80.947  91.697  1.00 26.28 ? 964  ASN A O     1 
ATOM   7135  C  CB    . ASN A  1  966  ? -4.288  78.322  89.937  1.00 25.06 ? 964  ASN A CB    1 
ATOM   7136  C  CG    . ASN A  1  966  ? -4.717  76.861  89.947  1.00 23.96 ? 964  ASN A CG    1 
ATOM   7137  O  OD1   . ASN A  1  966  ? -5.743  76.493  90.536  1.00 22.09 ? 964  ASN A OD1   1 
ATOM   7138  N  ND2   . ASN A  1  966  ? -3.912  76.012  89.309  1.00 24.39 ? 964  ASN A ND2   1 
ATOM   7139  N  N     . ALA A  1  967  ? -4.740  81.530  89.515  1.00 25.74 ? 965  ALA A N     1 
ATOM   7140  C  CA    . ALA A  1  967  ? -4.062  82.811  89.689  1.00 28.48 ? 965  ALA A CA    1 
ATOM   7141  C  C     . ALA A  1  967  ? -4.841  83.798  90.544  1.00 30.27 ? 965  ALA A C     1 
ATOM   7142  O  O     . ALA A  1  967  ? -4.259  84.798  90.978  1.00 31.56 ? 965  ALA A O     1 
ATOM   7143  C  CB    . ALA A  1  967  ? -3.773  83.447  88.328  1.00 32.72 ? 965  ALA A CB    1 
ATOM   7144  N  N     . THR A  1  968  ? -6.134  83.568  90.785  1.00 24.35 ? 966  THR A N     1 
ATOM   7145  C  CA    . THR A  1  968  ? -6.865  84.463  91.678  1.00 23.47 ? 966  THR A CA    1 
ATOM   7146  C  C     . THR A  1  968  ? -6.361  84.378  93.110  1.00 25.79 ? 966  THR A C     1 
ATOM   7147  O  O     . THR A  1  968  ? -6.656  85.278  93.904  1.00 28.12 ? 966  THR A O     1 
ATOM   7148  C  CB    . THR A  1  968  ? -8.359  84.156  91.698  1.00 24.55 ? 966  THR A CB    1 
ATOM   7149  O  OG1   . THR A  1  968  ? -8.569  82.894  92.343  1.00 25.24 ? 966  THR A OG1   1 
ATOM   7150  C  CG2   . THR A  1  968  ? -8.947  84.121  90.286  1.00 26.48 ? 966  THR A CG2   1 
ATOM   7151  N  N     . GLY A  1  969  ? -5.650  83.306  93.462  1.00 25.80 ? 967  GLY A N     1 
ATOM   7152  C  CA    . GLY A  1  969  ? -5.233  83.057  94.827  1.00 27.68 ? 967  GLY A CA    1 
ATOM   7153  C  C     . GLY A  1  969  ? -6.251  82.335  95.684  1.00 24.04 ? 967  GLY A C     1 
ATOM   7154  O  O     . GLY A  1  969  ? -5.902  81.875  96.781  1.00 21.47 ? 967  GLY A O     1 
ATOM   7155  N  N     . TYR A  1  970  ? -7.496  82.231  95.225  1.00 20.71 ? 968  TYR A N     1 
ATOM   7156  C  CA    . TYR A  1  970  ? -8.524  81.463  95.909  1.00 19.96 ? 968  TYR A CA    1 
ATOM   7157  C  C     . TYR A  1  970  ? -8.379  79.980  95.576  1.00 19.92 ? 968  TYR A C     1 
ATOM   7158  O  O     . TYR A  1  970  ? -7.604  79.582  94.702  1.00 24.17 ? 968  TYR A O     1 
ATOM   7159  C  CB    . TYR A  1  970  ? -9.912  81.962  95.509  1.00 19.36 ? 968  TYR A CB    1 
ATOM   7160  C  CG    . TYR A  1  970  ? -10.244 83.340  96.039  1.00 23.61 ? 968  TYR A CG    1 
ATOM   7161  C  CD1   . TYR A  1  970  ? -10.714 83.504  97.332  1.00 25.95 ? 968  TYR A CD1   1 
ATOM   7162  C  CD2   . TYR A  1  970  ? -10.115 84.462  95.236  1.00 31.85 ? 968  TYR A CD2   1 
ATOM   7163  C  CE1   . TYR A  1  970  ? -11.041 84.759  97.820  1.00 32.15 ? 968  TYR A CE1   1 
ATOM   7164  C  CE2   . TYR A  1  970  ? -10.434 85.718  95.712  1.00 27.61 ? 968  TYR A CE2   1 
ATOM   7165  C  CZ    . TYR A  1  970  ? -10.890 85.860  97.005  1.00 33.06 ? 968  TYR A CZ    1 
ATOM   7166  O  OH    . TYR A  1  970  ? -11.213 87.111  97.482  1.00 38.10 ? 968  TYR A OH    1 
ATOM   7167  N  N     . GLY A  1  971  ? -9.139  79.155  96.284  1.00 17.95 ? 969  GLY A N     1 
ATOM   7168  C  CA    . GLY A  1  971  ? -9.047  77.723  96.076  1.00 19.93 ? 969  GLY A CA    1 
ATOM   7169  C  C     . GLY A  1  971  ? -10.076 76.962  96.874  1.00 17.33 ? 969  GLY A C     1 
ATOM   7170  O  O     . GLY A  1  971  ? -9.729  76.062  97.644  1.00 18.83 ? 969  GLY A O     1 
ATOM   7171  N  N     . LEU A  1  972  ? -11.347 77.322  96.694  1.00 15.91 ? 970  LEU A N     1 
ATOM   7172  C  CA    . LEU A  1  972  ? -12.407 76.725  97.498  1.00 15.41 ? 970  LEU A CA    1 
ATOM   7173  C  C     . LEU A  1  972  ? -13.111 75.625  96.710  1.00 19.11 ? 970  LEU A C     1 
ATOM   7174  O  O     . LEU A  1  972  ? -12.722 74.465  96.816  1.00 17.98 ? 970  LEU A O     1 
ATOM   7175  C  CB    . LEU A  1  972  ? -13.384 77.798  97.978  1.00 17.94 ? 970  LEU A CB    1 
ATOM   7176  C  CG    . LEU A  1  972  ? -14.406 77.319  99.008  1.00 18.33 ? 970  LEU A CG    1 
ATOM   7177  C  CD1   . LEU A  1  972  ? -13.729 76.551  100.164 1.00 19.08 ? 970  LEU A CD1   1 
ATOM   7178  C  CD2   . LEU A  1  972  ? -15.190 78.505  99.545  1.00 19.51 ? 970  LEU A CD2   1 
ATOM   7179  N  N     . THR A  1  973  ? -14.134 75.951  95.919  1.00 16.45 ? 971  THR A N     1 
ATOM   7180  C  CA    . THR A  1  973  ? -14.786 74.933  95.111  1.00 16.42 ? 971  THR A CA    1 
ATOM   7181  C  C     . THR A  1  973  ? -14.413 75.107  93.648  1.00 16.06 ? 971  THR A C     1 
ATOM   7182  O  O     . THR A  1  973  ? -14.012 76.181  93.201  1.00 16.32 ? 971  THR A O     1 
ATOM   7183  C  CB    . THR A  1  973  ? -16.309 74.960  95.260  1.00 17.71 ? 971  THR A CB    1 
ATOM   7184  O  OG1   . THR A  1  973  ? -16.807 76.243  94.866  1.00 17.59 ? 971  THR A OG1   1 
ATOM   7185  C  CG2   . THR A  1  973  ? -16.704 74.684  96.713  1.00 16.96 ? 971  THR A CG2   1 
ATOM   7186  N  N     . PHE A  1  974  ? -14.560 74.021  92.903  1.00 15.73 ? 972  PHE A N     1 
ATOM   7187  C  CA    . PHE A  1  974  ? -14.218 74.002  91.489  1.00 15.67 ? 972  PHE A CA    1 
ATOM   7188  C  C     . PHE A  1  974  ? -15.037 72.909  90.832  1.00 15.29 ? 972  PHE A C     1 
ATOM   7189  O  O     . PHE A  1  974  ? -15.146 71.811  91.372  1.00 16.68 ? 972  PHE A O     1 
ATOM   7190  C  CB    . PHE A  1  974  ? -12.723 73.731  91.265  1.00 16.54 ? 972  PHE A CB    1 
ATOM   7191  C  CG    . PHE A  1  974  ? -12.381 73.515  89.831  1.00 15.09 ? 972  PHE A CG    1 
ATOM   7192  C  CD1   . PHE A  1  974  ? -12.193 74.596  89.003  1.00 16.19 ? 972  PHE A CD1   1 
ATOM   7193  C  CD2   . PHE A  1  974  ? -12.302 72.236  89.310  1.00 15.93 ? 972  PHE A CD2   1 
ATOM   7194  C  CE1   . PHE A  1  974  ? -11.912 74.416  87.655  1.00 19.25 ? 972  PHE A CE1   1 
ATOM   7195  C  CE2   . PHE A  1  974  ? -12.008 72.030  87.962  1.00 16.44 ? 972  PHE A CE2   1 
ATOM   7196  C  CZ    . PHE A  1  974  ? -11.810 73.121  87.136  1.00 17.55 ? 972  PHE A CZ    1 
ATOM   7197  N  N     . GLY A  1  975  ? -15.603 73.210  89.668  1.00 15.11 ? 973  GLY A N     1 
ATOM   7198  C  CA    . GLY A  1  975  ? -16.380 72.241  88.925  1.00 15.89 ? 973  GLY A CA    1 
ATOM   7199  C  C     . GLY A  1  975  ? -15.784 71.962  87.562  1.00 12.74 ? 973  GLY A C     1 
ATOM   7200  O  O     . GLY A  1  975  ? -15.205 72.839  86.929  1.00 15.08 ? 973  GLY A O     1 
ATOM   7201  N  N     . LEU A  1  976  ? -15.955 70.730  87.108  1.00 15.34 ? 974  LEU A N     1 
ATOM   7202  C  CA    . LEU A  1  976  ? -15.565 70.356  85.760  1.00 14.83 ? 974  LEU A CA    1 
ATOM   7203  C  C     . LEU A  1  976  ? -16.668 69.507  85.154  1.00 14.31 ? 974  LEU A C     1 
ATOM   7204  O  O     . LEU A  1  976  ? -17.099 68.518  85.757  1.00 17.07 ? 974  LEU A O     1 
ATOM   7205  C  CB    . LEU A  1  976  ? -14.247 69.580  85.773  1.00 16.19 ? 974  LEU A CB    1 
ATOM   7206  C  CG    . LEU A  1  976  ? -13.823 68.959  84.450  1.00 16.48 ? 974  LEU A CG    1 
ATOM   7207  C  CD1   . LEU A  1  976  ? -13.478 70.047  83.450  1.00 18.16 ? 974  LEU A CD1   1 
ATOM   7208  C  CD2   . LEU A  1  976  ? -12.632 68.074  84.732  1.00 18.40 ? 974  LEU A CD2   1 
ATOM   7209  N  N     . HIS A  1  977  ? -17.133 69.901  83.969  1.00 15.38 ? 975  HIS A N     1 
ATOM   7210  C  CA    . HIS A  1  977  ? -18.084 69.107  83.207  1.00 16.02 ? 975  HIS A CA    1 
ATOM   7211  C  C     . HIS A  1  977  ? -17.381 68.624  81.955  1.00 15.79 ? 975  HIS A C     1 
ATOM   7212  O  O     . HIS A  1  977  ? -17.064 69.415  81.058  1.00 16.91 ? 975  HIS A O     1 
ATOM   7213  C  CB    . HIS A  1  977  ? -19.328 69.914  82.853  1.00 15.80 ? 975  HIS A CB    1 
ATOM   7214  C  CG    . HIS A  1  977  ? -20.428 69.776  83.848  1.00 19.40 ? 975  HIS A CG    1 
ATOM   7215  N  ND1   . HIS A  1  977  ? -21.530 68.981  83.624  1.00 23.45 ? 975  HIS A ND1   1 
ATOM   7216  C  CD2   . HIS A  1  977  ? -20.585 70.302  85.085  1.00 26.96 ? 975  HIS A CD2   1 
ATOM   7217  C  CE1   . HIS A  1  977  ? -22.335 69.053  84.667  1.00 24.15 ? 975  HIS A CE1   1 
ATOM   7218  N  NE2   . HIS A  1  977  ? -21.783 69.843  85.568  1.00 24.04 ? 975  HIS A NE2   1 
ATOM   7219  N  N     . THR A  1  978  ? -17.123 67.328  81.918  1.00 15.86 ? 976  THR A N     1 
ATOM   7220  C  CA    . THR A  1  978  ? -16.508 66.687  80.774  1.00 16.50 ? 976  THR A CA    1 
ATOM   7221  C  C     . THR A  1  978  ? -16.813 65.210  80.887  1.00 18.03 ? 976  THR A C     1 
ATOM   7222  O  O     . THR A  1  978  ? -17.009 64.689  81.984  1.00 18.04 ? 976  THR A O     1 
ATOM   7223  C  CB    . THR A  1  978  ? -14.992 66.905  80.725  1.00 17.88 ? 976  THR A CB    1 
ATOM   7224  O  OG1   . THR A  1  978  ? -14.451 66.254  79.568  1.00 18.84 ? 976  THR A OG1   1 
ATOM   7225  C  CG2   . THR A  1  978  ? -14.325 66.307  81.941  1.00 17.49 ? 976  THR A CG2   1 
ATOM   7226  N  N     . ARG A  1  979  ? -16.837 64.544  79.743  1.00 19.40 ? 977  ARG A N     1 
ATOM   7227  C  CA    . ARG A  1  979  ? -16.925 63.096  79.712  1.00 18.06 ? 977  ARG A CA    1 
ATOM   7228  C  C     . ARG A  1  979  ? -15.568 62.438  79.540  1.00 20.25 ? 977  ARG A C     1 
ATOM   7229  O  O     . ARG A  1  979  ? -15.482 61.204  79.567  1.00 22.80 ? 977  ARG A O     1 
ATOM   7230  C  CB    . ARG A  1  979  ? -17.859 62.660  78.591  1.00 19.73 ? 977  ARG A CB    1 
ATOM   7231  C  CG    . ARG A  1  979  ? -19.285 63.053  78.855  1.00 24.98 ? 977  ARG A CG    1 
ATOM   7232  C  CD    . ARG A  1  979  ? -20.139 62.778  77.659  1.00 33.66 ? 977  ARG A CD    1 
ATOM   7233  N  NE    . ARG A  1  979  ? -21.542 63.005  77.968  1.00 40.75 ? 977  ARG A NE    1 
ATOM   7234  C  CZ    . ARG A  1  979  ? -22.538 62.733  77.140  1.00 44.80 ? 977  ARG A CZ    1 
ATOM   7235  N  NH1   . ARG A  1  979  ? -22.314 62.225  75.939  1.00 33.84 ? 977  ARG A NH1   1 
ATOM   7236  N  NH2   . ARG A  1  979  ? -23.789 62.968  77.532  1.00 43.39 ? 977  ARG A NH2   1 
ATOM   7237  N  N     . LEU A  1  980  ? -14.513 63.220  79.377  1.00 16.76 ? 978  LEU A N     1 
ATOM   7238  C  CA    . LEU A  1  980  ? -13.258 62.716  78.833  1.00 15.69 ? 978  LEU A CA    1 
ATOM   7239  C  C     . LEU A  1  980  ? -12.232 62.536  79.945  1.00 18.12 ? 978  LEU A C     1 
ATOM   7240  O  O     . LEU A  1  980  ? -11.857 63.509  80.612  1.00 18.15 ? 978  LEU A O     1 
ATOM   7241  C  CB    . LEU A  1  980  ? -12.713 63.673  77.781  1.00 17.43 ? 978  LEU A CB    1 
ATOM   7242  C  CG    . LEU A  1  980  ? -13.694 64.072  76.690  1.00 19.14 ? 978  LEU A CG    1 
ATOM   7243  C  CD1   . LEU A  1  980  ? -13.043 65.090  75.788  1.00 19.45 ? 978  LEU A CD1   1 
ATOM   7244  C  CD2   . LEU A  1  980  ? -14.129 62.828  75.911  1.00 19.69 ? 978  LEU A CD2   1 
ATOM   7245  N  N     . ASP A  1  981  ? -11.771 61.296  80.134  1.00 18.17 ? 979  ASP A N     1 
ATOM   7246  C  CA    . ASP A  1  981  ? -10.838 61.002  81.220  1.00 17.26 ? 979  ASP A CA    1 
ATOM   7247  C  C     . ASP A  1  981  ? -9.558  61.807  81.110  1.00 15.57 ? 979  ASP A C     1 
ATOM   7248  O  O     . ASP A  1  981  ? -8.976  62.185  82.136  1.00 17.47 ? 979  ASP A O     1 
ATOM   7249  C  CB    . ASP A  1  981  ? -10.490 59.513  81.243  1.00 17.14 ? 979  ASP A CB    1 
ATOM   7250  C  CG    . ASP A  1  981  ? -11.620 58.659  81.735  1.00 21.03 ? 979  ASP A CG    1 
ATOM   7251  O  OD1   . ASP A  1  981  ? -12.537 59.188  82.380  1.00 23.53 ? 979  ASP A OD1   1 
ATOM   7252  O  OD2   . ASP A  1  981  ? -11.575 57.436  81.487  1.00 23.57 ? 979  ASP A OD2   1 
ATOM   7253  N  N     . GLU A  1  982  ? -9.064  62.040  79.886  1.00 15.90 ? 980  GLU A N     1 
ATOM   7254  C  CA    . GLU A  1  982  ? -7.835  62.811  79.760  1.00 16.62 ? 980  GLU A CA    1 
ATOM   7255  C  C     . GLU A  1  982  ? -8.028  64.214  80.317  1.00 17.47 ? 980  GLU A C     1 
ATOM   7256  O  O     . GLU A  1  982  ? -7.145  64.758  80.982  1.00 18.31 ? 980  GLU A O     1 
ATOM   7257  C  CB    . GLU A  1  982  ? -7.379  62.892  78.307  1.00 18.90 ? 980  GLU A CB    1 
ATOM   7258  C  CG    . GLU A  1  982  ? -6.131  63.745  78.185  1.00 20.60 ? 980  GLU A CG    1 
ATOM   7259  C  CD    . GLU A  1  982  ? -5.827  64.184  76.767  1.00 27.92 ? 980  GLU A CD    1 
ATOM   7260  O  OE1   . GLU A  1  982  ? -6.745  64.674  76.076  1.00 29.32 ? 980  GLU A OE1   1 
ATOM   7261  O  OE2   . GLU A  1  982  ? -4.657  64.058  76.357  1.00 25.74 ? 980  GLU A OE2   1 
ATOM   7262  N  N     . THR A  1  983  ? -9.193  64.802  80.067  1.00 16.95 ? 981  THR A N     1 
ATOM   7263  C  CA    . THR A  1  983  ? -9.448  66.150  80.561  1.00 17.13 ? 981  THR A CA    1 
ATOM   7264  C  C     . THR A  1  983  ? -9.640  66.155  82.071  1.00 17.90 ? 981  THR A C     1 
ATOM   7265  O  O     . THR A  1  983  ? -9.151  67.063  82.761  1.00 17.61 ? 981  THR A O     1 
ATOM   7266  C  CB    . THR A  1  983  ? -10.660 66.729  79.834  1.00 19.61 ? 981  THR A CB    1 
ATOM   7267  O  OG1   . THR A  1  983  ? -10.347 66.851  78.439  1.00 20.77 ? 981  THR A OG1   1 
ATOM   7268  C  CG2   . THR A  1  983  ? -11.033 68.104  80.393  1.00 20.33 ? 981  THR A CG2   1 
ATOM   7269  N  N     . ILE A  1  984  ? -10.325 65.138  82.607  1.00 17.30 ? 982  ILE A N     1 
ATOM   7270  C  CA    . ILE A  1  984  ? -10.478 65.028  84.059  1.00 15.62 ? 982  ILE A CA    1 
ATOM   7271  C  C     . ILE A  1  984  ? -9.113  64.930  84.721  1.00 15.95 ? 982  ILE A C     1 
ATOM   7272  O  O     . ILE A  1  984  ? -8.827  65.619  85.710  1.00 17.56 ? 982  ILE A O     1 
ATOM   7273  C  CB    . ILE A  1  984  ? -11.355 63.820  84.425  1.00 16.70 ? 982  ILE A CB    1 
ATOM   7274  C  CG1   . ILE A  1  984  ? -12.769 64.026  83.912  1.00 18.70 ? 982  ILE A CG1   1 
ATOM   7275  C  CG2   . ILE A  1  984  ? -11.372 63.606  85.938  1.00 18.05 ? 982  ILE A CG2   1 
ATOM   7276  C  CD1   . ILE A  1  984  ? -13.655 62.782  84.027  1.00 20.21 ? 982  ILE A CD1   1 
ATOM   7277  N  N     . ALA A  1  985  ? -8.251  64.060  84.182  1.00 16.87 ? 983  ALA A N     1 
ATOM   7278  C  CA    . ALA A  1  985  ? -6.940  63.853  84.789  1.00 18.39 ? 983  ALA A CA    1 
ATOM   7279  C  C     . ALA A  1  985  ? -6.119  65.131  84.736  1.00 19.57 ? 983  ALA A C     1 
ATOM   7280  O  O     . ALA A  1  985  ? -5.525  65.541  85.737  1.00 20.22 ? 983  ALA A O     1 
ATOM   7281  C  CB    . ALA A  1  985  ? -6.211  62.710  84.084  1.00 19.40 ? 983  ALA A CB    1 
ATOM   7282  N  N     . HIS A  1  986  ? -6.099  65.780  83.573  1.00 18.63 ? 984  HIS A N     1 
ATOM   7283  C  CA    . HIS A  1  986  ? -5.365  67.027  83.397  1.00 19.10 ? 984  HIS A CA    1 
ATOM   7284  C  C     . HIS A  1  986  ? -5.872  68.091  84.359  1.00 20.62 ? 984  HIS A C     1 
ATOM   7285  O  O     . HIS A  1  986  ? -5.113  68.654  85.153  1.00 19.82 ? 984  HIS A O     1 
ATOM   7286  C  CB    . HIS A  1  986  ? -5.523  67.483  81.949  1.00 19.40 ? 984  HIS A CB    1 
ATOM   7287  C  CG    . HIS A  1  986  ? -4.974  68.844  81.664  1.00 17.68 ? 984  HIS A CG    1 
ATOM   7288  N  ND1   . HIS A  1  986  ? -5.203  69.487  80.467  1.00 27.87 ? 984  HIS A ND1   1 
ATOM   7289  C  CD2   . HIS A  1  986  ? -4.218  69.687  82.406  1.00 22.15 ? 984  HIS A CD2   1 
ATOM   7290  C  CE1   . HIS A  1  986  ? -4.606  70.665  80.482  1.00 30.35 ? 984  HIS A CE1   1 
ATOM   7291  N  NE2   . HIS A  1  986  ? -4.011  70.815  81.650  1.00 21.33 ? 984  HIS A NE2   1 
ATOM   7292  N  N     . VAL A  1  987  ? -7.168  68.380  84.298  1.00 18.62 ? 985  VAL A N     1 
ATOM   7293  C  CA    . VAL A  1  987  ? -7.689  69.511  85.051  1.00 17.21 ? 985  VAL A CA    1 
ATOM   7294  C  C     . VAL A  1  987  ? -7.602  69.258  86.545  1.00 19.24 ? 985  VAL A C     1 
ATOM   7295  O  O     . VAL A  1  987  ? -7.211  70.148  87.307  1.00 19.67 ? 985  VAL A O     1 
ATOM   7296  C  CB    . VAL A  1  987  ? -9.124  69.821  84.608  1.00 15.47 ? 985  VAL A CB    1 
ATOM   7297  C  CG1   . VAL A  1  987  ? -9.748  70.860  85.524  1.00 16.10 ? 985  VAL A CG1   1 
ATOM   7298  C  CG2   . VAL A  1  987  ? -9.111  70.341  83.176  1.00 20.11 ? 985  VAL A CG2   1 
ATOM   7299  N  N     . THR A  1  988  ? -7.975  68.062  87.002  1.00 17.74 ? 986  THR A N     1 
ATOM   7300  C  CA    . THR A  1  988  ? -7.933  67.841  88.447  1.00 18.41 ? 986  THR A CA    1 
ATOM   7301  C  C     . THR A  1  988  ? -6.505  67.768  88.968  1.00 25.24 ? 986  THR A C     1 
ATOM   7302  O  O     . THR A  1  988  ? -6.274  68.076  90.143  1.00 24.09 ? 986  THR A O     1 
ATOM   7303  C  CB    . THR A  1  988  ? -8.699  66.574  88.858  1.00 20.83 ? 986  THR A CB    1 
ATOM   7304  O  OG1   . THR A  1  988  ? -8.102  65.428  88.253  1.00 21.80 ? 986  THR A OG1   1 
ATOM   7305  C  CG2   . THR A  1  988  ? -10.175 66.663  88.434  1.00 21.98 ? 986  THR A CG2   1 
ATOM   7306  N  N     . SER A  1  989  ? -5.541  67.415  88.126  1.00 19.05 ? 987  SER A N     1 
ATOM   7307  C  CA    . SER A  1  989  ? -4.160  67.407  88.593  1.00 22.87 ? 987  SER A CA    1 
ATOM   7308  C  C     . SER A  1  989  ? -3.579  68.810  88.700  1.00 26.40 ? 987  SER A C     1 
ATOM   7309  O  O     . SER A  1  989  ? -2.673  69.030  89.508  1.00 31.87 ? 987  SER A O     1 
ATOM   7310  C  CB    . SER A  1  989  ? -3.277  66.537  87.685  1.00 22.07 ? 987  SER A CB    1 
ATOM   7311  O  OG    . SER A  1  989  ? -3.131  67.081  86.393  1.00 32.97 ? 987  SER A OG    1 
ATOM   7312  N  N     . ARG A  1  990  ? -4.097  69.765  87.933  1.00 19.51 ? 988  ARG A N     1 
ATOM   7313  C  CA    . ARG A  1  990  ? -3.508  71.099  87.869  1.00 21.94 ? 988  ARG A CA    1 
ATOM   7314  C  C     . ARG A  1  990  ? -4.265  72.136  88.680  1.00 19.93 ? 988  ARG A C     1 
ATOM   7315  O  O     . ARG A  1  990  ? -3.652  73.110  89.139  1.00 22.62 ? 988  ARG A O     1 
ATOM   7316  C  CB    . ARG A  1  990  ? -3.418  71.570  86.414  1.00 22.66 ? 988  ARG A CB    1 
ATOM   7317  C  CG    . ARG A  1  990  ? -2.651  70.611  85.512  1.00 34.76 ? 988  ARG A CG    1 
ATOM   7318  C  CD    . ARG A  1  990  ? -1.158  70.802  85.625  1.00 36.40 ? 988  ARG A CD    1 
ATOM   7319  N  NE    . ARG A  1  990  ? -0.660  71.679  84.574  1.00 33.71 ? 988  ARG A NE    1 
ATOM   7320  C  CZ    . ARG A  1  990  ? 0.589   72.117  84.498  1.00 31.47 ? 988  ARG A CZ    1 
ATOM   7321  N  NH1   . ARG A  1  990  ? 1.477   71.839  85.441  1.00 31.01 ? 988  ARG A NH1   1 
ATOM   7322  N  NH2   . ARG A  1  990  ? 0.959   72.842  83.447  1.00 29.31 ? 988  ARG A NH2   1 
ATOM   7323  N  N     . ILE A  1  991  ? -5.576  71.951  88.867  1.00 18.98 ? 989  ILE A N     1 
ATOM   7324  C  CA    . ILE A  1  991  ? -6.360  72.875  89.676  1.00 17.85 ? 989  ILE A CA    1 
ATOM   7325  C  C     . ILE A  1  991  ? -5.910  72.771  91.123  1.00 20.74 ? 989  ILE A C     1 
ATOM   7326  O  O     . ILE A  1  991  ? -5.487  71.709  91.597  1.00 21.52 ? 989  ILE A O     1 
ATOM   7327  C  CB    . ILE A  1  991  ? -7.866  72.580  89.540  1.00 17.63 ? 989  ILE A CB    1 
ATOM   7328  C  CG1   . ILE A  1  991  ? -8.697  73.736  90.095  1.00 22.15 ? 989  ILE A CG1   1 
ATOM   7329  C  CG2   . ILE A  1  991  ? -8.235  71.281  90.248  1.00 22.89 ? 989  ILE A CG2   1 
ATOM   7330  C  CD1   . ILE A  1  991  ? -8.646  74.963  89.226  1.00 23.83 ? 989  ILE A CD1   1 
ATOM   7331  N  N     . LYS A  1  992  ? -5.974  73.894  91.829  1.00 19.09 ? 990  LYS A N     1 
ATOM   7332  C  CA    . LYS A  1  992  ? -5.583  73.973  93.232  1.00 19.22 ? 990  LYS A CA    1 
ATOM   7333  C  C     . LYS A  1  992  ? -6.783  74.487  94.015  1.00 17.81 ? 990  LYS A C     1 
ATOM   7334  O  O     . LYS A  1  992  ? -6.904  75.681  94.297  1.00 23.93 ? 990  LYS A O     1 
ATOM   7335  C  CB    . LYS A  1  992  ? -4.367  74.859  93.401  1.00 19.44 ? 990  LYS A CB    1 
ATOM   7336  C  CG    . LYS A  1  992  ? -3.129  74.267  92.749  1.00 23.43 ? 990  LYS A CG    1 
ATOM   7337  C  CD    . LYS A  1  992  ? -1.982  75.285  92.593  1.00 37.85 ? 990  LYS A CD    1 
ATOM   7338  C  CE    . LYS A  1  992  ? -2.232  76.584  93.345  1.00 41.68 ? 990  LYS A CE    1 
ATOM   7339  N  NZ    . LYS A  1  992  ? -1.019  77.455  93.344  1.00 53.54 ? 990  LYS A NZ    1 
ATOM   7340  N  N     . ALA A  1  993  ? -7.688  73.576  94.344  1.00 20.66 ? 991  ALA A N     1 
ATOM   7341  C  CA    . ALA A  1  993  ? -8.870  73.924  95.119  1.00 18.75 ? 991  ALA A CA    1 
ATOM   7342  C  C     . ALA A  1  993  ? -9.190  72.783  96.063  1.00 19.10 ? 991  ALA A C     1 
ATOM   7343  O  O     . ALA A  1  993  ? -8.846  71.632  95.797  1.00 20.43 ? 991  ALA A O     1 
ATOM   7344  C  CB    . ALA A  1  993  ? -10.071 74.211  94.215  1.00 18.60 ? 991  ALA A CB    1 
ATOM   7345  N  N     . GLY A  1  994  ? -9.880  73.110  97.156  1.00 18.87 ? 992  GLY A N     1 
ATOM   7346  C  CA    . GLY A  1  994  ? -10.122 72.128  98.191  1.00 17.61 ? 992  GLY A CA    1 
ATOM   7347  C  C     . GLY A  1  994  ? -11.288 71.209  97.918  1.00 15.68 ? 992  GLY A C     1 
ATOM   7348  O  O     . GLY A  1  994  ? -11.313 70.088  98.422  1.00 16.20 ? 992  GLY A O     1 
ATOM   7349  N  N     . ASN A  1  995  ? -12.265 71.650  97.129  1.00 16.57 ? 993  ASN A N     1 
ATOM   7350  C  CA    . ASN A  1  995  ? -13.472 70.862  96.881  1.00 17.49 ? 993  ASN A CA    1 
ATOM   7351  C  C     . ASN A  1  995  ? -13.731 70.816  95.387  1.00 16.95 ? 993  ASN A C     1 
ATOM   7352  O  O     . ASN A  1  995  ? -14.121 71.826  94.790  1.00 17.04 ? 993  ASN A O     1 
ATOM   7353  C  CB    . ASN A  1  995  ? -14.673 71.436  97.620  1.00 17.74 ? 993  ASN A CB    1 
ATOM   7354  C  CG    . ASN A  1  995  ? -14.702 70.983  99.061  1.00 18.22 ? 993  ASN A CG    1 
ATOM   7355  O  OD1   . ASN A  1  995  ? -14.033 71.566  99.904  1.00 18.67 ? 993  ASN A OD1   1 
ATOM   7356  N  ND2   . ASN A  1  995  ? -15.428 69.907  99.335  1.00 17.74 ? 993  ASN A ND2   1 
ATOM   7357  N  N     . LEU A  1  996  ? -13.496 69.654  94.792  1.00 16.32 ? 994  LEU A N     1 
ATOM   7358  C  CA    . LEU A  1  996  ? -13.677 69.479  93.359  1.00 14.62 ? 994  LEU A CA    1 
ATOM   7359  C  C     . LEU A  1  996  ? -14.965 68.727  93.094  1.00 15.00 ? 994  LEU A C     1 
ATOM   7360  O  O     . LEU A  1  996  ? -15.338 67.827  93.850  1.00 15.27 ? 994  LEU A O     1 
ATOM   7361  C  CB    . LEU A  1  996  ? -12.509 68.705  92.746  1.00 15.20 ? 994  LEU A CB    1 
ATOM   7362  C  CG    . LEU A  1  996  ? -11.122 69.170  93.185  1.00 17.86 ? 994  LEU A CG    1 
ATOM   7363  C  CD1   . LEU A  1  996  ? -10.068 68.338  92.466  1.00 20.51 ? 994  LEU A CD1   1 
ATOM   7364  C  CD2   . LEU A  1  996  ? -10.932 70.662  92.905  1.00 18.95 ? 994  LEU A CD2   1 
ATOM   7365  N  N     . TYR A  1  997  ? -15.629 69.092  92.000  1.00 14.94 ? 995  TYR A N     1 
ATOM   7366  C  CA    . TYR A  1  997  ? -16.902 68.480  91.638  1.00 14.94 ? 995  TYR A CA    1 
ATOM   7367  C  C     . TYR A  1  997  ? -16.868 68.176  90.155  1.00 14.98 ? 995  TYR A C     1 
ATOM   7368  O  O     . TYR A  1  997  ? -16.584 69.067  89.356  1.00 15.81 ? 995  TYR A O     1 
ATOM   7369  C  CB    . TYR A  1  997  ? -18.071 69.416  91.965  1.00 16.33 ? 995  TYR A CB    1 
ATOM   7370  C  CG    . TYR A  1  997  ? -18.182 69.694  93.443  1.00 16.17 ? 995  TYR A CG    1 
ATOM   7371  C  CD1   . TYR A  1  997  ? -18.823 68.794  94.285  1.00 17.21 ? 995  TYR A CD1   1 
ATOM   7372  C  CD2   . TYR A  1  997  ? -17.611 70.831  93.992  1.00 16.19 ? 995  TYR A CD2   1 
ATOM   7373  C  CE1   . TYR A  1  997  ? -18.928 69.043  95.643  1.00 17.95 ? 995  TYR A CE1   1 
ATOM   7374  C  CE2   . TYR A  1  997  ? -17.719 71.089  95.352  1.00 17.04 ? 995  TYR A CE2   1 
ATOM   7375  C  CZ    . TYR A  1  997  ? -18.373 70.189  96.164  1.00 22.10 ? 995  TYR A CZ    1 
ATOM   7376  O  OH    . TYR A  1  997  ? -18.476 70.430  97.522  1.00 20.58 ? 995  TYR A OH    1 
ATOM   7377  N  N     . ILE A  1  998  ? -17.131 66.928  89.788  1.00 14.82 ? 996  ILE A N     1 
ATOM   7378  C  CA    A ILE A  1  998  ? -17.053 66.486  88.399  0.50 16.29 ? 996  ILE A CA    1 
ATOM   7379  C  CA    B ILE A  1  998  ? -17.057 66.493  88.398  0.50 16.29 ? 996  ILE A CA    1 
ATOM   7380  C  C     . ILE A  1  998  ? -18.452 66.094  87.945  1.00 15.35 ? 996  ILE A C     1 
ATOM   7381  O  O     . ILE A  1  998  ? -19.062 65.182  88.513  1.00 16.03 ? 996  ILE A O     1 
ATOM   7382  C  CB    A ILE A  1  998  ? -16.071 65.319  88.226  0.50 15.59 ? 996  ILE A CB    1 
ATOM   7383  C  CB    B ILE A  1  998  ? -16.060 65.342  88.212  0.50 15.60 ? 996  ILE A CB    1 
ATOM   7384  C  CG1   A ILE A  1  998  ? -14.717 65.673  88.844  0.50 19.23 ? 996  ILE A CG1   1 
ATOM   7385  C  CG1   B ILE A  1  998  ? -14.658 65.824  88.579  0.50 18.56 ? 996  ILE A CG1   1 
ATOM   7386  C  CG2   A ILE A  1  998  ? -15.920 64.974  86.731  0.50 15.48 ? 996  ILE A CG2   1 
ATOM   7387  C  CG2   B ILE A  1  998  ? -16.094 64.838  86.760  0.50 15.47 ? 996  ILE A CG2   1 
ATOM   7388  C  CD1   A ILE A  1  998  ? -14.043 66.847  88.194  0.50 19.11 ? 996  ILE A CD1   1 
ATOM   7389  C  CD1   B ILE A  1  998  ? -13.610 64.754  88.474  0.50 18.77 ? 996  ILE A CD1   1 
ATOM   7390  N  N     . ASN A  1  999  ? -18.957 66.798  86.925  1.00 14.71 ? 997  ASN A N     1 
ATOM   7391  C  CA    . ASN A  1  999  ? -20.246 66.503  86.287  1.00 14.83 ? 997  ASN A CA    1 
ATOM   7392  C  C     . ASN A  1  999  ? -21.423 66.627  87.250  1.00 14.43 ? 997  ASN A C     1 
ATOM   7393  O  O     . ASN A  1  999  ? -22.392 65.874  87.169  1.00 15.96 ? 997  ASN A O     1 
ATOM   7394  C  CB    . ASN A  1  999  ? -20.208 65.127  85.630  1.00 15.14 ? 997  ASN A CB    1 
ATOM   7395  C  CG    . ASN A  1  999  ? -19.251 65.097  84.465  1.00 17.81 ? 997  ASN A CG    1 
ATOM   7396  O  OD1   . ASN A  1  999  ? -19.081 66.105  83.792  1.00 17.59 ? 997  ASN A OD1   1 
ATOM   7397  N  ND2   . ASN A  1  999  ? -18.622 63.951  84.215  1.00 17.02 ? 997  ASN A ND2   1 
ATOM   7398  N  N     . ARG A  1  1000 ? -21.348 67.608  88.147  1.00 15.09 ? 998  ARG A N     1 
ATOM   7399  C  CA    . ARG A  1  1000 ? -22.437 67.920  89.068  1.00 15.90 ? 998  ARG A CA    1 
ATOM   7400  C  C     . ARG A  1  1000 ? -22.289 69.380  89.470  1.00 18.21 ? 998  ARG A C     1 
ATOM   7401  O  O     . ARG A  1  1000 ? -21.365 70.068  89.032  1.00 18.04 ? 998  ARG A O     1 
ATOM   7402  C  CB    . ARG A  1  1000 ? -22.429 66.994  90.282  1.00 16.28 ? 998  ARG A CB    1 
ATOM   7403  C  CG    . ARG A  1  1000 ? -21.043 66.849  90.909  1.00 17.14 ? 998  ARG A CG    1 
ATOM   7404  C  CD    . ARG A  1  1000 ? -21.148 66.511  92.390  1.00 16.68 ? 998  ARG A CD    1 
ATOM   7405  N  NE    . ARG A  1  1000 ? -21.744 67.616  93.122  1.00 15.96 ? 998  ARG A NE    1 
ATOM   7406  C  CZ    . ARG A  1  1000 ? -21.961 67.608  94.429  1.00 17.28 ? 998  ARG A CZ    1 
ATOM   7407  N  NH1   . ARG A  1  1000 ? -21.662 66.552  95.174  1.00 18.71 ? 998  ARG A NH1   1 
ATOM   7408  N  NH2   . ARG A  1  1000 ? -22.478 68.685  95.006  1.00 16.29 ? 998  ARG A NH2   1 
ATOM   7409  N  N     . ASN A  1  1001 ? -23.213 69.859  90.304  1.00 17.71 ? 999  ASN A N     1 
ATOM   7410  C  CA    . ASN A  1  1001 ? -23.057 71.225  90.787  1.00 16.18 ? 999  ASN A CA    1 
ATOM   7411  C  C     . ASN A  1  1001 ? -21.913 71.273  91.804  1.00 18.26 ? 999  ASN A C     1 
ATOM   7412  O  O     . ASN A  1  1001 ? -21.353 70.243  92.193  1.00 16.20 ? 999  ASN A O     1 
ATOM   7413  C  CB    . ASN A  1  1001 ? -24.388 71.760  91.351  1.00 16.34 ? 999  ASN A CB    1 
ATOM   7414  C  CG    . ASN A  1  1001 ? -24.812 71.093  92.647  1.00 21.07 ? 999  ASN A CG    1 
ATOM   7415  O  OD1   . ASN A  1  1001 ? -24.004 70.847  93.534  1.00 19.33 ? 999  ASN A OD1   1 
ATOM   7416  N  ND2   . ASN A  1  1001 ? -26.106 70.830  92.775  1.00 22.11 ? 999  ASN A ND2   1 
ATOM   7417  N  N     . ILE A  1  1002 ? -21.553 72.480  92.231  1.00 14.48 ? 1000 ILE A N     1 
ATOM   7418  C  CA    . ILE A  1  1002 ? -20.391 72.661  93.103  1.00 15.40 ? 1000 ILE A CA    1 
ATOM   7419  C  C     . ILE A  1  1002 ? -20.796 73.129  94.497  1.00 16.85 ? 1000 ILE A C     1 
ATOM   7420  O  O     . ILE A  1  1002 ? -19.953 73.615  95.256  1.00 18.43 ? 1000 ILE A O     1 
ATOM   7421  C  CB    . ILE A  1  1002 ? -19.351 73.611  92.477  1.00 14.52 ? 1000 ILE A CB    1 
ATOM   7422  C  CG1   . ILE A  1  1002 ? -19.870 75.053  92.386  1.00 16.09 ? 1000 ILE A CG1   1 
ATOM   7423  C  CG2   . ILE A  1  1002 ? -18.921 73.090  91.116  1.00 15.30 ? 1000 ILE A CG2   1 
ATOM   7424  C  CD1   . ILE A  1  1002 ? -18.794 76.051  91.937  1.00 17.50 ? 1000 ILE A CD1   1 
ATOM   7425  N  N     . ILE A  1  1003 ? -22.065 72.976  94.863  1.00 16.38 ? 1001 ILE A N     1 
ATOM   7426  C  CA    . ILE A  1  1003 ? -22.564 73.506  96.126  1.00 17.70 ? 1001 ILE A CA    1 
ATOM   7427  C  C     . ILE A  1  1003 ? -23.121 72.378  96.987  1.00 18.72 ? 1001 ILE A C     1 
ATOM   7428  O  O     . ILE A  1  1003 ? -23.271 71.240  96.558  1.00 19.55 ? 1001 ILE A O     1 
ATOM   7429  C  CB    . ILE A  1  1003 ? -23.633 74.593  95.924  1.00 16.98 ? 1001 ILE A CB    1 
ATOM   7430  C  CG1   . ILE A  1  1003 ? -24.869 74.030  95.213  1.00 18.18 ? 1001 ILE A CG1   1 
ATOM   7431  C  CG2   . ILE A  1  1003 ? -23.051 75.791  95.204  1.00 16.70 ? 1001 ILE A CG2   1 
ATOM   7432  C  CD1   . ILE A  1  1003 ? -26.094 74.977  95.304  1.00 19.04 ? 1001 ILE A CD1   1 
ATOM   7433  N  N     . GLY A  1  1004 ? -23.440 72.725  98.226  1.00 18.80 ? 1002 GLY A N     1 
ATOM   7434  C  CA    . GLY A  1  1004 ? -24.066 71.766  99.115  1.00 18.81 ? 1002 GLY A CA    1 
ATOM   7435  C  C     . GLY A  1  1004 ? -23.153 70.649  99.569  1.00 20.93 ? 1002 GLY A C     1 
ATOM   7436  O  O     . GLY A  1  1004 ? -23.591 69.492  99.649  1.00 21.57 ? 1002 GLY A O     1 
ATOM   7437  N  N     . ALA A  1  1005 ? -21.895 70.964  99.867  1.00 17.79 ? 1003 ALA A N     1 
ATOM   7438  C  CA    . ALA A  1  1005 ? -20.984 69.969  100.406 1.00 19.51 ? 1003 ALA A CA    1 
ATOM   7439  C  C     . ALA A  1  1005 ? -21.612 69.293  101.617 1.00 19.99 ? 1003 ALA A C     1 
ATOM   7440  O  O     . ALA A  1  1005 ? -22.249 69.945  102.451 1.00 22.71 ? 1003 ALA A O     1 
ATOM   7441  C  CB    . ALA A  1  1005 ? -19.657 70.620  100.806 1.00 21.22 ? 1003 ALA A CB    1 
ATOM   7442  N  N     . VAL A  1  1006 ? -21.429 67.977  101.693 1.00 19.08 ? 1004 VAL A N     1 
ATOM   7443  C  CA    . VAL A  1  1006 ? -22.054 67.131  102.700 1.00 18.21 ? 1004 VAL A CA    1 
ATOM   7444  C  C     . VAL A  1  1006 ? -21.007 66.726  103.725 1.00 18.86 ? 1004 VAL A C     1 
ATOM   7445  O  O     . VAL A  1  1006 ? -19.948 66.208  103.366 1.00 17.66 ? 1004 VAL A O     1 
ATOM   7446  C  CB    . VAL A  1  1006 ? -22.696 65.890  102.059 1.00 18.45 ? 1004 VAL A CB    1 
ATOM   7447  C  CG1   . VAL A  1  1006 ? -23.213 64.940  103.123 1.00 21.77 ? 1004 VAL A CG1   1 
ATOM   7448  C  CG2   . VAL A  1  1006 ? -23.824 66.313  101.134 1.00 21.18 ? 1004 VAL A CG2   1 
ATOM   7449  N  N     . VAL A  1  1007 ? -21.321 66.958  105.000 1.00 17.05 ? 1005 VAL A N     1 
ATOM   7450  C  CA    . VAL A  1  1007 ? -20.432 66.623  106.099 1.00 16.04 ? 1005 VAL A CA    1 
ATOM   7451  C  C     . VAL A  1  1007 ? -19.984 65.178  105.980 1.00 18.77 ? 1005 VAL A C     1 
ATOM   7452  O  O     . VAL A  1  1007 ? -20.807 64.279  105.784 1.00 17.40 ? 1005 VAL A O     1 
ATOM   7453  C  CB    . VAL A  1  1007 ? -21.160 66.864  107.432 1.00 16.67 ? 1005 VAL A CB    1 
ATOM   7454  C  CG1   . VAL A  1  1007 ? -20.284 66.423  108.592 1.00 19.35 ? 1005 VAL A CG1   1 
ATOM   7455  C  CG2   . VAL A  1  1007 ? -21.533 68.317  107.572 1.00 21.34 ? 1005 VAL A CG2   1 
ATOM   7456  N  N     . GLY A  1  1008 ? -18.674 64.949  106.115 1.00 17.72 ? 1006 GLY A N     1 
ATOM   7457  C  CA    . GLY A  1  1008 ? -18.121 63.601  106.121 1.00 18.32 ? 1006 GLY A CA    1 
ATOM   7458  C  C     . GLY A  1  1008 ? -18.141 62.903  104.784 1.00 18.63 ? 1006 GLY A C     1 
ATOM   7459  O  O     . GLY A  1  1008 ? -17.688 61.755  104.687 1.00 19.65 ? 1006 GLY A O     1 
ATOM   7460  N  N     . VAL A  1  1009 ? -18.664 63.554  103.755 1.00 17.16 ? 1007 VAL A N     1 
ATOM   7461  C  CA    . VAL A  1  1009 ? -18.737 63.003  102.409 1.00 18.89 ? 1007 VAL A CA    1 
ATOM   7462  C  C     . VAL A  1  1009 ? -17.948 63.857  101.432 1.00 18.60 ? 1007 VAL A C     1 
ATOM   7463  O  O     . VAL A  1  1009 ? -17.132 63.345  100.665 1.00 18.20 ? 1007 VAL A O     1 
ATOM   7464  C  CB    . VAL A  1  1009 ? -20.198 62.849  101.941 1.00 19.52 ? 1007 VAL A CB    1 
ATOM   7465  C  CG1   . VAL A  1  1009 ? -20.226 62.226  100.549 1.00 18.36 ? 1007 VAL A CG1   1 
ATOM   7466  C  CG2   . VAL A  1  1009 ? -20.984 61.978  102.915 1.00 18.40 ? 1007 VAL A CG2   1 
ATOM   7467  N  N     . GLN A  1  1010 ? -18.188 65.176  101.442 1.00 18.00 ? 1008 GLN A N     1 
ATOM   7468  C  CA    . GLN A  1  1010 ? -17.269 66.158  100.875 1.00 16.37 ? 1008 GLN A CA    1 
ATOM   7469  C  C     . GLN A  1  1010 ? -16.838 67.065  102.018 1.00 17.05 ? 1008 GLN A C     1 
ATOM   7470  O  O     . GLN A  1  1010 ? -17.408 68.150  102.209 1.00 19.28 ? 1008 GLN A O     1 
ATOM   7471  C  CB    . GLN A  1  1010 ? -17.900 66.971  99.747  1.00 18.36 ? 1008 GLN A CB    1 
ATOM   7472  C  CG    . GLN A  1  1010 ? -18.459 66.129  98.619  1.00 18.81 ? 1008 GLN A CG    1 
ATOM   7473  C  CD    . GLN A  1  1010 ? -19.947 65.891  98.737  1.00 19.50 ? 1008 GLN A CD    1 
ATOM   7474  O  OE1   . GLN A  1  1010 ? -20.684 66.708  99.316  1.00 19.93 ? 1008 GLN A OE1   1 
ATOM   7475  N  NE2   . GLN A  1  1010 ? -20.413 64.780  98.169  1.00 18.12 ? 1008 GLN A NE2   1 
ATOM   7476  N  N     . PRO A  1  1011 ? -15.886 66.621  102.834 1.00 16.53 ? 1009 PRO A N     1 
ATOM   7477  C  CA    . PRO A  1  1011 ? -15.256 67.517  103.814 1.00 19.38 ? 1009 PRO A CA    1 
ATOM   7478  C  C     . PRO A  1  1011 ? -14.887 68.817  103.137 1.00 17.48 ? 1009 PRO A C     1 
ATOM   7479  O  O     . PRO A  1  1011 ? -14.324 68.823  102.046 1.00 16.22 ? 1009 PRO A O     1 
ATOM   7480  C  CB    . PRO A  1  1011 ? -14.014 66.739  104.244 1.00 19.32 ? 1009 PRO A CB    1 
ATOM   7481  C  CG    . PRO A  1  1011 ? -14.411 65.308  104.091 1.00 18.60 ? 1009 PRO A CG    1 
ATOM   7482  C  CD    . PRO A  1  1011 ? -15.268 65.288  102.836 1.00 17.30 ? 1009 PRO A CD    1 
ATOM   7483  N  N     . PHE A  1  1012 ? -15.232 69.925  103.770 1.00 17.52 ? 1010 PHE A N     1 
ATOM   7484  C  CA    . PHE A  1  1012 ? -15.341 71.185  103.058 1.00 17.17 ? 1010 PHE A CA    1 
ATOM   7485  C  C     . PHE A  1  1012 ? -14.285 72.177  103.513 1.00 17.54 ? 1010 PHE A C     1 
ATOM   7486  O  O     . PHE A  1  1012 ? -14.120 72.419  104.715 1.00 19.12 ? 1010 PHE A O     1 
ATOM   7487  C  CB    . PHE A  1  1012 ? -16.726 71.809  103.238 1.00 16.88 ? 1010 PHE A CB    1 
ATOM   7488  C  CG    . PHE A  1  1012 ? -16.918 73.029  102.394 1.00 16.90 ? 1010 PHE A CG    1 
ATOM   7489  C  CD1   . PHE A  1  1012 ? -17.127 72.915  101.023 1.00 19.47 ? 1010 PHE A CD1   1 
ATOM   7490  C  CD2   . PHE A  1  1012 ? -16.828 74.300  102.956 1.00 20.04 ? 1010 PHE A CD2   1 
ATOM   7491  C  CE1   . PHE A  1  1012 ? -17.268 74.039  100.230 1.00 20.51 ? 1010 PHE A CE1   1 
ATOM   7492  C  CE2   . PHE A  1  1012 ? -16.980 75.436  102.171 1.00 16.74 ? 1010 PHE A CE2   1 
ATOM   7493  C  CZ    . PHE A  1  1012 ? -17.216 75.313  100.809 1.00 17.23 ? 1010 PHE A CZ    1 
ATOM   7494  N  N     . GLY A  1  1013 ? -13.614 72.777  102.562 1.00 16.22 ? 1011 GLY A N     1 
ATOM   7495  C  CA    . GLY A  1  1013 ? -12.683 73.836  102.887 1.00 20.26 ? 1011 GLY A CA    1 
ATOM   7496  C  C     . GLY A  1  1013 ? -11.593 73.881  101.851 1.00 18.75 ? 1011 GLY A C     1 
ATOM   7497  O  O     . GLY A  1  1013 ? -11.216 72.873  101.257 1.00 20.16 ? 1011 GLY A O     1 
ATOM   7498  N  N     . GLY A  1  1014 ? -11.060 75.079  101.651 1.00 18.20 ? 1012 GLY A N     1 
ATOM   7499  C  CA    . GLY A  1  1014 ? -10.103 75.306  100.601 1.00 21.62 ? 1012 GLY A CA    1 
ATOM   7500  C  C     . GLY A  1  1014 ? -8.768  75.819  101.081 1.00 23.46 ? 1012 GLY A C     1 
ATOM   7501  O  O     . GLY A  1  1014 ? -8.422  75.727  102.266 1.00 23.20 ? 1012 GLY A O     1 
ATOM   7502  N  N     . ARG A  1  1015 ? -8.017  76.381  100.145 1.00 18.40 ? 1013 ARG A N     1 
ATOM   7503  C  CA    . ARG A  1  1015 ? -6.632  76.750  100.351 1.00 18.89 ? 1013 ARG A CA    1 
ATOM   7504  C  C     . ARG A  1  1015 ? -6.434  78.172  99.869  1.00 20.75 ? 1013 ARG A C     1 
ATOM   7505  O  O     . ARG A  1  1015 ? -7.352  78.799  99.332  1.00 19.83 ? 1013 ARG A O     1 
ATOM   7506  C  CB    . ARG A  1  1015 ? -5.706  75.804  99.591  1.00 19.53 ? 1013 ARG A CB    1 
ATOM   7507  C  CG    . ARG A  1  1015 ? -5.990  75.819  98.107  1.00 20.16 ? 1013 ARG A CG    1 
ATOM   7508  C  CD    . ARG A  1  1015 ? -4.930  75.082  97.313  1.00 24.97 ? 1013 ARG A CD    1 
ATOM   7509  N  NE    . ARG A  1  1015 ? -3.607  75.250  97.899  1.00 29.45 ? 1013 ARG A NE    1 
ATOM   7510  C  CZ    . ARG A  1  1015 ? -2.855  76.327  97.742  1.00 34.14 ? 1013 ARG A CZ    1 
ATOM   7511  N  NH1   . ARG A  1  1015 ? -3.256  77.344  96.993  1.00 31.87 ? 1013 ARG A NH1   1 
ATOM   7512  N  NH2   . ARG A  1  1015 ? -1.680  76.392  98.366  1.00 26.19 ? 1013 ARG A NH2   1 
ATOM   7513  N  N     . GLY A  1  1016 ? -5.211  78.665  100.044 1.00 22.13 ? 1014 GLY A N     1 
ATOM   7514  C  CA    . GLY A  1  1016 ? -4.901  80.005  99.579  1.00 19.77 ? 1014 GLY A CA    1 
ATOM   7515  C  C     . GLY A  1  1016 ? -5.772  81.014  100.298 1.00 22.56 ? 1014 GLY A C     1 
ATOM   7516  O  O     . GLY A  1  1016 ? -5.968  80.948  101.517 1.00 21.56 ? 1014 GLY A O     1 
ATOM   7517  N  N     . LEU A  1  1017 ? -6.339  81.946  99.537  1.00 19.75 ? 1015 LEU A N     1 
ATOM   7518  C  CA    . LEU A  1  1017 ? -7.216  82.961  100.116 1.00 18.85 ? 1015 LEU A CA    1 
ATOM   7519  C  C     . LEU A  1  1017 ? -8.533  82.392  100.614 1.00 19.87 ? 1015 LEU A C     1 
ATOM   7520  O  O     . LEU A  1  1017 ? -9.317  83.131  101.213 1.00 21.21 ? 1015 LEU A O     1 
ATOM   7521  C  CB    . LEU A  1  1017 ? -7.514  84.052  99.085  1.00 20.76 ? 1015 LEU A CB    1 
ATOM   7522  C  CG    . LEU A  1  1017 ? -6.332  84.826  98.513  1.00 24.87 ? 1015 LEU A CG    1 
ATOM   7523  C  CD1   . LEU A  1  1017 ? -6.804  85.730  97.370  1.00 25.53 ? 1015 LEU A CD1   1 
ATOM   7524  C  CD2   . LEU A  1  1017 ? -5.660  85.646  99.612  1.00 24.44 ? 1015 LEU A CD2   1 
ATOM   7525  N  N     . SER A  1  1018 ? -8.789  81.106  100.393 1.00 17.88 ? 1016 SER A N     1 
ATOM   7526  C  CA    . SER A  1  1018 ? -10.044 80.498  100.799 1.00 18.30 ? 1016 SER A CA    1 
ATOM   7527  C  C     . SER A  1  1018 ? -9.988  79.845  102.167 1.00 20.03 ? 1016 SER A C     1 
ATOM   7528  O  O     . SER A  1  1018 ? -11.032 79.448  102.679 1.00 20.51 ? 1016 SER A O     1 
ATOM   7529  C  CB    . SER A  1  1018 ? -10.478 79.445  99.774  1.00 18.19 ? 1016 SER A CB    1 
ATOM   7530  O  OG    . SER A  1  1018 ? -10.704 80.080  98.528  1.00 17.89 ? 1016 SER A OG    1 
ATOM   7531  N  N     . GLY A  1  1019 ? -8.819  79.694  102.762 1.00 20.24 ? 1017 GLY A N     1 
ATOM   7532  C  CA    . GLY A  1  1019 ? -8.854  79.055  104.058 1.00 23.74 ? 1017 GLY A CA    1 
ATOM   7533  C  C     . GLY A  1  1019 ? -7.514  78.624  104.588 1.00 20.73 ? 1017 GLY A C     1 
ATOM   7534  O  O     . GLY A  1  1019 ? -6.550  78.501  103.835 1.00 19.89 ? 1017 GLY A O     1 
ATOM   7535  N  N     . THR A  1  1020 ? -7.460  78.422  105.899 1.00 20.10 ? 1018 THR A N     1 
ATOM   7536  C  CA    . THR A  1  1020 ? -6.317  77.816  106.558 1.00 20.87 ? 1018 THR A CA    1 
ATOM   7537  C  C     . THR A  1  1020 ? -6.425  76.306  106.618 1.00 19.78 ? 1018 THR A C     1 
ATOM   7538  O  O     . THR A  1  1020 ? -5.406  75.624  106.783 1.00 22.93 ? 1018 THR A O     1 
ATOM   7539  C  CB    . THR A  1  1020 ? -6.214  78.322  107.997 1.00 19.61 ? 1018 THR A CB    1 
ATOM   7540  O  OG1   . THR A  1  1020 ? -7.451  78.020  108.686 1.00 19.10 ? 1018 THR A OG1   1 
ATOM   7541  C  CG2   . THR A  1  1020 ? -5.965  79.822  108.016 1.00 24.64 ? 1018 THR A CG2   1 
ATOM   7542  N  N     . GLY A  1  1021 ? -7.646  75.787  106.567 1.00 19.08 ? 1019 GLY A N     1 
ATOM   7543  C  CA    . GLY A  1  1021 ? -7.909  74.442  106.996 1.00 20.34 ? 1019 GLY A CA    1 
ATOM   7544  C  C     . GLY A  1  1021 ? -7.692  74.315  108.493 1.00 20.68 ? 1019 GLY A C     1 
ATOM   7545  O  O     . GLY A  1  1021 ? -7.374  75.287  109.181 1.00 20.60 ? 1019 GLY A O     1 
ATOM   7546  N  N     . PRO A  1  1022 ? -7.894  73.112  109.030 1.00 20.92 ? 1020 PRO A N     1 
ATOM   7547  C  CA    . PRO A  1  1022 ? -8.360  71.904  108.341 1.00 21.29 ? 1020 PRO A CA    1 
ATOM   7548  C  C     . PRO A  1  1022 ? -9.816  72.016  107.921 1.00 19.84 ? 1020 PRO A C     1 
ATOM   7549  O  O     . PRO A  1  1022 ? -10.530 72.935  108.334 1.00 22.38 ? 1020 PRO A O     1 
ATOM   7550  C  CB    . PRO A  1  1022 ? -8.162  70.809  109.401 1.00 19.56 ? 1020 PRO A CB    1 
ATOM   7551  C  CG    . PRO A  1  1022 ? -8.347  71.540  110.709 1.00 19.92 ? 1020 PRO A CG    1 
ATOM   7552  C  CD    . PRO A  1  1022 ? -7.687  72.870  110.472 1.00 20.59 ? 1020 PRO A CD    1 
ATOM   7553  N  N     . LYS A  1  1023 ? -10.260 71.071  107.102 1.00 18.75 ? 1021 LYS A N     1 
ATOM   7554  C  CA    . LYS A  1  1023 ? -11.611 71.098  106.559 1.00 18.86 ? 1021 LYS A CA    1 
ATOM   7555  C  C     . LYS A  1  1023 ? -12.660 70.829  107.628 1.00 19.42 ? 1021 LYS A C     1 
ATOM   7556  O  O     . LYS A  1  1023 ? -12.535 69.897  108.420 1.00 18.67 ? 1021 LYS A O     1 
ATOM   7557  C  CB    . LYS A  1  1023 ? -11.755 70.041  105.469 1.00 19.54 ? 1021 LYS A CB    1 
ATOM   7558  C  CG    . LYS A  1  1023 ? -11.126 70.383  104.127 1.00 16.62 ? 1021 LYS A CG    1 
ATOM   7559  C  CD    . LYS A  1  1023 ? -11.305 69.164  103.255 1.00 15.63 ? 1021 LYS A CD    1 
ATOM   7560  C  CE    . LYS A  1  1023 ? -10.875 69.415  101.817 1.00 18.11 ? 1021 LYS A CE    1 
ATOM   7561  N  NZ    . LYS A  1  1023 ? -11.897 70.233  101.136 1.00 16.99 ? 1021 LYS A NZ    1 
ATOM   7562  N  N     . ALA A  1  1024 ? -13.721 71.630  107.613 1.00 19.73 ? 1022 ALA A N     1 
ATOM   7563  C  CA    . ALA A  1  1024 ? -14.908 71.328  108.397 1.00 20.36 ? 1022 ALA A CA    1 
ATOM   7564  C  C     . ALA A  1  1024 ? -15.578 70.074  107.849 1.00 19.22 ? 1022 ALA A C     1 
ATOM   7565  O  O     . ALA A  1  1024 ? -15.573 69.824  106.638 1.00 22.68 ? 1022 ALA A O     1 
ATOM   7566  C  CB    . ALA A  1  1024 ? -15.880 72.509  108.363 1.00 21.02 ? 1022 ALA A CB    1 
ATOM   7567  N  N     . GLY A  1  1025 ? -16.138 69.270  108.747 1.00 18.74 ? 1023 GLY A N     1 
ATOM   7568  C  CA    . GLY A  1  1025 ? -16.757 68.033  108.314 1.00 21.26 ? 1023 GLY A CA    1 
ATOM   7569  C  C     . GLY A  1  1025 ? -15.767 67.019  107.811 1.00 18.68 ? 1023 GLY A C     1 
ATOM   7570  O  O     . GLY A  1  1025 ? -16.135 66.124  107.034 1.00 17.29 ? 1023 GLY A O     1 
ATOM   7571  N  N     . GLY A  1  1026 ? -14.506 67.149  108.219 1.00 17.37 ? 1024 GLY A N     1 
ATOM   7572  C  CA    . GLY A  1  1026 ? -13.467 66.220  107.859 1.00 17.51 ? 1024 GLY A CA    1 
ATOM   7573  C  C     . GLY A  1  1026 ? -12.722 65.757  109.094 1.00 18.87 ? 1024 GLY A C     1 
ATOM   7574  O  O     . GLY A  1  1026 ? -12.897 66.286  110.197 1.00 18.60 ? 1024 GLY A O     1 
ATOM   7575  N  N     . PRO A  1  1027 ? -11.846 64.768  108.910 1.00 18.32 ? 1025 PRO A N     1 
ATOM   7576  C  CA    . PRO A  1  1027 ? -11.267 64.049  110.048 1.00 20.53 ? 1025 PRO A CA    1 
ATOM   7577  C  C     . PRO A  1  1027 ? -10.103 64.756  110.727 1.00 15.91 ? 1025 PRO A C     1 
ATOM   7578  O  O     . PRO A  1  1027 ? -9.676  64.298  111.795 1.00 18.83 ? 1025 PRO A O     1 
ATOM   7579  C  CB    . PRO A  1  1027 ? -10.807 62.733  109.405 1.00 19.69 ? 1025 PRO A CB    1 
ATOM   7580  C  CG    . PRO A  1  1027 ? -10.487 63.127  107.978 1.00 19.43 ? 1025 PRO A CG    1 
ATOM   7581  C  CD    . PRO A  1  1027 ? -11.549 64.121  107.617 1.00 17.19 ? 1025 PRO A CD    1 
ATOM   7582  N  N     . LEU A  1  1028 ? -9.567  65.828  110.142 1.00 17.53 ? 1026 LEU A N     1 
ATOM   7583  C  CA    . LEU A  1  1028 ? -8.496  66.584  110.785 1.00 16.43 ? 1026 LEU A CA    1 
ATOM   7584  C  C     . LEU A  1  1028 ? -9.004  67.709  111.666 1.00 18.16 ? 1026 LEU A C     1 
ATOM   7585  O  O     . LEU A  1  1028 ? -8.210  68.320  112.385 1.00 19.29 ? 1026 LEU A O     1 
ATOM   7586  C  CB    . LEU A  1  1028 ? -7.559  67.178  109.728 1.00 17.96 ? 1026 LEU A CB    1 
ATOM   7587  C  CG    . LEU A  1  1028 ? -6.788  66.136  108.919 1.00 21.57 ? 1026 LEU A CG    1 
ATOM   7588  C  CD1   . LEU A  1  1028 ? -5.899  66.839  107.897 1.00 22.92 ? 1026 LEU A CD1   1 
ATOM   7589  C  CD2   . LEU A  1  1028 ? -5.969  65.286  109.831 1.00 27.90 ? 1026 LEU A CD2   1 
ATOM   7590  N  N     . TYR A  1  1029 ? -10.308 67.952  111.671 1.00 19.18 ? 1027 TYR A N     1 
ATOM   7591  C  CA    . TYR A  1  1029 ? -10.836 69.177  112.256 1.00 20.26 ? 1027 TYR A CA    1 
ATOM   7592  C  C     . TYR A  1  1029 ? -10.664 69.200  113.765 1.00 19.16 ? 1027 TYR A C     1 
ATOM   7593  O  O     . TYR A  1  1029 ? -10.160 70.182  114.327 1.00 20.21 ? 1027 TYR A O     1 
ATOM   7594  C  CB    . TYR A  1  1029 ? -12.297 69.287  111.884 1.00 19.95 ? 1027 TYR A CB    1 
ATOM   7595  C  CG    . TYR A  1  1029 ? -12.925 70.641  111.967 1.00 18.35 ? 1027 TYR A CG    1 
ATOM   7596  C  CD1   . TYR A  1  1029 ? -12.556 71.657  111.099 1.00 19.25 ? 1027 TYR A CD1   1 
ATOM   7597  C  CD2   . TYR A  1  1029 ? -13.952 70.874  112.871 1.00 19.82 ? 1027 TYR A CD2   1 
ATOM   7598  C  CE1   . TYR A  1  1029 ? -13.189 72.886  111.132 1.00 19.34 ? 1027 TYR A CE1   1 
ATOM   7599  C  CE2   . TYR A  1  1029 ? -14.586 72.095  112.916 1.00 20.42 ? 1027 TYR A CE2   1 
ATOM   7600  C  CZ    . TYR A  1  1029 ? -14.198 73.093  112.046 1.00 19.29 ? 1027 TYR A CZ    1 
ATOM   7601  O  OH    . TYR A  1  1029 ? -14.854 74.299  112.093 1.00 21.72 ? 1027 TYR A OH    1 
ATOM   7602  N  N     . LEU A  1  1030 ? -11.122 68.148  114.447 1.00 19.41 ? 1028 LEU A N     1 
ATOM   7603  C  CA    . LEU A  1  1030 ? -11.074 68.168  115.903 1.00 19.23 ? 1028 LEU A CA    1 
ATOM   7604  C  C     . LEU A  1  1030 ? -9.646  68.271  116.402 1.00 20.95 ? 1028 LEU A C     1 
ATOM   7605  O  O     . LEU A  1  1030 ? -9.399  68.887  117.445 1.00 21.32 ? 1028 LEU A O     1 
ATOM   7606  C  CB    . LEU A  1  1030 ? -11.738 66.925  116.481 1.00 19.63 ? 1028 LEU A CB    1 
ATOM   7607  C  CG    . LEU A  1  1030 ? -13.216 66.747  116.149 1.00 19.31 ? 1028 LEU A CG    1 
ATOM   7608  C  CD1   . LEU A  1  1030 ? -13.737 65.513  116.869 1.00 23.48 ? 1028 LEU A CD1   1 
ATOM   7609  C  CD2   . LEU A  1  1030 ? -13.992 67.975  116.575 1.00 22.71 ? 1028 LEU A CD2   1 
ATOM   7610  N  N     . GLY A  1  1031 ? -8.692  67.695  115.668 1.00 19.50 ? 1029 GLY A N     1 
ATOM   7611  C  CA    . GLY A  1  1031 ? -7.317  67.691  116.130 1.00 21.29 ? 1029 GLY A CA    1 
ATOM   7612  C  C     . GLY A  1  1031 ? -6.699  69.066  116.225 1.00 23.09 ? 1029 GLY A C     1 
ATOM   7613  O  O     . GLY A  1  1031 ? -5.686  69.237  116.914 1.00 22.58 ? 1029 GLY A O     1 
ATOM   7614  N  N     . ARG A  1  1032 ? -7.274  70.051  115.536 1.00 19.17 ? 1030 ARG A N     1 
ATOM   7615  C  CA    . ARG A  1  1032 ? -6.814  71.425  115.629 1.00 19.07 ? 1030 ARG A CA    1 
ATOM   7616  C  C     . ARG A  1  1032 ? -7.287  72.104  116.912 1.00 22.07 ? 1030 ARG A C     1 
ATOM   7617  O  O     . ARG A  1  1032 ? -6.743  73.152  117.286 1.00 21.75 ? 1030 ARG A O     1 
ATOM   7618  C  CB    . ARG A  1  1032 ? -7.300  72.201  114.400 1.00 19.50 ? 1030 ARG A CB    1 
ATOM   7619  C  CG    . ARG A  1  1032 ? -6.668  73.574  114.212 1.00 19.86 ? 1030 ARG A CG    1 
ATOM   7620  C  CD    . ARG A  1  1032 ? -5.201  73.484  113.808 1.00 22.54 ? 1030 ARG A CD    1 
ATOM   7621  N  NE    . ARG A  1  1032 ? -4.692  74.793  113.405 1.00 21.04 ? 1030 ARG A NE    1 
ATOM   7622  C  CZ    . ARG A  1  1032 ? -3.671  75.424  113.974 1.00 24.39 ? 1030 ARG A CZ    1 
ATOM   7623  N  NH1   . ARG A  1  1032 ? -2.998  74.889  114.982 1.00 26.35 ? 1030 ARG A NH1   1 
ATOM   7624  N  NH2   . ARG A  1  1032 ? -3.318  76.621  113.517 1.00 27.05 ? 1030 ARG A NH2   1 
ATOM   7625  N  N     . LEU A  1  1033 ? -8.264  71.514  117.600 1.00 20.98 ? 1031 LEU A N     1 
ATOM   7626  C  CA    . LEU A  1  1033 ? -8.929  72.124  118.742 1.00 20.59 ? 1031 LEU A CA    1 
ATOM   7627  C  C     . LEU A  1  1033 ? -8.447  71.543  120.061 1.00 19.56 ? 1031 LEU A C     1 
ATOM   7628  O  O     . LEU A  1  1033 ? -9.070  71.773  121.103 1.00 21.26 ? 1031 LEU A O     1 
ATOM   7629  C  CB    . LEU A  1  1033 ? -10.448 71.958  118.608 1.00 21.01 ? 1031 LEU A CB    1 
ATOM   7630  C  CG    . LEU A  1  1033 ? -10.969 72.444  117.253 1.00 20.85 ? 1031 LEU A CG    1 
ATOM   7631  C  CD1   . LEU A  1  1033 ? -12.491 72.270  117.124 1.00 21.62 ? 1031 LEU A CD1   1 
ATOM   7632  C  CD2   . LEU A  1  1033 ? -10.568 73.892  117.051 1.00 24.56 ? 1031 LEU A CD2   1 
ATOM   7633  N  N     . VAL A  1  1034 ? -7.349  70.794  120.028 1.00 21.46 ? 1032 VAL A N     1 
ATOM   7634  C  CA    . VAL A  1  1034 ? -6.727  70.239  121.218 1.00 21.45 ? 1032 VAL A CA    1 
ATOM   7635  C  C     . VAL A  1  1034 ? -5.242  70.543  121.124 1.00 22.28 ? 1032 VAL A C     1 
ATOM   7636  O  O     . VAL A  1  1034 ? -4.710  70.829  120.051 1.00 23.99 ? 1032 VAL A O     1 
ATOM   7637  C  CB    . VAL A  1  1034 ? -6.976  68.726  121.358 1.00 21.94 ? 1032 VAL A CB    1 
ATOM   7638  C  CG1   . VAL A  1  1034 ? -8.462  68.450  121.654 1.00 23.90 ? 1032 VAL A CG1   1 
ATOM   7639  C  CG2   . VAL A  1  1034 ? -6.531  67.998  120.084 1.00 21.62 ? 1032 VAL A CG2   1 
ATOM   7640  N  N     . THR A  1  1035 ? -4.569  70.494  122.273 1.00 24.13 ? 1033 THR A N     1 
ATOM   7641  C  CA    . THR A  1  1035 ? -3.159  70.867  122.274 1.00 25.04 ? 1033 THR A CA    1 
ATOM   7642  C  C     . THR A  1  1035 ? -2.268  69.780  121.688 1.00 31.31 ? 1033 THR A C     1 
ATOM   7643  O  O     . THR A  1  1035 ? -1.176  70.086  121.196 1.00 33.94 ? 1033 THR A O     1 
ATOM   7644  C  CB    . THR A  1  1035 ? -2.712  71.215  123.693 1.00 31.69 ? 1033 THR A CB    1 
ATOM   7645  O  OG1   . THR A  1  1035 ? -3.058  70.146  124.576 1.00 37.42 ? 1033 THR A OG1   1 
ATOM   7646  C  CG2   . THR A  1  1035 ? -3.406  72.477  124.157 1.00 30.14 ? 1033 THR A CG2   1 
ATOM   7647  N  N     . THR A  1  1036 ? -2.702  68.520  121.733 1.00 25.03 ? 1034 THR A N     1 
ATOM   7648  C  CA    . THR A  1  1036 ? -1.978  67.412  121.120 1.00 25.37 ? 1034 THR A CA    1 
ATOM   7649  C  C     . THR A  1  1036 ? -2.942  66.691  120.194 1.00 25.38 ? 1034 THR A C     1 
ATOM   7650  O  O     . THR A  1  1036 ? -3.938  66.128  120.655 1.00 27.57 ? 1034 THR A O     1 
ATOM   7651  C  CB    . THR A  1  1036 ? -1.423  66.455  122.174 1.00 34.23 ? 1034 THR A CB    1 
ATOM   7652  O  OG1   . THR A  1  1036 ? -0.479  67.152  122.994 1.00 34.25 ? 1034 THR A OG1   1 
ATOM   7653  C  CG2   . THR A  1  1036 ? -0.735  65.271  121.507 1.00 35.24 ? 1034 THR A CG2   1 
ATOM   7654  N  N     . ALA A  1  1037 ? -2.660  66.727  118.904 1.00 25.33 ? 1035 ALA A N     1 
ATOM   7655  C  CA    . ALA A  1  1037 ? -3.609  66.200  117.928 1.00 25.84 ? 1035 ALA A CA    1 
ATOM   7656  C  C     . ALA A  1  1037 ? -3.635  64.676  117.984 1.00 22.80 ? 1035 ALA A C     1 
ATOM   7657  O  O     . ALA A  1  1037 ? -2.570  64.039  118.059 1.00 24.85 ? 1035 ALA A O     1 
ATOM   7658  C  CB    . ALA A  1  1037 ? -3.253  66.682  116.527 1.00 24.31 ? 1035 ALA A CB    1 
ATOM   7659  N  N     . PRO A  1  1038 ? -4.812  64.060  117.971 1.00 21.82 ? 1036 PRO A N     1 
ATOM   7660  C  CA    . PRO A  1  1038 ? -4.895  62.604  117.886 1.00 21.43 ? 1036 PRO A CA    1 
ATOM   7661  C  C     . PRO A  1  1038 ? -4.648  62.148  116.456 1.00 22.70 ? 1036 PRO A C     1 
ATOM   7662  O  O     . PRO A  1  1038 ? -4.581  62.938  115.513 1.00 21.89 ? 1036 PRO A O     1 
ATOM   7663  C  CB    . PRO A  1  1038 ? -6.333  62.308  118.300 1.00 22.60 ? 1036 PRO A CB    1 
ATOM   7664  C  CG    . PRO A  1  1038 ? -7.078  63.488  117.784 1.00 26.68 ? 1036 PRO A CG    1 
ATOM   7665  C  CD    . PRO A  1  1038 ? -6.152  64.678  118.010 1.00 21.96 ? 1036 PRO A CD    1 
ATOM   7666  N  N     . VAL A  1  1039 ? -4.546  60.833  116.302 1.00 20.57 ? 1037 VAL A N     1 
ATOM   7667  C  CA    . VAL A  1  1039 ? -4.455  60.206  114.987 1.00 23.29 ? 1037 VAL A CA    1 
ATOM   7668  C  C     . VAL A  1  1039 ? -5.881  60.024  114.473 1.00 18.78 ? 1037 VAL A C     1 
ATOM   7669  O  O     . VAL A  1  1039 ? -6.641  59.237  115.062 1.00 21.91 ? 1037 VAL A O     1 
ATOM   7670  C  CB    . VAL A  1  1039 ? -3.705  58.869  115.049 1.00 20.98 ? 1037 VAL A CB    1 
ATOM   7671  C  CG1   . VAL A  1  1039 ? -3.660  58.243  113.675 1.00 22.76 ? 1037 VAL A CG1   1 
ATOM   7672  C  CG2   . VAL A  1  1039 ? -2.291  59.088  115.596 1.00 23.80 ? 1037 VAL A CG2   1 
ATOM   7673  N  N     . PRO A  1  1040 ? -6.286  60.719  113.411 1.00 19.10 ? 1038 PRO A N     1 
ATOM   7674  C  CA    . PRO A  1  1040 ? -7.647  60.579  112.918 1.00 21.90 ? 1038 PRO A CA    1 
ATOM   7675  C  C     . PRO A  1  1040 ? -7.887  59.183  112.378 1.00 19.19 ? 1038 PRO A C     1 
ATOM   7676  O  O     . PRO A  1  1040 ? -6.934  58.477  112.007 1.00 19.84 ? 1038 PRO A O     1 
ATOM   7677  C  CB    . PRO A  1  1040 ? -7.734  61.629  111.795 1.00 19.54 ? 1038 PRO A CB    1 
ATOM   7678  C  CG    . PRO A  1  1040 ? -6.598  62.555  112.032 1.00 22.84 ? 1038 PRO A CG    1 
ATOM   7679  C  CD    . PRO A  1  1040 ? -5.516  61.704  112.639 1.00 20.43 ? 1038 PRO A CD    1 
ATOM   7680  N  N     . PRO A  1  1041 ? -9.143  58.751  112.335 1.00 18.97 ? 1039 PRO A N     1 
ATOM   7681  C  CA    . PRO A  1  1041 ? -9.474  57.495  111.662 1.00 21.17 ? 1039 PRO A CA    1 
ATOM   7682  C  C     . PRO A  1  1041 ? -8.946  57.502  110.241 1.00 19.44 ? 1039 PRO A C     1 
ATOM   7683  O  O     . PRO A  1  1041 ? -8.995  58.523  109.551 1.00 20.81 ? 1039 PRO A O     1 
ATOM   7684  C  CB    . PRO A  1  1041 ? -11.010 57.470  111.683 1.00 24.27 ? 1039 PRO A CB    1 
ATOM   7685  C  CG    . PRO A  1  1041 ? -11.401 58.438  112.767 1.00 25.23 ? 1039 PRO A CG    1 
ATOM   7686  C  CD    . PRO A  1  1041 ? -10.347 59.495  112.748 1.00 24.24 ? 1039 PRO A CD    1 
ATOM   7687  N  N     . GLN A  1  1042 ? -8.421  56.350  109.826 1.00 18.74 ? 1040 GLN A N     1 
ATOM   7688  C  CA    . GLN A  1  1042 ? -7.937  56.066  108.479 1.00 19.13 ? 1040 GLN A CA    1 
ATOM   7689  C  C     . GLN A  1  1042 ? -6.790  56.962  108.051 1.00 21.19 ? 1040 GLN A C     1 
ATOM   7690  O  O     . GLN A  1  1042 ? -6.427  56.968  106.870 1.00 21.08 ? 1040 GLN A O     1 
ATOM   7691  C  CB    . GLN A  1  1042 ? -9.070  56.168  107.445 1.00 21.53 ? 1040 GLN A CB    1 
ATOM   7692  C  CG    . GLN A  1  1042 ? -10.253 55.267  107.744 1.00 27.87 ? 1040 GLN A CG    1 
ATOM   7693  C  CD    . GLN A  1  1042 ? -11.348 55.413  106.698 1.00 34.06 ? 1040 GLN A CD    1 
ATOM   7694  O  OE1   . GLN A  1  1042 ? -11.507 54.558  105.832 1.00 42.93 ? 1040 GLN A OE1   1 
ATOM   7695  N  NE2   . GLN A  1  1042 ? -12.091 56.507  106.767 1.00 38.68 ? 1040 GLN A NE2   1 
ATOM   7696  N  N     . HIS A  1  1043 ? -6.176  57.690  108.979 1.00 18.30 ? 1041 HIS A N     1 
ATOM   7697  C  CA    . HIS A  1  1043 ? -5.189  58.707  108.641 1.00 17.73 ? 1041 HIS A CA    1 
ATOM   7698  C  C     . HIS A  1  1043 ? -3.809  58.072  108.648 1.00 20.63 ? 1041 HIS A C     1 
ATOM   7699  O  O     . HIS A  1  1043 ? -3.173  57.968  109.695 1.00 21.24 ? 1041 HIS A O     1 
ATOM   7700  C  CB    . HIS A  1  1043 ? -5.270  59.858  109.630 1.00 17.85 ? 1041 HIS A CB    1 
ATOM   7701  C  CG    . HIS A  1  1043 ? -4.319  60.972  109.343 1.00 18.47 ? 1041 HIS A CG    1 
ATOM   7702  N  ND1   . HIS A  1  1043 ? -4.624  62.014  108.493 1.00 17.10 ? 1041 HIS A ND1   1 
ATOM   7703  C  CD2   . HIS A  1  1043 ? -3.067  61.211  109.798 1.00 18.93 ? 1041 HIS A CD2   1 
ATOM   7704  C  CE1   . HIS A  1  1043 ? -3.604  62.850  108.443 1.00 19.25 ? 1041 HIS A CE1   1 
ATOM   7705  N  NE2   . HIS A  1  1043 ? -2.645  62.386  109.227 1.00 19.83 ? 1041 HIS A NE2   1 
ATOM   7706  N  N     . SER A  1  1044 ? -3.351  57.639  107.482 1.00 18.16 ? 1042 SER A N     1 
ATOM   7707  C  CA    . SER A  1  1044 ? -2.009  57.094  107.324 1.00 18.37 ? 1042 SER A CA    1 
ATOM   7708  C  C     . SER A  1  1044 ? -1.718  57.014  105.837 1.00 18.36 ? 1042 SER A C     1 
ATOM   7709  O  O     . SER A  1  1044 ? -2.612  57.159  104.999 1.00 19.60 ? 1042 SER A O     1 
ATOM   7710  C  CB    . SER A  1  1044 ? -1.864  55.710  107.951 1.00 18.11 ? 1042 SER A CB    1 
ATOM   7711  O  OG    . SER A  1  1044 ? -2.658  54.761  107.250 1.00 18.66 ? 1042 SER A OG    1 
ATOM   7712  N  N     . SER A  1  1045 ? -0.460  56.741  105.522 1.00 16.98 ? 1043 SER A N     1 
ATOM   7713  C  CA    . SER A  1  1045 ? -0.071  56.562  104.135 1.00 18.24 ? 1043 SER A CA    1 
ATOM   7714  C  C     . SER A  1  1045 ? 1.144   55.655  104.079 1.00 16.97 ? 1043 SER A C     1 
ATOM   7715  O  O     . SER A  1  1045 ? 2.082   55.820  104.858 1.00 18.43 ? 1043 SER A O     1 
ATOM   7716  C  CB    . SER A  1  1045 ? 0.246   57.906  103.478 1.00 18.56 ? 1043 SER A CB    1 
ATOM   7717  O  OG    . SER A  1  1045 ? 0.714   57.697  102.151 1.00 18.83 ? 1043 SER A OG    1 
ATOM   7718  N  N     . VAL A  1  1046 ? 1.124   54.703  103.141 1.00 18.02 ? 1044 VAL A N     1 
ATOM   7719  C  CA    . VAL A  1  1046 ? 2.289   53.840  102.967 1.00 18.52 ? 1044 VAL A CA    1 
ATOM   7720  C  C     . VAL A  1  1046 ? 3.336   54.467  102.076 1.00 18.76 ? 1044 VAL A C     1 
ATOM   7721  O  O     . VAL A  1  1046 ? 4.401   53.872  101.888 1.00 21.87 ? 1044 VAL A O     1 
ATOM   7722  C  CB    . VAL A  1  1046 ? 1.939   52.457  102.384 1.00 20.84 ? 1044 VAL A CB    1 
ATOM   7723  C  CG1   . VAL A  1  1046 ? 1.011   51.711  103.339 1.00 24.04 ? 1044 VAL A CG1   1 
ATOM   7724  C  CG2   . VAL A  1  1046 ? 1.313   52.598  101.022 1.00 19.61 ? 1044 VAL A CG2   1 
ATOM   7725  N  N     . HIS A  1  1047 ? 3.077   55.661  101.554 1.00 18.50 ? 1045 HIS A N     1 
ATOM   7726  C  CA    A HIS A  1  1047 ? 4.003   56.304  100.643 0.65 18.94 ? 1045 HIS A CA    1 
ATOM   7727  C  CA    B HIS A  1  1047 ? 3.977   56.345  100.632 0.35 18.99 ? 1045 HIS A CA    1 
ATOM   7728  C  C     . HIS A  1  1047 ? 4.950   57.222  101.401 1.00 20.63 ? 1045 HIS A C     1 
ATOM   7729  O  O     . HIS A  1  1047 ? 4.571   57.877  102.374 1.00 21.46 ? 1045 HIS A O     1 
ATOM   7730  C  CB    A HIS A  1  1047 ? 3.208   57.052  99.579  0.65 20.75 ? 1045 HIS A CB    1 
ATOM   7731  C  CB    B HIS A  1  1047 ? 3.185   57.207  99.646  0.35 20.64 ? 1045 HIS A CB    1 
ATOM   7732  C  CG    A HIS A  1  1047 ? 2.210   56.172  98.893  0.65 21.43 ? 1045 HIS A CG    1 
ATOM   7733  C  CG    B HIS A  1  1047 ? 3.999   58.274  98.977  0.35 19.56 ? 1045 HIS A CG    1 
ATOM   7734  N  ND1   A HIS A  1  1047 ? 2.582   55.171  98.019  0.65 25.37 ? 1045 HIS A ND1   1 
ATOM   7735  N  ND1   B HIS A  1  1047 ? 4.014   59.583  99.412  0.35 20.50 ? 1045 HIS A ND1   1 
ATOM   7736  C  CD2   A HIS A  1  1047 ? 0.863   56.094  99.003  0.65 24.59 ? 1045 HIS A CD2   1 
ATOM   7737  C  CD2   B HIS A  1  1047 ? 4.820   58.225  97.902  0.35 20.65 ? 1045 HIS A CD2   1 
ATOM   7738  C  CE1   A HIS A  1  1047 ? 1.503   54.536  97.599  0.65 24.12 ? 1045 HIS A CE1   1 
ATOM   7739  C  CE1   B HIS A  1  1047 ? 4.815   60.293  98.638  0.35 21.68 ? 1045 HIS A CE1   1 
ATOM   7740  N  NE2   A HIS A  1  1047 ? 0.447   55.079  98.177  0.65 22.42 ? 1045 HIS A NE2   1 
ATOM   7741  N  NE2   B HIS A  1  1047 ? 5.315   59.494  97.711  0.35 21.70 ? 1045 HIS A NE2   1 
ATOM   7742  N  N     . THR A  1  1048 ? 6.201   57.224  100.970 1.00 18.84 ? 1046 THR A N     1 
ATOM   7743  C  CA    . THR A  1  1048 ? 7.227   58.053  101.583 1.00 18.39 ? 1046 THR A CA    1 
ATOM   7744  C  C     . THR A  1  1048 ? 7.735   59.036  100.544 1.00 19.74 ? 1046 THR A C     1 
ATOM   7745  O  O     . THR A  1  1048 ? 8.101   58.640  99.439  1.00 21.15 ? 1046 THR A O     1 
ATOM   7746  C  CB    . THR A  1  1048 ? 8.383   57.218  102.105 1.00 18.16 ? 1046 THR A CB    1 
ATOM   7747  O  OG1   . THR A  1  1048 ? 7.871   56.171  102.931 1.00 20.87 ? 1046 THR A OG1   1 
ATOM   7748  C  CG2   . THR A  1  1048 ? 9.317   58.095  102.942 1.00 20.73 ? 1046 THR A CG2   1 
ATOM   7749  N  N     . ASP A  1  1049 ? 7.758   60.305  100.902 1.00 18.50 ? 1047 ASP A N     1 
ATOM   7750  C  CA    . ASP A  1  1049 ? 8.217   61.310  99.965  1.00 17.36 ? 1047 ASP A CA    1 
ATOM   7751  C  C     . ASP A  1  1049 ? 9.681   61.051  99.606  1.00 18.00 ? 1047 ASP A C     1 
ATOM   7752  O  O     . ASP A  1  1049 ? 10.503  60.816  100.497 1.00 18.24 ? 1047 ASP A O     1 
ATOM   7753  C  CB    . ASP A  1  1049 ? 8.034   62.698  100.568 1.00 16.06 ? 1047 ASP A CB    1 
ATOM   7754  C  CG    . ASP A  1  1049 ? 8.480   63.786  99.627  1.00 18.77 ? 1047 ASP A CG    1 
ATOM   7755  O  OD1   . ASP A  1  1049 ? 9.701   64.040  99.557  1.00 18.64 ? 1047 ASP A OD1   1 
ATOM   7756  O  OD2   . ASP A  1  1049 ? 7.611   64.347  98.914  1.00 20.70 ? 1047 ASP A OD2   1 
ATOM   7757  N  N     . PRO A  1  1050 ? 10.035  61.040  98.329  1.00 17.00 ? 1048 PRO A N     1 
ATOM   7758  C  CA    . PRO A  1  1050 ? 11.386  60.619  97.943  1.00 17.79 ? 1048 PRO A CA    1 
ATOM   7759  C  C     . PRO A  1  1050 ? 12.417  61.692  98.234  1.00 18.74 ? 1048 PRO A C     1 
ATOM   7760  O  O     . PRO A  1  1050 ? 13.603  61.398  98.416  1.00 20.14 ? 1048 PRO A O     1 
ATOM   7761  C  CB    . PRO A  1  1050 ? 11.261  60.354  96.436  1.00 20.88 ? 1048 PRO A CB    1 
ATOM   7762  C  CG    . PRO A  1  1050 ? 10.084  61.195  96.005  1.00 22.30 ? 1048 PRO A CG    1 
ATOM   7763  C  CD    . PRO A  1  1050 ? 9.134   61.223  97.177  1.00 19.91 ? 1048 PRO A CD    1 
ATOM   7764  N  N     . VAL A  1  1051 ? 11.974  62.951  98.248  1.00 18.28 ? 1049 VAL A N     1 
ATOM   7765  C  CA    . VAL A  1  1051 ? 12.889  64.031  98.585  1.00 18.20 ? 1049 VAL A CA    1 
ATOM   7766  C  C     . VAL A  1  1051 ? 13.206  63.993  100.067 1.00 16.83 ? 1049 VAL A C     1 
ATOM   7767  O  O     . VAL A  1  1051 ? 14.353  64.201  100.476 1.00 19.57 ? 1049 VAL A O     1 
ATOM   7768  C  CB    . VAL A  1  1051 ? 12.306  65.384  98.153  1.00 19.90 ? 1049 VAL A CB    1 
ATOM   7769  C  CG1   . VAL A  1  1051 ? 13.265  66.505  98.515  1.00 21.64 ? 1049 VAL A CG1   1 
ATOM   7770  C  CG2   . VAL A  1  1051 ? 12.044  65.367  96.646  1.00 21.44 ? 1049 VAL A CG2   1 
ATOM   7771  N  N     . LEU A  1  1052 ? 12.198  63.696  100.893 1.00 17.14 ? 1050 LEU A N     1 
ATOM   7772  C  CA    . LEU A  1  1052 ? 12.460  63.420  102.297 1.00 17.27 ? 1050 LEU A CA    1 
ATOM   7773  C  C     . LEU A  1  1052 ? 13.518  62.331  102.438 1.00 18.03 ? 1050 LEU A C     1 
ATOM   7774  O  O     . LEU A  1  1052 ? 14.477  62.476  103.200 1.00 17.69 ? 1050 LEU A O     1 
ATOM   7775  C  CB    . LEU A  1  1052 ? 11.152  63.034  102.984 1.00 18.39 ? 1050 LEU A CB    1 
ATOM   7776  C  CG    . LEU A  1  1052 ? 11.184  62.612  104.459 1.00 17.13 ? 1050 LEU A CG    1 
ATOM   7777  C  CD1   . LEU A  1  1052 ? 11.695  61.189  104.663 1.00 18.71 ? 1050 LEU A CD1   1 
ATOM   7778  C  CD2   . LEU A  1  1052 ? 11.993  63.605  105.308 1.00 17.99 ? 1050 LEU A CD2   1 
ATOM   7779  N  N     . LEU A  1  1053 ? 13.352  61.218  101.712 1.00 18.10 ? 1051 LEU A N     1 
ATOM   7780  C  CA    . LEU A  1  1053 ? 14.331  60.142  101.799 1.00 18.72 ? 1051 LEU A CA    1 
ATOM   7781  C  C     . LEU A  1  1053 ? 15.719  60.612  101.381 1.00 16.93 ? 1051 LEU A C     1 
ATOM   7782  O  O     . LEU A  1  1053 ? 16.709  60.244  102.011 1.00 19.41 ? 1051 LEU A O     1 
ATOM   7783  C  CB    . LEU A  1  1053 ? 13.890  58.955  100.940 1.00 19.84 ? 1051 LEU A CB    1 
ATOM   7784  C  CG    . LEU A  1  1053 ? 12.698  58.183  101.501 1.00 20.60 ? 1051 LEU A CG    1 
ATOM   7785  C  CD1   . LEU A  1  1053 ? 12.212  57.143  100.502 1.00 20.99 ? 1051 LEU A CD1   1 
ATOM   7786  C  CD2   . LEU A  1  1053 ? 13.017  57.532  102.826 1.00 20.35 ? 1051 LEU A CD2   1 
ATOM   7787  N  N     . ASP A  1  1054 ? 15.813  61.406  100.311 1.00 18.55 ? 1052 ASP A N     1 
ATOM   7788  C  CA    . ASP A  1  1054 ? 17.113  61.932  99.907  1.00 19.66 ? 1052 ASP A CA    1 
ATOM   7789  C  C     . ASP A  1  1054 ? 17.683  62.841  100.983 1.00 18.73 ? 1052 ASP A C     1 
ATOM   7790  O  O     . ASP A  1  1054 ? 18.890  62.830  101.239 1.00 20.32 ? 1052 ASP A O     1 
ATOM   7791  C  CB    . ASP A  1  1054 ? 17.000  62.701  98.596  1.00 19.25 ? 1052 ASP A CB    1 
ATOM   7792  C  CG    . ASP A  1  1054 ? 16.696  61.805  97.410  1.00 26.12 ? 1052 ASP A CG    1 
ATOM   7793  O  OD1   . ASP A  1  1054 ? 16.797  60.567  97.551  1.00 22.85 ? 1052 ASP A OD1   1 
ATOM   7794  O  OD2   . ASP A  1  1054 ? 16.344  62.358  96.343  1.00 27.13 ? 1052 ASP A OD2   1 
ATOM   7795  N  N     . PHE A  1  1055 ? 16.828  63.644  101.609 1.00 16.84 ? 1053 PHE A N     1 
ATOM   7796  C  CA    . PHE A  1  1055 ? 17.292  64.512  102.685 1.00 19.82 ? 1053 PHE A CA    1 
ATOM   7797  C  C     . PHE A  1  1055 ? 17.801  63.701  103.870 1.00 18.69 ? 1053 PHE A C     1 
ATOM   7798  O  O     . PHE A  1  1055 ? 18.851  64.020  104.441 1.00 19.87 ? 1053 PHE A O     1 
ATOM   7799  C  CB    . PHE A  1  1055 ? 16.160  65.450  103.095 1.00 17.73 ? 1053 PHE A CB    1 
ATOM   7800  C  CG    . PHE A  1  1055 ? 16.528  66.394  104.201 1.00 17.09 ? 1053 PHE A CG    1 
ATOM   7801  C  CD1   . PHE A  1  1055 ? 17.593  67.259  104.054 1.00 22.59 ? 1053 PHE A CD1   1 
ATOM   7802  C  CD2   . PHE A  1  1055 ? 15.804  66.417  105.368 1.00 18.66 ? 1053 PHE A CD2   1 
ATOM   7803  C  CE1   . PHE A  1  1055 ? 17.937  68.140  105.076 1.00 23.47 ? 1053 PHE A CE1   1 
ATOM   7804  C  CE2   . PHE A  1  1055 ? 16.142  67.296  106.392 1.00 20.47 ? 1053 PHE A CE2   1 
ATOM   7805  C  CZ    . PHE A  1  1055 ? 17.207  68.146  106.242 1.00 19.71 ? 1053 PHE A CZ    1 
ATOM   7806  N  N     . ALA A  1  1056 ? 17.074  62.648  104.257 1.00 19.37 ? 1054 ALA A N     1 
ATOM   7807  C  CA    . ALA A  1  1056 ? 17.536  61.807  105.362 1.00 19.37 ? 1054 ALA A CA    1 
ATOM   7808  C  C     . ALA A  1  1056 ? 18.888  61.175  105.058 1.00 21.54 ? 1054 ALA A C     1 
ATOM   7809  O  O     . ALA A  1  1056 ? 19.736  61.058  105.947 1.00 20.84 ? 1054 ALA A O     1 
ATOM   7810  C  CB    . ALA A  1  1056 ? 16.501  60.726  105.680 1.00 20.71 ? 1054 ALA A CB    1 
ATOM   7811  N  N     . LYS A  1  1057 ? 19.109  60.745  103.812 1.00 21.17 ? 1055 LYS A N     1 
ATOM   7812  C  CA    . LYS A  1  1057 ? 20.419  60.201  103.463 1.00 22.74 ? 1055 LYS A CA    1 
ATOM   7813  C  C     . LYS A  1  1057 ? 21.491  61.275  103.535 1.00 22.51 ? 1055 LYS A C     1 
ATOM   7814  O  O     . LYS A  1  1057 ? 22.620  61.004  103.964 1.00 26.91 ? 1055 LYS A O     1 
ATOM   7815  C  CB    . LYS A  1  1057 ? 20.390  59.585  102.062 1.00 28.63 ? 1055 LYS A CB    1 
ATOM   7816  C  CG    . LYS A  1  1057 ? 19.772  58.212  102.021 1.00 26.25 ? 1055 LYS A CG    1 
ATOM   7817  C  CD    . LYS A  1  1057 ? 19.979  57.549  100.662 1.00 25.82 ? 1055 LYS A CD    1 
ATOM   7818  C  CE    . LYS A  1  1057 ? 19.434  58.412  99.537  1.00 26.27 ? 1055 LYS A CE    1 
ATOM   7819  N  NZ    . LYS A  1  1057 ? 19.256  57.581  98.312  1.00 29.32 ? 1055 LYS A NZ    1 
ATOM   7820  N  N     . TRP A  1  1058 ? 21.169  62.485  103.071 1.00 21.44 ? 1056 TRP A N     1 
ATOM   7821  C  CA    . TRP A  1  1058 ? 22.120  63.589  103.143 1.00 22.34 ? 1056 TRP A CA    1 
ATOM   7822  C  C     . TRP A  1  1058 ? 22.480  63.899  104.586 1.00 24.25 ? 1056 TRP A C     1 
ATOM   7823  O  O     . TRP A  1  1058 ? 23.656  64.096  104.907 1.00 27.89 ? 1056 TRP A O     1 
ATOM   7824  C  CB    . TRP A  1  1058 ? 21.542  64.823  102.448 1.00 22.33 ? 1056 TRP A CB    1 
ATOM   7825  C  CG    . TRP A  1  1058 ? 22.396  66.060  102.551 1.00 24.17 ? 1056 TRP A CG    1 
ATOM   7826  C  CD1   . TRP A  1  1058 ? 23.418  66.430  101.709 1.00 26.44 ? 1056 TRP A CD1   1 
ATOM   7827  C  CD2   . TRP A  1  1058 ? 22.279  67.105  103.524 1.00 27.20 ? 1056 TRP A CD2   1 
ATOM   7828  N  NE1   . TRP A  1  1058 ? 23.948  67.636  102.114 1.00 28.41 ? 1056 TRP A NE1   1 
ATOM   7829  C  CE2   . TRP A  1  1058 ? 23.270  68.071  103.224 1.00 28.19 ? 1056 TRP A CE2   1 
ATOM   7830  C  CE3   . TRP A  1  1058 ? 21.443  67.315  104.623 1.00 24.34 ? 1056 TRP A CE3   1 
ATOM   7831  C  CZ2   . TRP A  1  1058 ? 23.443  69.227  103.986 1.00 28.86 ? 1056 TRP A CZ2   1 
ATOM   7832  C  CZ3   . TRP A  1  1058 ? 21.617  68.467  105.385 1.00 28.13 ? 1056 TRP A CZ3   1 
ATOM   7833  C  CH2   . TRP A  1  1058 ? 22.614  69.407  105.062 1.00 30.72 ? 1056 TRP A CH2   1 
ATOM   7834  N  N     . LEU A  1  1059 ? 21.479  63.932  105.470 1.00 21.44 ? 1057 LEU A N     1 
ATOM   7835  C  CA    . LEU A  1  1059 ? 21.737  64.135  106.896 1.00 23.68 ? 1057 LEU A CA    1 
ATOM   7836  C  C     . LEU A  1  1059 ? 22.681  63.079  107.440 1.00 26.83 ? 1057 LEU A C     1 
ATOM   7837  O  O     . LEU A  1  1059 ? 23.605  63.392  108.199 1.00 28.81 ? 1057 LEU A O     1 
ATOM   7838  C  CB    . LEU A  1  1059 ? 20.426  64.108  107.682 1.00 23.31 ? 1057 LEU A CB    1 
ATOM   7839  C  CG    . LEU A  1  1059 ? 19.509  65.318  107.549 1.00 21.79 ? 1057 LEU A CG    1 
ATOM   7840  C  CD1   . LEU A  1  1059 ? 18.149  65.032  108.160 1.00 20.47 ? 1057 LEU A CD1   1 
ATOM   7841  C  CD2   . LEU A  1  1059 ? 20.149  66.542  108.212 1.00 24.28 ? 1057 LEU A CD2   1 
ATOM   7842  N  N     . ASP A  1  1060 ? 22.446  61.811  107.090 1.00 26.59 ? 1058 ASP A N     1 
ATOM   7843  C  CA    . ASP A  1  1060 ? 23.338  60.753  107.558 1.00 30.33 ? 1058 ASP A CA    1 
ATOM   7844  C  C     . ASP A  1  1060 ? 24.749  60.955  107.028 1.00 30.53 ? 1058 ASP A C     1 
ATOM   7845  O  O     . ASP A  1  1060 ? 25.730  60.704  107.741 1.00 33.98 ? 1058 ASP A O     1 
ATOM   7846  C  CB    . ASP A  1  1060 ? 22.801  59.388  107.142 1.00 32.76 ? 1058 ASP A CB    1 
ATOM   7847  C  CG    . ASP A  1  1060 ? 21.950  58.755  108.212 1.00 32.17 ? 1058 ASP A CG    1 
ATOM   7848  O  OD1   . ASP A  1  1060 ? 22.237  58.977  109.410 1.00 36.37 ? 1058 ASP A OD1   1 
ATOM   7849  O  OD2   . ASP A  1  1060 ? 20.999  58.038  107.860 1.00 36.66 ? 1058 ASP A OD2   1 
ATOM   7850  N  N     . GLY A  1  1061 ? 24.872  61.429  105.787 1.00 28.77 ? 1059 GLY A N     1 
ATOM   7851  C  CA    . GLY A  1  1061 ? 26.185  61.700  105.228 1.00 30.87 ? 1059 GLY A CA    1 
ATOM   7852  C  C     . GLY A  1  1061 ? 26.890  62.861  105.899 1.00 36.88 ? 1059 GLY A C     1 
ATOM   7853  O  O     . GLY A  1  1061 ? 28.124  62.897  105.936 1.00 34.40 ? 1059 GLY A O     1 
ATOM   7854  N  N     . LYS A  1  1062 ? 26.130  63.820  106.433 1.00 31.38 ? 1060 LYS A N     1 
ATOM   7855  C  CA    . LYS A  1  1062 ? 26.703  64.942  107.168 1.00 30.16 ? 1060 LYS A CA    1 
ATOM   7856  C  C     . LYS A  1  1062 ? 27.011  64.606  108.623 1.00 34.16 ? 1060 LYS A C     1 
ATOM   7857  O  O     . LYS A  1  1062 ? 27.582  65.445  109.326 1.00 39.50 ? 1060 LYS A O     1 
ATOM   7858  C  CB    . LYS A  1  1062 ? 25.762  66.149  107.116 1.00 33.67 ? 1060 LYS A CB    1 
ATOM   7859  C  CG    . LYS A  1  1062 ? 25.648  66.825  105.752 1.00 38.25 ? 1060 LYS A CG    1 
ATOM   7860  C  CD    . LYS A  1  1062 ? 26.941  67.531  105.351 1.00 41.85 ? 1060 LYS A CD    1 
ATOM   7861  C  CE    . LYS A  1  1062 ? 26.799  68.223  103.999 1.00 47.56 ? 1060 LYS A CE    1 
ATOM   7862  N  NZ    . LYS A  1  1062 ? 28.042  68.929  103.572 1.00 45.41 ? 1060 LYS A NZ    1 
ATOM   7863  N  N     . GLY A  1  1063 ? 26.658  63.412  109.092 1.00 29.68 ? 1061 GLY A N     1 
ATOM   7864  C  CA    . GLY A  1  1063 ? 26.836  63.049  110.484 1.00 33.74 ? 1061 GLY A CA    1 
ATOM   7865  C  C     . GLY A  1  1063 ? 25.684  63.412  111.398 1.00 35.32 ? 1061 GLY A C     1 
ATOM   7866  O  O     . GLY A  1  1063 ? 25.778  63.172  112.612 1.00 32.99 ? 1061 GLY A O     1 
ATOM   7867  N  N     . ALA A  1  1064 ? 24.596  63.972  110.859 1.00 29.69 ? 1062 ALA A N     1 
ATOM   7868  C  CA    . ALA A  1  1064 ? 23.443  64.390  111.660 1.00 27.16 ? 1062 ALA A CA    1 
ATOM   7869  C  C     . ALA A  1  1064 ? 22.505  63.198  111.860 1.00 31.52 ? 1062 ALA A C     1 
ATOM   7870  O  O     . ALA A  1  1064 ? 21.382  63.133  111.346 1.00 24.76 ? 1062 ALA A O     1 
ATOM   7871  C  CB    . ALA A  1  1064 ? 22.741  65.571  110.999 1.00 28.23 ? 1062 ALA A CB    1 
ATOM   7872  N  N     . ARG A  1  1065 ? 23.003  62.236  112.637 1.00 27.78 ? 1063 ARG A N     1 
ATOM   7873  C  CA    . ARG A  1  1065 ? 22.352  60.935  112.731 1.00 27.56 ? 1063 ARG A CA    1 
ATOM   7874  C  C     . ARG A  1  1065 ? 20.998  61.027  113.428 1.00 27.52 ? 1063 ARG A C     1 
ATOM   7875  O  O     . ARG A  1  1065 ? 20.036  60.379  113.006 1.00 26.09 ? 1063 ARG A O     1 
ATOM   7876  C  CB    . ARG A  1  1065 ? 23.272  59.949  113.457 1.00 32.49 ? 1063 ARG A CB    1 
ATOM   7877  N  N     . ALA A  1  1066 ? 20.897  61.801  114.509 1.00 26.01 ? 1064 ALA A N     1 
ATOM   7878  C  CA    . ALA A  1  1066 ? 19.603  61.930  115.167 1.00 24.21 ? 1064 ALA A CA    1 
ATOM   7879  C  C     . ALA A  1  1066 ? 18.591  62.605  114.250 1.00 24.25 ? 1064 ALA A C     1 
ATOM   7880  O  O     . ALA A  1  1066 ? 17.429  62.199  114.198 1.00 22.93 ? 1064 ALA A O     1 
ATOM   7881  C  CB    . ALA A  1  1066 ? 19.742  62.705  116.479 1.00 27.21 ? 1064 ALA A CB    1 
ATOM   7882  N  N     . GLU A  1  1067 ? 19.015  63.636  113.521 1.00 24.37 ? 1065 GLU A N     1 
ATOM   7883  C  CA    . GLU A  1  1067 ? 18.090  64.307  112.620 1.00 24.22 ? 1065 GLU A CA    1 
ATOM   7884  C  C     . GLU A  1  1067 ? 17.698  63.405  111.461 1.00 21.78 ? 1065 GLU A C     1 
ATOM   7885  O  O     . GLU A  1  1067 ? 16.561  63.483  110.981 1.00 21.61 ? 1065 GLU A O     1 
ATOM   7886  C  CB    . GLU A  1  1067 ? 18.705  65.602  112.093 1.00 21.47 ? 1065 GLU A CB    1 
ATOM   7887  C  CG    . GLU A  1  1067 ? 18.799  66.731  113.130 1.00 21.32 ? 1065 GLU A CG    1 
ATOM   7888  C  CD    . GLU A  1  1067 ? 19.949  66.566  114.107 1.00 29.02 ? 1065 GLU A CD    1 
ATOM   7889  O  OE1   . GLU A  1  1067 ? 20.795  65.661  113.930 1.00 26.16 ? 1065 GLU A OE1   1 
ATOM   7890  O  OE2   . GLU A  1  1067 ? 19.998  67.354  115.075 1.00 30.75 ? 1065 GLU A OE2   1 
ATOM   7891  N  N     . ALA A  1  1068 ? 18.626  62.567  110.988 1.00 23.60 ? 1066 ALA A N     1 
ATOM   7892  C  CA    . ALA A  1  1068 ? 18.295  61.634  109.914 1.00 22.13 ? 1066 ALA A CA    1 
ATOM   7893  C  C     . ALA A  1  1068 ? 17.234  60.643  110.363 1.00 23.41 ? 1066 ALA A C     1 
ATOM   7894  O  O     . ALA A  1  1068 ? 16.317  60.309  109.597 1.00 20.88 ? 1066 ALA A O     1 
ATOM   7895  C  CB    . ALA A  1  1068 ? 19.551  60.895  109.452 1.00 24.23 ? 1066 ALA A CB    1 
ATOM   7896  N  N     . GLU A  1  1069 ? 17.355  60.147  111.595 1.00 22.37 ? 1067 GLU A N     1 
ATOM   7897  C  CA    . GLU A  1  1069 ? 16.330  59.281  112.160 1.00 23.48 ? 1067 GLU A CA    1 
ATOM   7898  C  C     . GLU A  1  1069 ? 15.000  60.012  112.265 1.00 25.10 ? 1067 GLU A C     1 
ATOM   7899  O  O     . GLU A  1  1069 ? 13.947  59.460  111.932 1.00 23.94 ? 1067 GLU A O     1 
ATOM   7900  C  CB    . GLU A  1  1069 ? 16.784  58.777  113.536 1.00 25.39 ? 1067 GLU A CB    1 
ATOM   7901  C  CG    . GLU A  1  1069 ? 15.684  58.144  114.371 1.00 31.74 ? 1067 GLU A CG    1 
ATOM   7902  C  CD    . GLU A  1  1069 ? 15.424  56.696  114.004 1.00 48.84 ? 1067 GLU A CD    1 
ATOM   7903  O  OE1   . GLU A  1  1069 ? 15.913  56.255  112.941 1.00 51.06 ? 1067 GLU A OE1   1 
ATOM   7904  O  OE2   . GLU A  1  1069 ? 14.735  55.998  114.781 1.00 58.63 ? 1067 GLU A OE2   1 
ATOM   7905  N  N     . ALA A  1  1070 ? 15.031  61.258  112.740 1.00 24.62 ? 1068 ALA A N     1 
ATOM   7906  C  CA    . ALA A  1  1070 ? 13.808  62.042  112.836 1.00 21.01 ? 1068 ALA A CA    1 
ATOM   7907  C  C     . ALA A  1  1070 ? 13.211  62.285  111.460 1.00 19.14 ? 1068 ALA A C     1 
ATOM   7908  O  O     . ALA A  1  1070 ? 11.984  62.312  111.302 1.00 21.74 ? 1068 ALA A O     1 
ATOM   7909  C  CB    . ALA A  1  1070 ? 14.089  63.371  113.535 1.00 23.15 ? 1068 ALA A CB    1 
ATOM   7910  N  N     . ALA A  1  1071 ? 14.065  62.475  110.457 1.00 20.05 ? 1069 ALA A N     1 
ATOM   7911  C  CA    . ALA A  1  1071 ? 13.573  62.656  109.098 1.00 16.95 ? 1069 ALA A CA    1 
ATOM   7912  C  C     . ALA A  1  1071 ? 12.892  61.386  108.611 1.00 21.23 ? 1069 ALA A C     1 
ATOM   7913  O  O     . ALA A  1  1071 ? 11.785  61.434  108.062 1.00 19.22 ? 1069 ALA A O     1 
ATOM   7914  C  CB    . ALA A  1  1071 ? 14.723  63.054  108.171 1.00 17.93 ? 1069 ALA A CB    1 
ATOM   7915  N  N     . ARG A  1  1072 ? 13.532  60.234  108.824 1.00 20.13 ? 1070 ARG A N     1 
ATOM   7916  C  CA    . ARG A  1  1072 ? 12.901  58.984  108.414 1.00 19.54 ? 1070 ARG A CA    1 
ATOM   7917  C  C     . ARG A  1  1072 ? 11.581  58.778  109.144 1.00 18.95 ? 1070 ARG A C     1 
ATOM   7918  O  O     . ARG A  1  1072 ? 10.592  58.333  108.550 1.00 20.98 ? 1070 ARG A O     1 
ATOM   7919  C  CB    . ARG A  1  1072 ? 13.851  57.813  108.657 1.00 20.14 ? 1070 ARG A CB    1 
ATOM   7920  C  CG    . ARG A  1  1072 ? 14.934  57.732  107.596 1.00 23.57 ? 1070 ARG A CG    1 
ATOM   7921  C  CD    . ARG A  1  1072 ? 15.772  56.468  107.751 1.00 26.86 ? 1070 ARG A CD    1 
ATOM   7922  N  NE    . ARG A  1  1072 ? 16.463  56.443  109.033 1.00 29.64 ? 1070 ARG A NE    1 
ATOM   7923  C  CZ    . ARG A  1  1072 ? 17.682  56.925  109.236 1.00 29.85 ? 1070 ARG A CZ    1 
ATOM   7924  N  NH1   . ARG A  1  1072 ? 18.386  57.472  108.254 1.00 30.73 ? 1070 ARG A NH1   1 
ATOM   7925  N  NH2   . ARG A  1  1072 ? 18.212  56.849  110.455 1.00 31.90 ? 1070 ARG A NH2   1 
ATOM   7926  N  N     . ASN A  1  1073 ? 11.539  59.119  110.428 1.00 20.14 ? 1071 ASN A N     1 
ATOM   7927  C  CA    . ASN A  1  1073 ? 10.300  58.989  111.177 1.00 20.29 ? 1071 ASN A CA    1 
ATOM   7928  C  C     . ASN A  1  1073 ? 9.227   59.923  110.633 1.00 22.64 ? 1071 ASN A C     1 
ATOM   7929  O  O     . ASN A  1  1073 ? 8.057   59.541  110.548 1.00 22.74 ? 1071 ASN A O     1 
ATOM   7930  C  CB    . ASN A  1  1073 ? 10.563  59.257  112.656 1.00 23.28 ? 1071 ASN A CB    1 
ATOM   7931  C  CG    . ASN A  1  1073 ? 11.312  58.124  113.320 1.00 29.61 ? 1071 ASN A CG    1 
ATOM   7932  O  OD1   . ASN A  1  1073 ? 11.337  56.999  112.817 1.00 32.74 ? 1071 ASN A OD1   1 
ATOM   7933  N  ND2   . ASN A  1  1073 ? 11.921  58.412  114.457 1.00 31.00 ? 1071 ASN A ND2   1 
ATOM   7934  N  N     . ALA A  1  1074 ? 9.612   61.146  110.250 1.00 19.60 ? 1072 ALA A N     1 
ATOM   7935  C  CA    . ALA A  1  1074 ? 8.660   62.055  109.624 1.00 19.60 ? 1072 ALA A CA    1 
ATOM   7936  C  C     . ALA A  1  1074 ? 8.146   61.475  108.319 1.00 18.81 ? 1072 ALA A C     1 
ATOM   7937  O  O     . ALA A  1  1074 ? 6.956   61.579  108.017 1.00 19.05 ? 1072 ALA A O     1 
ATOM   7938  C  CB    . ALA A  1  1074 ? 9.311   63.420  109.389 1.00 21.69 ? 1072 ALA A CB    1 
ATOM   7939  N  N     . GLY A  1  1075 ? 9.035   60.866  107.531 1.00 18.36 ? 1073 GLY A N     1 
ATOM   7940  C  CA    . GLY A  1  1075 ? 8.609   60.258  106.279 1.00 17.65 ? 1073 GLY A CA    1 
ATOM   7941  C  C     . GLY A  1  1075 ? 7.531   59.211  106.479 1.00 20.27 ? 1073 GLY A C     1 
ATOM   7942  O  O     . GLY A  1  1075 ? 6.565   59.150  105.714 1.00 20.68 ? 1073 GLY A O     1 
ATOM   7943  N  N     . SER A  1  1076 ? 7.679   58.381  107.517 1.00 18.69 ? 1074 SER A N     1 
ATOM   7944  C  CA    . SER A  1  1076 ? 6.688   57.350  107.829 1.00 20.21 ? 1074 SER A CA    1 
ATOM   7945  C  C     . SER A  1  1076 ? 5.426   57.935  108.441 1.00 21.34 ? 1074 SER A C     1 
ATOM   7946  O  O     . SER A  1  1076 ? 4.318   57.490  108.126 1.00 23.56 ? 1074 SER A O     1 
ATOM   7947  C  CB    . SER A  1  1076 ? 7.276   56.318  108.795 1.00 22.40 ? 1074 SER A CB    1 
ATOM   7948  O  OG    . SER A  1  1076 ? 8.307   55.599  108.177 1.00 30.48 ? 1074 SER A OG    1 
ATOM   7949  N  N     . SER A  1  1077 ? 5.578   58.915  109.336 1.00 19.89 ? 1075 SER A N     1 
ATOM   7950  C  CA    A SER A  1  1077 ? 4.422   59.483  110.023 0.42 21.86 ? 1075 SER A CA    1 
ATOM   7951  C  CA    B SER A  1  1077 ? 4.442   59.512  110.034 0.58 21.86 ? 1075 SER A CA    1 
ATOM   7952  C  C     . SER A  1  1077 ? 3.562   60.332  109.096 1.00 22.58 ? 1075 SER A C     1 
ATOM   7953  O  O     . SER A  1  1077 ? 2.363   60.495  109.348 1.00 22.93 ? 1075 SER A O     1 
ATOM   7954  C  CB    A SER A  1  1077 ? 4.879   60.310  111.223 0.42 21.73 ? 1075 SER A CB    1 
ATOM   7955  C  CB    B SER A  1  1077 ? 4.963   60.382  111.184 0.58 21.66 ? 1075 SER A CB    1 
ATOM   7956  O  OG    A SER A  1  1077 ? 5.390   59.468  112.236 0.42 25.00 ? 1075 SER A OG    1 
ATOM   7957  O  OG    B SER A  1  1077 ? 3.930   61.118  111.813 0.58 24.94 ? 1075 SER A OG    1 
ATOM   7958  N  N     . SER A  1  1078 ? 4.140   60.874  108.037 1.00 18.96 ? 1076 SER A N     1 
ATOM   7959  C  CA    . SER A  1  1078 ? 3.380   61.691  107.107 1.00 18.62 ? 1076 SER A CA    1 
ATOM   7960  C  C     . SER A  1  1078 ? 2.234   60.889  106.508 1.00 20.32 ? 1076 SER A C     1 
ATOM   7961  O  O     . SER A  1  1078 ? 2.387   59.715  106.172 1.00 19.64 ? 1076 SER A O     1 
ATOM   7962  C  CB    . SER A  1  1078 ? 4.294   62.169  105.992 1.00 16.96 ? 1076 SER A CB    1 
ATOM   7963  O  OG    . SER A  1  1078 ? 3.520   62.860  105.025 1.00 16.48 ? 1076 SER A OG    1 
ATOM   7964  N  N     . ALA A  1  1079 ? 1.080   61.525  106.364 1.00 15.77 ? 1077 ALA A N     1 
ATOM   7965  C  CA    . ALA A  1  1079 ? -0.028  60.892  105.672 1.00 18.70 ? 1077 ALA A CA    1 
ATOM   7966  C  C     . ALA A  1  1079 ? -0.176  61.417  104.257 1.00 17.29 ? 1077 ALA A C     1 
ATOM   7967  O  O     . ALA A  1  1079 ? -1.205  61.185  103.618 1.00 17.78 ? 1077 ALA A O     1 
ATOM   7968  C  CB    . ALA A  1  1079 ? -1.328  61.079  106.455 1.00 18.03 ? 1077 ALA A CB    1 
ATOM   7969  N  N     . LEU A  1  1080 ? 0.823   62.142  103.764 1.00 15.01 ? 1078 LEU A N     1 
ATOM   7970  C  CA    . LEU A  1  1080 ? 0.872   62.512  102.358 1.00 15.68 ? 1078 LEU A CA    1 
ATOM   7971  C  C     . LEU A  1  1080 ? 0.630   61.282  101.506 1.00 17.20 ? 1078 LEU A C     1 
ATOM   7972  O  O     . LEU A  1  1080 ? 1.281   60.253  101.693 1.00 18.04 ? 1078 LEU A O     1 
ATOM   7973  C  CB    . LEU A  1  1080 ? 2.243   63.102  102.046 1.00 15.87 ? 1078 LEU A CB    1 
ATOM   7974  C  CG    . LEU A  1  1080 ? 2.516   63.412  100.579 1.00 16.36 ? 1078 LEU A CG    1 
ATOM   7975  C  CD1   . LEU A  1  1080 ? 1.661   64.600  100.136 1.00 21.30 ? 1078 LEU A CD1   1 
ATOM   7976  C  CD2   . LEU A  1  1080 ? 4.009   63.678  100.377 1.00 17.74 ? 1078 LEU A CD2   1 
ATOM   7977  N  N     . GLY A  1  1081 ? -0.309  61.384  100.571 1.00 16.18 ? 1079 GLY A N     1 
ATOM   7978  C  CA    . GLY A  1  1081 ? -0.610  60.251  99.723  1.00 19.50 ? 1079 GLY A CA    1 
ATOM   7979  C  C     . GLY A  1  1081 ? -1.838  59.477  100.137 1.00 16.93 ? 1079 GLY A C     1 
ATOM   7980  O  O     . GLY A  1  1081 ? -2.270  58.590  99.389  1.00 18.86 ? 1079 GLY A O     1 
ATOM   7981  N  N     . LEU A  1  1082 ? -2.397  59.769  101.308 1.00 15.70 ? 1080 LEU A N     1 
ATOM   7982  C  CA    A LEU A  1  1082 ? -3.673  59.181  101.686 0.52 16.18 ? 1080 LEU A CA    1 
ATOM   7983  C  CA    B LEU A  1  1082 ? -3.676  59.181  101.687 0.48 16.18 ? 1080 LEU A CA    1 
ATOM   7984  C  C     . LEU A  1  1082 ? -4.689  59.407  100.572 1.00 16.31 ? 1080 LEU A C     1 
ATOM   7985  O  O     . LEU A  1  1082 ? -4.780  60.498  100.007 1.00 17.54 ? 1080 LEU A O     1 
ATOM   7986  C  CB    A LEU A  1  1082 ? -4.163  59.805  102.993 0.52 16.89 ? 1080 LEU A CB    1 
ATOM   7987  C  CB    B LEU A  1  1082 ? -4.173  59.800  102.997 0.48 16.89 ? 1080 LEU A CB    1 
ATOM   7988  C  CG    A LEU A  1  1082 ? -5.495  59.310  103.540 0.52 16.98 ? 1080 LEU A CG    1 
ATOM   7989  C  CG    B LEU A  1  1082 ? -5.544  59.402  103.545 0.48 17.00 ? 1080 LEU A CG    1 
ATOM   7990  C  CD1   A LEU A  1  1082 ? -5.450  57.814  103.722 0.52 17.86 ? 1080 LEU A CD1   1 
ATOM   7991  C  CD1   B LEU A  1  1082 ? -5.559  59.585  105.051 0.48 17.67 ? 1080 LEU A CD1   1 
ATOM   7992  C  CD2   A LEU A  1  1082 ? -5.807  60.009  104.853 0.52 17.78 ? 1080 LEU A CD2   1 
ATOM   7993  C  CD2   B LEU A  1  1082 ? -6.676  60.218  102.905 0.48 16.28 ? 1080 LEU A CD2   1 
ATOM   7994  N  N     . ASP A  1  1083 ? -5.443  58.361  100.250 1.00 17.40 ? 1081 ASP A N     1 
ATOM   7995  C  CA    . ASP A  1  1083 ? -6.345  58.413  99.102  1.00 18.69 ? 1081 ASP A CA    1 
ATOM   7996  C  C     . ASP A  1  1083 ? -7.523  57.501  99.425  1.00 20.62 ? 1081 ASP A C     1 
ATOM   7997  O  O     . ASP A  1  1083 ? -7.419  56.277  99.293  1.00 25.11 ? 1081 ASP A O     1 
ATOM   7998  C  CB    . ASP A  1  1083 ? -5.611  57.981  97.837  1.00 22.74 ? 1081 ASP A CB    1 
ATOM   7999  C  CG    . ASP A  1  1083 ? -6.433  58.159  96.584  1.00 34.64 ? 1081 ASP A CG    1 
ATOM   8000  O  OD1   . ASP A  1  1083 ? -7.536  58.730  96.655  1.00 36.04 ? 1081 ASP A OD1   1 
ATOM   8001  O  OD2   . ASP A  1  1083 ? -5.961  57.723  95.517  1.00 36.15 ? 1081 ASP A OD2   1 
ATOM   8002  N  N     . LEU A  1  1084 ? -8.624  58.100  99.862  1.00 18.67 ? 1082 LEU A N     1 
ATOM   8003  C  CA    . LEU A  1  1084 ? -9.750  57.344  100.384 1.00 17.65 ? 1082 LEU A CA    1 
ATOM   8004  C  C     . LEU A  1  1084 ? -10.998 57.636  99.578  1.00 18.69 ? 1082 LEU A C     1 
ATOM   8005  O  O     . LEU A  1  1084 ? -11.141 58.710  98.991  1.00 21.01 ? 1082 LEU A O     1 
ATOM   8006  C  CB    . LEU A  1  1084 ? -10.045 57.689  101.844 1.00 19.27 ? 1082 LEU A CB    1 
ATOM   8007  C  CG    . LEU A  1  1084 ? -8.945  57.437  102.853 1.00 22.71 ? 1082 LEU A CG    1 
ATOM   8008  C  CD1   . LEU A  1  1084 ? -9.396  57.983  104.201 1.00 22.78 ? 1082 LEU A CD1   1 
ATOM   8009  C  CD2   . LEU A  1  1084 ? -8.663  55.957  102.908 1.00 23.93 ? 1082 LEU A CD2   1 
ATOM   8010  N  N     . GLU A  1  1085 ? -11.896 56.663  99.560  1.00 21.40 ? 1083 GLU A N     1 
ATOM   8011  C  CA    . GLU A  1  1085 ? -13.254 56.878  99.093  1.00 19.16 ? 1083 GLU A CA    1 
ATOM   8012  C  C     . GLU A  1  1085 ? -14.161 56.865  100.310 1.00 20.89 ? 1083 GLU A C     1 
ATOM   8013  O  O     . GLU A  1  1085 ? -14.119 55.924  101.113 1.00 23.85 ? 1083 GLU A O     1 
ATOM   8014  C  CB    . GLU A  1  1085 ? -13.695 55.826  98.074  1.00 18.68 ? 1083 GLU A CB    1 
ATOM   8015  C  CG    . GLU A  1  1085 ? -15.165 56.015  97.722  1.00 23.07 ? 1083 GLU A CG    1 
ATOM   8016  C  CD    . GLU A  1  1085 ? -15.649 55.223  96.521  1.00 29.23 ? 1083 GLU A CD    1 
ATOM   8017  O  OE1   . GLU A  1  1085 ? -14.819 54.633  95.797  1.00 31.66 ? 1083 GLU A OE1   1 
ATOM   8018  O  OE2   . GLU A  1  1085 ? -16.885 55.202  96.314  1.00 31.27 ? 1083 GLU A OE2   1 
ATOM   8019  N  N     . LEU A  1  1086 ? -14.942 57.921  100.466 1.00 19.72 ? 1084 LEU A N     1 
ATOM   8020  C  CA    . LEU A  1  1086 ? -15.824 58.074  101.608 1.00 20.56 ? 1084 LEU A CA    1 
ATOM   8021  C  C     . LEU A  1  1086 ? -17.211 57.536  101.274 1.00 22.08 ? 1084 LEU A C     1 
ATOM   8022  O  O     . LEU A  1  1086 ? -17.682 57.692  100.144 1.00 20.96 ? 1084 LEU A O     1 
ATOM   8023  C  CB    . LEU A  1  1086 ? -15.932 59.542  102.011 1.00 20.57 ? 1084 LEU A CB    1 
ATOM   8024  C  CG    . LEU A  1  1086 ? -14.582 60.218  102.273 1.00 21.28 ? 1084 LEU A CG    1 
ATOM   8025  C  CD1   . LEU A  1  1086 ? -14.790 61.667  102.708 1.00 21.25 ? 1084 LEU A CD1   1 
ATOM   8026  C  CD2   . LEU A  1  1086 ? -13.782 59.439  103.320 1.00 22.06 ? 1084 LEU A CD2   1 
ATOM   8027  N  N     . PRO A  1  1087 ? -17.852 56.892  102.241 1.00 22.67 ? 1085 PRO A N     1 
ATOM   8028  C  CA    . PRO A  1  1087 ? -19.212 56.394  102.016 1.00 21.64 ? 1085 PRO A CA    1 
ATOM   8029  C  C     . PRO A  1  1087 ? -20.169 57.532  101.723 1.00 20.99 ? 1085 PRO A C     1 
ATOM   8030  O  O     . PRO A  1  1087 ? -20.119 58.592  102.348 1.00 23.36 ? 1085 PRO A O     1 
ATOM   8031  C  CB    . PRO A  1  1087 ? -19.568 55.711  103.342 1.00 22.44 ? 1085 PRO A CB    1 
ATOM   8032  C  CG    . PRO A  1  1087 ? -18.272 55.430  103.996 1.00 24.12 ? 1085 PRO A CG    1 
ATOM   8033  C  CD    . PRO A  1  1087 ? -17.306 56.476  103.543 1.00 20.19 ? 1085 PRO A CD    1 
ATOM   8034  N  N     . GLY A  1  1088 ? -21.074 57.286  100.784 1.00 20.73 ? 1086 GLY A N     1 
ATOM   8035  C  CA    . GLY A  1  1088 ? -22.074 58.258  100.442 1.00 21.72 ? 1086 GLY A CA    1 
ATOM   8036  C  C     . GLY A  1  1088 ? -23.143 57.639  99.577  1.00 17.05 ? 1086 GLY A C     1 
ATOM   8037  O  O     . GLY A  1  1088 ? -23.331 56.422  99.550  1.00 18.87 ? 1086 GLY A O     1 
ATOM   8038  N  N     . PRO A  1  1089 ? -23.842 58.477  98.827  1.00 20.38 ? 1087 PRO A N     1 
ATOM   8039  C  CA    . PRO A  1  1089 ? -24.947 57.984  98.010  1.00 18.58 ? 1087 PRO A CA    1 
ATOM   8040  C  C     . PRO A  1  1089 ? -24.437 57.200  96.813  1.00 22.54 ? 1087 PRO A C     1 
ATOM   8041  O  O     . PRO A  1  1089 ? -23.302 57.356  96.358  1.00 21.03 ? 1087 PRO A O     1 
ATOM   8042  C  CB    . PRO A  1  1089 ? -25.651 59.266  97.566  1.00 21.52 ? 1087 PRO A CB    1 
ATOM   8043  C  CG    . PRO A  1  1089 ? -24.533 60.290  97.558  1.00 24.34 ? 1087 PRO A CG    1 
ATOM   8044  C  CD    . PRO A  1  1089 ? -23.652 59.932  98.704  1.00 23.27 ? 1087 PRO A CD    1 
ATOM   8045  N  N     . VAL A  1  1090 ? -25.316 56.338  96.302  1.00 19.07 ? 1088 VAL A N     1 
ATOM   8046  C  CA    . VAL A  1  1090 ? -25.019 55.663  95.046  1.00 16.81 ? 1088 VAL A CA    1 
ATOM   8047  C  C     . VAL A  1  1090 ? -24.913 56.693  93.936  1.00 17.39 ? 1088 VAL A C     1 
ATOM   8048  O  O     . VAL A  1  1090 ? -25.406 57.822  94.041  1.00 19.85 ? 1088 VAL A O     1 
ATOM   8049  C  CB    . VAL A  1  1090 ? -26.085 54.613  94.699  1.00 18.55 ? 1088 VAL A CB    1 
ATOM   8050  C  CG1   . VAL A  1  1090 ? -26.115 53.529  95.755  1.00 21.48 ? 1088 VAL A CG1   1 
ATOM   8051  C  CG2   . VAL A  1  1090 ? -27.460 55.269  94.582  1.00 20.65 ? 1088 VAL A CG2   1 
ATOM   8052  N  N     . GLY A  1  1091 ? -24.254 56.297  92.854  1.00 18.45 ? 1089 GLY A N     1 
ATOM   8053  C  CA    . GLY A  1  1091 ? -24.170 57.195  91.715  1.00 18.87 ? 1089 GLY A CA    1 
ATOM   8054  C  C     . GLY A  1  1091 ? -23.216 58.342  91.903  1.00 17.66 ? 1089 GLY A C     1 
ATOM   8055  O  O     . GLY A  1  1091 ? -23.252 59.300  91.133  1.00 17.19 ? 1089 GLY A O     1 
ATOM   8056  N  N     . GLU A  1  1092 ? -22.358 58.268  92.914  1.00 16.88 ? 1090 GLU A N     1 
ATOM   8057  C  CA    . GLU A  1  1092 ? -21.382 59.300  93.181  1.00 19.22 ? 1090 GLU A CA    1 
ATOM   8058  C  C     . GLU A  1  1092 ? -20.175 58.612  93.791  1.00 18.12 ? 1090 GLU A C     1 
ATOM   8059  O  O     . GLU A  1  1092 ? -20.321 57.641  94.543  1.00 20.40 ? 1090 GLU A O     1 
ATOM   8060  C  CB    . GLU A  1  1092 ? -21.959 60.342  94.138  1.00 19.94 ? 1090 GLU A CB    1 
ATOM   8061  C  CG    . GLU A  1  1092 ? -21.307 61.706  94.112  1.00 23.48 ? 1090 GLU A CG    1 
ATOM   8062  C  CD    . GLU A  1  1092 ? -22.107 62.693  94.944  1.00 26.19 ? 1090 GLU A CD    1 
ATOM   8063  O  OE1   . GLU A  1  1092 ? -21.999 62.619  96.179  1.00 22.64 ? 1090 GLU A OE1   1 
ATOM   8064  O  OE2   . GLU A  1  1092 ? -22.884 63.498  94.371  1.00 25.64 ? 1090 GLU A OE2   1 
ATOM   8065  N  N     . ARG A  1  1093 ? -18.991 59.099  93.451  1.00 16.25 ? 1091 ARG A N     1 
ATOM   8066  C  CA    . ARG A  1  1093 ? -17.755 58.666  94.093  1.00 17.58 ? 1091 ARG A CA    1 
ATOM   8067  C  C     . ARG A  1  1093 ? -17.182 59.868  94.816  1.00 19.55 ? 1091 ARG A C     1 
ATOM   8068  O  O     . ARG A  1  1093 ? -16.901 60.898  94.197  1.00 17.83 ? 1091 ARG A O     1 
ATOM   8069  C  CB    . ARG A  1  1093 ? -16.743 58.116  93.086  1.00 23.61 ? 1091 ARG A CB    1 
ATOM   8070  C  CG    . ARG A  1  1093 ? -16.983 56.677  92.679  1.00 34.42 ? 1091 ARG A CG    1 
ATOM   8071  C  CD    . ARG A  1  1093 ? -15.971 56.191  91.628  1.00 42.05 ? 1091 ARG A CD    1 
ATOM   8072  N  NE    . ARG A  1  1093 ? -14.594 56.151  92.112  1.00 43.52 ? 1091 ARG A NE    1 
ATOM   8073  C  CZ    . ARG A  1  1093 ? -13.569 56.750  91.515  1.00 54.25 ? 1091 ARG A CZ    1 
ATOM   8074  N  NH1   . ARG A  1  1093 ? -13.732 57.469  90.415  1.00 52.26 ? 1091 ARG A NH1   1 
ATOM   8075  N  NH2   . ARG A  1  1093 ? -12.347 56.613  92.025  1.00 51.26 ? 1091 ARG A NH2   1 
ATOM   8076  N  N     . ASN A  1  1094 ? -17.015 59.742  96.119  1.00 17.13 ? 1092 ASN A N     1 
ATOM   8077  C  CA    . ASN A  1  1094 ? -16.548 60.850  96.926  1.00 15.94 ? 1092 ASN A CA    1 
ATOM   8078  C  C     . ASN A  1  1094 ? -15.183 60.505  97.481  1.00 17.81 ? 1092 ASN A C     1 
ATOM   8079  O  O     . ASN A  1  1094 ? -15.044 59.550  98.248  1.00 19.09 ? 1092 ASN A O     1 
ATOM   8080  C  CB    . ASN A  1  1094 ? -17.563 61.155  98.008  1.00 16.20 ? 1092 ASN A CB    1 
ATOM   8081  C  CG    . ASN A  1  1094 ? -18.781 61.793  97.424  1.00 17.52 ? 1092 ASN A CG    1 
ATOM   8082  O  OD1   . ASN A  1  1094 ? -18.696 62.909  96.938  1.00 18.38 ? 1092 ASN A OD1   1 
ATOM   8083  N  ND2   . ASN A  1  1094 ? -19.905 61.077  97.402  1.00 18.88 ? 1092 ASN A ND2   1 
ATOM   8084  N  N     . LEU A  1  1095 ? -14.182 61.256  97.045  1.00 17.31 ? 1093 LEU A N     1 
ATOM   8085  C  CA    . LEU A  1  1095 ? -12.787 60.949  97.290  1.00 15.84 ? 1093 LEU A CA    1 
ATOM   8086  C  C     . LEU A  1  1095 ? -12.177 61.986  98.214  1.00 15.62 ? 1093 LEU A C     1 
ATOM   8087  O  O     . LEU A  1  1095 ? -12.535 63.164  98.195  1.00 18.74 ? 1093 LEU A O     1 
ATOM   8088  C  CB    . LEU A  1  1095 ? -12.008 60.921  95.981  1.00 18.58 ? 1093 LEU A CB    1 
ATOM   8089  C  CG    . LEU A  1  1095 ? -12.689 59.994  94.972  1.00 20.37 ? 1093 LEU A CG    1 
ATOM   8090  C  CD1   . LEU A  1  1095 ? -11.920 60.012  93.662  1.00 27.25 ? 1093 LEU A CD1   1 
ATOM   8091  C  CD2   . LEU A  1  1095 ? -12.838 58.558  95.499  1.00 24.90 ? 1093 LEU A CD2   1 
ATOM   8092  N  N     . TYR A  1  1096 ? -11.240 61.526  99.027  1.00 17.64 ? 1094 TYR A N     1 
ATOM   8093  C  CA    . TYR A  1  1096 ? -10.602 62.391  100.007 1.00 17.12 ? 1094 TYR A CA    1 
ATOM   8094  C  C     . TYR A  1  1096 ? -9.131  62.059  99.954  1.00 15.69 ? 1094 TYR A C     1 
ATOM   8095  O  O     . TYR A  1  1096 ? -8.768  60.890  100.124 1.00 17.70 ? 1094 TYR A O     1 
ATOM   8096  C  CB    . TYR A  1  1096 ? -11.174 62.139  101.392 1.00 16.85 ? 1094 TYR A CB    1 
ATOM   8097  C  CG    . TYR A  1  1096 ? -10.457 62.829  102.533 1.00 16.55 ? 1094 TYR A CG    1 
ATOM   8098  C  CD1   . TYR A  1  1096 ? -10.796 64.117  102.919 1.00 18.94 ? 1094 TYR A CD1   1 
ATOM   8099  C  CD2   . TYR A  1  1096 ? -9.470  62.163  103.254 1.00 18.57 ? 1094 TYR A CD2   1 
ATOM   8100  C  CE1   . TYR A  1  1096 ? -10.145 64.732  103.975 1.00 22.09 ? 1094 TYR A CE1   1 
ATOM   8101  C  CE2   . TYR A  1  1096 ? -8.821  62.774  104.316 1.00 19.31 ? 1094 TYR A CE2   1 
ATOM   8102  C  CZ    . TYR A  1  1096 ? -9.171  64.057  104.670 1.00 20.13 ? 1094 TYR A CZ    1 
ATOM   8103  O  OH    . TYR A  1  1096 ? -8.547  64.676  105.732 1.00 18.92 ? 1094 TYR A OH    1 
ATOM   8104  N  N     . THR A  1  1097 ? -8.300  63.063  99.687  1.00 16.45 ? 1095 THR A N     1 
ATOM   8105  C  CA    A THR A  1  1097 ? -6.880  62.832  99.455  0.59 17.55 ? 1095 THR A CA    1 
ATOM   8106  C  CA    B THR A  1  1097 ? -6.888  62.844  99.438  0.41 17.56 ? 1095 THR A CA    1 
ATOM   8107  C  C     . THR A  1  1097 ? -6.055  63.883  100.178 1.00 17.66 ? 1095 THR A C     1 
ATOM   8108  O  O     . THR A  1  1097 ? -6.489  65.021  100.369 1.00 17.97 ? 1095 THR A O     1 
ATOM   8109  C  CB    A THR A  1  1097 ? -6.513  62.864  97.966  0.59 18.78 ? 1095 THR A CB    1 
ATOM   8110  C  CB    B THR A  1  1097 ? -6.635  62.901  97.938  0.41 18.81 ? 1095 THR A CB    1 
ATOM   8111  O  OG1   A THR A  1  1097 ? -6.924  64.108  97.393  0.59 16.66 ? 1095 THR A OG1   1 
ATOM   8112  O  OG1   B THR A  1  1097 ? -7.626  62.106  97.276  0.41 21.80 ? 1095 THR A OG1   1 
ATOM   8113  C  CG2   A THR A  1  1097 ? -7.173  61.728  97.216  0.59 19.98 ? 1095 THR A CG2   1 
ATOM   8114  C  CG2   B THR A  1  1097 ? -5.303  62.341  97.626  0.41 17.77 ? 1095 THR A CG2   1 
ATOM   8115  N  N     . LEU A  1  1098 ? -4.852  63.487  100.584 1.00 17.55 ? 1096 LEU A N     1 
ATOM   8116  C  CA    . LEU A  1  1098 ? -3.911  64.395  101.236 1.00 16.25 ? 1096 LEU A CA    1 
ATOM   8117  C  C     . LEU A  1  1098 ? -2.728  64.661  100.317 1.00 15.08 ? 1096 LEU A C     1 
ATOM   8118  O  O     . LEU A  1  1098 ? -2.025  63.727  99.901  1.00 16.80 ? 1096 LEU A O     1 
ATOM   8119  C  CB    . LEU A  1  1098 ? -3.422  63.834  102.570 1.00 17.20 ? 1096 LEU A CB    1 
ATOM   8120  C  CG    . LEU A  1  1098 ? -4.520  63.625  103.609 1.00 14.75 ? 1096 LEU A CG    1 
ATOM   8121  C  CD1   . LEU A  1  1098 ? -3.878  63.090  104.886 1.00 17.41 ? 1096 LEU A CD1   1 
ATOM   8122  C  CD2   . LEU A  1  1098 ? -5.330  64.922  103.863 1.00 16.10 ? 1096 LEU A CD2   1 
ATOM   8123  N  N     . HIS A  1  1099 ? -2.508  65.938  100.017 1.00 16.75 ? 1097 HIS A N     1 
ATOM   8124  C  CA    . HIS A  1  1099 ? -1.479  66.425  99.119  1.00 18.56 ? 1097 HIS A CA    1 
ATOM   8125  C  C     . HIS A  1  1099 ? -0.528  67.327  99.886  1.00 17.64 ? 1097 HIS A C     1 
ATOM   8126  O  O     . HIS A  1  1099 ? -0.777  67.687  101.034 1.00 18.03 ? 1097 HIS A O     1 
ATOM   8127  C  CB    . HIS A  1  1099 ? -2.110  67.223  97.974  1.00 17.17 ? 1097 HIS A CB    1 
ATOM   8128  C  CG    . HIS A  1  1099 ? -3.082  66.434  97.159  1.00 23.77 ? 1097 HIS A CG    1 
ATOM   8129  N  ND1   . HIS A  1  1099 ? -2.749  65.877  95.943  1.00 25.16 ? 1097 HIS A ND1   1 
ATOM   8130  C  CD2   . HIS A  1  1099 ? -4.373  66.096  97.390  1.00 23.33 ? 1097 HIS A CD2   1 
ATOM   8131  C  CE1   . HIS A  1  1099 ? -3.797  65.242  95.450  1.00 25.47 ? 1097 HIS A CE1   1 
ATOM   8132  N  NE2   . HIS A  1  1099 ? -4.797  65.364  96.306  1.00 23.81 ? 1097 HIS A NE2   1 
ATOM   8133  N  N     . ALA A  1  1100 ? 0.555   67.717  99.223  1.00 17.99 ? 1098 ALA A N     1 
ATOM   8134  C  CA    . ALA A  1  1100 ? 1.397   68.769  99.772  1.00 16.48 ? 1098 ALA A CA    1 
ATOM   8135  C  C     . ALA A  1  1100 ? 0.607   70.072  99.849  1.00 20.25 ? 1098 ALA A C     1 
ATOM   8136  O  O     . ALA A  1  1100 ? -0.312  70.314  99.064  1.00 21.21 ? 1098 ALA A O     1 
ATOM   8137  C  CB    . ALA A  1  1100 ? 2.638   68.966  98.902  1.00 17.91 ? 1098 ALA A CB    1 
ATOM   8138  N  N     . ARG A  1  1101 ? 0.969   70.921  100.807 1.00 20.03 ? 1099 ARG A N     1 
ATOM   8139  C  CA    A ARG A  1  1101 ? 0.361   72.245  100.871 0.56 20.87 ? 1099 ARG A CA    1 
ATOM   8140  C  CA    B ARG A  1  1101 ? 0.357   72.242  100.869 0.44 20.88 ? 1099 ARG A CA    1 
ATOM   8141  C  C     . ARG A  1  1101 ? 0.941   73.177  99.819  1.00 18.81 ? 1099 ARG A C     1 
ATOM   8142  O  O     . ARG A  1  1101 ? 0.208   73.958  99.208  1.00 21.30 ? 1099 ARG A O     1 
ATOM   8143  C  CB    A ARG A  1  1101 ? 0.549   72.860  102.256 0.56 22.76 ? 1099 ARG A CB    1 
ATOM   8144  C  CB    B ARG A  1  1101 ? 0.525   72.844  102.265 0.44 22.75 ? 1099 ARG A CB    1 
ATOM   8145  C  CG    A ARG A  1  1101 ? -0.222  72.163  103.351 0.56 23.60 ? 1099 ARG A CG    1 
ATOM   8146  C  CG    B ARG A  1  1101 ? -0.438  72.287  103.304 0.44 24.09 ? 1099 ARG A CG    1 
ATOM   8147  C  CD    A ARG A  1  1101 ? -0.104  72.908  104.662 0.56 19.02 ? 1099 ARG A CD    1 
ATOM   8148  C  CD    B ARG A  1  1101 ? -1.218  73.403  103.982 0.44 24.35 ? 1099 ARG A CD    1 
ATOM   8149  N  NE    A ARG A  1  1101 ? -1.018  74.037  104.786 0.56 20.03 ? 1099 ARG A NE    1 
ATOM   8150  N  NE    B ARG A  1  1101 ? -2.293  72.901  104.835 0.44 21.40 ? 1099 ARG A NE    1 
ATOM   8151  C  CZ    A ARG A  1  1101 ? -2.263  73.943  105.235 0.56 21.37 ? 1099 ARG A CZ    1 
ATOM   8152  C  CZ    B ARG A  1  1101 ? -3.021  73.659  105.648 0.44 24.55 ? 1099 ARG A CZ    1 
ATOM   8153  N  NH1   A ARG A  1  1101 ? -2.798  72.774  105.557 0.56 24.14 ? 1099 ARG A NH1   1 
ATOM   8154  N  NH1   B ARG A  1  1101 ? -2.808  74.962  105.759 0.44 22.04 ? 1099 ARG A NH1   1 
ATOM   8155  N  NH2   A ARG A  1  1101 ? -2.997  75.048  105.356 0.56 22.57 ? 1099 ARG A NH2   1 
ATOM   8156  N  NH2   B ARG A  1  1101 ? -3.984  73.096  106.373 0.44 22.20 ? 1099 ARG A NH2   1 
ATOM   8157  N  N     . GLY A  1  1102 ? 2.245   73.114  99.599  1.00 19.85 ? 1100 GLY A N     1 
ATOM   8158  C  CA    . GLY A  1  1102 ? 2.872   74.025  98.665  1.00 20.78 ? 1100 GLY A CA    1 
ATOM   8159  C  C     . GLY A  1  1102 ? 4.249   74.396  99.150  1.00 19.88 ? 1100 GLY A C     1 
ATOM   8160  O  O     . GLY A  1  1102 ? 5.060   73.516  99.446  1.00 20.25 ? 1100 GLY A O     1 
ATOM   8161  N  N     . ARG A  1  1103 ? 4.535   75.690  99.250  1.00 19.82 ? 1101 ARG A N     1 
ATOM   8162  C  CA    . ARG A  1  1103 ? 5.825   76.142  99.742  1.00 19.00 ? 1101 ARG A CA    1 
ATOM   8163  C  C     . ARG A  1  1103 ? 5.639   76.594  101.181 1.00 17.57 ? 1101 ARG A C     1 
ATOM   8164  O  O     . ARG A  1  1103 ? 4.800   77.459  101.461 1.00 21.19 ? 1101 ARG A O     1 
ATOM   8165  C  CB    . ARG A  1  1103 ? 6.406   77.274  98.891  1.00 21.64 ? 1101 ARG A CB    1 
ATOM   8166  C  CG    . ARG A  1  1103 ? 7.886   77.533  99.232  1.00 24.78 ? 1101 ARG A CG    1 
ATOM   8167  C  CD    . ARG A  1  1103 ? 8.591   78.438  98.227  1.00 25.32 ? 1101 ARG A CD    1 
ATOM   8168  N  NE    . ARG A  1  1103 ? 8.698   77.803  96.915  1.00 31.98 ? 1101 ARG A NE    1 
ATOM   8169  C  CZ    . ARG A  1  1103 ? 9.729   77.082  96.483  1.00 35.65 ? 1101 ARG A CZ    1 
ATOM   8170  N  NH1   . ARG A  1  1103 ? 10.802  76.860  97.236  1.00 27.64 ? 1101 ARG A NH1   1 
ATOM   8171  N  NH2   . ARG A  1  1103 ? 9.683   76.566  95.258  1.00 42.48 ? 1101 ARG A NH2   1 
ATOM   8172  N  N     . ILE A  1  1104 ? 6.388   75.979  102.093 1.00 16.37 ? 1102 ILE A N     1 
ATOM   8173  C  CA    . ILE A  1  1104 ? 6.288   76.293  103.516 1.00 18.40 ? 1102 ILE A CA    1 
ATOM   8174  C  C     . ILE A  1  1104 ? 7.406   77.256  103.869 1.00 19.06 ? 1102 ILE A C     1 
ATOM   8175  O  O     . ILE A  1  1104 ? 8.567   77.022  103.516 1.00 18.24 ? 1102 ILE A O     1 
ATOM   8176  C  CB    . ILE A  1  1104 ? 6.372   75.020  104.379 1.00 16.60 ? 1102 ILE A CB    1 
ATOM   8177  C  CG1   . ILE A  1  1104 ? 5.322   73.995  103.930 1.00 18.39 ? 1102 ILE A CG1   1 
ATOM   8178  C  CG2   . ILE A  1  1104 ? 6.171   75.369  105.850 1.00 17.65 ? 1102 ILE A CG2   1 
ATOM   8179  C  CD1   . ILE A  1  1104 ? 3.902   74.460  104.086 1.00 19.88 ? 1102 ILE A CD1   1 
ATOM   8180  N  N     . LEU A  1  1105 ? 7.053   78.346  104.548 1.00 17.56 ? 1103 LEU A N     1 
ATOM   8181  C  CA    . LEU A  1  1105 ? 8.040   79.278  105.079 1.00 20.46 ? 1103 LEU A CA    1 
ATOM   8182  C  C     . LEU A  1  1105 ? 8.693   78.669  106.310 1.00 18.90 ? 1103 LEU A C     1 
ATOM   8183  O  O     . LEU A  1  1105 ? 8.002   78.329  107.275 1.00 21.30 ? 1103 LEU A O     1 
ATOM   8184  C  CB    . LEU A  1  1105 ? 7.379   80.609  105.435 1.00 20.52 ? 1103 LEU A CB    1 
ATOM   8185  C  CG    . LEU A  1  1105 ? 8.300   81.646  106.091 1.00 19.84 ? 1103 LEU A CG    1 
ATOM   8186  C  CD1   . LEU A  1  1105 ? 9.423   82.054  105.138 1.00 22.33 ? 1103 LEU A CD1   1 
ATOM   8187  C  CD2   . LEU A  1  1105 ? 7.490   82.867  106.547 1.00 22.27 ? 1103 LEU A CD2   1 
ATOM   8188  N  N     . LEU A  1  1106 ? 10.010  78.515  106.279 1.00 17.24 ? 1104 LEU A N     1 
ATOM   8189  C  CA    . LEU A  1  1106 ? 10.761  78.006  107.422 1.00 16.92 ? 1104 LEU A CA    1 
ATOM   8190  C  C     . LEU A  1  1106 ? 11.487  79.161  108.084 1.00 22.65 ? 1104 LEU A C     1 
ATOM   8191  O  O     . LEU A  1  1106 ? 12.259  79.867  107.430 1.00 21.37 ? 1104 LEU A O     1 
ATOM   8192  C  CB    . LEU A  1  1106 ? 11.784  76.947  107.022 1.00 19.69 ? 1104 LEU A CB    1 
ATOM   8193  C  CG    . LEU A  1  1106 ? 11.258  75.670  106.380 1.00 26.15 ? 1104 LEU A CG    1 
ATOM   8194  C  CD1   . LEU A  1  1106 ? 12.331  74.595  106.426 1.00 20.98 ? 1104 LEU A CD1   1 
ATOM   8195  C  CD2   . LEU A  1  1106 ? 9.992   75.194  107.032 1.00 25.01 ? 1104 LEU A CD2   1 
ATOM   8196  N  N     . VAL A  1  1107 ? 11.269  79.326  109.380 1.00 19.23 ? 1105 VAL A N     1 
ATOM   8197  C  CA    . VAL A  1  1107 ? 11.977  80.363  110.122 1.00 20.15 ? 1105 VAL A CA    1 
ATOM   8198  C  C     . VAL A  1  1107 ? 12.732  79.662  111.239 1.00 18.55 ? 1105 VAL A C     1 
ATOM   8199  O  O     . VAL A  1  1107 ? 12.245  79.580  112.372 1.00 20.94 ? 1105 VAL A O     1 
ATOM   8200  C  CB    . VAL A  1  1107 ? 11.019  81.440  110.649 1.00 19.56 ? 1105 VAL A CB    1 
ATOM   8201  C  CG1   . VAL A  1  1107 ? 11.809  82.602  111.252 1.00 21.77 ? 1105 VAL A CG1   1 
ATOM   8202  C  CG2   . VAL A  1  1107 ? 10.086  81.932  109.523 1.00 22.41 ? 1105 VAL A CG2   1 
ATOM   8203  N  N     . PRO A  1  1108 ? 13.906  79.122  110.959 1.00 19.17 ? 1106 PRO A N     1 
ATOM   8204  C  CA    . PRO A  1  1108 ? 14.648  78.383  111.977 1.00 21.28 ? 1106 PRO A CA    1 
ATOM   8205  C  C     . PRO A  1  1108 ? 15.510  79.308  112.822 1.00 21.62 ? 1106 PRO A C     1 
ATOM   8206  O  O     . PRO A  1  1108 ? 15.784  80.455  112.460 1.00 24.21 ? 1106 PRO A O     1 
ATOM   8207  C  CB    . PRO A  1  1108 ? 15.525  77.454  111.136 1.00 21.45 ? 1106 PRO A CB    1 
ATOM   8208  C  CG    . PRO A  1  1108 ? 15.838  78.296  109.921 1.00 20.85 ? 1106 PRO A CG    1 
ATOM   8209  C  CD    . PRO A  1  1108 ? 14.572  79.073  109.642 1.00 22.87 ? 1106 PRO A CD    1 
ATOM   8210  N  N     . ALA A  1  1109 ? 15.929  78.777  113.958 1.00 20.40 ? 1107 ALA A N     1 
ATOM   8211  C  CA    . ALA A  1  1109 ? 16.889  79.441  114.828 1.00 22.60 ? 1107 ALA A CA    1 
ATOM   8212  C  C     . ALA A  1  1109 ? 18.197  78.674  114.979 1.00 25.71 ? 1107 ALA A C     1 
ATOM   8213  O  O     . ALA A  1  1109 ? 19.257  79.297  115.098 1.00 26.08 ? 1107 ALA A O     1 
ATOM   8214  C  CB    . ALA A  1  1109 ? 16.258  79.680  116.215 1.00 22.09 ? 1107 ALA A CB    1 
ATOM   8215  N  N     . THR A  1  1110 ? 18.157  77.347  114.959 1.00 22.84 ? 1108 THR A N     1 
ATOM   8216  C  CA    . THR A  1  1110 ? 19.337  76.509  115.083 1.00 22.65 ? 1108 THR A CA    1 
ATOM   8217  C  C     . THR A  1  1110 ? 19.428  75.572  113.889 1.00 23.42 ? 1108 THR A C     1 
ATOM   8218  O  O     . THR A  1  1110 ? 18.439  75.306  113.202 1.00 21.83 ? 1108 THR A O     1 
ATOM   8219  C  CB    . THR A  1  1110 ? 19.311  75.676  116.366 1.00 22.94 ? 1108 THR A CB    1 
ATOM   8220  O  OG1   . THR A  1  1110 ? 18.199  74.773  116.325 1.00 22.14 ? 1108 THR A OG1   1 
ATOM   8221  C  CG2   . THR A  1  1110 ? 19.164  76.581  117.577 1.00 25.60 ? 1108 THR A CG2   1 
ATOM   8222  N  N     . GLU A  1  1111 ? 20.633  75.054  113.676 1.00 24.67 ? 1109 GLU A N     1 
ATOM   8223  C  CA    . GLU A  1  1111 ? 20.839  74.071  112.616 1.00 23.38 ? 1109 GLU A CA    1 
ATOM   8224  C  C     . GLU A  1  1111 ? 19.947  72.848  112.809 1.00 24.26 ? 1109 GLU A C     1 
ATOM   8225  O  O     . GLU A  1  1111 ? 19.292  72.393  111.863 1.00 21.92 ? 1109 GLU A O     1 
ATOM   8226  C  CB    . GLU A  1  1111 ? 22.308  73.665  112.578 1.00 27.36 ? 1109 GLU A CB    1 
ATOM   8227  C  CG    . GLU A  1  1111 ? 22.563  72.493  111.666 1.00 27.74 ? 1109 GLU A CG    1 
ATOM   8228  C  CD    . GLU A  1  1111 ? 24.035  72.252  111.472 1.00 28.06 ? 1109 GLU A CD    1 
ATOM   8229  O  OE1   . GLU A  1  1111 ? 24.671  73.060  110.769 1.00 32.89 ? 1109 GLU A OE1   1 
ATOM   8230  O  OE2   . GLU A  1  1111 ? 24.550  71.273  112.031 1.00 32.14 ? 1109 GLU A OE2   1 
ATOM   8231  N  N     . SER A  1  1112 ? 19.915  72.295  114.027 1.00 23.24 ? 1110 SER A N     1 
ATOM   8232  C  CA    . SER A  1  1112 ? 19.060  71.135  114.275 1.00 20.59 ? 1110 SER A CA    1 
ATOM   8233  C  C     . SER A  1  1112 ? 17.596  71.487  114.069 1.00 23.90 ? 1110 SER A C     1 
ATOM   8234  O  O     . SER A  1  1112 ? 16.832  70.695  113.507 1.00 22.15 ? 1110 SER A O     1 
ATOM   8235  C  CB    . SER A  1  1112 ? 19.280  70.588  115.685 1.00 24.83 ? 1110 SER A CB    1 
ATOM   8236  O  OG    . SER A  1  1112 ? 18.514  69.404  115.865 1.00 24.91 ? 1110 SER A OG    1 
ATOM   8237  N  N     . GLY A  1  1113 ? 17.183  72.673  114.517 1.00 20.41 ? 1111 GLY A N     1 
ATOM   8238  C  CA    . GLY A  1  1113 ? 15.818  73.096  114.266 1.00 18.03 ? 1111 GLY A CA    1 
ATOM   8239  C  C     . GLY A  1  1113 ? 15.501  73.158  112.786 1.00 18.26 ? 1111 GLY A C     1 
ATOM   8240  O  O     . GLY A  1  1113 ? 14.444  72.689  112.344 1.00 21.35 ? 1111 GLY A O     1 
ATOM   8241  N  N     . LEU A  1  1114 ? 16.421  73.719  111.997 1.00 18.95 ? 1112 LEU A N     1 
ATOM   8242  C  CA    . LEU A  1  1114 ? 16.234  73.760  110.551 1.00 20.36 ? 1112 LEU A CA    1 
ATOM   8243  C  C     . LEU A  1  1114 ? 16.072  72.361  109.980 1.00 19.18 ? 1112 LEU A C     1 
ATOM   8244  O  O     . LEU A  1  1114 ? 15.176  72.114  109.165 1.00 19.71 ? 1112 LEU A O     1 
ATOM   8245  C  CB    . LEU A  1  1114 ? 17.411  74.467  109.884 1.00 20.80 ? 1112 LEU A CB    1 
ATOM   8246  C  CG    . LEU A  1  1114 ? 17.389  74.434  108.356 1.00 23.35 ? 1112 LEU A CG    1 
ATOM   8247  C  CD1   . LEU A  1  1114 ? 16.056  74.946  107.809 1.00 20.28 ? 1112 LEU A CD1   1 
ATOM   8248  C  CD2   . LEU A  1  1114 ? 18.551  75.242  107.790 1.00 24.85 ? 1112 LEU A CD2   1 
ATOM   8249  N  N     . TYR A  1  1115 ? 16.940  71.432  110.383 1.00 20.62 ? 1113 TYR A N     1 
ATOM   8250  C  CA    . TYR A  1  1115 ? 16.840  70.078  109.850 1.00 19.40 ? 1113 TYR A CA    1 
ATOM   8251  C  C     . TYR A  1  1115 ? 15.503  69.442  110.211 1.00 19.88 ? 1113 TYR A C     1 
ATOM   8252  O  O     . TYR A  1  1115 ? 14.893  68.757  109.378 1.00 19.24 ? 1113 TYR A O     1 
ATOM   8253  C  CB    . TYR A  1  1115 ? 17.988  69.216  110.358 1.00 19.23 ? 1113 TYR A CB    1 
ATOM   8254  C  CG    . TYR A  1  1115 ? 19.371  69.633  109.877 1.00 17.40 ? 1113 TYR A CG    1 
ATOM   8255  C  CD1   . TYR A  1  1115 ? 19.545  70.467  108.767 1.00 20.33 ? 1113 TYR A CD1   1 
ATOM   8256  C  CD2   . TYR A  1  1115 ? 20.500  69.164  110.528 1.00 21.82 ? 1113 TYR A CD2   1 
ATOM   8257  C  CE1   . TYR A  1  1115 ? 20.841  70.831  108.335 1.00 22.00 ? 1113 TYR A CE1   1 
ATOM   8258  C  CE2   . TYR A  1  1115 ? 21.775  69.506  110.105 1.00 21.39 ? 1113 TYR A CE2   1 
ATOM   8259  C  CZ    . TYR A  1  1115 ? 21.938  70.337  109.017 1.00 25.53 ? 1113 TYR A CZ    1 
ATOM   8260  O  OH    . TYR A  1  1115 ? 23.226  70.672  108.631 1.00 27.83 ? 1113 TYR A OH    1 
ATOM   8261  N  N     . HIS A  1  1116 ? 15.037  69.642  111.451 1.00 19.70 ? 1114 HIS A N     1 
ATOM   8262  C  CA    . HIS A  1  1116 ? 13.729  69.119  111.833 1.00 19.01 ? 1114 HIS A CA    1 
ATOM   8263  C  C     . HIS A  1  1116 ? 12.618  69.788  111.030 1.00 19.81 ? 1114 HIS A C     1 
ATOM   8264  O  O     . HIS A  1  1116 ? 11.664  69.126  110.602 1.00 19.12 ? 1114 HIS A O     1 
ATOM   8265  C  CB    . HIS A  1  1116 ? 13.494  69.312  113.335 1.00 21.73 ? 1114 HIS A CB    1 
ATOM   8266  C  CG    . HIS A  1  1116 ? 14.120  68.253  114.190 1.00 22.92 ? 1114 HIS A CG    1 
ATOM   8267  N  ND1   . HIS A  1  1116 ? 15.422  68.325  114.638 1.00 27.52 ? 1114 HIS A ND1   1 
ATOM   8268  C  CD2   . HIS A  1  1116 ? 13.617  67.095  114.680 1.00 23.05 ? 1114 HIS A CD2   1 
ATOM   8269  C  CE1   . HIS A  1  1116 ? 15.693  67.257  115.370 1.00 23.07 ? 1114 HIS A CE1   1 
ATOM   8270  N  NE2   . HIS A  1  1116 ? 14.614  66.498  115.412 1.00 25.44 ? 1114 HIS A NE2   1 
ATOM   8271  N  N     . GLN A  1  1117 ? 12.708  71.107  110.832 1.00 18.03 ? 1115 GLN A N     1 
ATOM   8272  C  CA    . GLN A  1  1117 ? 11.698  71.799  110.040 1.00 16.62 ? 1115 GLN A CA    1 
ATOM   8273  C  C     . GLN A  1  1117 ? 11.680  71.276  108.617 1.00 18.12 ? 1115 GLN A C     1 
ATOM   8274  O  O     . GLN A  1  1117 ? 10.615  71.022  108.050 1.00 18.46 ? 1115 GLN A O     1 
ATOM   8275  C  CB    . GLN A  1  1117 ? 11.959  73.307  110.040 1.00 18.53 ? 1115 GLN A CB    1 
ATOM   8276  C  CG    . GLN A  1  1117 ? 11.675  73.997  111.362 1.00 18.39 ? 1115 GLN A CG    1 
ATOM   8277  C  CD    . GLN A  1  1117 ? 11.939  75.474  111.270 1.00 21.86 ? 1115 GLN A CD    1 
ATOM   8278  O  OE1   . GLN A  1  1117 ? 12.550  75.936  110.305 1.00 21.00 ? 1115 GLN A OE1   1 
ATOM   8279  N  NE2   . GLN A  1  1117 ? 11.486  76.229  112.268 1.00 19.57 ? 1115 GLN A NE2   1 
ATOM   8280  N  N     . LEU A  1  1118 ? 12.864  71.122  108.028 1.00 17.90 ? 1116 LEU A N     1 
ATOM   8281  C  CA    A LEU A  1  1118 ? 12.936  70.653  106.654 0.55 18.24 ? 1116 LEU A CA    1 
ATOM   8282  C  CA    B LEU A  1  1118 ? 12.960  70.638  106.657 0.45 18.26 ? 1116 LEU A CA    1 
ATOM   8283  C  C     . LEU A  1  1118 ? 12.413  69.229  106.542 1.00 18.19 ? 1116 LEU A C     1 
ATOM   8284  O  O     . LEU A  1  1118 ? 11.692  68.903  105.591 1.00 19.22 ? 1116 LEU A O     1 
ATOM   8285  C  CB    A LEU A  1  1118 ? 14.374  70.764  106.150 0.55 20.10 ? 1116 LEU A CB    1 
ATOM   8286  C  CB    B LEU A  1  1118 ? 14.412  70.671  106.193 0.45 20.13 ? 1116 LEU A CB    1 
ATOM   8287  C  CG    A LEU A  1  1118 ? 14.650  70.570  104.660 0.55 18.72 ? 1116 LEU A CG    1 
ATOM   8288  C  CG    B LEU A  1  1118 ? 14.972  72.016  105.762 0.45 18.44 ? 1116 LEU A CG    1 
ATOM   8289  C  CD1   A LEU A  1  1118 ? 13.653  71.341  103.798 0.55 18.35 ? 1116 LEU A CD1   1 
ATOM   8290  C  CD1   B LEU A  1  1118 ? 16.478  71.922  105.710 0.45 19.77 ? 1116 LEU A CD1   1 
ATOM   8291  C  CD2   A LEU A  1  1118 ? 16.062  71.038  104.383 0.55 23.67 ? 1116 LEU A CD2   1 
ATOM   8292  C  CD2   B LEU A  1  1118 ? 14.426  72.403  104.408 0.45 18.64 ? 1116 LEU A CD2   1 
ATOM   8293  N  N     . ALA A  1  1119 ? 12.750  68.375  107.505 1.00 19.69 ? 1117 ALA A N     1 
ATOM   8294  C  CA    . ALA A  1  1119 ? 12.227  67.014  107.486 1.00 20.71 ? 1117 ALA A CA    1 
ATOM   8295  C  C     . ALA A  1  1119 ? 10.703  67.024  107.522 1.00 19.63 ? 1117 ALA A C     1 
ATOM   8296  O  O     . ALA A  1  1119 ? 10.050  66.321  106.746 1.00 20.20 ? 1117 ALA A O     1 
ATOM   8297  C  CB    . ALA A  1  1119 ? 12.793  66.220  108.662 1.00 22.11 ? 1117 ALA A CB    1 
ATOM   8298  N  N     . ALA A  1  1120 ? 10.115  67.837  108.406 1.00 17.93 ? 1118 ALA A N     1 
ATOM   8299  C  CA    . ALA A  1  1120 ? 8.655   67.876  108.499 1.00 17.46 ? 1118 ALA A CA    1 
ATOM   8300  C  C     . ALA A  1  1120 ? 8.038   68.342  107.189 1.00 19.08 ? 1118 ALA A C     1 
ATOM   8301  O  O     . ALA A  1  1120 ? 7.057   67.757  106.710 1.00 18.19 ? 1118 ALA A O     1 
ATOM   8302  C  CB    . ALA A  1  1120 ? 8.213   68.793  109.644 1.00 18.13 ? 1118 ALA A CB    1 
ATOM   8303  N  N     . ALA A  1  1121 ? 8.618   69.382  106.586 1.00 16.66 ? 1119 ALA A N     1 
ATOM   8304  C  CA    . ALA A  1  1121 ? 8.057   69.938  105.361 1.00 16.92 ? 1119 ALA A CA    1 
ATOM   8305  C  C     . ALA A  1  1121 ? 8.245   68.995  104.185 1.00 15.97 ? 1119 ALA A C     1 
ATOM   8306  O  O     . ALA A  1  1121 ? 7.330   68.826  103.371 1.00 15.40 ? 1119 ALA A O     1 
ATOM   8307  C  CB    . ALA A  1  1121 ? 8.706   71.290  105.063 1.00 18.71 ? 1119 ALA A CB    1 
ATOM   8308  N  N     . LEU A  1  1122 ? 9.429   68.404  104.057 1.00 17.02 ? 1120 LEU A N     1 
ATOM   8309  C  CA    . LEU A  1  1122 ? 9.670   67.509  102.925 1.00 16.21 ? 1120 LEU A CA    1 
ATOM   8310  C  C     . LEU A  1  1122 ? 8.864   66.226  103.055 1.00 16.77 ? 1120 LEU A C     1 
ATOM   8311  O  O     . LEU A  1  1122 ? 8.384   65.693  102.051 1.00 18.20 ? 1120 LEU A O     1 
ATOM   8312  C  CB    . LEU A  1  1122 ? 11.152  67.179  102.807 1.00 18.99 ? 1120 LEU A CB    1 
ATOM   8313  C  CG    . LEU A  1  1122 ? 12.108  68.333  102.514 1.00 19.01 ? 1120 LEU A CG    1 
ATOM   8314  C  CD1   . LEU A  1  1122 ? 13.516  67.807  102.561 1.00 22.17 ? 1120 LEU A CD1   1 
ATOM   8315  C  CD2   . LEU A  1  1122 ? 11.780  68.927  101.147 1.00 19.14 ? 1120 LEU A CD2   1 
ATOM   8316  N  N     . ALA A  1  1123 ? 8.711   65.710  104.276 1.00 17.30 ? 1121 ALA A N     1 
ATOM   8317  C  CA    . ALA A  1  1123 ? 7.947   64.482  104.469 1.00 17.85 ? 1121 ALA A CA    1 
ATOM   8318  C  C     . ALA A  1  1123 ? 6.503   64.635  104.030 1.00 19.13 ? 1121 ALA A C     1 
ATOM   8319  O  O     . ALA A  1  1123 ? 5.856   63.634  103.707 1.00 17.84 ? 1121 ALA A O     1 
ATOM   8320  C  CB    . ALA A  1  1123 ? 7.973   64.070  105.941 1.00 16.39 ? 1121 ALA A CB    1 
ATOM   8321  N  N     . THR A  1  1124 ? 5.988   65.863  104.026 1.00 15.36 ? 1122 THR A N     1 
ATOM   8322  C  CA    . THR A  1  1124 ? 4.622   66.148  103.633 1.00 15.70 ? 1122 THR A CA    1 
ATOM   8323  C  C     . THR A  1  1124 ? 4.556   66.716  102.221 1.00 17.48 ? 1122 THR A C     1 
ATOM   8324  O  O     . THR A  1  1124 ? 3.517   67.241  101.817 1.00 16.85 ? 1122 THR A O     1 
ATOM   8325  C  CB    . THR A  1  1124 ? 3.974   67.073  104.667 1.00 16.99 ? 1122 THR A CB    1 
ATOM   8326  O  OG1   . THR A  1  1124 ? 4.901   68.098  105.022 1.00 16.13 ? 1122 THR A OG1   1 
ATOM   8327  C  CG2   . THR A  1  1124 ? 3.646   66.288  105.955 1.00 18.66 ? 1122 THR A CG2   1 
ATOM   8328  N  N     . GLY A  1  1125 ? 5.639   66.571  101.450 1.00 15.43 ? 1123 GLY A N     1 
ATOM   8329  C  CA    . GLY A  1  1125 ? 5.643   66.829  100.022 1.00 17.53 ? 1123 GLY A CA    1 
ATOM   8330  C  C     . GLY A  1  1125 ? 5.885   68.259  99.632  1.00 18.11 ? 1123 GLY A C     1 
ATOM   8331  O  O     . GLY A  1  1125 ? 5.814   68.581  98.437  1.00 19.57 ? 1123 GLY A O     1 
ATOM   8332  N  N     . ASN A  1  1126 ? 6.189   69.120  100.590 1.00 17.61 ? 1124 ASN A N     1 
ATOM   8333  C  CA    . ASN A  1  1126 ? 6.273   70.548  100.354 1.00 15.35 ? 1124 ASN A CA    1 
ATOM   8334  C  C     . ASN A  1  1126 ? 7.660   70.957  99.890  1.00 17.05 ? 1124 ASN A C     1 
ATOM   8335  O  O     . ASN A  1  1126 ? 8.664   70.274  100.128 1.00 17.86 ? 1124 ASN A O     1 
ATOM   8336  C  CB    . ASN A  1  1126 ? 5.944   71.323  101.631 1.00 15.20 ? 1124 ASN A CB    1 
ATOM   8337  C  CG    . ASN A  1  1126 ? 4.567   71.026  102.131 1.00 15.86 ? 1124 ASN A CG    1 
ATOM   8338  O  OD1   . ASN A  1  1126 ? 3.588   71.435  101.529 1.00 19.19 ? 1124 ASN A OD1   1 
ATOM   8339  N  ND2   . ASN A  1  1126 ? 4.477   70.293  103.234 1.00 16.60 ? 1124 ASN A ND2   1 
ATOM   8340  N  N     . SER A  1  1127 ? 7.697   72.110  99.235  1.00 19.09 ? 1125 SER A N     1 
ATOM   8341  C  CA    . SER A  1  1127 ? 8.933   72.857  99.099  1.00 17.35 ? 1125 SER A CA    1 
ATOM   8342  C  C     . SER A  1  1127 ? 9.023   73.844  100.252 1.00 19.62 ? 1125 SER A C     1 
ATOM   8343  O  O     . SER A  1  1127 ? 8.083   74.003  101.033 1.00 19.43 ? 1125 SER A O     1 
ATOM   8344  C  CB    . SER A  1  1127 ? 8.980   73.590  97.765  1.00 21.09 ? 1125 SER A CB    1 
ATOM   8345  O  OG    . SER A  1  1127 ? 7.915   74.504  97.656  1.00 26.05 ? 1125 SER A OG    1 
ATOM   8346  N  N     . VAL A  1  1128 ? 10.168  74.510  100.369 1.00 20.60 ? 1126 VAL A N     1 
ATOM   8347  C  CA    . VAL A  1  1128 ? 10.363  75.447  101.468 1.00 18.30 ? 1126 VAL A CA    1 
ATOM   8348  C  C     . VAL A  1  1128 ? 11.027  76.715  100.973 1.00 21.48 ? 1126 VAL A C     1 
ATOM   8349  O  O     . VAL A  1  1128 ? 11.767  76.721  99.983  1.00 20.24 ? 1126 VAL A O     1 
ATOM   8350  C  CB    . VAL A  1  1128 ? 11.208  74.851  102.612 1.00 20.15 ? 1126 VAL A CB    1 
ATOM   8351  C  CG1   . VAL A  1  1128 ? 10.580  73.573  103.120 1.00 19.10 ? 1126 VAL A CG1   1 
ATOM   8352  C  CG2   . VAL A  1  1128 ? 12.642  74.606  102.142 1.00 22.64 ? 1126 VAL A CG2   1 
ATOM   8353  N  N     . ALA A  1  1129 ? 10.761  77.789  101.696 1.00 19.73 ? 1127 ALA A N     1 
ATOM   8354  C  CA    . ALA A  1  1129 ? 11.539  79.016  101.640 1.00 21.21 ? 1127 ALA A CA    1 
ATOM   8355  C  C     . ALA A  1  1129 ? 12.094  79.225  103.039 1.00 19.27 ? 1127 ALA A C     1 
ATOM   8356  O  O     . ALA A  1  1129 ? 11.324  79.337  103.997 1.00 21.98 ? 1127 ALA A O     1 
ATOM   8357  C  CB    . ALA A  1  1129 ? 10.674  80.195  101.204 1.00 23.80 ? 1127 ALA A CB    1 
ATOM   8358  N  N     . ILE A  1  1130 ? 13.420  79.232  103.167 1.00 20.10 ? 1128 ILE A N     1 
ATOM   8359  C  CA    . ILE A  1  1130 ? 14.067  79.327  104.468 1.00 21.26 ? 1128 ILE A CA    1 
ATOM   8360  C  C     . ILE A  1  1130 ? 14.469  80.771  104.701 1.00 24.84 ? 1128 ILE A C     1 
ATOM   8361  O  O     . ILE A  1  1130 ? 15.086  81.398  103.833 1.00 23.70 ? 1128 ILE A O     1 
ATOM   8362  C  CB    . ILE A  1  1130 ? 15.293  78.406  104.568 1.00 20.61 ? 1128 ILE A CB    1 
ATOM   8363  C  CG1   . ILE A  1  1130 ? 14.927  76.991  104.144 1.00 22.30 ? 1128 ILE A CG1   1 
ATOM   8364  C  CG2   . ILE A  1  1130 ? 15.828  78.398  106.003 1.00 20.47 ? 1128 ILE A CG2   1 
ATOM   8365  C  CD1   . ILE A  1  1130 ? 16.140  76.117  103.960 1.00 20.81 ? 1128 ILE A CD1   1 
ATOM   8366  N  N     . ASP A  1  1131 ? 14.151  81.287  105.887 1.00 20.75 ? 1129 ASP A N     1 
ATOM   8367  C  CA    . ASP A  1  1131 ? 14.536  82.644  106.237 1.00 24.00 ? 1129 ASP A CA    1 
ATOM   8368  C  C     . ASP A  1  1131 ? 16.045  82.828  106.129 1.00 23.26 ? 1129 ASP A C     1 
ATOM   8369  O  O     . ASP A  1  1131 ? 16.813  82.204  106.866 1.00 23.38 ? 1129 ASP A O     1 
ATOM   8370  C  CB    . ASP A  1  1131 ? 14.051  82.971  107.645 1.00 22.60 ? 1129 ASP A CB    1 
ATOM   8371  C  CG    . ASP A  1  1131 ? 14.461  84.341  108.083 1.00 30.47 ? 1129 ASP A CG    1 
ATOM   8372  O  OD1   . ASP A  1  1131 ? 14.565  85.238  107.221 1.00 24.79 ? 1129 ASP A OD1   1 
ATOM   8373  O  OD2   . ASP A  1  1131 ? 14.682  84.516  109.290 1.00 26.36 ? 1129 ASP A OD2   1 
ATOM   8374  N  N     . ALA A  1  1132 ? 16.482  83.665  105.188 1.00 26.09 ? 1130 ALA A N     1 
ATOM   8375  C  CA    . ALA A  1  1132 ? 17.909  83.917  105.047 1.00 29.30 ? 1130 ALA A CA    1 
ATOM   8376  C  C     . ALA A  1  1132 ? 18.476  84.674  106.241 1.00 30.27 ? 1130 ALA A C     1 
ATOM   8377  O  O     . ALA A  1  1132 ? 19.677  84.571  106.510 1.00 32.08 ? 1130 ALA A O     1 
ATOM   8378  C  CB    . ALA A  1  1132 ? 18.176  84.680  103.748 1.00 27.15 ? 1130 ALA A CB    1 
ATOM   8379  N  N     . ALA A  1  1133 ? 17.642  85.411  106.980 1.00 27.59 ? 1131 ALA A N     1 
ATOM   8380  C  CA    . ALA A  1  1133 ? 18.134  86.109  108.164 1.00 30.67 ? 1131 ALA A CA    1 
ATOM   8381  C  C     . ALA A  1  1133 ? 18.503  85.164  109.299 1.00 32.02 ? 1131 ALA A C     1 
ATOM   8382  O  O     . ALA A  1  1133 ? 19.057  85.611  110.304 1.00 32.63 ? 1131 ALA A O     1 
ATOM   8383  C  CB    . ALA A  1  1133 ? 17.096  87.123  108.648 1.00 32.16 ? 1131 ALA A CB    1 
ATOM   8384  N  N     . SER A  1  1134 ? 18.207  83.874  109.172 1.00 28.14 ? 1132 SER A N     1 
ATOM   8385  C  CA    . SER A  1  1134 ? 18.620  82.913  110.181 1.00 27.76 ? 1132 SER A CA    1 
ATOM   8386  C  C     . SER A  1  1134 ? 20.124  82.711  110.206 1.00 28.94 ? 1132 SER A C     1 
ATOM   8387  O  O     . SER A  1  1134 ? 20.647  82.200  111.201 1.00 26.72 ? 1132 SER A O     1 
ATOM   8388  C  CB    . SER A  1  1134 ? 17.948  81.567  109.922 1.00 26.48 ? 1132 SER A CB    1 
ATOM   8389  O  OG    . SER A  1  1134 ? 18.458  80.975  108.734 1.00 26.71 ? 1132 SER A OG    1 
ATOM   8390  N  N     . GLY A  1  1135 ? 20.821  83.063  109.125 1.00 28.04 ? 1133 GLY A N     1 
ATOM   8391  C  CA    . GLY A  1  1135 ? 22.250  82.837  109.046 1.00 29.24 ? 1133 GLY A CA    1 
ATOM   8392  C  C     . GLY A  1  1135 ? 22.662  81.386  108.951 1.00 31.89 ? 1133 GLY A C     1 
ATOM   8393  O  O     . GLY A  1  1135 ? 23.835  81.069  109.154 1.00 31.43 ? 1133 GLY A O     1 
ATOM   8394  N  N     . LEU A  1  1136 ? 21.730  80.486  108.637 1.00 26.25 ? 1134 LEU A N     1 
ATOM   8395  C  CA    . LEU A  1  1136 ? 22.006  79.055  108.640 1.00 26.57 ? 1134 LEU A CA    1 
ATOM   8396  C  C     . LEU A  1  1136 ? 22.336  78.508  107.253 1.00 31.37 ? 1134 LEU A C     1 
ATOM   8397  O  O     . LEU A  1  1136 ? 22.265  77.291  107.049 1.00 29.09 ? 1134 LEU A O     1 
ATOM   8398  C  CB    . LEU A  1  1136 ? 20.822  78.294  109.241 1.00 24.21 ? 1134 LEU A CB    1 
ATOM   8399  C  CG    . LEU A  1  1136 ? 20.583  78.524  110.742 1.00 28.35 ? 1134 LEU A CG    1 
ATOM   8400  C  CD1   . LEU A  1  1136 ? 19.251  77.923  111.159 1.00 23.98 ? 1134 LEU A CD1   1 
ATOM   8401  C  CD2   . LEU A  1  1136 ? 21.700  77.950  111.582 1.00 29.71 ? 1134 LEU A CD2   1 
ATOM   8402  N  N     . GLN A  1  1137 ? 22.718  79.373  106.306 1.00 30.84 ? 1135 GLN A N     1 
ATOM   8403  C  CA    . GLN A  1  1137 ? 22.997  78.908  104.946 1.00 30.96 ? 1135 GLN A CA    1 
ATOM   8404  C  C     . GLN A  1  1137 ? 24.066  77.818  104.927 1.00 30.15 ? 1135 GLN A C     1 
ATOM   8405  O  O     . GLN A  1  1137 ? 23.956  76.842  104.173 1.00 28.50 ? 1135 GLN A O     1 
ATOM   8406  C  CB    . GLN A  1  1137 ? 23.423  80.077  104.055 1.00 32.71 ? 1135 GLN A CB    1 
ATOM   8407  C  CG    . GLN A  1  1137 ? 22.288  80.993  103.605 1.00 34.04 ? 1135 GLN A CG    1 
ATOM   8408  C  CD    . GLN A  1  1137 ? 21.971  82.067  104.625 1.00 29.92 ? 1135 GLN A CD    1 
ATOM   8409  O  OE1   . GLN A  1  1137 ? 22.435  82.016  105.768 1.00 32.39 ? 1135 GLN A OE1   1 
ATOM   8410  N  NE2   . GLN A  1  1137 ? 21.192  83.057  104.213 1.00 35.92 ? 1135 GLN A NE2   1 
ATOM   8411  N  N     . ALA A  1  1138 ? 25.106  77.956  105.753 1.00 31.83 ? 1136 ALA A N     1 
ATOM   8412  C  CA    . ALA A  1  1138 ? 26.186  76.977  105.748 1.00 31.20 ? 1136 ALA A CA    1 
ATOM   8413  C  C     . ALA A  1  1138 ? 25.769  75.613  106.284 1.00 34.45 ? 1136 ALA A C     1 
ATOM   8414  O  O     . ALA A  1  1138 ? 26.549  74.660  106.173 1.00 37.63 ? 1136 ALA A O     1 
ATOM   8415  C  CB    . ALA A  1  1138 ? 27.375  77.500  106.558 1.00 30.01 ? 1136 ALA A CB    1 
ATOM   8416  N  N     . SER A  1  1139 ? 24.574  75.493  106.860 1.00 31.89 ? 1137 SER A N     1 
ATOM   8417  C  CA    . SER A  1  1139 ? 24.092  74.215  107.360 1.00 30.30 ? 1137 SER A CA    1 
ATOM   8418  C  C     . SER A  1  1139 ? 23.499  73.336  106.267 1.00 27.31 ? 1137 SER A C     1 
ATOM   8419  O  O     . SER A  1  1139 ? 23.244  72.158  106.525 1.00 29.35 ? 1137 SER A O     1 
ATOM   8420  C  CB    . SER A  1  1139 ? 23.034  74.434  108.451 1.00 30.75 ? 1137 SER A CB    1 
ATOM   8421  O  OG    . SER A  1  1139 ? 23.599  75.002  109.619 1.00 31.30 ? 1137 SER A OG    1 
ATOM   8422  N  N     . LEU A  1  1140 ? 23.267  73.872  105.074 1.00 27.65 ? 1138 LEU A N     1 
ATOM   8423  C  CA    . LEU A  1  1140 ? 22.656  73.129  103.977 1.00 30.08 ? 1138 LEU A CA    1 
ATOM   8424  C  C     . LEU A  1  1140 ? 23.566  73.081  102.762 1.00 31.58 ? 1138 LEU A C     1 
ATOM   8425  O  O     . LEU A  1  1140 ? 23.115  73.231  101.628 1.00 37.96 ? 1138 LEU A O     1 
ATOM   8426  C  CB    . LEU A  1  1140 ? 21.312  73.733  103.582 1.00 33.27 ? 1138 LEU A CB    1 
ATOM   8427  C  CG    . LEU A  1  1140 ? 20.111  73.484  104.478 1.00 33.38 ? 1138 LEU A CG    1 
ATOM   8428  C  CD1   . LEU A  1  1140 ? 18.868  73.898  103.725 1.00 33.19 ? 1138 LEU A CD1   1 
ATOM   8429  C  CD2   . LEU A  1  1140 ? 20.040  72.024  104.901 1.00 28.19 ? 1138 LEU A CD2   1 
ATOM   8430  N  N     . LYS A  1  1141 ? 24.860  72.888  102.986 1.00 29.02 ? 1139 LYS A N     1 
ATOM   8431  C  CA    . LYS A  1  1141 ? 25.814  72.819  101.888 1.00 40.03 ? 1139 LYS A CA    1 
ATOM   8432  C  C     . LYS A  1  1141 ? 25.736  71.467  101.187 1.00 36.14 ? 1139 LYS A C     1 
ATOM   8433  O  O     . LYS A  1  1141 ? 25.586  70.423  101.828 1.00 33.92 ? 1139 LYS A O     1 
ATOM   8434  C  CB    . LYS A  1  1141 ? 27.235  73.058  102.397 1.00 38.67 ? 1139 LYS A CB    1 
ATOM   8435  N  N     . ASN A  1  1142 ? 25.840  71.497  99.861  1.00 32.95 ? 1140 ASN A N     1 
ATOM   8436  C  CA    . ASN A  1  1142 ? 25.971  70.282  99.056  1.00 29.61 ? 1140 ASN A CA    1 
ATOM   8437  C  C     . ASN A  1  1142 ? 24.725  69.404  99.146  1.00 30.65 ? 1140 ASN A C     1 
ATOM   8438  O  O     . ASN A  1  1142 ? 24.821  68.182  99.273  1.00 31.23 ? 1140 ASN A O     1 
ATOM   8439  C  CB    . ASN A  1  1142 ? 27.208  69.474  99.458  1.00 40.46 ? 1140 ASN A CB    1 
ATOM   8440  C  CG    . ASN A  1  1142 ? 28.450  70.333  99.609  1.00 54.30 ? 1140 ASN A CG    1 
ATOM   8441  O  OD1   . ASN A  1  1142 ? 28.959  70.514  100.717 1.00 51.59 ? 1140 ASN A OD1   1 
ATOM   8442  N  ND2   . ASN A  1  1142 ? 28.951  70.856  98.495  1.00 47.27 ? 1140 ASN A ND2   1 
ATOM   8443  N  N     . LEU A  1  1143 ? 23.546  70.021  99.080  1.00 30.91 ? 1141 LEU A N     1 
ATOM   8444  C  CA    . LEU A  1  1143 ? 22.324  69.234  99.075  1.00 29.49 ? 1141 LEU A CA    1 
ATOM   8445  C  C     . LEU A  1  1143 ? 22.218  68.408  97.794  1.00 33.37 ? 1141 LEU A C     1 
ATOM   8446  O  O     . LEU A  1  1143 ? 22.670  68.831  96.723  1.00 31.65 ? 1141 LEU A O     1 
ATOM   8447  C  CB    . LEU A  1  1143 ? 21.094  70.128  99.195  1.00 26.87 ? 1141 LEU A CB    1 
ATOM   8448  C  CG    . LEU A  1  1143 ? 20.714  70.636  100.580 1.00 32.38 ? 1141 LEU A CG    1 
ATOM   8449  C  CD1   . LEU A  1  1143 ? 19.609  71.655  100.416 1.00 30.00 ? 1141 LEU A CD1   1 
ATOM   8450  C  CD2   . LEU A  1  1143 ? 20.288  69.489  101.505 1.00 28.57 ? 1141 LEU A CD2   1 
ATOM   8451  N  N     . PRO A  1  1144 ? 21.622  67.224  97.875  1.00 29.44 ? 1142 PRO A N     1 
ATOM   8452  C  CA    . PRO A  1  1144 ? 21.242  66.519  96.651  1.00 30.21 ? 1142 PRO A CA    1 
ATOM   8453  C  C     . PRO A  1  1144 ? 20.372  67.428  95.794  1.00 27.90 ? 1142 PRO A C     1 
ATOM   8454  O  O     . PRO A  1  1144 ? 19.576  68.221  96.307  1.00 27.41 ? 1142 PRO A O     1 
ATOM   8455  C  CB    . PRO A  1  1144 ? 20.464  65.304  97.167  1.00 30.43 ? 1142 PRO A CB    1 
ATOM   8456  C  CG    . PRO A  1  1144 ? 20.900  65.143  98.596  1.00 31.17 ? 1142 PRO A CG    1 
ATOM   8457  C  CD    . PRO A  1  1144 ? 21.185  66.519  99.091  1.00 31.20 ? 1142 PRO A CD    1 
ATOM   8458  N  N     . GLN A  1  1145 ? 20.546  67.321  94.475  1.00 30.36 ? 1143 GLN A N     1 
ATOM   8459  C  CA    . GLN A  1  1145 ? 19.775  68.147  93.553  1.00 30.57 ? 1143 GLN A CA    1 
ATOM   8460  C  C     . GLN A  1  1145 ? 18.275  68.036  93.814  1.00 28.54 ? 1143 GLN A C     1 
ATOM   8461  O  O     . GLN A  1  1145 ? 17.549  69.030  93.713  1.00 27.74 ? 1143 GLN A O     1 
ATOM   8462  C  CB    . GLN A  1  1145 ? 20.102  67.755  92.108  1.00 34.20 ? 1143 GLN A CB    1 
ATOM   8463  N  N     . THR A  1  1146 ? 17.788  66.831  94.142  1.00 27.08 ? 1144 THR A N     1 
ATOM   8464  C  CA    . THR A  1  1146 ? 16.357  66.656  94.386  1.00 29.02 ? 1144 THR A CA    1 
ATOM   8465  C  C     . THR A  1  1146 ? 15.878  67.512  95.550  1.00 22.85 ? 1144 THR A C     1 
ATOM   8466  O  O     . THR A  1  1146 ? 14.755  68.035  95.531  1.00 24.55 ? 1144 THR A O     1 
ATOM   8467  C  CB    . THR A  1  1146 ? 16.044  65.194  94.685  1.00 31.59 ? 1144 THR A CB    1 
ATOM   8468  O  OG1   . THR A  1  1146 ? 16.893  64.757  95.749  1.00 27.27 ? 1144 THR A OG1   1 
ATOM   8469  C  CG2   . THR A  1  1146 ? 16.256  64.319  93.449  1.00 30.66 ? 1144 THR A CG2   1 
ATOM   8470  N  N     . VAL A  1  1147 ? 16.698  67.620  96.595  1.00 25.31 ? 1145 VAL A N     1 
ATOM   8471  C  CA    . VAL A  1  1147 ? 16.316  68.433  97.740  1.00 21.88 ? 1145 VAL A CA    1 
ATOM   8472  C  C     . VAL A  1  1147 ? 16.517  69.904  97.422  1.00 21.60 ? 1145 VAL A C     1 
ATOM   8473  O  O     . VAL A  1  1147 ? 15.653  70.735  97.719  1.00 23.80 ? 1145 VAL A O     1 
ATOM   8474  C  CB    . VAL A  1  1147 ? 17.106  68.009  98.994  1.00 21.90 ? 1145 VAL A CB    1 
ATOM   8475  C  CG1   . VAL A  1  1147 ? 16.644  68.814  100.197 1.00 22.65 ? 1145 VAL A CG1   1 
ATOM   8476  C  CG2   . VAL A  1  1147 ? 16.953  66.507  99.273  1.00 23.66 ? 1145 VAL A CG2   1 
ATOM   8477  N  N     . GLY A  1  1148 ? 17.639  70.241  96.779  1.00 24.17 ? 1146 GLY A N     1 
ATOM   8478  C  CA    . GLY A  1  1148 ? 17.870  71.620  96.384  1.00 23.27 ? 1146 GLY A CA    1 
ATOM   8479  C  C     . GLY A  1  1148 ? 16.743  72.186  95.543  1.00 25.29 ? 1146 GLY A C     1 
ATOM   8480  O  O     . GLY A  1  1148 ? 16.411  73.369  95.654  1.00 27.51 ? 1146 GLY A O     1 
ATOM   8481  N  N     . LEU A  1  1149 ? 16.130  71.347  94.695  1.00 24.23 ? 1147 LEU A N     1 
ATOM   8482  C  CA    . LEU A  1  1149 ? 14.993  71.799  93.895  1.00 25.94 ? 1147 LEU A CA    1 
ATOM   8483  C  C     . LEU A  1  1149 ? 13.841  72.267  94.770  1.00 24.77 ? 1147 LEU A C     1 
ATOM   8484  O  O     . LEU A  1  1149 ? 13.040  73.105  94.343  1.00 28.58 ? 1147 LEU A O     1 
ATOM   8485  C  CB    . LEU A  1  1149 ? 14.502  70.687  92.965  1.00 29.80 ? 1147 LEU A CB    1 
ATOM   8486  C  CG    . LEU A  1  1149 ? 15.388  70.279  91.784  1.00 41.00 ? 1147 LEU A CG    1 
ATOM   8487  C  CD1   . LEU A  1  1149 ? 14.671  69.251  90.920  1.00 38.95 ? 1147 LEU A CD1   1 
ATOM   8488  C  CD2   . LEU A  1  1149 ? 15.801  71.492  90.962  1.00 42.23 ? 1147 LEU A CD2   1 
ATOM   8489  N  N     . ARG A  1  1150 ? 13.745  71.745  95.991  1.00 24.40 ? 1148 ARG A N     1 
ATOM   8490  C  CA    . ARG A  1  1150 ? 12.660  72.087  96.891  1.00 21.47 ? 1148 ARG A CA    1 
ATOM   8491  C  C     . ARG A  1  1150 ? 13.013  73.205  97.847  1.00 20.79 ? 1148 ARG A C     1 
ATOM   8492  O  O     . ARG A  1  1150 ? 12.142  73.626  98.608  1.00 24.44 ? 1148 ARG A O     1 
ATOM   8493  C  CB    . ARG A  1  1150 ? 12.240  70.870  97.709  1.00 20.40 ? 1148 ARG A CB    1 
ATOM   8494  C  CG    . ARG A  1  1150 ? 11.532  69.806  96.900  1.00 22.34 ? 1148 ARG A CG    1 
ATOM   8495  C  CD    . ARG A  1  1150 ? 10.325  69.353  97.653  1.00 24.01 ? 1148 ARG A CD    1 
ATOM   8496  N  NE    . ARG A  1  1150 ? 9.762   68.142  97.085  1.00 24.28 ? 1148 ARG A NE    1 
ATOM   8497  C  CZ    . ARG A  1  1150 ? 9.170   67.208  97.810  1.00 23.33 ? 1148 ARG A CZ    1 
ATOM   8498  N  NH1   . ARG A  1  1150 ? 9.028   67.343  99.125  1.00 19.56 ? 1148 ARG A NH1   1 
ATOM   8499  N  NH2   . ARG A  1  1150 ? 8.723   66.112  97.208  1.00 20.55 ? 1148 ARG A NH2   1 
ATOM   8500  N  N     . VAL A  1  1151 ? 14.255  73.686  97.832  1.00 22.29 ? 1149 VAL A N     1 
ATOM   8501  C  CA    . VAL A  1  1151 ? 14.756  74.614  98.844  1.00 19.93 ? 1149 VAL A CA    1 
ATOM   8502  C  C     . VAL A  1  1151 ? 15.055  75.950  98.183  1.00 27.51 ? 1149 VAL A C     1 
ATOM   8503  O  O     . VAL A  1  1151 ? 15.774  76.010  97.182  1.00 27.71 ? 1149 VAL A O     1 
ATOM   8504  C  CB    . VAL A  1  1151 ? 16.007  74.059  99.548  1.00 21.66 ? 1149 VAL A CB    1 
ATOM   8505  C  CG1   . VAL A  1  1151 ? 16.645  75.112  100.446 1.00 23.92 ? 1149 VAL A CG1   1 
ATOM   8506  C  CG2   . VAL A  1  1151 ? 15.653  72.847  100.371 1.00 22.36 ? 1149 VAL A CG2   1 
ATOM   8507  N  N     . SER A  1  1152 ? 14.493  77.017  98.734  1.00 23.21 ? 1150 SER A N     1 
ATOM   8508  C  CA    . SER A  1  1152 ? 14.900  78.363  98.389  1.00 28.54 ? 1150 SER A CA    1 
ATOM   8509  C  C     . SER A  1  1152 ? 15.188  79.100  99.685  1.00 26.93 ? 1150 SER A C     1 
ATOM   8510  O  O     . SER A  1  1152 ? 14.726  78.708  100.761 1.00 25.80 ? 1150 SER A O     1 
ATOM   8511  C  CB    . SER A  1  1152 ? 13.836  79.104  97.564  1.00 26.60 ? 1150 SER A CB    1 
ATOM   8512  O  OG    . SER A  1  1152 ? 12.656  79.336  98.311  1.00 32.58 ? 1150 SER A OG    1 
ATOM   8513  N  N     . TRP A  1  1153 ? 16.003  80.139  99.582  1.00 24.33 ? 1151 TRP A N     1 
ATOM   8514  C  CA    . TRP A  1  1153 ? 16.289  81.015  100.705 1.00 28.94 ? 1151 TRP A CA    1 
ATOM   8515  C  C     . TRP A  1  1153 ? 15.628  82.360  100.453 1.00 29.49 ? 1151 TRP A C     1 
ATOM   8516  O  O     . TRP A  1  1153 ? 15.633  82.862  99.325  1.00 32.34 ? 1151 TRP A O     1 
ATOM   8517  C  CB    . TRP A  1  1153 ? 17.790  81.179  100.899 1.00 26.31 ? 1151 TRP A CB    1 
ATOM   8518  C  CG    . TRP A  1  1153 ? 18.449  79.944  101.419 1.00 30.14 ? 1151 TRP A CG    1 
ATOM   8519  C  CD1   . TRP A  1  1153 ? 18.911  78.889  100.684 1.00 28.67 ? 1151 TRP A CD1   1 
ATOM   8520  C  CD2   . TRP A  1  1153 ? 18.712  79.627  102.789 1.00 27.29 ? 1151 TRP A CD2   1 
ATOM   8521  N  NE1   . TRP A  1  1153 ? 19.451  77.938  101.515 1.00 29.47 ? 1151 TRP A NE1   1 
ATOM   8522  C  CE2   . TRP A  1  1153 ? 19.343  78.366  102.813 1.00 27.35 ? 1151 TRP A CE2   1 
ATOM   8523  C  CE3   . TRP A  1  1153 ? 18.477  80.284  103.997 1.00 25.93 ? 1151 TRP A CE3   1 
ATOM   8524  C  CZ2   . TRP A  1  1153 ? 19.742  77.749  104.000 1.00 25.51 ? 1151 TRP A CZ2   1 
ATOM   8525  C  CZ3   . TRP A  1  1153 ? 18.885  79.670  105.177 1.00 24.67 ? 1151 TRP A CZ3   1 
ATOM   8526  C  CH2   . TRP A  1  1153 ? 19.509  78.418  105.168 1.00 28.71 ? 1151 TRP A CH2   1 
ATOM   8527  N  N     . SER A  1  1154 ? 15.035  82.934  101.495 1.00 24.33 ? 1152 SER A N     1 
ATOM   8528  C  CA    . SER A  1  1154 ? 14.222  84.129  101.338 1.00 24.84 ? 1152 SER A CA    1 
ATOM   8529  C  C     . SER A  1  1154 ? 14.755  85.208  102.262 1.00 28.92 ? 1152 SER A C     1 
ATOM   8530  O  O     . SER A  1  1154 ? 14.837  85.003  103.478 1.00 27.55 ? 1152 SER A O     1 
ATOM   8531  C  CB    . SER A  1  1154 ? 12.752  83.843  101.639 1.00 26.57 ? 1152 SER A CB    1 
ATOM   8532  O  OG    . SER A  1  1154 ? 11.963  85.007  101.448 1.00 28.55 ? 1152 SER A OG    1 
ATOM   8533  N  N     . LYS A  1  1155 ? 15.148  86.339  101.681 1.00 28.33 ? 1153 LYS A N     1 
ATOM   8534  C  CA    . LYS A  1  1155 ? 15.450  87.517  102.485 1.00 30.61 ? 1153 LYS A CA    1 
ATOM   8535  C  C     . LYS A  1  1155 ? 14.234  88.419  102.631 1.00 33.11 ? 1153 LYS A C     1 
ATOM   8536  O  O     . LYS A  1  1155 ? 14.098  89.114  103.643 1.00 46.74 ? 1153 LYS A O     1 
ATOM   8537  C  CB    . LYS A  1  1155 ? 16.620  88.296  101.868 1.00 30.13 ? 1153 LYS A CB    1 
ATOM   8538  N  N     . ASP A  1  1156 ? 13.334  88.391  101.656 1.00 30.02 ? 1154 ASP A N     1 
ATOM   8539  C  CA    . ASP A  1  1156 ? 12.137  89.219  101.618 1.00 29.56 ? 1154 ASP A CA    1 
ATOM   8540  C  C     . ASP A  1  1156 ? 10.959  88.257  101.512 1.00 30.57 ? 1154 ASP A C     1 
ATOM   8541  O  O     . ASP A  1  1156 ? 10.568  87.868  100.410 1.00 28.12 ? 1154 ASP A O     1 
ATOM   8542  C  CB    . ASP A  1  1156 ? 12.203  90.197  100.430 1.00 32.91 ? 1154 ASP A CB    1 
ATOM   8543  C  CG    . ASP A  1  1156 ? 10.976  91.085  100.317 1.00 43.70 ? 1154 ASP A CG    1 
ATOM   8544  O  OD1   . ASP A  1  1156 ? 10.060  90.975  101.158 1.00 44.83 ? 1154 ASP A OD1   1 
ATOM   8545  O  OD2   . ASP A  1  1156 ? 10.931  91.905  99.375  1.00 50.02 ? 1154 ASP A OD2   1 
ATOM   8546  N  N     . TRP A  1  1157 ? 10.399  87.871  102.662 1.00 26.41 ? 1155 TRP A N     1 
ATOM   8547  C  CA    . TRP A  1  1157 ? 9.357   86.845  102.661 1.00 24.88 ? 1155 TRP A CA    1 
ATOM   8548  C  C     . TRP A  1  1157 ? 8.161   87.261  101.824 1.00 27.43 ? 1155 TRP A C     1 
ATOM   8549  O  O     . TRP A  1  1157 ? 7.528   86.424  101.174 1.00 27.76 ? 1155 TRP A O     1 
ATOM   8550  C  CB    . TRP A  1  1157 ? 8.890   86.553  104.082 1.00 26.10 ? 1155 TRP A CB    1 
ATOM   8551  C  CG    . TRP A  1  1157 ? 9.945   86.147  105.041 1.00 24.79 ? 1155 TRP A CG    1 
ATOM   8552  C  CD1   . TRP A  1  1157 ? 11.229  85.792  104.765 1.00 27.12 ? 1155 TRP A CD1   1 
ATOM   8553  C  CD2   . TRP A  1  1157 ? 9.803   86.068  106.458 1.00 22.69 ? 1155 TRP A CD2   1 
ATOM   8554  N  NE1   . TRP A  1  1157 ? 11.896  85.487  105.926 1.00 26.74 ? 1155 TRP A NE1   1 
ATOM   8555  C  CE2   . TRP A  1  1157 ? 11.037  85.653  106.981 1.00 23.96 ? 1155 TRP A CE2   1 
ATOM   8556  C  CE3   . TRP A  1  1157 ? 8.745   86.318  107.337 1.00 28.51 ? 1155 TRP A CE3   1 
ATOM   8557  C  CZ2   . TRP A  1  1157 ? 11.244  85.465  108.348 1.00 26.64 ? 1155 TRP A CZ2   1 
ATOM   8558  C  CZ3   . TRP A  1  1157 ? 8.949   86.130  108.686 1.00 24.38 ? 1155 TRP A CZ3   1 
ATOM   8559  C  CH2   . TRP A  1  1157 ? 10.187  85.718  109.182 1.00 26.75 ? 1155 TRP A CH2   1 
ATOM   8560  N  N     . ALA A  1  1158 ? 7.806   88.545  101.855 1.00 25.43 ? 1156 ALA A N     1 
ATOM   8561  C  CA    . ALA A  1  1158 ? 6.635   88.985  101.105 1.00 26.04 ? 1156 ALA A CA    1 
ATOM   8562  C  C     . ALA A  1  1158 ? 6.843   88.843  99.604  1.00 30.06 ? 1156 ALA A C     1 
ATOM   8563  O  O     . ALA A  1  1158 ? 5.876   88.628  98.865  1.00 39.45 ? 1156 ALA A O     1 
ATOM   8564  C  CB    . ALA A  1  1158 ? 6.295   90.433  101.457 1.00 33.90 ? 1156 ALA A CB    1 
ATOM   8565  N  N     . ALA A  1  1159 ? 8.083   88.956  99.136  1.00 27.73 ? 1157 ALA A N     1 
ATOM   8566  C  CA    . ALA A  1  1159 ? 8.351   88.847  97.708  1.00 34.06 ? 1157 ALA A CA    1 
ATOM   8567  C  C     . ALA A  1  1159 ? 8.368   87.407  97.219  1.00 34.25 ? 1157 ALA A C     1 
ATOM   8568  O  O     . ALA A  1  1159 ? 8.182   87.171  96.022  1.00 35.73 ? 1157 ALA A O     1 
ATOM   8569  C  CB    . ALA A  1  1159 ? 9.687   89.515  97.367  1.00 32.69 ? 1157 ALA A CB    1 
ATOM   8570  N  N     . ASP A  1  1160 ? 8.576   86.443  98.108  1.00 34.14 ? 1158 ASP A N     1 
ATOM   8571  C  CA    . ASP A  1  1160 ? 8.780   85.060  97.709  1.00 33.24 ? 1158 ASP A CA    1 
ATOM   8572  C  C     . ASP A  1  1160 ? 7.564   84.179  97.954  1.00 28.02 ? 1158 ASP A C     1 
ATOM   8573  O  O     . ASP A  1  1160 ? 7.643   82.967  97.746  1.00 30.93 ? 1158 ASP A O     1 
ATOM   8574  C  CB    . ASP A  1  1160 ? 10.006  84.495  98.424  1.00 33.21 ? 1158 ASP A CB    1 
ATOM   8575  C  CG    . ASP A  1  1160 ? 11.267  85.250  98.072  1.00 33.68 ? 1158 ASP A CG    1 
ATOM   8576  O  OD1   . ASP A  1  1160 ? 11.283  85.896  97.002  1.00 44.47 ? 1158 ASP A OD1   1 
ATOM   8577  O  OD2   . ASP A  1  1160 ? 12.236  85.213  98.854  1.00 33.72 ? 1158 ASP A OD2   1 
ATOM   8578  N  N     . GLY A  1  1161 ? 6.446   84.756  98.384  1.00 27.23 ? 1159 GLY A N     1 
ATOM   8579  C  CA    . GLY A  1  1161 ? 5.231   84.003  98.559  1.00 28.06 ? 1159 GLY A CA    1 
ATOM   8580  C  C     . GLY A  1  1161 ? 4.480   83.820  97.251  1.00 33.87 ? 1159 GLY A C     1 
ATOM   8581  O  O     . GLY A  1  1161 ? 5.006   84.086  96.166  1.00 36.49 ? 1159 GLY A O     1 
ATOM   8582  N  N     . PRO A  1  1162 ? 3.230   83.348  97.330  1.00 29.28 ? 1160 PRO A N     1 
ATOM   8583  C  CA    . PRO A  1  1162 ? 2.504   82.968  98.551  1.00 29.90 ? 1160 PRO A CA    1 
ATOM   8584  C  C     . PRO A  1  1162 ? 3.018   81.670  99.161  1.00 30.06 ? 1160 PRO A C     1 
ATOM   8585  O  O     . PRO A  1  1162 ? 3.397   80.716  98.482  1.00 28.34 ? 1160 PRO A O     1 
ATOM   8586  C  CB    . PRO A  1  1162 ? 1.056   82.826  98.062  1.00 29.41 ? 1160 PRO A CB    1 
ATOM   8587  C  CG    . PRO A  1  1162 ? 1.204   82.376  96.640  1.00 38.29 ? 1160 PRO A CG    1 
ATOM   8588  C  CD    . PRO A  1  1162 ? 2.420   83.113  96.123  1.00 33.56 ? 1160 PRO A CD    1 
ATOM   8589  N  N     . PHE A  1  1163 ? 3.051   81.628  100.483 1.00 22.34 ? 1161 PHE A N     1 
ATOM   8590  C  CA    . PHE A  1  1163 ? 3.354   80.389  101.169 1.00 19.92 ? 1161 PHE A CA    1 
ATOM   8591  C  C     . PHE A  1  1163 ? 2.057   79.680  101.519 1.00 21.03 ? 1161 PHE A C     1 
ATOM   8592  O  O     . PHE A  1  1163 ? 0.960   80.233  101.402 1.00 22.03 ? 1161 PHE A O     1 
ATOM   8593  C  CB    . PHE A  1  1163 ? 4.197   80.678  102.402 1.00 19.47 ? 1161 PHE A CB    1 
ATOM   8594  C  CG    . PHE A  1  1163 ? 5.438   81.441  102.080 1.00 22.12 ? 1161 PHE A CG    1 
ATOM   8595  C  CD1   . PHE A  1  1163 ? 6.406   80.882  101.265 1.00 24.78 ? 1161 PHE A CD1   1 
ATOM   8596  C  CD2   . PHE A  1  1163 ? 5.626   82.723  102.557 1.00 21.38 ? 1161 PHE A CD2   1 
ATOM   8597  C  CE1   . PHE A  1  1163 ? 7.553   81.581  100.945 1.00 25.76 ? 1161 PHE A CE1   1 
ATOM   8598  C  CE2   . PHE A  1  1163 ? 6.769   83.432  102.237 1.00 24.60 ? 1161 PHE A CE2   1 
ATOM   8599  C  CZ    . PHE A  1  1163 ? 7.735   82.859  101.436 1.00 26.28 ? 1161 PHE A CZ    1 
ATOM   8600  N  N     . ALA A  1  1164 ? 2.186   78.417  101.918 1.00 20.00 ? 1162 ALA A N     1 
ATOM   8601  C  CA    . ALA A  1  1164 ? 1.027   77.624  102.296 1.00 21.65 ? 1162 ALA A CA    1 
ATOM   8602  C  C     . ALA A  1  1164 ? 1.082   77.202  103.753 1.00 20.64 ? 1162 ALA A C     1 
ATOM   8603  O  O     . ALA A  1  1164 ? 0.254   76.400  104.193 1.00 23.07 ? 1162 ALA A O     1 
ATOM   8604  C  CB    . ALA A  1  1164 ? 0.901   76.399  101.384 1.00 23.87 ? 1162 ALA A CB    1 
ATOM   8605  N  N     . GLY A  1  1165 ? 2.032   77.729  104.508 1.00 18.90 ? 1163 GLY A N     1 
ATOM   8606  C  CA    . GLY A  1  1165 ? 2.139   77.467  105.926 1.00 20.75 ? 1163 GLY A CA    1 
ATOM   8607  C  C     . GLY A  1  1165 ? 3.502   77.941  106.375 1.00 20.05 ? 1163 GLY A C     1 
ATOM   8608  O  O     . GLY A  1  1165 ? 4.318   78.386  105.565 1.00 19.78 ? 1163 GLY A O     1 
ATOM   8609  N  N     . ALA A  1  1166 ? 3.743   77.837  107.680 1.00 19.79 ? 1164 ALA A N     1 
ATOM   8610  C  CA    . ALA A  1  1166 ? 5.036   78.249  108.206 1.00 20.08 ? 1164 ALA A CA    1 
ATOM   8611  C  C     . ALA A  1  1166 ? 5.415   77.377  109.390 1.00 20.71 ? 1164 ALA A C     1 
ATOM   8612  O  O     . ALA A  1  1166 ? 4.554   76.910  110.143 1.00 22.37 ? 1164 ALA A O     1 
ATOM   8613  C  CB    . ALA A  1  1166 ? 5.052   79.721  108.648 1.00 19.85 ? 1164 ALA A CB    1 
ATOM   8614  N  N     . LEU A  1  1167 ? 6.720   77.174  109.542 1.00 18.55 ? 1165 LEU A N     1 
ATOM   8615  C  CA    . LEU A  1  1167 ? 7.305   76.538  110.715 1.00 16.99 ? 1165 LEU A CA    1 
ATOM   8616  C  C     . LEU A  1  1167 ? 8.304   77.507  111.322 1.00 20.81 ? 1165 LEU A C     1 
ATOM   8617  O  O     . LEU A  1  1167 ? 9.147   78.056  110.609 1.00 21.94 ? 1165 LEU A O     1 
ATOM   8618  C  CB    . LEU A  1  1167 ? 7.993   75.226  110.349 1.00 21.32 ? 1165 LEU A CB    1 
ATOM   8619  C  CG    . LEU A  1  1167 ? 7.101   74.192  109.660 1.00 18.52 ? 1165 LEU A CG    1 
ATOM   8620  C  CD1   . LEU A  1  1167 ? 7.947   73.017  109.188 1.00 20.55 ? 1165 LEU A CD1   1 
ATOM   8621  C  CD2   . LEU A  1  1167 ? 5.990   73.725  110.608 1.00 20.48 ? 1165 LEU A CD2   1 
ATOM   8622  N  N     . VAL A  1  1168 ? 8.201   77.718  112.631 1.00 18.05 ? 1166 VAL A N     1 
ATOM   8623  C  CA    . VAL A  1  1168 ? 8.984   78.732  113.328 1.00 17.99 ? 1166 VAL A CA    1 
ATOM   8624  C  C     . VAL A  1  1168 ? 9.662   78.092  114.522 1.00 18.62 ? 1166 VAL A C     1 
ATOM   8625  O  O     . VAL A  1  1168 ? 9.044   77.319  115.261 1.00 20.45 ? 1166 VAL A O     1 
ATOM   8626  C  CB    . VAL A  1  1168 ? 8.105   79.914  113.785 1.00 21.37 ? 1166 VAL A CB    1 
ATOM   8627  C  CG1   . VAL A  1  1168 ? 8.957   80.979  114.496 1.00 20.11 ? 1166 VAL A CG1   1 
ATOM   8628  C  CG2   . VAL A  1  1168 ? 7.349   80.517  112.597 1.00 21.82 ? 1166 VAL A CG2   1 
ATOM   8629  N  N     . GLU A  1  1169 ? 10.927  78.433  114.719 1.00 18.72 ? 1167 GLU A N     1 
ATOM   8630  C  CA    . GLU A  1  1169 ? 11.694  78.007  115.878 1.00 19.53 ? 1167 GLU A CA    1 
ATOM   8631  C  C     . GLU A  1  1169 ? 12.152  79.246  116.630 1.00 22.86 ? 1167 GLU A C     1 
ATOM   8632  O  O     . GLU A  1  1169 ? 12.684  80.179  116.022 1.00 22.07 ? 1167 GLU A O     1 
ATOM   8633  C  CB    . GLU A  1  1169 ? 12.899  77.181  115.455 1.00 19.67 ? 1167 GLU A CB    1 
ATOM   8634  C  CG    . GLU A  1  1169 ? 13.782  76.728  116.607 1.00 21.61 ? 1167 GLU A CG    1 
ATOM   8635  C  CD    . GLU A  1  1169 ? 15.105  76.176  116.123 1.00 21.86 ? 1167 GLU A CD    1 
ATOM   8636  O  OE1   . GLU A  1  1169 ? 15.413  76.311  114.916 1.00 21.83 ? 1167 GLU A OE1   1 
ATOM   8637  O  OE2   . GLU A  1  1169 ? 15.834  75.601  116.950 1.00 22.17 ? 1167 GLU A OE2   1 
ATOM   8638  N  N     . GLY A  1  1170 ? 11.952  79.258  117.937 1.00 21.16 ? 1168 GLY A N     1 
ATOM   8639  C  CA    . GLY A  1  1170 ? 12.494  80.347  118.719 1.00 21.00 ? 1168 GLY A CA    1 
ATOM   8640  C  C     . GLY A  1  1170 ? 11.911  80.343  120.111 1.00 21.92 ? 1168 GLY A C     1 
ATOM   8641  O  O     . GLY A  1  1170 ? 11.011  79.563  120.435 1.00 25.57 ? 1168 GLY A O     1 
ATOM   8642  N  N     . ASP A  1  1171 ? 12.427  81.256  120.929 1.00 24.81 ? 1169 ASP A N     1 
ATOM   8643  C  CA    . ASP A  1  1171 ? 11.803  81.472  122.221 1.00 23.61 ? 1169 ASP A CA    1 
ATOM   8644  C  C     . ASP A  1  1171 ? 10.509  82.259  122.033 1.00 25.64 ? 1169 ASP A C     1 
ATOM   8645  O  O     . ASP A  1  1171 ? 10.112  82.609  120.913 1.00 22.64 ? 1169 ASP A O     1 
ATOM   8646  C  CB    . ASP A  1  1171 ? 12.778  82.139  123.202 1.00 25.10 ? 1169 ASP A CB    1 
ATOM   8647  C  CG    . ASP A  1  1171 ? 13.257  83.528  122.767 1.00 33.53 ? 1169 ASP A CG    1 
ATOM   8648  O  OD1   . ASP A  1  1171 ? 12.589  84.240  121.993 1.00 26.93 ? 1169 ASP A OD1   1 
ATOM   8649  O  OD2   . ASP A  1  1171 ? 14.339  83.927  123.249 1.00 39.07 ? 1169 ASP A OD2   1 
ATOM   8650  N  N     . ALA A  1  1172 ? 9.815   82.519  123.144 1.00 26.84 ? 1170 ALA A N     1 
ATOM   8651  C  CA    . ALA A  1  1172 ? 8.466   83.060  123.039 1.00 26.11 ? 1170 ALA A CA    1 
ATOM   8652  C  C     . ALA A  1  1172 ? 8.458   84.396  122.311 1.00 26.91 ? 1170 ALA A C     1 
ATOM   8653  O  O     . ALA A  1  1172 ? 7.628   84.616  121.425 1.00 26.12 ? 1170 ALA A O     1 
ATOM   8654  C  CB    . ALA A  1  1172 ? 7.831   83.196  124.420 1.00 29.99 ? 1170 ALA A CB    1 
ATOM   8655  N  N     . GLU A  1  1173 ? 9.391   85.294  122.640 1.00 28.34 ? 1171 GLU A N     1 
ATOM   8656  C  CA    . GLU A  1  1173 ? 9.347   86.597  121.988 1.00 29.50 ? 1171 GLU A CA    1 
ATOM   8657  C  C     . GLU A  1  1173 ? 9.809   86.520  120.538 1.00 27.31 ? 1171 GLU A C     1 
ATOM   8658  O  O     . GLU A  1  1173 ? 9.354   87.316  119.707 1.00 30.26 ? 1171 GLU A O     1 
ATOM   8659  C  CB    . GLU A  1  1173 ? 10.157  87.622  122.782 1.00 34.68 ? 1171 GLU A CB    1 
ATOM   8660  C  CG    . GLU A  1  1173 ? 9.472   88.003  124.090 1.00 38.82 ? 1171 GLU A CG    1 
ATOM   8661  C  CD    . GLU A  1  1173 ? 8.001   88.394  123.911 1.00 46.43 ? 1171 GLU A CD    1 
ATOM   8662  O  OE1   . GLU A  1  1173 ? 7.685   89.169  122.980 1.00 40.77 ? 1171 GLU A OE1   1 
ATOM   8663  O  OE2   . GLU A  1  1173 ? 7.154   87.926  124.706 1.00 42.34 ? 1171 GLU A OE2   1 
ATOM   8664  N  N     . ARG A  1  1174 ? 10.683  85.566  120.203 1.00 23.86 ? 1172 ARG A N     1 
ATOM   8665  C  CA    . ARG A  1  1174 ? 11.019  85.370  118.795 1.00 24.60 ? 1172 ARG A CA    1 
ATOM   8666  C  C     . ARG A  1  1174 ? 9.807   84.871  118.025 1.00 25.59 ? 1172 ARG A C     1 
ATOM   8667  O  O     . ARG A  1  1174 ? 9.528   85.337  116.911 1.00 23.48 ? 1172 ARG A O     1 
ATOM   8668  C  CB    . ARG A  1  1174 ? 12.187  84.390  118.661 1.00 24.46 ? 1172 ARG A CB    1 
ATOM   8669  C  CG    . ARG A  1  1174 ? 12.510  83.984  117.220 1.00 25.14 ? 1172 ARG A CG    1 
ATOM   8670  C  CD    . ARG A  1  1174 ? 12.977  85.186  116.416 1.00 27.34 ? 1172 ARG A CD    1 
ATOM   8671  N  NE    . ARG A  1  1174 ? 13.337  84.827  115.048 1.00 25.03 ? 1172 ARG A NE    1 
ATOM   8672  C  CZ    . ARG A  1  1174 ? 13.348  85.683  114.036 1.00 26.77 ? 1172 ARG A CZ    1 
ATOM   8673  N  NH1   . ARG A  1  1174 ? 13.022  86.956  114.206 1.00 28.16 ? 1172 ARG A NH1   1 
ATOM   8674  N  NH2   . ARG A  1  1174 ? 13.684  85.250  112.823 1.00 24.28 ? 1172 ARG A NH2   1 
ATOM   8675  N  N     . ILE A  1  1175 ? 9.067   83.933  118.616 1.00 22.82 ? 1173 ILE A N     1 
ATOM   8676  C  CA    . ILE A  1  1175 ? 7.854   83.418  117.986 1.00 24.55 ? 1173 ILE A CA    1 
ATOM   8677  C  C     . ILE A  1  1175 ? 6.851   84.542  117.767 1.00 20.58 ? 1173 ILE A C     1 
ATOM   8678  O  O     . ILE A  1  1175 ? 6.269   84.678  116.683 1.00 25.07 ? 1173 ILE A O     1 
ATOM   8679  C  CB    . ILE A  1  1175 ? 7.254   82.285  118.838 1.00 21.33 ? 1173 ILE A CB    1 
ATOM   8680  C  CG1   . ILE A  1  1175 ? 8.162   81.054  118.794 1.00 22.53 ? 1173 ILE A CG1   1 
ATOM   8681  C  CG2   . ILE A  1  1175 ? 5.850   81.959  118.370 1.00 21.96 ? 1173 ILE A CG2   1 
ATOM   8682  C  CD1   . ILE A  1  1175 ? 7.764   79.961  119.769 1.00 24.61 ? 1173 ILE A CD1   1 
ATOM   8683  N  N     . ARG A  1  1176 ? 6.629   85.364  118.796 1.00 27.20 ? 1174 ARG A N     1 
ATOM   8684  C  CA    . ARG A  1  1176 ? 5.690   86.470  118.665 1.00 22.78 ? 1174 ARG A CA    1 
ATOM   8685  C  C     . ARG A  1  1176 ? 6.105   87.415  117.546 1.00 20.91 ? 1174 ARG A C     1 
ATOM   8686  O  O     . ARG A  1  1176 ? 5.274   87.818  116.725 1.00 23.99 ? 1174 ARG A O     1 
ATOM   8687  C  CB    . ARG A  1  1176 ? 5.573   87.232  119.988 1.00 22.43 ? 1174 ARG A CB    1 
ATOM   8688  C  CG    . ARG A  1  1176 ? 4.309   88.098  120.030 1.00 28.15 ? 1174 ARG A CG    1 
ATOM   8689  C  CD    . ARG A  1  1176 ? 4.349   89.164  121.118 1.00 29.55 ? 1174 ARG A CD    1 
ATOM   8690  N  NE    . ARG A  1  1176 ? 4.702   88.605  122.415 1.00 30.91 ? 1174 ARG A NE    1 
ATOM   8691  C  CZ    . ARG A  1  1176 ? 3.827   88.145  123.298 1.00 38.04 ? 1174 ARG A CZ    1 
ATOM   8692  N  NH1   . ARG A  1  1176 ? 2.527   88.137  123.045 1.00 30.95 ? 1174 ARG A NH1   1 
ATOM   8693  N  NH2   . ARG A  1  1176 ? 4.267   87.689  124.471 1.00 36.77 ? 1174 ARG A NH2   1 
ATOM   8694  N  N     . ALA A  1  1177 ? 7.391   87.757  117.481 1.00 22.18 ? 1175 ALA A N     1 
ATOM   8695  C  CA    . ALA A  1  1177 ? 7.870   88.668  116.442 1.00 27.76 ? 1175 ALA A CA    1 
ATOM   8696  C  C     . ALA A  1  1177 ? 7.686   88.065  115.058 1.00 25.61 ? 1175 ALA A C     1 
ATOM   8697  O  O     . ALA A  1  1177 ? 7.240   88.741  114.124 1.00 26.76 ? 1175 ALA A O     1 
ATOM   8698  C  CB    . ALA A  1  1177 ? 9.340   89.009  116.677 1.00 25.52 ? 1175 ALA A CB    1 
ATOM   8699  N  N     . VAL A  1  1178 ? 8.046   86.792  114.905 1.00 23.88 ? 1176 VAL A N     1 
ATOM   8700  C  CA    . VAL A  1  1178 ? 7.876   86.128  113.617 1.00 20.83 ? 1176 VAL A CA    1 
ATOM   8701  C  C     . VAL A  1  1178 ? 6.403   86.039  113.252 1.00 25.79 ? 1176 VAL A C     1 
ATOM   8702  O  O     . VAL A  1  1178 ? 6.022   86.271  112.098 1.00 23.95 ? 1176 VAL A O     1 
ATOM   8703  C  CB    . VAL A  1  1178 ? 8.544   84.743  113.643 1.00 22.22 ? 1176 VAL A CB    1 
ATOM   8704  C  CG1   . VAL A  1  1178 ? 8.224   83.981  112.381 1.00 19.56 ? 1176 VAL A CG1   1 
ATOM   8705  C  CG2   . VAL A  1  1178 ? 10.045  84.881  113.789 1.00 23.26 ? 1176 VAL A CG2   1 
ATOM   8706  N  N     . ASN A  1  1179 ? 5.552   85.704  114.225 1.00 23.78 ? 1177 ASN A N     1 
ATOM   8707  C  CA    . ASN A  1  1179 ? 4.123   85.575  113.946 1.00 23.00 ? 1177 ASN A CA    1 
ATOM   8708  C  C     . ASN A  1  1179 ? 3.552   86.895  113.440 1.00 26.21 ? 1177 ASN A C     1 
ATOM   8709  O  O     . ASN A  1  1179 ? 2.704   86.909  112.540 1.00 26.08 ? 1177 ASN A O     1 
ATOM   8710  C  CB    . ASN A  1  1179 ? 3.396   85.109  115.214 1.00 29.89 ? 1177 ASN A CB    1 
ATOM   8711  C  CG    . ASN A  1  1179 ? 2.126   84.344  114.925 1.00 33.90 ? 1177 ASN A CG    1 
ATOM   8712  O  OD1   . ASN A  1  1179 ? 1.919   83.844  113.816 1.00 34.35 ? 1177 ASN A OD1   1 
ATOM   8713  N  ND2   . ASN A  1  1179 ? 1.256   84.245  115.932 1.00 30.07 ? 1177 ASN A ND2   1 
ATOM   8714  N  N     . LYS A  1  1180 ? 4.018   88.018  113.998 1.00 25.55 ? 1178 LYS A N     1 
ATOM   8715  C  CA    . LYS A  1  1180 ? 3.592   89.326  113.512 1.00 27.03 ? 1178 LYS A CA    1 
ATOM   8716  C  C     . LYS A  1  1180 ? 4.086   89.580  112.096 1.00 26.07 ? 1178 LYS A C     1 
ATOM   8717  O  O     . LYS A  1  1180 ? 3.334   90.078  111.251 1.00 26.47 ? 1178 LYS A O     1 
ATOM   8718  C  CB    . LYS A  1  1180 ? 4.100   90.418  114.447 1.00 27.21 ? 1178 LYS A CB    1 
ATOM   8719  C  CG    . LYS A  1  1180 ? 3.438   90.432  115.801 1.00 31.85 ? 1178 LYS A CG    1 
ATOM   8720  C  CD    . LYS A  1  1180 ? 4.167   91.416  116.715 1.00 31.24 ? 1178 LYS A CD    1 
ATOM   8721  C  CE    . LYS A  1  1180 ? 3.272   91.887  117.824 1.00 49.21 ? 1178 LYS A CE    1 
ATOM   8722  N  NZ    . LYS A  1  1180 ? 2.943   90.757  118.720 1.00 49.68 ? 1178 LYS A NZ    1 
ATOM   8723  N  N     . ALA A  1  1181 ? 5.353   89.261  111.824 1.00 24.55 ? 1179 ALA A N     1 
ATOM   8724  C  CA    . ALA A  1  1181 ? 5.878   89.410  110.471 1.00 26.29 ? 1179 ALA A CA    1 
ATOM   8725  C  C     . ALA A  1  1181 ? 5.125   88.532  109.478 1.00 25.73 ? 1179 ALA A C     1 
ATOM   8726  O  O     . ALA A  1  1181 ? 4.882   88.943  108.338 1.00 26.29 ? 1179 ALA A O     1 
ATOM   8727  C  CB    . ALA A  1  1181 ? 7.365   89.077  110.446 1.00 23.93 ? 1179 ALA A CB    1 
ATOM   8728  N  N     . ILE A  1  1182 ? 4.753   87.317  109.883 1.00 22.21 ? 1180 ILE A N     1 
ATOM   8729  C  CA    . ILE A  1  1182 ? 4.029   86.442  108.961 1.00 22.02 ? 1180 ILE A CA    1 
ATOM   8730  C  C     . ILE A  1  1182 ? 2.633   86.984  108.704 1.00 26.82 ? 1180 ILE A C     1 
ATOM   8731  O  O     . ILE A  1  1182 ? 2.142   86.972  107.566 1.00 24.93 ? 1180 ILE A O     1 
ATOM   8732  C  CB    . ILE A  1  1182 ? 3.995   85.008  109.511 1.00 19.82 ? 1180 ILE A CB    1 
ATOM   8733  C  CG1   . ILE A  1  1182 ? 5.390   84.397  109.438 1.00 23.15 ? 1180 ILE A CG1   1 
ATOM   8734  C  CG2   . ILE A  1  1182 ? 2.969   84.160  108.746 1.00 22.96 ? 1180 ILE A CG2   1 
ATOM   8735  C  CD1   . ILE A  1  1182 ? 5.505   83.046  110.151 1.00 24.35 ? 1180 ILE A CD1   1 
ATOM   8736  N  N     . ALA A  1  1183 ? 1.972   87.482  109.749 1.00 21.99 ? 1181 ALA A N     1 
ATOM   8737  C  CA    . ALA A  1  1183 ? 0.644   88.043  109.552 1.00 24.73 ? 1181 ALA A CA    1 
ATOM   8738  C  C     . ALA A  1  1183 ? 0.681   89.208  108.573 1.00 28.61 ? 1181 ALA A C     1 
ATOM   8739  O  O     . ALA A  1  1183 ? -0.308  89.461  107.877 1.00 27.02 ? 1181 ALA A O     1 
ATOM   8740  C  CB    . ALA A  1  1183 ? 0.049   88.471  110.895 1.00 23.33 ? 1181 ALA A CB    1 
ATOM   8741  N  N     . ALA A  1  1184 ? 1.822   89.898  108.474 1.00 25.24 ? 1182 ALA A N     1 
ATOM   8742  C  CA    . ALA A  1  1184 ? 1.939   91.045  107.578 1.00 25.76 ? 1182 ALA A CA    1 
ATOM   8743  C  C     . ALA A  1  1184 ? 2.164   90.650  106.129 1.00 27.84 ? 1182 ALA A C     1 
ATOM   8744  O  O     . ALA A  1  1184 ? 2.127   91.523  105.257 1.00 27.65 ? 1182 ALA A O     1 
ATOM   8745  C  CB    . ALA A  1  1184 ? 3.079   91.968  108.024 1.00 25.44 ? 1182 ALA A CB    1 
ATOM   8746  N  N     . LEU A  1  1185 ? 2.400   89.375  105.849 1.00 23.06 ? 1183 LEU A N     1 
ATOM   8747  C  CA    . LEU A  1  1185 ? 2.623   88.968  104.473 1.00 27.95 ? 1183 LEU A CA    1 
ATOM   8748  C  C     . LEU A  1  1185 ? 1.322   89.091  103.687 1.00 28.47 ? 1183 LEU A C     1 
ATOM   8749  O  O     . LEU A  1  1185 ? 0.255   88.718  104.182 1.00 27.46 ? 1183 LEU A O     1 
ATOM   8750  C  CB    . LEU A  1  1185 ? 3.144   87.537  104.408 1.00 22.81 ? 1183 LEU A CB    1 
ATOM   8751  C  CG    . LEU A  1  1185 ? 4.446   87.278  105.155 1.00 25.83 ? 1183 LEU A CG    1 
ATOM   8752  C  CD1   . LEU A  1  1185 ? 4.738   85.794  105.139 1.00 23.79 ? 1183 LEU A CD1   1 
ATOM   8753  C  CD2   . LEU A  1  1185 ? 5.601   88.073  104.544 1.00 25.64 ? 1183 LEU A CD2   1 
ATOM   8754  N  N     . PRO A  1  1186 ? 1.371   89.630  102.475 1.00 27.84 ? 1184 PRO A N     1 
ATOM   8755  C  CA    . PRO A  1  1186 ? 0.152   89.736  101.672 1.00 25.07 ? 1184 PRO A CA    1 
ATOM   8756  C  C     . PRO A  1  1186 ? -0.364  88.359  101.290 1.00 23.10 ? 1184 PRO A C     1 
ATOM   8757  O  O     . PRO A  1  1186 ? 0.375   87.377  101.230 1.00 26.52 ? 1184 PRO A O     1 
ATOM   8758  C  CB    . PRO A  1  1186 ? 0.599   90.519  100.431 1.00 35.16 ? 1184 PRO A CB    1 
ATOM   8759  C  CG    . PRO A  1  1186 ? 1.928   91.142  100.814 1.00 41.05 ? 1184 PRO A CG    1 
ATOM   8760  C  CD    . PRO A  1  1186 ? 2.547   90.176  101.781 1.00 32.24 ? 1184 PRO A CD    1 
ATOM   8761  N  N     . GLY A  1  1187 ? -1.664  88.296  101.043 1.00 22.27 ? 1185 GLY A N     1 
ATOM   8762  C  CA    . GLY A  1  1187 ? -2.251  87.091  100.507 1.00 25.65 ? 1185 GLY A CA    1 
ATOM   8763  C  C     . GLY A  1  1187 ? -2.826  86.185  101.576 1.00 22.93 ? 1185 GLY A C     1 
ATOM   8764  O  O     . GLY A  1  1187 ? -3.530  86.630  102.491 1.00 26.52 ? 1185 GLY A O     1 
ATOM   8765  N  N     . PRO A  1  1188 ? -2.542  84.892  101.474 1.00 22.11 ? 1186 PRO A N     1 
ATOM   8766  C  CA    . PRO A  1  1188 ? -3.266  83.920  102.293 1.00 23.56 ? 1186 PRO A CA    1 
ATOM   8767  C  C     . PRO A  1  1188 ? -2.846  83.982  103.748 1.00 22.51 ? 1186 PRO A C     1 
ATOM   8768  O  O     . PRO A  1  1188 ? -1.703  84.306  104.087 1.00 23.02 ? 1186 PRO A O     1 
ATOM   8769  C  CB    . PRO A  1  1188 ? -2.890  82.574  101.665 1.00 25.60 ? 1186 PRO A CB    1 
ATOM   8770  C  CG    . PRO A  1  1188 ? -1.554  82.803  101.074 1.00 26.45 ? 1186 PRO A CG    1 
ATOM   8771  C  CD    . PRO A  1  1188 ? -1.546  84.250  100.604 1.00 22.97 ? 1186 PRO A CD    1 
ATOM   8772  N  N     . LEU A  1  1189 ? -3.808  83.674  104.609 1.00 21.02 ? 1187 LEU A N     1 
ATOM   8773  C  CA    . LEU A  1  1189 ? -3.502  83.440  106.009 1.00 20.01 ? 1187 LEU A CA    1 
ATOM   8774  C  C     . LEU A  1  1189 ? -2.702  82.154  106.105 1.00 24.62 ? 1187 LEU A C     1 
ATOM   8775  O  O     . LEU A  1  1189 ? -3.095  81.130  105.541 1.00 31.93 ? 1187 LEU A O     1 
ATOM   8776  C  CB    . LEU A  1  1189 ? -4.782  83.335  106.831 1.00 23.13 ? 1187 LEU A CB    1 
ATOM   8777  C  CG    . LEU A  1  1189 ? -5.461  84.648  107.227 1.00 26.16 ? 1187 LEU A CG    1 
ATOM   8778  C  CD1   . LEU A  1  1189 ? -6.131  85.322  106.027 1.00 25.79 ? 1187 LEU A CD1   1 
ATOM   8779  C  CD2   . LEU A  1  1189 ? -6.478  84.414  108.330 1.00 32.73 ? 1187 LEU A CD2   1 
ATOM   8780  N  N     . LEU A  1  1190 ? -1.562  82.209  106.778 1.00 21.36 ? 1188 LEU A N     1 
ATOM   8781  C  CA    . LEU A  1  1190 ? -0.698  81.043  106.874 1.00 19.27 ? 1188 LEU A CA    1 
ATOM   8782  C  C     . LEU A  1  1190 ? -0.984  80.309  108.172 1.00 21.86 ? 1188 LEU A C     1 
ATOM   8783  O  O     . LEU A  1  1190 ? -1.112  80.932  109.228 1.00 22.86 ? 1188 LEU A O     1 
ATOM   8784  C  CB    . LEU A  1  1190 ? 0.777   81.432  106.827 1.00 21.39 ? 1188 LEU A CB    1 
ATOM   8785  C  CG    . LEU A  1  1190 ? 1.262   82.149  105.572 1.00 24.85 ? 1188 LEU A CG    1 
ATOM   8786  C  CD1   . LEU A  1  1190 ? 2.775   82.105  105.539 1.00 26.03 ? 1188 LEU A CD1   1 
ATOM   8787  C  CD2   . LEU A  1  1190 ? 0.671   81.485  104.341 1.00 27.79 ? 1188 LEU A CD2   1 
ATOM   8788  N  N     . LEU A  1  1191 ? -1.103  78.993  108.082 1.00 20.65 ? 1189 LEU A N     1 
ATOM   8789  C  CA    . LEU A  1  1191 ? -1.154  78.157  109.276 1.00 21.01 ? 1189 LEU A CA    1 
ATOM   8790  C  C     . LEU A  1  1191 ? 0.268   78.027  109.798 1.00 20.49 ? 1189 LEU A C     1 
ATOM   8791  O  O     . LEU A  1  1191 ? 1.113   77.371  109.169 1.00 22.16 ? 1189 LEU A O     1 
ATOM   8792  C  CB    . LEU A  1  1191 ? -1.769  76.804  108.948 1.00 19.82 ? 1189 LEU A CB    1 
ATOM   8793  C  CG    . LEU A  1  1191 ? -2.296  75.967  110.110 1.00 18.63 ? 1189 LEU A CG    1 
ATOM   8794  C  CD1   . LEU A  1  1191 ? -3.153  74.827  109.587 1.00 20.71 ? 1189 LEU A CD1   1 
ATOM   8795  C  CD2   . LEU A  1  1191 ? -1.146  75.410  110.952 1.00 20.05 ? 1189 LEU A CD2   1 
ATOM   8796  N  N     . VAL A  1  1192 ? 0.524   78.663  110.942 1.00 20.55 ? 1190 VAL A N     1 
ATOM   8797  C  CA    . VAL A  1  1192 ? 1.848   78.763  111.534 1.00 20.07 ? 1190 VAL A CA    1 
ATOM   8798  C  C     . VAL A  1  1192 ? 1.954   77.774  112.684 1.00 17.94 ? 1190 VAL A C     1 
ATOM   8799  O  O     . VAL A  1  1192 ? 1.073   77.721  113.556 1.00 22.90 ? 1190 VAL A O     1 
ATOM   8800  C  CB    . VAL A  1  1192 ? 2.113   80.192  112.036 1.00 23.80 ? 1190 VAL A CB    1 
ATOM   8801  C  CG1   . VAL A  1  1192 ? 3.507   80.291  112.662 1.00 25.11 ? 1190 VAL A CG1   1 
ATOM   8802  C  CG2   . VAL A  1  1192 ? 1.952   81.189  110.900 1.00 24.87 ? 1190 VAL A CG2   1 
ATOM   8803  N  N     . GLN A  1  1193 ? 3.046   77.013  112.708 1.00 20.48 ? 1191 GLN A N     1 
ATOM   8804  C  CA    . GLN A  1  1193 ? 3.404   76.178  113.845 1.00 17.30 ? 1191 GLN A CA    1 
ATOM   8805  C  C     . GLN A  1  1193 ? 4.737   76.649  114.388 1.00 19.62 ? 1191 GLN A C     1 
ATOM   8806  O  O     . GLN A  1  1193 ? 5.701   76.804  113.627 1.00 19.57 ? 1191 GLN A O     1 
ATOM   8807  C  CB    . GLN A  1  1193 ? 3.519   74.714  113.461 1.00 18.19 ? 1191 GLN A CB    1 
ATOM   8808  C  CG    . GLN A  1  1193 ? 2.261   74.144  112.865 1.00 21.53 ? 1191 GLN A CG    1 
ATOM   8809  C  CD    . GLN A  1  1193 ? 2.328   72.640  112.806 1.00 21.13 ? 1191 GLN A CD    1 
ATOM   8810  O  OE1   . GLN A  1  1193 ? 2.275   71.972  113.836 1.00 23.03 ? 1191 GLN A OE1   1 
ATOM   8811  N  NE2   . GLN A  1  1193 ? 2.455   72.100  111.609 1.00 22.10 ? 1191 GLN A NE2   1 
ATOM   8812  N  N     . ALA A  1  1194 ? 4.800   76.844  115.699 1.00 19.55 ? 1192 ALA A N     1 
ATOM   8813  C  CA    . ALA A  1  1194 ? 6.010   77.311  116.343 1.00 19.17 ? 1192 ALA A CA    1 
ATOM   8814  C  C     . ALA A  1  1194 ? 6.439   76.330  117.425 1.00 21.18 ? 1192 ALA A C     1 
ATOM   8815  O  O     . ALA A  1  1194 ? 5.616   75.617  118.010 1.00 22.61 ? 1192 ALA A O     1 
ATOM   8816  C  CB    . ALA A  1  1194 ? 5.792   78.699  116.945 1.00 19.96 ? 1192 ALA A CB    1 
ATOM   8817  N  N     . ALA A  1  1195 ? 7.741   76.308  117.682 1.00 19.87 ? 1193 ALA A N     1 
ATOM   8818  C  CA    . ALA A  1  1195 ? 8.311   75.483  118.729 1.00 22.47 ? 1193 ALA A CA    1 
ATOM   8819  C  C     . ALA A  1  1195 ? 9.617   76.122  119.168 1.00 19.29 ? 1193 ALA A C     1 
ATOM   8820  O  O     . ALA A  1  1195 ? 10.303  76.772  118.374 1.00 22.95 ? 1193 ALA A O     1 
ATOM   8821  C  CB    . ALA A  1  1195 ? 8.551   74.045  118.251 1.00 20.47 ? 1193 ALA A CB    1 
ATOM   8822  N  N     . SER A  1  1196 ? 9.946   75.939  120.441 1.00 21.60 ? 1194 SER A N     1 
ATOM   8823  C  CA    . SER A  1  1196 ? 11.261  76.312  120.914 1.00 23.89 ? 1194 SER A CA    1 
ATOM   8824  C  C     . SER A  1  1196 ? 12.280  75.262  120.498 1.00 23.39 ? 1194 SER A C     1 
ATOM   8825  O  O     . SER A  1  1196 ? 11.935  74.136  120.126 1.00 22.58 ? 1194 SER A O     1 
ATOM   8826  C  CB    . SER A  1  1196 ? 11.261  76.438  122.429 1.00 24.20 ? 1194 SER A CB    1 
ATOM   8827  O  OG    . SER A  1  1196 ? 11.045  75.158  123.004 1.00 24.41 ? 1194 SER A OG    1 
ATOM   8828  N  N     . SER A  1  1197 ? 13.555  75.636  120.579 1.00 21.12 ? 1195 SER A N     1 
ATOM   8829  C  CA    . SER A  1  1197 ? 14.613  74.671  120.304 1.00 21.36 ? 1195 SER A CA    1 
ATOM   8830  C  C     . SER A  1  1197 ? 14.510  73.473  121.238 1.00 23.63 ? 1195 SER A C     1 
ATOM   8831  O  O     . SER A  1  1197 ? 14.687  72.325  120.811 1.00 21.90 ? 1195 SER A O     1 
ATOM   8832  C  CB    . SER A  1  1197 ? 15.983  75.338  120.438 1.00 25.67 ? 1195 SER A CB    1 
ATOM   8833  O  OG    . SER A  1  1197 ? 16.135  76.377  119.483 1.00 25.55 ? 1195 SER A OG    1 
ATOM   8834  N  N     . GLY A  1  1198 ? 14.222  73.724  122.517 1.00 27.77 ? 1196 GLY A N     1 
ATOM   8835  C  CA    . GLY A  1  1198 ? 14.100  72.628  123.467 1.00 23.59 ? 1196 GLY A CA    1 
ATOM   8836  C  C     . GLY A  1  1198 ? 12.919  71.732  123.163 1.00 26.17 ? 1196 GLY A C     1 
ATOM   8837  O  O     . GLY A  1  1198 ? 12.996  70.510  123.317 1.00 24.08 ? 1196 GLY A O     1 
ATOM   8838  N  N     . GLU A  1  1199 ? 11.810  72.328  122.724 1.00 23.52 ? 1197 GLU A N     1 
ATOM   8839  C  CA    . GLU A  1  1199 ? 10.650  71.539  122.335 1.00 23.74 ? 1197 GLU A CA    1 
ATOM   8840  C  C     . GLU A  1  1199 ? 10.971  70.648  121.143 1.00 24.38 ? 1197 GLU A C     1 
ATOM   8841  O  O     . GLU A  1  1199 ? 10.573  69.479  121.106 1.00 23.79 ? 1197 GLU A O     1 
ATOM   8842  C  CB    . GLU A  1  1199 ? 9.493   72.478  122.015 1.00 25.70 ? 1197 GLU A CB    1 
ATOM   8843  C  CG    . GLU A  1  1199 ? 8.170   71.809  121.774 1.00 31.08 ? 1197 GLU A CG    1 
ATOM   8844  C  CD    . GLU A  1  1199 ? 7.073   72.829  121.510 1.00 41.66 ? 1197 GLU A CD    1 
ATOM   8845  O  OE1   . GLU A  1  1199 ? 7.358   74.048  121.609 1.00 35.86 ? 1197 GLU A OE1   1 
ATOM   8846  O  OE2   . GLU A  1  1199 ? 5.934   72.412  121.206 1.00 46.17 ? 1197 GLU A OE2   1 
ATOM   8847  N  N     . ILE A  1  1200 ? 11.710  71.177  120.166 1.00 22.35 ? 1198 ILE A N     1 
ATOM   8848  C  CA    . ILE A  1  1200 ? 12.121  70.355  119.032 1.00 19.81 ? 1198 ILE A CA    1 
ATOM   8849  C  C     . ILE A  1  1200 ? 12.962  69.175  119.512 1.00 25.54 ? 1198 ILE A C     1 
ATOM   8850  O  O     . ILE A  1  1200 ? 12.812  68.050  119.025 1.00 24.56 ? 1198 ILE A O     1 
ATOM   8851  C  CB    . ILE A  1  1200 ? 12.873  71.215  117.993 1.00 20.47 ? 1198 ILE A CB    1 
ATOM   8852  C  CG1   . ILE A  1  1200 ? 11.915  72.201  117.333 1.00 21.77 ? 1198 ILE A CG1   1 
ATOM   8853  C  CG2   . ILE A  1  1200 ? 13.539  70.344  116.941 1.00 20.47 ? 1198 ILE A CG2   1 
ATOM   8854  C  CD1   . ILE A  1  1200 ? 12.596  73.219  116.434 1.00 22.12 ? 1198 ILE A CD1   1 
ATOM   8855  N  N     . ALA A  1  1201 ? 13.833  69.400  120.500 1.00 23.26 ? 1199 ALA A N     1 
ATOM   8856  C  CA    . ALA A  1  1201 ? 14.665  68.309  121.001 1.00 25.29 ? 1199 ALA A CA    1 
ATOM   8857  C  C     . ALA A  1  1201 ? 13.849  67.309  121.813 1.00 26.10 ? 1199 ALA A C     1 
ATOM   8858  O  O     . ALA A  1  1201 ? 14.125  66.104  121.777 1.00 24.87 ? 1199 ALA A O     1 
ATOM   8859  C  CB    . ALA A  1  1201 ? 15.815  68.861  121.843 1.00 26.69 ? 1199 ALA A CB    1 
ATOM   8860  N  N     . ARG A  1  1202 ? 12.838  67.779  122.537 1.00 22.64 ? 1200 ARG A N     1 
ATOM   8861  C  CA    . ARG A  1  1202 ? 12.106  66.897  123.437 1.00 25.61 ? 1200 ARG A CA    1 
ATOM   8862  C  C     . ARG A  1  1202 ? 10.952  66.183  122.755 1.00 27.41 ? 1200 ARG A C     1 
ATOM   8863  O  O     . ARG A  1  1202 ? 10.654  65.035  123.099 1.00 27.96 ? 1200 ARG A O     1 
ATOM   8864  C  CB    . ARG A  1  1202 ? 11.564  67.681  124.637 1.00 22.86 ? 1200 ARG A CB    1 
ATOM   8865  C  CG    . ARG A  1  1202 ? 12.629  68.146  125.627 1.00 24.07 ? 1200 ARG A CG    1 
ATOM   8866  C  CD    . ARG A  1  1202 ? 11.975  68.771  126.854 1.00 28.16 ? 1200 ARG A CD    1 
ATOM   8867  N  NE    . ARG A  1  1202 ? 11.122  69.885  126.466 1.00 30.72 ? 1200 ARG A NE    1 
ATOM   8868  C  CZ    . ARG A  1  1202 ? 11.506  71.154  126.453 1.00 31.52 ? 1200 ARG A CZ    1 
ATOM   8869  N  NH1   . ARG A  1  1202 ? 12.696  71.524  126.906 1.00 28.50 ? 1200 ARG A NH1   1 
ATOM   8870  N  NH2   . ARG A  1  1202 ? 10.675  72.075  125.973 1.00 30.19 ? 1200 ARG A NH2   1 
ATOM   8871  N  N     . ASN A  1  1203 ? 10.296  66.825  121.804 1.00 23.57 ? 1201 ASN A N     1 
ATOM   8872  C  CA    . ASN A  1  1203 ? 9.034   66.318  121.275 1.00 25.82 ? 1201 ASN A CA    1 
ATOM   8873  C  C     . ASN A  1  1203 ? 9.157   66.021  119.792 1.00 30.07 ? 1201 ASN A C     1 
ATOM   8874  O  O     . ASN A  1  1203 ? 9.237   66.961  118.976 1.00 25.18 ? 1201 ASN A O     1 
ATOM   8875  C  CB    . ASN A  1  1203 ? 7.911   67.322  121.524 1.00 26.29 ? 1201 ASN A CB    1 
ATOM   8876  C  CG    . ASN A  1  1203 ? 6.572   66.832  121.019 1.00 28.94 ? 1201 ASN A CG    1 
ATOM   8877  O  OD1   . ASN A  1  1203 ? 6.444   65.694  120.576 1.00 28.96 ? 1201 ASN A OD1   1 
ATOM   8878  N  ND2   . ASN A  1  1203 ? 5.560   67.694  121.087 1.00 29.18 ? 1201 ASN A ND2   1 
ATOM   8879  N  N     . PRO A  1  1204 ? 9.137   64.748  119.395 1.00 27.30 ? 1202 PRO A N     1 
ATOM   8880  C  CA    . PRO A  1  1204 ? 9.201   64.419  117.967 1.00 30.27 ? 1202 PRO A CA    1 
ATOM   8881  C  C     . PRO A  1  1204 ? 8.057   65.004  117.176 1.00 27.87 ? 1202 PRO A C     1 
ATOM   8882  O  O     . PRO A  1  1204 ? 8.180   65.162  115.957 1.00 28.46 ? 1202 PRO A O     1 
ATOM   8883  C  CB    . PRO A  1  1204 ? 9.156   62.883  117.959 1.00 33.20 ? 1202 PRO A CB    1 
ATOM   8884  C  CG    . PRO A  1  1204 ? 9.539   62.472  119.352 1.00 39.35 ? 1202 PRO A CG    1 
ATOM   8885  C  CD    . PRO A  1  1204 ? 8.996   63.551  120.239 1.00 29.64 ? 1202 PRO A CD    1 
ATOM   8886  N  N     . ASP A  1  1205 ? 6.941   65.323  117.830 1.00 27.57 ? 1203 ASP A N     1 
ATOM   8887  C  CA    . ASP A  1  1205 ? 5.791   65.928  117.175 1.00 28.34 ? 1203 ASP A CA    1 
ATOM   8888  C  C     . ASP A  1  1205 ? 5.701   67.427  117.433 1.00 28.79 ? 1203 ASP A C     1 
ATOM   8889  O  O     . ASP A  1  1205 ? 4.603   67.993  117.367 1.00 29.72 ? 1203 ASP A O     1 
ATOM   8890  C  CB    . ASP A  1  1205 ? 4.503   65.246  117.634 1.00 31.64 ? 1203 ASP A CB    1 
ATOM   8891  C  CG    . ASP A  1  1205 ? 4.453   63.776  117.269 1.00 37.27 ? 1203 ASP A CG    1 
ATOM   8892  O  OD1   . ASP A  1  1205 ? 5.136   63.356  116.305 1.00 34.16 ? 1203 ASP A OD1   1 
ATOM   8893  O  OD2   . ASP A  1  1205 ? 3.718   63.041  117.958 1.00 38.42 ? 1203 ASP A OD2   1 
ATOM   8894  N  N     . ALA A  1  1206 ? 6.830   68.070  117.747 1.00 22.62 ? 1204 ALA A N     1 
ATOM   8895  C  CA    . ALA A  1  1206 ? 6.830   69.511  117.980 1.00 24.45 ? 1204 ALA A CA    1 
ATOM   8896  C  C     . ALA A  1  1206 ? 6.131   70.243  116.845 1.00 25.39 ? 1204 ALA A C     1 
ATOM   8897  O  O     . ALA A  1  1206 ? 5.345   71.168  117.078 1.00 27.85 ? 1204 ALA A O     1 
ATOM   8898  C  CB    . ALA A  1  1206 ? 8.264   70.017  118.140 1.00 23.87 ? 1204 ALA A CB    1 
ATOM   8899  N  N     . TYR A  1  1207 ? 6.396   69.832  115.610 1.00 23.74 ? 1205 TYR A N     1 
ATOM   8900  C  CA    . TYR A  1  1207 ? 5.632   70.283  114.458 1.00 19.88 ? 1205 TYR A CA    1 
ATOM   8901  C  C     . TYR A  1  1207 ? 4.709   69.152  114.033 1.00 23.20 ? 1205 TYR A C     1 
ATOM   8902  O  O     . TYR A  1  1207 ? 5.171   68.040  113.764 1.00 31.17 ? 1205 TYR A O     1 
ATOM   8903  C  CB    . TYR A  1  1207 ? 6.558   70.680  113.313 1.00 20.57 ? 1205 TYR A CB    1 
ATOM   8904  C  CG    . TYR A  1  1207 ? 7.499   71.801  113.677 1.00 21.49 ? 1205 TYR A CG    1 
ATOM   8905  C  CD1   . TYR A  1  1207 ? 7.006   73.062  114.007 1.00 23.69 ? 1205 TYR A CD1   1 
ATOM   8906  C  CD2   . TYR A  1  1207 ? 8.874   71.603  113.697 1.00 18.87 ? 1205 TYR A CD2   1 
ATOM   8907  C  CE1   . TYR A  1  1207 ? 7.865   74.101  114.335 1.00 21.70 ? 1205 TYR A CE1   1 
ATOM   8908  C  CE2   . TYR A  1  1207 ? 9.741   72.640  114.027 1.00 20.62 ? 1205 TYR A CE2   1 
ATOM   8909  C  CZ    . TYR A  1  1207 ? 9.225   73.882  114.343 1.00 21.41 ? 1205 TYR A CZ    1 
ATOM   8910  O  OH    . TYR A  1  1207 ? 10.081  74.902  114.676 1.00 21.36 ? 1205 TYR A OH    1 
ATOM   8911  N  N     . CYS A  1  1208 ? 3.417   69.426  113.985 1.00 21.64 ? 1206 CYS A N     1 
ATOM   8912  C  CA    . CYS A  1  1208 ? 2.450   68.388  113.679 1.00 22.88 ? 1206 CYS A CA    1 
ATOM   8913  C  C     . CYS A  1  1208 ? 2.279   68.275  112.167 1.00 22.82 ? 1206 CYS A C     1 
ATOM   8914  O  O     . CYS A  1  1208 ? 2.031   69.274  111.484 1.00 20.66 ? 1206 CYS A O     1 
ATOM   8915  C  CB    . CYS A  1  1208 ? 1.129   68.702  114.376 1.00 23.97 ? 1206 CYS A CB    1 
ATOM   8916  S  SG    . CYS A  1  1208 ? -0.193  67.551  113.977 1.00 25.34 ? 1206 CYS A SG    1 
ATOM   8917  N  N     . LEU A  1  1209 ? 2.427   67.057  111.640 1.00 17.76 ? 1207 LEU A N     1 
ATOM   8918  C  CA    . LEU A  1  1209 ? 2.349   66.870  110.198 1.00 17.61 ? 1207 LEU A CA    1 
ATOM   8919  C  C     . LEU A  1  1209 ? 0.928   66.975  109.651 1.00 18.98 ? 1207 LEU A C     1 
ATOM   8920  O  O     . LEU A  1  1209 ? 0.768   67.108  108.433 1.00 18.44 ? 1207 LEU A O     1 
ATOM   8921  C  CB    . LEU A  1  1209 ? 2.962   65.517  109.819 1.00 17.62 ? 1207 LEU A CB    1 
ATOM   8922  C  CG    . LEU A  1  1209 ? 4.419   65.332  110.247 1.00 20.22 ? 1207 LEU A CG    1 
ATOM   8923  C  CD1   . LEU A  1  1209 ? 4.939   64.031  109.664 1.00 21.56 ? 1207 LEU A CD1   1 
ATOM   8924  C  CD2   . LEU A  1  1209 ? 5.308   66.482  109.816 1.00 21.34 ? 1207 LEU A CD2   1 
ATOM   8925  N  N     . ASN A  1  1210 ? -0.097  66.922  110.508 1.00 20.07 ? 1208 ASN A N     1 
ATOM   8926  C  CA    . ASN A  1  1210 ? -1.471  67.130  110.053 1.00 21.59 ? 1208 ASN A CA    1 
ATOM   8927  C  C     . ASN A  1  1210 ? -1.611  68.447  109.306 1.00 17.75 ? 1208 ASN A C     1 
ATOM   8928  O  O     . ASN A  1  1210 ? -2.403  68.558  108.368 1.00 20.95 ? 1208 ASN A O     1 
ATOM   8929  C  CB    . ASN A  1  1210 ? -2.453  67.141  111.232 1.00 21.26 ? 1208 ASN A CB    1 
ATOM   8930  C  CG    . ASN A  1  1210 ? -2.519  65.826  111.974 1.00 24.94 ? 1208 ASN A CG    1 
ATOM   8931  O  OD1   . ASN A  1  1210 ? -1.733  64.910  111.735 1.00 30.49 ? 1208 ASN A OD1   1 
ATOM   8932  N  ND2   . ASN A  1  1210 ? -3.455  65.740  112.910 1.00 33.01 ? 1208 ASN A ND2   1 
ATOM   8933  N  N     . TRP A  1  1211 ? -0.893  69.478  109.751 1.00 18.90 ? 1209 TRP A N     1 
ATOM   8934  C  CA    . TRP A  1  1211 ? -1.121  70.822  109.240 1.00 18.57 ? 1209 TRP A CA    1 
ATOM   8935  C  C     . TRP A  1  1211 ? -0.177  71.176  108.116 1.00 19.32 ? 1209 TRP A C     1 
ATOM   8936  O  O     . TRP A  1  1211 ? -0.206  72.310  107.635 1.00 22.78 ? 1209 TRP A O     1 
ATOM   8937  C  CB    . TRP A  1  1211 ? -0.999  71.848  110.384 1.00 20.60 ? 1209 TRP A CB    1 
ATOM   8938  C  CG    . TRP A  1  1211 ? -1.598  71.347  111.658 1.00 19.93 ? 1209 TRP A CG    1 
ATOM   8939  C  CD1   . TRP A  1  1211 ? -0.990  71.290  112.893 1.00 20.74 ? 1209 TRP A CD1   1 
ATOM   8940  C  CD2   . TRP A  1  1211 ? -2.899  70.774  111.828 1.00 19.90 ? 1209 TRP A CD2   1 
ATOM   8941  N  NE1   . TRP A  1  1211 ? -1.848  70.731  113.816 1.00 22.81 ? 1209 TRP A NE1   1 
ATOM   8942  C  CE2   . TRP A  1  1211 ? -3.024  70.409  113.186 1.00 19.26 ? 1209 TRP A CE2   1 
ATOM   8943  C  CE3   . TRP A  1  1211 ? -3.984  70.544  110.964 1.00 19.79 ? 1209 TRP A CE3   1 
ATOM   8944  C  CZ2   . TRP A  1  1211 ? -4.181  69.825  113.704 1.00 22.89 ? 1209 TRP A CZ2   1 
ATOM   8945  C  CZ3   . TRP A  1  1211 ? -5.138  69.962  111.489 1.00 22.45 ? 1209 TRP A CZ3   1 
ATOM   8946  C  CH2   . TRP A  1  1211 ? -5.224  69.616  112.841 1.00 22.14 ? 1209 TRP A CH2   1 
ATOM   8947  N  N     . LEU A  1  1212 ? 0.653   70.229  107.685 1.00 17.18 ? 1210 LEU A N     1 
ATOM   8948  C  CA    . LEU A  1  1212 ? 1.587   70.412  106.588 1.00 16.23 ? 1210 LEU A CA    1 
ATOM   8949  C  C     . LEU A  1  1212 ? 1.139   69.695  105.318 1.00 16.36 ? 1210 LEU A C     1 
ATOM   8950  O  O     . LEU A  1  1212 ? 1.858   69.722  104.315 1.00 17.39 ? 1210 LEU A O     1 
ATOM   8951  C  CB    . LEU A  1  1212 ? 2.984   69.933  107.010 1.00 16.75 ? 1210 LEU A CB    1 
ATOM   8952  C  CG    . LEU A  1  1212 ? 3.653   70.920  107.959 1.00 17.49 ? 1210 LEU A CG    1 
ATOM   8953  C  CD1   . LEU A  1  1212 ? 4.799   70.253  108.727 1.00 18.57 ? 1210 LEU A CD1   1 
ATOM   8954  C  CD2   . LEU A  1  1212 ? 4.162   72.147  107.173 1.00 18.96 ? 1210 LEU A CD2   1 
ATOM   8955  N  N     . VAL A  1  1213 ? -0.025  69.053  105.343 1.00 17.80 ? 1211 VAL A N     1 
ATOM   8956  C  CA    . VAL A  1  1213 ? -0.639  68.501  104.145 1.00 17.23 ? 1211 VAL A CA    1 
ATOM   8957  C  C     . VAL A  1  1213 ? -1.899  69.288  103.871 1.00 17.20 ? 1211 VAL A C     1 
ATOM   8958  O  O     . VAL A  1  1213 ? -2.453  69.966  104.745 1.00 18.78 ? 1211 VAL A O     1 
ATOM   8959  C  CB    . VAL A  1  1213 ? -0.975  66.996  104.256 1.00 17.51 ? 1211 VAL A CB    1 
ATOM   8960  C  CG1   . VAL A  1  1213 ? 0.293   66.164  104.306 1.00 20.32 ? 1211 VAL A CG1   1 
ATOM   8961  C  CG2   . VAL A  1  1213 ? -1.868  66.722  105.467 1.00 17.74 ? 1211 VAL A CG2   1 
ATOM   8962  N  N     . GLU A  1  1214 ? -2.364  69.173  102.638 1.00 17.18 ? 1212 GLU A N     1 
ATOM   8963  C  CA    . GLU A  1  1214 ? -3.564  69.847  102.178 1.00 21.20 ? 1212 GLU A CA    1 
ATOM   8964  C  C     . GLU A  1  1214 ? -4.601  68.789  101.852 1.00 16.82 ? 1212 GLU A C     1 
ATOM   8965  O  O     . GLU A  1  1214 ? -4.312  67.838  101.119 1.00 17.60 ? 1212 GLU A O     1 
ATOM   8966  C  CB    . GLU A  1  1214 ? -3.263  70.693  100.945 1.00 22.60 ? 1212 GLU A CB    1 
ATOM   8967  C  CG    . GLU A  1  1214 ? -4.479  71.355  100.341 1.00 34.32 ? 1212 GLU A CG    1 
ATOM   8968  C  CD    . GLU A  1  1214 ? -4.131  72.108  99.076  1.00 32.48 ? 1212 GLU A CD    1 
ATOM   8969  O  OE1   . GLU A  1  1214 ? -3.122  72.845  99.095  1.00 41.62 ? 1212 GLU A OE1   1 
ATOM   8970  O  OE2   . GLU A  1  1214 ? -4.852  71.954  98.069  1.00 50.92 ? 1212 GLU A OE2   1 
ATOM   8971  N  N     . GLU A  1  1215 ? -5.798  68.954  102.402 1.00 17.17 ? 1213 GLU A N     1 
ATOM   8972  C  CA    . GLU A  1  1215 ? -6.886  68.039  102.110 1.00 15.78 ? 1213 GLU A CA    1 
ATOM   8973  C  C     . GLU A  1  1215 ? -7.568  68.450  100.821 1.00 16.69 ? 1213 GLU A C     1 
ATOM   8974  O  O     . GLU A  1  1215 ? -7.801  69.636  100.579 1.00 17.74 ? 1213 GLU A O     1 
ATOM   8975  C  CB    . GLU A  1  1215 ? -7.918  68.066  103.226 1.00 16.23 ? 1213 GLU A CB    1 
ATOM   8976  C  CG    . GLU A  1  1215 ? -7.381  67.698  104.587 1.00 17.10 ? 1213 GLU A CG    1 
ATOM   8977  C  CD    . GLU A  1  1215 ? -8.369  68.060  105.666 1.00 18.73 ? 1213 GLU A CD    1 
ATOM   8978  O  OE1   . GLU A  1  1215 ? -8.376  69.237  106.067 1.00 19.32 ? 1213 GLU A OE1   1 
ATOM   8979  O  OE2   . GLU A  1  1215 ? -9.163  67.188  106.069 1.00 19.44 ? 1213 GLU A OE2   1 
ATOM   8980  N  N     . VAL A  1  1216 ? -7.914  67.462  100.007 1.00 16.01 ? 1214 VAL A N     1 
ATOM   8981  C  CA    . VAL A  1  1216 ? -8.682  67.706  98.794  1.00 15.93 ? 1214 VAL A CA    1 
ATOM   8982  C  C     . VAL A  1  1216 ? -9.838  66.725  98.755  1.00 16.63 ? 1214 VAL A C     1 
ATOM   8983  O  O     . VAL A  1  1216 ? -9.648  65.515  98.921  1.00 16.03 ? 1214 VAL A O     1 
ATOM   8984  C  CB    . VAL A  1  1216 ? -7.819  67.574  97.530  1.00 17.10 ? 1214 VAL A CB    1 
ATOM   8985  C  CG1   . VAL A  1  1216 ? -8.683  67.704  96.278  1.00 18.10 ? 1214 VAL A CG1   1 
ATOM   8986  C  CG2   . VAL A  1  1216 ? -6.729  68.642  97.541  1.00 17.01 ? 1214 VAL A CG2   1 
ATOM   8987  N  N     . SER A  1  1217 ? -11.028 67.251  98.537  1.00 17.24 ? 1215 SER A N     1 
ATOM   8988  C  CA    . SER A  1  1217 ? -12.224 66.449  98.368  1.00 15.61 ? 1215 SER A CA    1 
ATOM   8989  C  C     . SER A  1  1217 ? -12.611 66.512  96.905  1.00 15.74 ? 1215 SER A C     1 
ATOM   8990  O  O     . SER A  1  1217 ? -12.547 67.577  96.293  1.00 16.96 ? 1215 SER A O     1 
ATOM   8991  C  CB    . SER A  1  1217 ? -13.362 66.996  99.210  1.00 18.66 ? 1215 SER A CB    1 
ATOM   8992  O  OG    . SER A  1  1217 ? -14.613 66.476  98.808  1.00 21.10 ? 1215 SER A OG    1 
ATOM   8993  N  N     . ALA A  1  1218 ? -12.973 65.370  96.346  1.00 14.47 ? 1216 ALA A N     1 
ATOM   8994  C  CA    . ALA A  1  1218 ? -13.463 65.336  94.973  1.00 15.26 ? 1216 ALA A CA    1 
ATOM   8995  C  C     . ALA A  1  1218 ? -14.735 64.509  94.937  1.00 16.88 ? 1216 ALA A C     1 
ATOM   8996  O  O     . ALA A  1  1218 ? -14.762 63.381  95.424  1.00 18.57 ? 1216 ALA A O     1 
ATOM   8997  C  CB    . ALA A  1  1218 ? -12.417 64.758  94.023  1.00 16.84 ? 1216 ALA A CB    1 
ATOM   8998  N  N     . SER A  1  1219 ? -15.786 65.070  94.363  1.00 16.38 ? 1217 SER A N     1 
ATOM   8999  C  CA    . SER A  1  1219 ? -17.071 64.398  94.248  1.00 16.77 ? 1217 SER A CA    1 
ATOM   9000  C  C     . SER A  1  1219 ? -17.383 64.240  92.772  1.00 15.35 ? 1217 SER A C     1 
ATOM   9001  O  O     . SER A  1  1219 ? -17.553 65.238  92.070  1.00 16.10 ? 1217 SER A O     1 
ATOM   9002  C  CB    . SER A  1  1219 ? -18.166 65.204  94.945  1.00 18.99 ? 1217 SER A CB    1 
ATOM   9003  O  OG    . SER A  1  1219 ? -19.424 64.565  94.815  1.00 17.29 ? 1217 SER A OG    1 
ATOM   9004  N  N     . ILE A  1  1220 ? -17.461 62.999  92.315  1.00 15.19 ? 1218 ILE A N     1 
ATOM   9005  C  CA    . ILE A  1  1220 ? -17.659 62.672  90.905  1.00 15.99 ? 1218 ILE A CA    1 
ATOM   9006  C  C     . ILE A  1  1220 ? -19.053 62.084  90.745  1.00 15.65 ? 1218 ILE A C     1 
ATOM   9007  O  O     . ILE A  1  1220 ? -19.382 61.079  91.377  1.00 16.27 ? 1218 ILE A O     1 
ATOM   9008  C  CB    . ILE A  1  1220 ? -16.600 61.682  90.407  1.00 19.40 ? 1218 ILE A CB    1 
ATOM   9009  C  CG1   . ILE A  1  1220 ? -15.202 62.250  90.642  1.00 22.97 ? 1218 ILE A CG1   1 
ATOM   9010  C  CG2   . ILE A  1  1220 ? -16.830 61.386  88.942  1.00 22.64 ? 1218 ILE A CG2   1 
ATOM   9011  C  CD1   . ILE A  1  1220 ? -14.275 61.279  91.328  1.00 36.17 ? 1218 ILE A CD1   1 
ATOM   9012  N  N     . ASN A  1  1221 ? -19.872 62.708  89.905  1.00 16.87 ? 1219 ASN A N     1 
ATOM   9013  C  CA    . ASN A  1  1221 ? -21.196 62.179  89.584  1.00 16.00 ? 1219 ASN A CA    1 
ATOM   9014  C  C     . ASN A  1  1221 ? -21.004 61.046  88.585  1.00 17.32 ? 1219 ASN A C     1 
ATOM   9015  O  O     . ASN A  1  1221 ? -20.726 61.280  87.413  1.00 20.70 ? 1219 ASN A O     1 
ATOM   9016  C  CB    . ASN A  1  1221 ? -22.077 63.285  89.017  1.00 18.00 ? 1219 ASN A CB    1 
ATOM   9017  C  CG    . ASN A  1  1221 ? -23.413 62.771  88.527  1.00 17.45 ? 1219 ASN A CG    1 
ATOM   9018  O  OD1   . ASN A  1  1221 ? -23.799 61.635  88.789  1.00 18.07 ? 1219 ASN A OD1   1 
ATOM   9019  N  ND2   . ASN A  1  1221 ? -24.144 63.628  87.825  1.00 19.30 ? 1219 ASN A ND2   1 
ATOM   9020  N  N     . THR A  1  1222 ? -21.139 59.811  89.046  1.00 16.08 ? 1220 THR A N     1 
ATOM   9021  C  CA    . THR A  1  1222 ? -20.909 58.664  88.184  1.00 18.17 ? 1220 THR A CA    1 
ATOM   9022  C  C     . THR A  1  1222 ? -22.181 58.202  87.501  1.00 20.63 ? 1220 THR A C     1 
ATOM   9023  O  O     . THR A  1  1222 ? -22.148 57.225  86.750  1.00 26.79 ? 1220 THR A O     1 
ATOM   9024  C  CB    . THR A  1  1222 ? -20.288 57.514  88.979  1.00 20.99 ? 1220 THR A CB    1 
ATOM   9025  O  OG1   . THR A  1  1222 ? -21.170 57.116  90.038  1.00 21.37 ? 1220 THR A OG1   1 
ATOM   9026  C  CG2   . THR A  1  1222 ? -18.932 57.928  89.544  1.00 20.54 ? 1220 THR A CG2   1 
ATOM   9027  N  N     . ALA A  1  1223 ? -23.290 58.883  87.740  1.00 17.30 ? 1221 ALA A N     1 
ATOM   9028  C  CA    . ALA A  1  1223 ? -24.507 58.643  86.990  1.00 23.55 ? 1221 ALA A CA    1 
ATOM   9029  C  C     . ALA A  1  1223 ? -24.629 59.565  85.788  1.00 29.50 ? 1221 ALA A C     1 
ATOM   9030  O  O     . ALA A  1  1223 ? -25.642 59.509  85.086  1.00 32.59 ? 1221 ALA A O     1 
ATOM   9031  C  CB    . ALA A  1  1223 ? -25.726 58.813  87.904  1.00 23.10 ? 1221 ALA A CB    1 
ATOM   9032  N  N     . ALA A  1  1224 ? -23.613 60.403  85.536  1.00 30.02 ? 1222 ALA A N     1 
ATOM   9033  C  CA    . ALA A  1  1224 ? -23.759 61.507  84.594  1.00 33.03 ? 1222 ALA A CA    1 
ATOM   9034  C  C     . ALA A  1  1224 ? -24.031 61.021  83.177  1.00 35.42 ? 1222 ALA A C     1 
ATOM   9035  O  O     . ALA A  1  1224 ? -24.742 61.694  82.424  1.00 38.03 ? 1222 ALA A O     1 
ATOM   9036  C  CB    . ALA A  1  1224 ? -22.511 62.390  84.622  1.00 32.26 ? 1222 ALA A CB    1 
ATOM   9037  N  N     . ALA A  1  1225 ? -23.496 59.858  82.797  1.00 31.87 ? 1223 ALA A N     1 
ATOM   9038  C  CA    . ALA A  1  1225 ? -23.718 59.362  81.442  1.00 35.95 ? 1223 ALA A CA    1 
ATOM   9039  C  C     . ALA A  1  1225 ? -25.158 58.939  81.202  1.00 41.10 ? 1223 ALA A C     1 
ATOM   9040  O  O     . ALA A  1  1225 ? -25.525 58.684  80.051  1.00 41.77 ? 1223 ALA A O     1 
ATOM   9041  C  CB    . ALA A  1  1225 ? -22.785 58.190  81.135  1.00 33.98 ? 1223 ALA A CB    1 
ATOM   9042  N  N     . GLY A  1  1226 ? -25.978 58.868  82.246  1.00 36.25 ? 1224 GLY A N     1 
ATOM   9043  C  CA    . GLY A  1  1226 ? -27.373 58.495  82.103  1.00 34.45 ? 1224 GLY A CA    1 
ATOM   9044  C  C     . GLY A  1  1226 ? -27.786 57.297  82.926  1.00 36.39 ? 1224 GLY A C     1 
ATOM   9045  O  O     . GLY A  1  1226 ? -28.976 56.949  82.926  1.00 36.20 ? 1224 GLY A O     1 
ATOM   9046  N  N     . GLY A  1  1227 ? -26.863 56.646  83.623  1.00 27.30 ? 1225 GLY A N     1 
ATOM   9047  C  CA    . GLY A  1  1227 ? -27.211 55.500  84.443  1.00 32.52 ? 1225 GLY A CA    1 
ATOM   9048  C  C     . GLY A  1  1227 ? -26.086 55.161  85.394  1.00 33.17 ? 1225 GLY A C     1 
ATOM   9049  O  O     . GLY A  1  1227 ? -24.991 55.728  85.330  1.00 31.46 ? 1225 GLY A O     1 
ATOM   9050  N  N     . ASN A  1  1228 ? -26.374 54.202  86.272  1.00 26.78 ? 1226 ASN A N     1 
ATOM   9051  C  CA    . ASN A  1  1228 ? -25.470 53.779  87.336  1.00 32.75 ? 1226 ASN A CA    1 
ATOM   9052  C  C     . ASN A  1  1228 ? -24.973 52.365  87.030  1.00 36.34 ? 1226 ASN A C     1 
ATOM   9053  O  O     . ASN A  1  1228 ? -25.740 51.397  87.108  1.00 34.54 ? 1226 ASN A O     1 
ATOM   9054  C  CB    . ASN A  1  1228 ? -26.192 53.846  88.681  1.00 34.93 ? 1226 ASN A CB    1 
ATOM   9055  C  CG    . ASN A  1  1228 ? -25.282 53.567  89.864  1.00 37.17 ? 1226 ASN A CG    1 
ATOM   9056  O  OD1   . ASN A  1  1228 ? -24.387 52.718  89.804  1.00 37.50 ? 1226 ASN A OD1   1 
ATOM   9057  N  ND2   . ASN A  1  1228 ? -25.529 54.273  90.966  1.00 34.27 ? 1226 ASN A ND2   1 
ATOM   9058  N  N     . ALA A  1  1229 ? -23.683 52.244  86.705  1.00 31.94 ? 1227 ALA A N     1 
ATOM   9059  C  CA    . ALA A  1  1229 ? -23.137 50.943  86.322  1.00 30.15 ? 1227 ALA A CA    1 
ATOM   9060  C  C     . ALA A  1  1229 ? -23.148 49.966  87.493  1.00 33.30 ? 1227 ALA A C     1 
ATOM   9061  O  O     . ALA A  1  1229 ? -23.489 48.790  87.321  1.00 37.05 ? 1227 ALA A O     1 
ATOM   9062  C  CB    . ALA A  1  1229 ? -21.720 51.115  85.769  1.00 32.76 ? 1227 ALA A CB    1 
ATOM   9063  N  N     . SER A  1  1230 ? -22.783 50.432  88.692  1.00 34.19 ? 1228 SER A N     1 
ATOM   9064  C  CA    . SER A  1  1230 ? -22.792 49.558  89.864  1.00 39.01 ? 1228 SER A CA    1 
ATOM   9065  C  C     . SER A  1  1230 ? -24.185 49.001  90.142  1.00 44.15 ? 1228 SER A C     1 
ATOM   9066  O  O     . SER A  1  1230 ? -24.335 47.822  90.490  1.00 44.11 ? 1228 SER A O     1 
ATOM   9067  C  CB    . SER A  1  1230 ? -22.271 50.313  91.086  1.00 43.98 ? 1228 SER A CB    1 
ATOM   9068  O  OG    . SER A  1  1230 ? -20.885 50.565  90.962  1.00 53.72 ? 1228 SER A OG    1 
ATOM   9069  N  N     . LEU A  1  1231 ? -25.218 49.825  89.988  1.00 35.33 ? 1229 LEU A N     1 
ATOM   9070  C  CA    . LEU A  1  1231 ? -26.569 49.372  90.288  1.00 38.61 ? 1229 LEU A CA    1 
ATOM   9071  C  C     . LEU A  1  1231 ? -27.174 48.523  89.176  1.00 44.08 ? 1229 LEU A C     1 
ATOM   9072  O  O     . LEU A  1  1231 ? -28.243 47.932  89.383  1.00 49.73 ? 1229 LEU A O     1 
ATOM   9073  C  CB    . LEU A  1  1231 ? -27.466 50.573  90.593  1.00 39.93 ? 1229 LEU A CB    1 
ATOM   9074  C  CG    . LEU A  1  1231 ? -27.684 50.865  92.083  1.00 38.16 ? 1229 LEU A CG    1 
ATOM   9075  C  CD1   . LEU A  1  1231 ? -26.372 50.900  92.843  1.00 46.34 ? 1229 LEU A CD1   1 
ATOM   9076  C  CD2   . LEU A  1  1231 ? -28.429 52.169  92.260  1.00 32.54 ? 1229 LEU A CD2   1 
ATOM   9077  N  N     . MET A  1  1232 ? -26.521 48.432  88.014  1.00 43.14 ? 1230 MET A N     1 
ATOM   9078  C  CA    . MET A  1  1232 ? -26.945 47.463  87.009  1.00 43.65 ? 1230 MET A CA    1 
ATOM   9079  C  C     . MET A  1  1232 ? -26.787 46.030  87.503  1.00 42.22 ? 1230 MET A C     1 
ATOM   9080  O  O     . MET A  1  1232 ? -27.447 45.125  86.979  1.00 42.02 ? 1230 MET A O     1 
ATOM   9081  C  CB    . MET A  1  1232 ? -26.152 47.656  85.712  1.00 38.67 ? 1230 MET A CB    1 
ATOM   9082  C  CG    . MET A  1  1232 ? -26.517 48.917  84.944  1.00 39.69 ? 1230 MET A CG    1 
ATOM   9083  S  SD    . MET A  1  1232 ? -25.459 49.151  83.494  1.00 54.10 ? 1230 MET A SD    1 
ATOM   9084  C  CE    . MET A  1  1232 ? -25.945 47.754  82.463  1.00 48.72 ? 1230 MET A CE    1 
ATOM   9085  N  N     . ALA A  1  1233 ? -25.928 45.807  88.496  1.00 46.18 ? 1231 ALA A N     1 
ATOM   9086  C  CA    . ALA A  1  1233 ? -25.718 44.493  89.087  1.00 52.32 ? 1231 ALA A CA    1 
ATOM   9087  C  C     . ALA A  1  1233 ? -26.591 44.251  90.311  1.00 54.74 ? 1231 ALA A C     1 
ATOM   9088  O  O     . ALA A  1  1233 ? -26.426 43.226  90.983  1.00 60.33 ? 1231 ALA A O     1 
ATOM   9089  C  CB    . ALA A  1  1233 ? -24.245 44.312  89.462  1.00 46.22 ? 1231 ALA A CB    1 
ATOM   9090  N  N     . ILE A  1  1234 ? -27.510 45.163  90.614  1.00 53.83 ? 1232 ILE A N     1 
ATOM   9091  C  CA    . ILE A  1  1234 ? -28.358 45.070  91.796  1.00 52.80 ? 1232 ILE A CA    1 
ATOM   9092  C  C     . ILE A  1  1234 ? -29.786 44.824  91.328  1.00 51.75 ? 1232 ILE A C     1 
ATOM   9093  O  O     . ILE A  1  1234 ? -30.428 45.705  90.739  1.00 42.08 ? 1232 ILE A O     1 
ATOM   9094  C  CB    . ILE A  1  1234 ? -28.255 46.325  92.675  1.00 44.58 ? 1232 ILE A CB    1 
ATOM   9095  C  CG1   . ILE A  1  1234 ? -26.818 46.473  93.189  1.00 48.98 ? 1232 ILE A CG1   1 
ATOM   9096  C  CG2   . ILE A  1  1234 ? -29.243 46.251  93.823  1.00 38.24 ? 1232 ILE A CG2   1 
ATOM   9097  C  CD1   . ILE A  1  1234 ? -26.676 47.306  94.442  1.00 41.56 ? 1232 ILE A CD1   1 
ATOM   9098  N  N     . GLY A  1  1235 ? -30.273 43.616  91.577  1.00 46.67 ? 1233 GLY A N     1 
ATOM   9099  C  CA    . GLY A  1  1235 ? -31.635 43.253  91.251  1.00 40.39 ? 1233 GLY A CA    1 
ATOM   9100  C  C     . GLY A  1  1235 ? -32.201 42.382  92.348  1.00 42.12 ? 1233 GLY A C     1 
ATOM   9101  O  O     . GLY A  1  1235 ? -33.368 42.478  92.684  1.00 29.84 ? 1233 GLY A O     1 
ATOM   9102  O  OXT   . GLY A  1  1235 ? -31.496 41.560  92.935  1.00 40.94 ? 1233 GLY A OXT   1 
ATOM   9103  N  N     . ALA B  1  16   ? 30.198  4.807   80.996  1.00 49.47 ? 14   ALA B N     1 
ATOM   9104  C  CA    . ALA B  1  16   ? 29.233  5.853   81.325  1.00 52.21 ? 14   ALA B CA    1 
ATOM   9105  C  C     . ALA B  1  16   ? 27.819  5.293   81.398  1.00 49.49 ? 14   ALA B C     1 
ATOM   9106  O  O     . ALA B  1  16   ? 27.457  4.417   80.614  1.00 51.38 ? 14   ALA B O     1 
ATOM   9107  C  CB    . ALA B  1  16   ? 29.300  6.986   80.303  1.00 42.37 ? 14   ALA B CB    1 
ATOM   9108  N  N     . PRO B  1  17   ? 27.020  5.789   82.340  1.00 45.72 ? 15   PRO B N     1 
ATOM   9109  C  CA    . PRO B  1  17   ? 25.615  5.371   82.401  1.00 39.14 ? 15   PRO B CA    1 
ATOM   9110  C  C     . PRO B  1  17   ? 24.875  5.818   81.149  1.00 39.22 ? 15   PRO B C     1 
ATOM   9111  O  O     . PRO B  1  17   ? 25.067  6.935   80.663  1.00 42.90 ? 15   PRO B O     1 
ATOM   9112  C  CB    . PRO B  1  17   ? 25.083  6.074   83.656  1.00 44.80 ? 15   PRO B CB    1 
ATOM   9113  C  CG    . PRO B  1  17   ? 26.304  6.489   84.429  1.00 51.26 ? 15   PRO B CG    1 
ATOM   9114  C  CD    . PRO B  1  17   ? 27.368  6.736   83.412  1.00 47.08 ? 15   PRO B CD    1 
ATOM   9115  N  N     . ALA B  1  18   ? 24.042  4.924   80.618  1.00 34.59 ? 16   ALA B N     1 
ATOM   9116  C  CA    . ALA B  1  18   ? 23.268  5.245   79.428  1.00 31.99 ? 16   ALA B CA    1 
ATOM   9117  C  C     . ALA B  1  18   ? 22.337  6.418   79.718  1.00 31.35 ? 16   ALA B C     1 
ATOM   9118  O  O     . ALA B  1  18   ? 21.799  6.526   80.826  1.00 29.91 ? 16   ALA B O     1 
ATOM   9119  C  CB    . ALA B  1  18   ? 22.446  4.045   78.969  1.00 33.02 ? 16   ALA B CB    1 
ATOM   9120  N  N     . PRO B  1  19   ? 22.136  7.317   78.761  1.00 28.11 ? 17   PRO B N     1 
ATOM   9121  C  CA    . PRO B  1  19   ? 21.260  8.467   79.015  1.00 28.15 ? 17   PRO B CA    1 
ATOM   9122  C  C     . PRO B  1  19   ? 19.861  8.023   79.423  1.00 27.77 ? 17   PRO B C     1 
ATOM   9123  O  O     . PRO B  1  19   ? 19.248  7.163   78.783  1.00 27.75 ? 17   PRO B O     1 
ATOM   9124  C  CB    . PRO B  1  19   ? 21.260  9.209   77.673  1.00 27.85 ? 17   PRO B CB    1 
ATOM   9125  C  CG    . PRO B  1  19   ? 22.587  8.879   77.085  1.00 31.56 ? 17   PRO B CG    1 
ATOM   9126  C  CD    . PRO B  1  19   ? 22.861  7.449   77.487  1.00 31.38 ? 17   PRO B CD    1 
ATOM   9127  N  N     . PHE B  1  20   ? 19.380  8.598   80.522  1.00 27.90 ? 18   PHE B N     1 
ATOM   9128  C  CA    . PHE B  1  20   ? 18.023  8.435   81.038  1.00 25.08 ? 18   PHE B CA    1 
ATOM   9129  C  C     . PHE B  1  20   ? 17.716  7.013   81.476  1.00 29.06 ? 18   PHE B C     1 
ATOM   9130  O  O     . PHE B  1  20   ? 16.547  6.675   81.678  1.00 29.12 ? 18   PHE B O     1 
ATOM   9131  C  CB    . PHE B  1  20   ? 16.984  8.900   80.019  1.00 25.85 ? 18   PHE B CB    1 
ATOM   9132  C  CG    . PHE B  1  20   ? 17.179  10.313  79.584  1.00 24.47 ? 18   PHE B CG    1 
ATOM   9133  C  CD1   . PHE B  1  20   ? 16.841  11.357  80.431  1.00 22.63 ? 18   PHE B CD1   1 
ATOM   9134  C  CD2   . PHE B  1  20   ? 17.719  10.599  78.343  1.00 22.40 ? 18   PHE B CD2   1 
ATOM   9135  C  CE1   . PHE B  1  20   ? 17.018  12.676  80.035  1.00 25.09 ? 18   PHE B CE1   1 
ATOM   9136  C  CE2   . PHE B  1  20   ? 17.895  11.908  77.942  1.00 23.95 ? 18   PHE B CE2   1 
ATOM   9137  C  CZ    . PHE B  1  20   ? 17.552  12.945  78.789  1.00 25.43 ? 18   PHE B CZ    1 
ATOM   9138  N  N     . ALA B  1  21   ? 18.742  6.176   81.633  1.00 31.88 ? 19   ALA B N     1 
ATOM   9139  C  CA    . ALA B  1  21   ? 18.529  4.798   82.065  1.00 33.83 ? 19   ALA B CA    1 
ATOM   9140  C  C     . ALA B  1  21   ? 17.906  4.721   83.457  1.00 33.30 ? 19   ALA B C     1 
ATOM   9141  O  O     . ALA B  1  21   ? 17.228  3.737   83.776  1.00 35.97 ? 19   ALA B O     1 
ATOM   9142  C  CB    . ALA B  1  21   ? 19.859  4.044   82.035  1.00 36.71 ? 19   ALA B CB    1 
ATOM   9143  N  N     . ASP B  1  22   ? 18.113  5.737   84.292  1.00 28.16 ? 20   ASP B N     1 
ATOM   9144  C  CA    . ASP B  1  22   ? 17.582  5.755   85.656  1.00 27.75 ? 20   ASP B CA    1 
ATOM   9145  C  C     . ASP B  1  22   ? 16.865  7.069   85.920  1.00 24.44 ? 20   ASP B C     1 
ATOM   9146  O  O     . ASP B  1  22   ? 17.004  7.688   86.978  1.00 28.37 ? 20   ASP B O     1 
ATOM   9147  C  CB    . ASP B  1  22   ? 18.694  5.530   86.677  1.00 34.67 ? 20   ASP B CB    1 
ATOM   9148  N  N     . PHE B  1  23   ? 16.065  7.505   84.946  1.00 21.72 ? 21   PHE B N     1 
ATOM   9149  C  CA    . PHE B  1  23   ? 15.507  8.852   85.011  1.00 22.80 ? 21   PHE B CA    1 
ATOM   9150  C  C     . PHE B  1  23   ? 14.550  9.004   86.185  1.00 21.73 ? 21   PHE B C     1 
ATOM   9151  O  O     . PHE B  1  23   ? 14.717  9.899   87.023  1.00 21.88 ? 21   PHE B O     1 
ATOM   9152  C  CB    . PHE B  1  23   ? 14.794  9.200   83.707  1.00 22.26 ? 21   PHE B CB    1 
ATOM   9153  C  CG    . PHE B  1  23   ? 14.086  10.503  83.772  1.00 23.68 ? 21   PHE B CG    1 
ATOM   9154  C  CD1   . PHE B  1  23   ? 14.802  11.673  83.961  1.00 20.76 ? 21   PHE B CD1   1 
ATOM   9155  C  CD2   . PHE B  1  23   ? 12.701  10.562  83.680  1.00 21.94 ? 21   PHE B CD2   1 
ATOM   9156  C  CE1   . PHE B  1  23   ? 14.143  12.910  84.058  1.00 19.74 ? 21   PHE B CE1   1 
ATOM   9157  C  CE2   . PHE B  1  23   ? 12.041  11.785  83.765  1.00 25.00 ? 21   PHE B CE2   1 
ATOM   9158  C  CZ    . PHE B  1  23   ? 12.765  12.957  83.958  1.00 22.42 ? 21   PHE B CZ    1 
ATOM   9159  N  N     . ALA B  1  24   ? 13.517  8.155   86.242  1.00 21.50 ? 22   ALA B N     1 
ATOM   9160  C  CA    . ALA B  1  24   ? 12.524  8.241   87.310  1.00 21.06 ? 22   ALA B CA    1 
ATOM   9161  C  C     . ALA B  1  24   ? 11.824  6.905   87.525  1.00 21.70 ? 22   ALA B C     1 
ATOM   9162  O  O     . ALA B  1  24   ? 10.599  6.817   87.400  1.00 24.01 ? 22   ALA B O     1 
ATOM   9163  C  CB    . ALA B  1  24   ? 11.491  9.324   87.002  1.00 23.64 ? 22   ALA B CB    1 
ATOM   9164  N  N     . PRO B  1  25   ? 12.555  5.854   87.870  1.00 25.09 ? 23   PRO B N     1 
ATOM   9165  C  CA    . PRO B  1  25   ? 11.912  4.563   88.102  1.00 26.92 ? 23   PRO B CA    1 
ATOM   9166  C  C     . PRO B  1  25   ? 10.947  4.657   89.270  1.00 23.80 ? 23   PRO B C     1 
ATOM   9167  O  O     . PRO B  1  25   ? 11.257  5.285   90.293  1.00 23.49 ? 23   PRO B O     1 
ATOM   9168  C  CB    . PRO B  1  25   ? 13.094  3.636   88.418  1.00 28.57 ? 23   PRO B CB    1 
ATOM   9169  C  CG    . PRO B  1  25   ? 14.115  4.541   89.007  1.00 25.67 ? 23   PRO B CG    1 
ATOM   9170  C  CD    . PRO B  1  25   ? 13.972  5.850   88.267  1.00 24.29 ? 23   PRO B CD    1 
ATOM   9171  N  N     . PRO B  1  26   ? 9.761   4.068   89.155  1.00 22.90 ? 24   PRO B N     1 
ATOM   9172  C  CA    . PRO B  1  26   ? 8.806   4.127   90.264  1.00 25.83 ? 24   PRO B CA    1 
ATOM   9173  C  C     . PRO B  1  26   ? 9.295   3.323   91.458  1.00 25.09 ? 24   PRO B C     1 
ATOM   9174  O  O     . PRO B  1  26   ? 10.094  2.389   91.338  1.00 25.92 ? 24   PRO B O     1 
ATOM   9175  C  CB    . PRO B  1  26   ? 7.531   3.521   89.671  1.00 26.45 ? 24   PRO B CB    1 
ATOM   9176  C  CG    . PRO B  1  26   ? 8.016   2.641   88.572  1.00 27.12 ? 24   PRO B CG    1 
ATOM   9177  C  CD    . PRO B  1  26   ? 9.217   3.342   87.996  1.00 27.54 ? 24   PRO B CD    1 
ATOM   9178  N  N     . VAL B  1  27   ? 8.797   3.709   92.635  1.00 25.73 ? 25   VAL B N     1 
ATOM   9179  C  CA    . VAL B  1  27   ? 9.117   2.967   93.850  1.00 25.10 ? 25   VAL B CA    1 
ATOM   9180  C  C     . VAL B  1  27   ? 8.751   1.495   93.683  1.00 26.46 ? 25   VAL B C     1 
ATOM   9181  O  O     . VAL B  1  27   ? 9.495   0.603   94.109  1.00 27.17 ? 25   VAL B O     1 
ATOM   9182  C  CB    . VAL B  1  27   ? 8.406   3.597   95.062  1.00 24.96 ? 25   VAL B CB    1 
ATOM   9183  C  CG1   . VAL B  1  27   ? 8.614   2.740   96.299  1.00 27.54 ? 25   VAL B CG1   1 
ATOM   9184  C  CG2   . VAL B  1  27   ? 8.929   4.995   95.307  1.00 25.67 ? 25   VAL B CG2   1 
ATOM   9185  N  N     . ARG B  1  28   ? 7.627   1.216   93.032  1.00 25.18 ? 26   ARG B N     1 
ATOM   9186  C  CA    . ARG B  1  28   ? 7.186   -0.157  92.831  1.00 26.74 ? 26   ARG B CA    1 
ATOM   9187  C  C     . ARG B  1  28   ? 6.415   -0.234  91.521  1.00 30.35 ? 26   ARG B C     1 
ATOM   9188  O  O     . ARG B  1  28   ? 5.940   0.789   91.014  1.00 25.65 ? 26   ARG B O     1 
ATOM   9189  C  CB    . ARG B  1  28   ? 6.319   -0.643  94.006  1.00 30.96 ? 26   ARG B CB    1 
ATOM   9190  C  CG    . ARG B  1  28   ? 4.967   0.059   94.112  1.00 29.10 ? 26   ARG B CG    1 
ATOM   9191  C  CD    . ARG B  1  28   ? 4.224   -0.327  95.385  1.00 31.52 ? 26   ARG B CD    1 
ATOM   9192  N  NE    . ARG B  1  28   ? 4.848   0.266   96.563  1.00 33.87 ? 26   ARG B NE    1 
ATOM   9193  C  CZ    . ARG B  1  28   ? 5.602   -0.394  97.432  1.00 43.37 ? 26   ARG B CZ    1 
ATOM   9194  N  NH1   . ARG B  1  28   ? 5.822   -1.695  97.312  1.00 39.76 ? 26   ARG B NH1   1 
ATOM   9195  N  NH2   . ARG B  1  28   ? 6.145   0.266   98.450  1.00 36.25 ? 26   ARG B NH2   1 
ATOM   9196  N  N     . PRO B  1  29   ? 6.305   -1.418  90.927  1.00 29.78 ? 27   PRO B N     1 
ATOM   9197  C  CA    . PRO B  1  29   ? 5.427   -1.559  89.763  1.00 29.78 ? 27   PRO B CA    1 
ATOM   9198  C  C     . PRO B  1  29   ? 4.001   -1.180  90.134  1.00 28.92 ? 27   PRO B C     1 
ATOM   9199  O  O     . PRO B  1  29   ? 3.502   -1.523  91.211  1.00 30.93 ? 27   PRO B O     1 
ATOM   9200  C  CB    . PRO B  1  29   ? 5.546   -3.046  89.398  1.00 30.65 ? 27   PRO B CB    1 
ATOM   9201  C  CG    . PRO B  1  29   ? 6.857   -3.476  90.001  1.00 34.10 ? 27   PRO B CG    1 
ATOM   9202  C  CD    . PRO B  1  29   ? 6.994   -2.677  91.260  1.00 33.35 ? 27   PRO B CD    1 
ATOM   9203  N  N     . GLN B  1  30   ? 3.354   -0.444  89.238  1.00 28.19 ? 28   GLN B N     1 
ATOM   9204  C  CA    . GLN B  1  30   ? 2.048   0.126   89.531  1.00 30.55 ? 28   GLN B CA    1 
ATOM   9205  C  C     . GLN B  1  30   ? 0.968   -0.924  89.310  1.00 28.60 ? 28   GLN B C     1 
ATOM   9206  O  O     . GLN B  1  30   ? 0.793   -1.420  88.190  1.00 29.95 ? 28   GLN B O     1 
ATOM   9207  C  CB    . GLN B  1  30   ? 1.809   1.362   88.663  1.00 29.19 ? 28   GLN B CB    1 
ATOM   9208  C  CG    . GLN B  1  30   ? 2.891   2.433   88.832  1.00 25.25 ? 28   GLN B CG    1 
ATOM   9209  C  CD    . GLN B  1  30   ? 2.861   3.080   90.208  1.00 25.50 ? 28   GLN B CD    1 
ATOM   9210  O  OE1   . GLN B  1  30   ? 1.985   3.892   90.495  1.00 26.47 ? 28   GLN B OE1   1 
ATOM   9211  N  NE2   . GLN B  1  30   ? 3.818   2.720   91.068  1.00 26.08 ? 28   GLN B NE2   1 
ATOM   9212  N  N     . SER B  1  31   ? 0.244   -1.257  90.376  1.00 29.05 ? 29   SER B N     1 
ATOM   9213  C  CA    . SER B  1  31   ? -0.855  -2.202  90.300  1.00 25.82 ? 29   SER B CA    1 
ATOM   9214  C  C     . SER B  1  31   ? -2.011  -1.616  89.496  1.00 29.45 ? 29   SER B C     1 
ATOM   9215  O  O     . SER B  1  31   ? -2.046  -0.427  89.177  1.00 27.61 ? 29   SER B O     1 
ATOM   9216  C  CB    . SER B  1  31   ? -1.349  -2.570  91.695  1.00 29.15 ? 29   SER B CB    1 
ATOM   9217  O  OG    . SER B  1  31   ? -2.021  -1.470  92.295  1.00 28.94 ? 29   SER B OG    1 
ATOM   9218  N  N     . THR B  1  32   ? -2.979  -2.481  89.179  1.00 30.33 ? 30   THR B N     1 
ATOM   9219  C  CA    . THR B  1  32   ? -4.200  -2.022  88.531  1.00 27.67 ? 30   THR B CA    1 
ATOM   9220  C  C     . THR B  1  32   ? -4.858  -0.908  89.341  1.00 28.25 ? 30   THR B C     1 
ATOM   9221  O  O     . THR B  1  32   ? -5.241  0.133   88.794  1.00 30.00 ? 30   THR B O     1 
ATOM   9222  C  CB    . THR B  1  32   ? -5.158  -3.199  88.336  1.00 32.82 ? 30   THR B CB    1 
ATOM   9223  O  OG1   . THR B  1  32   ? -4.571  -4.132  87.421  1.00 38.89 ? 30   THR B OG1   1 
ATOM   9224  C  CG2   . THR B  1  32   ? -6.497  -2.725  87.769  1.00 40.32 ? 30   THR B CG2   1 
ATOM   9225  N  N     . LEU B  1  33   ? -4.957  -1.096  90.659  1.00 28.27 ? 31   LEU B N     1 
ATOM   9226  C  CA    . LEU B  1  33   ? -5.584  -0.087  91.509  1.00 28.71 ? 31   LEU B CA    1 
ATOM   9227  C  C     . LEU B  1  33   ? -4.757  1.190   91.575  1.00 27.98 ? 31   LEU B C     1 
ATOM   9228  O  O     . LEU B  1  33   ? -5.318  2.291   91.590  1.00 28.51 ? 31   LEU B O     1 
ATOM   9229  C  CB    . LEU B  1  33   ? -5.811  -0.654  92.909  1.00 28.42 ? 31   LEU B CB    1 
ATOM   9230  C  CG    . LEU B  1  33   ? -6.888  -1.735  92.901  1.00 32.69 ? 31   LEU B CG    1 
ATOM   9231  C  CD1   . LEU B  1  33   ? -6.934  -2.439  94.233  1.00 33.35 ? 31   LEU B CD1   1 
ATOM   9232  C  CD2   . LEU B  1  33   ? -8.247  -1.144  92.556  1.00 35.47 ? 31   LEU B CD2   1 
ATOM   9233  N  N     . ARG B  1  34   ? -3.426  1.070   91.632  1.00 25.45 ? 32   ARG B N     1 
ATOM   9234  C  CA    . ARG B  1  34   ? -2.593  2.273   91.613  1.00 24.60 ? 32   ARG B CA    1 
ATOM   9235  C  C     . ARG B  1  34   ? -2.716  3.000   90.279  1.00 26.60 ? 32   ARG B C     1 
ATOM   9236  O  O     . ARG B  1  34   ? -2.775  4.235   90.240  1.00 23.34 ? 32   ARG B O     1 
ATOM   9237  C  CB    . ARG B  1  34   ? -1.132  1.930   91.901  1.00 24.49 ? 32   ARG B CB    1 
ATOM   9238  C  CG    . ARG B  1  34   ? -0.866  1.487   93.328  1.00 26.95 ? 32   ARG B CG    1 
ATOM   9239  C  CD    . ARG B  1  34   ? -0.919  2.656   94.309  1.00 26.09 ? 32   ARG B CD    1 
ATOM   9240  N  NE    . ARG B  1  34   ? 0.087   3.668   94.013  1.00 25.40 ? 32   ARG B NE    1 
ATOM   9241  C  CZ    . ARG B  1  34   ? 1.297   3.721   94.557  1.00 27.86 ? 32   ARG B CZ    1 
ATOM   9242  N  NH1   . ARG B  1  34   ? 1.695   2.828   95.453  1.00 25.93 ? 32   ARG B NH1   1 
ATOM   9243  N  NH2   . ARG B  1  34   ? 2.126   4.696   94.196  1.00 24.51 ? 32   ARG B NH2   1 
ATOM   9244  N  N     . ARG B  1  35   ? -2.772  2.255   89.173  1.00 24.21 ? 33   ARG B N     1 
ATOM   9245  C  CA    . ARG B  1  35   ? -2.939  2.904   87.882  1.00 25.26 ? 33   ARG B CA    1 
ATOM   9246  C  C     . ARG B  1  35   ? -4.281  3.612   87.779  1.00 22.10 ? 33   ARG B C     1 
ATOM   9247  O  O     . ARG B  1  35   ? -4.374  4.654   87.123  1.00 24.11 ? 33   ARG B O     1 
ATOM   9248  C  CB    . ARG B  1  35   ? -2.805  1.884   86.752  1.00 26.47 ? 33   ARG B CB    1 
ATOM   9249  C  CG    . ARG B  1  35   ? -1.405  1.377   86.546  1.00 33.36 ? 33   ARG B CG    1 
ATOM   9250  C  CD    . ARG B  1  35   ? -1.335  0.463   85.320  1.00 34.36 ? 33   ARG B CD    1 
ATOM   9251  N  NE    . ARG B  1  35   ? -0.035  -0.189  85.243  1.00 51.66 ? 33   ARG B NE    1 
ATOM   9252  C  CZ    . ARG B  1  35   ? 1.085   0.417   84.870  1.00 56.22 ? 33   ARG B CZ    1 
ATOM   9253  N  NH1   . ARG B  1  35   ? 1.092   1.686   84.491  1.00 54.36 ? 33   ARG B NH1   1 
ATOM   9254  N  NH2   . ARG B  1  35   ? 2.229   -0.263  84.889  1.00 50.76 ? 33   ARG B NH2   1 
ATOM   9255  N  N     . ALA B  1  36   ? -5.328  3.067   88.403  1.00 23.82 ? 34   ALA B N     1 
ATOM   9256  C  CA    . ALA B  1  36   ? -6.626  3.726   88.326  1.00 25.91 ? 34   ALA B CA    1 
ATOM   9257  C  C     . ALA B  1  36   ? -6.602  5.056   89.062  1.00 27.04 ? 34   ALA B C     1 
ATOM   9258  O  O     . ALA B  1  36   ? -7.260  6.013   88.640  1.00 25.17 ? 34   ALA B O     1 
ATOM   9259  C  CB    . ALA B  1  36   ? -7.725  2.818   88.876  1.00 27.52 ? 34   ALA B CB    1 
ATOM   9260  N  N     . ILE B  1  37   ? -5.836  5.137   90.149  1.00 23.27 ? 35   ILE B N     1 
ATOM   9261  C  CA    . ILE B  1  37   ? -5.630  6.413   90.829  1.00 21.87 ? 35   ILE B CA    1 
ATOM   9262  C  C     . ILE B  1  37   ? -4.970  7.410   89.891  1.00 24.74 ? 35   ILE B C     1 
ATOM   9263  O  O     . ILE B  1  37   ? -5.454  8.533   89.703  1.00 22.28 ? 35   ILE B O     1 
ATOM   9264  C  CB    . ILE B  1  37   ? -4.791  6.194   92.100  1.00 20.46 ? 35   ILE B CB    1 
ATOM   9265  C  CG1   . ILE B  1  37   ? -5.583  5.384   93.128  1.00 19.87 ? 35   ILE B CG1   1 
ATOM   9266  C  CG2   . ILE B  1  37   ? -4.278  7.536   92.673  1.00 21.34 ? 35   ILE B CG2   1 
ATOM   9267  C  CD1   . ILE B  1  37   ? -4.689  4.844   94.241  1.00 20.28 ? 35   ILE B CD1   1 
ATOM   9268  N  N     . THR B  1  38   ? -3.842  7.018   89.295  1.00 21.28 ? 36   THR B N     1 
ATOM   9269  C  CA    . THR B  1  38   ? -3.083  7.941   88.461  1.00 21.66 ? 36   THR B CA    1 
ATOM   9270  C  C     . THR B  1  38   ? -3.904  8.407   87.263  1.00 20.77 ? 36   THR B C     1 
ATOM   9271  O  O     . THR B  1  38   ? -3.842  9.581   86.875  1.00 22.19 ? 36   THR B O     1 
ATOM   9272  C  CB    . THR B  1  38   ? -1.780  7.279   88.008  1.00 23.28 ? 36   THR B CB    1 
ATOM   9273  O  OG1   . THR B  1  38   ? -1.078  6.763   89.151  1.00 21.59 ? 36   THR B OG1   1 
ATOM   9274  C  CG2   . THR B  1  38   ? -0.903  8.283   87.276  1.00 21.66 ? 36   THR B CG2   1 
ATOM   9275  N  N     . ALA B  1  39   ? -4.703  7.506   86.691  1.00 21.70 ? 37   ALA B N     1 
ATOM   9276  C  CA    . ALA B  1  39   ? -5.527  7.851   85.536  1.00 22.45 ? 37   ALA B CA    1 
ATOM   9277  C  C     . ALA B  1  39   ? -6.533  8.952   85.838  1.00 25.41 ? 37   ALA B C     1 
ATOM   9278  O  O     . ALA B  1  39   ? -6.952  9.658   84.915  1.00 23.95 ? 37   ALA B O     1 
ATOM   9279  C  CB    . ALA B  1  39   ? -6.255  6.603   85.040  1.00 24.41 ? 37   ALA B CB    1 
ATOM   9280  N  N     . ALA B  1  40   ? -6.926  9.121   87.098  1.00 21.90 ? 38   ALA B N     1 
ATOM   9281  C  CA    . ALA B  1  40   ? -7.912  10.121  87.482  1.00 23.97 ? 38   ALA B CA    1 
ATOM   9282  C  C     . ALA B  1  40   ? -7.293  11.452  87.878  1.00 20.16 ? 38   ALA B C     1 
ATOM   9283  O  O     . ALA B  1  40   ? -8.042  12.388  88.176  1.00 23.20 ? 38   ALA B O     1 
ATOM   9284  C  CB    . ALA B  1  40   ? -8.758  9.602   88.647  1.00 22.86 ? 38   ALA B CB    1 
ATOM   9285  N  N     . TYR B  1  41   ? -5.959  11.553  87.888  1.00 22.12 ? 39   TYR B N     1 
ATOM   9286  C  CA    . TYR B  1  41   ? -5.270  12.678  88.518  1.00 18.88 ? 39   TYR B CA    1 
ATOM   9287  C  C     . TYR B  1  41   ? -5.878  14.013  88.089  1.00 24.13 ? 39   TYR B C     1 
ATOM   9288  O  O     . TYR B  1  41   ? -6.257  14.841  88.930  1.00 20.50 ? 39   TYR B O     1 
ATOM   9289  C  CB    . TYR B  1  41   ? -3.782  12.600  88.148  1.00 18.74 ? 39   TYR B CB    1 
ATOM   9290  C  CG    . TYR B  1  41   ? -2.784  13.295  89.035  1.00 19.42 ? 39   TYR B CG    1 
ATOM   9291  C  CD1   . TYR B  1  41   ? -3.116  14.435  89.771  1.00 20.52 ? 39   TYR B CD1   1 
ATOM   9292  C  CD2   . TYR B  1  41   ? -1.483  12.826  89.111  1.00 21.82 ? 39   TYR B CD2   1 
ATOM   9293  C  CE1   . TYR B  1  41   ? -2.166  15.078  90.560  1.00 18.98 ? 39   TYR B CE1   1 
ATOM   9294  C  CE2   . TYR B  1  41   ? -0.536  13.452  89.895  1.00 20.34 ? 39   TYR B CE2   1 
ATOM   9295  C  CZ    . TYR B  1  41   ? -0.878  14.583  90.617  1.00 20.03 ? 39   TYR B CZ    1 
ATOM   9296  O  OH    . TYR B  1  41   ? 0.077   15.216  91.386  1.00 21.07 ? 39   TYR B OH    1 
ATOM   9297  N  N     . ARG B  1  42   ? -6.030  14.215  86.782  1.00 22.42 ? 40   ARG B N     1 
ATOM   9298  C  CA    . ARG B  1  42   ? -6.539  15.482  86.263  1.00 20.21 ? 40   ARG B CA    1 
ATOM   9299  C  C     . ARG B  1  42   ? -7.725  15.252  85.347  1.00 21.95 ? 40   ARG B C     1 
ATOM   9300  O  O     . ARG B  1  42   ? -7.922  15.966  84.360  1.00 23.09 ? 40   ARG B O     1 
ATOM   9301  C  CB    . ARG B  1  42   ? -5.434  16.263  85.563  1.00 22.21 ? 40   ARG B CB    1 
ATOM   9302  C  CG    . ARG B  1  42   ? -4.433  16.737  86.583  1.00 22.33 ? 40   ARG B CG    1 
ATOM   9303  C  CD    . ARG B  1  42   ? -3.186  17.300  85.991  1.00 22.23 ? 40   ARG B CD    1 
ATOM   9304  N  NE    . ARG B  1  42   ? -2.136  17.204  86.988  1.00 20.19 ? 40   ARG B NE    1 
ATOM   9305  C  CZ    . ARG B  1  42   ? -1.915  18.102  87.941  1.00 21.74 ? 40   ARG B CZ    1 
ATOM   9306  N  NH1   . ARG B  1  42   ? -2.633  19.214  88.029  1.00 22.68 ? 40   ARG B NH1   1 
ATOM   9307  N  NH2   . ARG B  1  42   ? -0.934  17.889  88.816  1.00 20.04 ? 40   ARG B NH2   1 
ATOM   9308  N  N     . ARG B  1  43   ? -8.551  14.275  85.694  1.00 22.21 ? 41   ARG B N     1 
ATOM   9309  C  CA    . ARG B  1  43   ? -9.707  13.932  84.883  1.00 23.79 ? 41   ARG B CA    1 
ATOM   9310  C  C     . ARG B  1  43   ? -10.649 15.130  84.780  1.00 24.86 ? 41   ARG B C     1 
ATOM   9311  O  O     . ARG B  1  43   ? -10.842 15.860  85.759  1.00 23.48 ? 41   ARG B O     1 
ATOM   9312  C  CB    . ARG B  1  43   ? -10.423 12.726  85.500  1.00 22.26 ? 41   ARG B CB    1 
ATOM   9313  C  CG    . ARG B  1  43   ? -11.736 12.307  84.835  1.00 22.51 ? 41   ARG B CG    1 
ATOM   9314  C  CD    . ARG B  1  43   ? -12.112 10.912  85.297  1.00 24.84 ? 41   ARG B CD    1 
ATOM   9315  N  NE    . ARG B  1  43   ? -11.092 9.945   84.906  1.00 27.31 ? 41   ARG B NE    1 
ATOM   9316  C  CZ    . ARG B  1  43   ? -10.813 8.837   85.581  1.00 26.25 ? 41   ARG B CZ    1 
ATOM   9317  N  NH1   . ARG B  1  43   ? -11.452 8.527   86.699  1.00 26.93 ? 41   ARG B NH1   1 
ATOM   9318  N  NH2   . ARG B  1  43   ? -9.867  8.021   85.125  1.00 25.90 ? 41   ARG B NH2   1 
ATOM   9319  N  N     . PRO B  1  44   ? -11.217 15.395  83.609  1.00 23.69 ? 42   PRO B N     1 
ATOM   9320  C  CA    . PRO B  1  44   ? -12.146 16.522  83.493  1.00 22.32 ? 42   PRO B CA    1 
ATOM   9321  C  C     . PRO B  1  44   ? -13.260 16.431  84.526  1.00 22.33 ? 42   PRO B C     1 
ATOM   9322  O  O     . PRO B  1  44   ? -13.758 15.350  84.851  1.00 22.37 ? 42   PRO B O     1 
ATOM   9323  C  CB    . PRO B  1  44   ? -12.679 16.387  82.062  1.00 25.37 ? 42   PRO B CB    1 
ATOM   9324  C  CG    . PRO B  1  44   ? -11.492 15.791  81.322  1.00 28.30 ? 42   PRO B CG    1 
ATOM   9325  C  CD    . PRO B  1  44   ? -10.925 14.782  82.300  1.00 24.73 ? 42   PRO B CD    1 
ATOM   9326  N  N     . GLU B  1  45   ? -13.642 17.600  85.042  1.00 24.06 ? 43   GLU B N     1 
ATOM   9327  C  CA    . GLU B  1  45   ? -14.646 17.671  86.093  1.00 24.72 ? 43   GLU B CA    1 
ATOM   9328  C  C     . GLU B  1  45   ? -15.974 17.076  85.636  1.00 23.46 ? 43   GLU B C     1 
ATOM   9329  O  O     . GLU B  1  45   ? -16.658 16.396  86.407  1.00 26.87 ? 43   GLU B O     1 
ATOM   9330  C  CB    . GLU B  1  45   ? -14.790 19.131  86.529  1.00 29.80 ? 43   GLU B CB    1 
ATOM   9331  C  CG    . GLU B  1  45   ? -15.176 19.281  87.963  1.00 30.69 ? 43   GLU B CG    1 
ATOM   9332  C  CD    . GLU B  1  45   ? -14.654 20.554  88.601  1.00 21.53 ? 43   GLU B CD    1 
ATOM   9333  O  OE1   . GLU B  1  45   ? -13.843 21.288  87.991  1.00 22.49 ? 43   GLU B OE1   1 
ATOM   9334  O  OE2   . GLU B  1  45   ? -15.090 20.800  89.737  1.00 24.62 ? 43   GLU B OE2   1 
ATOM   9335  N  N     . THR B  1  46   ? -16.331 17.280  84.365  1.00 25.20 ? 44   THR B N     1 
ATOM   9336  C  CA    . THR B  1  46   ? -17.569 16.710  83.857  1.00 23.09 ? 44   THR B CA    1 
ATOM   9337  C  C     . THR B  1  46   ? -17.536 15.188  83.799  1.00 25.93 ? 44   THR B C     1 
ATOM   9338  O  O     . THR B  1  46   ? -18.600 14.563  83.791  1.00 28.15 ? 44   THR B O     1 
ATOM   9339  C  CB    . THR B  1  46   ? -17.873 17.260  82.464  1.00 27.90 ? 44   THR B CB    1 
ATOM   9340  O  OG1   . THR B  1  46   ? -16.719 17.088  81.632  1.00 27.07 ? 44   THR B OG1   1 
ATOM   9341  C  CG2   . THR B  1  46   ? -18.230 18.742  82.540  1.00 29.74 ? 44   THR B CG2   1 
ATOM   9342  N  N     . GLU B  1  47   ? -16.354 14.580  83.725  1.00 24.37 ? 45   GLU B N     1 
ATOM   9343  C  CA    . GLU B  1  47   ? -16.293 13.125  83.794  1.00 23.19 ? 45   GLU B CA    1 
ATOM   9344  C  C     . GLU B  1  47   ? -16.280 12.623  85.233  1.00 25.22 ? 45   GLU B C     1 
ATOM   9345  O  O     . GLU B  1  47   ? -16.769 11.520  85.503  1.00 27.81 ? 45   GLU B O     1 
ATOM   9346  C  CB    . GLU B  1  47   ? -15.060 12.612  83.047  1.00 24.36 ? 45   GLU B CB    1 
ATOM   9347  C  CG    . GLU B  1  47   ? -15.051 12.932  81.561  1.00 30.27 ? 45   GLU B CG    1 
ATOM   9348  C  CD    . GLU B  1  47   ? -13.724 12.590  80.916  1.00 37.31 ? 45   GLU B CD    1 
ATOM   9349  O  OE1   . GLU B  1  47   ? -13.014 11.710  81.453  1.00 40.98 ? 45   GLU B OE1   1 
ATOM   9350  O  OE2   . GLU B  1  47   ? -13.386 13.205  79.884  1.00 43.16 ? 45   GLU B OE2   1 
ATOM   9351  N  N     . CYS B  1  48   ? -15.734 13.411  86.167  1.00 24.55 ? 46   CYS B N     1 
ATOM   9352  C  CA    . CYS B  1  48   ? -15.638 12.955  87.552  1.00 25.47 ? 46   CYS B CA    1 
ATOM   9353  C  C     . CYS B  1  48   ? -16.997 12.911  88.226  1.00 26.58 ? 46   CYS B C     1 
ATOM   9354  O  O     . CYS B  1  48   ? -17.270 12.011  89.025  1.00 27.10 ? 46   CYS B O     1 
ATOM   9355  C  CB    . CYS B  1  48   ? -14.720 13.873  88.362  1.00 23.82 ? 46   CYS B CB    1 
ATOM   9356  S  SG    . CYS B  1  48   ? -13.003 13.877  87.898  1.00 25.42 ? 46   CYS B SG    1 
ATOM   9357  N  N     . LEU B  1  49   ? -17.846 13.882  87.941  1.00 26.77 ? 47   LEU B N     1 
ATOM   9358  C  CA    . LEU B  1  49   ? -19.022 14.072  88.781  1.00 26.10 ? 47   LEU B CA    1 
ATOM   9359  C  C     . LEU B  1  49   ? -20.129 13.039  88.604  1.00 25.71 ? 47   LEU B C     1 
ATOM   9360  O  O     . LEU B  1  49   ? -20.740 12.664  89.606  1.00 26.69 ? 47   LEU B O     1 
ATOM   9361  C  CB    . LEU B  1  49   ? -19.592 15.478  88.579  1.00 29.40 ? 47   LEU B CB    1 
ATOM   9362  C  CG    . LEU B  1  49   ? -19.162 16.446  89.694  1.00 26.82 ? 47   LEU B CG    1 
ATOM   9363  C  CD1   . LEU B  1  49   ? -19.726 16.011  91.049  1.00 27.56 ? 47   LEU B CD1   1 
ATOM   9364  C  CD2   . LEU B  1  49   ? -17.637 16.561  89.767  1.00 23.80 ? 47   LEU B CD2   1 
ATOM   9365  N  N     . PRO B  1  50   ? -20.455 12.566  87.400  1.00 29.27 ? 48   PRO B N     1 
ATOM   9366  C  CA    . PRO B  1  50   ? -21.626 11.681  87.272  1.00 29.75 ? 48   PRO B CA    1 
ATOM   9367  C  C     . PRO B  1  50   ? -21.513 10.420  88.116  1.00 30.43 ? 48   PRO B C     1 
ATOM   9368  O  O     . PRO B  1  50   ? -22.498 10.045  88.768  1.00 33.25 ? 48   PRO B O     1 
ATOM   9369  C  CB    . PRO B  1  50   ? -21.675 11.368  85.769  1.00 28.60 ? 48   PRO B CB    1 
ATOM   9370  C  CG    . PRO B  1  50   ? -21.125 12.590  85.149  1.00 28.11 ? 48   PRO B CG    1 
ATOM   9371  C  CD    . PRO B  1  50   ? -19.979 12.998  86.068  1.00 28.26 ? 48   PRO B CD    1 
ATOM   9372  N  N     . PRO B  1  51   ? -20.362 9.728   88.159  1.00 28.14 ? 49   PRO B N     1 
ATOM   9373  C  CA    . PRO B  1  51   ? -20.301 8.553   89.048  1.00 27.84 ? 49   PRO B CA    1 
ATOM   9374  C  C     . PRO B  1  51   ? -20.332 8.911   90.523  1.00 30.15 ? 49   PRO B C     1 
ATOM   9375  O  O     . PRO B  1  51   ? -20.780 8.093   91.334  1.00 29.64 ? 49   PRO B O     1 
ATOM   9376  C  CB    . PRO B  1  51   ? -18.986 7.866   88.656  1.00 33.16 ? 49   PRO B CB    1 
ATOM   9377  C  CG    . PRO B  1  51   ? -18.177 8.921   88.007  1.00 31.55 ? 49   PRO B CG    1 
ATOM   9378  C  CD    . PRO B  1  51   ? -19.147 9.830   87.325  1.00 28.42 ? 49   PRO B CD    1 
ATOM   9379  N  N     . LEU B  1  52   ? -19.874 10.109  90.897  1.00 28.60 ? 50   LEU B N     1 
ATOM   9380  C  CA    . LEU B  1  52   ? -19.997 10.527  92.292  1.00 26.17 ? 50   LEU B CA    1 
ATOM   9381  C  C     . LEU B  1  52   ? -21.447 10.836  92.643  1.00 34.81 ? 50   LEU B C     1 
ATOM   9382  O  O     . LEU B  1  52   ? -21.924 10.470  93.723  1.00 30.87 ? 50   LEU B O     1 
ATOM   9383  C  CB    . LEU B  1  52   ? -19.107 11.741  92.553  1.00 26.57 ? 50   LEU B CB    1 
ATOM   9384  C  CG    . LEU B  1  52   ? -17.603 11.554  92.350  1.00 28.26 ? 50   LEU B CG    1 
ATOM   9385  C  CD1   . LEU B  1  52   ? -16.897 12.903  92.375  1.00 27.46 ? 50   LEU B CD1   1 
ATOM   9386  C  CD2   . LEU B  1  52   ? -17.033 10.625  93.416  1.00 28.95 ? 50   LEU B CD2   1 
ATOM   9387  N  N     . VAL B  1  53   ? -22.163 11.513  91.743  1.00 29.77 ? 51   VAL B N     1 
ATOM   9388  C  CA    . VAL B  1  53   ? -23.588 11.759  91.955  1.00 29.46 ? 51   VAL B CA    1 
ATOM   9389  C  C     . VAL B  1  53   ? -24.316 10.443  92.183  1.00 34.25 ? 51   VAL B C     1 
ATOM   9390  O  O     . VAL B  1  53   ? -25.127 10.312  93.108  1.00 34.18 ? 51   VAL B O     1 
ATOM   9391  C  CB    . VAL B  1  53   ? -24.184 12.529  90.762  1.00 29.98 ? 51   VAL B CB    1 
ATOM   9392  C  CG1   . VAL B  1  53   ? -25.714 12.533  90.838  1.00 33.28 ? 51   VAL B CG1   1 
ATOM   9393  C  CG2   . VAL B  1  53   ? -23.638 13.947  90.731  1.00 29.43 ? 51   VAL B CG2   1 
ATOM   9394  N  N     . GLU B  1  54   ? -24.013 9.439   91.358  1.00 33.17 ? 52   GLU B N     1 
ATOM   9395  C  CA    . GLU B  1  54   ? -24.689 8.152   91.484  1.00 34.08 ? 52   GLU B CA    1 
ATOM   9396  C  C     . GLU B  1  54   ? -24.364 7.491   92.814  1.00 37.83 ? 52   GLU B C     1 
ATOM   9397  O  O     . GLU B  1  54   ? -25.259 6.975   93.494  1.00 35.56 ? 52   GLU B O     1 
ATOM   9398  C  CB    . GLU B  1  54   ? -24.307 7.238   90.320  1.00 38.29 ? 52   GLU B CB    1 
ATOM   9399  N  N     . ALA B  1  55   ? -23.090 7.515   93.213  1.00 32.36 ? 53   ALA B N     1 
ATOM   9400  C  CA    . ALA B  1  55   ? -22.708 6.917   94.488  1.00 35.72 ? 53   ALA B CA    1 
ATOM   9401  C  C     . ALA B  1  55   ? -23.294 7.679   95.674  1.00 34.16 ? 53   ALA B C     1 
ATOM   9402  O  O     . ALA B  1  55   ? -23.598 7.074   96.708  1.00 36.00 ? 53   ALA B O     1 
ATOM   9403  C  CB    . ALA B  1  55   ? -21.184 6.861   94.604  1.00 35.07 ? 53   ALA B CB    1 
ATOM   9404  N  N     . ALA B  1  56   ? -23.460 8.995   95.546  1.00 32.68 ? 54   ALA B N     1 
ATOM   9405  C  CA    . ALA B  1  56   ? -23.944 9.824   96.643  1.00 35.67 ? 54   ALA B CA    1 
ATOM   9406  C  C     . ALA B  1  56   ? -25.458 9.827   96.770  1.00 36.64 ? 54   ALA B C     1 
ATOM   9407  O  O     . ALA B  1  56   ? -25.976 10.348  97.766  1.00 38.54 ? 54   ALA B O     1 
ATOM   9408  C  CB    . ALA B  1  56   ? -23.453 11.260  96.467  1.00 34.07 ? 54   ALA B CB    1 
ATOM   9409  N  N     . THR B  1  57   ? -26.171 9.263   95.797  1.00 35.40 ? 55   THR B N     1 
ATOM   9410  C  CA    . THR B  1  57   ? -27.627 9.318   95.784  1.00 40.99 ? 55   THR B CA    1 
ATOM   9411  C  C     . THR B  1  57   ? -28.217 8.527   96.944  1.00 43.47 ? 55   THR B C     1 
ATOM   9412  O  O     . THR B  1  57   ? -27.788 7.404   97.224  1.00 40.61 ? 55   THR B O     1 
ATOM   9413  C  CB    . THR B  1  57   ? -28.151 8.779   94.455  1.00 38.72 ? 55   THR B CB    1 
ATOM   9414  O  OG1   . THR B  1  57   ? -27.904 9.744   93.430  1.00 39.77 ? 55   THR B OG1   1 
ATOM   9415  C  CG2   . THR B  1  57   ? -29.648 8.494   94.526  1.00 37.35 ? 55   THR B CG2   1 
ATOM   9416  N  N     . GLN B  1  58   ? -29.199 9.124   97.619  1.00 40.86 ? 56   GLN B N     1 
ATOM   9417  C  CA    . GLN B  1  58   ? -29.927 8.480   98.702  1.00 42.32 ? 56   GLN B CA    1 
ATOM   9418  C  C     . GLN B  1  58   ? -31.425 8.587   98.438  1.00 42.33 ? 56   GLN B C     1 
ATOM   9419  O  O     . GLN B  1  58   ? -31.879 9.437   97.669  1.00 44.12 ? 56   GLN B O     1 
ATOM   9420  C  CB    . GLN B  1  58   ? -29.593 9.110   100.056 1.00 43.81 ? 56   GLN B CB    1 
ATOM   9421  C  CG    . GLN B  1  58   ? -28.108 9.285   100.318 1.00 42.02 ? 56   GLN B CG    1 
ATOM   9422  C  CD    . GLN B  1  58   ? -27.803 9.395   101.795 1.00 49.72 ? 56   GLN B CD    1 
ATOM   9423  O  OE1   . GLN B  1  58   ? -27.938 8.425   102.540 1.00 47.91 ? 56   GLN B OE1   1 
ATOM   9424  N  NE2   . GLN B  1  58   ? -27.398 10.582  102.232 1.00 46.30 ? 56   GLN B NE2   1 
ATOM   9425  N  N     . SER B  1  59   ? -32.192 7.717   99.096  1.00 46.35 ? 57   SER B N     1 
ATOM   9426  C  CA    . SER B  1  59   ? -33.642 7.722   98.946  1.00 49.51 ? 57   SER B CA    1 
ATOM   9427  C  C     . SER B  1  59   ? -34.234 9.042   99.432  1.00 50.13 ? 57   SER B C     1 
ATOM   9428  O  O     . SER B  1  59   ? -33.617 9.787   100.194 1.00 46.94 ? 57   SER B O     1 
ATOM   9429  C  CB    . SER B  1  59   ? -34.263 6.574   99.738  1.00 48.80 ? 57   SER B CB    1 
ATOM   9430  O  OG    . SER B  1  59   ? -34.114 6.794   101.134 1.00 47.44 ? 57   SER B OG    1 
ATOM   9431  N  N     . LYS B  1  60   ? -35.462 9.324   98.991  1.00 46.36 ? 58   LYS B N     1 
ATOM   9432  C  CA    . LYS B  1  60   ? -36.146 10.522  99.471  1.00 48.62 ? 58   LYS B CA    1 
ATOM   9433  C  C     . LYS B  1  60   ? -36.379 10.462  100.975 1.00 44.98 ? 58   LYS B C     1 
ATOM   9434  O  O     . LYS B  1  60   ? -36.355 11.498  101.647 1.00 50.15 ? 58   LYS B O     1 
ATOM   9435  C  CB    . LYS B  1  60   ? -37.476 10.712  98.734  1.00 48.11 ? 58   LYS B CB    1 
ATOM   9436  N  N     . GLU B  1  61   ? -36.605 9.265   101.522 1.00 47.68 ? 59   GLU B N     1 
ATOM   9437  C  CA    . GLU B  1  61   ? -36.812 9.137   102.960 1.00 43.77 ? 59   GLU B CA    1 
ATOM   9438  C  C     . GLU B  1  61   ? -35.545 9.499   103.724 1.00 51.60 ? 59   GLU B C     1 
ATOM   9439  O  O     . GLU B  1  61   ? -35.585 10.292  104.672 1.00 48.23 ? 59   GLU B O     1 
ATOM   9440  C  CB    . GLU B  1  61   ? -37.268 7.717   103.307 1.00 49.43 ? 59   GLU B CB    1 
ATOM   9441  N  N     . ILE B  1  62   ? -34.408 8.929   103.320 1.00 47.59 ? 60   ILE B N     1 
ATOM   9442  C  CA    . ILE B  1  62   ? -33.144 9.264   103.969 1.00 44.65 ? 60   ILE B CA    1 
ATOM   9443  C  C     . ILE B  1  62   ? -32.802 10.729  103.730 1.00 40.52 ? 60   ILE B C     1 
ATOM   9444  O  O     . ILE B  1  62   ? -32.398 11.446  104.653 1.00 48.36 ? 60   ILE B O     1 
ATOM   9445  C  CB    . ILE B  1  62   ? -32.027 8.325   103.477 1.00 48.75 ? 60   ILE B CB    1 
ATOM   9446  N  N     . ARG B  1  63   ? -32.981 11.203  102.491 1.00 44.95 ? 61   ARG B N     1 
ATOM   9447  C  CA    . ARG B  1  63   ? -32.747 12.613  102.190 1.00 44.12 ? 61   ARG B CA    1 
ATOM   9448  C  C     . ARG B  1  63   ? -33.601 13.515  103.069 1.00 42.94 ? 61   ARG B C     1 
ATOM   9449  O  O     . ARG B  1  63   ? -33.114 14.520  103.598 1.00 44.68 ? 61   ARG B O     1 
ATOM   9450  C  CB    . ARG B  1  63   ? -33.030 12.897  100.716 1.00 48.04 ? 61   ARG B CB    1 
ATOM   9451  C  CG    . ARG B  1  63   ? -31.916 12.502  99.768  1.00 44.05 ? 61   ARG B CG    1 
ATOM   9452  C  CD    . ARG B  1  63   ? -32.460 12.361  98.353  1.00 52.12 ? 61   ARG B CD    1 
ATOM   9453  N  NE    . ARG B  1  63   ? -33.347 13.462  97.999  1.00 51.65 ? 61   ARG B NE    1 
ATOM   9454  C  CZ    . ARG B  1  63   ? -34.305 13.387  97.085  1.00 54.69 ? 61   ARG B CZ    1 
ATOM   9455  N  NH1   . ARG B  1  63   ? -34.542 12.266  96.422  1.00 50.88 ? 61   ARG B NH1   1 
ATOM   9456  N  NH2   . ARG B  1  63   ? -35.051 14.460  96.839  1.00 60.52 ? 61   ARG B NH2   1 
ATOM   9457  N  N     . ASP B  1  64   ? -34.883 13.187  103.225 1.00 45.76 ? 62   ASP B N     1 
ATOM   9458  C  CA    . ASP B  1  64   ? -35.727 13.986  104.104 1.00 48.53 ? 62   ASP B CA    1 
ATOM   9459  C  C     . ASP B  1  64   ? -35.263 13.879  105.549 1.00 37.53 ? 62   ASP B C     1 
ATOM   9460  O  O     . ASP B  1  64   ? -35.188 14.888  106.257 1.00 40.07 ? 62   ASP B O     1 
ATOM   9461  C  CB    . ASP B  1  64   ? -37.190 13.560  103.969 1.00 45.00 ? 62   ASP B CB    1 
ATOM   9462  C  CG    . ASP B  1  64   ? -37.787 13.934  102.616 1.00 51.38 ? 62   ASP B CG    1 
ATOM   9463  O  OD1   . ASP B  1  64   ? -37.244 14.839  101.951 1.00 51.60 ? 62   ASP B OD1   1 
ATOM   9464  O  OD2   . ASP B  1  64   ? -38.805 13.326  102.221 1.00 51.21 ? 62   ASP B OD2   1 
ATOM   9465  N  N     . ALA B  1  65   ? -34.936 12.664  105.999 1.00 42.85 ? 63   ALA B N     1 
ATOM   9466  C  CA    . ALA B  1  65   ? -34.462 12.478  107.367 1.00 41.62 ? 63   ALA B CA    1 
ATOM   9467  C  C     . ALA B  1  65   ? -33.169 13.246  107.620 1.00 44.69 ? 63   ALA B C     1 
ATOM   9468  O  O     . ALA B  1  65   ? -32.967 13.793  108.711 1.00 48.00 ? 63   ALA B O     1 
ATOM   9469  C  CB    . ALA B  1  65   ? -34.266 10.989  107.655 1.00 46.07 ? 63   ALA B CB    1 
ATOM   9470  N  N     . ALA B  1  66   ? -32.283 13.307  106.620 1.00 44.43 ? 64   ALA B N     1 
ATOM   9471  C  CA    . ALA B  1  66   ? -31.016 14.007  106.799 1.00 43.40 ? 64   ALA B CA    1 
ATOM   9472  C  C     . ALA B  1  66   ? -31.212 15.518  106.829 1.00 42.22 ? 64   ALA B C     1 
ATOM   9473  O  O     . ALA B  1  66   ? -30.554 16.219  107.605 1.00 45.61 ? 64   ALA B O     1 
ATOM   9474  C  CB    . ALA B  1  66   ? -30.040 13.611  105.693 1.00 40.48 ? 64   ALA B CB    1 
ATOM   9475  N  N     . ALA B  1  67   ? -32.114 16.038  105.996 1.00 41.66 ? 65   ALA B N     1 
ATOM   9476  C  CA    . ALA B  1  67   ? -32.377 17.473  106.001 1.00 38.53 ? 65   ALA B CA    1 
ATOM   9477  C  C     . ALA B  1  67   ? -33.004 17.914  107.314 1.00 47.12 ? 65   ALA B C     1 
ATOM   9478  O  O     . ALA B  1  67   ? -32.791 19.052  107.750 1.00 50.68 ? 65   ALA B O     1 
ATOM   9479  C  CB    . ALA B  1  67   ? -33.282 17.850  104.829 1.00 43.09 ? 65   ALA B CB    1 
ATOM   9480  N  N     . SER B  1  68   ? -33.781 17.033  107.950 1.00 48.04 ? 66   SER B N     1 
ATOM   9481  C  CA    . SER B  1  68   ? -34.287 17.329  109.284 1.00 43.42 ? 66   SER B CA    1 
ATOM   9482  C  C     . SER B  1  68   ? -33.151 17.327  110.298 1.00 46.95 ? 66   SER B C     1 
ATOM   9483  O  O     . SER B  1  68   ? -32.997 18.276  111.075 1.00 53.81 ? 66   SER B O     1 
ATOM   9484  C  CB    . SER B  1  68   ? -35.369 16.318  109.674 1.00 51.74 ? 66   SER B CB    1 
ATOM   9485  N  N     . THR B  1  69   ? -32.335 16.269  110.288 1.00 48.66 ? 67   THR B N     1 
ATOM   9486  C  CA    . THR B  1  69   ? -31.196 16.187  111.196 1.00 40.36 ? 67   THR B CA    1 
ATOM   9487  C  C     . THR B  1  69   ? -30.277 17.391  111.045 1.00 42.44 ? 67   THR B C     1 
ATOM   9488  O  O     . THR B  1  69   ? -29.811 17.950  112.043 1.00 46.29 ? 67   THR B O     1 
ATOM   9489  C  CB    . THR B  1  69   ? -30.423 14.889  110.950 1.00 47.57 ? 67   THR B CB    1 
ATOM   9490  O  OG1   . THR B  1  69   ? -31.244 13.768  111.305 1.00 45.76 ? 67   THR B OG1   1 
ATOM   9491  C  CG2   . THR B  1  69   ? -29.127 14.853  111.770 1.00 39.95 ? 67   THR B CG2   1 
ATOM   9492  N  N     . ALA B  1  70   ? -30.006 17.806  109.803 1.00 41.51 ? 68   ALA B N     1 
ATOM   9493  C  CA    . ALA B  1  70   ? -29.151 18.967  109.581 1.00 45.20 ? 68   ALA B CA    1 
ATOM   9494  C  C     . ALA B  1  70   ? -29.788 20.238  110.124 1.00 46.80 ? 68   ALA B C     1 
ATOM   9495  O  O     . ALA B  1  70   ? -29.102 21.082  110.709 1.00 45.62 ? 68   ALA B O     1 
ATOM   9496  C  CB    . ALA B  1  70   ? -28.843 19.119  108.090 1.00 44.08 ? 68   ALA B CB    1 
ATOM   9497  N  N     . ARG B  1  71   ? -31.103 20.395  109.938 1.00 47.84 ? 69   ARG B N     1 
ATOM   9498  C  CA    . ARG B  1  71   ? -31.774 21.603  110.410 1.00 46.90 ? 69   ARG B CA    1 
ATOM   9499  C  C     . ARG B  1  71   ? -31.713 21.711  111.930 1.00 40.27 ? 69   ARG B C     1 
ATOM   9500  O  O     . ARG B  1  71   ? -31.491 22.799  112.473 1.00 48.03 ? 69   ARG B O     1 
ATOM   9501  C  CB    . ARG B  1  71   ? -33.224 21.625  109.926 1.00 52.94 ? 69   ARG B CB    1 
ATOM   9502  C  CG    . ARG B  1  71   ? -34.011 22.816  110.440 1.00 53.62 ? 69   ARG B CG    1 
ATOM   9503  C  CD    . ARG B  1  71   ? -35.429 22.844  109.888 1.00 58.97 ? 69   ARG B CD    1 
ATOM   9504  N  NE    . ARG B  1  71   ? -35.497 23.453  108.565 1.00 54.80 ? 69   ARG B NE    1 
ATOM   9505  C  CZ    . ARG B  1  71   ? -35.474 24.761  108.342 1.00 56.95 ? 69   ARG B CZ    1 
ATOM   9506  N  NH1   . ARG B  1  71   ? -35.343 25.629  109.333 1.00 53.79 ? 69   ARG B NH1   1 
ATOM   9507  N  NH2   . ARG B  1  71   ? -35.583 25.209  107.094 1.00 58.63 ? 69   ARG B NH2   1 
ATOM   9508  N  N     . LYS B  1  72   ? -31.894 20.589  112.632 1.00 44.75 ? 70   LYS B N     1 
ATOM   9509  C  CA    . LYS B  1  72   ? -31.760 20.599  114.085 1.00 41.23 ? 70   LYS B CA    1 
ATOM   9510  C  C     . LYS B  1  72   ? -30.336 20.949  114.506 1.00 48.04 ? 70   LYS B C     1 
ATOM   9511  O  O     . LYS B  1  72   ? -30.133 21.702  115.466 1.00 47.10 ? 70   LYS B O     1 
ATOM   9512  C  CB    . LYS B  1  72   ? -32.176 19.244  114.660 1.00 47.22 ? 70   LYS B CB    1 
ATOM   9513  N  N     . LEU B  1  73   ? -29.332 20.422  113.797 1.00 49.68 ? 71   LEU B N     1 
ATOM   9514  C  CA    . LEU B  1  73   ? -27.950 20.750  114.137 1.00 48.29 ? 71   LEU B CA    1 
ATOM   9515  C  C     . LEU B  1  73   ? -27.650 22.222  113.879 1.00 48.37 ? 71   LEU B C     1 
ATOM   9516  O  O     . LEU B  1  73   ? -26.953 22.867  114.670 1.00 46.08 ? 71   LEU B O     1 
ATOM   9517  C  CB    . LEU B  1  73   ? -26.985 19.863  113.351 1.00 43.16 ? 71   LEU B CB    1 
ATOM   9518  C  CG    . LEU B  1  73   ? -27.068 18.355  113.598 1.00 47.53 ? 71   LEU B CG    1 
ATOM   9519  C  CD1   . LEU B  1  73   ? -26.140 17.608  112.653 1.00 39.50 ? 71   LEU B CD1   1 
ATOM   9520  C  CD2   . LEU B  1  73   ? -26.739 18.022  115.043 1.00 48.11 ? 71   LEU B CD2   1 
ATOM   9521  N  N     . ILE B  1  74   ? -28.175 22.772  112.782 1.00 48.74 ? 72   ILE B N     1 
ATOM   9522  C  CA    . ILE B  1  74   ? -27.889 24.161  112.435 1.00 44.58 ? 72   ILE B CA    1 
ATOM   9523  C  C     . ILE B  1  74   ? -28.629 25.106  113.368 1.00 48.87 ? 72   ILE B C     1 
ATOM   9524  O  O     . ILE B  1  74   ? -28.095 26.147  113.774 1.00 53.68 ? 72   ILE B O     1 
ATOM   9525  C  CB    . ILE B  1  74   ? -28.236 24.417  110.956 1.00 50.22 ? 72   ILE B CB    1 
ATOM   9526  C  CG1   . ILE B  1  74   ? -27.196 23.744  110.056 1.00 48.69 ? 72   ILE B CG1   1 
ATOM   9527  C  CG2   . ILE B  1  74   ? -28.298 25.910  110.662 1.00 47.78 ? 72   ILE B CG2   1 
ATOM   9528  C  CD1   . ILE B  1  74   ? -27.654 23.531  108.648 1.00 42.84 ? 72   ILE B CD1   1 
ATOM   9529  N  N     . GLU B  1  75   ? -29.867 24.762  113.724 1.00 51.64 ? 73   GLU B N     1 
ATOM   9530  C  CA    . GLU B  1  75   ? -30.596 25.552  114.710 1.00 51.43 ? 73   GLU B CA    1 
ATOM   9531  C  C     . GLU B  1  75   ? -29.842 25.584  116.034 1.00 50.26 ? 73   GLU B C     1 
ATOM   9532  O  O     . GLU B  1  75   ? -29.555 26.661  116.571 1.00 50.21 ? 73   GLU B O     1 
ATOM   9533  C  CB    . GLU B  1  75   ? -32.007 24.988  114.888 1.00 49.21 ? 73   GLU B CB    1 
ATOM   9534  N  N     . ALA B  1  76   ? -29.484 24.408  116.557 1.00 48.61 ? 74   ALA B N     1 
ATOM   9535  C  CA    . ALA B  1  76   ? -28.675 24.338  117.771 1.00 42.85 ? 74   ALA B CA    1 
ATOM   9536  C  C     . ALA B  1  76   ? -27.398 25.160  117.634 1.00 50.47 ? 74   ALA B C     1 
ATOM   9537  O  O     . ALA B  1  76   ? -27.046 25.934  118.532 1.00 55.22 ? 74   ALA B O     1 
ATOM   9538  C  CB    . ALA B  1  76   ? -28.347 22.881  118.102 1.00 43.70 ? 74   ALA B CB    1 
ATOM   9539  N  N     . LEU B  1  77   ? -26.695 25.011  116.507 1.00 47.96 ? 75   LEU B N     1 
ATOM   9540  C  CA    . LEU B  1  77   ? -25.473 25.779  116.287 1.00 49.40 ? 75   LEU B CA    1 
ATOM   9541  C  C     . LEU B  1  77   ? -25.740 27.275  116.360 1.00 45.80 ? 75   LEU B C     1 
ATOM   9542  O  O     . LEU B  1  77   ? -25.009 28.019  117.024 1.00 52.28 ? 75   LEU B O     1 
ATOM   9543  C  CB    . LEU B  1  77   ? -24.854 25.419  114.932 1.00 41.38 ? 75   LEU B CB    1 
ATOM   9544  C  CG    . LEU B  1  77   ? -23.879 24.247  114.920 1.00 46.87 ? 75   LEU B CG    1 
ATOM   9545  C  CD1   . LEU B  1  77   ? -23.435 23.932  113.502 1.00 46.32 ? 75   LEU B CD1   1 
ATOM   9546  C  CD2   . LEU B  1  77   ? -22.691 24.585  115.784 1.00 47.02 ? 75   LEU B CD2   1 
ATOM   9547  N  N     . ARG B  1  78   ? -26.780 27.739  115.672 1.00 43.50 ? 76   ARG B N     1 
ATOM   9548  C  CA    . ARG B  1  78   ? -27.040 29.169  115.599 1.00 43.92 ? 76   ARG B CA    1 
ATOM   9549  C  C     . ARG B  1  78   ? -27.762 29.708  116.827 1.00 53.82 ? 76   ARG B C     1 
ATOM   9550  O  O     . ARG B  1  78   ? -27.808 30.930  117.010 1.00 45.95 ? 76   ARG B O     1 
ATOM   9551  C  CB    . ARG B  1  78   ? -27.845 29.490  114.342 1.00 53.36 ? 76   ARG B CB    1 
ATOM   9552  C  CG    . ARG B  1  78   ? -27.027 29.434  113.069 1.00 50.25 ? 76   ARG B CG    1 
ATOM   9553  C  CD    . ARG B  1  78   ? -27.894 29.719  111.861 1.00 54.17 ? 76   ARG B CD    1 
ATOM   9554  N  NE    . ARG B  1  78   ? -27.130 30.352  110.795 1.00 49.29 ? 76   ARG B NE    1 
ATOM   9555  C  CZ    . ARG B  1  78   ? -27.643 30.729  109.633 1.00 56.08 ? 76   ARG B CZ    1 
ATOM   9556  N  NH1   . ARG B  1  78   ? -28.912 30.501  109.332 1.00 57.11 ? 76   ARG B NH1   1 
ATOM   9557  N  NH2   . ARG B  1  78   ? -26.864 31.357  108.755 1.00 51.86 ? 76   ARG B NH2   1 
ATOM   9558  N  N     . GLY B  1  79   ? -28.323 28.838  117.666 1.00 54.21 ? 77   GLY B N     1 
ATOM   9559  C  CA    . GLY B  1  79   ? -28.936 29.307  118.897 1.00 52.83 ? 77   GLY B CA    1 
ATOM   9560  C  C     . GLY B  1  79   ? -27.920 29.702  119.949 1.00 61.44 ? 77   GLY B C     1 
ATOM   9561  O  O     . GLY B  1  79   ? -28.183 30.586  120.772 1.00 52.58 ? 77   GLY B O     1 
ATOM   9562  N  N     . LYS B  1  80   ? -26.753 29.065  119.935 1.00 57.32 ? 78   LYS B N     1 
ATOM   9563  C  CA    . LYS B  1  80   ? -25.694 29.333  120.901 1.00 57.44 ? 78   LYS B CA    1 
ATOM   9564  C  C     . LYS B  1  80   ? -25.103 30.729  120.718 1.00 59.91 ? 78   LYS B C     1 
ATOM   9565  O  O     . LYS B  1  80   ? -24.043 30.897  120.113 1.00 61.61 ? 78   LYS B O     1 
ATOM   9566  C  CB    . LYS B  1  80   ? -24.600 28.271  120.777 1.00 54.69 ? 78   LYS B CB    1 
ATOM   9567  C  CG    . LYS B  1  80   ? -25.122 26.849  120.939 1.00 52.43 ? 78   LYS B CG    1 
ATOM   9568  C  CD    . LYS B  1  80   ? -24.120 25.809  120.457 1.00 52.75 ? 78   LYS B CD    1 
ATOM   9569  C  CE    . LYS B  1  80   ? -24.646 24.405  120.723 1.00 56.39 ? 78   LYS B CE    1 
ATOM   9570  N  NZ    . LYS B  1  80   ? -23.626 23.346  120.490 1.00 46.31 ? 78   LYS B NZ    1 
ATOM   9571  N  N     . SER B  1  84   ? -18.000 35.612  120.012 1.00 67.58 ? 82   SER B N     1 
ATOM   9572  C  CA    . SER B  1  84   ? -16.542 35.659  120.028 1.00 56.53 ? 82   SER B CA    1 
ATOM   9573  C  C     . SER B  1  84   ? -16.036 36.583  121.127 1.00 55.60 ? 82   SER B C     1 
ATOM   9574  O  O     . SER B  1  84   ? -16.657 37.603  121.433 1.00 54.05 ? 82   SER B O     1 
ATOM   9575  C  CB    . SER B  1  84   ? -15.997 36.120  118.673 1.00 44.74 ? 82   SER B CB    1 
ATOM   9576  N  N     . GLY B  1  85   ? -14.905 36.214  121.729 1.00 45.59 ? 83   GLY B N     1 
ATOM   9577  C  CA    . GLY B  1  85   ? -14.253 37.123  122.652 1.00 48.10 ? 83   GLY B CA    1 
ATOM   9578  C  C     . GLY B  1  85   ? -13.720 38.360  121.959 1.00 42.53 ? 83   GLY B C     1 
ATOM   9579  O  O     . GLY B  1  85   ? -13.754 39.456  122.526 1.00 44.37 ? 83   GLY B O     1 
ATOM   9580  N  N     . VAL B  1  86   ? -13.231 38.210  120.729 1.00 43.54 ? 84   VAL B N     1 
ATOM   9581  C  CA    . VAL B  1  86   ? -12.695 39.361  120.012 1.00 41.99 ? 84   VAL B CA    1 
ATOM   9582  C  C     . VAL B  1  86   ? -13.825 40.293  119.588 1.00 43.63 ? 84   VAL B C     1 
ATOM   9583  O  O     . VAL B  1  86   ? -13.684 41.520  119.637 1.00 45.29 ? 84   VAL B O     1 
ATOM   9584  C  CB    . VAL B  1  86   ? -11.838 38.898  118.819 1.00 41.58 ? 84   VAL B CB    1 
ATOM   9585  C  CG1   . VAL B  1  86   ? -12.635 37.980  117.906 1.00 50.96 ? 84   VAL B CG1   1 
ATOM   9586  C  CG2   . VAL B  1  86   ? -11.294 40.100  118.050 1.00 44.75 ? 84   VAL B CG2   1 
ATOM   9587  N  N     . GLU B  1  87   ? -14.975 39.732  119.197 1.00 46.92 ? 85   GLU B N     1 
ATOM   9588  C  CA    . GLU B  1  87   ? -16.128 40.563  118.861 1.00 46.62 ? 85   GLU B CA    1 
ATOM   9589  C  C     . GLU B  1  87   ? -16.571 41.398  120.056 1.00 41.73 ? 85   GLU B C     1 
ATOM   9590  O  O     . GLU B  1  87   ? -16.887 42.586  119.912 1.00 41.20 ? 85   GLU B O     1 
ATOM   9591  C  CB    . GLU B  1  87   ? -17.279 39.689  118.361 1.00 50.06 ? 85   GLU B CB    1 
ATOM   9592  N  N     . GLY B  1  88   ? -16.601 40.795  121.246 1.00 43.49 ? 86   GLY B N     1 
ATOM   9593  C  CA    . GLY B  1  88   ? -16.974 41.545  122.433 1.00 40.79 ? 86   GLY B CA    1 
ATOM   9594  C  C     . GLY B  1  88   ? -15.944 42.579  122.832 1.00 39.39 ? 86   GLY B C     1 
ATOM   9595  O  O     . GLY B  1  88   ? -16.292 43.628  123.381 1.00 38.12 ? 86   GLY B O     1 
ATOM   9596  N  N     . LEU B  1  89   ? -14.666 42.300  122.571 1.00 39.53 ? 87   LEU B N     1 
ATOM   9597  C  CA    . LEU B  1  89   ? -13.624 43.283  122.846 1.00 39.01 ? 87   LEU B CA    1 
ATOM   9598  C  C     . LEU B  1  89   ? -13.751 44.476  121.908 1.00 36.22 ? 87   LEU B C     1 
ATOM   9599  O  O     . LEU B  1  89   ? -13.658 45.630  122.345 1.00 34.47 ? 87   LEU B O     1 
ATOM   9600  C  CB    . LEU B  1  89   ? -12.251 42.621  122.713 1.00 38.54 ? 87   LEU B CB    1 
ATOM   9601  C  CG    . LEU B  1  89   ? -11.000 43.492  122.747 1.00 39.29 ? 87   LEU B CG    1 
ATOM   9602  C  CD1   . LEU B  1  89   ? -10.831 44.095  124.111 1.00 44.25 ? 87   LEU B CD1   1 
ATOM   9603  C  CD2   . LEU B  1  89   ? -9.779  42.661  122.360 1.00 44.54 ? 87   LEU B CD2   1 
ATOM   9604  N  N     . VAL B  1  90   ? -13.991 44.206  120.623 1.00 37.31 ? 88   VAL B N     1 
ATOM   9605  C  CA    . VAL B  1  90   ? -14.183 45.262  119.632 1.00 37.18 ? 88   VAL B CA    1 
ATOM   9606  C  C     . VAL B  1  90   ? -15.375 46.135  120.007 1.00 44.23 ? 88   VAL B C     1 
ATOM   9607  O  O     . VAL B  1  90   ? -15.308 47.369  119.941 1.00 37.94 ? 88   VAL B O     1 
ATOM   9608  C  CB    . VAL B  1  90   ? -14.348 44.639  118.232 1.00 36.41 ? 88   VAL B CB    1 
ATOM   9609  C  CG1   . VAL B  1  90   ? -14.863 45.666  117.233 1.00 38.99 ? 88   VAL B CG1   1 
ATOM   9610  C  CG2   . VAL B  1  90   ? -13.026 44.045  117.751 1.00 33.27 ? 88   VAL B CG2   1 
ATOM   9611  N  N     . GLN B  1  91   ? -16.479 45.513  120.428 1.00 39.28 ? 89   GLN B N     1 
ATOM   9612  C  CA    . GLN B  1  91   ? -17.653 46.292  120.810 1.00 44.17 ? 89   GLN B CA    1 
ATOM   9613  C  C     . GLN B  1  91   ? -17.421 47.063  122.105 1.00 41.65 ? 89   GLN B C     1 
ATOM   9614  O  O     . GLN B  1  91   ? -17.856 48.214  122.232 1.00 43.73 ? 89   GLN B O     1 
ATOM   9615  C  CB    . GLN B  1  91   ? -18.873 45.376  120.928 1.00 47.07 ? 89   GLN B CB    1 
ATOM   9616  N  N     . GLU B  1  92   ? -16.729 46.460  123.079 1.00 36.34 ? 90   GLU B N     1 
ATOM   9617  C  CA    . GLU B  1  92   ? -16.566 47.121  124.371 1.00 40.64 ? 90   GLU B CA    1 
ATOM   9618  C  C     . GLU B  1  92   ? -15.713 48.380  124.256 1.00 35.96 ? 90   GLU B C     1 
ATOM   9619  O  O     . GLU B  1  92   ? -15.969 49.378  124.941 1.00 37.31 ? 90   GLU B O     1 
ATOM   9620  C  CB    . GLU B  1  92   ? -15.954 46.160  125.393 1.00 42.30 ? 90   GLU B CB    1 
ATOM   9621  C  CG    . GLU B  1  92   ? -15.815 46.776  126.774 1.00 46.31 ? 90   GLU B CG    1 
ATOM   9622  C  CD    . GLU B  1  92   ? -15.111 45.877  127.778 1.00 45.16 ? 90   GLU B CD    1 
ATOM   9623  O  OE1   . GLU B  1  92   ? -14.841 44.698  127.452 1.00 47.80 ? 90   GLU B OE1   1 
ATOM   9624  O  OE2   . GLU B  1  92   ? -14.828 46.364  128.893 1.00 42.83 ? 90   GLU B OE2   1 
ATOM   9625  N  N     . TYR B  1  93   ? -14.694 48.358  123.402 1.00 37.96 ? 91   TYR B N     1 
ATOM   9626  C  CA    . TYR B  1  93   ? -13.814 49.507  123.253 1.00 36.67 ? 91   TYR B CA    1 
ATOM   9627  C  C     . TYR B  1  93   ? -14.036 50.244  121.941 1.00 34.47 ? 91   TYR B C     1 
ATOM   9628  O  O     . TYR B  1  93   ? -13.235 51.115  121.595 1.00 33.83 ? 91   TYR B O     1 
ATOM   9629  C  CB    . TYR B  1  93   ? -12.356 49.074  123.400 1.00 33.70 ? 91   TYR B CB    1 
ATOM   9630  C  CG    . TYR B  1  93   ? -12.044 48.686  124.824 1.00 32.96 ? 91   TYR B CG    1 
ATOM   9631  C  CD1   . TYR B  1  93   ? -11.706 49.648  125.762 1.00 31.08 ? 91   TYR B CD1   1 
ATOM   9632  C  CD2   . TYR B  1  93   ? -12.127 47.362  125.240 1.00 36.00 ? 91   TYR B CD2   1 
ATOM   9633  C  CE1   . TYR B  1  93   ? -11.441 49.307  127.078 1.00 34.52 ? 91   TYR B CE1   1 
ATOM   9634  C  CE2   . TYR B  1  93   ? -11.865 47.009  126.562 1.00 38.54 ? 91   TYR B CE2   1 
ATOM   9635  C  CZ    . TYR B  1  93   ? -11.521 47.988  127.471 1.00 36.67 ? 91   TYR B CZ    1 
ATOM   9636  O  OH    . TYR B  1  93   ? -11.256 47.652  128.783 1.00 37.60 ? 91   TYR B OH    1 
ATOM   9637  N  N     . SER B  1  94   ? -15.117 49.933  121.225 1.00 31.25 ? 92   SER B N     1 
ATOM   9638  C  CA    . SER B  1  94   ? -15.482 50.619  119.984 1.00 30.73 ? 92   SER B CA    1 
ATOM   9639  C  C     . SER B  1  94   ? -14.308 50.642  119.011 1.00 34.16 ? 92   SER B C     1 
ATOM   9640  O  O     . SER B  1  94   ? -13.964 51.675  118.429 1.00 33.77 ? 92   SER B O     1 
ATOM   9641  C  CB    . SER B  1  94   ? -15.984 52.033  120.262 1.00 35.53 ? 92   SER B CB    1 
ATOM   9642  O  OG    . SER B  1  94   ? -17.092 52.008  121.142 1.00 39.85 ? 92   SER B OG    1 
ATOM   9643  N  N     . LEU B  1  95   ? -13.678 49.484  118.847 1.00 27.94 ? 93   LEU B N     1 
ATOM   9644  C  CA    . LEU B  1  95   ? -12.522 49.387  117.976 1.00 28.77 ? 93   LEU B CA    1 
ATOM   9645  C  C     . LEU B  1  95   ? -12.951 49.295  116.526 1.00 27.59 ? 93   LEU B C     1 
ATOM   9646  O  O     . LEU B  1  95   ? -13.924 48.619  116.189 1.00 32.13 ? 93   LEU B O     1 
ATOM   9647  C  CB    . LEU B  1  95   ? -11.683 48.160  118.319 1.00 27.80 ? 93   LEU B CB    1 
ATOM   9648  C  CG    . LEU B  1  95   ? -11.157 48.098  119.749 1.00 29.19 ? 93   LEU B CG    1 
ATOM   9649  C  CD1   . LEU B  1  95   ? -10.239 46.900  119.932 1.00 28.90 ? 93   LEU B CD1   1 
ATOM   9650  C  CD2   . LEU B  1  95   ? -10.441 49.393  120.130 1.00 29.00 ? 93   LEU B CD2   1 
ATOM   9651  N  N     . SER B  1  96   ? -12.189 49.952  115.661 1.00 25.74 ? 94   SER B N     1 
ATOM   9652  C  CA    . SER B  1  96   ? -12.263 49.638  114.256 1.00 25.47 ? 94   SER B CA    1 
ATOM   9653  C  C     . SER B  1  96   ? -11.600 48.286  114.003 1.00 27.97 ? 94   SER B C     1 
ATOM   9654  O  O     . SER B  1  96   ? -10.931 47.720  114.876 1.00 26.92 ? 94   SER B O     1 
ATOM   9655  C  CB    . SER B  1  96   ? -11.565 50.713  113.433 1.00 29.01 ? 94   SER B CB    1 
ATOM   9656  O  OG    . SER B  1  96   ? -10.172 50.674  113.696 1.00 25.07 ? 94   SER B OG    1 
ATOM   9657  N  N     . SER B  1  97   ? -11.769 47.780  112.780 1.00 24.84 ? 95   SER B N     1 
ATOM   9658  C  CA    . SER B  1  97   ? -11.116 46.532  112.405 1.00 23.08 ? 95   SER B CA    1 
ATOM   9659  C  C     . SER B  1  97   ? -9.603  46.654  112.522 1.00 25.82 ? 95   SER B C     1 
ATOM   9660  O  O     . SER B  1  97   ? -8.949  45.799  113.125 1.00 23.82 ? 95   SER B O     1 
ATOM   9661  C  CB    . SER B  1  97   ? -11.510 46.125  110.985 1.00 28.46 ? 95   SER B CB    1 
ATOM   9662  O  OG    . SER B  1  97   ? -12.868 45.719  110.971 1.00 36.31 ? 95   SER B OG    1 
ATOM   9663  N  N     . GLN B  1  98   ? -9.033  47.725  111.965 1.00 25.08 ? 96   GLN B N     1 
ATOM   9664  C  CA    . GLN B  1  98   ? -7.585  47.899  112.024 1.00 23.03 ? 96   GLN B CA    1 
ATOM   9665  C  C     . GLN B  1  98   ? -7.105  48.045  113.463 1.00 21.23 ? 96   GLN B C     1 
ATOM   9666  O  O     . GLN B  1  98   ? -6.005  47.593  113.800 1.00 22.29 ? 96   GLN B O     1 
ATOM   9667  C  CB    . GLN B  1  98   ? -7.151  49.110  111.192 1.00 23.48 ? 96   GLN B CB    1 
ATOM   9668  C  CG    . GLN B  1  98   ? -7.243  48.872  109.711 1.00 22.54 ? 96   GLN B CG    1 
ATOM   9669  C  CD    . GLN B  1  98   ? -6.249  47.826  109.258 1.00 25.04 ? 96   GLN B CD    1 
ATOM   9670  O  OE1   . GLN B  1  98   ? -6.524  46.625  109.322 1.00 27.34 ? 96   GLN B OE1   1 
ATOM   9671  N  NE2   . GLN B  1  98   ? -5.081  48.272  108.802 1.00 23.78 ? 96   GLN B NE2   1 
ATOM   9672  N  N     . GLU B  1  99   ? -7.901  48.698  114.316 1.00 19.68 ? 97   GLU B N     1 
ATOM   9673  C  CA    . GLU B  1  99   ? -7.537  48.773  115.729 1.00 21.00 ? 97   GLU B CA    1 
ATOM   9674  C  C     . GLU B  1  99   ? -7.594  47.398  116.374 1.00 24.88 ? 97   GLU B C     1 
ATOM   9675  O  O     . GLU B  1  99   ? -6.725  47.050  117.179 1.00 23.53 ? 97   GLU B O     1 
ATOM   9676  C  CB    . GLU B  1  99   ? -8.439  49.758  116.469 1.00 25.79 ? 97   GLU B CB    1 
ATOM   9677  C  CG    . GLU B  1  99   ? -8.135  51.214  116.133 1.00 22.74 ? 97   GLU B CG    1 
ATOM   9678  C  CD    . GLU B  1  99   ? -9.234  52.153  116.590 1.00 25.90 ? 97   GLU B CD    1 
ATOM   9679  O  OE1   . GLU B  1  99   ? -10.238 51.677  117.161 1.00 26.09 ? 97   GLU B OE1   1 
ATOM   9680  O  OE2   . GLU B  1  99   ? -9.080  53.374  116.396 1.00 25.98 ? 97   GLU B OE2   1 
ATOM   9681  N  N     . GLY B  1  100  ? -8.604  46.599  116.031 1.00 22.85 ? 98   GLY B N     1 
ATOM   9682  C  CA    . GLY B  1  100  ? -8.662  45.251  116.570 1.00 24.64 ? 98   GLY B CA    1 
ATOM   9683  C  C     . GLY B  1  100  ? -7.460  44.428  116.152 1.00 24.70 ? 98   GLY B C     1 
ATOM   9684  O  O     . GLY B  1  100  ? -6.840  43.749  116.979 1.00 25.38 ? 98   GLY B O     1 
ATOM   9685  N  N     . VAL B  1  101  ? -7.085  44.519  114.877 1.00 22.82 ? 99   VAL B N     1 
ATOM   9686  C  CA    . VAL B  1  101  ? -5.919  43.792  114.386 1.00 20.69 ? 99   VAL B CA    1 
ATOM   9687  C  C     . VAL B  1  101  ? -4.654  44.284  115.077 1.00 23.31 ? 99   VAL B C     1 
ATOM   9688  O  O     . VAL B  1  101  ? -3.823  43.490  115.538 1.00 23.25 ? 99   VAL B O     1 
ATOM   9689  C  CB    . VAL B  1  101  ? -5.815  43.936  112.858 1.00 21.42 ? 99   VAL B CB    1 
ATOM   9690  C  CG1   . VAL B  1  101  ? -4.520  43.323  112.372 1.00 21.42 ? 99   VAL B CG1   1 
ATOM   9691  C  CG2   . VAL B  1  101  ? -7.023  43.292  112.201 1.00 22.78 ? 99   VAL B CG2   1 
ATOM   9692  N  N     . ALA B  1  102  ? -4.488  45.607  115.149 1.00 21.38 ? 100  ALA B N     1 
ATOM   9693  C  CA    . ALA B  1  102  ? -3.300  46.181  115.773 1.00 21.71 ? 100  ALA B CA    1 
ATOM   9694  C  C     . ALA B  1  102  ? -3.201  45.781  117.237 1.00 24.07 ? 100  ALA B C     1 
ATOM   9695  O  O     . ALA B  1  102  ? -2.107  45.494  117.738 1.00 22.02 ? 100  ALA B O     1 
ATOM   9696  C  CB    . ALA B  1  102  ? -3.326  47.709  115.657 1.00 23.53 ? 100  ALA B CB    1 
ATOM   9697  N  N     . LEU B  1  103  ? -4.337  45.760  117.939 1.00 22.02 ? 101  LEU B N     1 
ATOM   9698  C  CA    . LEU B  1  103  ? -4.331  45.380  119.345 1.00 24.15 ? 101  LEU B CA    1 
ATOM   9699  C  C     . LEU B  1  103  ? -3.889  43.936  119.515 1.00 23.44 ? 101  LEU B C     1 
ATOM   9700  O  O     . LEU B  1  103  ? -3.104  43.624  120.424 1.00 24.60 ? 101  LEU B O     1 
ATOM   9701  C  CB    . LEU B  1  103  ? -5.713  45.593  119.952 1.00 25.91 ? 101  LEU B CB    1 
ATOM   9702  C  CG    . LEU B  1  103  ? -5.883  45.157  121.398 1.00 23.38 ? 101  LEU B CG    1 
ATOM   9703  C  CD1   . LEU B  1  103  ? -4.995  45.996  122.302 1.00 24.40 ? 101  LEU B CD1   1 
ATOM   9704  C  CD2   . LEU B  1  103  ? -7.333  45.315  121.799 1.00 24.96 ? 101  LEU B CD2   1 
ATOM   9705  N  N     . MET B  1  104  ? -4.370  43.046  118.646 1.00 21.13 ? 102  MET B N     1 
ATOM   9706  C  CA    . MET B  1  104  ? -3.974  41.645  118.759 1.00 25.75 ? 102  MET B CA    1 
ATOM   9707  C  C     . MET B  1  104  ? -2.506  41.457  118.424 1.00 23.44 ? 102  MET B C     1 
ATOM   9708  O  O     . MET B  1  104  ? -1.839  40.616  119.032 1.00 24.94 ? 102  MET B O     1 
ATOM   9709  C  CB    . MET B  1  104  ? -4.853  40.771  117.867 1.00 24.71 ? 102  MET B CB    1 
ATOM   9710  C  CG    . MET B  1  104  ? -6.325  40.819  118.276 1.00 24.75 ? 102  MET B CG    1 
ATOM   9711  S  SD    . MET B  1  104  ? -6.612  40.380  120.010 1.00 34.43 ? 102  MET B SD    1 
ATOM   9712  C  CE    . MET B  1  104  ? -6.239  38.633  119.962 1.00 45.21 ? 102  MET B CE    1 
ATOM   9713  N  N     . CYS B  1  105  ? -1.975  42.251  117.498 1.00 20.43 ? 103  CYS B N     1 
ATOM   9714  C  CA    . CYS B  1  105  ? -0.538  42.216  117.241 1.00 20.90 ? 103  CYS B CA    1 
ATOM   9715  C  C     . CYS B  1  105  ? 0.240   42.664  118.463 1.00 24.08 ? 103  CYS B C     1 
ATOM   9716  O  O     . CYS B  1  105  ? 1.249   42.052  118.834 1.00 24.89 ? 103  CYS B O     1 
ATOM   9717  C  CB    . CYS B  1  105  ? -0.187  43.111  116.059 1.00 19.77 ? 103  CYS B CB    1 
ATOM   9718  S  SG    . CYS B  1  105  ? -0.798  42.506  114.505 1.00 22.69 ? 103  CYS B SG    1 
ATOM   9719  N  N     . LEU B  1  106  ? -0.189  43.770  119.076 1.00 22.35 ? 104  LEU B N     1 
ATOM   9720  C  CA    . LEU B  1  106  ? 0.447   44.213  120.309 1.00 20.67 ? 104  LEU B CA    1 
ATOM   9721  C  C     . LEU B  1  106  ? 0.371   43.131  121.369 1.00 24.40 ? 104  LEU B C     1 
ATOM   9722  O  O     . LEU B  1  106  ? 1.356   42.865  122.068 1.00 25.06 ? 104  LEU B O     1 
ATOM   9723  C  CB    . LEU B  1  106  ? -0.211  45.491  120.829 1.00 20.91 ? 104  LEU B CB    1 
ATOM   9724  C  CG    . LEU B  1  106  ? 0.315   45.930  122.195 1.00 21.86 ? 104  LEU B CG    1 
ATOM   9725  C  CD1   . LEU B  1  106  ? 1.734   46.421  122.052 1.00 28.06 ? 104  LEU B CD1   1 
ATOM   9726  C  CD2   . LEU B  1  106  ? -0.570  47.000  122.801 1.00 25.89 ? 104  LEU B CD2   1 
ATOM   9727  N  N     . ALA B  1  107  ? -0.793  42.491  121.497 1.00 21.47 ? 105  ALA B N     1 
ATOM   9728  C  CA    . ALA B  1  107  ? -0.958  41.464  122.520 1.00 25.00 ? 105  ALA B CA    1 
ATOM   9729  C  C     . ALA B  1  107  ? -0.036  40.284  122.250 1.00 25.31 ? 105  ALA B C     1 
ATOM   9730  O  O     . ALA B  1  107  ? 0.624   39.779  123.166 1.00 27.42 ? 105  ALA B O     1 
ATOM   9731  C  CB    . ALA B  1  107  ? -2.414  41.011  122.574 1.00 25.39 ? 105  ALA B CB    1 
ATOM   9732  N  N     . GLU B  1  108  ? 0.039   39.849  120.993 1.00 25.26 ? 106  GLU B N     1 
ATOM   9733  C  CA    . GLU B  1  108  ? 0.972   38.790  120.621 1.00 24.55 ? 106  GLU B CA    1 
ATOM   9734  C  C     . GLU B  1  108  ? 2.395   39.143  121.033 1.00 29.50 ? 106  GLU B C     1 
ATOM   9735  O  O     . GLU B  1  108  ? 3.113   38.309  121.597 1.00 28.05 ? 106  GLU B O     1 
ATOM   9736  C  CB    . GLU B  1  108  ? 0.890   38.541  119.111 1.00 25.76 ? 106  GLU B CB    1 
ATOM   9737  C  CG    . GLU B  1  108  ? 1.995   37.652  118.551 1.00 27.50 ? 106  GLU B CG    1 
ATOM   9738  C  CD    . GLU B  1  108  ? 2.146   37.785  117.043 1.00 33.11 ? 106  GLU B CD    1 
ATOM   9739  O  OE1   . GLU B  1  108  ? 1.223   38.331  116.398 1.00 31.73 ? 106  GLU B OE1   1 
ATOM   9740  O  OE2   . GLU B  1  108  ? 3.198   37.358  116.509 1.00 34.69 ? 106  GLU B OE2   1 
ATOM   9741  N  N     . ALA B  1  109  ? 2.820   40.379  120.771 1.00 25.78 ? 107  ALA B N     1 
ATOM   9742  C  CA    . ALA B  1  109  ? 4.180   40.764  121.122 1.00 29.82 ? 107  ALA B CA    1 
ATOM   9743  C  C     . ALA B  1  109  ? 4.372   40.762  122.630 1.00 30.01 ? 107  ALA B C     1 
ATOM   9744  O  O     . ALA B  1  109  ? 5.405   40.295  123.131 1.00 29.11 ? 107  ALA B O     1 
ATOM   9745  C  CB    . ALA B  1  109  ? 4.511   42.137  120.538 1.00 29.62 ? 107  ALA B CB    1 
ATOM   9746  N  N     . LEU B  1  110  ? 3.386   41.271  123.373 1.00 25.10 ? 108  LEU B N     1 
ATOM   9747  C  CA    . LEU B  1  110  ? 3.515   41.299  124.825 1.00 24.79 ? 108  LEU B CA    1 
ATOM   9748  C  C     . LEU B  1  110  ? 3.553   39.895  125.409 1.00 28.64 ? 108  LEU B C     1 
ATOM   9749  O  O     . LEU B  1  110  ? 4.188   39.678  126.448 1.00 31.78 ? 108  LEU B O     1 
ATOM   9750  C  CB    . LEU B  1  110  ? 2.372   42.106  125.446 1.00 25.28 ? 108  LEU B CB    1 
ATOM   9751  C  CG    . LEU B  1  110  ? 2.492   43.612  125.183 1.00 25.53 ? 108  LEU B CG    1 
ATOM   9752  C  CD1   . LEU B  1  110  ? 1.184   44.308  125.513 1.00 26.97 ? 108  LEU B CD1   1 
ATOM   9753  C  CD2   . LEU B  1  110  ? 3.640   44.206  126.007 1.00 29.05 ? 108  LEU B CD2   1 
ATOM   9754  N  N     . LEU B  1  111  ? 2.898   38.936  124.760 1.00 28.19 ? 109  LEU B N     1 
ATOM   9755  C  CA    . LEU B  1  111  ? 2.913   37.565  125.251 1.00 32.08 ? 109  LEU B CA    1 
ATOM   9756  C  C     . LEU B  1  111  ? 4.224   36.849  124.966 1.00 35.74 ? 109  LEU B C     1 
ATOM   9757  O  O     . LEU B  1  111  ? 4.460   35.781  125.541 1.00 35.65 ? 109  LEU B O     1 
ATOM   9758  C  CB    . LEU B  1  111  ? 1.757   36.778  124.649 1.00 32.28 ? 109  LEU B CB    1 
ATOM   9759  C  CG    . LEU B  1  111  ? 0.402   37.190  125.212 1.00 29.34 ? 109  LEU B CG    1 
ATOM   9760  C  CD1   . LEU B  1  111  ? -0.701  36.553  124.392 1.00 32.52 ? 109  LEU B CD1   1 
ATOM   9761  C  CD2   . LEU B  1  111  ? 0.293   36.807  126.682 1.00 30.81 ? 109  LEU B CD2   1 
ATOM   9762  N  N     . ARG B  1  112  ? 5.076   37.403  124.102 1.00 31.60 ? 110  ARG B N     1 
ATOM   9763  C  CA    . ARG B  1  112  ? 6.435   36.894  123.967 1.00 35.15 ? 110  ARG B CA    1 
ATOM   9764  C  C     . ARG B  1  112  ? 7.295   37.226  125.182 1.00 38.88 ? 110  ARG B C     1 
ATOM   9765  O  O     . ARG B  1  112  ? 8.389   36.669  125.319 1.00 40.12 ? 110  ARG B O     1 
ATOM   9766  C  CB    . ARG B  1  112  ? 7.072   37.434  122.684 1.00 31.75 ? 110  ARG B CB    1 
ATOM   9767  C  CG    . ARG B  1  112  ? 6.313   37.018  121.422 1.00 35.40 ? 110  ARG B CG    1 
ATOM   9768  C  CD    . ARG B  1  112  ? 7.136   37.192  120.150 1.00 46.18 ? 110  ARG B CD    1 
ATOM   9769  N  NE    . ARG B  1  112  ? 7.295   38.587  119.755 1.00 41.92 ? 110  ARG B NE    1 
ATOM   9770  C  CZ    . ARG B  1  112  ? 6.567   39.200  118.830 1.00 49.62 ? 110  ARG B CZ    1 
ATOM   9771  N  NH1   . ARG B  1  112  ? 5.601   38.572  118.178 1.00 51.49 ? 110  ARG B NH1   1 
ATOM   9772  N  NH2   . ARG B  1  112  ? 6.816   40.477  118.550 1.00 54.82 ? 110  ARG B NH2   1 
ATOM   9773  N  N     . ILE B  1  113  ? 6.829   38.110  126.058 1.00 31.88 ? 111  ILE B N     1 
ATOM   9774  C  CA    . ILE B  1  113  ? 7.454   38.336  127.358 1.00 34.79 ? 111  ILE B CA    1 
ATOM   9775  C  C     . ILE B  1  113  ? 6.950   37.243  128.290 1.00 38.24 ? 111  ILE B C     1 
ATOM   9776  O  O     . ILE B  1  113  ? 5.751   37.203  128.604 1.00 39.32 ? 111  ILE B O     1 
ATOM   9777  C  CB    . ILE B  1  113  ? 7.132   39.735  127.908 1.00 35.11 ? 111  ILE B CB    1 
ATOM   9778  C  CG1   . ILE B  1  113  ? 7.607   40.813  126.934 1.00 35.06 ? 111  ILE B CG1   1 
ATOM   9779  C  CG2   . ILE B  1  113  ? 7.757   39.927  129.297 1.00 32.51 ? 111  ILE B CG2   1 
ATOM   9780  C  CD1   . ILE B  1  113  ? 7.174   42.205  127.328 1.00 35.87 ? 111  ILE B CD1   1 
ATOM   9781  N  N     . PRO B  1  114  ? 7.821   36.337  128.749 1.00 41.60 ? 112  PRO B N     1 
ATOM   9782  C  CA    . PRO B  1  114  ? 7.333   35.165  129.493 1.00 43.43 ? 112  PRO B CA    1 
ATOM   9783  C  C     . PRO B  1  114  ? 6.877   35.484  130.905 1.00 38.90 ? 112  PRO B C     1 
ATOM   9784  O  O     . PRO B  1  114  ? 5.931   34.857  131.398 1.00 43.52 ? 112  PRO B O     1 
ATOM   9785  C  CB    . PRO B  1  114  ? 8.548   34.219  129.502 1.00 35.58 ? 112  PRO B CB    1 
ATOM   9786  C  CG    . PRO B  1  114  ? 9.549   34.827  128.537 1.00 43.51 ? 112  PRO B CG    1 
ATOM   9787  C  CD    . PRO B  1  114  ? 9.274   36.294  128.537 1.00 40.12 ? 112  PRO B CD    1 
ATOM   9788  N  N     . ASP B  1  115  ? 7.521   36.433  131.574 1.00 45.14 ? 113  ASP B N     1 
ATOM   9789  C  CA    . ASP B  1  115  ? 7.258   36.706  132.980 1.00 47.27 ? 113  ASP B CA    1 
ATOM   9790  C  C     . ASP B  1  115  ? 6.108   37.699  133.104 1.00 41.95 ? 113  ASP B C     1 
ATOM   9791  O  O     . ASP B  1  115  ? 6.209   38.833  132.628 1.00 41.34 ? 113  ASP B O     1 
ATOM   9792  C  CB    . ASP B  1  115  ? 8.519   37.241  133.656 1.00 46.98 ? 113  ASP B CB    1 
ATOM   9793  C  CG    . ASP B  1  115  ? 8.245   37.833  135.016 1.00 49.97 ? 113  ASP B CG    1 
ATOM   9794  O  OD1   . ASP B  1  115  ? 7.608   37.159  135.855 1.00 57.77 ? 113  ASP B OD1   1 
ATOM   9795  O  OD2   . ASP B  1  115  ? 8.676   38.979  135.250 1.00 50.46 ? 113  ASP B OD2   1 
ATOM   9796  N  N     . THR B  1  116  ? 5.025   37.266  133.753 1.00 42.21 ? 114  THR B N     1 
ATOM   9797  C  CA    . THR B  1  116  ? 3.832   38.097  133.887 1.00 46.79 ? 114  THR B CA    1 
ATOM   9798  C  C     . THR B  1  116  ? 4.151   39.460  134.495 1.00 45.93 ? 114  THR B C     1 
ATOM   9799  O  O     . THR B  1  116  ? 3.649   40.491  134.029 1.00 44.69 ? 114  THR B O     1 
ATOM   9800  C  CB    . THR B  1  116  ? 2.785   37.362  134.729 1.00 52.95 ? 114  THR B CB    1 
ATOM   9801  O  OG1   . THR B  1  116  ? 2.377   36.167  134.047 1.00 57.98 ? 114  THR B OG1   1 
ATOM   9802  C  CG2   . THR B  1  116  ? 1.567   38.245  134.978 1.00 53.69 ? 114  THR B CG2   1 
ATOM   9803  N  N     . ALA B  1  117  ? 4.991   39.491  135.531 1.00 46.48 ? 115  ALA B N     1 
ATOM   9804  C  CA    . ALA B  1  117  ? 5.275   40.756  136.198 1.00 47.00 ? 115  ALA B CA    1 
ATOM   9805  C  C     . ALA B  1  117  ? 6.035   41.708  135.284 1.00 41.14 ? 115  ALA B C     1 
ATOM   9806  O  O     . ALA B  1  117  ? 5.780   42.919  135.291 1.00 45.40 ? 115  ALA B O     1 
ATOM   9807  C  CB    . ALA B  1  117  ? 6.057   40.505  137.488 1.00 47.53 ? 115  ALA B CB    1 
ATOM   9808  N  N     . THR B  1  118  ? 6.973   41.183  134.493 1.00 40.59 ? 116  THR B N     1 
ATOM   9809  C  CA    . THR B  1  118  ? 7.717   42.031  133.568 1.00 39.59 ? 116  THR B CA    1 
ATOM   9810  C  C     . THR B  1  118  ? 6.811   42.549  132.461 1.00 38.31 ? 116  THR B C     1 
ATOM   9811  O  O     . THR B  1  118  ? 6.918   43.713  132.053 1.00 40.94 ? 116  THR B O     1 
ATOM   9812  C  CB    . THR B  1  118  ? 8.895   41.260  132.976 1.00 38.29 ? 116  THR B CB    1 
ATOM   9813  O  OG1   . THR B  1  118  ? 9.777   40.861  134.034 1.00 44.96 ? 116  THR B OG1   1 
ATOM   9814  C  CG2   . THR B  1  118  ? 9.662   42.120  131.988 1.00 36.88 ? 116  THR B CG2   1 
ATOM   9815  N  N     . ARG B  1  119  ? 5.917   41.693  131.966 1.00 40.57 ? 117  ARG B N     1 
ATOM   9816  C  CA    . ARG B  1  119  ? 4.971   42.104  130.934 1.00 38.93 ? 117  ARG B CA    1 
ATOM   9817  C  C     . ARG B  1  119  ? 4.010   43.159  131.466 1.00 39.51 ? 117  ARG B C     1 
ATOM   9818  O  O     . ARG B  1  119  ? 3.822   44.213  130.847 1.00 37.77 ? 117  ARG B O     1 
ATOM   9819  C  CB    . ARG B  1  119  ? 4.201   40.887  130.430 1.00 35.69 ? 117  ARG B CB    1 
ATOM   9820  C  CG    . ARG B  1  119  ? 3.220   41.196  129.306 1.00 28.50 ? 117  ARG B CG    1 
ATOM   9821  C  CD    . ARG B  1  119  ? 2.259   40.053  129.154 1.00 35.69 ? 117  ARG B CD    1 
ATOM   9822  N  NE    . ARG B  1  119  ? 2.968   38.789  129.003 1.00 38.04 ? 117  ARG B NE    1 
ATOM   9823  C  CZ    . ARG B  1  119  ? 2.609   37.659  129.597 1.00 45.49 ? 117  ARG B CZ    1 
ATOM   9824  N  NH1   . ARG B  1  119  ? 1.567   37.609  130.414 1.00 39.12 ? 117  ARG B NH1   1 
ATOM   9825  N  NH2   . ARG B  1  119  ? 3.316   36.556  129.373 1.00 42.60 ? 117  ARG B NH2   1 
ATOM   9826  N  N     . ASP B  1  120  ? 3.397   42.887  132.624 1.00 39.13 ? 118  ASP B N     1 
ATOM   9827  C  CA    . ASP B  1  120  ? 2.446   43.821  133.220 1.00 40.13 ? 118  ASP B CA    1 
ATOM   9828  C  C     . ASP B  1  120  ? 3.099   45.152  133.562 1.00 41.56 ? 118  ASP B C     1 
ATOM   9829  O  O     . ASP B  1  120  ? 2.445   46.199  133.484 1.00 37.71 ? 118  ASP B O     1 
ATOM   9830  C  CB    . ASP B  1  120  ? 1.815   43.206  134.471 1.00 42.14 ? 118  ASP B CB    1 
ATOM   9831  C  CG    . ASP B  1  120  ? 0.873   42.062  134.144 1.00 49.59 ? 118  ASP B CG    1 
ATOM   9832  O  OD1   . ASP B  1  120  ? 0.659   41.798  132.943 1.00 52.33 ? 118  ASP B OD1   1 
ATOM   9833  O  OD2   . ASP B  1  120  ? 0.344   41.427  135.082 1.00 53.80 ? 118  ASP B OD2   1 
ATOM   9834  N  N     . ALA B  1  121  ? 4.378   45.136  133.939 1.00 40.28 ? 119  ALA B N     1 
ATOM   9835  C  CA    . ALA B  1  121  ? 5.072   46.385  134.233 1.00 44.54 ? 119  ALA B CA    1 
ATOM   9836  C  C     . ALA B  1  121  ? 5.281   47.201  132.964 1.00 42.13 ? 119  ALA B C     1 
ATOM   9837  O  O     . ALA B  1  121  ? 5.063   48.417  132.954 1.00 40.46 ? 119  ALA B O     1 
ATOM   9838  C  CB    . ALA B  1  121  ? 6.407   46.101  134.925 1.00 43.56 ? 119  ALA B CB    1 
ATOM   9839  N  N     . LEU B  1  122  ? 5.703   46.544  131.880 1.00 35.79 ? 120  LEU B N     1 
ATOM   9840  C  CA    . LEU B  1  122  ? 5.890   47.252  130.618 1.00 41.35 ? 120  LEU B CA    1 
ATOM   9841  C  C     . LEU B  1  122  ? 4.586   47.890  130.158 1.00 38.10 ? 120  LEU B C     1 
ATOM   9842  O  O     . LEU B  1  122  ? 4.582   49.009  129.632 1.00 41.26 ? 120  LEU B O     1 
ATOM   9843  C  CB    . LEU B  1  122  ? 6.423   46.295  129.551 1.00 38.44 ? 120  LEU B CB    1 
ATOM   9844  C  CG    . LEU B  1  122  ? 6.843   46.952  128.235 1.00 40.63 ? 120  LEU B CG    1 
ATOM   9845  C  CD1   . LEU B  1  122  ? 8.114   47.771  128.437 1.00 46.30 ? 120  LEU B CD1   1 
ATOM   9846  C  CD2   . LEU B  1  122  ? 7.022   45.915  127.137 1.00 36.17 ? 120  LEU B CD2   1 
ATOM   9847  N  N     . ILE B  1  123  ? 3.469   47.194  130.371 1.00 36.57 ? 121  ILE B N     1 
ATOM   9848  C  CA    . ILE B  1  123  ? 2.168   47.697  129.940 1.00 38.29 ? 121  ILE B CA    1 
ATOM   9849  C  C     . ILE B  1  123  ? 1.813   48.966  130.702 1.00 48.44 ? 121  ILE B C     1 
ATOM   9850  O  O     . ILE B  1  123  ? 1.425   49.981  130.109 1.00 44.56 ? 121  ILE B O     1 
ATOM   9851  C  CB    . ILE B  1  123  ? 1.094   46.610  130.123 1.00 31.55 ? 121  ILE B CB    1 
ATOM   9852  C  CG1   . ILE B  1  123  ? 1.345   45.454  129.148 1.00 26.78 ? 121  ILE B CG1   1 
ATOM   9853  C  CG2   . ILE B  1  123  ? -0.303  47.191  129.939 1.00 32.83 ? 121  ILE B CG2   1 
ATOM   9854  C  CD1   . ILE B  1  123  ? 0.474   44.243  129.419 1.00 30.66 ? 121  ILE B CD1   1 
ATOM   9855  N  N     . ARG B  1  124  ? 1.954   48.931  132.029 1.00 38.37 ? 122  ARG B N     1 
ATOM   9856  C  CA    . ARG B  1  124  ? 1.543   50.065  132.848 1.00 43.20 ? 122  ARG B CA    1 
ATOM   9857  C  C     . ARG B  1  124  ? 2.499   51.241  132.690 1.00 48.42 ? 122  ARG B C     1 
ATOM   9858  O  O     . ARG B  1  124  ? 2.065   52.398  132.653 1.00 51.96 ? 122  ARG B O     1 
ATOM   9859  C  CB    . ARG B  1  124  ? 1.446   49.643  134.316 1.00 49.23 ? 122  ARG B CB    1 
ATOM   9860  N  N     . ASP B  1  125  ? 3.798   50.969  132.573 1.00 48.62 ? 123  ASP B N     1 
ATOM   9861  C  CA    . ASP B  1  125  ? 4.805   52.016  132.663 1.00 52.02 ? 123  ASP B CA    1 
ATOM   9862  C  C     . ASP B  1  125  ? 5.356   52.470  131.315 1.00 43.22 ? 123  ASP B C     1 
ATOM   9863  O  O     . ASP B  1  125  ? 6.012   53.514  131.260 1.00 50.61 ? 123  ASP B O     1 
ATOM   9864  C  CB    . ASP B  1  125  ? 5.961   51.551  133.558 1.00 55.07 ? 123  ASP B CB    1 
ATOM   9865  C  CG    . ASP B  1  125  ? 5.484   51.053  134.909 1.00 56.73 ? 123  ASP B CG    1 
ATOM   9866  O  OD1   . ASP B  1  125  ? 4.479   51.590  135.423 1.00 57.33 ? 123  ASP B OD1   1 
ATOM   9867  O  OD2   . ASP B  1  125  ? 6.111   50.120  135.457 1.00 61.49 ? 123  ASP B OD2   1 
ATOM   9868  N  N     . LYS B  1  126  ? 5.112   51.738  130.237 1.00 46.26 ? 124  LYS B N     1 
ATOM   9869  C  CA    . LYS B  1  126  ? 5.678   52.166  128.963 1.00 46.15 ? 124  LYS B CA    1 
ATOM   9870  C  C     . LYS B  1  126  ? 4.687   52.109  127.810 1.00 47.14 ? 124  LYS B C     1 
ATOM   9871  O  O     . LYS B  1  126  ? 4.652   53.034  126.995 1.00 51.84 ? 124  LYS B O     1 
ATOM   9872  C  CB    . LYS B  1  126  ? 6.913   51.311  128.625 1.00 49.33 ? 124  LYS B CB    1 
ATOM   9873  N  N     . ILE B  1  127  ? 3.883   51.050  127.718 1.00 43.73 ? 125  ILE B N     1 
ATOM   9874  C  CA    . ILE B  1  127  ? 2.994   50.902  126.569 1.00 41.96 ? 125  ILE B CA    1 
ATOM   9875  C  C     . ILE B  1  127  ? 1.777   51.806  126.707 1.00 43.32 ? 125  ILE B C     1 
ATOM   9876  O  O     . ILE B  1  127  ? 1.364   52.463  125.744 1.00 43.33 ? 125  ILE B O     1 
ATOM   9877  C  CB    . ILE B  1  127  ? 2.570   49.434  126.390 1.00 34.65 ? 125  ILE B CB    1 
ATOM   9878  C  CG1   . ILE B  1  127  ? 3.789   48.505  126.361 1.00 37.77 ? 125  ILE B CG1   1 
ATOM   9879  C  CG2   . ILE B  1  127  ? 1.750   49.281  125.112 1.00 35.00 ? 125  ILE B CG2   1 
ATOM   9880  C  CD1   . ILE B  1  127  ? 4.809   48.870  125.319 1.00 39.63 ? 125  ILE B CD1   1 
ATOM   9881  N  N     . ALA B  1  128  ? 1.171   51.838  127.898 1.00 38.75 ? 126  ALA B N     1 
ATOM   9882  C  CA    . ALA B  1  128  ? -0.051  52.612  128.088 1.00 39.73 ? 126  ALA B CA    1 
ATOM   9883  C  C     . ALA B  1  128  ? 0.171   54.101  127.871 1.00 47.95 ? 126  ALA B C     1 
ATOM   9884  O  O     . ALA B  1  128  ? -0.792  54.828  127.605 1.00 49.25 ? 126  ALA B O     1 
ATOM   9885  C  CB    . ALA B  1  128  ? -0.627  52.361  129.482 1.00 42.36 ? 126  ALA B CB    1 
ATOM   9886  N  N     . ASP B  1  129  ? 1.416   54.567  127.971 1.00 53.45 ? 127  ASP B N     1 
ATOM   9887  C  CA    . ASP B  1  129  ? 1.776   55.939  127.652 1.00 59.29 ? 127  ASP B CA    1 
ATOM   9888  C  C     . ASP B  1  129  ? 2.086   56.130  126.171 1.00 59.13 ? 127  ASP B C     1 
ATOM   9889  O  O     . ASP B  1  129  ? 2.775   57.090  125.808 1.00 69.06 ? 127  ASP B O     1 
ATOM   9890  C  CB    . ASP B  1  129  ? 2.969   56.382  128.504 1.00 59.04 ? 127  ASP B CB    1 
ATOM   9891  N  N     . GLY B  1  130  ? 1.602   55.233  125.311 1.00 59.25 ? 128  GLY B N     1 
ATOM   9892  C  CA    . GLY B  1  130  ? 1.820   55.327  123.881 1.00 54.97 ? 128  GLY B CA    1 
ATOM   9893  C  C     . GLY B  1  130  ? 3.223   55.025  123.403 1.00 60.15 ? 128  GLY B C     1 
ATOM   9894  O  O     . GLY B  1  130  ? 3.421   54.867  122.192 1.00 57.43 ? 128  GLY B O     1 
ATOM   9895  N  N     . ASN B  1  131  ? 4.206   54.925  124.299 1.00 66.91 ? 129  ASN B N     1 
ATOM   9896  C  CA    . ASN B  1  131  ? 5.586   54.687  123.892 1.00 64.19 ? 129  ASN B CA    1 
ATOM   9897  C  C     . ASN B  1  131  ? 5.787   53.242  123.452 1.00 61.90 ? 129  ASN B C     1 
ATOM   9898  O  O     . ASN B  1  131  ? 6.745   52.585  123.873 1.00 68.24 ? 129  ASN B O     1 
ATOM   9899  C  CB    . ASN B  1  131  ? 6.546   55.031  125.034 1.00 65.70 ? 129  ASN B CB    1 
ATOM   9900  N  N     . TRP B  1  132  ? 4.895   52.739  122.597 1.00 54.77 ? 130  TRP B N     1 
ATOM   9901  C  CA    . TRP B  1  132  ? 4.953   51.338  122.205 1.00 47.72 ? 130  TRP B CA    1 
ATOM   9902  C  C     . TRP B  1  132  ? 5.979   51.091  121.108 1.00 49.23 ? 130  TRP B C     1 
ATOM   9903  O  O     . TRP B  1  132  ? 6.583   50.014  121.065 1.00 54.72 ? 130  TRP B O     1 
ATOM   9904  C  CB    . TRP B  1  132  ? 3.565   50.857  121.763 1.00 45.82 ? 130  TRP B CB    1 
ATOM   9905  C  CG    . TRP B  1  132  ? 3.023   51.525  120.529 1.00 39.82 ? 130  TRP B CG    1 
ATOM   9906  C  CD1   . TRP B  1  132  ? 2.179   52.596  120.474 1.00 37.78 ? 130  TRP B CD1   1 
ATOM   9907  C  CD2   . TRP B  1  132  ? 3.286   51.151  119.173 1.00 37.11 ? 130  TRP B CD2   1 
ATOM   9908  N  NE1   . TRP B  1  132  ? 1.898   52.914  119.164 1.00 36.32 ? 130  TRP B NE1   1 
ATOM   9909  C  CE2   . TRP B  1  132  ? 2.567   52.042  118.345 1.00 33.88 ? 130  TRP B CE2   1 
ATOM   9910  C  CE3   . TRP B  1  132  ? 4.053   50.148  118.580 1.00 34.03 ? 130  TRP B CE3   1 
ATOM   9911  C  CZ2   . TRP B  1  132  ? 2.602   51.960  116.959 1.00 29.94 ? 130  TRP B CZ2   1 
ATOM   9912  C  CZ3   . TRP B  1  132  ? 4.090   50.069  117.204 1.00 30.50 ? 130  TRP B CZ3   1 
ATOM   9913  C  CH2   . TRP B  1  132  ? 3.364   50.968  116.406 1.00 28.89 ? 130  TRP B CH2   1 
ATOM   9914  N  N     . LYS B  1  133  ? 6.190   52.063  120.217 1.00 51.18 ? 131  LYS B N     1 
ATOM   9915  C  CA    . LYS B  1  133  ? 7.156   51.873  119.140 1.00 56.35 ? 131  LYS B CA    1 
ATOM   9916  C  C     . LYS B  1  133  ? 8.559   51.647  119.692 1.00 62.91 ? 131  LYS B C     1 
ATOM   9917  O  O     . LYS B  1  133  ? 9.326   50.838  119.155 1.00 62.99 ? 131  LYS B O     1 
ATOM   9918  C  CB    . LYS B  1  133  ? 7.131   53.077  118.196 1.00 48.15 ? 131  LYS B CB    1 
ATOM   9919  N  N     . SER B  1  134  ? 8.904   52.336  120.774 1.00 68.97 ? 132  SER B N     1 
ATOM   9920  C  CA    . SER B  1  134  ? 10.238  52.267  121.371 1.00 69.75 ? 132  SER B CA    1 
ATOM   9921  C  C     . SER B  1  134  ? 10.271  51.317  122.562 1.00 65.79 ? 132  SER B C     1 
ATOM   9922  O  O     . SER B  1  134  ? 10.783  51.663  123.627 1.00 75.38 ? 132  SER B O     1 
ATOM   9923  C  CB    . SER B  1  134  ? 10.697  53.663  121.778 1.00 58.56 ? 132  SER B CB    1 
ATOM   9924  N  N     . HIS B  1  135  ? 9.734   50.106  122.403 1.00 61.99 ? 133  HIS B N     1 
ATOM   9925  C  CA    . HIS B  1  135  ? 9.698   49.160  123.514 1.00 64.16 ? 133  HIS B CA    1 
ATOM   9926  C  C     . HIS B  1  135  ? 9.369   47.745  123.053 1.00 64.53 ? 133  HIS B C     1 
ATOM   9927  O  O     . HIS B  1  135  ? 9.516   46.790  123.824 1.00 65.48 ? 133  HIS B O     1 
ATOM   9928  C  CB    . HIS B  1  135  ? 8.685   49.614  124.570 1.00 54.21 ? 133  HIS B CB    1 
ATOM   9929  N  N     . LEU B  1  136  ? 8.914   47.597  121.812 1.00 61.86 ? 134  LEU B N     1 
ATOM   9930  C  CA    . LEU B  1  136  ? 8.596   46.279  121.268 1.00 52.83 ? 134  LEU B CA    1 
ATOM   9931  C  C     . LEU B  1  136  ? 8.974   46.193  119.793 1.00 50.95 ? 134  LEU B C     1 
ATOM   9932  O  O     . LEU B  1  136  ? 8.836   45.141  119.170 1.00 54.23 ? 134  LEU B O     1 
ATOM   9933  C  CB    . LEU B  1  136  ? 7.108   45.959  121.451 1.00 45.84 ? 134  LEU B CB    1 
ATOM   9934  C  CG    . LEU B  1  136  ? 6.577   45.741  122.871 1.00 44.37 ? 134  LEU B CG    1 
ATOM   9935  C  CD1   . LEU B  1  136  ? 5.069   45.622  122.851 1.00 37.83 ? 134  LEU B CD1   1 
ATOM   9936  C  CD2   . LEU B  1  136  ? 7.199   44.507  123.514 1.00 46.46 ? 134  LEU B CD2   1 
ATOM   9937  N  N     . ARG B  1  140  ? 12.116  44.320  114.369 1.00 40.47 ? 138  ARG B N     1 
ATOM   9938  C  CA    . ARG B  1  140  ? 10.991  43.512  113.908 1.00 49.09 ? 138  ARG B CA    1 
ATOM   9939  C  C     . ARG B  1  140  ? 9.665   44.237  114.136 1.00 49.29 ? 138  ARG B C     1 
ATOM   9940  O  O     . ARG B  1  140  ? 9.360   44.667  115.251 1.00 35.66 ? 138  ARG B O     1 
ATOM   9941  C  CB    . ARG B  1  140  ? 10.977  42.152  114.613 1.00 45.24 ? 138  ARG B CB    1 
ATOM   9942  N  N     . SER B  1  141  ? 8.886   44.371  113.067 1.00 35.41 ? 139  SER B N     1 
ATOM   9943  C  CA    . SER B  1  141  ? 7.607   45.059  113.158 1.00 28.25 ? 139  SER B CA    1 
ATOM   9944  C  C     . SER B  1  141  ? 6.683   44.345  114.137 1.00 32.64 ? 139  SER B C     1 
ATOM   9945  O  O     . SER B  1  141  ? 6.639   43.114  114.202 1.00 30.36 ? 139  SER B O     1 
ATOM   9946  C  CB    . SER B  1  141  ? 6.955   45.139  111.774 1.00 32.79 ? 139  SER B CB    1 
ATOM   9947  O  OG    . SER B  1  141  ? 5.629   45.653  111.844 1.00 35.19 ? 139  SER B OG    1 
ATOM   9948  N  N     . LEU B  1  142  ? 5.944   45.133  114.913 1.00 27.83 ? 140  LEU B N     1 
ATOM   9949  C  CA    . LEU B  1  142  ? 4.877   44.574  115.728 1.00 25.19 ? 140  LEU B CA    1 
ATOM   9950  C  C     . LEU B  1  142  ? 3.846   43.828  114.893 1.00 25.01 ? 140  LEU B C     1 
ATOM   9951  O  O     . LEU B  1  142  ? 3.111   42.986  115.424 1.00 23.25 ? 140  LEU B O     1 
ATOM   9952  C  CB    . LEU B  1  142  ? 4.181   45.701  116.483 1.00 27.02 ? 140  LEU B CB    1 
ATOM   9953  C  CG    . LEU B  1  142  ? 3.595   45.301  117.817 1.00 31.01 ? 140  LEU B CG    1 
ATOM   9954  C  CD1   . LEU B  1  142  ? 4.705   45.274  118.822 1.00 33.49 ? 140  LEU B CD1   1 
ATOM   9955  C  CD2   . LEU B  1  142  ? 2.550   46.290  118.199 1.00 34.55 ? 140  LEU B CD2   1 
ATOM   9956  N  N     . PHE B  1  143  ? 3.760   44.138  113.599 1.00 21.56 ? 141  PHE B N     1 
ATOM   9957  C  CA    . PHE B  1  143  ? 2.650   43.713  112.763 1.00 21.24 ? 141  PHE B CA    1 
ATOM   9958  C  C     . PHE B  1  143  ? 3.021   42.593  111.796 1.00 23.81 ? 141  PHE B C     1 
ATOM   9959  O  O     . PHE B  1  143  ? 2.289   42.352  110.832 1.00 22.58 ? 141  PHE B O     1 
ATOM   9960  C  CB    . PHE B  1  143  ? 2.104   44.929  112.016 1.00 20.25 ? 141  PHE B CB    1 
ATOM   9961  C  CG    . PHE B  1  143  ? 1.774   46.072  112.927 1.00 20.46 ? 141  PHE B CG    1 
ATOM   9962  C  CD1   . PHE B  1  143  ? 0.827   45.924  113.933 1.00 20.47 ? 141  PHE B CD1   1 
ATOM   9963  C  CD2   . PHE B  1  143  ? 2.437   47.284  112.807 1.00 21.24 ? 141  PHE B CD2   1 
ATOM   9964  C  CE1   . PHE B  1  143  ? 0.541   46.966  114.786 1.00 22.56 ? 141  PHE B CE1   1 
ATOM   9965  C  CE2   . PHE B  1  143  ? 2.155   48.329  113.655 1.00 20.25 ? 141  PHE B CE2   1 
ATOM   9966  C  CZ    . PHE B  1  143  ? 1.208   48.185  114.643 1.00 21.63 ? 141  PHE B CZ    1 
ATOM   9967  N  N     . VAL B  1  144  ? 4.107   41.864  112.075 1.00 24.76 ? 142  VAL B N     1 
ATOM   9968  C  CA    A VAL B  1  144  ? 4.555   40.781  111.197 0.61 25.31 ? 142  VAL B CA    1 
ATOM   9969  C  CA    B VAL B  1  144  ? 4.546   40.801  111.174 0.39 25.32 ? 142  VAL B CA    1 
ATOM   9970  C  C     . VAL B  1  144  ? 3.427   39.791  110.930 1.00 22.89 ? 142  VAL B C     1 
ATOM   9971  O  O     . VAL B  1  144  ? 3.255   39.303  109.808 1.00 26.95 ? 142  VAL B O     1 
ATOM   9972  C  CB    A VAL B  1  144  ? 5.786   40.083  111.810 0.61 25.81 ? 142  VAL B CB    1 
ATOM   9973  C  CB    B VAL B  1  144  ? 5.820   40.121  111.714 0.39 25.88 ? 142  VAL B CB    1 
ATOM   9974  C  CG1   A VAL B  1  144  ? 6.159   38.842  111.017 0.61 26.68 ? 142  VAL B CG1   1 
ATOM   9975  C  CG1   B VAL B  1  144  ? 6.980   41.103  111.714 0.39 31.04 ? 142  VAL B CG1   1 
ATOM   9976  C  CG2   A VAL B  1  144  ? 6.958   41.043  111.860 0.61 31.27 ? 142  VAL B CG2   1 
ATOM   9977  C  CG2   B VAL B  1  144  ? 5.592   39.558  113.107 0.39 26.23 ? 142  VAL B CG2   1 
ATOM   9978  N  N     . ASN B  1  145  ? 2.637   39.474  111.958 1.00 24.04 ? 143  ASN B N     1 
ATOM   9979  C  CA    . ASN B  1  145  ? 1.579   38.479  111.822 1.00 24.78 ? 143  ASN B CA    1 
ATOM   9980  C  C     . ASN B  1  145  ? 0.200   39.107  111.689 1.00 26.05 ? 143  ASN B C     1 
ATOM   9981  O  O     . ASN B  1  145  ? -0.806  38.458  111.988 1.00 24.78 ? 143  ASN B O     1 
ATOM   9982  C  CB    . ASN B  1  145  ? 1.604   37.512  113.004 1.00 26.05 ? 143  ASN B CB    1 
ATOM   9983  C  CG    . ASN B  1  145  ? 2.712   36.494  112.890 1.00 32.33 ? 143  ASN B CG    1 
ATOM   9984  O  OD1   . ASN B  1  145  ? 2.908   35.889  111.833 1.00 37.31 ? 143  ASN B OD1   1 
ATOM   9985  N  ND2   . ASN B  1  145  ? 3.451   36.301  113.975 1.00 30.68 ? 143  ASN B ND2   1 
ATOM   9986  N  N     . ALA B  1  146  ? 0.126   40.354  111.222 1.00 24.42 ? 144  ALA B N     1 
ATOM   9987  C  CA    . ALA B  1  146  ? -1.166  41.029  111.180 1.00 24.79 ? 144  ALA B CA    1 
ATOM   9988  C  C     . ALA B  1  146  ? -2.121  40.422  110.157 1.00 20.93 ? 144  ALA B C     1 
ATOM   9989  O  O     . ALA B  1  146  ? -3.340  40.578  110.299 1.00 25.72 ? 144  ALA B O     1 
ATOM   9990  C  CB    . ALA B  1  146  ? -0.968  42.518  110.891 1.00 24.02 ? 144  ALA B CB    1 
ATOM   9991  N  N     . ALA B  1  147  ? -1.615  39.760  109.116 1.00 25.31 ? 145  ALA B N     1 
ATOM   9992  C  CA    . ALA B  1  147  ? -2.531  39.089  108.200 1.00 22.99 ? 145  ALA B CA    1 
ATOM   9993  C  C     . ALA B  1  147  ? -3.308  38.009  108.935 1.00 27.25 ? 145  ALA B C     1 
ATOM   9994  O  O     . ALA B  1  147  ? -4.507  37.822  108.703 1.00 25.66 ? 145  ALA B O     1 
ATOM   9995  C  CB    . ALA B  1  147  ? -1.772  38.503  107.012 1.00 25.17 ? 145  ALA B CB    1 
ATOM   9996  N  N     . THR B  1  148  ? -2.644  37.311  109.852 1.00 25.72 ? 146  THR B N     1 
ATOM   9997  C  CA    . THR B  1  148  ? -3.325  36.291  110.634 1.00 25.12 ? 146  THR B CA    1 
ATOM   9998  C  C     . THR B  1  148  ? -4.379  36.915  111.541 1.00 26.60 ? 146  THR B C     1 
ATOM   9999  O  O     . THR B  1  148  ? -5.536  36.486  111.547 1.00 29.63 ? 146  THR B O     1 
ATOM   10000 C  CB    . THR B  1  148  ? -2.303  35.493  111.439 1.00 31.82 ? 146  THR B CB    1 
ATOM   10001 O  OG1   . THR B  1  148  ? -1.400  34.857  110.526 1.00 33.48 ? 146  THR B OG1   1 
ATOM   10002 C  CG2   . THR B  1  148  ? -2.997  34.438  112.288 1.00 32.76 ? 146  THR B CG2   1 
ATOM   10003 N  N     . TRP B  1  149  ? -4.007  37.951  112.295 1.00 24.23 ? 147  TRP B N     1 
ATOM   10004 C  CA    . TRP B  1  149  ? -4.992  38.600  113.150 1.00 22.95 ? 147  TRP B CA    1 
ATOM   10005 C  C     . TRP B  1  149  ? -6.071  39.291  112.330 1.00 23.83 ? 147  TRP B C     1 
ATOM   10006 O  O     . TRP B  1  149  ? -7.214  39.394  112.783 1.00 25.24 ? 147  TRP B O     1 
ATOM   10007 C  CB    . TRP B  1  149  ? -4.317  39.589  114.097 1.00 24.65 ? 147  TRP B CB    1 
ATOM   10008 C  CG    . TRP B  1  149  ? -3.401  38.897  115.052 1.00 24.53 ? 147  TRP B CG    1 
ATOM   10009 C  CD1   . TRP B  1  149  ? -2.047  38.996  115.099 1.00 23.52 ? 147  TRP B CD1   1 
ATOM   10010 C  CD2   . TRP B  1  149  ? -3.775  37.947  116.049 1.00 27.84 ? 147  TRP B CD2   1 
ATOM   10011 N  NE1   . TRP B  1  149  ? -1.548  38.190  116.096 1.00 24.56 ? 147  TRP B NE1   1 
ATOM   10012 C  CE2   . TRP B  1  149  ? -2.590  37.532  116.692 1.00 27.15 ? 147  TRP B CE2   1 
ATOM   10013 C  CE3   . TRP B  1  149  ? -4.998  37.419  116.477 1.00 30.14 ? 147  TRP B CE3   1 
ATOM   10014 C  CZ2   . TRP B  1  149  ? -2.590  36.611  117.741 1.00 30.33 ? 147  TRP B CZ2   1 
ATOM   10015 C  CZ3   . TRP B  1  149  ? -4.997  36.501  117.528 1.00 31.49 ? 147  TRP B CZ3   1 
ATOM   10016 C  CH2   . TRP B  1  149  ? -3.799  36.110  118.142 1.00 32.79 ? 147  TRP B CH2   1 
ATOM   10017 N  N     . GLY B  1  150  ? -5.729  39.768  111.134 1.00 21.63 ? 148  GLY B N     1 
ATOM   10018 C  CA    . GLY B  1  150  ? -6.754  40.277  110.235 1.00 25.19 ? 148  GLY B CA    1 
ATOM   10019 C  C     . GLY B  1  150  ? -7.814  39.237  109.928 1.00 27.54 ? 148  GLY B C     1 
ATOM   10020 O  O     . GLY B  1  150  ? -9.012  39.539  109.895 1.00 27.32 ? 148  GLY B O     1 
ATOM   10021 N  N     . LEU B  1  151  ? -7.389  37.996  109.694 1.00 27.59 ? 149  LEU B N     1 
ATOM   10022 C  CA    A LEU B  1  151  ? -8.351  36.918  109.493 0.54 30.24 ? 149  LEU B CA    1 
ATOM   10023 C  CA    B LEU B  1  151  ? -8.348  36.917  109.492 0.46 30.25 ? 149  LEU B CA    1 
ATOM   10024 C  C     . LEU B  1  151  ? -9.193  36.703  110.741 1.00 32.18 ? 149  LEU B C     1 
ATOM   10025 O  O     . LEU B  1  151  ? -10.414 36.529  110.655 1.00 33.90 ? 149  LEU B O     1 
ATOM   10026 C  CB    A LEU B  1  151  ? -7.624  35.630  109.111 0.54 33.04 ? 149  LEU B CB    1 
ATOM   10027 C  CB    B LEU B  1  151  ? -7.606  35.639  109.106 0.46 33.04 ? 149  LEU B CB    1 
ATOM   10028 C  CG    A LEU B  1  151  ? -7.802  35.159  107.669 0.54 34.39 ? 149  LEU B CG    1 
ATOM   10029 C  CG    B LEU B  1  151  ? -8.319  34.589  108.257 0.46 37.51 ? 149  LEU B CG    1 
ATOM   10030 C  CD1   A LEU B  1  151  ? -6.982  33.907  107.428 0.54 38.39 ? 149  LEU B CD1   1 
ATOM   10031 C  CD1   B LEU B  1  151  ? -9.236  35.241  107.238 0.46 36.82 ? 149  LEU B CD1   1 
ATOM   10032 C  CD2   A LEU B  1  151  ? -9.275  34.902  107.368 0.54 36.99 ? 149  LEU B CD2   1 
ATOM   10033 C  CD2   B LEU B  1  151  ? -7.277  33.740  107.553 0.46 38.47 ? 149  LEU B CD2   1 
ATOM   10034 N  N     . VAL B  1  152  ? -8.560  36.731  111.913 1.00 28.18 ? 150  VAL B N     1 
ATOM   10035 C  CA    . VAL B  1  152  ? -9.288  36.525  113.160 1.00 31.30 ? 150  VAL B CA    1 
ATOM   10036 C  C     . VAL B  1  152  ? -10.330 37.617  113.366 1.00 32.68 ? 150  VAL B C     1 
ATOM   10037 O  O     . VAL B  1  152  ? -11.469 37.344  113.762 1.00 37.14 ? 150  VAL B O     1 
ATOM   10038 C  CB    . VAL B  1  152  ? -8.304  36.468  114.341 1.00 27.96 ? 150  VAL B CB    1 
ATOM   10039 C  CG1   . VAL B  1  152  ? -9.051  36.532  115.654 1.00 36.08 ? 150  VAL B CG1   1 
ATOM   10040 C  CG2   . VAL B  1  152  ? -7.457  35.218  114.263 1.00 34.74 ? 150  VAL B CG2   1 
ATOM   10041 N  N     . VAL B  1  153  ? -9.961  38.867  113.096 1.00 29.89 ? 151  VAL B N     1 
ATOM   10042 C  CA    . VAL B  1  153  ? -10.807 39.997  113.470 1.00 29.33 ? 151  VAL B CA    1 
ATOM   10043 C  C     . VAL B  1  153  ? -11.879 40.258  112.422 1.00 28.51 ? 151  VAL B C     1 
ATOM   10044 O  O     . VAL B  1  153  ? -13.033 40.539  112.761 1.00 31.91 ? 151  VAL B O     1 
ATOM   10045 C  CB    . VAL B  1  153  ? -9.927  41.241  113.697 1.00 29.14 ? 151  VAL B CB    1 
ATOM   10046 C  CG1   . VAL B  1  153  ? -10.791 42.482  113.911 1.00 30.57 ? 151  VAL B CG1   1 
ATOM   10047 C  CG2   . VAL B  1  153  ? -9.009  41.012  114.868 1.00 26.62 ? 151  VAL B CG2   1 
ATOM   10048 N  N     . THR B  1  154  ? -11.513 40.197  111.141 1.00 28.56 ? 152  THR B N     1 
ATOM   10049 C  CA    . THR B  1  154  ? -12.397 40.597  110.057 1.00 31.79 ? 152  THR B CA    1 
ATOM   10050 C  C     . THR B  1  154  ? -12.934 39.433  109.248 1.00 33.71 ? 152  THR B C     1 
ATOM   10051 O  O     . THR B  1  154  ? -13.905 39.615  108.512 1.00 38.89 ? 152  THR B O     1 
ATOM   10052 C  CB    . THR B  1  154  ? -11.669 41.536  109.080 1.00 32.34 ? 152  THR B CB    1 
ATOM   10053 O  OG1   . THR B  1  154  ? -10.722 40.779  108.317 1.00 32.19 ? 152  THR B OG1   1 
ATOM   10054 C  CG2   . THR B  1  154  ? -10.936 42.636  109.821 1.00 36.17 ? 152  THR B CG2   1 
ATOM   10055 N  N     . GLY B  1  155  ? -12.308 38.260  109.334 1.00 28.54 ? 153  GLY B N     1 
ATOM   10056 C  CA    . GLY B  1  155  ? -12.667 37.161  108.468 1.00 30.65 ? 153  GLY B CA    1 
ATOM   10057 C  C     . GLY B  1  155  ? -12.110 37.253  107.068 1.00 37.96 ? 153  GLY B C     1 
ATOM   10058 O  O     . GLY B  1  155  ? -12.384 36.365  106.250 1.00 39.31 ? 153  GLY B O     1 
ATOM   10059 N  N     . LYS B  1  156  ? -11.344 38.293  106.763 1.00 32.59 ? 154  LYS B N     1 
ATOM   10060 C  CA    . LYS B  1  156  ? -10.748 38.471  105.451 1.00 34.27 ? 154  LYS B CA    1 
ATOM   10061 C  C     . LYS B  1  156  ? -9.236  38.352  105.561 1.00 33.16 ? 154  LYS B C     1 
ATOM   10062 O  O     . LYS B  1  156  ? -8.634  38.722  106.575 1.00 29.72 ? 154  LYS B O     1 
ATOM   10063 C  CB    . LYS B  1  156  ? -11.129 39.825  104.843 1.00 38.59 ? 154  LYS B CB    1 
ATOM   10064 N  N     . LEU B  1  157  ? -8.630  37.809  104.514 1.00 33.08 ? 155  LEU B N     1 
ATOM   10065 C  CA    . LEU B  1  157  ? -7.190  37.632  104.440 1.00 35.63 ? 155  LEU B CA    1 
ATOM   10066 C  C     . LEU B  1  157  ? -6.603  38.646  103.471 1.00 42.76 ? 155  LEU B C     1 
ATOM   10067 O  O     . LEU B  1  157  ? -7.121  38.828  102.365 1.00 43.22 ? 155  LEU B O     1 
ATOM   10068 C  CB    . LEU B  1  157  ? -6.830  36.217  103.985 1.00 42.09 ? 155  LEU B CB    1 
ATOM   10069 C  CG    . LEU B  1  157  ? -5.334  35.945  103.799 1.00 42.77 ? 155  LEU B CG    1 
ATOM   10070 C  CD1   . LEU B  1  157  ? -4.609  35.982  105.138 1.00 43.43 ? 155  LEU B CD1   1 
ATOM   10071 C  CD2   . LEU B  1  157  ? -5.109  34.611  103.098 1.00 47.43 ? 155  LEU B CD2   1 
ATOM   10072 N  N     . THR B  1  158  ? -5.533  39.307  103.892 1.00 43.17 ? 156  THR B N     1 
ATOM   10073 C  CA    . THR B  1  158  ? -4.685  40.074  102.996 1.00 45.76 ? 156  THR B CA    1 
ATOM   10074 C  C     . THR B  1  158  ? -3.310  39.427  102.983 1.00 43.11 ? 156  THR B C     1 
ATOM   10075 O  O     . THR B  1  158  ? -2.887  38.821  103.972 1.00 45.57 ? 156  THR B O     1 
ATOM   10076 C  CB    . THR B  1  158  ? -4.572  41.531  103.431 1.00 53.37 ? 156  THR B CB    1 
ATOM   10077 O  OG1   . THR B  1  158  ? -3.670  41.621  104.541 1.00 52.45 ? 156  THR B OG1   1 
ATOM   10078 C  CG2   . THR B  1  158  ? -5.937  42.069  103.847 1.00 47.30 ? 156  THR B CG2   1 
ATOM   10079 N  N     . SER B  1  159  ? -2.613  39.541  101.858 1.00 35.58 ? 157  SER B N     1 
ATOM   10080 C  CA    . SER B  1  159  ? -1.309  38.900  101.761 1.00 34.25 ? 157  SER B CA    1 
ATOM   10081 C  C     . SER B  1  159  ? -0.227  39.721  102.444 1.00 34.96 ? 157  SER B C     1 
ATOM   10082 O  O     . SER B  1  159  ? 0.714   39.160  103.016 1.00 33.23 ? 157  SER B O     1 
ATOM   10083 C  CB    . SER B  1  159  ? -0.946  38.672  100.293 1.00 44.21 ? 157  SER B CB    1 
ATOM   10084 O  OG    . SER B  1  159  ? -1.723  39.508  99.451  1.00 46.58 ? 157  SER B OG    1 
ATOM   10085 N  N     . THR B  1  160  ? -0.345  41.039  102.394 1.00 32.49 ? 158  THR B N     1 
ATOM   10086 C  CA    . THR B  1  160  ? 0.599   41.919  103.052 1.00 24.65 ? 158  THR B CA    1 
ATOM   10087 C  C     . THR B  1  160  ? -0.174  42.861  103.960 1.00 23.98 ? 158  THR B C     1 
ATOM   10088 O  O     . THR B  1  160  ? -1.403  42.960  103.904 1.00 28.04 ? 158  THR B O     1 
ATOM   10089 C  CB    . THR B  1  160  ? 1.440   42.707  102.038 1.00 26.09 ? 158  THR B CB    1 
ATOM   10090 O  OG1   . THR B  1  160  ? 0.571   43.433  101.171 1.00 30.00 ? 158  THR B OG1   1 
ATOM   10091 C  CG2   . THR B  1  160  ? 2.314   41.769  101.214 1.00 29.08 ? 158  THR B CG2   1 
ATOM   10092 N  N     . VAL B  1  161  ? 0.576   43.562  104.797 1.00 19.24 ? 159  VAL B N     1 
ATOM   10093 C  CA    . VAL B  1  161  ? 0.048   44.269  105.951 1.00 24.51 ? 159  VAL B CA    1 
ATOM   10094 C  C     . VAL B  1  161  ? 0.245   45.758  105.729 1.00 21.54 ? 159  VAL B C     1 
ATOM   10095 O  O     . VAL B  1  161  ? 1.341   46.184  105.352 1.00 21.84 ? 159  VAL B O     1 
ATOM   10096 C  CB    . VAL B  1  161  ? 0.769   43.781  107.219 1.00 26.91 ? 159  VAL B CB    1 
ATOM   10097 C  CG1   . VAL B  1  161  ? 0.735   44.798  108.315 1.00 32.29 ? 159  VAL B CG1   1 
ATOM   10098 C  CG2   . VAL B  1  161  ? 0.173   42.448  107.645 1.00 36.97 ? 159  VAL B CG2   1 
ATOM   10099 N  N     . ASN B  1  162  ? -0.811  46.548  105.931 1.00 20.74 ? 160  ASN B N     1 
ATOM   10100 C  CA    . ASN B  1  162  ? -0.631  47.998  105.890 1.00 20.67 ? 160  ASN B CA    1 
ATOM   10101 C  C     . ASN B  1  162  ? -0.133  48.425  107.263 1.00 19.12 ? 160  ASN B C     1 
ATOM   10102 O  O     . ASN B  1  162  ? -0.906  48.762  108.160 1.00 19.01 ? 160  ASN B O     1 
ATOM   10103 C  CB    . ASN B  1  162  ? -1.909  48.722  105.491 1.00 21.58 ? 160  ASN B CB    1 
ATOM   10104 C  CG    . ASN B  1  162  ? -1.689  50.218  105.343 1.00 19.73 ? 160  ASN B CG    1 
ATOM   10105 O  OD1   . ASN B  1  162  ? -0.754  50.769  105.918 1.00 21.38 ? 160  ASN B OD1   1 
ATOM   10106 N  ND2   . ASN B  1  162  ? -2.551  50.880  104.588 1.00 24.36 ? 160  ASN B ND2   1 
ATOM   10107 N  N     . ASP B  1  163  ? 1.194   48.411  107.421 1.00 20.10 ? 161  ASP B N     1 
ATOM   10108 C  CA    . ASP B  1  163  ? 1.785   48.690  108.720 1.00 19.75 ? 161  ASP B CA    1 
ATOM   10109 C  C     . ASP B  1  163  ? 1.666   50.150  109.113 1.00 18.57 ? 161  ASP B C     1 
ATOM   10110 O  O     . ASP B  1  163  ? 1.704   50.451  110.310 1.00 19.46 ? 161  ASP B O     1 
ATOM   10111 C  CB    . ASP B  1  163  ? 3.249   48.234  108.766 1.00 20.50 ? 161  ASP B CB    1 
ATOM   10112 C  CG    . ASP B  1  163  ? 4.082   48.738  107.594 1.00 21.43 ? 161  ASP B CG    1 
ATOM   10113 O  OD1   . ASP B  1  163  ? 3.622   48.704  106.440 1.00 20.76 ? 161  ASP B OD1   1 
ATOM   10114 O  OD2   . ASP B  1  163  ? 5.226   49.159  107.855 1.00 25.26 ? 161  ASP B OD2   1 
ATOM   10115 N  N     . ARG B  1  164  ? 1.505   51.071  108.157 1.00 18.03 ? 162  ARG B N     1 
ATOM   10116 C  CA    . ARG B  1  164  ? 1.257   52.450  108.575 1.00 17.72 ? 162  ARG B CA    1 
ATOM   10117 C  C     . ARG B  1  164  ? -0.150  52.616  109.132 1.00 16.04 ? 162  ARG B C     1 
ATOM   10118 O  O     . ARG B  1  164  ? -0.356  53.345  110.111 1.00 17.06 ? 162  ARG B O     1 
ATOM   10119 C  CB    . ARG B  1  164  ? 1.491   53.418  107.416 1.00 17.26 ? 162  ARG B CB    1 
ATOM   10120 C  CG    . ARG B  1  164  ? 2.922   53.437  106.907 1.00 19.08 ? 162  ARG B CG    1 
ATOM   10121 C  CD    . ARG B  1  164  ? 3.933   53.493  108.037 1.00 28.14 ? 162  ARG B CD    1 
ATOM   10122 N  NE    . ARG B  1  164  ? 3.655   54.553  108.990 1.00 35.60 ? 162  ARG B NE    1 
ATOM   10123 C  CZ    . ARG B  1  164  ? 4.097   54.555  110.239 1.00 39.03 ? 162  ARG B CZ    1 
ATOM   10124 N  NH1   . ARG B  1  164  ? 4.823   53.555  110.716 1.00 38.58 ? 162  ARG B NH1   1 
ATOM   10125 N  NH2   . ARG B  1  164  ? 3.799   55.580  111.029 1.00 36.40 ? 162  ARG B NH2   1 
ATOM   10126 N  N     . SER B  1  165  ? -1.132  51.955  108.511 1.00 19.08 ? 163  SER B N     1 
ATOM   10127 C  CA    . SER B  1  165  ? -2.496  51.993  109.024 1.00 17.00 ? 163  SER B CA    1 
ATOM   10128 C  C     . SER B  1  165  ? -2.574  51.339  110.394 1.00 17.96 ? 163  SER B C     1 
ATOM   10129 O  O     . SER B  1  165  ? -3.231  51.854  111.300 1.00 18.16 ? 163  SER B O     1 
ATOM   10130 C  CB    . SER B  1  165  ? -3.428  51.291  108.041 1.00 17.15 ? 163  SER B CB    1 
ATOM   10131 O  OG    . SER B  1  165  ? -4.712  51.112  108.602 1.00 19.68 ? 163  SER B OG    1 
ATOM   10132 N  N     . LEU B  1  166  ? -1.872  50.218  110.566 1.00 19.24 ? 164  LEU B N     1 
ATOM   10133 C  CA    . LEU B  1  166  ? -1.884  49.538  111.855 1.00 17.97 ? 164  LEU B CA    1 
ATOM   10134 C  C     . LEU B  1  166  ? -1.172  50.352  112.925 1.00 18.25 ? 164  LEU B C     1 
ATOM   10135 O  O     . LEU B  1  166  ? -1.610  50.374  114.073 1.00 18.98 ? 164  LEU B O     1 
ATOM   10136 C  CB    . LEU B  1  166  ? -1.233  48.167  111.716 1.00 18.31 ? 164  LEU B CB    1 
ATOM   10137 C  CG    . LEU B  1  166  ? -2.152  47.239  110.936 1.00 21.75 ? 164  LEU B CG    1 
ATOM   10138 C  CD1   . LEU B  1  166  ? -1.447  45.964  110.605 1.00 24.23 ? 164  LEU B CD1   1 
ATOM   10139 C  CD2   . LEU B  1  166  ? -3.418  46.964  111.738 1.00 21.44 ? 164  LEU B CD2   1 
ATOM   10140 N  N     . ALA B  1  167  ? -0.043  50.981  112.580 1.00 17.55 ? 165  ALA B N     1 
ATOM   10141 C  CA    . ALA B  1  167  ? 0.639   51.831  113.552 1.00 19.08 ? 165  ALA B CA    1 
ATOM   10142 C  C     . ALA B  1  167  ? -0.257  52.983  113.977 1.00 19.07 ? 165  ALA B C     1 
ATOM   10143 O  O     . ALA B  1  167  ? -0.370  53.295  115.166 1.00 20.21 ? 165  ALA B O     1 
ATOM   10144 C  CB    . ALA B  1  167  ? 1.943   52.362  112.967 1.00 20.34 ? 165  ALA B CB    1 
ATOM   10145 N  N     . ALA B  1  168  ? -0.931  53.606  113.008 1.00 19.33 ? 166  ALA B N     1 
ATOM   10146 C  CA    . ALA B  1  168  ? -1.864  54.672  113.333 1.00 19.26 ? 166  ALA B CA    1 
ATOM   10147 C  C     . ALA B  1  168  ? -2.992  54.164  114.221 1.00 18.10 ? 166  ALA B C     1 
ATOM   10148 O  O     . ALA B  1  168  ? -3.399  54.835  115.167 1.00 20.08 ? 166  ALA B O     1 
ATOM   10149 C  CB    . ALA B  1  168  ? -2.427  55.264  112.040 1.00 20.62 ? 166  ALA B CB    1 
ATOM   10150 N  N     . ALA B  1  169  ? -3.515  52.979  113.910 1.00 18.60 ? 167  ALA B N     1 
ATOM   10151 C  CA    . ALA B  1  169  ? -4.618  52.422  114.686 1.00 18.85 ? 167  ALA B CA    1 
ATOM   10152 C  C     . ALA B  1  169  ? -4.182  52.090  116.104 1.00 21.22 ? 167  ALA B C     1 
ATOM   10153 O  O     . ALA B  1  169  ? -4.928  52.326  117.059 1.00 20.59 ? 167  ALA B O     1 
ATOM   10154 C  CB    . ALA B  1  169  ? -5.159  51.177  113.983 1.00 20.41 ? 167  ALA B CB    1 
ATOM   10155 N  N     . LEU B  1  170  ? -2.978  51.547  116.265 1.00 20.31 ? 168  LEU B N     1 
ATOM   10156 C  CA    . LEU B  1  170  ? -2.522  51.213  117.612 1.00 18.48 ? 168  LEU B CA    1 
ATOM   10157 C  C     . LEU B  1  170  ? -2.294  52.465  118.445 1.00 20.47 ? 168  LEU B C     1 
ATOM   10158 O  O     . LEU B  1  170  ? -2.697  52.528  119.611 1.00 21.03 ? 168  LEU B O     1 
ATOM   10159 C  CB    . LEU B  1  170  ? -1.250  50.382  117.532 1.00 20.85 ? 168  LEU B CB    1 
ATOM   10160 C  CG    . LEU B  1  170  ? -0.756  49.800  118.851 1.00 19.94 ? 168  LEU B CG    1 
ATOM   10161 C  CD1   . LEU B  1  170  ? -1.826  48.944  119.501 1.00 22.81 ? 168  LEU B CD1   1 
ATOM   10162 C  CD2   . LEU B  1  170  ? 0.473   49.001  118.541 1.00 25.84 ? 168  LEU B CD2   1 
ATOM   10163 N  N     . THR B  1  171  ? -1.645  53.473  117.866 1.00 20.74 ? 169  THR B N     1 
ATOM   10164 C  CA    . THR B  1  171  ? -1.502  54.737  118.572 1.00 22.14 ? 169  THR B CA    1 
ATOM   10165 C  C     . THR B  1  171  ? -2.859  55.297  118.961 1.00 21.59 ? 169  THR B C     1 
ATOM   10166 O  O     . THR B  1  171  ? -3.062  55.755  120.090 1.00 20.74 ? 169  THR B O     1 
ATOM   10167 C  CB    . THR B  1  171  ? -0.750  55.734  117.699 1.00 24.02 ? 169  THR B CB    1 
ATOM   10168 O  OG1   . THR B  1  171  ? 0.580   55.254  117.473 1.00 26.40 ? 169  THR B OG1   1 
ATOM   10169 C  CG2   . THR B  1  171  ? -0.702  57.099  118.354 1.00 23.34 ? 169  THR B CG2   1 
ATOM   10170 N  N     . ARG B  1  172  ? -3.811  55.258  118.028 1.00 21.49 ? 170  ARG B N     1 
ATOM   10171 C  CA    . ARG B  1  172  ? -5.115  55.824  118.314 1.00 21.27 ? 170  ARG B CA    1 
ATOM   10172 C  C     . ARG B  1  172  ? -5.793  55.074  119.451 1.00 20.55 ? 170  ARG B C     1 
ATOM   10173 O  O     . ARG B  1  172  ? -6.343  55.683  120.372 1.00 22.53 ? 170  ARG B O     1 
ATOM   10174 C  CB    . ARG B  1  172  ? -5.980  55.803  117.059 1.00 20.18 ? 170  ARG B CB    1 
ATOM   10175 C  CG    . ARG B  1  172  ? -7.257  56.620  117.199 1.00 20.56 ? 170  ARG B CG    1 
ATOM   10176 C  CD    . ARG B  1  172  ? -8.163  56.468  115.959 1.00 22.05 ? 170  ARG B CD    1 
ATOM   10177 N  NE    . ARG B  1  172  ? -7.441  56.574  114.694 1.00 20.50 ? 170  ARG B NE    1 
ATOM   10178 C  CZ    . ARG B  1  172  ? -7.141  55.546  113.911 1.00 19.93 ? 170  ARG B CZ    1 
ATOM   10179 N  NH1   . ARG B  1  172  ? -7.450  54.309  114.255 1.00 20.67 ? 170  ARG B NH1   1 
ATOM   10180 N  NH2   . ARG B  1  172  ? -6.493  55.762  112.769 1.00 20.32 ? 170  ARG B NH2   1 
ATOM   10181 N  N     . LEU B  1  173  ? -5.745  53.744  119.422 1.00 22.09 ? 171  LEU B N     1 
ATOM   10182 C  CA    . LEU B  1  173  ? -6.511  53.014  120.424 1.00 22.99 ? 171  LEU B CA    1 
ATOM   10183 C  C     . LEU B  1  173  ? -5.870  53.131  121.800 1.00 23.87 ? 171  LEU B C     1 
ATOM   10184 O  O     . LEU B  1  173  ? -6.578  53.198  122.804 1.00 24.14 ? 171  LEU B O     1 
ATOM   10185 C  CB    . LEU B  1  173  ? -6.689  51.551  120.008 1.00 24.99 ? 171  LEU B CB    1 
ATOM   10186 C  CG    . LEU B  1  173  ? -5.536  50.552  120.042 1.00 24.96 ? 171  LEU B CG    1 
ATOM   10187 C  CD1   . LEU B  1  173  ? -5.400  49.912  121.428 1.00 24.26 ? 171  LEU B CD1   1 
ATOM   10188 C  CD2   . LEU B  1  173  ? -5.750  49.487  118.991 1.00 25.58 ? 171  LEU B CD2   1 
ATOM   10189 N  N     . ILE B  1  174  ? -4.536  53.165  121.866 1.00 22.62 ? 172  ILE B N     1 
ATOM   10190 C  CA    . ILE B  1  174  ? -3.887  53.308  123.165 1.00 21.23 ? 172  ILE B CA    1 
ATOM   10191 C  C     . ILE B  1  174  ? -4.113  54.705  123.722 1.00 22.28 ? 172  ILE B C     1 
ATOM   10192 O  O     . ILE B  1  174  ? -4.371  54.874  124.921 1.00 24.23 ? 172  ILE B O     1 
ATOM   10193 C  CB    . ILE B  1  174  ? -2.389  52.982  123.062 1.00 22.69 ? 172  ILE B CB    1 
ATOM   10194 C  CG1   . ILE B  1  174  ? -2.179  51.513  122.695 1.00 23.03 ? 172  ILE B CG1   1 
ATOM   10195 C  CG2   . ILE B  1  174  ? -1.700  53.324  124.375 1.00 23.78 ? 172  ILE B CG2   1 
ATOM   10196 C  CD1   . ILE B  1  174  ? -0.737  51.179  122.355 1.00 24.19 ? 172  ILE B CD1   1 
ATOM   10197 N  N     . SER B  1  175  ? -4.002  55.733  122.869 1.00 23.82 ? 173  SER B N     1 
ATOM   10198 C  CA    . SER B  1  175  ? -4.240  57.084  123.359 1.00 24.34 ? 173  SER B CA    1 
ATOM   10199 C  C     . SER B  1  175  ? -5.695  57.285  123.761 1.00 22.63 ? 173  SER B C     1 
ATOM   10200 O  O     . SER B  1  175  ? -5.982  58.128  124.606 1.00 26.88 ? 173  SER B O     1 
ATOM   10201 C  CB    . SER B  1  175  ? -3.845  58.119  122.309 1.00 25.15 ? 173  SER B CB    1 
ATOM   10202 O  OG    . SER B  1  175  ? -2.456  58.083  122.045 1.00 30.37 ? 173  SER B OG    1 
ATOM   10203 N  N     . ARG B  1  176  ? -6.618  56.524  123.171 1.00 24.22 ? 174  ARG B N     1 
ATOM   10204 C  CA    . ARG B  1  176  ? -8.029  56.682  123.504 1.00 23.71 ? 174  ARG B CA    1 
ATOM   10205 C  C     . ARG B  1  176  ? -8.416  55.870  124.739 1.00 28.63 ? 174  ARG B C     1 
ATOM   10206 O  O     . ARG B  1  176  ? -9.172  56.352  125.588 1.00 28.99 ? 174  ARG B O     1 
ATOM   10207 C  CB    . ARG B  1  176  ? -8.886  56.276  122.298 1.00 27.18 ? 174  ARG B CB    1 
ATOM   10208 C  CG    . ARG B  1  176  ? -10.383 56.576  122.451 1.00 27.43 ? 174  ARG B CG    1 
ATOM   10209 C  CD    . ARG B  1  176  ? -11.107 56.267  121.136 1.00 26.56 ? 174  ARG B CD    1 
ATOM   10210 N  NE    . ARG B  1  176  ? -11.297 54.832  120.922 1.00 27.85 ? 174  ARG B NE    1 
ATOM   10211 C  CZ    . ARG B  1  176  ? -10.763 54.094  119.952 1.00 28.80 ? 174  ARG B CZ    1 
ATOM   10212 N  NH1   . ARG B  1  176  ? -10.010 54.621  118.975 1.00 25.41 ? 174  ARG B NH1   1 
ATOM   10213 N  NH2   . ARG B  1  176  ? -10.997 52.785  119.941 1.00 32.28 ? 174  ARG B NH2   1 
ATOM   10214 N  N     . CYS B  1  177  ? -7.907  54.642  124.857 1.00 25.55 ? 175  CYS B N     1 
ATOM   10215 C  CA    . CYS B  1  177  ? -8.416  53.694  125.836 1.00 25.57 ? 175  CYS B CA    1 
ATOM   10216 C  C     . CYS B  1  177  ? -7.401  53.276  126.882 1.00 30.32 ? 175  CYS B C     1 
ATOM   10217 O  O     . CYS B  1  177  ? -7.807  52.754  127.924 1.00 31.98 ? 175  CYS B O     1 
ATOM   10218 C  CB    . CYS B  1  177  ? -8.945  52.434  125.136 1.00 26.29 ? 175  CYS B CB    1 
ATOM   10219 S  SG    . CYS B  1  177  ? -10.243 52.791  123.904 1.00 34.22 ? 175  CYS B SG    1 
ATOM   10220 N  N     . GLY B  1  178  ? -6.108  53.469  126.633 1.00 30.10 ? 176  GLY B N     1 
ATOM   10221 C  CA    . GLY B  1  178  ? -5.112  53.281  127.669 1.00 30.02 ? 176  GLY B CA    1 
ATOM   10222 C  C     . GLY B  1  178  ? -4.898  51.829  128.060 1.00 31.07 ? 176  GLY B C     1 
ATOM   10223 O  O     . GLY B  1  178  ? -5.175  50.887  127.312 1.00 29.40 ? 176  GLY B O     1 
ATOM   10224 N  N     . GLU B  1  179  ? -4.388  51.660  129.282 1.00 31.68 ? 177  GLU B N     1 
ATOM   10225 C  CA    . GLU B  1  179  ? -4.056  50.324  129.769 1.00 34.46 ? 177  GLU B CA    1 
ATOM   10226 C  C     . GLU B  1  179  ? -5.229  49.349  129.745 1.00 29.61 ? 177  GLU B C     1 
ATOM   10227 O  O     . GLU B  1  179  ? -5.005  48.179  129.384 1.00 28.06 ? 177  GLU B O     1 
ATOM   10228 C  CB    . GLU B  1  179  ? -3.461  50.420  131.184 1.00 35.21 ? 177  GLU B CB    1 
ATOM   10229 C  CG    . GLU B  1  179  ? -3.112  49.057  131.771 1.00 38.71 ? 177  GLU B CG    1 
ATOM   10230 C  CD    . GLU B  1  179  ? -2.251  49.133  133.014 1.00 55.33 ? 177  GLU B CD    1 
ATOM   10231 O  OE1   . GLU B  1  179  ? -2.045  50.249  133.540 1.00 54.01 ? 177  GLU B OE1   1 
ATOM   10232 O  OE2   . GLU B  1  179  ? -1.775  48.068  133.462 1.00 55.41 ? 177  GLU B OE2   1 
ATOM   10233 N  N     . PRO B  1  180  ? -6.469  49.733  130.092 1.00 28.01 ? 178  PRO B N     1 
ATOM   10234 C  CA    . PRO B  1  180  ? -7.553  48.732  130.107 1.00 32.64 ? 178  PRO B CA    1 
ATOM   10235 C  C     . PRO B  1  180  ? -7.735  47.979  128.801 1.00 33.19 ? 178  PRO B C     1 
ATOM   10236 O  O     . PRO B  1  180  ? -8.011  46.773  128.832 1.00 30.79 ? 178  PRO B O     1 
ATOM   10237 C  CB    . PRO B  1  180  ? -8.786  49.573  130.460 1.00 33.54 ? 178  PRO B CB    1 
ATOM   10238 C  CG    . PRO B  1  180  ? -8.243  50.639  131.349 1.00 31.44 ? 178  PRO B CG    1 
ATOM   10239 C  CD    . PRO B  1  180  ? -6.903  50.995  130.730 1.00 33.41 ? 178  PRO B CD    1 
ATOM   10240 N  N     . VAL B  1  181  ? -7.585  48.634  127.648 1.00 26.28 ? 179  VAL B N     1 
ATOM   10241 C  CA    . VAL B  1  181  ? -7.761  47.898  126.404 1.00 24.11 ? 179  VAL B CA    1 
ATOM   10242 C  C     . VAL B  1  181  ? -6.563  47.001  126.134 1.00 25.42 ? 179  VAL B C     1 
ATOM   10243 O  O     . VAL B  1  181  ? -6.710  45.924  125.542 1.00 25.85 ? 179  VAL B O     1 
ATOM   10244 C  CB    . VAL B  1  181  ? -8.027  48.852  125.219 1.00 27.32 ? 179  VAL B CB    1 
ATOM   10245 C  CG1   . VAL B  1  181  ? -6.775  49.624  124.831 1.00 30.84 ? 179  VAL B CG1   1 
ATOM   10246 C  CG2   . VAL B  1  181  ? -8.531  48.064  124.026 1.00 31.23 ? 179  VAL B CG2   1 
ATOM   10247 N  N     . ILE B  1  182  ? -5.365  47.421  126.553 1.00 26.65 ? 180  ILE B N     1 
ATOM   10248 C  CA    . ILE B  1  182  ? -4.186  46.579  126.376 1.00 26.39 ? 180  ILE B CA    1 
ATOM   10249 C  C     . ILE B  1  182  ? -4.332  45.313  127.206 1.00 28.29 ? 180  ILE B C     1 
ATOM   10250 O  O     . ILE B  1  182  ? -4.111  44.197  126.712 1.00 28.13 ? 180  ILE B O     1 
ATOM   10251 C  CB    . ILE B  1  182  ? -2.906  47.350  126.747 1.00 27.51 ? 180  ILE B CB    1 
ATOM   10252 C  CG1   . ILE B  1  182  ? -2.710  48.550  125.828 1.00 25.76 ? 180  ILE B CG1   1 
ATOM   10253 C  CG2   . ILE B  1  182  ? -1.685  46.439  126.645 1.00 28.37 ? 180  ILE B CG2   1 
ATOM   10254 C  CD1   . ILE B  1  182  ? -1.736  49.561  126.391 1.00 29.54 ? 180  ILE B CD1   1 
ATOM   10255 N  N     . ARG B  1  183  ? -4.722  45.475  128.476 1.00 28.18 ? 181  ARG B N     1 
ATOM   10256 C  CA    . ARG B  1  183  ? -4.948  44.328  129.351 1.00 30.80 ? 181  ARG B CA    1 
ATOM   10257 C  C     . ARG B  1  183  ? -5.966  43.368  128.745 1.00 33.20 ? 181  ARG B C     1 
ATOM   10258 O  O     . ARG B  1  183  ? -5.728  42.156  128.678 1.00 33.34 ? 181  ARG B O     1 
ATOM   10259 C  CB    . ARG B  1  183  ? -5.386  44.818  130.736 1.00 32.82 ? 181  ARG B CB    1 
ATOM   10260 C  CG    . ARG B  1  183  ? -6.005  43.763  131.656 1.00 43.33 ? 181  ARG B CG    1 
ATOM   10261 C  CD    . ARG B  1  183  ? -5.147  42.506  131.759 1.00 48.26 ? 181  ARG B CD    1 
ATOM   10262 N  NE    . ARG B  1  183  ? -3.747  42.810  132.016 1.00 50.63 ? 181  ARG B NE    1 
ATOM   10263 C  CZ    . ARG B  1  183  ? -2.741  42.008  131.700 1.00 45.80 ? 181  ARG B CZ    1 
ATOM   10264 N  NH1   . ARG B  1  183  ? -2.944  40.856  131.080 1.00 39.15 ? 181  ARG B NH1   1 
ATOM   10265 N  NH2   . ARG B  1  183  ? -1.499  42.376  132.004 1.00 51.59 ? 181  ARG B NH2   1 
ATOM   10266 N  N     . ARG B  1  184  ? -7.092  43.898  128.261 1.00 31.87 ? 182  ARG B N     1 
ATOM   10267 C  CA    . ARG B  1  184  ? -8.113  43.043  127.663 1.00 32.91 ? 182  ARG B CA    1 
ATOM   10268 C  C     . ARG B  1  184  ? -7.590  42.329  126.424 1.00 32.89 ? 182  ARG B C     1 
ATOM   10269 O  O     . ARG B  1  184  ? -7.894  41.152  126.207 1.00 32.37 ? 182  ARG B O     1 
ATOM   10270 C  CB    . ARG B  1  184  ? -9.356  43.866  127.327 1.00 33.99 ? 182  ARG B CB    1 
ATOM   10271 C  CG    . ARG B  1  184  ? -10.219 44.195  128.538 1.00 40.13 ? 182  ARG B CG    1 
ATOM   10272 C  CD    . ARG B  1  184  ? -11.258 43.105  128.799 1.00 45.87 ? 182  ARG B CD    1 
ATOM   10273 N  NE    . ARG B  1  184  ? -12.447 43.273  127.970 1.00 46.28 ? 182  ARG B NE    1 
ATOM   10274 C  CZ    . ARG B  1  184  ? -12.880 42.397  127.072 1.00 43.11 ? 182  ARG B CZ    1 
ATOM   10275 N  NH1   . ARG B  1  184  ? -12.257 41.247  126.868 1.00 45.37 ? 182  ARG B NH1   1 
ATOM   10276 N  NH2   . ARG B  1  184  ? -13.974 42.678  126.367 1.00 39.38 ? 182  ARG B NH2   1 
ATOM   10277 N  N     . GLY B  1  185  ? -6.811  43.025  125.592 1.00 29.61 ? 183  GLY B N     1 
ATOM   10278 C  CA    . GLY B  1  185  ? -6.259  42.385  124.408 1.00 26.62 ? 183  GLY B CA    1 
ATOM   10279 C  C     . GLY B  1  185  ? -5.255  41.298  124.741 1.00 28.89 ? 183  GLY B C     1 
ATOM   10280 O  O     . GLY B  1  185  ? -5.228  40.247  124.094 1.00 28.80 ? 183  GLY B O     1 
ATOM   10281 N  N     . VAL B  1  186  ? -4.418  41.533  125.755 1.00 28.07 ? 184  VAL B N     1 
ATOM   10282 C  CA    . VAL B  1  186  ? -3.449  40.519  126.168 1.00 30.06 ? 184  VAL B CA    1 
ATOM   10283 C  C     . VAL B  1  186  ? -4.170  39.275  126.674 1.00 31.26 ? 184  VAL B C     1 
ATOM   10284 O  O     . VAL B  1  186  ? -3.859  38.148  126.268 1.00 30.58 ? 184  VAL B O     1 
ATOM   10285 C  CB    . VAL B  1  186  ? -2.490  41.094  127.223 1.00 26.88 ? 184  VAL B CB    1 
ATOM   10286 C  CG1   . VAL B  1  186  ? -1.718  39.966  127.924 1.00 29.29 ? 184  VAL B CG1   1 
ATOM   10287 C  CG2   . VAL B  1  186  ? -1.530  42.067  126.572 1.00 30.13 ? 184  VAL B CG2   1 
ATOM   10288 N  N     . ASP B  1  187  ? -5.163  39.465  127.546 1.00 33.09 ? 185  ASP B N     1 
ATOM   10289 C  CA    . ASP B  1  187  ? -5.923  38.330  128.061 1.00 34.08 ? 185  ASP B CA    1 
ATOM   10290 C  C     . ASP B  1  187  ? -6.617  37.579  126.936 1.00 37.85 ? 185  ASP B C     1 
ATOM   10291 O  O     . ASP B  1  187  ? -6.656  36.343  126.936 1.00 33.49 ? 185  ASP B O     1 
ATOM   10292 C  CB    . ASP B  1  187  ? -6.940  38.801  129.095 1.00 34.17 ? 185  ASP B CB    1 
ATOM   10293 C  CG    . ASP B  1  187  ? -6.280  39.302  130.372 1.00 38.54 ? 185  ASP B CG    1 
ATOM   10294 O  OD1   . ASP B  1  187  ? -5.059  39.084  130.525 1.00 42.49 ? 185  ASP B OD1   1 
ATOM   10295 O  OD2   . ASP B  1  187  ? -6.971  39.918  131.210 1.00 36.81 ? 185  ASP B OD2   1 
ATOM   10296 N  N     . MET B  1  188  ? -7.161  38.315  125.961 1.00 33.60 ? 186  MET B N     1 
ATOM   10297 C  CA    . MET B  1  188  ? -7.863  37.697  124.842 1.00 32.94 ? 186  MET B CA    1 
ATOM   10298 C  C     . MET B  1  188  ? -6.911  36.883  123.974 1.00 31.76 ? 186  MET B C     1 
ATOM   10299 O  O     . MET B  1  188  ? -7.222  35.751  123.584 1.00 40.37 ? 186  MET B O     1 
ATOM   10300 C  CB    . MET B  1  188  ? -8.555  38.775  124.012 1.00 36.14 ? 186  MET B CB    1 
ATOM   10301 C  CG    . MET B  1  188  ? -9.340  38.243  122.836 1.00 39.65 ? 186  MET B CG    1 
ATOM   10302 S  SD    . MET B  1  188  ? -10.683 37.196  123.398 1.00 53.10 ? 186  MET B SD    1 
ATOM   10303 C  CE    . MET B  1  188  ? -11.452 38.270  124.614 1.00 46.52 ? 186  MET B CE    1 
ATOM   10304 N  N     . ALA B  1  189  ? -5.752  37.452  123.641 1.00 33.02 ? 187  ALA B N     1 
ATOM   10305 C  CA    . ALA B  1  189  ? -4.793  36.723  122.818 1.00 33.78 ? 187  ALA B CA    1 
ATOM   10306 C  C     . ALA B  1  189  ? -4.234  35.520  123.566 1.00 33.80 ? 187  ALA B C     1 
ATOM   10307 O  O     . ALA B  1  189  ? -3.994  34.467  122.966 1.00 31.93 ? 187  ALA B O     1 
ATOM   10308 C  CB    . ALA B  1  189  ? -3.663  37.650  122.377 1.00 34.73 ? 187  ALA B CB    1 
ATOM   10309 N  N     . MET B  1  190  ? -4.026  35.658  124.877 1.00 31.63 ? 188  MET B N     1 
ATOM   10310 C  CA    . MET B  1  190  ? -3.525  34.534  125.661 1.00 33.17 ? 188  MET B CA    1 
ATOM   10311 C  C     . MET B  1  190  ? -4.505  33.367  125.624 1.00 40.36 ? 188  MET B C     1 
ATOM   10312 O  O     . MET B  1  190  ? -4.100  32.207  125.464 1.00 33.35 ? 188  MET B O     1 
ATOM   10313 C  CB    . MET B  1  190  ? -3.262  34.978  127.098 1.00 33.46 ? 188  MET B CB    1 
ATOM   10314 C  CG    . MET B  1  190  ? -2.574  33.933  127.942 1.00 41.21 ? 188  MET B CG    1 
ATOM   10315 S  SD    . MET B  1  190  ? -2.519  34.427  129.671 1.00 46.06 ? 188  MET B SD    1 
ATOM   10316 C  CE    . MET B  1  190  ? -1.688  36.011  129.543 1.00 38.67 ? 188  MET B CE    1 
ATOM   10317 N  N     . ARG B  1  191  ? -5.803  33.658  125.742 1.00 32.13 ? 189  ARG B N     1 
ATOM   10318 C  CA    . ARG B  1  191  ? -6.804  32.599  125.665 1.00 37.58 ? 189  ARG B CA    1 
ATOM   10319 C  C     . ARG B  1  191  ? -6.831  31.973  124.277 1.00 37.99 ? 189  ARG B C     1 
ATOM   10320 O  O     . ARG B  1  191  ? -6.794  30.745  124.137 1.00 34.36 ? 189  ARG B O     1 
ATOM   10321 C  CB    . ARG B  1  191  ? -8.184  33.146  126.040 1.00 34.85 ? 189  ARG B CB    1 
ATOM   10322 N  N     . MET B  1  192  ? -6.885  32.804  123.235 1.00 32.63 ? 190  MET B N     1 
ATOM   10323 C  CA    . MET B  1  192  ? -6.989  32.270  121.884 1.00 29.72 ? 190  MET B CA    1 
ATOM   10324 C  C     . MET B  1  192  ? -5.767  31.434  121.535 1.00 32.54 ? 190  MET B C     1 
ATOM   10325 O  O     . MET B  1  192  ? -5.888  30.320  121.011 1.00 33.42 ? 190  MET B O     1 
ATOM   10326 C  CB    . MET B  1  192  ? -7.168  33.406  120.874 1.00 34.62 ? 190  MET B CB    1 
ATOM   10327 C  CG    . MET B  1  192  ? -8.420  34.231  121.097 1.00 36.95 ? 190  MET B CG    1 
ATOM   10328 S  SD    . MET B  1  192  ? -8.618  35.465  119.808 1.00 50.32 ? 190  MET B SD    1 
ATOM   10329 C  CE    . MET B  1  192  ? -9.042  34.398  118.443 1.00 37.02 ? 190  MET B CE    1 
ATOM   10330 N  N     . MET B  1  193  ? -4.577  31.949  121.830 1.00 31.66 ? 191  MET B N     1 
ATOM   10331 C  CA    . MET B  1  193  ? -3.372  31.247  121.425 1.00 33.38 ? 191  MET B CA    1 
ATOM   10332 C  C     . MET B  1  193  ? -3.004  30.120  122.375 1.00 31.86 ? 191  MET B C     1 
ATOM   10333 O  O     . MET B  1  193  ? -2.232  29.238  121.992 1.00 33.74 ? 191  MET B O     1 
ATOM   10334 C  CB    . MET B  1  193  ? -2.209  32.230  121.308 1.00 35.04 ? 191  MET B CB    1 
ATOM   10335 C  CG    . MET B  1  193  ? -2.240  33.029  120.033 1.00 38.79 ? 191  MET B CG    1 
ATOM   10336 S  SD    . MET B  1  193  ? -0.704  33.928  119.814 1.00 42.75 ? 191  MET B SD    1 
ATOM   10337 C  CE    . MET B  1  193  ? -0.944  35.223  121.002 1.00 30.98 ? 191  MET B CE    1 
ATOM   10338 N  N     . GLY B  1  194  ? -3.546  30.118  123.587 1.00 31.85 ? 192  GLY B N     1 
ATOM   10339 C  CA    . GLY B  1  194  ? -3.217  29.078  124.541 1.00 31.41 ? 192  GLY B CA    1 
ATOM   10340 C  C     . GLY B  1  194  ? -4.265  27.991  124.654 1.00 36.12 ? 192  GLY B C     1 
ATOM   10341 O  O     . GLY B  1  194  ? -3.957  26.880  125.101 1.00 33.95 ? 192  GLY B O     1 
ATOM   10342 N  N     . GLU B  1  195  ? -5.507  28.291  124.262 1.00 33.29 ? 193  GLU B N     1 
ATOM   10343 C  CA    . GLU B  1  195  ? -6.630  27.400  124.533 1.00 37.07 ? 193  GLU B CA    1 
ATOM   10344 C  C     . GLU B  1  195  ? -7.563  27.172  123.358 1.00 33.75 ? 193  GLU B C     1 
ATOM   10345 O  O     . GLU B  1  195  ? -8.279  26.165  123.362 1.00 31.48 ? 193  GLU B O     1 
ATOM   10346 C  CB    . GLU B  1  195  ? -7.474  27.929  125.704 1.00 36.73 ? 193  GLU B CB    1 
ATOM   10347 C  CG    . GLU B  1  195  ? -6.703  28.149  126.990 1.00 43.43 ? 193  GLU B CG    1 
ATOM   10348 C  CD    . GLU B  1  195  ? -7.545  28.819  128.055 1.00 50.52 ? 193  GLU B CD    1 
ATOM   10349 O  OE1   . GLU B  1  195  ? -8.788  28.729  127.970 1.00 53.49 ? 193  GLU B OE1   1 
ATOM   10350 O  OE2   . GLU B  1  195  ? -6.964  29.442  128.969 1.00 59.89 ? 193  GLU B OE2   1 
ATOM   10351 N  N     . GLN B  1  196  ? -7.611  28.069  122.376 1.00 36.48 ? 194  GLN B N     1 
ATOM   10352 C  CA    . GLN B  1  196  ? -8.516  27.912  121.245 1.00 34.38 ? 194  GLN B CA    1 
ATOM   10353 C  C     . GLN B  1  196  ? -7.786  27.450  119.992 1.00 35.63 ? 194  GLN B C     1 
ATOM   10354 O  O     . GLN B  1  196  ? -8.187  26.465  119.367 1.00 37.18 ? 194  GLN B O     1 
ATOM   10355 C  CB    . GLN B  1  196  ? -9.258  29.228  120.978 1.00 35.25 ? 194  GLN B CB    1 
ATOM   10356 N  N     . PHE B  1  197  ? -6.700  28.130  119.629 1.00 33.01 ? 195  PHE B N     1 
ATOM   10357 C  CA    . PHE B  1  197  ? -5.931  27.725  118.458 1.00 34.96 ? 195  PHE B CA    1 
ATOM   10358 C  C     . PHE B  1  197  ? -5.160  26.438  118.709 1.00 34.37 ? 195  PHE B C     1 
ATOM   10359 O  O     . PHE B  1  197  ? -4.842  25.707  117.762 1.00 34.67 ? 195  PHE B O     1 
ATOM   10360 C  CB    . PHE B  1  197  ? -4.971  28.839  118.053 1.00 34.15 ? 195  PHE B CB    1 
ATOM   10361 C  CG    . PHE B  1  197  ? -5.660  30.076  117.563 1.00 33.59 ? 195  PHE B CG    1 
ATOM   10362 C  CD1   . PHE B  1  197  ? -6.887  29.990  116.925 1.00 40.27 ? 195  PHE B CD1   1 
ATOM   10363 C  CD2   . PHE B  1  197  ? -5.080  31.322  117.738 1.00 38.55 ? 195  PHE B CD2   1 
ATOM   10364 C  CE1   . PHE B  1  197  ? -7.524  31.124  116.464 1.00 44.78 ? 195  PHE B CE1   1 
ATOM   10365 C  CE2   . PHE B  1  197  ? -5.716  32.464  117.283 1.00 39.66 ? 195  PHE B CE2   1 
ATOM   10366 C  CZ    . PHE B  1  197  ? -6.938  32.362  116.648 1.00 39.94 ? 195  PHE B CZ    1 
ATOM   10367 N  N     . VAL B  1  198  ? -4.821  26.161  119.961 1.00 32.19 ? 196  VAL B N     1 
ATOM   10368 C  CA    . VAL B  1  198  ? -4.194  24.905  120.335 1.00 29.56 ? 196  VAL B CA    1 
ATOM   10369 C  C     . VAL B  1  198  ? -4.948  24.360  121.532 1.00 32.15 ? 196  VAL B C     1 
ATOM   10370 O  O     . VAL B  1  198  ? -5.555  25.107  122.306 1.00 33.96 ? 196  VAL B O     1 
ATOM   10371 C  CB    . VAL B  1  198  ? -2.688  25.048  120.661 1.00 28.69 ? 196  VAL B CB    1 
ATOM   10372 C  CG1   . VAL B  1  198  ? -1.917  25.511  119.440 1.00 31.48 ? 196  VAL B CG1   1 
ATOM   10373 C  CG2   . VAL B  1  198  ? -2.481  25.996  121.820 1.00 33.08 ? 196  VAL B CG2   1 
ATOM   10374 N  N     . THR B  1  199  ? -4.933  23.039  121.666 1.00 30.53 ? 197  THR B N     1 
ATOM   10375 C  CA    . THR B  1  199  ? -5.506  22.443  122.859 1.00 30.08 ? 197  THR B CA    1 
ATOM   10376 C  C     . THR B  1  199  ? -4.621  22.703  124.064 1.00 32.84 ? 197  THR B C     1 
ATOM   10377 O  O     . THR B  1  199  ? -5.123  22.883  125.176 1.00 35.31 ? 197  THR B O     1 
ATOM   10378 C  CB    . THR B  1  199  ? -5.724  20.953  122.625 1.00 33.26 ? 197  THR B CB    1 
ATOM   10379 O  OG1   . THR B  1  199  ? -6.530  20.800  121.448 1.00 36.49 ? 197  THR B OG1   1 
ATOM   10380 C  CG2   . THR B  1  199  ? -6.443  20.321  123.806 1.00 32.30 ? 197  THR B CG2   1 
ATOM   10381 N  N     . GLY B  1  200  ? -3.314  22.768  123.847 1.00 30.54 ? 198  GLY B N     1 
ATOM   10382 C  CA    . GLY B  1  200  ? -2.379  23.168  124.876 1.00 30.86 ? 198  GLY B CA    1 
ATOM   10383 C  C     . GLY B  1  200  ? -1.057  23.518  124.236 1.00 28.99 ? 198  GLY B C     1 
ATOM   10384 O  O     . GLY B  1  200  ? -0.793  23.175  123.081 1.00 27.38 ? 198  GLY B O     1 
ATOM   10385 N  N     . GLU B  1  201  ? -0.219  24.211  125.009 1.00 36.91 ? 199  GLU B N     1 
ATOM   10386 C  CA    . GLU B  1  201  ? 1.108   24.567  124.520 1.00 36.55 ? 199  GLU B CA    1 
ATOM   10387 C  C     . GLU B  1  201  ? 2.029   23.352  124.472 1.00 30.99 ? 199  GLU B C     1 
ATOM   10388 O  O     . GLU B  1  201  ? 2.871   23.246  123.573 1.00 35.77 ? 199  GLU B O     1 
ATOM   10389 C  CB    . GLU B  1  201  ? 1.702   25.660  125.405 1.00 35.13 ? 199  GLU B CB    1 
ATOM   10390 C  CG    . GLU B  1  201  ? 2.929   26.324  124.822 1.00 46.92 ? 199  GLU B CG    1 
ATOM   10391 C  CD    . GLU B  1  201  ? 3.621   27.232  125.821 1.00 50.17 ? 199  GLU B CD    1 
ATOM   10392 O  OE1   . GLU B  1  201  ? 3.144   27.319  126.974 1.00 49.32 ? 199  GLU B OE1   1 
ATOM   10393 O  OE2   . GLU B  1  201  ? 4.642   27.851  125.454 1.00 56.75 ? 199  GLU B OE2   1 
ATOM   10394 N  N     . THR B  1  202  ? 1.876   22.429  125.416 1.00 28.91 ? 200  THR B N     1 
ATOM   10395 C  CA    . THR B  1  202  ? 2.637   21.190  125.475 1.00 29.81 ? 200  THR B CA    1 
ATOM   10396 C  C     . THR B  1  202  ? 1.675   20.009  125.445 1.00 35.75 ? 200  THR B C     1 
ATOM   10397 O  O     . THR B  1  202  ? 0.475   20.158  125.694 1.00 30.77 ? 200  THR B O     1 
ATOM   10398 C  CB    . THR B  1  202  ? 3.480   21.108  126.753 1.00 34.12 ? 200  THR B CB    1 
ATOM   10399 O  OG1   . THR B  1  202  ? 2.613   21.015  127.890 1.00 34.79 ? 200  THR B OG1   1 
ATOM   10400 C  CG2   . THR B  1  202  ? 4.352   22.339  126.903 1.00 37.63 ? 200  THR B CG2   1 
ATOM   10401 N  N     . ILE B  1  203  ? 2.215   18.821  125.166 1.00 30.02 ? 201  ILE B N     1 
ATOM   10402 C  CA    . ILE B  1  203  ? 1.368   17.633  125.149 1.00 28.94 ? 201  ILE B CA    1 
ATOM   10403 C  C     . ILE B  1  203  ? 0.820   17.352  126.545 1.00 29.96 ? 201  ILE B C     1 
ATOM   10404 O  O     . ILE B  1  203  ? -0.330  16.924  126.699 1.00 29.03 ? 201  ILE B O     1 
ATOM   10405 C  CB    . ILE B  1  203  ? 2.124   16.427  124.560 1.00 28.69 ? 201  ILE B CB    1 
ATOM   10406 C  CG1   . ILE B  1  203  ? 1.156   15.264  124.317 1.00 28.44 ? 201  ILE B CG1   1 
ATOM   10407 C  CG2   . ILE B  1  203  ? 3.286   15.996  125.458 1.00 29.97 ? 201  ILE B CG2   1 
ATOM   10408 C  CD1   . ILE B  1  203  ? 0.064   15.603  123.303 1.00 26.50 ? 201  ILE B CD1   1 
ATOM   10409 N  N     . ARG B  1  204  ? 1.612   17.633  127.586 1.00 31.61 ? 202  ARG B N     1 
ATOM   10410 C  CA    . ARG B  1  204  ? 1.142   17.461  128.958 1.00 36.36 ? 202  ARG B CA    1 
ATOM   10411 C  C     . ARG B  1  204  ? -0.105  18.302  129.211 1.00 30.69 ? 202  ARG B C     1 
ATOM   10412 O  O     . ARG B  1  204  ? -1.095  17.818  129.772 1.00 34.91 ? 202  ARG B O     1 
ATOM   10413 C  CB    . ARG B  1  204  ? 2.266   17.842  129.931 1.00 35.25 ? 202  ARG B CB    1 
ATOM   10414 C  CG    . ARG B  1  204  ? 2.208   17.207  131.298 1.00 47.36 ? 202  ARG B CG    1 
ATOM   10415 C  CD    . ARG B  1  204  ? 3.427   17.628  132.127 1.00 44.61 ? 202  ARG B CD    1 
ATOM   10416 N  NE    . ARG B  1  204  ? 3.500   19.080  132.242 1.00 35.54 ? 202  ARG B NE    1 
ATOM   10417 C  CZ    . ARG B  1  204  ? 2.801   19.793  133.113 1.00 45.83 ? 202  ARG B CZ    1 
ATOM   10418 N  NH1   . ARG B  1  204  ? 2.029   19.214  134.018 1.00 47.46 ? 202  ARG B NH1   1 
ATOM   10419 N  NH2   . ARG B  1  204  ? 2.870   21.120  133.069 1.00 48.48 ? 202  ARG B NH2   1 
ATOM   10420 N  N     . GLU B  1  205  ? -0.071  19.569  128.789 1.00 31.06 ? 203  GLU B N     1 
ATOM   10421 C  CA    . GLU B  1  205  ? -1.216  20.450  128.982 1.00 32.70 ? 203  GLU B CA    1 
ATOM   10422 C  C     . GLU B  1  205  ? -2.388  20.017  128.111 1.00 30.34 ? 203  GLU B C     1 
ATOM   10423 O  O     . GLU B  1  205  ? -3.542  20.043  128.555 1.00 32.38 ? 203  GLU B O     1 
ATOM   10424 C  CB    . GLU B  1  205  ? -0.812  21.890  128.673 1.00 35.88 ? 203  GLU B CB    1 
ATOM   10425 C  CG    . GLU B  1  205  ? -1.869  22.929  128.975 1.00 41.98 ? 203  GLU B CG    1 
ATOM   10426 C  CD    . GLU B  1  205  ? -1.385  24.343  128.690 1.00 48.26 ? 203  GLU B CD    1 
ATOM   10427 O  OE1   . GLU B  1  205  ? -1.154  24.673  127.509 1.00 47.60 ? 203  GLU B OE1   1 
ATOM   10428 O  OE2   . GLU B  1  205  ? -1.226  25.124  129.652 1.00 56.53 ? 203  GLU B OE2   1 
ATOM   10429 N  N     . ALA B  1  206  ? -2.108  19.616  126.871 1.00 30.59 ? 204  ALA B N     1 
ATOM   10430 C  CA    . ALA B  1  206  ? -3.170  19.150  125.986 1.00 29.94 ? 204  ALA B CA    1 
ATOM   10431 C  C     . ALA B  1  206  ? -3.848  17.914  126.552 1.00 32.57 ? 204  ALA B C     1 
ATOM   10432 O  O     . ALA B  1  206  ? -5.080  17.819  126.553 1.00 31.04 ? 204  ALA B O     1 
ATOM   10433 C  CB    . ALA B  1  206  ? -2.609  18.860  124.596 1.00 28.54 ? 204  ALA B CB    1 
ATOM   10434 N  N     . LEU B  1  207  ? -3.057  16.961  127.057 1.00 27.12 ? 205  LEU B N     1 
ATOM   10435 C  CA    . LEU B  1  207  ? -3.628  15.729  127.591 1.00 31.64 ? 205  LEU B CA    1 
ATOM   10436 C  C     . LEU B  1  207  ? -4.499  16.006  128.805 1.00 32.49 ? 205  LEU B C     1 
ATOM   10437 O  O     . LEU B  1  207  ? -5.577  15.418  128.947 1.00 34.50 ? 205  LEU B O     1 
ATOM   10438 C  CB    . LEU B  1  207  ? -2.516  14.740  127.942 1.00 30.22 ? 205  LEU B CB    1 
ATOM   10439 C  CG    . LEU B  1  207  ? -1.849  14.080  126.735 1.00 34.05 ? 205  LEU B CG    1 
ATOM   10440 C  CD1   . LEU B  1  207  ? -0.605  13.308  127.149 1.00 34.79 ? 205  LEU B CD1   1 
ATOM   10441 C  CD2   . LEU B  1  207  ? -2.834  13.170  126.015 1.00 29.33 ? 205  LEU B CD2   1 
ATOM   10442 N  N     . LYS B  1  208  ? -4.049  16.893  129.701 1.00 31.45 ? 206  LYS B N     1 
ATOM   10443 C  CA    . LYS B  1  208  ? -4.852  17.217  130.877 1.00 34.06 ? 206  LYS B CA    1 
ATOM   10444 C  C     . LYS B  1  208  ? -6.162  17.890  130.483 1.00 37.13 ? 206  LYS B C     1 
ATOM   10445 O  O     . LYS B  1  208  ? -7.218  17.594  131.055 1.00 39.72 ? 206  LYS B O     1 
ATOM   10446 C  CB    . LYS B  1  208  ? -4.057  18.111  131.833 1.00 35.92 ? 206  LYS B CB    1 
ATOM   10447 N  N     . ARG B  1  209  ? -6.116  18.792  129.504 1.00 34.72 ? 207  ARG B N     1 
ATOM   10448 C  CA    . ARG B  1  209  ? -7.326  19.489  129.088 1.00 33.92 ? 207  ARG B CA    1 
ATOM   10449 C  C     . ARG B  1  209  ? -8.265  18.608  128.281 1.00 41.53 ? 207  ARG B C     1 
ATOM   10450 O  O     . ARG B  1  209  ? -9.414  19.002  128.056 1.00 38.54 ? 207  ARG B O     1 
ATOM   10451 C  CB    . ARG B  1  209  ? -6.966  20.725  128.278 1.00 35.80 ? 207  ARG B CB    1 
ATOM   10452 C  CG    . ARG B  1  209  ? -6.251  21.785  129.089 1.00 35.59 ? 207  ARG B CG    1 
ATOM   10453 C  CD    . ARG B  1  209  ? -5.866  22.936  128.191 1.00 36.06 ? 207  ARG B CD    1 
ATOM   10454 N  NE    . ARG B  1  209  ? -5.317  24.064  128.931 1.00 45.70 ? 207  ARG B NE    1 
ATOM   10455 C  CZ    . ARG B  1  209  ? -4.828  25.156  128.358 1.00 50.14 ? 207  ARG B CZ    1 
ATOM   10456 N  NH1   . ARG B  1  209  ? -4.802  25.291  127.041 1.00 41.01 ? 207  ARG B NH1   1 
ATOM   10457 N  NH2   . ARG B  1  209  ? -4.357  26.135  129.125 1.00 52.42 ? 207  ARG B NH2   1 
ATOM   10458 N  N     . SER B  1  210  ? -7.815  17.429  127.862 1.00 33.45 ? 208  SER B N     1 
ATOM   10459 C  CA    . SER B  1  210  ? -8.645  16.553  127.047 1.00 32.32 ? 208  SER B CA    1 
ATOM   10460 C  C     . SER B  1  210  ? -9.606  15.715  127.869 1.00 33.57 ? 208  SER B C     1 
ATOM   10461 O  O     . SER B  1  210  ? -10.590 15.205  127.322 1.00 37.01 ? 208  SER B O     1 
ATOM   10462 C  CB    . SER B  1  210  ? -7.759  15.632  126.223 1.00 29.19 ? 208  SER B CB    1 
ATOM   10463 O  OG    . SER B  1  210  ? -6.998  16.392  125.297 1.00 33.39 ? 208  SER B OG    1 
ATOM   10464 N  N     . LYS B  1  211  ? -9.338  15.549  129.162 1.00 32.85 ? 209  LYS B N     1 
ATOM   10465 C  CA    . LYS B  1  211  ? -10.153 14.661  129.977 1.00 32.86 ? 209  LYS B CA    1 
ATOM   10466 C  C     . LYS B  1  211  ? -11.618 15.087  129.970 1.00 35.34 ? 209  LYS B C     1 
ATOM   10467 O  O     . LYS B  1  211  ? -12.515 14.236  129.956 1.00 38.13 ? 209  LYS B O     1 
ATOM   10468 C  CB    . LYS B  1  211  ? -9.598  14.627  131.399 1.00 33.54 ? 209  LYS B CB    1 
ATOM   10469 N  N     . GLU B  1  212  ? -11.879 16.398  129.945 1.00 35.50 ? 210  GLU B N     1 
ATOM   10470 C  CA    . GLU B  1  212  ? -13.249 16.892  130.071 1.00 41.79 ? 210  GLU B CA    1 
ATOM   10471 C  C     . GLU B  1  212  ? -14.137 16.368  128.948 1.00 40.45 ? 210  GLU B C     1 
ATOM   10472 O  O     . GLU B  1  212  ? -15.173 15.743  129.199 1.00 40.23 ? 210  GLU B O     1 
ATOM   10473 C  CB    . GLU B  1  212  ? -13.272 18.422  130.083 1.00 44.80 ? 210  GLU B CB    1 
ATOM   10474 C  CG    . GLU B  1  212  ? -14.695 18.975  130.112 1.00 54.83 ? 210  GLU B CG    1 
ATOM   10475 C  CD    . GLU B  1  212  ? -14.755 20.482  129.983 1.00 62.24 ? 210  GLU B CD    1 
ATOM   10476 O  OE1   . GLU B  1  212  ? -13.926 21.167  130.615 1.00 67.25 ? 210  GLU B OE1   1 
ATOM   10477 O  OE2   . GLU B  1  212  ? -15.635 20.981  129.246 1.00 70.05 ? 210  GLU B OE2   1 
ATOM   10478 N  N     . LEU B  1  213  ? -13.754 16.629  127.697 1.00 39.51 ? 211  LEU B N     1 
ATOM   10479 C  CA    . LEU B  1  213  ? -14.587 16.181  126.589 1.00 39.28 ? 211  LEU B CA    1 
ATOM   10480 C  C     . LEU B  1  213  ? -14.496 14.673  126.397 1.00 33.29 ? 211  LEU B C     1 
ATOM   10481 O  O     . LEU B  1  213  ? -15.455 14.057  125.919 1.00 35.65 ? 211  LEU B O     1 
ATOM   10482 C  CB    . LEU B  1  213  ? -14.217 16.930  125.306 1.00 31.21 ? 211  LEU B CB    1 
ATOM   10483 C  CG    . LEU B  1  213  ? -14.565 18.427  125.322 1.00 39.96 ? 211  LEU B CG    1 
ATOM   10484 C  CD1   . LEU B  1  213  ? -14.300 19.098  123.993 1.00 37.04 ? 211  LEU B CD1   1 
ATOM   10485 C  CD2   . LEU B  1  213  ? -16.009 18.637  125.730 1.00 41.63 ? 211  LEU B CD2   1 
ATOM   10486 N  N     . GLU B  1  214  ? -13.373 14.055  126.772 1.00 32.09 ? 212  GLU B N     1 
ATOM   10487 C  CA    . GLU B  1  214  ? -13.303 12.597  126.723 1.00 34.37 ? 212  GLU B CA    1 
ATOM   10488 C  C     . GLU B  1  214  ? -14.361 11.965  127.619 1.00 37.40 ? 212  GLU B C     1 
ATOM   10489 O  O     . GLU B  1  214  ? -14.988 10.968  127.240 1.00 38.06 ? 212  GLU B O     1 
ATOM   10490 C  CB    . GLU B  1  214  ? -11.909 12.110  127.115 1.00 33.99 ? 212  GLU B CB    1 
ATOM   10491 C  CG    . GLU B  1  214  ? -10.870 12.284  126.008 1.00 35.05 ? 212  GLU B CG    1 
ATOM   10492 C  CD    . GLU B  1  214  ? -9.533  11.650  126.351 1.00 35.11 ? 212  GLU B CD    1 
ATOM   10493 O  OE1   . GLU B  1  214  ? -9.326  11.287  127.523 1.00 37.18 ? 212  GLU B OE1   1 
ATOM   10494 O  OE2   . GLU B  1  214  ? -8.688  11.516  125.442 1.00 34.68 ? 212  GLU B OE2   1 
ATOM   10495 N  N     . GLU B  1  215  ? -14.581 12.535  128.808 1.00 36.63 ? 213  GLU B N     1 
ATOM   10496 C  CA    . GLU B  1  215  ? -15.610 12.025  129.707 1.00 36.35 ? 213  GLU B CA    1 
ATOM   10497 C  C     . GLU B  1  215  ? -17.006 12.135  129.106 1.00 44.44 ? 213  GLU B C     1 
ATOM   10498 O  O     . GLU B  1  215  ? -17.895 11.369  129.492 1.00 41.32 ? 213  GLU B O     1 
ATOM   10499 C  CB    . GLU B  1  215  ? -15.553 12.765  131.047 1.00 39.97 ? 213  GLU B CB    1 
ATOM   10500 N  N     . LYS B  1  216  ? -17.214 13.061  128.168 1.00 38.51 ? 214  LYS B N     1 
ATOM   10501 C  CA    . LYS B  1  216  ? -18.482 13.176  127.458 1.00 45.03 ? 214  LYS B CA    1 
ATOM   10502 C  C     . LYS B  1  216  ? -18.588 12.225  126.273 1.00 49.03 ? 214  LYS B C     1 
ATOM   10503 O  O     . LYS B  1  216  ? -19.688 12.063  125.731 1.00 41.85 ? 214  LYS B O     1 
ATOM   10504 C  CB    . LYS B  1  216  ? -18.692 14.611  126.967 1.00 41.99 ? 214  LYS B CB    1 
ATOM   10505 C  CG    . LYS B  1  216  ? -18.898 15.639  128.073 1.00 45.59 ? 214  LYS B CG    1 
ATOM   10506 C  CD    . LYS B  1  216  ? -18.878 17.051  127.505 1.00 54.86 ? 214  LYS B CD    1 
ATOM   10507 C  CE    . LYS B  1  216  ? -18.994 18.094  128.604 1.00 60.49 ? 214  LYS B CE    1 
ATOM   10508 N  NZ    . LYS B  1  216  ? -18.249 19.340  128.258 1.00 67.08 ? 214  LYS B NZ    1 
ATOM   10509 N  N     . GLY B  1  217  ? -17.488 11.595  125.860 1.00 39.45 ? 215  GLY B N     1 
ATOM   10510 C  CA    . GLY B  1  217  ? -17.503 10.664  124.749 1.00 33.78 ? 215  GLY B CA    1 
ATOM   10511 C  C     . GLY B  1  217  ? -16.700 11.098  123.539 1.00 39.87 ? 215  GLY B C     1 
ATOM   10512 O  O     . GLY B  1  217  ? -16.706 10.382  122.529 1.00 38.68 ? 215  GLY B O     1 
ATOM   10513 N  N     . PHE B  1  218  ? -16.039 12.252  123.588 1.00 33.49 ? 216  PHE B N     1 
ATOM   10514 C  CA    . PHE B  1  218  ? -15.113 12.620  122.525 1.00 35.86 ? 216  PHE B CA    1 
ATOM   10515 C  C     . PHE B  1  218  ? -13.817 11.827  122.663 1.00 34.33 ? 216  PHE B C     1 
ATOM   10516 O  O     . PHE B  1  218  ? -13.516 11.258  123.716 1.00 34.01 ? 216  PHE B O     1 
ATOM   10517 C  CB    . PHE B  1  218  ? -14.788 14.117  122.558 1.00 33.91 ? 216  PHE B CB    1 
ATOM   10518 C  CG    . PHE B  1  218  ? -15.935 15.012  122.175 1.00 38.11 ? 216  PHE B CG    1 
ATOM   10519 C  CD1   . PHE B  1  218  ? -16.924 15.332  123.095 1.00 37.89 ? 216  PHE B CD1   1 
ATOM   10520 C  CD2   . PHE B  1  218  ? -16.003 15.570  120.905 1.00 37.61 ? 216  PHE B CD2   1 
ATOM   10521 C  CE1   . PHE B  1  218  ? -17.971 16.171  122.746 1.00 37.58 ? 216  PHE B CE1   1 
ATOM   10522 C  CE2   . PHE B  1  218  ? -17.046 16.413  120.552 1.00 40.64 ? 216  PHE B CE2   1 
ATOM   10523 C  CZ    . PHE B  1  218  ? -18.033 16.710  121.475 1.00 38.43 ? 216  PHE B CZ    1 
ATOM   10524 N  N     . SER B  1  219  ? -13.052 11.781  121.576 1.00 31.07 ? 217  SER B N     1 
ATOM   10525 C  CA    . SER B  1  219  ? -11.690 11.266  121.607 1.00 30.71 ? 217  SER B CA    1 
ATOM   10526 C  C     . SER B  1  219  ? -10.781 12.296  120.961 1.00 29.08 ? 217  SER B C     1 
ATOM   10527 O  O     . SER B  1  219  ? -11.231 13.344  120.491 1.00 30.53 ? 217  SER B O     1 
ATOM   10528 C  CB    . SER B  1  219  ? -11.565 9.919   120.890 1.00 29.08 ? 217  SER B CB    1 
ATOM   10529 O  OG    . SER B  1  219  ? -11.899 10.062  119.520 1.00 33.12 ? 217  SER B OG    1 
ATOM   10530 N  N     . TYR B  1  220  ? -9.485  11.998  120.936 1.00 27.40 ? 218  TYR B N     1 
ATOM   10531 C  CA    . TYR B  1  220  ? -8.521  12.990  120.499 1.00 26.53 ? 218  TYR B CA    1 
ATOM   10532 C  C     . TYR B  1  220  ? -7.513  12.391  119.536 1.00 23.93 ? 218  TYR B C     1 
ATOM   10533 O  O     . TYR B  1  220  ? -7.191  11.204  119.591 1.00 25.82 ? 218  TYR B O     1 
ATOM   10534 C  CB    . TYR B  1  220  ? -7.785  13.607  121.696 1.00 23.73 ? 218  TYR B CB    1 
ATOM   10535 C  CG    . TYR B  1  220  ? -8.569  14.724  122.336 1.00 26.87 ? 218  TYR B CG    1 
ATOM   10536 C  CD1   . TYR B  1  220  ? -9.566  14.459  123.275 1.00 30.04 ? 218  TYR B CD1   1 
ATOM   10537 C  CD2   . TYR B  1  220  ? -8.325  16.047  121.987 1.00 23.49 ? 218  TYR B CD2   1 
ATOM   10538 C  CE1   . TYR B  1  220  ? -10.294 15.490  123.855 1.00 29.19 ? 218  TYR B CE1   1 
ATOM   10539 C  CE2   . TYR B  1  220  ? -9.045  17.079  122.558 1.00 30.35 ? 218  TYR B CE2   1 
ATOM   10540 C  CZ    . TYR B  1  220  ? -10.030 16.796  123.484 1.00 27.98 ? 218  TYR B CZ    1 
ATOM   10541 O  OH    . TYR B  1  220  ? -10.742 17.827  124.050 1.00 32.97 ? 218  TYR B OH    1 
ATOM   10542 N  N     . SER B  1  221  ? -7.031  13.247  118.645 1.00 24.17 ? 219  SER B N     1 
ATOM   10543 C  CA    . SER B  1  221  ? -5.855  12.985  117.832 1.00 22.48 ? 219  SER B CA    1 
ATOM   10544 C  C     . SER B  1  221  ? -4.995  14.236  117.896 1.00 24.50 ? 219  SER B C     1 
ATOM   10545 O  O     . SER B  1  221  ? -5.420  15.302  117.446 1.00 25.01 ? 219  SER B O     1 
ATOM   10546 C  CB    . SER B  1  221  ? -6.237  12.672  116.384 1.00 26.06 ? 219  SER B CB    1 
ATOM   10547 O  OG    . SER B  1  221  ? -5.076  12.460  115.614 1.00 25.15 ? 219  SER B OG    1 
ATOM   10548 N  N     . TYR B  1  222  ? -3.800  14.117  118.463 1.00 24.92 ? 220  TYR B N     1 
ATOM   10549 C  CA    . TYR B  1  222  ? -2.955  15.285  118.676 1.00 22.84 ? 220  TYR B CA    1 
ATOM   10550 C  C     . TYR B  1  222  ? -2.075  15.579  117.474 1.00 23.29 ? 220  TYR B C     1 
ATOM   10551 O  O     . TYR B  1  222  ? -1.491  14.675  116.872 1.00 25.09 ? 220  TYR B O     1 
ATOM   10552 C  CB    . TYR B  1  222  ? -2.101  15.089  119.925 1.00 21.19 ? 220  TYR B CB    1 
ATOM   10553 C  CG    . TYR B  1  222  ? -2.987  14.942  121.114 1.00 21.81 ? 220  TYR B CG    1 
ATOM   10554 C  CD1   . TYR B  1  222  ? -3.586  16.055  121.677 1.00 25.15 ? 220  TYR B CD1   1 
ATOM   10555 C  CD2   . TYR B  1  222  ? -3.290  13.691  121.634 1.00 22.60 ? 220  TYR B CD2   1 
ATOM   10556 C  CE1   . TYR B  1  222  ? -4.431  15.941  122.743 1.00 24.71 ? 220  TYR B CE1   1 
ATOM   10557 C  CE2   . TYR B  1  222  ? -4.140  13.562  122.724 1.00 25.62 ? 220  TYR B CE2   1 
ATOM   10558 C  CZ    . TYR B  1  222  ? -4.702  14.695  123.272 1.00 25.72 ? 220  TYR B CZ    1 
ATOM   10559 O  OH    . TYR B  1  222  ? -5.558  14.595  124.330 1.00 27.20 ? 220  TYR B OH    1 
ATOM   10560 N  N     . ASP B  1  223  ? -1.977  16.865  117.153 1.00 23.63 ? 221  ASP B N     1 
ATOM   10561 C  CA    . ASP B  1  223  ? -1.254  17.392  116.000 1.00 26.89 ? 221  ASP B CA    1 
ATOM   10562 C  C     . ASP B  1  223  ? -0.150  18.274  116.562 1.00 29.15 ? 221  ASP B C     1 
ATOM   10563 O  O     . ASP B  1  223  ? -0.419  19.376  117.044 1.00 29.90 ? 221  ASP B O     1 
ATOM   10564 C  CB    . ASP B  1  223  ? -2.210  18.162  115.094 1.00 28.32 ? 221  ASP B CB    1 
ATOM   10565 C  CG    . ASP B  1  223  ? -1.494  19.039  114.084 1.00 32.22 ? 221  ASP B CG    1 
ATOM   10566 O  OD1   . ASP B  1  223  ? -0.347  18.722  113.713 1.00 32.75 ? 221  ASP B OD1   1 
ATOM   10567 O  OD2   . ASP B  1  223  ? -2.092  20.054  113.672 1.00 37.43 ? 221  ASP B OD2   1 
ATOM   10568 N  N     . MET B  1  224  ? 1.085   17.784  116.532 1.00 27.16 ? 222  MET B N     1 
ATOM   10569 C  CA    . MET B  1  224  ? 2.187   18.498  117.154 1.00 30.16 ? 222  MET B CA    1 
ATOM   10570 C  C     . MET B  1  224  ? 2.711   19.653  116.297 1.00 32.80 ? 222  MET B C     1 
ATOM   10571 O  O     . MET B  1  224  ? 3.797   20.169  116.582 1.00 44.27 ? 222  MET B O     1 
ATOM   10572 C  CB    . MET B  1  224  ? 3.311   17.517  117.497 1.00 34.45 ? 222  MET B CB    1 
ATOM   10573 C  CG    . MET B  1  224  ? 2.870   16.395  118.440 1.00 33.82 ? 222  MET B CG    1 
ATOM   10574 S  SD    . MET B  1  224  ? 2.127   16.977  119.980 1.00 34.99 ? 222  MET B SD    1 
ATOM   10575 C  CE    . MET B  1  224  ? 3.536   17.812  120.689 1.00 32.28 ? 222  MET B CE    1 
ATOM   10576 N  N     . LEU B  1  225  ? 1.964   20.058  115.274 1.00 40.16 ? 223  LEU B N     1 
ATOM   10577 C  CA    . LEU B  1  225  ? 2.194   21.314  114.549 1.00 29.04 ? 223  LEU B CA    1 
ATOM   10578 C  C     . LEU B  1  225  ? 3.573   21.366  113.890 1.00 52.25 ? 223  LEU B C     1 
ATOM   10579 O  O     . LEU B  1  225  ? 4.218   22.416  113.834 1.00 60.14 ? 223  LEU B O     1 
ATOM   10580 C  CB    . LEU B  1  225  ? 1.976   22.523  115.459 1.00 33.37 ? 223  LEU B CB    1 
ATOM   10581 C  CG    . LEU B  1  225  ? 0.488   22.783  115.746 1.00 39.57 ? 223  LEU B CG    1 
ATOM   10582 C  CD1   . LEU B  1  225  ? 0.293   24.020  116.615 1.00 38.38 ? 223  LEU B CD1   1 
ATOM   10583 C  CD2   . LEU B  1  225  ? -0.329  22.882  114.449 1.00 36.02 ? 223  LEU B CD2   1 
ATOM   10584 N  N     . GLY B  1  226  ? 4.020   20.232  113.367 1.00 44.55 ? 224  GLY B N     1 
ATOM   10585 C  CA    . GLY B  1  226  ? 5.229   20.163  112.559 1.00 39.76 ? 224  GLY B CA    1 
ATOM   10586 C  C     . GLY B  1  226  ? 4.860   19.904  111.109 1.00 34.03 ? 224  GLY B C     1 
ATOM   10587 O  O     . GLY B  1  226  ? 3.959   19.114  110.825 1.00 33.41 ? 224  GLY B O     1 
ATOM   10588 N  N     . GLU B  1  227  ? 5.538   20.597  110.201 1.00 36.84 ? 225  GLU B N     1 
ATOM   10589 C  CA    . GLU B  1  227  ? 5.364   20.310  108.784 1.00 34.19 ? 225  GLU B CA    1 
ATOM   10590 C  C     . GLU B  1  227  ? 6.453   21.019  108.002 1.00 28.86 ? 225  GLU B C     1 
ATOM   10591 O  O     . GLU B  1  227  ? 7.085   21.961  108.490 1.00 29.96 ? 225  GLU B O     1 
ATOM   10592 C  CB    . GLU B  1  227  ? 3.984   20.732  108.272 1.00 37.28 ? 225  GLU B CB    1 
ATOM   10593 C  CG    . GLU B  1  227  ? 3.780   22.219  108.116 1.00 32.17 ? 225  GLU B CG    1 
ATOM   10594 C  CD    . GLU B  1  227  ? 2.361   22.528  107.683 1.00 45.04 ? 225  GLU B CD    1 
ATOM   10595 O  OE1   . GLU B  1  227  ? 1.482   22.617  108.563 1.00 37.25 ? 225  GLU B OE1   1 
ATOM   10596 O  OE2   . GLU B  1  227  ? 2.120   22.646  106.461 1.00 35.42 ? 225  GLU B OE2   1 
ATOM   10597 N  N     . ALA B  1  228  ? 6.665   20.536  106.782 1.00 25.30 ? 226  ALA B N     1 
ATOM   10598 C  CA    . ALA B  1  228  ? 7.542   21.175  105.811 1.00 24.21 ? 226  ALA B CA    1 
ATOM   10599 C  C     . ALA B  1  228  ? 8.918   21.459  106.410 1.00 28.04 ? 226  ALA B C     1 
ATOM   10600 O  O     . ALA B  1  228  ? 9.371   22.603  106.493 1.00 29.75 ? 226  ALA B O     1 
ATOM   10601 C  CB    . ALA B  1  228  ? 6.901   22.454  105.264 1.00 27.31 ? 226  ALA B CB    1 
ATOM   10602 N  N     . ALA B  1  229  ? 9.573   20.387  106.855 1.00 23.35 ? 227  ALA B N     1 
ATOM   10603 C  CA    . ALA B  1  229  ? 10.966  20.490  107.267 1.00 22.49 ? 227  ALA B CA    1 
ATOM   10604 C  C     . ALA B  1  229  ? 11.790  21.112  106.149 1.00 18.82 ? 227  ALA B C     1 
ATOM   10605 O  O     . ALA B  1  229  ? 11.664  20.729  104.985 1.00 23.60 ? 227  ALA B O     1 
ATOM   10606 C  CB    . ALA B  1  229  ? 11.514  19.109  107.625 1.00 21.65 ? 227  ALA B CB    1 
ATOM   10607 N  N     . THR B  1  230  ? 12.618  22.089  106.508 1.00 21.98 ? 228  THR B N     1 
ATOM   10608 C  CA    . THR B  1  230  ? 13.514  22.730  105.553 1.00 21.93 ? 228  THR B CA    1 
ATOM   10609 C  C     . THR B  1  230  ? 14.917  22.146  105.583 1.00 22.01 ? 228  THR B C     1 
ATOM   10610 O  O     . THR B  1  230  ? 15.584  22.089  104.544 1.00 21.15 ? 228  THR B O     1 
ATOM   10611 C  CB    . THR B  1  230  ? 13.587  24.237  105.839 1.00 22.53 ? 228  THR B CB    1 
ATOM   10612 O  OG1   . THR B  1  230  ? 12.255  24.766  105.867 1.00 29.16 ? 228  THR B OG1   1 
ATOM   10613 C  CG2   . THR B  1  230  ? 14.364  24.954  104.755 1.00 23.36 ? 228  THR B CG2   1 
ATOM   10614 N  N     . THR B  1  231  ? 15.360  21.685  106.744 1.00 20.86 ? 229  THR B N     1 
ATOM   10615 C  CA    . THR B  1  231  ? 16.700  21.152  106.918 1.00 17.48 ? 229  THR B CA    1 
ATOM   10616 C  C     . THR B  1  231  ? 16.619  19.783  107.573 1.00 21.03 ? 229  THR B C     1 
ATOM   10617 O  O     . THR B  1  231  ? 15.596  19.402  108.143 1.00 18.51 ? 229  THR B O     1 
ATOM   10618 C  CB    . THR B  1  231  ? 17.557  22.064  107.792 1.00 19.85 ? 229  THR B CB    1 
ATOM   10619 O  OG1   . THR B  1  231  ? 17.084  21.996  109.151 1.00 22.88 ? 229  THR B OG1   1 
ATOM   10620 C  CG2   . THR B  1  231  ? 17.497  23.512  107.298 1.00 20.42 ? 229  THR B CG2   1 
ATOM   10621 N  N     . ALA B  1  232  ? 17.743  19.066  107.514 1.00 18.67 ? 230  ALA B N     1 
ATOM   10622 C  CA    . ALA B  1  232  ? 17.843  17.800  108.227 1.00 21.51 ? 230  ALA B CA    1 
ATOM   10623 C  C     . ALA B  1  232  ? 17.566  17.980  109.709 1.00 23.28 ? 230  ALA B C     1 
ATOM   10624 O  O     . ALA B  1  232  ? 16.907  17.138  110.330 1.00 22.28 ? 230  ALA B O     1 
ATOM   10625 C  CB    . ALA B  1  232  ? 19.222  17.188  108.010 1.00 21.45 ? 230  ALA B CB    1 
ATOM   10626 N  N     . ALA B  1  233  ? 18.069  19.067  110.298 1.00 20.94 ? 231  ALA B N     1 
ATOM   10627 C  CA    . ALA B  1  233  ? 17.868  19.290  111.727 1.00 21.85 ? 231  ALA B CA    1 
ATOM   10628 C  C     . ALA B  1  233  ? 16.394  19.487  112.050 1.00 22.68 ? 231  ALA B C     1 
ATOM   10629 O  O     . ALA B  1  233  ? 15.917  19.027  113.097 1.00 22.57 ? 231  ALA B O     1 
ATOM   10630 C  CB    . ALA B  1  233  ? 18.689  20.495  112.183 1.00 20.94 ? 231  ALA B CB    1 
ATOM   10631 N  N     . ASP B  1  234  ? 15.660  20.172  111.161 1.00 19.40 ? 232  ASP B N     1 
ATOM   10632 C  CA    . ASP B  1  234  ? 14.215  20.326  111.330 1.00 19.92 ? 232  ASP B CA    1 
ATOM   10633 C  C     . ASP B  1  234  ? 13.532  18.970  111.387 1.00 20.47 ? 232  ASP B C     1 
ATOM   10634 O  O     . ASP B  1  234  ? 12.713  18.705  112.274 1.00 21.74 ? 232  ASP B O     1 
ATOM   10635 C  CB    . ASP B  1  234  ? 13.604  21.114  110.168 1.00 21.68 ? 232  ASP B CB    1 
ATOM   10636 C  CG    . ASP B  1  234  ? 14.017  22.554  110.131 1.00 28.47 ? 232  ASP B CG    1 
ATOM   10637 O  OD1   . ASP B  1  234  ? 14.400  23.112  111.171 1.00 28.68 ? 232  ASP B OD1   1 
ATOM   10638 O  OD2   . ASP B  1  234  ? 13.912  23.132  109.030 1.00 28.47 ? 232  ASP B OD2   1 
ATOM   10639 N  N     . ALA B  1  235  ? 13.821  18.115  110.403 1.00 18.43 ? 233  ALA B N     1 
ATOM   10640 C  CA    . ALA B  1  235  ? 13.132  16.839  110.306 1.00 18.86 ? 233  ALA B CA    1 
ATOM   10641 C  C     . ALA B  1  235  ? 13.484  15.954  111.487 1.00 21.56 ? 233  ALA B C     1 
ATOM   10642 O  O     . ALA B  1  235  ? 12.626  15.250  112.028 1.00 20.66 ? 233  ALA B O     1 
ATOM   10643 C  CB    . ALA B  1  235  ? 13.490  16.152  108.991 1.00 19.99 ? 233  ALA B CB    1 
ATOM   10644 N  N     . GLU B  1  236  ? 14.747  15.987  111.912 1.00 20.18 ? 234  GLU B N     1 
ATOM   10645 C  CA    . GLU B  1  236  ? 15.133  15.201  113.074 1.00 21.46 ? 234  GLU B CA    1 
ATOM   10646 C  C     . GLU B  1  236  ? 14.427  15.692  114.331 1.00 21.00 ? 234  GLU B C     1 
ATOM   10647 O  O     . GLU B  1  236  ? 13.996  14.886  115.165 1.00 21.77 ? 234  GLU B O     1 
ATOM   10648 C  CB    . GLU B  1  236  ? 16.652  15.241  113.244 1.00 22.18 ? 234  GLU B CB    1 
ATOM   10649 C  CG    . GLU B  1  236  ? 17.158  14.240  114.255 1.00 24.95 ? 234  GLU B CG    1 
ATOM   10650 C  CD    . GLU B  1  236  ? 18.663  14.302  114.417 1.00 38.26 ? 234  GLU B CD    1 
ATOM   10651 O  OE1   . GLU B  1  236  ? 19.307  15.115  113.719 1.00 42.50 ? 234  GLU B OE1   1 
ATOM   10652 O  OE2   . GLU B  1  236  ? 19.198  13.536  115.239 1.00 38.75 ? 234  GLU B OE2   1 
ATOM   10653 N  N     . ARG B  1  237  ? 14.272  17.009  114.472 1.00 19.95 ? 235  ARG B N     1 
ATOM   10654 C  CA    . ARG B  1  237  ? 13.557  17.533  115.626 1.00 22.44 ? 235  ARG B CA    1 
ATOM   10655 C  C     . ARG B  1  237  ? 12.089  17.126  115.594 1.00 21.44 ? 235  ARG B C     1 
ATOM   10656 O  O     . ARG B  1  237  ? 11.540  16.677  116.608 1.00 22.28 ? 235  ARG B O     1 
ATOM   10657 C  CB    . ARG B  1  237  ? 13.687  19.052  115.684 1.00 22.59 ? 235  ARG B CB    1 
ATOM   10658 C  CG    . ARG B  1  237  ? 12.978  19.619  116.889 1.00 26.20 ? 235  ARG B CG    1 
ATOM   10659 C  CD    . ARG B  1  237  ? 12.752  21.105  116.814 1.00 34.29 ? 235  ARG B CD    1 
ATOM   10660 N  NE    . ARG B  1  237  ? 12.089  21.537  118.038 1.00 39.45 ? 235  ARG B NE    1 
ATOM   10661 C  CZ    . ARG B  1  237  ? 12.109  22.773  118.513 1.00 39.82 ? 235  ARG B CZ    1 
ATOM   10662 N  NH1   . ARG B  1  237  ? 12.737  23.747  117.876 1.00 42.52 ? 235  ARG B NH1   1 
ATOM   10663 N  NH2   . ARG B  1  237  ? 11.490  23.035  119.662 1.00 34.36 ? 235  ARG B NH2   1 
ATOM   10664 N  N     . TYR B  1  238  ? 11.435  17.285  114.440 1.00 20.23 ? 236  TYR B N     1 
ATOM   10665 C  CA    . TYR B  1  238  ? 10.029  16.898  114.334 1.00 19.78 ? 236  TYR B CA    1 
ATOM   10666 C  C     . TYR B  1  238  ? 9.852   15.419  114.642 1.00 21.00 ? 236  TYR B C     1 
ATOM   10667 O  O     . TYR B  1  238  ? 8.891   15.027  115.318 1.00 19.56 ? 236  TYR B O     1 
ATOM   10668 C  CB    . TYR B  1  238  ? 9.482   17.217  112.941 1.00 19.90 ? 236  TYR B CB    1 
ATOM   10669 C  CG    . TYR B  1  238  ? 9.293   18.688  112.643 1.00 23.54 ? 236  TYR B CG    1 
ATOM   10670 C  CD1   . TYR B  1  238  ? 8.850   19.572  113.618 1.00 29.84 ? 236  TYR B CD1   1 
ATOM   10671 C  CD2   . TYR B  1  238  ? 9.571   19.189  111.381 1.00 23.44 ? 236  TYR B CD2   1 
ATOM   10672 C  CE1   . TYR B  1  238  ? 8.680   20.925  113.330 1.00 35.46 ? 236  TYR B CE1   1 
ATOM   10673 C  CE2   . TYR B  1  238  ? 9.398   20.527  111.079 1.00 29.20 ? 236  TYR B CE2   1 
ATOM   10674 C  CZ    . TYR B  1  238  ? 8.961   21.392  112.057 1.00 39.24 ? 236  TYR B CZ    1 
ATOM   10675 O  OH    . TYR B  1  238  ? 8.806   22.724  111.747 1.00 34.88 ? 236  TYR B OH    1 
ATOM   10676 N  N     . TYR B  1  239  ? 10.780  14.582  114.171 1.00 19.67 ? 237  TYR B N     1 
ATOM   10677 C  CA    . TYR B  1  239  ? 10.733  13.165  114.510 1.00 19.13 ? 237  TYR B CA    1 
ATOM   10678 C  C     . TYR B  1  239  ? 10.806  12.960  116.015 1.00 21.51 ? 237  TYR B C     1 
ATOM   10679 O  O     . TYR B  1  239  ? 10.013  12.205  116.595 1.00 21.62 ? 237  TYR B O     1 
ATOM   10680 C  CB    . TYR B  1  239  ? 11.875  12.420  113.819 1.00 20.70 ? 237  TYR B CB    1 
ATOM   10681 C  CG    . TYR B  1  239  ? 12.023  10.993  114.287 1.00 22.99 ? 237  TYR B CG    1 
ATOM   10682 C  CD1   . TYR B  1  239  ? 11.181  10.000  113.811 1.00 24.36 ? 237  TYR B CD1   1 
ATOM   10683 C  CD2   . TYR B  1  239  ? 12.993  10.636  115.207 1.00 31.55 ? 237  TYR B CD2   1 
ATOM   10684 C  CE1   . TYR B  1  239  ? 11.307  8.698   114.237 1.00 21.92 ? 237  TYR B CE1   1 
ATOM   10685 C  CE2   . TYR B  1  239  ? 13.119  9.329   115.639 1.00 35.54 ? 237  TYR B CE2   1 
ATOM   10686 C  CZ    . TYR B  1  239  ? 12.275  8.364   115.140 1.00 30.75 ? 237  TYR B CZ    1 
ATOM   10687 O  OH    . TYR B  1  239  ? 12.395  7.062   115.567 1.00 35.46 ? 237  TYR B OH    1 
ATOM   10688 N  N     . ARG B  1  240  ? 11.764  13.619  116.671 1.00 22.23 ? 238  ARG B N     1 
ATOM   10689 C  CA    . ARG B  1  240  ? 11.908  13.430  118.103 1.00 23.88 ? 238  ARG B CA    1 
ATOM   10690 C  C     . ARG B  1  240  ? 10.704  13.970  118.855 1.00 20.87 ? 238  ARG B C     1 
ATOM   10691 O  O     . ARG B  1  240  ? 10.316  13.401  119.879 1.00 22.70 ? 238  ARG B O     1 
ATOM   10692 C  CB    . ARG B  1  240  ? 13.195  14.095  118.602 1.00 23.59 ? 238  ARG B CB    1 
ATOM   10693 C  CG    . ARG B  1  240  ? 14.469  13.418  118.106 1.00 23.03 ? 238  ARG B CG    1 
ATOM   10694 C  CD    . ARG B  1  240  ? 14.577  11.994  118.615 1.00 29.18 ? 238  ARG B CD    1 
ATOM   10695 N  NE    . ARG B  1  240  ? 15.678  11.301  117.960 1.00 33.09 ? 238  ARG B NE    1 
ATOM   10696 C  CZ    . ARG B  1  240  ? 15.899  9.997   118.040 1.00 41.87 ? 238  ARG B CZ    1 
ATOM   10697 N  NH1   . ARG B  1  240  ? 15.096  9.202   118.724 1.00 35.34 ? 238  ARG B NH1   1 
ATOM   10698 N  NH2   . ARG B  1  240  ? 16.953  9.478   117.418 1.00 45.90 ? 238  ARG B NH2   1 
ATOM   10699 N  N     . ASP B  1  241  ? 10.101  15.052  118.358 1.00 22.39 ? 239  ASP B N     1 
ATOM   10700 C  CA    . ASP B  1  241  ? 8.904   15.599  118.989 1.00 23.69 ? 239  ASP B CA    1 
ATOM   10701 C  C     . ASP B  1  241  ? 7.716   14.650  118.840 1.00 20.82 ? 239  ASP B C     1 
ATOM   10702 O  O     . ASP B  1  241  ? 6.943   14.474  119.786 1.00 23.78 ? 239  ASP B O     1 
ATOM   10703 C  CB    . ASP B  1  241  ? 8.584   16.973  118.404 1.00 24.37 ? 239  ASP B CB    1 
ATOM   10704 C  CG    . ASP B  1  241  ? 9.541   18.062  118.897 1.00 31.29 ? 239  ASP B CG    1 
ATOM   10705 O  OD1   . ASP B  1  241  ? 10.322  17.812  119.845 1.00 34.43 ? 239  ASP B OD1   1 
ATOM   10706 O  OD2   . ASP B  1  241  ? 9.504   19.169  118.324 1.00 39.45 ? 239  ASP B OD2   1 
ATOM   10707 N  N     . TYR B  1  242  ? 7.567   14.018  117.672 1.00 22.80 ? 240  TYR B N     1 
ATOM   10708 C  CA    . TYR B  1  242  ? 6.534   12.999  117.507 1.00 23.48 ? 240  TYR B CA    1 
ATOM   10709 C  C     . TYR B  1  242  ? 6.772   11.825  118.441 1.00 23.15 ? 240  TYR B C     1 
ATOM   10710 O  O     . TYR B  1  242  ? 5.839   11.312  119.073 1.00 20.74 ? 240  TYR B O     1 
ATOM   10711 C  CB    . TYR B  1  242  ? 6.516   12.489  116.073 1.00 20.34 ? 240  TYR B CB    1 
ATOM   10712 C  CG    . TYR B  1  242  ? 5.906   13.399  115.038 1.00 19.36 ? 240  TYR B CG    1 
ATOM   10713 C  CD1   . TYR B  1  242  ? 4.804   14.199  115.324 1.00 22.20 ? 240  TYR B CD1   1 
ATOM   10714 C  CD2   . TYR B  1  242  ? 6.421   13.426  113.761 1.00 19.43 ? 240  TYR B CD2   1 
ATOM   10715 C  CE1   . TYR B  1  242  ? 4.237   15.019  114.327 1.00 23.81 ? 240  TYR B CE1   1 
ATOM   10716 C  CE2   . TYR B  1  242  ? 5.875   14.229  112.782 1.00 21.80 ? 240  TYR B CE2   1 
ATOM   10717 C  CZ    . TYR B  1  242  ? 4.792   15.019  113.064 1.00 24.10 ? 240  TYR B CZ    1 
ATOM   10718 O  OH    . TYR B  1  242  ? 4.274   15.799  112.043 1.00 23.78 ? 240  TYR B OH    1 
ATOM   10719 N  N     . GLU B  1  243  ? 8.022   11.362  118.510 1.00 20.66 ? 241  GLU B N     1 
ATOM   10720 C  CA    . GLU B  1  243  ? 8.359   10.239  119.376 1.00 20.98 ? 241  GLU B CA    1 
ATOM   10721 C  C     . GLU B  1  243  ? 8.003   10.546  120.824 1.00 22.80 ? 241  GLU B C     1 
ATOM   10722 O  O     . GLU B  1  243  ? 7.388   9.728   121.520 1.00 22.30 ? 241  GLU B O     1 
ATOM   10723 C  CB    . GLU B  1  243  ? 9.850   9.925   119.234 1.00 21.76 ? 241  GLU B CB    1 
ATOM   10724 C  CG    . GLU B  1  243  ? 10.341  8.790   120.088 1.00 26.44 ? 241  GLU B CG    1 
ATOM   10725 C  CD    . GLU B  1  243  ? 11.854  8.675   120.048 1.00 32.38 ? 241  GLU B CD    1 
ATOM   10726 O  OE1   . GLU B  1  243  ? 12.522  9.710   119.876 1.00 31.82 ? 241  GLU B OE1   1 
ATOM   10727 O  OE2   . GLU B  1  243  ? 12.375  7.550   120.189 1.00 34.79 ? 241  GLU B OE2   1 
ATOM   10728 N  N     . SER B  1  244  ? 8.381   11.736  121.292 1.00 20.67 ? 242  SER B N     1 
ATOM   10729 C  CA    . SER B  1  244  ? 8.087   12.120  122.663 1.00 20.99 ? 242  SER B CA    1 
ATOM   10730 C  C     . SER B  1  244  ? 6.583   12.214  122.897 1.00 21.80 ? 242  SER B C     1 
ATOM   10731 O  O     . SER B  1  244  ? 6.073   11.760  123.928 1.00 21.77 ? 242  SER B O     1 
ATOM   10732 C  CB    . SER B  1  244  ? 8.775   13.448  122.964 1.00 23.95 ? 242  SER B CB    1 
ATOM   10733 O  OG    . SER B  1  244  ? 8.397   13.912  124.239 1.00 30.39 ? 242  SER B OG    1 
ATOM   10734 N  N     . ALA B  1  245  ? 5.852   12.766  121.924 1.00 23.40 ? 243  ALA B N     1 
ATOM   10735 C  CA    . ALA B  1  245  ? 4.403   12.867  122.063 1.00 21.13 ? 243  ALA B CA    1 
ATOM   10736 C  C     . ALA B  1  245  ? 3.747   11.492  122.089 1.00 23.92 ? 243  ALA B C     1 
ATOM   10737 O  O     . ALA B  1  245  ? 2.786   11.274  122.834 1.00 23.50 ? 243  ALA B O     1 
ATOM   10738 C  CB    . ALA B  1  245  ? 3.825   13.715  120.932 1.00 21.76 ? 243  ALA B CB    1 
ATOM   10739 N  N     . ILE B  1  246  ? 4.242   10.552  121.284 1.00 21.64 ? 244  ILE B N     1 
ATOM   10740 C  CA    . ILE B  1  246  ? 3.656   9.211   121.292 1.00 23.36 ? 244  ILE B CA    1 
ATOM   10741 C  C     . ILE B  1  246  ? 3.798   8.564   122.662 1.00 23.92 ? 244  ILE B C     1 
ATOM   10742 O  O     . ILE B  1  246  ? 2.865   7.922   123.159 1.00 25.89 ? 244  ILE B O     1 
ATOM   10743 C  CB    . ILE B  1  246  ? 4.282   8.345   120.185 1.00 22.05 ? 244  ILE B CB    1 
ATOM   10744 C  CG1   . ILE B  1  246  ? 3.801   8.835   118.825 1.00 24.65 ? 244  ILE B CG1   1 
ATOM   10745 C  CG2   . ILE B  1  246  ? 3.902   6.888   120.375 1.00 24.50 ? 244  ILE B CG2   1 
ATOM   10746 C  CD1   . ILE B  1  246  ? 4.458   8.130   117.632 1.00 25.76 ? 244  ILE B CD1   1 
ATOM   10747 N  N     . HIS B  1  247  ? 4.958   8.721   123.302 1.00 23.98 ? 245  HIS B N     1 
ATOM   10748 C  CA    . HIS B  1  247  ? 5.107   8.187   124.651 1.00 23.89 ? 245  HIS B CA    1 
ATOM   10749 C  C     . HIS B  1  247  ? 4.105   8.819   125.604 1.00 23.58 ? 245  HIS B C     1 
ATOM   10750 O  O     . HIS B  1  247  ? 3.484   8.121   126.400 1.00 26.32 ? 245  HIS B O     1 
ATOM   10751 C  CB    . HIS B  1  247  ? 6.533   8.396   125.162 1.00 24.01 ? 245  HIS B CB    1 
ATOM   10752 C  CG    . HIS B  1  247  ? 7.529   7.464   124.546 1.00 23.36 ? 245  HIS B CG    1 
ATOM   10753 N  ND1   . HIS B  1  247  ? 7.520   6.105   124.785 1.00 26.75 ? 245  HIS B ND1   1 
ATOM   10754 C  CD2   . HIS B  1  247  ? 8.568   7.695   123.710 1.00 24.84 ? 245  HIS B CD2   1 
ATOM   10755 C  CE1   . HIS B  1  247  ? 8.508   5.539   124.114 1.00 29.21 ? 245  HIS B CE1   1 
ATOM   10756 N  NE2   . HIS B  1  247  ? 9.160   6.482   123.455 1.00 28.81 ? 245  HIS B NE2   1 
ATOM   10757 N  N     . ALA B  1  248  ? 3.898   10.135  125.501 1.00 23.14 ? 246  ALA B N     1 
ATOM   10758 C  CA    . ALA B  1  248  ? 2.966   10.800  126.403 1.00 23.40 ? 246  ALA B CA    1 
ATOM   10759 C  C     . ALA B  1  248  ? 1.532   10.394  126.098 1.00 25.37 ? 246  ALA B C     1 
ATOM   10760 O  O     . ALA B  1  248  ? 0.746   10.111  127.010 1.00 27.08 ? 246  ALA B O     1 
ATOM   10761 C  CB    . ALA B  1  248  ? 3.128   12.319  126.298 1.00 23.75 ? 246  ALA B CB    1 
ATOM   10762 N  N     . ILE B  1  249  ? 1.175   10.382  124.810 1.00 24.68 ? 247  ILE B N     1 
ATOM   10763 C  CA    . ILE B  1  249  ? -0.177  10.001  124.417 1.00 26.54 ? 247  ILE B CA    1 
ATOM   10764 C  C     . ILE B  1  249  ? -0.423  8.536   124.734 1.00 26.71 ? 247  ILE B C     1 
ATOM   10765 O  O     . ILE B  1  249  ? -1.491  8.167   125.238 1.00 27.40 ? 247  ILE B O     1 
ATOM   10766 C  CB    . ILE B  1  249  ? -0.398  10.309  122.927 1.00 23.56 ? 247  ILE B CB    1 
ATOM   10767 C  CG1   . ILE B  1  249  ? -0.300  11.809  122.670 1.00 23.20 ? 247  ILE B CG1   1 
ATOM   10768 C  CG2   . ILE B  1  249  ? -1.756  9.744   122.453 1.00 27.14 ? 247  ILE B CG2   1 
ATOM   10769 C  CD1   . ILE B  1  249  ? -0.013  12.159  121.219 1.00 24.73 ? 247  ILE B CD1   1 
ATOM   10770 N  N     . GLY B  1  250  ? 0.574   7.684   124.476 1.00 26.51 ? 248  GLY B N     1 
ATOM   10771 C  CA    . GLY B  1  250  ? 0.404   6.263   124.722 1.00 25.37 ? 248  GLY B CA    1 
ATOM   10772 C  C     . GLY B  1  250  ? 0.239   5.934   126.193 1.00 31.85 ? 248  GLY B C     1 
ATOM   10773 O  O     . GLY B  1  250  ? -0.573  5.078   126.562 1.00 30.82 ? 248  GLY B O     1 
ATOM   10774 N  N     . LYS B  1  251  ? 1.001   6.607   127.059 1.00 27.82 ? 249  LYS B N     1 
ATOM   10775 C  CA    . LYS B  1  251  ? 0.828   6.383   128.489 1.00 30.13 ? 249  LYS B CA    1 
ATOM   10776 C  C     . LYS B  1  251  ? -0.522  6.912   128.960 1.00 29.83 ? 249  LYS B C     1 
ATOM   10777 O  O     . LYS B  1  251  ? -1.203  6.261   129.758 1.00 31.77 ? 249  LYS B O     1 
ATOM   10778 C  CB    . LYS B  1  251  ? 1.977   7.029   129.268 1.00 32.30 ? 249  LYS B CB    1 
ATOM   10779 N  N     . ALA B  1  252  ? -0.940  8.072   128.443 1.00 28.15 ? 250  ALA B N     1 
ATOM   10780 C  CA    . ALA B  1  252  ? -2.245  8.623   128.802 1.00 29.90 ? 250  ALA B CA    1 
ATOM   10781 C  C     . ALA B  1  252  ? -3.382  7.747   128.291 1.00 30.90 ? 250  ALA B C     1 
ATOM   10782 O  O     . ALA B  1  252  ? -4.429  7.646   128.939 1.00 33.28 ? 250  ALA B O     1 
ATOM   10783 C  CB    . ALA B  1  252  ? -2.391  10.042  128.253 1.00 30.59 ? 250  ALA B CB    1 
ATOM   10784 N  N     . SER B  1  253  ? -3.209  7.134   127.117 1.00 29.49 ? 251  SER B N     1 
ATOM   10785 C  CA    . SER B  1  253  ? -4.225  6.211   126.617 1.00 29.28 ? 251  SER B CA    1 
ATOM   10786 C  C     . SER B  1  253  ? -4.494  5.094   127.613 1.00 31.34 ? 251  SER B C     1 
ATOM   10787 O  O     . SER B  1  253  ? -5.649  4.695   127.810 1.00 33.74 ? 251  SER B O     1 
ATOM   10788 C  CB    . SER B  1  253  ? -3.798  5.622   125.279 1.00 29.69 ? 251  SER B CB    1 
ATOM   10789 O  OG    . SER B  1  253  ? -4.787  4.722   124.806 1.00 31.28 ? 251  SER B OG    1 
ATOM   10790 N  N     . ALA B  1  254  ? -3.436  4.567   128.235 1.00 29.74 ? 252  ALA B N     1 
ATOM   10791 C  CA    . ALA B  1  254  ? -3.553  3.581   129.307 1.00 35.58 ? 252  ALA B CA    1 
ATOM   10792 C  C     . ALA B  1  254  ? -4.407  2.390   128.880 1.00 35.21 ? 252  ALA B C     1 
ATOM   10793 O  O     . ALA B  1  254  ? -5.255  1.903   129.631 1.00 37.03 ? 252  ALA B O     1 
ATOM   10794 C  CB    . ALA B  1  254  ? -4.096  4.221   130.585 1.00 36.47 ? 252  ALA B CB    1 
ATOM   10795 N  N     . GLY B  1  255  ? -4.186  1.921   127.653 1.00 37.13 ? 253  GLY B N     1 
ATOM   10796 C  CA    . GLY B  1  255  ? -4.847  0.720   127.187 1.00 36.55 ? 253  GLY B CA    1 
ATOM   10797 C  C     . GLY B  1  255  ? -6.261  0.908   126.691 1.00 38.69 ? 253  GLY B C     1 
ATOM   10798 O  O     . GLY B  1  255  ? -6.948  -0.090  126.453 1.00 42.17 ? 253  GLY B O     1 
ATOM   10799 N  N     . ARG B  1  256  ? -6.721  2.149   126.522 1.00 33.06 ? 254  ARG B N     1 
ATOM   10800 C  CA    . ARG B  1  256  ? -8.081  2.388   126.055 1.00 37.25 ? 254  ARG B CA    1 
ATOM   10801 C  C     . ARG B  1  256  ? -8.298  1.975   124.610 1.00 38.27 ? 254  ARG B C     1 
ATOM   10802 O  O     . ARG B  1  256  ? -9.456  1.896   124.179 1.00 38.01 ? 254  ARG B O     1 
ATOM   10803 C  CB    . ARG B  1  256  ? -8.450  3.863   126.223 1.00 32.16 ? 254  ARG B CB    1 
ATOM   10804 C  CG    . ARG B  1  256  ? -8.950  4.197   127.621 1.00 36.10 ? 254  ARG B CG    1 
ATOM   10805 C  CD    . ARG B  1  256  ? -9.286  5.655   127.740 1.00 36.58 ? 254  ARG B CD    1 
ATOM   10806 N  NE    . ARG B  1  256  ? -8.080  6.473   127.794 1.00 37.77 ? 254  ARG B NE    1 
ATOM   10807 C  CZ    . ARG B  1  256  ? -8.063  7.787   127.638 1.00 33.72 ? 254  ARG B CZ    1 
ATOM   10808 N  NH1   . ARG B  1  256  ? -9.165  8.464   127.359 1.00 36.87 ? 254  ARG B NH1   1 
ATOM   10809 N  NH2   . ARG B  1  256  ? -6.908  8.441   127.765 1.00 36.60 ? 254  ARG B NH2   1 
ATOM   10810 N  N     . GLY B  1  257  ? -7.229  1.711   123.859 1.00 34.79 ? 255  GLY B N     1 
ATOM   10811 C  CA    . GLY B  1  257  ? -7.359  1.288   122.480 1.00 32.94 ? 255  GLY B CA    1 
ATOM   10812 C  C     . GLY B  1  257  ? -7.526  2.449   121.522 1.00 31.80 ? 255  GLY B C     1 
ATOM   10813 O  O     . GLY B  1  257  ? -7.612  3.619   121.897 1.00 33.76 ? 255  GLY B O     1 
ATOM   10814 N  N     . ILE B  1  258  ? -7.610  2.098   120.238 1.00 30.14 ? 256  ILE B N     1 
ATOM   10815 C  CA    . ILE B  1  258  ? -7.522  3.111   119.192 1.00 30.85 ? 256  ILE B CA    1 
ATOM   10816 C  C     . ILE B  1  258  ? -8.821  3.881   118.980 1.00 30.50 ? 256  ILE B C     1 
ATOM   10817 O  O     . ILE B  1  258  ? -8.793  4.957   118.374 1.00 30.42 ? 256  ILE B O     1 
ATOM   10818 C  CB    . ILE B  1  258  ? -7.060  2.461   117.879 1.00 36.84 ? 256  ILE B CB    1 
ATOM   10819 C  CG1   . ILE B  1  258  ? -8.050  1.387   117.442 1.00 33.96 ? 256  ILE B CG1   1 
ATOM   10820 C  CG2   . ILE B  1  258  ? -5.674  1.847   118.054 1.00 29.41 ? 256  ILE B CG2   1 
ATOM   10821 C  CD1   . ILE B  1  258  ? -7.644  0.692   116.165 1.00 33.78 ? 256  ILE B CD1   1 
ATOM   10822 N  N     . TYR B  1  259  ? -9.955  3.386   119.473 1.00 32.77 ? 257  TYR B N     1 
ATOM   10823 C  CA    . TYR B  1  259  ? -11.223 4.073   119.249 1.00 32.77 ? 257  TYR B CA    1 
ATOM   10824 C  C     . TYR B  1  259  ? -11.575 5.020   120.392 1.00 35.63 ? 257  TYR B C     1 
ATOM   10825 O  O     . TYR B  1  259  ? -11.806 6.210   120.157 1.00 33.55 ? 257  TYR B O     1 
ATOM   10826 C  CB    . TYR B  1  259  ? -12.337 3.039   119.012 1.00 33.94 ? 257  TYR B CB    1 
ATOM   10827 C  CG    . TYR B  1  259  ? -11.958 2.088   117.903 1.00 33.20 ? 257  TYR B CG    1 
ATOM   10828 C  CD1   . TYR B  1  259  ? -11.826 2.541   116.598 1.00 35.79 ? 257  TYR B CD1   1 
ATOM   10829 C  CD2   . TYR B  1  259  ? -11.690 0.754   118.159 1.00 37.66 ? 257  TYR B CD2   1 
ATOM   10830 C  CE1   . TYR B  1  259  ? -11.452 1.688   115.576 1.00 39.02 ? 257  TYR B CE1   1 
ATOM   10831 C  CE2   . TYR B  1  259  ? -11.319 -0.108  117.141 1.00 32.18 ? 257  TYR B CE2   1 
ATOM   10832 C  CZ    . TYR B  1  259  ? -11.199 0.367   115.856 1.00 37.44 ? 257  TYR B CZ    1 
ATOM   10833 O  OH    . TYR B  1  259  ? -10.824 -0.484  114.842 1.00 37.53 ? 257  TYR B OH    1 
ATOM   10834 N  N     . GLU B  1  260  ? -11.607 4.518   121.629 1.00 32.62 ? 258  GLU B N     1 
ATOM   10835 C  CA    . GLU B  1  260  ? -11.849 5.392   122.772 1.00 35.56 ? 258  GLU B CA    1 
ATOM   10836 C  C     . GLU B  1  260  ? -10.620 6.231   123.101 1.00 34.26 ? 258  GLU B C     1 
ATOM   10837 O  O     . GLU B  1  260  ? -10.742 7.414   123.446 1.00 37.85 ? 258  GLU B O     1 
ATOM   10838 C  CB    . GLU B  1  260  ? -12.267 4.567   123.995 1.00 34.50 ? 258  GLU B CB    1 
ATOM   10839 C  CG    . GLU B  1  260  ? -12.437 5.402   125.252 1.00 45.99 ? 258  GLU B CG    1 
ATOM   10840 C  CD    . GLU B  1  260  ? -12.618 4.560   126.497 1.00 47.42 ? 258  GLU B CD    1 
ATOM   10841 O  OE1   . GLU B  1  260  ? -12.800 3.330   126.360 1.00 47.73 ? 258  GLU B OE1   1 
ATOM   10842 O  OE2   . GLU B  1  260  ? -12.574 5.131   127.612 1.00 49.73 ? 258  GLU B OE2   1 
ATOM   10843 N  N     . GLY B  1  261  ? -9.433  5.649   122.973 1.00 36.09 ? 259  GLY B N     1 
ATOM   10844 C  CA    . GLY B  1  261  ? -8.218  6.303   123.392 1.00 32.36 ? 259  GLY B CA    1 
ATOM   10845 C  C     . GLY B  1  261  ? -7.672  7.260   122.361 1.00 32.92 ? 259  GLY B C     1 
ATOM   10846 O  O     . GLY B  1  261  ? -8.003  7.195   121.174 1.00 28.95 ? 259  GLY B O     1 
ATOM   10847 N  N     . PRO B  1  262  ? -6.793  8.155   122.808 1.00 26.96 ? 260  PRO B N     1 
ATOM   10848 C  CA    . PRO B  1  262  ? -6.258  9.192   121.925 1.00 29.22 ? 260  PRO B CA    1 
ATOM   10849 C  C     . PRO B  1  262  ? -5.262  8.626   120.931 1.00 27.99 ? 260  PRO B C     1 
ATOM   10850 O  O     . PRO B  1  262  ? -4.702  7.542   121.107 1.00 30.54 ? 260  PRO B O     1 
ATOM   10851 C  CB    . PRO B  1  262  ? -5.569  10.156  122.898 1.00 27.05 ? 260  PRO B CB    1 
ATOM   10852 C  CG    . PRO B  1  262  ? -5.160  9.266   124.046 1.00 27.70 ? 260  PRO B CG    1 
ATOM   10853 C  CD    . PRO B  1  262  ? -6.277  8.264   124.184 1.00 27.09 ? 260  PRO B CD    1 
ATOM   10854 N  N     . GLY B  1  263  ? -5.036  9.402   119.877 1.00 24.40 ? 261  GLY B N     1 
ATOM   10855 C  CA    . GLY B  1  263  ? -4.030  9.066   118.892 1.00 24.17 ? 261  GLY B CA    1 
ATOM   10856 C  C     . GLY B  1  263  ? -3.187  10.268  118.534 1.00 23.52 ? 261  GLY B C     1 
ATOM   10857 O  O     . GLY B  1  263  ? -3.316  11.331  119.151 1.00 25.40 ? 261  GLY B O     1 
ATOM   10858 N  N     . ILE B  1  264  ? -2.338  10.114  117.526 1.00 23.46 ? 262  ILE B N     1 
ATOM   10859 C  CA    . ILE B  1  264  ? -1.472  11.180  117.046 1.00 23.65 ? 262  ILE B CA    1 
ATOM   10860 C  C     . ILE B  1  264  ? -1.607  11.270  115.534 1.00 26.26 ? 262  ILE B C     1 
ATOM   10861 O  O     . ILE B  1  264  ? -1.890  10.277  114.854 1.00 24.66 ? 262  ILE B O     1 
ATOM   10862 C  CB    . ILE B  1  264  ? -0.003  10.940  117.465 1.00 28.12 ? 262  ILE B CB    1 
ATOM   10863 C  CG1   . ILE B  1  264  ? 0.821   12.213  117.306 1.00 23.79 ? 262  ILE B CG1   1 
ATOM   10864 C  CG2   . ILE B  1  264  ? 0.623   9.816   116.657 1.00 23.63 ? 262  ILE B CG2   1 
ATOM   10865 C  CD1   . ILE B  1  264  ? 2.231   12.089  117.871 1.00 23.85 ? 262  ILE B CD1   1 
ATOM   10866 N  N     . SER B  1  265  ? -1.442  12.487  115.015 1.00 21.75 ? 263  SER B N     1 
ATOM   10867 C  CA    . SER B  1  265  ? -1.432  12.756  113.589 1.00 21.32 ? 263  SER B CA    1 
ATOM   10868 C  C     . SER B  1  265  ? -0.060  13.302  113.233 1.00 23.53 ? 263  SER B C     1 
ATOM   10869 O  O     . SER B  1  265  ? 0.533   14.066  114.004 1.00 27.20 ? 263  SER B O     1 
ATOM   10870 C  CB    . SER B  1  265  ? -2.523  13.757  113.192 1.00 27.97 ? 263  SER B CB    1 
ATOM   10871 O  OG    . SER B  1  265  ? -3.818  13.171  113.205 1.00 27.66 ? 263  SER B OG    1 
ATOM   10872 N  N     . ILE B  1  266  ? 0.464   12.876  112.092 1.00 20.78 ? 264  ILE B N     1 
ATOM   10873 C  CA    . ILE B  1  266  ? 1.760   13.334  111.624 1.00 20.35 ? 264  ILE B CA    1 
ATOM   10874 C  C     . ILE B  1  266  ? 1.645   13.788  110.178 1.00 21.75 ? 264  ILE B C     1 
ATOM   10875 O  O     . ILE B  1  266  ? 0.721   13.427  109.449 1.00 20.59 ? 264  ILE B O     1 
ATOM   10876 C  CB    . ILE B  1  266  ? 2.843   12.245  111.740 1.00 20.44 ? 264  ILE B CB    1 
ATOM   10877 C  CG1   . ILE B  1  266  ? 2.525   11.086  110.793 1.00 22.10 ? 264  ILE B CG1   1 
ATOM   10878 C  CG2   . ILE B  1  266  ? 2.953   11.751  113.171 1.00 22.74 ? 264  ILE B CG2   1 
ATOM   10879 C  CD1   . ILE B  1  266  ? 3.678   10.118  110.599 1.00 28.02 ? 264  ILE B CD1   1 
ATOM   10880 N  N     . LYS B  1  267  ? 2.625   14.576  109.762 1.00 20.73 ? 265  LYS B N     1 
ATOM   10881 C  CA    . LYS B  1  267  ? 2.754   15.000  108.380 1.00 18.25 ? 265  LYS B CA    1 
ATOM   10882 C  C     . LYS B  1  267  ? 4.086   14.485  107.861 1.00 18.54 ? 265  LYS B C     1 
ATOM   10883 O  O     . LYS B  1  267  ? 5.129   14.708  108.488 1.00 20.31 ? 265  LYS B O     1 
ATOM   10884 C  CB    . LYS B  1  267  ? 2.661   16.523  108.270 1.00 22.34 ? 265  LYS B CB    1 
ATOM   10885 C  CG    . LYS B  1  267  ? 1.252   17.038  108.557 1.00 23.82 ? 265  LYS B CG    1 
ATOM   10886 C  CD    . LYS B  1  267  ? 1.107   18.520  108.232 1.00 33.40 ? 265  LYS B CD    1 
ATOM   10887 C  CE    . LYS B  1  267  ? -0.329  18.994  108.434 1.00 37.38 ? 265  LYS B CE    1 
ATOM   10888 N  NZ    . LYS B  1  267  ? -0.863  18.614  109.771 1.00 36.21 ? 265  LYS B NZ    1 
ATOM   10889 N  N     . LEU B  1  268  ? 4.053   13.774  106.733 1.00 18.74 ? 266  LEU B N     1 
ATOM   10890 C  CA    . LEU B  1  268  ? 5.299   13.237  106.202 1.00 19.96 ? 266  LEU B CA    1 
ATOM   10891 C  C     . LEU B  1  268  ? 6.274   14.349  105.829 1.00 18.30 ? 266  LEU B C     1 
ATOM   10892 O  O     . LEU B  1  268  ? 7.489   14.174  105.971 1.00 18.71 ? 266  LEU B O     1 
ATOM   10893 C  CB    . LEU B  1  268  ? 5.014   12.317  105.012 1.00 18.39 ? 266  LEU B CB    1 
ATOM   10894 C  CG    . LEU B  1  268  ? 4.141   11.093  105.323 1.00 20.96 ? 266  LEU B CG    1 
ATOM   10895 C  CD1   . LEU B  1  268  ? 3.983   10.238  104.080 1.00 21.80 ? 266  LEU B CD1   1 
ATOM   10896 C  CD2   . LEU B  1  268  ? 4.741   10.277  106.455 1.00 23.55 ? 266  LEU B CD2   1 
ATOM   10897 N  N     . SER B  1  269  ? 5.774   15.518  105.409 1.00 17.89 ? 267  SER B N     1 
ATOM   10898 C  CA    . SER B  1  269  ? 6.678   16.617  105.091 1.00 18.27 ? 267  SER B CA    1 
ATOM   10899 C  C     . SER B  1  269  ? 7.458   17.103  106.306 1.00 17.97 ? 267  SER B C     1 
ATOM   10900 O  O     . SER B  1  269  ? 8.499   17.743  106.136 1.00 21.26 ? 267  SER B O     1 
ATOM   10901 C  CB    . SER B  1  269  ? 5.902   17.783  104.479 1.00 18.98 ? 267  SER B CB    1 
ATOM   10902 O  OG    . SER B  1  269  ? 5.087   18.401  105.475 1.00 21.17 ? 267  SER B OG    1 
ATOM   10903 N  N     . ALA B  1  270  ? 6.981   16.824  107.522 1.00 16.65 ? 268  ALA B N     1 
ATOM   10904 C  CA    . ALA B  1  270  ? 7.747   17.165  108.715 1.00 17.80 ? 268  ALA B CA    1 
ATOM   10905 C  C     . ALA B  1  270  ? 8.954   16.265  108.891 1.00 19.90 ? 268  ALA B C     1 
ATOM   10906 O  O     . ALA B  1  270  ? 9.889   16.627  109.612 1.00 19.33 ? 268  ALA B O     1 
ATOM   10907 C  CB    . ALA B  1  270  ? 6.876   17.057  109.976 1.00 19.65 ? 268  ALA B CB    1 
ATOM   10908 N  N     . LEU B  1  271  ? 8.948   15.091  108.274 1.00 19.17 ? 269  LEU B N     1 
ATOM   10909 C  CA    . LEU B  1  271  ? 9.915   14.060  108.615 1.00 20.55 ? 269  LEU B CA    1 
ATOM   10910 C  C     . LEU B  1  271  ? 11.070  13.979  107.634 1.00 18.25 ? 269  LEU B C     1 
ATOM   10911 O  O     . LEU B  1  271  ? 11.995  13.190  107.850 1.00 21.37 ? 269  LEU B O     1 
ATOM   10912 C  CB    . LEU B  1  271  ? 9.217   12.701  108.720 1.00 19.85 ? 269  LEU B CB    1 
ATOM   10913 C  CG    . LEU B  1  271  ? 8.250   12.636  109.905 1.00 22.03 ? 269  LEU B CG    1 
ATOM   10914 C  CD1   . LEU B  1  271  ? 7.482   11.323  109.931 1.00 24.94 ? 269  LEU B CD1   1 
ATOM   10915 C  CD2   . LEU B  1  271  ? 9.002   12.820  111.212 1.00 25.19 ? 269  LEU B CD2   1 
ATOM   10916 N  N     . HIS B  1  272  ? 11.060  14.804  106.587 1.00 17.82 ? 270  HIS B N     1 
ATOM   10917 C  CA    . HIS B  1  272  ? 12.175  14.806  105.663 1.00 20.48 ? 270  HIS B CA    1 
ATOM   10918 C  C     . HIS B  1  272  ? 12.174  16.126  104.915 1.00 18.29 ? 270  HIS B C     1 
ATOM   10919 O  O     . HIS B  1  272  ? 11.100  16.588  104.507 1.00 21.55 ? 270  HIS B O     1 
ATOM   10920 C  CB    . HIS B  1  272  ? 12.076  13.635  104.681 1.00 21.72 ? 270  HIS B CB    1 
ATOM   10921 C  CG    . HIS B  1  272  ? 13.370  13.314  104.017 1.00 21.60 ? 270  HIS B CG    1 
ATOM   10922 N  ND1   . HIS B  1  272  ? 13.881  14.068  102.984 1.00 22.64 ? 270  HIS B ND1   1 
ATOM   10923 C  CD2   . HIS B  1  272  ? 14.283  12.344  104.266 1.00 25.60 ? 270  HIS B CD2   1 
ATOM   10924 C  CE1   . HIS B  1  272  ? 15.048  13.572  102.616 1.00 24.97 ? 270  HIS B CE1   1 
ATOM   10925 N  NE2   . HIS B  1  272  ? 15.313  12.521  103.375 1.00 26.98 ? 270  HIS B NE2   1 
ATOM   10926 N  N     . PRO B  1  273  ? 13.333  16.749  104.698 1.00 18.61 ? 271  PRO B N     1 
ATOM   10927 C  CA    . PRO B  1  273  ? 13.347  18.023  103.966 1.00 18.74 ? 271  PRO B CA    1 
ATOM   10928 C  C     . PRO B  1  273  ? 13.111  17.881  102.474 1.00 18.18 ? 271  PRO B C     1 
ATOM   10929 O  O     . PRO B  1  273  ? 12.855  18.897  101.824 1.00 19.82 ? 271  PRO B O     1 
ATOM   10930 C  CB    . PRO B  1  273  ? 14.750  18.580  104.260 1.00 21.97 ? 271  PRO B CB    1 
ATOM   10931 C  CG    . PRO B  1  273  ? 15.578  17.374  104.501 1.00 22.75 ? 271  PRO B CG    1 
ATOM   10932 C  CD    . PRO B  1  273  ? 14.664  16.394  105.215 1.00 20.18 ? 271  PRO B CD    1 
ATOM   10933 N  N     . ARG B  1  274  ? 13.190  16.672  101.909 1.00 17.47 ? 272  ARG B N     1 
ATOM   10934 C  CA    . ARG B  1  274  ? 12.968  16.493  100.476 1.00 17.50 ? 272  ARG B CA    1 
ATOM   10935 C  C     . ARG B  1  274  ? 11.854  15.486  100.243 1.00 20.83 ? 272  ARG B C     1 
ATOM   10936 O  O     . ARG B  1  274  ? 12.035  14.488  99.532  1.00 20.89 ? 272  ARG B O     1 
ATOM   10937 C  CB    . ARG B  1  274  ? 14.252  16.042  99.772  1.00 19.09 ? 272  ARG B CB    1 
ATOM   10938 C  CG    . ARG B  1  274  ? 15.389  17.065  99.833  1.00 20.10 ? 272  ARG B CG    1 
ATOM   10939 C  CD    . ARG B  1  274  ? 14.976  18.414  99.238  1.00 19.98 ? 272  ARG B CD    1 
ATOM   10940 N  NE    . ARG B  1  274  ? 14.485  18.297  97.868  1.00 21.77 ? 272  ARG B NE    1 
ATOM   10941 C  CZ    . ARG B  1  274  ? 15.269  18.201  96.799  1.00 20.68 ? 272  ARG B CZ    1 
ATOM   10942 N  NH1   . ARG B  1  274  ? 16.589  18.132  96.915  1.00 21.51 ? 272  ARG B NH1   1 
ATOM   10943 N  NH2   . ARG B  1  274  ? 14.719  18.206  95.589  1.00 20.37 ? 272  ARG B NH2   1 
ATOM   10944 N  N     . TYR B  1  275  ? 10.697  15.731  100.844 1.00 19.24 ? 273  TYR B N     1 
ATOM   10945 C  CA    . TYR B  1  275  ? 9.562   14.829  100.692 1.00 20.47 ? 273  TYR B CA    1 
ATOM   10946 C  C     . TYR B  1  275  ? 8.873   15.148  99.369  1.00 18.66 ? 273  TYR B C     1 
ATOM   10947 O  O     . TYR B  1  275  ? 8.009   16.021  99.287  1.00 19.38 ? 273  TYR B O     1 
ATOM   10948 C  CB    . TYR B  1  275  ? 8.618   14.957  101.884 1.00 18.12 ? 273  TYR B CB    1 
ATOM   10949 C  CG    . TYR B  1  275  ? 7.362   14.145  101.726 1.00 18.52 ? 273  TYR B CG    1 
ATOM   10950 C  CD1   . TYR B  1  275  ? 7.418   12.817  101.326 1.00 20.29 ? 273  TYR B CD1   1 
ATOM   10951 C  CD2   . TYR B  1  275  ? 6.120   14.707  101.958 1.00 19.75 ? 273  TYR B CD2   1 
ATOM   10952 C  CE1   . TYR B  1  275  ? 6.267   12.078  101.166 1.00 22.01 ? 273  TYR B CE1   1 
ATOM   10953 C  CE2   . TYR B  1  275  ? 4.961   13.969  101.813 1.00 19.13 ? 273  TYR B CE2   1 
ATOM   10954 C  CZ    . TYR B  1  275  ? 5.044   12.661  101.409 1.00 20.24 ? 273  TYR B CZ    1 
ATOM   10955 O  OH    . TYR B  1  275  ? 3.895   11.932  101.246 1.00 21.14 ? 273  TYR B OH    1 
ATOM   10956 N  N     . SER B  1  276  ? 9.265   14.440  98.307  1.00 17.83 ? 274  SER B N     1 
ATOM   10957 C  CA    . SER B  1  276  ? 8.696   14.682  96.980  1.00 18.06 ? 274  SER B CA    1 
ATOM   10958 C  C     . SER B  1  276  ? 8.960   13.486  96.079  1.00 17.93 ? 274  SER B C     1 
ATOM   10959 O  O     . SER B  1  276  ? 9.869   12.685  96.320  1.00 19.88 ? 274  SER B O     1 
ATOM   10960 C  CB    . SER B  1  276  ? 9.275   15.935  96.326  1.00 23.77 ? 274  SER B CB    1 
ATOM   10961 O  OG    . SER B  1  276  ? 10.629  15.716  95.996  1.00 25.95 ? 274  SER B OG    1 
ATOM   10962 N  N     . ARG B  1  277  ? 8.131   13.372  95.039  1.00 16.97 ? 275  ARG B N     1 
ATOM   10963 C  CA    . ARG B  1  277  ? 8.311   12.289  94.084  1.00 18.06 ? 275  ARG B CA    1 
ATOM   10964 C  C     . ARG B  1  277  ? 9.688   12.335  93.444  1.00 18.74 ? 275  ARG B C     1 
ATOM   10965 O  O     . ARG B  1  277  ? 10.272  11.279  93.170  1.00 20.03 ? 275  ARG B O     1 
ATOM   10966 C  CB    . ARG B  1  277  ? 7.216   12.336  93.015  1.00 17.95 ? 275  ARG B CB    1 
ATOM   10967 C  CG    . ARG B  1  277  ? 7.401   11.362  91.852  1.00 20.29 ? 275  ARG B CG    1 
ATOM   10968 C  CD    . ARG B  1  277  ? 7.436   9.922   92.351  1.00 19.67 ? 275  ARG B CD    1 
ATOM   10969 N  NE    . ARG B  1  277  ? 7.619   8.988   91.244  1.00 20.16 ? 275  ARG B NE    1 
ATOM   10970 C  CZ    . ARG B  1  277  ? 8.792   8.638   90.737  1.00 20.91 ? 275  ARG B CZ    1 
ATOM   10971 N  NH1   . ARG B  1  277  ? 9.927   9.163   91.181  1.00 21.79 ? 275  ARG B NH1   1 
ATOM   10972 N  NH2   . ARG B  1  277  ? 8.829   7.727   89.765  1.00 21.18 ? 275  ARG B NH2   1 
ATOM   10973 N  N     . ALA B  1  278  ? 10.226  13.535  93.203  1.00 20.96 ? 276  ALA B N     1 
ATOM   10974 C  CA    . ALA B  1  278  ? 11.538  13.624  92.578  1.00 19.42 ? 276  ALA B CA    1 
ATOM   10975 C  C     . ALA B  1  278  ? 12.616  13.004  93.445  1.00 19.65 ? 276  ALA B C     1 
ATOM   10976 O  O     . ALA B  1  278  ? 13.636  12.554  92.914  1.00 22.26 ? 276  ALA B O     1 
ATOM   10977 C  CB    . ALA B  1  278  ? 11.896  15.079  92.267  1.00 19.40 ? 276  ALA B CB    1 
ATOM   10978 N  N     . GLN B  1  279  ? 12.405  12.945  94.754  1.00 19.52 ? 277  GLN B N     1 
ATOM   10979 C  CA    . GLN B  1  279  ? 13.357  12.338  95.677  1.00 17.80 ? 277  GLN B CA    1 
ATOM   10980 C  C     . GLN B  1  279  ? 12.790  11.060  96.282  1.00 21.94 ? 277  GLN B C     1 
ATOM   10981 O  O     . GLN B  1  279  ? 13.036  10.756  97.449  1.00 21.90 ? 277  GLN B O     1 
ATOM   10982 C  CB    . GLN B  1  279  ? 13.743  13.324  96.778  1.00 20.72 ? 277  GLN B CB    1 
ATOM   10983 C  CG    . GLN B  1  279  ? 14.381  14.602  96.249  1.00 20.67 ? 277  GLN B CG    1 
ATOM   10984 C  CD    . GLN B  1  279  ? 15.663  14.322  95.495  1.00 26.06 ? 277  GLN B CD    1 
ATOM   10985 O  OE1   . GLN B  1  279  ? 16.375  13.359  95.789  1.00 29.49 ? 277  GLN B OE1   1 
ATOM   10986 N  NE2   . GLN B  1  279  ? 15.955  15.151  94.503  1.00 19.34 ? 277  GLN B NE2   1 
ATOM   10987 N  N     . ALA B  1  280  ? 12.036  10.292  95.484  1.00 19.73 ? 278  ALA B N     1 
ATOM   10988 C  CA    . ALA B  1  280  ? 11.358  9.112   96.013  1.00 19.53 ? 278  ALA B CA    1 
ATOM   10989 C  C     . ALA B  1  280  ? 12.335  8.146   96.673  1.00 21.29 ? 278  ALA B C     1 
ATOM   10990 O  O     . ALA B  1  280  ? 12.004  7.529   97.690  1.00 21.07 ? 278  ALA B O     1 
ATOM   10991 C  CB    . ALA B  1  280  ? 10.582  8.404   94.899  1.00 21.88 ? 278  ALA B CB    1 
ATOM   10992 N  N     . ALA B  1  281  ? 13.538  7.996   96.114  1.00 20.44 ? 279  ALA B N     1 
ATOM   10993 C  CA    . ALA B  1  281  ? 14.480  7.039   96.693  1.00 23.98 ? 279  ALA B CA    1 
ATOM   10994 C  C     . ALA B  1  281  ? 14.897  7.457   98.096  1.00 23.35 ? 279  ALA B C     1 
ATOM   10995 O  O     . ALA B  1  281  ? 14.968  6.620   99.003  1.00 23.75 ? 279  ALA B O     1 
ATOM   10996 C  CB    . ALA B  1  281  ? 15.700  6.881   95.785  1.00 26.34 ? 279  ALA B CB    1 
ATOM   10997 N  N     . ARG B  1  282  ? 15.157  8.750   98.299  1.00 22.36 ? 280  ARG B N     1 
ATOM   10998 C  CA    . ARG B  1  282  ? 15.486  9.230   99.635  1.00 21.02 ? 280  ARG B CA    1 
ATOM   10999 C  C     . ARG B  1  282  ? 14.282  9.128   100.557 1.00 21.35 ? 280  ARG B C     1 
ATOM   11000 O  O     . ARG B  1  282  ? 14.429  8.848   101.748 1.00 23.18 ? 280  ARG B O     1 
ATOM   11001 C  CB    . ARG B  1  282  ? 15.981  10.678  99.577  1.00 25.61 ? 280  ARG B CB    1 
ATOM   11002 C  CG    . ARG B  1  282  ? 17.307  10.872  98.858  1.00 25.63 ? 280  ARG B CG    1 
ATOM   11003 C  CD    . ARG B  1  282  ? 17.846  12.266  99.114  1.00 24.53 ? 280  ARG B CD    1 
ATOM   11004 N  NE    . ARG B  1  282  ? 18.165  12.452  100.524 1.00 22.61 ? 280  ARG B NE    1 
ATOM   11005 C  CZ    . ARG B  1  282  ? 18.301  13.633  101.110 1.00 25.28 ? 280  ARG B CZ    1 
ATOM   11006 N  NH1   . ARG B  1  282  ? 18.145  14.762  100.432 1.00 21.53 ? 280  ARG B NH1   1 
ATOM   11007 N  NH2   . ARG B  1  282  ? 18.584  13.683  102.411 1.00 25.13 ? 280  ARG B NH2   1 
ATOM   11008 N  N     . VAL B  1  283  ? 13.083  9.365   100.027 1.00 20.87 ? 281  VAL B N     1 
ATOM   11009 C  CA    . VAL B  1  283  ? 11.881  9.250   100.847 1.00 19.31 ? 281  VAL B CA    1 
ATOM   11010 C  C     . VAL B  1  283  ? 11.735  7.828   101.373 1.00 20.64 ? 281  VAL B C     1 
ATOM   11011 O  O     . VAL B  1  283  ? 11.545  7.604   102.575 1.00 23.96 ? 281  VAL B O     1 
ATOM   11012 C  CB    . VAL B  1  283  ? 10.643  9.690   100.046 1.00 19.49 ? 281  VAL B CB    1 
ATOM   11013 C  CG1   . VAL B  1  283  ? 9.380   9.248   100.746 1.00 21.41 ? 281  VAL B CG1   1 
ATOM   11014 C  CG2   . VAL B  1  283  ? 10.660  11.217  99.887  1.00 20.75 ? 281  VAL B CG2   1 
ATOM   11015 N  N     . MET B  1  284  ? 11.837  6.839   100.479 1.00 20.44 ? 282  MET B N     1 
ATOM   11016 C  CA    . MET B  1  284  ? 11.700  5.459   100.923 1.00 21.98 ? 282  MET B CA    1 
ATOM   11017 C  C     . MET B  1  284  ? 12.870  5.021   101.794 1.00 24.84 ? 282  MET B C     1 
ATOM   11018 O  O     . MET B  1  284  ? 12.695  4.194   102.696 1.00 25.54 ? 282  MET B O     1 
ATOM   11019 C  CB    . MET B  1  284  ? 11.576  4.531   99.723  1.00 20.51 ? 282  MET B CB    1 
ATOM   11020 C  CG    . MET B  1  284  ? 10.389  4.851   98.821  1.00 24.11 ? 282  MET B CG    1 
ATOM   11021 S  SD    . MET B  1  284  ? 8.816   4.733   99.701  1.00 26.34 ? 282  MET B SD    1 
ATOM   11022 C  CE    . MET B  1  284  ? 8.672   2.962   99.936  1.00 29.85 ? 282  MET B CE    1 
ATOM   11023 N  N     . GLY B  1  285  ? 14.064  5.554   101.539 1.00 23.46 ? 283  GLY B N     1 
ATOM   11024 C  CA    . GLY B  1  285  ? 15.233  5.122   102.287 1.00 24.76 ? 283  GLY B CA    1 
ATOM   11025 C  C     . GLY B  1  285  ? 15.397  5.796   103.631 1.00 26.05 ? 283  GLY B C     1 
ATOM   11026 O  O     . GLY B  1  285  ? 15.949  5.197   104.561 1.00 26.88 ? 283  GLY B O     1 
ATOM   11027 N  N     . GLU B  1  286  ? 14.916  7.029   103.765 1.00 22.78 ? 284  GLU B N     1 
ATOM   11028 C  CA    . GLU B  1  286  ? 15.198  7.864   104.924 1.00 19.51 ? 284  GLU B CA    1 
ATOM   11029 C  C     . GLU B  1  286  ? 13.956  8.284   105.685 1.00 23.85 ? 284  GLU B C     1 
ATOM   11030 O  O     . GLU B  1  286  ? 13.971  8.288   106.921 1.00 27.28 ? 284  GLU B O     1 
ATOM   11031 C  CB    . GLU B  1  286  ? 15.959  9.124   104.487 1.00 22.32 ? 284  GLU B CB    1 
ATOM   11032 C  CG    . GLU B  1  286  ? 17.258  8.825   103.757 1.00 24.10 ? 284  GLU B CG    1 
ATOM   11033 C  CD    . GLU B  1  286  ? 17.878  10.055  103.111 1.00 29.01 ? 284  GLU B CD    1 
ATOM   11034 O  OE1   . GLU B  1  286  ? 17.639  11.181  103.602 1.00 29.63 ? 284  GLU B OE1   1 
ATOM   11035 O  OE2   . GLU B  1  286  ? 18.610  9.887   102.116 1.00 32.49 ? 284  GLU B OE2   1 
ATOM   11036 N  N     . LEU B  1  287  ? 12.891  8.659   104.977 1.00 23.29 ? 285  LEU B N     1 
ATOM   11037 C  CA    . LEU B  1  287  ? 11.652  9.062   105.624 1.00 22.76 ? 285  LEU B CA    1 
ATOM   11038 C  C     . LEU B  1  287  ? 10.885  7.853   106.129 1.00 22.84 ? 285  LEU B C     1 
ATOM   11039 O  O     . LEU B  1  287  ? 10.482  7.813   107.293 1.00 22.38 ? 285  LEU B O     1 
ATOM   11040 C  CB    . LEU B  1  287  ? 10.793  9.872   104.648 1.00 23.25 ? 285  LEU B CB    1 
ATOM   11041 C  CG    . LEU B  1  287  ? 9.747   10.846  105.204 1.00 25.34 ? 285  LEU B CG    1 
ATOM   11042 C  CD1   . LEU B  1  287  ? 9.189   11.684  104.074 1.00 22.80 ? 285  LEU B CD1   1 
ATOM   11043 C  CD2   . LEU B  1  287  ? 8.607   10.147  105.934 1.00 24.33 ? 285  LEU B CD2   1 
ATOM   11044 N  N     . LEU B  1  288  ? 10.668  6.864   105.263 1.00 23.49 ? 286  LEU B N     1 
ATOM   11045 C  CA    . LEU B  1  288  ? 9.902   5.683   105.660 1.00 22.76 ? 286  LEU B CA    1 
ATOM   11046 C  C     . LEU B  1  288  ? 10.401  5.036   106.949 1.00 22.54 ? 286  LEU B C     1 
ATOM   11047 O  O     . LEU B  1  288  ? 9.566   4.746   107.821 1.00 22.97 ? 286  LEU B O     1 
ATOM   11048 C  CB    . LEU B  1  288  ? 9.882   4.690   104.489 1.00 25.03 ? 286  LEU B CB    1 
ATOM   11049 C  CG    . LEU B  1  288  ? 9.292   3.322   104.825 1.00 28.43 ? 286  LEU B CG    1 
ATOM   11050 C  CD1   . LEU B  1  288  ? 7.849   3.448   105.314 1.00 27.01 ? 286  LEU B CD1   1 
ATOM   11051 C  CD2   . LEU B  1  288  ? 9.384   2.396   103.625 1.00 32.59 ? 286  LEU B CD2   1 
ATOM   11052 N  N     . PRO B  1  289  ? 11.706  4.814   107.163 1.00 24.46 ? 287  PRO B N     1 
ATOM   11053 C  CA    . PRO B  1  289  ? 12.123  4.212   108.444 1.00 23.70 ? 287  PRO B CA    1 
ATOM   11054 C  C     . PRO B  1  289  ? 11.748  5.049   109.655 1.00 23.36 ? 287  PRO B C     1 
ATOM   11055 O  O     . PRO B  1  289  ? 11.529  4.493   110.739 1.00 26.90 ? 287  PRO B O     1 
ATOM   11056 C  CB    . PRO B  1  289  ? 13.644  4.088   108.294 1.00 30.50 ? 287  PRO B CB    1 
ATOM   11057 C  CG    . PRO B  1  289  ? 13.860  3.987   106.825 1.00 33.08 ? 287  PRO B CG    1 
ATOM   11058 C  CD    . PRO B  1  289  ? 12.829  4.876   106.207 1.00 29.18 ? 287  PRO B CD    1 
ATOM   11059 N  N     . ARG B  1  290  ? 11.678  6.371   109.518 1.00 23.30 ? 288  ARG B N     1 
ATOM   11060 C  CA    . ARG B  1  290  ? 11.228  7.184   110.640 1.00 24.06 ? 288  ARG B CA    1 
ATOM   11061 C  C     . ARG B  1  290  ? 9.751   6.963   110.921 1.00 22.92 ? 288  ARG B C     1 
ATOM   11062 O  O     . ARG B  1  290  ? 9.350   6.828   112.084 1.00 23.16 ? 288  ARG B O     1 
ATOM   11063 C  CB    . ARG B  1  290  ? 11.513  8.652   110.364 1.00 23.08 ? 288  ARG B CB    1 
ATOM   11064 C  CG    . ARG B  1  290  ? 12.985  8.955   110.458 1.00 27.60 ? 288  ARG B CG    1 
ATOM   11065 C  CD    . ARG B  1  290  ? 13.307  10.241  109.763 1.00 33.27 ? 288  ARG B CD    1 
ATOM   11066 N  NE    . ARG B  1  290  ? 14.498  10.848  110.335 1.00 37.36 ? 288  ARG B NE    1 
ATOM   11067 C  CZ    . ARG B  1  290  ? 15.106  11.911  109.830 1.00 41.45 ? 288  ARG B CZ    1 
ATOM   11068 N  NH1   . ARG B  1  290  ? 14.666  12.500  108.728 1.00 38.88 ? 288  ARG B NH1   1 
ATOM   11069 N  NH2   . ARG B  1  290  ? 16.178  12.397  110.446 1.00 34.95 ? 288  ARG B NH2   1 
ATOM   11070 N  N     . VAL B  1  291  ? 8.928   6.888   109.871 1.00 23.45 ? 289  VAL B N     1 
ATOM   11071 C  CA    . VAL B  1  291  ? 7.512   6.633   110.093 1.00 21.01 ? 289  VAL B CA    1 
ATOM   11072 C  C     . VAL B  1  291  ? 7.323   5.263   110.708 1.00 22.21 ? 289  VAL B C     1 
ATOM   11073 O  O     . VAL B  1  291  ? 6.501   5.082   111.616 1.00 23.81 ? 289  VAL B O     1 
ATOM   11074 C  CB    . VAL B  1  291  ? 6.714   6.757   108.785 1.00 22.96 ? 289  VAL B CB    1 
ATOM   11075 C  CG1   . VAL B  1  291  ? 5.236   6.571   109.074 1.00 25.50 ? 289  VAL B CG1   1 
ATOM   11076 C  CG2   . VAL B  1  291  ? 6.983   8.089   108.133 1.00 22.76 ? 289  VAL B CG2   1 
ATOM   11077 N  N     . LYS B  1  292  ? 8.074   4.268   110.226 1.00 22.04 ? 290  LYS B N     1 
ATOM   11078 C  CA    . LYS B  1  292  ? 7.921   2.934   110.796 1.00 21.66 ? 290  LYS B CA    1 
ATOM   11079 C  C     . LYS B  1  292  ? 8.267   2.947   112.272 1.00 24.39 ? 290  LYS B C     1 
ATOM   11080 O  O     . LYS B  1  292  ? 7.579   2.319   113.085 1.00 25.08 ? 290  LYS B O     1 
ATOM   11081 C  CB    . LYS B  1  292  ? 8.785   1.920   110.049 1.00 24.82 ? 290  LYS B CB    1 
ATOM   11082 C  CG    . LYS B  1  292  ? 8.583   0.478   110.549 1.00 28.69 ? 290  LYS B CG    1 
ATOM   11083 C  CD    . LYS B  1  292  ? 9.645   0.052   111.532 1.00 34.57 ? 290  LYS B CD    1 
ATOM   11084 C  CE    . LYS B  1  292  ? 9.423   -1.404  111.960 1.00 34.99 ? 290  LYS B CE    1 
ATOM   11085 N  NZ    . LYS B  1  292  ? 9.640   -2.369  110.848 1.00 35.72 ? 290  LYS B NZ    1 
ATOM   11086 N  N     . ALA B  1  293  ? 9.318   3.683   112.641 1.00 23.92 ? 291  ALA B N     1 
ATOM   11087 C  CA    . ALA B  1  293  ? 9.699   3.745   114.046 1.00 28.05 ? 291  ALA B CA    1 
ATOM   11088 C  C     . ALA B  1  293  ? 8.575   4.328   114.893 1.00 24.85 ? 291  ALA B C     1 
ATOM   11089 O  O     . ALA B  1  293  ? 8.288   3.831   115.994 1.00 25.41 ? 291  ALA B O     1 
ATOM   11090 C  CB    . ALA B  1  293  ? 10.977  4.570   114.204 1.00 26.70 ? 291  ALA B CB    1 
ATOM   11091 N  N     . LEU B  1  294  ? 7.940   5.394   114.403 1.00 22.92 ? 292  LEU B N     1 
ATOM   11092 C  CA    . LEU B  1  294  ? 6.841   6.013   115.136 1.00 24.57 ? 292  LEU B CA    1 
ATOM   11093 C  C     . LEU B  1  294  ? 5.638   5.087   115.189 1.00 24.05 ? 292  LEU B C     1 
ATOM   11094 O  O     . LEU B  1  294  ? 4.975   4.975   116.222 1.00 25.68 ? 292  LEU B O     1 
ATOM   11095 C  CB    . LEU B  1  294  ? 6.458   7.345   114.489 1.00 21.71 ? 292  LEU B CB    1 
ATOM   11096 C  CG    . LEU B  1  294  ? 7.562   8.398   114.454 1.00 21.81 ? 292  LEU B CG    1 
ATOM   11097 C  CD1   . LEU B  1  294  ? 7.105   9.583   113.636 1.00 21.04 ? 292  LEU B CD1   1 
ATOM   11098 C  CD2   . LEU B  1  294  ? 7.936   8.830   115.872 1.00 23.11 ? 292  LEU B CD2   1 
ATOM   11099 N  N     . ALA B  1  295  ? 5.337   4.422   114.075 1.00 25.45 ? 293  ALA B N     1 
ATOM   11100 C  CA    . ALA B  1  295  ? 4.206   3.506   114.055 1.00 23.50 ? 293  ALA B CA    1 
ATOM   11101 C  C     . ALA B  1  295  ? 4.421   2.340   115.011 1.00 27.34 ? 293  ALA B C     1 
ATOM   11102 O  O     . ALA B  1  295  ? 3.476   1.876   115.656 1.00 27.71 ? 293  ALA B O     1 
ATOM   11103 C  CB    . ALA B  1  295  ? 3.974   3.020   112.621 1.00 23.43 ? 293  ALA B CB    1 
ATOM   11104 N  N     . LEU B  1  296  ? 5.662   1.859   115.121 1.00 24.62 ? 294  LEU B N     1 
ATOM   11105 C  CA    . LEU B  1  296  ? 5.969   0.796   116.071 1.00 25.87 ? 294  LEU B CA    1 
ATOM   11106 C  C     . LEU B  1  296  ? 5.698   1.243   117.501 1.00 31.41 ? 294  LEU B C     1 
ATOM   11107 O  O     . LEU B  1  296  ? 5.114   0.497   118.292 1.00 30.59 ? 294  LEU B O     1 
ATOM   11108 C  CB    . LEU B  1  296  ? 7.422   0.361   115.904 1.00 30.20 ? 294  LEU B CB    1 
ATOM   11109 C  CG    . LEU B  1  296  ? 7.900   -0.823  116.735 1.00 34.60 ? 294  LEU B CG    1 
ATOM   11110 C  CD1   . LEU B  1  296  ? 6.981   -2.003  116.494 1.00 37.74 ? 294  LEU B CD1   1 
ATOM   11111 C  CD2   . LEU B  1  296  ? 9.336   -1.167  116.367 1.00 43.10 ? 294  LEU B CD2   1 
ATOM   11112 N  N     . LEU B  1  297  ? 6.105   2.465   117.849 1.00 26.48 ? 295  LEU B N     1 
ATOM   11113 C  CA    . LEU B  1  297  ? 5.774   2.994   119.171 1.00 26.12 ? 295  LEU B CA    1 
ATOM   11114 C  C     . LEU B  1  297  ? 4.266   3.115   119.361 1.00 27.87 ? 295  LEU B C     1 
ATOM   11115 O  O     . LEU B  1  297  ? 3.734   2.751   120.420 1.00 26.46 ? 295  LEU B O     1 
ATOM   11116 C  CB    . LEU B  1  297  ? 6.443   4.353   119.374 1.00 23.91 ? 295  LEU B CB    1 
ATOM   11117 C  CG    . LEU B  1  297  ? 7.960   4.346   119.551 1.00 33.47 ? 295  LEU B CG    1 
ATOM   11118 C  CD1   . LEU B  1  297  ? 8.484   5.767   119.404 1.00 32.12 ? 295  LEU B CD1   1 
ATOM   11119 C  CD2   . LEU B  1  297  ? 8.351   3.774   120.906 1.00 32.80 ? 295  LEU B CD2   1 
ATOM   11120 N  N     . ALA B  1  298  ? 3.561   3.637   118.353 1.00 26.01 ? 296  ALA B N     1 
ATOM   11121 C  CA    . ALA B  1  298  ? 2.106   3.715   118.437 1.00 24.68 ? 296  ALA B CA    1 
ATOM   11122 C  C     . ALA B  1  298  ? 1.499   2.335   118.620 1.00 31.16 ? 296  ALA B C     1 
ATOM   11123 O  O     . ALA B  1  298  ? 0.566   2.157   119.412 1.00 29.87 ? 296  ALA B O     1 
ATOM   11124 C  CB    . ALA B  1  298  ? 1.529   4.375   117.183 1.00 23.40 ? 296  ALA B CB    1 
ATOM   11125 N  N     . LYS B  1  299  ? 2.023   1.342   117.899 1.00 26.43 ? 297  LYS B N     1 
ATOM   11126 C  CA    . LYS B  1  299  ? 1.540   -0.026  118.072 1.00 30.64 ? 297  LYS B CA    1 
ATOM   11127 C  C     . LYS B  1  299  ? 1.758   -0.510  119.498 1.00 37.00 ? 297  LYS B C     1 
ATOM   11128 O  O     . LYS B  1  299  ? 0.866   -1.125  120.102 1.00 34.63 ? 297  LYS B O     1 
ATOM   11129 C  CB    . LYS B  1  299  ? 2.237   -0.966  117.092 1.00 32.33 ? 297  LYS B CB    1 
ATOM   11130 C  CG    . LYS B  1  299  ? 1.897   -2.436  117.353 1.00 37.62 ? 297  LYS B CG    1 
ATOM   11131 C  CD    . LYS B  1  299  ? 2.921   -3.381  116.753 1.00 43.62 ? 297  LYS B CD    1 
ATOM   11132 C  CE    . LYS B  1  299  ? 2.458   -4.831  116.872 1.00 41.86 ? 297  LYS B CE    1 
ATOM   11133 N  NZ    . LYS B  1  299  ? 2.173   -5.206  118.275 1.00 48.63 ? 297  LYS B NZ    1 
ATOM   11134 N  N     . ASN B  1  300  ? 2.951   -0.266  120.047 1.00 30.71 ? 298  ASN B N     1 
ATOM   11135 C  CA    . ASN B  1  300  ? 3.246   -0.772  121.384 1.00 31.26 ? 298  ASN B CA    1 
ATOM   11136 C  C     . ASN B  1  300  ? 2.284   -0.208  122.419 1.00 29.33 ? 298  ASN B C     1 
ATOM   11137 O  O     . ASN B  1  300  ? 1.937   -0.900  123.381 1.00 32.09 ? 298  ASN B O     1 
ATOM   11138 C  CB    . ASN B  1  300  ? 4.691   -0.455  121.767 1.00 33.37 ? 298  ASN B CB    1 
ATOM   11139 C  CG    . ASN B  1  300  ? 5.698   -1.236  120.935 1.00 41.05 ? 298  ASN B CG    1 
ATOM   11140 O  OD1   . ASN B  1  300  ? 5.366   -2.260  120.340 1.00 43.16 ? 298  ASN B OD1   1 
ATOM   11141 N  ND2   . ASN B  1  300  ? 6.935   -0.752  120.889 1.00 49.73 ? 298  ASN B ND2   1 
ATOM   11142 N  N     . TYR B  1  301  ? 1.820   1.023   122.225 1.00 26.37 ? 299  TYR B N     1 
ATOM   11143 C  CA    . TYR B  1  301  ? 0.852   1.638   123.123 1.00 30.92 ? 299  TYR B CA    1 
ATOM   11144 C  C     . TYR B  1  301  ? -0.586  1.402   122.687 1.00 27.97 ? 299  TYR B C     1 
ATOM   11145 O  O     . TYR B  1  301  ? -1.505  1.801   123.408 1.00 29.69 ? 299  TYR B O     1 
ATOM   11146 C  CB    . TYR B  1  301  ? 1.098   3.145   123.218 1.00 28.20 ? 299  TYR B CB    1 
ATOM   11147 C  CG    . TYR B  1  301  ? 2.338   3.545   123.993 1.00 26.39 ? 299  TYR B CG    1 
ATOM   11148 C  CD1   . TYR B  1  301  ? 2.416   3.348   125.366 1.00 30.36 ? 299  TYR B CD1   1 
ATOM   11149 C  CD2   . TYR B  1  301  ? 3.415   4.142   123.350 1.00 26.12 ? 299  TYR B CD2   1 
ATOM   11150 C  CE1   . TYR B  1  301  ? 3.549   3.728   126.075 1.00 28.58 ? 299  TYR B CE1   1 
ATOM   11151 C  CE2   . TYR B  1  301  ? 4.545   4.527   124.046 1.00 28.62 ? 299  TYR B CE2   1 
ATOM   11152 C  CZ    . TYR B  1  301  ? 4.605   4.312   125.400 1.00 31.00 ? 299  TYR B CZ    1 
ATOM   11153 O  OH    . TYR B  1  301  ? 5.724   4.692   126.083 1.00 29.17 ? 299  TYR B OH    1 
ATOM   11154 N  N     . ASP B  1  302  ? -0.786  0.787   121.521 1.00 27.05 ? 300  ASP B N     1 
ATOM   11155 C  CA    . ASP B  1  302  ? -2.088  0.609   120.878 1.00 29.93 ? 300  ASP B CA    1 
ATOM   11156 C  C     . ASP B  1  302  ? -2.861  1.927   120.801 1.00 27.47 ? 300  ASP B C     1 
ATOM   11157 O  O     . ASP B  1  302  ? -3.980  2.061   121.297 1.00 30.12 ? 300  ASP B O     1 
ATOM   11158 C  CB    . ASP B  1  302  ? -2.915  -0.473  121.580 1.00 31.28 ? 300  ASP B CB    1 
ATOM   11159 C  CG    . ASP B  1  302  ? -3.989  -1.052  120.671 1.00 31.65 ? 300  ASP B CG    1 
ATOM   11160 O  OD1   . ASP B  1  302  ? -3.781  -1.058  119.439 1.00 35.25 ? 300  ASP B OD1   1 
ATOM   11161 O  OD2   . ASP B  1  302  ? -5.043  -1.479  121.192 1.00 36.65 ? 300  ASP B OD2   1 
ATOM   11162 N  N     . ILE B  1  303  ? -2.223  2.917   120.180 1.00 25.57 ? 301  ILE B N     1 
ATOM   11163 C  CA    . ILE B  1  303  ? -2.879  4.166   119.824 1.00 25.74 ? 301  ILE B CA    1 
ATOM   11164 C  C     . ILE B  1  303  ? -2.893  4.290   118.306 1.00 27.72 ? 301  ILE B C     1 
ATOM   11165 O  O     . ILE B  1  303  ? -2.145  3.621   117.585 1.00 26.41 ? 301  ILE B O     1 
ATOM   11166 C  CB    . ILE B  1  303  ? -2.209  5.409   120.458 1.00 25.29 ? 301  ILE B CB    1 
ATOM   11167 C  CG1   . ILE B  1  303  ? -0.850  5.696   119.799 1.00 28.00 ? 301  ILE B CG1   1 
ATOM   11168 C  CG2   . ILE B  1  303  ? -2.062  5.235   121.956 1.00 25.56 ? 301  ILE B CG2   1 
ATOM   11169 C  CD1   . ILE B  1  303  ? -0.250  7.034   120.204 1.00 27.40 ? 301  ILE B CD1   1 
ATOM   11170 N  N     . GLY B  1  304  ? -3.747  5.186   117.823 1.00 24.70 ? 302  GLY B N     1 
ATOM   11171 C  CA    . GLY B  1  304  ? -3.789  5.472   116.402 1.00 24.61 ? 302  GLY B CA    1 
ATOM   11172 C  C     . GLY B  1  304  ? -2.668  6.416   115.994 1.00 25.44 ? 302  GLY B C     1 
ATOM   11173 O  O     . GLY B  1  304  ? -2.279  7.319   116.735 1.00 27.60 ? 302  GLY B O     1 
ATOM   11174 N  N     . LEU B  1  305  ? -2.133  6.185   114.803 1.00 22.64 ? 303  LEU B N     1 
ATOM   11175 C  CA    . LEU B  1  305  ? -1.149  7.084   114.209 1.00 24.89 ? 303  LEU B CA    1 
ATOM   11176 C  C     . LEU B  1  305  ? -1.637  7.389   112.806 1.00 26.02 ? 303  LEU B C     1 
ATOM   11177 O  O     . LEU B  1  305  ? -1.679  6.492   111.961 1.00 24.44 ? 303  LEU B O     1 
ATOM   11178 C  CB    . LEU B  1  305  ? 0.243   6.458   114.194 1.00 27.32 ? 303  LEU B CB    1 
ATOM   11179 C  CG    . LEU B  1  305  ? 1.347   7.349   113.618 1.00 25.14 ? 303  LEU B CG    1 
ATOM   11180 C  CD1   . LEU B  1  305  ? 2.594   7.262   114.461 1.00 30.58 ? 303  LEU B CD1   1 
ATOM   11181 C  CD2   . LEU B  1  305  ? 1.637   6.960   112.181 1.00 28.45 ? 303  LEU B CD2   1 
ATOM   11182 N  N     . ASN B  1  306  ? -2.006  8.646   112.567 1.00 22.11 ? 304  ASN B N     1 
ATOM   11183 C  CA    . ASN B  1  306  ? -2.635  9.066   111.328 1.00 24.15 ? 304  ASN B CA    1 
ATOM   11184 C  C     . ASN B  1  306  ? -1.657  9.861   110.483 1.00 21.51 ? 304  ASN B C     1 
ATOM   11185 O  O     . ASN B  1  306  ? -0.962  10.747  110.992 1.00 23.20 ? 304  ASN B O     1 
ATOM   11186 C  CB    . ASN B  1  306  ? -3.869  9.925   111.601 1.00 27.02 ? 304  ASN B CB    1 
ATOM   11187 C  CG    . ASN B  1  306  ? -4.441  10.504  110.343 1.00 28.82 ? 304  ASN B CG    1 
ATOM   11188 O  OD1   . ASN B  1  306  ? -5.176  9.829   109.618 1.00 27.84 ? 304  ASN B OD1   1 
ATOM   11189 N  ND2   . ASN B  1  306  ? -4.084  11.752  110.046 1.00 23.49 ? 304  ASN B ND2   1 
ATOM   11190 N  N     . ILE B  1  307  ? -1.621  9.559   109.191 1.00 21.64 ? 305  ILE B N     1 
ATOM   11191 C  CA    . ILE B  1  307  ? -0.817  10.319  108.244 1.00 20.07 ? 305  ILE B CA    1 
ATOM   11192 C  C     . ILE B  1  307  ? -1.725  11.357  107.597 1.00 22.69 ? 305  ILE B C     1 
ATOM   11193 O  O     . ILE B  1  307  ? -2.641  11.015  106.838 1.00 22.03 ? 305  ILE B O     1 
ATOM   11194 C  CB    . ILE B  1  307  ? -0.160  9.415   107.193 1.00 21.59 ? 305  ILE B CB    1 
ATOM   11195 C  CG1   . ILE B  1  307  ? 0.845   8.472   107.871 1.00 26.29 ? 305  ILE B CG1   1 
ATOM   11196 C  CG2   . ILE B  1  307  ? 0.497   10.257  106.100 1.00 21.16 ? 305  ILE B CG2   1 
ATOM   11197 C  CD1   . ILE B  1  307  ? 1.380   7.407   106.935 1.00 28.87 ? 305  ILE B CD1   1 
ATOM   11198 N  N     . ASP B  1  308  ? -1.481  12.627  107.921 1.00 21.05 ? 306  ASP B N     1 
ATOM   11199 C  CA    . ASP B  1  308  ? -2.224  13.718  107.311 1.00 21.58 ? 306  ASP B CA    1 
ATOM   11200 C  C     . ASP B  1  308  ? -1.945  13.776  105.817 1.00 20.83 ? 306  ASP B C     1 
ATOM   11201 O  O     . ASP B  1  308  ? -0.876  13.385  105.348 1.00 22.07 ? 306  ASP B O     1 
ATOM   11202 C  CB    . ASP B  1  308  ? -1.831  15.055  107.945 1.00 22.13 ? 306  ASP B CB    1 
ATOM   11203 C  CG    . ASP B  1  308  ? -2.371  15.234  109.358 1.00 23.90 ? 306  ASP B CG    1 
ATOM   11204 O  OD1   . ASP B  1  308  ? -3.181  14.407  109.822 1.00 22.64 ? 306  ASP B OD1   1 
ATOM   11205 O  OD2   . ASP B  1  308  ? -1.954  16.213  110.019 1.00 26.73 ? 306  ASP B OD2   1 
ATOM   11206 N  N     . ALA B  1  309  ? -2.911  14.284  105.068 1.00 19.57 ? 307  ALA B N     1 
ATOM   11207 C  CA    . ALA B  1  309  ? -2.769  14.436  103.627 1.00 18.24 ? 307  ALA B CA    1 
ATOM   11208 C  C     . ALA B  1  309  ? -2.375  15.866  103.312 1.00 21.04 ? 307  ALA B C     1 
ATOM   11209 O  O     . ALA B  1  309  ? -2.889  16.808  103.917 1.00 19.55 ? 307  ALA B O     1 
ATOM   11210 C  CB    . ALA B  1  309  ? -4.063  14.075  102.900 1.00 20.60 ? 307  ALA B CB    1 
ATOM   11211 N  N     . GLU B  1  310  ? -1.439  16.017  102.381 1.00 18.85 ? 308  GLU B N     1 
ATOM   11212 C  CA    . GLU B  1  310  ? -0.876  17.326  102.091 1.00 18.23 ? 308  GLU B CA    1 
ATOM   11213 C  C     . GLU B  1  310  ? -1.159  17.689  100.639 1.00 17.75 ? 308  GLU B C     1 
ATOM   11214 O  O     . GLU B  1  310  ? -2.292  17.507  100.183 1.00 17.87 ? 308  GLU B O     1 
ATOM   11215 C  CB    . GLU B  1  310  ? 0.615   17.321  102.451 1.00 18.55 ? 308  GLU B CB    1 
ATOM   11216 C  CG    . GLU B  1  310  ? 0.809   17.005  103.944 1.00 20.29 ? 308  GLU B CG    1 
ATOM   11217 C  CD    . GLU B  1  310  ? 2.245   17.126  104.404 1.00 22.24 ? 308  GLU B CD    1 
ATOM   11218 O  OE1   . GLU B  1  310  ? 2.709   18.273  104.580 1.00 22.41 ? 308  GLU B OE1   1 
ATOM   11219 O  OE2   . GLU B  1  310  ? 2.897   16.078  104.608 1.00 19.62 ? 308  GLU B OE2   1 
ATOM   11220 N  N     . GLU B  1  311  ? -0.166  18.190  99.912  1.00 16.25 ? 309  GLU B N     1 
ATOM   11221 C  CA    . GLU B  1  311  ? -0.398  18.667  98.554  1.00 15.81 ? 309  GLU B CA    1 
ATOM   11222 C  C     . GLU B  1  311  ? -0.713  17.504  97.620  1.00 19.05 ? 309  GLU B C     1 
ATOM   11223 O  O     . GLU B  1  311  ? -0.353  16.351  97.875  1.00 19.06 ? 309  GLU B O     1 
ATOM   11224 C  CB    . GLU B  1  311  ? 0.821   19.425  98.037  1.00 16.86 ? 309  GLU B CB    1 
ATOM   11225 C  CG    . GLU B  1  311  ? 1.128   20.708  98.811  1.00 21.80 ? 309  GLU B CG    1 
ATOM   11226 C  CD    . GLU B  1  311  ? 2.039   20.504  100.008 1.00 24.17 ? 309  GLU B CD    1 
ATOM   11227 O  OE1   . GLU B  1  311  ? 2.215   19.354  100.471 1.00 20.89 ? 309  GLU B OE1   1 
ATOM   11228 O  OE2   . GLU B  1  311  ? 2.597   21.519  100.485 1.00 28.28 ? 309  GLU B OE2   1 
ATOM   11229 N  N     . ALA B  1  312  ? -1.378  17.830  96.509  1.00 16.36 ? 310  ALA B N     1 
ATOM   11230 C  CA    . ALA B  1  312  ? -1.819  16.798  95.576  1.00 19.34 ? 310  ALA B CA    1 
ATOM   11231 C  C     . ALA B  1  312  ? -0.645  16.006  95.010  1.00 17.77 ? 310  ALA B C     1 
ATOM   11232 O  O     . ALA B  1  312  ? -0.780  14.799  94.778  1.00 19.60 ? 310  ALA B O     1 
ATOM   11233 C  CB    . ALA B  1  312  ? -2.621  17.429  94.435  1.00 17.92 ? 310  ALA B CB    1 
ATOM   11234 N  N     . ASP B  1  313  ? 0.522   16.641  94.830  1.00 18.48 ? 311  ASP B N     1 
ATOM   11235 C  CA    . ASP B  1  313  ? 1.651   15.920  94.244  1.00 17.99 ? 311  ASP B CA    1 
ATOM   11236 C  C     . ASP B  1  313  ? 2.383   15.046  95.250  1.00 19.51 ? 311  ASP B C     1 
ATOM   11237 O  O     . ASP B  1  313  ? 3.379   14.416  94.887  1.00 20.53 ? 311  ASP B O     1 
ATOM   11238 C  CB    . ASP B  1  313  ? 2.635   16.878  93.546  1.00 18.27 ? 311  ASP B CB    1 
ATOM   11239 C  CG    . ASP B  1  313  ? 3.295   17.885  94.478  1.00 21.19 ? 311  ASP B CG    1 
ATOM   11240 O  OD1   . ASP B  1  313  ? 3.136   17.831  95.713  1.00 21.45 ? 311  ASP B OD1   1 
ATOM   11241 O  OD2   . ASP B  1  313  ? 4.011   18.757  93.930  1.00 24.33 ? 311  ASP B OD2   1 
ATOM   11242 N  N     . ARG B  1  314  ? 1.894   14.960  96.483  1.00 17.09 ? 312  ARG B N     1 
ATOM   11243 C  CA    . ARG B  1  314  ? 2.417   14.021  97.463  1.00 18.89 ? 312  ARG B CA    1 
ATOM   11244 C  C     . ARG B  1  314  ? 1.479   12.855  97.732  1.00 18.85 ? 312  ARG B C     1 
ATOM   11245 O  O     . ARG B  1  314  ? 1.866   11.928  98.446  1.00 17.63 ? 312  ARG B O     1 
ATOM   11246 C  CB    . ARG B  1  314  ? 2.725   14.760  98.769  1.00 19.47 ? 312  ARG B CB    1 
ATOM   11247 C  CG    . ARG B  1  314  ? 4.003   15.564  98.661  1.00 19.14 ? 312  ARG B CG    1 
ATOM   11248 C  CD    . ARG B  1  314  ? 4.065   16.638  99.728  1.00 20.43 ? 312  ARG B CD    1 
ATOM   11249 N  NE    . ARG B  1  314  ? 5.422   17.157  99.849  1.00 20.32 ? 312  ARG B NE    1 
ATOM   11250 C  CZ    . ARG B  1  314  ? 5.769   18.168  100.633 1.00 21.54 ? 312  ARG B CZ    1 
ATOM   11251 N  NH1   . ARG B  1  314  ? 4.860   18.909  101.247 1.00 19.79 ? 312  ARG B NH1   1 
ATOM   11252 N  NH2   . ARG B  1  314  ? 7.064   18.437  100.813 1.00 21.87 ? 312  ARG B NH2   1 
ATOM   11253 N  N     . LEU B  1  315  ? 0.272   12.864  97.161  1.00 18.10 ? 313  LEU B N     1 
ATOM   11254 C  CA    . LEU B  1  315  ? -0.712  11.834  97.477  1.00 19.17 ? 313  LEU B CA    1 
ATOM   11255 C  C     . LEU B  1  315  ? -0.190  10.451  97.123  1.00 21.43 ? 313  LEU B C     1 
ATOM   11256 O  O     . LEU B  1  315  ? -0.131  9.557   97.976  1.00 21.03 ? 313  LEU B O     1 
ATOM   11257 C  CB    . LEU B  1  315  ? -2.025  12.113  96.741  1.00 19.62 ? 313  LEU B CB    1 
ATOM   11258 C  CG    . LEU B  1  315  ? -3.315  11.488  97.285  1.00 19.39 ? 313  LEU B CG    1 
ATOM   11259 C  CD1   . LEU B  1  315  ? -4.493  12.022  96.452  1.00 21.06 ? 313  LEU B CD1   1 
ATOM   11260 C  CD2   . LEU B  1  315  ? -3.303  9.965   97.252  1.00 24.72 ? 313  LEU B CD2   1 
ATOM   11261 N  N     . GLU B  1  316  ? 0.184   10.249  95.861  1.00 20.42 ? 314  GLU B N     1 
ATOM   11262 C  CA    . GLU B  1  316  ? 0.517   8.891   95.451  1.00 19.72 ? 314  GLU B CA    1 
ATOM   11263 C  C     . GLU B  1  316  ? 1.827   8.433   96.078  1.00 20.46 ? 314  GLU B C     1 
ATOM   11264 O  O     . GLU B  1  316  ? 1.954   7.266   96.461  1.00 22.57 ? 314  GLU B O     1 
ATOM   11265 C  CB    . GLU B  1  316  ? 0.532   8.799   93.926  1.00 23.19 ? 314  GLU B CB    1 
ATOM   11266 C  CG    . GLU B  1  316  ? -0.893  8.890   93.388  1.00 19.85 ? 314  GLU B CG    1 
ATOM   11267 C  CD    . GLU B  1  316  ? -0.990  8.791   91.875  1.00 23.79 ? 314  GLU B CD    1 
ATOM   11268 O  OE1   . GLU B  1  316  ? -0.360  7.889   91.293  1.00 25.33 ? 314  GLU B OE1   1 
ATOM   11269 O  OE2   . GLU B  1  316  ? -1.707  9.611   91.265  1.00 23.68 ? 314  GLU B OE2   1 
ATOM   11270 N  N     . LEU B  1  317  ? 2.784   9.346   96.250  1.00 20.08 ? 315  LEU B N     1 
ATOM   11271 C  CA    . LEU B  1  317  ? 3.995   8.999   96.985  1.00 22.48 ? 315  LEU B CA    1 
ATOM   11272 C  C     . LEU B  1  317  ? 3.662   8.476   98.374  1.00 22.49 ? 315  LEU B C     1 
ATOM   11273 O  O     . LEU B  1  317  ? 4.223   7.468   98.821  1.00 21.76 ? 315  LEU B O     1 
ATOM   11274 C  CB    . LEU B  1  317  ? 4.912   10.215  97.080  1.00 21.63 ? 315  LEU B CB    1 
ATOM   11275 C  CG    . LEU B  1  317  ? 6.217   10.009  97.844  1.00 22.55 ? 315  LEU B CG    1 
ATOM   11276 C  CD1   . LEU B  1  317  ? 6.980   8.807   97.298  1.00 29.13 ? 315  LEU B CD1   1 
ATOM   11277 C  CD2   . LEU B  1  317  ? 7.059   11.251  97.750  1.00 22.89 ? 315  LEU B CD2   1 
ATOM   11278 N  N     . SER B  1  318  ? 2.733   9.135   99.072  1.00 20.00 ? 316  SER B N     1 
ATOM   11279 C  CA    . SER B  1  318  ? 2.408   8.691   100.424 1.00 19.15 ? 316  SER B CA    1 
ATOM   11280 C  C     . SER B  1  318  ? 1.833   7.274   100.434 1.00 18.59 ? 316  SER B C     1 
ATOM   11281 O  O     . SER B  1  318  ? 2.025   6.541   101.410 1.00 22.46 ? 316  SER B O     1 
ATOM   11282 C  CB    . SER B  1  318  ? 1.445   9.677   101.092 1.00 20.58 ? 316  SER B CB    1 
ATOM   11283 O  OG    . SER B  1  318  ? 0.134   9.558   100.574 1.00 21.52 ? 316  SER B OG    1 
ATOM   11284 N  N     . LEU B  1  319  ? 1.160   6.855   99.354  1.00 20.42 ? 317  LEU B N     1 
ATOM   11285 C  CA    . LEU B  1  319  ? 0.630   5.499   99.290  1.00 21.48 ? 317  LEU B CA    1 
ATOM   11286 C  C     . LEU B  1  319  ? 1.735   4.454   99.278  1.00 21.51 ? 317  LEU B C     1 
ATOM   11287 O  O     . LEU B  1  319  ? 1.525   3.333   99.746  1.00 22.02 ? 317  LEU B O     1 
ATOM   11288 C  CB    . LEU B  1  319  ? -0.233  5.327   98.041  1.00 21.39 ? 317  LEU B CB    1 
ATOM   11289 C  CG    . LEU B  1  319  ? -1.446  6.245   97.951  1.00 22.88 ? 317  LEU B CG    1 
ATOM   11290 C  CD1   . LEU B  1  319  ? -2.108  6.009   96.606  1.00 20.08 ? 317  LEU B CD1   1 
ATOM   11291 C  CD2   . LEU B  1  319  ? -2.416  5.969   99.093  1.00 22.57 ? 317  LEU B CD2   1 
ATOM   11292 N  N     . ASP B  1  320  ? 2.898   4.778   98.712  1.00 21.42 ? 318  ASP B N     1 
ATOM   11293 C  CA    . ASP B  1  320  ? 3.990   3.815   98.746  1.00 25.02 ? 318  ASP B CA    1 
ATOM   11294 C  C     . ASP B  1  320  ? 4.482   3.576   100.164 1.00 24.44 ? 318  ASP B C     1 
ATOM   11295 O  O     . ASP B  1  320  ? 4.917   2.467   100.485 1.00 26.78 ? 318  ASP B O     1 
ATOM   11296 C  CB    . ASP B  1  320  ? 5.127   4.287   97.856  1.00 23.80 ? 318  ASP B CB    1 
ATOM   11297 C  CG    . ASP B  1  320  ? 4.811   4.101   96.391  1.00 24.26 ? 318  ASP B CG    1 
ATOM   11298 O  OD1   . ASP B  1  320  ? 4.433   2.974   96.006  1.00 27.01 ? 318  ASP B OD1   1 
ATOM   11299 O  OD2   . ASP B  1  320  ? 4.895   5.075   95.630  1.00 25.91 ? 318  ASP B OD2   1 
ATOM   11300 N  N     . LEU B  1  321  ? 4.418   4.593   101.027 1.00 20.89 ? 319  LEU B N     1 
ATOM   11301 C  CA    . LEU B  1  321  ? 4.752   4.368   102.429 1.00 21.94 ? 319  LEU B CA    1 
ATOM   11302 C  C     . LEU B  1  321  ? 3.652   3.589   103.134 1.00 23.42 ? 319  LEU B C     1 
ATOM   11303 O  O     . LEU B  1  321  ? 3.936   2.663   103.903 1.00 25.51 ? 319  LEU B O     1 
ATOM   11304 C  CB    . LEU B  1  321  ? 5.013   5.699   103.135 1.00 22.15 ? 319  LEU B CB    1 
ATOM   11305 C  CG    . LEU B  1  321  ? 6.358   6.366   102.846 1.00 22.51 ? 319  LEU B CG    1 
ATOM   11306 C  CD1   . LEU B  1  321  ? 6.308   7.214   101.587 1.00 23.32 ? 319  LEU B CD1   1 
ATOM   11307 C  CD2   . LEU B  1  321  ? 6.801   7.205   104.035 1.00 26.83 ? 319  LEU B CD2   1 
ATOM   11308 N  N     . LEU B  1  322  ? 2.388   3.930   102.867 1.00 21.90 ? 320  LEU B N     1 
ATOM   11309 C  CA    . LEU B  1  322  ? 1.280   3.199   103.475 1.00 22.67 ? 320  LEU B CA    1 
ATOM   11310 C  C     . LEU B  1  322  ? 1.352   1.717   103.141 1.00 24.20 ? 320  LEU B C     1 
ATOM   11311 O  O     . LEU B  1  322  ? 1.107   0.863   104.004 1.00 26.30 ? 320  LEU B O     1 
ATOM   11312 C  CB    . LEU B  1  322  ? -0.051  3.783   103.000 1.00 21.43 ? 320  LEU B CB    1 
ATOM   11313 C  CG    . LEU B  1  322  ? -1.289  3.163   103.657 1.00 25.89 ? 320  LEU B CG    1 
ATOM   11314 C  CD1   . LEU B  1  322  ? -1.252  3.425   105.164 1.00 26.36 ? 320  LEU B CD1   1 
ATOM   11315 C  CD2   . LEU B  1  322  ? -2.563  3.711   103.027 1.00 25.07 ? 320  LEU B CD2   1 
ATOM   11316 N  N     . GLU B  1  323  ? 1.696   1.401   101.892 1.00 23.44 ? 321  GLU B N     1 
ATOM   11317 C  CA    . GLU B  1  323  ? 1.825   0.014   101.449 1.00 25.10 ? 321  GLU B CA    1 
ATOM   11318 C  C     . GLU B  1  323  ? 2.826   -0.744  102.308 1.00 23.79 ? 321  GLU B C     1 
ATOM   11319 O  O     . GLU B  1  323  ? 2.535   -1.839  102.804 1.00 27.83 ? 321  GLU B O     1 
ATOM   11320 C  CB    . GLU B  1  323  ? 2.246   -0.018  99.977  1.00 28.13 ? 321  GLU B CB    1 
ATOM   11321 C  CG    . GLU B  1  323  ? 2.543   -1.416  99.411  1.00 31.32 ? 321  GLU B CG    1 
ATOM   11322 C  CD    . GLU B  1  323  ? 1.315   -2.108  98.839  1.00 36.08 ? 321  GLU B CD    1 
ATOM   11323 O  OE1   . GLU B  1  323  ? 0.288   -1.436  98.618  1.00 32.23 ? 321  GLU B OE1   1 
ATOM   11324 O  OE2   . GLU B  1  323  ? 1.373   -3.336  98.623  1.00 34.19 ? 321  GLU B OE2   1 
ATOM   11325 N  N     . VAL B  1  324  ? 4.022   -0.174  102.486 1.00 24.09 ? 322  VAL B N     1 
ATOM   11326 C  CA    . VAL B  1  324  ? 5.062   -0.852  103.256 1.00 28.74 ? 322  VAL B CA    1 
ATOM   11327 C  C     . VAL B  1  324  ? 4.624   -1.032  104.704 1.00 27.89 ? 322  VAL B C     1 
ATOM   11328 O  O     . VAL B  1  324  ? 4.787   -2.109  105.289 1.00 28.14 ? 322  VAL B O     1 
ATOM   11329 C  CB    . VAL B  1  324  ? 6.389   -0.075  103.153 1.00 29.67 ? 322  VAL B CB    1 
ATOM   11330 C  CG1   . VAL B  1  324  ? 7.435   -0.662  104.098 1.00 31.31 ? 322  VAL B CG1   1 
ATOM   11331 C  CG2   . VAL B  1  324  ? 6.892   -0.066  101.712 1.00 30.08 ? 322  VAL B CG2   1 
ATOM   11332 N  N     . LEU B  1  325  ? 4.049   0.013   105.300 1.00 27.75 ? 323  LEU B N     1 
ATOM   11333 C  CA    . LEU B  1  325  ? 3.663   -0.062  106.706 1.00 31.26 ? 323  LEU B CA    1 
ATOM   11334 C  C     . LEU B  1  325  ? 2.585   -1.113  106.941 1.00 28.46 ? 323  LEU B C     1 
ATOM   11335 O  O     . LEU B  1  325  ? 2.621   -1.838  107.943 1.00 28.60 ? 323  LEU B O     1 
ATOM   11336 C  CB    . LEU B  1  325  ? 3.190   1.305   107.184 1.00 28.98 ? 323  LEU B CB    1 
ATOM   11337 C  CG    . LEU B  1  325  ? 4.278   2.375   107.139 1.00 25.92 ? 323  LEU B CG    1 
ATOM   11338 C  CD1   . LEU B  1  325  ? 3.675   3.756   107.271 1.00 27.08 ? 323  LEU B CD1   1 
ATOM   11339 C  CD2   . LEU B  1  325  ? 5.284   2.111   108.248 1.00 26.13 ? 323  LEU B CD2   1 
ATOM   11340 N  N     . CYS B  1  326  ? 1.616   -1.220  106.032 1.00 27.53 ? 324  CYS B N     1 
ATOM   11341 C  CA    . CYS B  1  326  ? 0.557   -2.202  106.231 1.00 27.27 ? 324  CYS B CA    1 
ATOM   11342 C  C     . CYS B  1  326  ? 1.042   -3.634  106.043 1.00 27.67 ? 324  CYS B C     1 
ATOM   11343 O  O     . CYS B  1  326  ? 0.418   -4.554  106.579 1.00 29.05 ? 324  CYS B O     1 
ATOM   11344 C  CB    . CYS B  1  326  ? -0.616  -1.917  105.296 1.00 29.34 ? 324  CYS B CB    1 
ATOM   11345 S  SG    . CYS B  1  326  ? -1.485  -0.409  105.761 1.00 30.35 ? 324  CYS B SG    1 
ATOM   11346 N  N     . LEU B  1  327  ? 2.140   -3.840  105.309 1.00 26.37 ? 325  LEU B N     1 
ATOM   11347 C  CA    . LEU B  1  327  ? 2.713   -5.168  105.116 1.00 28.14 ? 325  LEU B CA    1 
ATOM   11348 C  C     . LEU B  1  327  ? 3.855   -5.467  106.077 1.00 30.28 ? 325  LEU B C     1 
ATOM   11349 O  O     . LEU B  1  327  ? 4.394   -6.581  106.062 1.00 32.96 ? 325  LEU B O     1 
ATOM   11350 C  CB    . LEU B  1  327  ? 3.198   -5.324  103.672 1.00 26.77 ? 325  LEU B CB    1 
ATOM   11351 C  CG    . LEU B  1  327  ? 2.061   -5.404  102.645 1.00 31.11 ? 325  LEU B CG    1 
ATOM   11352 C  CD1   . LEU B  1  327  ? 2.570   -5.182  101.225 1.00 37.02 ? 325  LEU B CD1   1 
ATOM   11353 C  CD2   . LEU B  1  327  ? 1.354   -6.741  102.749 1.00 42.00 ? 325  LEU B CD2   1 
ATOM   11354 N  N     . ASP B  1  328  ? 4.226   -4.513  106.922 1.00 29.19 ? 326  ASP B N     1 
ATOM   11355 C  CA    . ASP B  1  328  ? 5.335   -4.702  107.850 1.00 29.71 ? 326  ASP B CA    1 
ATOM   11356 C  C     . ASP B  1  328  ? 4.880   -5.569  109.016 1.00 28.48 ? 326  ASP B C     1 
ATOM   11357 O  O     . ASP B  1  328  ? 4.059   -5.141  109.835 1.00 35.32 ? 326  ASP B O     1 
ATOM   11358 C  CB    . ASP B  1  328  ? 5.835   -3.341  108.329 1.00 30.28 ? 326  ASP B CB    1 
ATOM   11359 C  CG    . ASP B  1  328  ? 7.129   -3.429  109.129 1.00 34.78 ? 326  ASP B CG    1 
ATOM   11360 O  OD1   . ASP B  1  328  ? 7.389   -4.467  109.768 1.00 34.73 ? 326  ASP B OD1   1 
ATOM   11361 O  OD2   . ASP B  1  328  ? 7.887   -2.438  109.124 1.00 38.61 ? 326  ASP B OD2   1 
ATOM   11362 N  N     . GLY B  1  329  ? 5.432   -6.781  109.112 1.00 35.52 ? 327  GLY B N     1 
ATOM   11363 C  CA    . GLY B  1  329  ? 5.056   -7.692  110.176 1.00 34.18 ? 327  GLY B CA    1 
ATOM   11364 C  C     . GLY B  1  329  ? 5.341   -7.180  111.571 1.00 32.20 ? 327  GLY B C     1 
ATOM   11365 O  O     . GLY B  1  329  ? 4.699   -7.624  112.528 1.00 34.81 ? 327  GLY B O     1 
ATOM   11366 N  N     . ASP B  1  330  ? 6.285   -6.247  111.717 1.00 32.58 ? 328  ASP B N     1 
ATOM   11367 C  CA    . ASP B  1  330  ? 6.512   -5.664  113.035 1.00 32.42 ? 328  ASP B CA    1 
ATOM   11368 C  C     . ASP B  1  330  ? 5.274   -4.954  113.566 1.00 35.78 ? 328  ASP B C     1 
ATOM   11369 O  O     . ASP B  1  330  ? 5.139   -4.788  114.784 1.00 36.91 ? 328  ASP B O     1 
ATOM   11370 C  CB    . ASP B  1  330  ? 7.702   -4.697  112.993 1.00 35.87 ? 328  ASP B CB    1 
ATOM   11371 C  CG    . ASP B  1  330  ? 9.025   -5.407  112.775 1.00 39.41 ? 328  ASP B CG    1 
ATOM   11372 O  OD1   . ASP B  1  330  ? 9.090   -6.634  113.018 1.00 40.58 ? 328  ASP B OD1   1 
ATOM   11373 O  OD2   . ASP B  1  330  ? 10.005  -4.747  112.372 1.00 35.86 ? 328  ASP B OD2   1 
ATOM   11374 N  N     . LEU B  1  331  ? 4.360   -4.543  112.685 1.00 31.94 ? 329  LEU B N     1 
ATOM   11375 C  CA    . LEU B  1  331  ? 3.133   -3.870  113.085 1.00 30.23 ? 329  LEU B CA    1 
ATOM   11376 C  C     . LEU B  1  331  ? 1.940   -4.814  113.115 1.00 29.93 ? 329  LEU B C     1 
ATOM   11377 O  O     . LEU B  1  331  ? 0.796   -4.353  113.128 1.00 31.35 ? 329  LEU B O     1 
ATOM   11378 C  CB    . LEU B  1  331  ? 2.857   -2.690  112.154 1.00 27.58 ? 329  LEU B CB    1 
ATOM   11379 C  CG    . LEU B  1  331  ? 4.021   -1.713  112.013 1.00 26.19 ? 329  LEU B CG    1 
ATOM   11380 C  CD1   . LEU B  1  331  ? 3.708   -0.627  110.999 1.00 28.01 ? 329  LEU B CD1   1 
ATOM   11381 C  CD2   . LEU B  1  331  ? 4.349   -1.116  113.378 1.00 31.82 ? 329  LEU B CD2   1 
ATOM   11382 N  N     . SER B  1  332  ? 2.199   -6.121  113.146 1.00 33.55 ? 330  SER B N     1 
ATOM   11383 C  CA    . SER B  1  332  ? 1.158   -7.143  113.088 1.00 30.69 ? 330  SER B CA    1 
ATOM   11384 C  C     . SER B  1  332  ? 0.030   -6.894  114.084 1.00 36.95 ? 330  SER B C     1 
ATOM   11385 O  O     . SER B  1  332  ? 0.269   -6.677  115.275 1.00 42.69 ? 330  SER B O     1 
ATOM   11386 C  CB    . SER B  1  332  ? 1.789   -8.505  113.367 1.00 35.10 ? 330  SER B CB    1 
ATOM   11387 O  OG    . SER B  1  332  ? 0.807   -9.524  113.375 1.00 46.34 ? 330  SER B OG    1 
ATOM   11388 N  N     . GLY B  1  333  ? -1.205  -6.949  113.589 1.00 32.65 ? 331  GLY B N     1 
ATOM   11389 C  CA    . GLY B  1  333  ? -2.380  -6.864  114.431 1.00 44.14 ? 331  GLY B CA    1 
ATOM   11390 C  C     . GLY B  1  333  ? -2.751  -5.473  114.900 1.00 44.46 ? 331  GLY B C     1 
ATOM   11391 O  O     . GLY B  1  333  ? -3.783  -5.318  115.567 1.00 38.14 ? 331  GLY B O     1 
ATOM   11392 N  N     . TRP B  1  334  ? -1.951  -4.462  114.581 1.00 34.56 ? 332  TRP B N     1 
ATOM   11393 C  CA    . TRP B  1  334  ? -2.226  -3.091  114.985 1.00 38.47 ? 332  TRP B CA    1 
ATOM   11394 C  C     . TRP B  1  334  ? -3.171  -2.456  113.975 1.00 31.28 ? 332  TRP B C     1 
ATOM   11395 O  O     . TRP B  1  334  ? -2.838  -2.346  112.792 1.00 36.69 ? 332  TRP B O     1 
ATOM   11396 C  CB    . TRP B  1  334  ? -0.919  -2.311  115.082 1.00 33.91 ? 332  TRP B CB    1 
ATOM   11397 C  CG    . TRP B  1  334  ? -1.062  -0.842  115.350 1.00 33.89 ? 332  TRP B CG    1 
ATOM   11398 C  CD1   . TRP B  1  334  ? -1.672  -0.253  116.422 1.00 35.07 ? 332  TRP B CD1   1 
ATOM   11399 C  CD2   . TRP B  1  334  ? -0.542  0.219   114.550 1.00 32.09 ? 332  TRP B CD2   1 
ATOM   11400 N  NE1   . TRP B  1  334  ? -1.569  1.119   116.330 1.00 30.15 ? 332  TRP B NE1   1 
ATOM   11401 C  CE2   . TRP B  1  334  ? -0.882  1.433   115.185 1.00 27.64 ? 332  TRP B CE2   1 
ATOM   11402 C  CE3   . TRP B  1  334  ? 0.172   0.263   113.350 1.00 30.65 ? 332  TRP B CE3   1 
ATOM   11403 C  CZ2   . TRP B  1  334  ? -0.530  2.677   114.655 1.00 24.53 ? 332  TRP B CZ2   1 
ATOM   11404 C  CZ3   . TRP B  1  334  ? 0.524   1.494   112.831 1.00 32.40 ? 332  TRP B CZ3   1 
ATOM   11405 C  CH2   . TRP B  1  334  ? 0.173   2.688   113.485 1.00 32.46 ? 332  TRP B CH2   1 
ATOM   11406 N  N     . ASN B  1  335  ? -4.351  -2.051  114.429 1.00 32.99 ? 333  ASN B N     1 
ATOM   11407 C  CA    . ASN B  1  335  ? -5.327  -1.431  113.546 1.00 33.48 ? 333  ASN B CA    1 
ATOM   11408 C  C     . ASN B  1  335  ? -5.315  0.085   113.650 1.00 30.87 ? 333  ASN B C     1 
ATOM   11409 O  O     . ASN B  1  335  ? -6.263  0.741   113.208 1.00 31.77 ? 333  ASN B O     1 
ATOM   11410 C  CB    . ASN B  1  335  ? -6.723  -1.973  113.842 1.00 31.72 ? 333  ASN B CB    1 
ATOM   11411 C  CG    . ASN B  1  335  ? -6.870  -3.427  113.450 1.00 40.55 ? 333  ASN B CG    1 
ATOM   11412 O  OD1   . ASN B  1  335  ? -6.228  -3.888  112.505 1.00 34.41 ? 333  ASN B OD1   1 
ATOM   11413 N  ND2   . ASN B  1  335  ? -7.710  -4.159  114.178 1.00 39.76 ? 333  ASN B ND2   1 
ATOM   11414 N  N     . GLY B  1  336  ? -4.273  0.652   114.237 1.00 31.05 ? 334  GLY B N     1 
ATOM   11415 C  CA    . GLY B  1  336  ? -4.230  2.081   114.445 1.00 28.74 ? 334  GLY B CA    1 
ATOM   11416 C  C     . GLY B  1  336  ? -3.617  2.890   113.336 1.00 28.16 ? 334  GLY B C     1 
ATOM   11417 O  O     . GLY B  1  336  ? -3.538  4.114   113.457 1.00 27.19 ? 334  GLY B O     1 
ATOM   11418 N  N     . MET B  1  337  ? -3.155  2.260   112.261 1.00 28.30 ? 335  MET B N     1 
ATOM   11419 C  CA    A MET B  1  337  ? -2.617  3.021   111.140 0.67 26.14 ? 335  MET B CA    1 
ATOM   11420 C  CA    B MET B  1  337  ? -2.625  3.003   111.127 0.33 26.24 ? 335  MET B CA    1 
ATOM   11421 C  C     . MET B  1  337  ? -3.734  3.828   110.491 1.00 30.13 ? 335  MET B C     1 
ATOM   11422 O  O     . MET B  1  337  ? -4.744  3.270   110.044 1.00 29.78 ? 335  MET B O     1 
ATOM   11423 C  CB    A MET B  1  337  ? -1.957  2.098   110.122 0.67 28.80 ? 335  MET B CB    1 
ATOM   11424 C  CB    B MET B  1  337  ? -2.027  2.026   110.118 0.33 28.83 ? 335  MET B CB    1 
ATOM   11425 C  CG    A MET B  1  337  ? -1.155  2.830   109.053 0.67 25.91 ? 335  MET B CG    1 
ATOM   11426 C  CG    B MET B  1  337  ? -1.722  2.614   108.765 0.33 30.73 ? 335  MET B CG    1 
ATOM   11427 S  SD    A MET B  1  337  ? 0.323   3.597   109.726 0.67 34.32 ? 335  MET B SD    1 
ATOM   11428 S  SD    B MET B  1  337  ? -0.271  3.660   108.820 0.33 26.68 ? 335  MET B SD    1 
ATOM   11429 C  CE    A MET B  1  337  ? -0.078  5.316   109.438 0.67 26.02 ? 335  MET B CE    1 
ATOM   11430 C  CE    B MET B  1  337  ? 0.931   2.583   109.587 0.33 33.59 ? 335  MET B CE    1 
ATOM   11431 N  N     . GLY B  1  338  ? -3.556  5.145   110.461 1.00 26.34 ? 336  GLY B N     1 
ATOM   11432 C  CA    . GLY B  1  338  ? -4.539  6.060   109.916 1.00 26.52 ? 336  GLY B CA    1 
ATOM   11433 C  C     . GLY B  1  338  ? -4.014  6.775   108.687 1.00 27.42 ? 336  GLY B C     1 
ATOM   11434 O  O     . GLY B  1  338  ? -2.812  7.019   108.555 1.00 25.35 ? 336  GLY B O     1 
ATOM   11435 N  N     . PHE B  1  339  ? -4.924  7.117   107.777 1.00 24.55 ? 337  PHE B N     1 
ATOM   11436 C  CA    . PHE B  1  339  ? -4.519  7.731   106.520 1.00 22.70 ? 337  PHE B CA    1 
ATOM   11437 C  C     . PHE B  1  339  ? -5.637  8.642   106.045 1.00 24.36 ? 337  PHE B C     1 
ATOM   11438 O  O     . PHE B  1  339  ? -6.798  8.229   105.999 1.00 24.65 ? 337  PHE B O     1 
ATOM   11439 C  CB    . PHE B  1  339  ? -4.202  6.653   105.474 1.00 23.16 ? 337  PHE B CB    1 
ATOM   11440 C  CG    . PHE B  1  339  ? -3.535  7.167   104.235 1.00 20.44 ? 337  PHE B CG    1 
ATOM   11441 C  CD1   . PHE B  1  339  ? -2.157  7.298   104.161 1.00 24.93 ? 337  PHE B CD1   1 
ATOM   11442 C  CD2   . PHE B  1  339  ? -4.286  7.497   103.118 1.00 21.24 ? 337  PHE B CD2   1 
ATOM   11443 C  CE1   . PHE B  1  339  ? -1.545  7.755   102.987 1.00 21.17 ? 337  PHE B CE1   1 
ATOM   11444 C  CE2   . PHE B  1  339  ? -3.676  7.946   101.949 1.00 23.84 ? 337  PHE B CE2   1 
ATOM   11445 C  CZ    . PHE B  1  339  ? -2.306  8.083   101.896 1.00 24.70 ? 337  PHE B CZ    1 
ATOM   11446 N  N     . VAL B  1  340  ? -5.292  9.881   105.734 1.00 21.77 ? 338  VAL B N     1 
ATOM   11447 C  CA    . VAL B  1  340  ? -6.262  10.871  105.282 1.00 19.93 ? 338  VAL B CA    1 
ATOM   11448 C  C     . VAL B  1  340  ? -6.423  10.774  103.774 1.00 24.32 ? 338  VAL B C     1 
ATOM   11449 O  O     . VAL B  1  340  ? -5.441  10.653  103.040 1.00 22.34 ? 338  VAL B O     1 
ATOM   11450 C  CB    . VAL B  1  340  ? -5.816  12.288  105.683 1.00 20.34 ? 338  VAL B CB    1 
ATOM   11451 C  CG1   . VAL B  1  340  ? -6.790  13.306  105.141 1.00 22.19 ? 338  VAL B CG1   1 
ATOM   11452 C  CG2   . VAL B  1  340  ? -5.707  12.404  107.187 1.00 20.94 ? 338  VAL B CG2   1 
ATOM   11453 N  N     . VAL B  1  341  ? -7.664  10.857  103.306 1.00 20.91 ? 339  VAL B N     1 
ATOM   11454 C  CA    . VAL B  1  341  ? -7.955  11.034  101.892 1.00 21.79 ? 339  VAL B CA    1 
ATOM   11455 C  C     . VAL B  1  341  ? -8.820  12.276  101.741 1.00 20.39 ? 339  VAL B C     1 
ATOM   11456 O  O     . VAL B  1  341  ? -9.746  12.501  102.535 1.00 22.84 ? 339  VAL B O     1 
ATOM   11457 C  CB    . VAL B  1  341  ? -8.640  9.789   101.299 1.00 25.91 ? 339  VAL B CB    1 
ATOM   11458 C  CG1   . VAL B  1  341  ? -7.715  8.596   101.422 1.00 28.52 ? 339  VAL B CG1   1 
ATOM   11459 C  CG2   . VAL B  1  341  ? -9.961  9.515   102.001 1.00 35.83 ? 339  VAL B CG2   1 
ATOM   11460 N  N     . GLN B  1  342  ? -8.510  13.072  100.717 1.00 20.98 ? 340  GLN B N     1 
ATOM   11461 C  CA    . GLN B  1  342  ? -9.094  14.393  100.500 1.00 20.20 ? 340  GLN B CA    1 
ATOM   11462 C  C     . GLN B  1  342  ? -10.164 14.305  99.417  1.00 21.57 ? 340  GLN B C     1 
ATOM   11463 O  O     . GLN B  1  342  ? -9.850  14.073  98.244  1.00 20.47 ? 340  GLN B O     1 
ATOM   11464 C  CB    . GLN B  1  342  ? -8.013  15.396  100.099 1.00 19.49 ? 340  GLN B CB    1 
ATOM   11465 C  CG    . GLN B  1  342  ? -6.974  15.655  101.180 1.00 19.50 ? 340  GLN B CG    1 
ATOM   11466 C  CD    . GLN B  1  342  ? -5.626  16.016  100.589 1.00 19.23 ? 340  GLN B CD    1 
ATOM   11467 O  OE1   . GLN B  1  342  ? -5.188  15.395  99.628  1.00 20.42 ? 340  GLN B OE1   1 
ATOM   11468 N  NE2   . GLN B  1  342  ? -4.967  17.038  101.151 1.00 18.76 ? 340  GLN B NE2   1 
ATOM   11469 N  N     . ALA B  1  343  ? -11.415 14.541  99.812  1.00 21.38 ? 341  ALA B N     1 
ATOM   11470 C  CA    . ALA B  1  343  ? -12.531 14.422  98.881  1.00 20.16 ? 341  ALA B CA    1 
ATOM   11471 C  C     . ALA B  1  343  ? -12.574 15.549  97.858  1.00 20.98 ? 341  ALA B C     1 
ATOM   11472 O  O     . ALA B  1  343  ? -13.243 15.395  96.832  1.00 23.38 ? 341  ALA B O     1 
ATOM   11473 C  CB    . ALA B  1  343  ? -13.848 14.367  99.650  1.00 23.18 ? 341  ALA B CB    1 
ATOM   11474 N  N     . TYR B  1  344  ? -11.866 16.668  98.088  1.00 21.46 ? 342  TYR B N     1 
ATOM   11475 C  CA    . TYR B  1  344  ? -11.808 17.628  96.994  1.00 20.68 ? 342  TYR B CA    1 
ATOM   11476 C  C     . TYR B  1  344  ? -10.912 17.153  95.864  1.00 19.26 ? 342  TYR B C     1 
ATOM   11477 O  O     . TYR B  1  344  ? -10.839 17.831  94.837  1.00 20.67 ? 342  TYR B O     1 
ATOM   11478 C  CB    . TYR B  1  344  ? -11.378 19.031  97.477  1.00 20.80 ? 342  TYR B CB    1 
ATOM   11479 C  CG    . TYR B  1  344  ? -9.942  19.306  97.901  1.00 20.45 ? 342  TYR B CG    1 
ATOM   11480 C  CD1   . TYR B  1  344  ? -8.980  18.310  97.992  1.00 19.21 ? 342  TYR B CD1   1 
ATOM   11481 C  CD2   . TYR B  1  344  ? -9.561  20.605  98.220  1.00 17.08 ? 342  TYR B CD2   1 
ATOM   11482 C  CE1   . TYR B  1  344  ? -7.665  18.608  98.391  1.00 18.74 ? 342  TYR B CE1   1 
ATOM   11483 C  CE2   . TYR B  1  344  ? -8.270  20.909  98.627  1.00 20.25 ? 342  TYR B CE2   1 
ATOM   11484 C  CZ    . TYR B  1  344  ? -7.330  19.913  98.712  1.00 20.28 ? 342  TYR B CZ    1 
ATOM   11485 O  OH    . TYR B  1  344  ? -6.056  20.235  99.119  1.00 19.24 ? 342  TYR B OH    1 
ATOM   11486 N  N     . GLY B  1  345  ? -10.250 16.009  96.026  1.00 19.96 ? 343  GLY B N     1 
ATOM   11487 C  CA    . GLY B  1  345  ? -9.348  15.499  95.014  1.00 22.54 ? 343  GLY B CA    1 
ATOM   11488 C  C     . GLY B  1  345  ? -10.056 14.529  94.080  1.00 20.55 ? 343  GLY B C     1 
ATOM   11489 O  O     . GLY B  1  345  ? -10.874 13.717  94.504  1.00 21.91 ? 343  GLY B O     1 
ATOM   11490 N  N     . LYS B  1  346  ? -9.716  14.630  92.795  1.00 18.86 ? 344  LYS B N     1 
ATOM   11491 C  CA    . LYS B  1  346  ? -10.365 13.789  91.797  1.00 19.97 ? 344  LYS B CA    1 
ATOM   11492 C  C     . LYS B  1  346  ? -10.025 12.317  91.965  1.00 22.02 ? 344  LYS B C     1 
ATOM   11493 O  O     . LYS B  1  346  ? -10.779 11.462  91.492  1.00 23.21 ? 344  LYS B O     1 
ATOM   11494 C  CB    . LYS B  1  346  ? -9.971  14.259  90.397  1.00 20.72 ? 344  LYS B CB    1 
ATOM   11495 C  CG    . LYS B  1  346  ? -10.452 15.656  90.100  1.00 21.46 ? 344  LYS B CG    1 
ATOM   11496 C  CD    . LYS B  1  346  ? -9.947  16.143  88.777  1.00 21.39 ? 344  LYS B CD    1 
ATOM   11497 C  CE    . LYS B  1  346  ? -10.620 17.462  88.451  1.00 20.66 ? 344  LYS B CE    1 
ATOM   11498 N  NZ    . LYS B  1  346  ? -10.067 18.081  87.207  1.00 21.03 ? 344  LYS B NZ    1 
ATOM   11499 N  N     . ARG B  1  347  ? -8.912  12.000  92.612  1.00 21.20 ? 345  ARG B N     1 
ATOM   11500 C  CA    . ARG B  1  347  ? -8.520  10.607  92.755  1.00 21.77 ? 345  ARG B CA    1 
ATOM   11501 C  C     . ARG B  1  347  ? -9.144  9.939   93.967  1.00 24.38 ? 345  ARG B C     1 
ATOM   11502 O  O     . ARG B  1  347  ? -8.987  8.724   94.130  1.00 23.88 ? 345  ARG B O     1 
ATOM   11503 C  CB    . ARG B  1  347  ? -7.000  10.517  92.818  1.00 19.25 ? 345  ARG B CB    1 
ATOM   11504 C  CG    . ARG B  1  347  ? -6.353  10.948  91.519  1.00 19.19 ? 345  ARG B CG    1 
ATOM   11505 C  CD    . ARG B  1  347  ? -4.882  11.183  91.730  1.00 20.29 ? 345  ARG B CD    1 
ATOM   11506 N  NE    . ARG B  1  347  ? -4.625  12.444  92.428  1.00 19.53 ? 345  ARG B NE    1 
ATOM   11507 C  CZ    . ARG B  1  347  ? -3.440  12.795  92.904  1.00 20.44 ? 345  ARG B CZ    1 
ATOM   11508 N  NH1   . ARG B  1  347  ? -2.371  12.037  92.721  1.00 19.41 ? 345  ARG B NH1   1 
ATOM   11509 N  NH2   . ARG B  1  347  ? -3.324  13.937  93.580  1.00 17.88 ? 345  ARG B NH2   1 
ATOM   11510 N  N     . CYS B  1  348  ? -9.881  10.693  94.786  1.00 22.66 ? 346  CYS B N     1 
ATOM   11511 C  CA    . CYS B  1  348  ? -10.315 10.212  96.098  1.00 22.98 ? 346  CYS B CA    1 
ATOM   11512 C  C     . CYS B  1  348  ? -11.020 8.860   96.072  1.00 24.20 ? 346  CYS B C     1 
ATOM   11513 O  O     . CYS B  1  348  ? -10.609 7.972   96.835  1.00 24.45 ? 346  CYS B O     1 
ATOM   11514 C  CB    . CYS B  1  348  ? -11.199 11.272  96.767  1.00 20.15 ? 346  CYS B CB    1 
ATOM   11515 S  SG    . CYS B  1  348  ? -11.501 10.919  98.545  1.00 28.57 ? 346  CYS B SG    1 
ATOM   11516 N  N     . PRO B  1  349  ? -12.054 8.622   95.252  1.00 23.57 ? 347  PRO B N     1 
ATOM   11517 C  CA    . PRO B  1  349  ? -12.685 7.295   95.288  1.00 25.96 ? 347  PRO B CA    1 
ATOM   11518 C  C     . PRO B  1  349  ? -11.738 6.183   94.886  1.00 25.21 ? 347  PRO B C     1 
ATOM   11519 O  O     . PRO B  1  349  ? -11.835 5.073   95.424  1.00 25.69 ? 347  PRO B O     1 
ATOM   11520 C  CB    . PRO B  1  349  ? -13.870 7.426   94.314  1.00 24.89 ? 347  PRO B CB    1 
ATOM   11521 C  CG    . PRO B  1  349  ? -13.554 8.562   93.465  1.00 23.30 ? 347  PRO B CG    1 
ATOM   11522 C  CD    . PRO B  1  349  ? -12.676 9.498   94.239  1.00 22.92 ? 347  PRO B CD    1 
ATOM   11523 N  N     . PHE B  1  350  ? -10.805 6.462   93.977  1.00 24.92 ? 348  PHE B N     1 
ATOM   11524 C  CA    . PHE B  1  350  ? -9.871  5.447   93.511  1.00 24.94 ? 348  PHE B CA    1 
ATOM   11525 C  C     . PHE B  1  350  ? -8.799  5.176   94.551  1.00 25.72 ? 348  PHE B C     1 
ATOM   11526 O  O     . PHE B  1  350  ? -8.371  4.027   94.727  1.00 24.76 ? 348  PHE B O     1 
ATOM   11527 C  CB    . PHE B  1  350  ? -9.267  5.891   92.184  1.00 23.28 ? 348  PHE B CB    1 
ATOM   11528 C  CG    . PHE B  1  350  ? -10.303 6.286   91.188  1.00 26.25 ? 348  PHE B CG    1 
ATOM   11529 C  CD1   . PHE B  1  350  ? -11.031 5.313   90.536  1.00 29.30 ? 348  PHE B CD1   1 
ATOM   11530 C  CD2   . PHE B  1  350  ? -10.597 7.618   90.949  1.00 24.08 ? 348  PHE B CD2   1 
ATOM   11531 C  CE1   . PHE B  1  350  ? -12.021 5.651   89.633  1.00 31.90 ? 348  PHE B CE1   1 
ATOM   11532 C  CE2   . PHE B  1  350  ? -11.595 7.963   90.043  1.00 26.34 ? 348  PHE B CE2   1 
ATOM   11533 C  CZ    . PHE B  1  350  ? -12.301 6.973   89.388  1.00 29.08 ? 348  PHE B CZ    1 
ATOM   11534 N  N     . VAL B  1  351  ? -8.379  6.222   95.264  1.00 22.76 ? 349  VAL B N     1 
ATOM   11535 C  CA    . VAL B  1  351  ? -7.496  6.037   96.414  1.00 22.06 ? 349  VAL B CA    1 
ATOM   11536 C  C     . VAL B  1  351  ? -8.178  5.184   97.482  1.00 25.25 ? 349  VAL B C     1 
ATOM   11537 O  O     . VAL B  1  351  ? -7.556  4.302   98.083  1.00 25.09 ? 349  VAL B O     1 
ATOM   11538 C  CB    . VAL B  1  351  ? -7.056  7.409   96.960  1.00 22.47 ? 349  VAL B CB    1 
ATOM   11539 C  CG1   . VAL B  1  351  ? -6.251  7.238   98.254  1.00 24.92 ? 349  VAL B CG1   1 
ATOM   11540 C  CG2   . VAL B  1  351  ? -6.238  8.149   95.919  1.00 23.15 ? 349  VAL B CG2   1 
ATOM   11541 N  N     . LEU B  1  352  ? -9.474  5.409   97.715  1.00 23.25 ? 350  LEU B N     1 
ATOM   11542 C  CA    . LEU B  1  352  ? -10.191 4.611   98.701  1.00 22.58 ? 350  LEU B CA    1 
ATOM   11543 C  C     . LEU B  1  352  ? -10.274 3.153   98.277  1.00 25.17 ? 350  LEU B C     1 
ATOM   11544 O  O     . LEU B  1  352  ? -10.167 2.250   99.117  1.00 27.82 ? 350  LEU B O     1 
ATOM   11545 C  CB    . LEU B  1  352  ? -11.582 5.187   98.921  1.00 26.44 ? 350  LEU B CB    1 
ATOM   11546 C  CG    . LEU B  1  352  ? -11.571 6.505   99.688  1.00 30.36 ? 350  LEU B CG    1 
ATOM   11547 C  CD1   . LEU B  1  352  ? -12.955 7.076   99.740  1.00 28.81 ? 350  LEU B CD1   1 
ATOM   11548 C  CD2   . LEU B  1  352  ? -11.050 6.260   101.105 1.00 27.69 ? 350  LEU B CD2   1 
ATOM   11549 N  N     . ASP B  1  353  ? -10.487 2.905   96.982  1.00 27.84 ? 351  ASP B N     1 
ATOM   11550 C  CA    . ASP B  1  353  ? -10.437 1.541   96.461  1.00 27.90 ? 351  ASP B CA    1 
ATOM   11551 C  C     . ASP B  1  353  ? -9.092  0.895   96.748  1.00 26.74 ? 351  ASP B C     1 
ATOM   11552 O  O     . ASP B  1  353  ? -9.027  -0.275  97.153  1.00 28.97 ? 351  ASP B O     1 
ATOM   11553 C  CB    . ASP B  1  353  ? -10.687 1.531   94.948  1.00 28.12 ? 351  ASP B CB    1 
ATOM   11554 C  CG    . ASP B  1  353  ? -12.127 1.844   94.572  1.00 33.18 ? 351  ASP B CG    1 
ATOM   11555 O  OD1   . ASP B  1  353  ? -13.034 1.671   95.407  1.00 33.23 ? 351  ASP B OD1   1 
ATOM   11556 O  OD2   . ASP B  1  353  ? -12.345 2.263   93.415  1.00 35.23 ? 351  ASP B OD2   1 
ATOM   11557 N  N     . PHE B  1  354  ? -8.006  1.636   96.523  1.00 26.36 ? 352  PHE B N     1 
ATOM   11558 C  CA    . PHE B  1  354  ? -6.674  1.110   96.800  1.00 27.79 ? 352  PHE B CA    1 
ATOM   11559 C  C     . PHE B  1  354  ? -6.504  0.808   98.284  1.00 29.08 ? 352  PHE B C     1 
ATOM   11560 O  O     . PHE B  1  354  ? -5.992  -0.252  98.653  1.00 27.02 ? 352  PHE B O     1 
ATOM   11561 C  CB    . PHE B  1  354  ? -5.600  2.094   96.329  1.00 26.98 ? 352  PHE B CB    1 
ATOM   11562 C  CG    . PHE B  1  354  ? -4.220  1.751   96.831  1.00 25.45 ? 352  PHE B CG    1 
ATOM   11563 C  CD1   . PHE B  1  354  ? -3.442  0.827   96.157  1.00 29.87 ? 352  PHE B CD1   1 
ATOM   11564 C  CD2   . PHE B  1  354  ? -3.712  2.338   97.988  1.00 26.08 ? 352  PHE B CD2   1 
ATOM   11565 C  CE1   . PHE B  1  354  ? -2.184  0.488   96.619  1.00 26.88 ? 352  PHE B CE1   1 
ATOM   11566 C  CE2   . PHE B  1  354  ? -2.449  1.999   98.460  1.00 28.31 ? 352  PHE B CE2   1 
ATOM   11567 C  CZ    . PHE B  1  354  ? -1.685  1.077   97.773  1.00 29.28 ? 352  PHE B CZ    1 
ATOM   11568 N  N     . ILE B  1  355  ? -6.921  1.738   99.151  1.00 23.90 ? 353  ILE B N     1 
ATOM   11569 C  CA    . ILE B  1  355  ? -6.746  1.554   100.594 1.00 25.12 ? 353  ILE B CA    1 
ATOM   11570 C  C     . ILE B  1  355  ? -7.599  0.402   101.106 1.00 27.01 ? 353  ILE B C     1 
ATOM   11571 O  O     . ILE B  1  355  ? -7.151  -0.400  101.938 1.00 28.52 ? 353  ILE B O     1 
ATOM   11572 C  CB    . ILE B  1  355  ? -7.077  2.855   101.344 1.00 26.50 ? 353  ILE B CB    1 
ATOM   11573 C  CG1   . ILE B  1  355  ? -6.084  3.944   100.965 1.00 28.65 ? 353  ILE B CG1   1 
ATOM   11574 C  CG2   . ILE B  1  355  ? -7.096  2.607   102.856 1.00 27.88 ? 353  ILE B CG2   1 
ATOM   11575 C  CD1   . ILE B  1  355  ? -6.457  5.284   101.526 1.00 25.99 ? 353  ILE B CD1   1 
ATOM   11576 N  N     . ILE B  1  356  ? -8.851  0.315   100.647 1.00 25.89 ? 354  ILE B N     1 
ATOM   11577 C  CA    . ILE B  1  356  ? -9.726  -0.769  101.089 1.00 30.91 ? 354  ILE B CA    1 
ATOM   11578 C  C     . ILE B  1  356  ? -9.155  -2.112  100.664 1.00 28.80 ? 354  ILE B C     1 
ATOM   11579 O  O     . ILE B  1  356  ? -9.175  -3.087  101.428 1.00 29.81 ? 354  ILE B O     1 
ATOM   11580 C  CB    . ILE B  1  356  ? -11.148 -0.563  100.537 1.00 28.92 ? 354  ILE B CB    1 
ATOM   11581 C  CG1   . ILE B  1  356  ? -11.825 0.620   101.228 1.00 32.78 ? 354  ILE B CG1   1 
ATOM   11582 C  CG2   . ILE B  1  356  ? -11.975 -1.834  100.701 1.00 28.75 ? 354  ILE B CG2   1 
ATOM   11583 C  CD1   . ILE B  1  356  ? -13.094 1.083   100.535 1.00 30.31 ? 354  ILE B CD1   1 
ATOM   11584 N  N     . ASP B  1  357  ? -8.636  -2.182  99.437  1.00 29.52 ? 355  ASP B N     1 
ATOM   11585 C  CA    . ASP B  1  357  ? -7.988  -3.405  98.985  1.00 31.50 ? 355  ASP B CA    1 
ATOM   11586 C  C     . ASP B  1  357  ? -6.741  -3.707  99.805  1.00 31.30 ? 355  ASP B C     1 
ATOM   11587 O  O     . ASP B  1  357  ? -6.505  -4.861  100.180 1.00 27.81 ? 355  ASP B O     1 
ATOM   11588 C  CB    . ASP B  1  357  ? -7.632  -3.301  97.510  1.00 30.74 ? 355  ASP B CB    1 
ATOM   11589 C  CG    . ASP B  1  357  ? -6.810  -4.472  97.043  1.00 32.05 ? 355  ASP B CG    1 
ATOM   11590 O  OD1   . ASP B  1  357  ? -7.388  -5.573  96.901  1.00 34.31 ? 355  ASP B OD1   1 
ATOM   11591 O  OD2   . ASP B  1  357  ? -5.590  -4.297  96.839  1.00 30.87 ? 355  ASP B OD2   1 
ATOM   11592 N  N     . LEU B  1  358  ? -5.932  -2.680  100.095 1.00 29.34 ? 356  LEU B N     1 
ATOM   11593 C  CA    . LEU B  1  358  ? -4.741  -2.883  100.909 1.00 29.60 ? 356  LEU B CA    1 
ATOM   11594 C  C     . LEU B  1  358  ? -5.107  -3.424  102.282 1.00 28.45 ? 356  LEU B C     1 
ATOM   11595 O  O     . LEU B  1  358  ? -4.455  -4.343  102.794 1.00 29.31 ? 356  LEU B O     1 
ATOM   11596 C  CB    . LEU B  1  358  ? -3.975  -1.569  101.039 1.00 24.51 ? 356  LEU B CB    1 
ATOM   11597 C  CG    . LEU B  1  358  ? -2.754  -1.546  101.970 1.00 26.82 ? 356  LEU B CG    1 
ATOM   11598 C  CD1   . LEU B  1  358  ? -1.749  -2.616  101.574 1.00 27.14 ? 356  LEU B CD1   1 
ATOM   11599 C  CD2   . LEU B  1  358  ? -2.113  -0.162  101.911 1.00 24.11 ? 356  LEU B CD2   1 
ATOM   11600 N  N     . ALA B  1  359  ? -6.163  -2.878  102.885 1.00 27.06 ? 357  ALA B N     1 
ATOM   11601 C  CA    . ALA B  1  359  ? -6.592  -3.346  104.197 1.00 26.96 ? 357  ALA B CA    1 
ATOM   11602 C  C     . ALA B  1  359  ? -7.063  -4.790  104.131 1.00 32.16 ? 357  ALA B C     1 
ATOM   11603 O  O     . ALA B  1  359  ? -6.722  -5.603  104.995 1.00 32.08 ? 357  ALA B O     1 
ATOM   11604 C  CB    . ALA B  1  359  ? -7.706  -2.449  104.732 1.00 36.07 ? 357  ALA B CB    1 
ATOM   11605 N  N     . ARG B  1  360  ? -7.839  -5.123  103.097 1.00 33.64 ? 358  ARG B N     1 
ATOM   11606 C  CA    . ARG B  1  360  ? -8.311  -6.492  102.927 1.00 36.53 ? 358  ARG B CA    1 
ATOM   11607 C  C     . ARG B  1  360  ? -7.150  -7.468  102.825 1.00 33.23 ? 358  ARG B C     1 
ATOM   11608 O  O     . ARG B  1  360  ? -7.140  -8.509  103.490 1.00 34.12 ? 358  ARG B O     1 
ATOM   11609 C  CB    . ARG B  1  360  ? -9.196  -6.591  101.684 1.00 33.44 ? 358  ARG B CB    1 
ATOM   11610 C  CG    . ARG B  1  360  ? -10.653 -6.401  101.973 1.00 37.92 ? 358  ARG B CG    1 
ATOM   11611 C  CD    . ARG B  1  360  ? -11.491 -6.864  100.789 1.00 39.97 ? 358  ARG B CD    1 
ATOM   11612 N  NE    . ARG B  1  360  ? -12.221 -5.758  100.194 1.00 47.14 ? 358  ARG B NE    1 
ATOM   11613 C  CZ    . ARG B  1  360  ? -13.403 -5.335  100.617 1.00 46.91 ? 358  ARG B CZ    1 
ATOM   11614 N  NH1   . ARG B  1  360  ? -14.002 -5.891  101.658 1.00 54.88 ? 358  ARG B NH1   1 
ATOM   11615 N  NH2   . ARG B  1  360  ? -14.002 -4.334  99.977  1.00 52.98 ? 358  ARG B NH2   1 
ATOM   11616 N  N     . ARG B  1  361  ? -6.162  -7.157  101.989 1.00 29.28 ? 359  ARG B N     1 
ATOM   11617 C  CA    . ARG B  1  361  ? -5.118  -8.141  101.748 1.00 37.77 ? 359  ARG B CA    1 
ATOM   11618 C  C     . ARG B  1  361  ? -4.026  -8.132  102.809 1.00 35.03 ? 359  ARG B C     1 
ATOM   11619 O  O     . ARG B  1  361  ? -3.288  -9.114  102.908 1.00 31.11 ? 359  ARG B O     1 
ATOM   11620 C  CB    . ARG B  1  361  ? -4.504  -7.945  100.363 1.00 37.77 ? 359  ARG B CB    1 
ATOM   11621 C  CG    . ARG B  1  361  ? -3.751  -6.657  100.164 1.00 38.15 ? 359  ARG B CG    1 
ATOM   11622 C  CD    . ARG B  1  361  ? -3.385  -6.484  98.685  1.00 33.87 ? 359  ARG B CD    1 
ATOM   11623 N  NE    . ARG B  1  361  ? -3.195  -5.076  98.349  1.00 28.06 ? 359  ARG B NE    1 
ATOM   11624 C  CZ    . ARG B  1  361  ? -2.033  -4.439  98.370  1.00 28.31 ? 359  ARG B CZ    1 
ATOM   11625 N  NH1   . ARG B  1  361  ? -0.910  -5.051  98.710  1.00 32.81 ? 359  ARG B NH1   1 
ATOM   11626 N  NH2   . ARG B  1  361  ? -1.999  -3.146  98.059  1.00 25.04 ? 359  ARG B NH2   1 
ATOM   11627 N  N     . SER B  1  362  ? -3.906  -7.065  103.605 1.00 32.73 ? 360  SER B N     1 
ATOM   11628 C  CA    . SER B  1  362  ? -2.878  -7.002  104.640 1.00 33.43 ? 360  SER B CA    1 
ATOM   11629 C  C     . SER B  1  362  ? -3.371  -7.421  106.019 1.00 31.34 ? 360  SER B C     1 
ATOM   11630 O  O     . SER B  1  362  ? -2.551  -7.551  106.940 1.00 31.87 ? 360  SER B O     1 
ATOM   11631 C  CB    . SER B  1  362  ? -2.305  -5.584  104.729 1.00 35.57 ? 360  SER B CB    1 
ATOM   11632 O  OG    . SER B  1  362  ? -3.302  -4.681  105.167 1.00 28.88 ? 360  SER B OG    1 
ATOM   11633 N  N     . GLY B  1  363  ? -4.672  -7.615  106.203 1.00 28.73 ? 361  GLY B N     1 
ATOM   11634 C  CA    . GLY B  1  363  ? -5.164  -7.975  107.517 1.00 33.38 ? 361  GLY B CA    1 
ATOM   11635 C  C     . GLY B  1  363  ? -5.072  -6.840  108.507 1.00 31.42 ? 361  GLY B C     1 
ATOM   11636 O  O     . GLY B  1  363  ? -4.965  -7.076  109.710 1.00 34.52 ? 361  GLY B O     1 
ATOM   11637 N  N     . ARG B  1  364  ? -5.100  -5.608  108.019 1.00 32.78 ? 362  ARG B N     1 
ATOM   11638 C  CA    . ARG B  1  364  ? -5.084  -4.410  108.845 1.00 38.09 ? 362  ARG B CA    1 
ATOM   11639 C  C     . ARG B  1  364  ? -6.396  -3.681  108.634 1.00 33.52 ? 362  ARG B C     1 
ATOM   11640 O  O     . ARG B  1  364  ? -6.803  -3.460  107.492 1.00 37.27 ? 362  ARG B O     1 
ATOM   11641 C  CB    . ARG B  1  364  ? -3.933  -3.476  108.463 1.00 33.63 ? 362  ARG B CB    1 
ATOM   11642 C  CG    . ARG B  1  364  ? -2.564  -4.086  108.539 1.00 34.82 ? 362  ARG B CG    1 
ATOM   11643 C  CD    . ARG B  1  364  ? -2.104  -4.215  109.980 1.00 31.83 ? 362  ARG B CD    1 
ATOM   11644 N  NE    . ARG B  1  364  ? -0.821  -4.900  110.039 1.00 33.94 ? 362  ARG B NE    1 
ATOM   11645 C  CZ    . ARG B  1  364  ? 0.349   -4.327  109.802 1.00 31.28 ? 362  ARG B CZ    1 
ATOM   11646 N  NH1   . ARG B  1  364  ? 0.449   -3.031  109.538 1.00 30.98 ? 362  ARG B NH1   1 
ATOM   11647 N  NH2   . ARG B  1  364  ? 1.450   -5.070  109.839 1.00 34.07 ? 362  ARG B NH2   1 
ATOM   11648 N  N     . ARG B  1  365  ? -7.058  -3.306  109.716 1.00 31.21 ? 363  ARG B N     1 
ATOM   11649 C  CA    . ARG B  1  365  ? -8.155  -2.360  109.587 1.00 33.22 ? 363  ARG B CA    1 
ATOM   11650 C  C     . ARG B  1  365  ? -7.539  -0.971  109.571 1.00 26.24 ? 363  ARG B C     1 
ATOM   11651 O  O     . ARG B  1  365  ? -7.011  -0.507  110.583 1.00 29.15 ? 363  ARG B O     1 
ATOM   11652 C  CB    . ARG B  1  365  ? -9.169  -2.524  110.711 1.00 32.75 ? 363  ARG B CB    1 
ATOM   11653 C  CG    . ARG B  1  365  ? -10.421 -1.694  110.500 1.00 31.65 ? 363  ARG B CG    1 
ATOM   11654 C  CD    . ARG B  1  365  ? -11.515 -2.069  111.495 1.00 38.38 ? 363  ARG B CD    1 
ATOM   11655 N  NE    . ARG B  1  365  ? -12.789 -1.447  111.156 1.00 41.08 ? 363  ARG B NE    1 
ATOM   11656 C  CZ    . ARG B  1  365  ? -13.468 -0.637  111.957 1.00 42.64 ? 363  ARG B CZ    1 
ATOM   11657 N  NH1   . ARG B  1  365  ? -13.047 -0.363  113.185 1.00 38.14 ? 363  ARG B NH1   1 
ATOM   11658 N  NH2   . ARG B  1  365  ? -14.606 -0.101  111.523 1.00 35.47 ? 363  ARG B NH2   1 
ATOM   11659 N  N     . ILE B  1  366  ? -7.548  -0.335  108.411 1.00 27.10 ? 364  ILE B N     1 
ATOM   11660 C  CA    . ILE B  1  366  ? -6.939  0.978   108.260 1.00 29.98 ? 364  ILE B CA    1 
ATOM   11661 C  C     . ILE B  1  366  ? -7.950  2.040   108.665 1.00 28.92 ? 364  ILE B C     1 
ATOM   11662 O  O     . ILE B  1  366  ? -9.114  2.002   108.248 1.00 29.93 ? 364  ILE B O     1 
ATOM   11663 C  CB    . ILE B  1  366  ? -6.454  1.184   106.817 1.00 26.64 ? 364  ILE B CB    1 
ATOM   11664 C  CG1   . ILE B  1  366  ? -5.409  0.123   106.460 1.00 29.12 ? 364  ILE B CG1   1 
ATOM   11665 C  CG2   . ILE B  1  366  ? -5.896  2.590   106.644 1.00 24.87 ? 364  ILE B CG2   1 
ATOM   11666 C  CD1   . ILE B  1  366  ? -4.973  0.136   105.020 1.00 31.38 ? 364  ILE B CD1   1 
ATOM   11667 N  N     . MET B  1  367  ? -7.517  2.978   109.502 1.00 28.39 ? 365  MET B N     1 
ATOM   11668 C  CA    . MET B  1  367  ? -8.343  4.123   109.857 1.00 28.65 ? 365  MET B CA    1 
ATOM   11669 C  C     . MET B  1  367  ? -8.246  5.129   108.728 1.00 30.50 ? 365  MET B C     1 
ATOM   11670 O  O     . MET B  1  367  ? -7.144  5.545   108.368 1.00 26.99 ? 365  MET B O     1 
ATOM   11671 C  CB    . MET B  1  367  ? -7.875  4.738   111.174 1.00 28.63 ? 365  MET B CB    1 
ATOM   11672 C  CG    . MET B  1  367  ? -7.751  3.727   112.278 1.00 27.59 ? 365  MET B CG    1 
ATOM   11673 S  SD    . MET B  1  367  ? -7.187  4.405   113.858 1.00 32.09 ? 365  MET B SD    1 
ATOM   11674 C  CE    . MET B  1  367  ? -8.691  4.956   114.649 1.00 43.99 ? 365  MET B CE    1 
ATOM   11675 N  N     . VAL B  1  368  ? -9.378  5.498   108.142 1.00 25.36 ? 366  VAL B N     1 
ATOM   11676 C  CA    . VAL B  1  368  ? -9.379  6.367   106.973 1.00 24.51 ? 366  VAL B CA    1 
ATOM   11677 C  C     . VAL B  1  368  ? -10.106 7.643   107.340 1.00 24.97 ? 366  VAL B C     1 
ATOM   11678 O  O     . VAL B  1  368  ? -11.325 7.639   107.545 1.00 26.25 ? 366  VAL B O     1 
ATOM   11679 C  CB    . VAL B  1  368  ? -10.022 5.704   105.754 1.00 28.31 ? 366  VAL B CB    1 
ATOM   11680 C  CG1   . VAL B  1  368  ? -9.914  6.646   104.566 1.00 28.85 ? 366  VAL B CG1   1 
ATOM   11681 C  CG2   . VAL B  1  368  ? -9.343  4.384   105.460 1.00 28.83 ? 366  VAL B CG2   1 
ATOM   11682 N  N     . ARG B  1  369  ? -9.370  8.742   107.417 1.00 26.09 ? 367  ARG B N     1 
ATOM   11683 C  CA    . ARG B  1  369  ? -9.984  10.027  107.698 1.00 24.74 ? 367  ARG B CA    1 
ATOM   11684 C  C     . ARG B  1  369  ? -10.368 10.648  106.369 1.00 27.85 ? 367  ARG B C     1 
ATOM   11685 O  O     . ARG B  1  369  ? -9.499  10.983  105.557 1.00 25.81 ? 367  ARG B O     1 
ATOM   11686 C  CB    . ARG B  1  369  ? -9.056  10.948  108.489 1.00 24.94 ? 367  ARG B CB    1 
ATOM   11687 C  CG    . ARG B  1  369  ? -9.728  12.278  108.781 1.00 26.66 ? 367  ARG B CG    1 
ATOM   11688 C  CD    . ARG B  1  369  ? -8.735  13.338  109.160 1.00 25.16 ? 367  ARG B CD    1 
ATOM   11689 N  NE    . ARG B  1  369  ? -8.055  13.020  110.406 1.00 23.99 ? 367  ARG B NE    1 
ATOM   11690 C  CZ    . ARG B  1  369  ? -6.852  13.471  110.720 1.00 25.41 ? 367  ARG B CZ    1 
ATOM   11691 N  NH1   . ARG B  1  369  ? -6.163  14.231  109.881 1.00 21.69 ? 367  ARG B NH1   1 
ATOM   11692 N  NH2   . ARG B  1  369  ? -6.327  13.138  111.898 1.00 25.96 ? 367  ARG B NH2   1 
ATOM   11693 N  N     . LEU B  1  370  ? -11.667 10.769  106.132 1.00 24.10 ? 368  LEU B N     1 
ATOM   11694 C  CA    . LEU B  1  370  ? -12.167 11.453  104.954 1.00 24.23 ? 368  LEU B CA    1 
ATOM   11695 C  C     . LEU B  1  370  ? -12.309 12.930  105.281 1.00 24.21 ? 368  LEU B C     1 
ATOM   11696 O  O     . LEU B  1  370  ? -13.061 13.305  106.187 1.00 27.80 ? 368  LEU B O     1 
ATOM   11697 C  CB    . LEU B  1  370  ? -13.499 10.855  104.510 1.00 23.46 ? 368  LEU B CB    1 
ATOM   11698 C  CG    . LEU B  1  370  ? -14.109 11.466  103.255 1.00 25.32 ? 368  LEU B CG    1 
ATOM   11699 C  CD1   . LEU B  1  370  ? -13.245 11.143  102.061 1.00 25.00 ? 368  LEU B CD1   1 
ATOM   11700 C  CD2   . LEU B  1  370  ? -15.513 10.918  103.055 1.00 25.52 ? 368  LEU B CD2   1 
ATOM   11701 N  N     . VAL B  1  371  ? -11.558 13.761  104.572 1.00 21.21 ? 369  VAL B N     1 
ATOM   11702 C  CA    . VAL B  1  371  ? -11.635 15.205  104.706 1.00 21.93 ? 369  VAL B CA    1 
ATOM   11703 C  C     . VAL B  1  371  ? -12.038 15.762  103.360 1.00 24.11 ? 369  VAL B C     1 
ATOM   11704 O  O     . VAL B  1  371  ? -12.033 15.059  102.352 1.00 24.18 ? 369  VAL B O     1 
ATOM   11705 C  CB    . VAL B  1  371  ? -10.302 15.822  105.167 1.00 20.64 ? 369  VAL B CB    1 
ATOM   11706 C  CG1   . VAL B  1  371  ? -9.856  15.158  106.430 1.00 21.55 ? 369  VAL B CG1   1 
ATOM   11707 C  CG2   . VAL B  1  371  ? -9.241  15.676  104.078 1.00 21.35 ? 369  VAL B CG2   1 
ATOM   11708 N  N     . LYS B  1  372  ? -12.353 17.051  103.335 1.00 21.46 ? 370  LYS B N     1 
ATOM   11709 C  CA    . LYS B  1  372  ? -12.502 17.681  102.033 1.00 23.98 ? 370  LYS B CA    1 
ATOM   11710 C  C     . LYS B  1  372  ? -11.138 18.091  101.478 1.00 21.81 ? 370  LYS B C     1 
ATOM   11711 O  O     . LYS B  1  372  ? -10.714 17.584  100.440 1.00 22.95 ? 370  LYS B O     1 
ATOM   11712 C  CB    . LYS B  1  372  ? -13.502 18.839  102.123 1.00 24.46 ? 370  LYS B CB    1 
ATOM   11713 C  CG    . LYS B  1  372  ? -14.905 18.275  102.387 1.00 24.53 ? 370  LYS B CG    1 
ATOM   11714 C  CD    . LYS B  1  372  ? -16.017 19.303  102.463 1.00 27.57 ? 370  LYS B CD    1 
ATOM   11715 C  CE    . LYS B  1  372  ? -17.308 18.622  102.904 1.00 28.76 ? 370  LYS B CE    1 
ATOM   11716 N  NZ    . LYS B  1  372  ? -18.380 19.619  103.163 1.00 28.40 ? 370  LYS B NZ    1 
ATOM   11717 N  N     . GLY B  1  373  ? -10.404 18.947  102.188 1.00 22.33 ? 371  GLY B N     1 
ATOM   11718 C  CA    . GLY B  1  373  ? -9.036  19.235  101.789 1.00 21.21 ? 371  GLY B CA    1 
ATOM   11719 C  C     . GLY B  1  373  ? -8.617  20.649  102.123 1.00 20.21 ? 371  GLY B C     1 
ATOM   11720 O  O     . GLY B  1  373  ? -9.416  21.575  101.972 1.00 23.95 ? 371  GLY B O     1 
ATOM   11721 N  N     . ALA B  1  374  ? -7.368  20.841  102.556 1.00 19.50 ? 372  ALA B N     1 
ATOM   11722 C  CA    . ALA B  1  374  ? -6.942  22.108  103.131 1.00 19.97 ? 372  ALA B CA    1 
ATOM   11723 C  C     . ALA B  1  374  ? -6.121  22.987  102.194 1.00 20.35 ? 372  ALA B C     1 
ATOM   11724 O  O     . ALA B  1  374  ? -5.732  24.083  102.607 1.00 22.61 ? 372  ALA B O     1 
ATOM   11725 C  CB    . ALA B  1  374  ? -6.125  21.856  104.394 1.00 20.84 ? 372  ALA B CB    1 
ATOM   11726 N  N     . TYR B  1  375  ? -5.845  22.555  100.953 1.00 17.98 ? 373  TYR B N     1 
ATOM   11727 C  CA    . TYR B  1  375  ? -4.881  23.258  100.114 1.00 18.44 ? 373  TYR B CA    1 
ATOM   11728 C  C     . TYR B  1  375  ? -5.501  23.755  98.819  1.00 19.82 ? 373  TYR B C     1 
ATOM   11729 O  O     . TYR B  1  375  ? -4.791  23.937  97.835  1.00 18.69 ? 373  TYR B O     1 
ATOM   11730 C  CB    . TYR B  1  375  ? -3.682  22.367  99.789  1.00 20.92 ? 373  TYR B CB    1 
ATOM   11731 C  CG    . TYR B  1  375  ? -2.997  21.779  100.992 1.00 18.85 ? 373  TYR B CG    1 
ATOM   11732 C  CD1   . TYR B  1  375  ? -3.530  20.684  101.655 1.00 19.77 ? 373  TYR B CD1   1 
ATOM   11733 C  CD2   . TYR B  1  375  ? -1.804  22.308  101.463 1.00 21.88 ? 373  TYR B CD2   1 
ATOM   11734 C  CE1   . TYR B  1  375  ? -2.911  20.150  102.758 1.00 20.02 ? 373  TYR B CE1   1 
ATOM   11735 C  CE2   . TYR B  1  375  ? -1.177  21.772  102.556 1.00 23.07 ? 373  TYR B CE2   1 
ATOM   11736 C  CZ    . TYR B  1  375  ? -1.730  20.692  103.198 1.00 23.29 ? 373  TYR B CZ    1 
ATOM   11737 O  OH    . TYR B  1  375  ? -1.112  20.141  104.300 1.00 27.04 ? 373  TYR B OH    1 
ATOM   11738 N  N     . TRP B  1  376  ? -6.805  24.033  98.831  1.00 19.13 ? 374  TRP B N     1 
ATOM   11739 C  CA    . TRP B  1  376  ? -7.529  24.234  97.581  1.00 18.69 ? 374  TRP B CA    1 
ATOM   11740 C  C     . TRP B  1  376  ? -6.956  25.392  96.763  1.00 18.37 ? 374  TRP B C     1 
ATOM   11741 O  O     . TRP B  1  376  ? -6.639  25.220  95.584  1.00 19.08 ? 374  TRP B O     1 
ATOM   11742 C  CB    . TRP B  1  376  ? -9.013  24.450  97.852  1.00 19.47 ? 374  TRP B CB    1 
ATOM   11743 C  CG    . TRP B  1  376  ? -9.750  24.619  96.577  1.00 19.23 ? 374  TRP B CG    1 
ATOM   11744 C  CD1   . TRP B  1  376  ? -10.142 23.633  95.716  1.00 21.13 ? 374  TRP B CD1   1 
ATOM   11745 C  CD2   . TRP B  1  376  ? -10.187 25.848  96.006  1.00 21.57 ? 374  TRP B CD2   1 
ATOM   11746 N  NE1   . TRP B  1  376  ? -10.795 24.182  94.641  1.00 20.57 ? 374  TRP B NE1   1 
ATOM   11747 C  CE2   . TRP B  1  376  ? -10.834 25.542  94.794  1.00 21.78 ? 374  TRP B CE2   1 
ATOM   11748 C  CE3   . TRP B  1  376  ? -10.090 27.187  96.402  1.00 24.37 ? 374  TRP B CE3   1 
ATOM   11749 C  CZ2   . TRP B  1  376  ? -11.378 26.520  93.972  1.00 22.21 ? 374  TRP B CZ2   1 
ATOM   11750 C  CZ3   . TRP B  1  376  ? -10.636 28.163  95.590  1.00 21.38 ? 374  TRP B CZ3   1 
ATOM   11751 C  CH2   . TRP B  1  376  ? -11.275 27.824  94.387  1.00 23.18 ? 374  TRP B CH2   1 
ATOM   11752 N  N     . ASP B  1  377  ? -6.815  26.588  97.357  1.00 19.00 ? 375  ASP B N     1 
ATOM   11753 C  CA    A ASP B  1  377  ? -6.314  27.747  96.611  0.57 19.38 ? 375  ASP B CA    1 
ATOM   11754 C  CA    B ASP B  1  377  ? -6.368  27.686  96.512  0.43 19.44 ? 375  ASP B CA    1 
ATOM   11755 C  C     . ASP B  1  377  ? -4.943  27.470  96.024  1.00 16.63 ? 375  ASP B C     1 
ATOM   11756 O  O     . ASP B  1  377  ? -4.621  27.902  94.913  1.00 19.67 ? 375  ASP B O     1 
ATOM   11757 C  CB    A ASP B  1  377  ? -6.217  28.976  97.519  0.57 23.67 ? 375  ASP B CB    1 
ATOM   11758 C  CB    B ASP B  1  377  ? -6.513  29.046  97.207  0.43 23.68 ? 375  ASP B CB    1 
ATOM   11759 C  CG    A ASP B  1  377  ? -7.556  29.436  98.039  0.57 28.47 ? 375  ASP B CG    1 
ATOM   11760 C  CG    B ASP B  1  377  ? -5.922  29.077  98.595  0.43 25.93 ? 375  ASP B CG    1 
ATOM   11761 O  OD1   A ASP B  1  377  ? -8.502  29.501  97.248  0.57 39.29 ? 375  ASP B OD1   1 
ATOM   11762 O  OD1   B ASP B  1  377  ? -4.800  28.579  98.782  0.43 30.23 ? 375  ASP B OD1   1 
ATOM   11763 O  OD2   A ASP B  1  377  ? -7.658  29.751  99.240  0.57 40.12 ? 375  ASP B OD2   1 
ATOM   11764 O  OD2   B ASP B  1  377  ? -6.576  29.638  99.497  0.43 33.52 ? 375  ASP B OD2   1 
ATOM   11765 N  N     . ALA B  1  378  ? -4.097  26.794  96.803  1.00 18.28 ? 376  ALA B N     1 
ATOM   11766 C  CA    . ALA B  1  378  ? -2.742  26.508  96.357  1.00 18.10 ? 376  ALA B CA    1 
ATOM   11767 C  C     . ALA B  1  378  ? -2.742  25.527  95.200  1.00 19.28 ? 376  ALA B C     1 
ATOM   11768 O  O     . ALA B  1  378  ? -1.899  25.633  94.296  1.00 18.55 ? 376  ALA B O     1 
ATOM   11769 C  CB    . ALA B  1  378  ? -1.924  25.954  97.528  1.00 18.70 ? 376  ALA B CB    1 
ATOM   11770 N  N     . GLU B  1  379  ? -3.684  24.582  95.206  1.00 17.41 ? 377  GLU B N     1 
ATOM   11771 C  CA    . GLU B  1  379  ? -3.737  23.607  94.124  1.00 16.92 ? 377  GLU B CA    1 
ATOM   11772 C  C     . GLU B  1  379  ? -4.186  24.265  92.828  1.00 19.48 ? 377  GLU B C     1 
ATOM   11773 O  O     . GLU B  1  379  ? -3.710  23.904  91.747  1.00 18.21 ? 377  GLU B O     1 
ATOM   11774 C  CB    . GLU B  1  379  ? -4.661  22.440  94.490  1.00 17.68 ? 377  GLU B CB    1 
ATOM   11775 C  CG    . GLU B  1  379  ? -4.242  21.617  95.715  1.00 19.20 ? 377  GLU B CG    1 
ATOM   11776 C  CD    . GLU B  1  379  ? -2.945  20.840  95.548  1.00 20.85 ? 377  GLU B CD    1 
ATOM   11777 O  OE1   . GLU B  1  379  ? -2.347  20.851  94.445  1.00 20.31 ? 377  GLU B OE1   1 
ATOM   11778 O  OE2   . GLU B  1  379  ? -2.524  20.200  96.540  1.00 19.18 ? 377  GLU B OE2   1 
ATOM   11779 N  N     . ILE B  1  380  ? -5.117  25.219  92.912  1.00 17.37 ? 378  ILE B N     1 
ATOM   11780 C  CA    . ILE B  1  380  ? -5.527  25.948  91.710  1.00 16.95 ? 378  ILE B CA    1 
ATOM   11781 C  C     . ILE B  1  380  ? -4.347  26.723  91.142  1.00 17.55 ? 378  ILE B C     1 
ATOM   11782 O  O     . ILE B  1  380  ? -4.041  26.641  89.948  1.00 17.68 ? 378  ILE B O     1 
ATOM   11783 C  CB    . ILE B  1  380  ? -6.708  26.883  92.020  1.00 19.59 ? 378  ILE B CB    1 
ATOM   11784 C  CG1   . ILE B  1  380  ? -7.902  26.108  92.598  1.00 18.30 ? 378  ILE B CG1   1 
ATOM   11785 C  CG2   . ILE B  1  380  ? -7.098  27.655  90.759  1.00 19.06 ? 378  ILE B CG2   1 
ATOM   11786 C  CD1   . ILE B  1  380  ? -8.503  25.071  91.651  1.00 21.04 ? 378  ILE B CD1   1 
ATOM   11787 N  N     . LYS B  1  381  ? -3.671  27.500  91.994  1.00 17.71 ? 379  LYS B N     1 
ATOM   11788 C  CA    . LYS B  1  381  ? -2.539  28.291  91.524  1.00 16.55 ? 379  LYS B CA    1 
ATOM   11789 C  C     . LYS B  1  381  ? -1.458  27.406  90.910  1.00 16.53 ? 379  LYS B C     1 
ATOM   11790 O  O     . LYS B  1  381  ? -0.934  27.712  89.837  1.00 16.94 ? 379  LYS B O     1 
ATOM   11791 C  CB    . LYS B  1  381  ? -1.965  29.108  92.679  1.00 17.05 ? 379  LYS B CB    1 
ATOM   11792 C  CG    . LYS B  1  381  ? -0.726  29.878  92.296  1.00 17.96 ? 379  LYS B CG    1 
ATOM   11793 C  CD    . LYS B  1  381  ? -0.306  30.811  93.431  1.00 16.02 ? 379  LYS B CD    1 
ATOM   11794 C  CE    . LYS B  1  381  ? 0.795   31.738  92.944  1.00 19.28 ? 379  LYS B CE    1 
ATOM   11795 N  NZ    . LYS B  1  381  ? 1.351   32.556  94.089  1.00 17.05 ? 379  LYS B NZ    1 
ATOM   11796 N  N     . ARG B  1  382  ? -1.129  26.293  91.572  1.00 17.51 ? 380  ARG B N     1 
ATOM   11797 C  CA    . ARG B  1  382  ? -0.035  25.442  91.111  1.00 18.19 ? 380  ARG B CA    1 
ATOM   11798 C  C     . ARG B  1  382  ? -0.322  24.858  89.734  1.00 17.49 ? 380  ARG B C     1 
ATOM   11799 O  O     . ARG B  1  382  ? 0.553   24.841  88.860  1.00 17.41 ? 380  ARG B O     1 
ATOM   11800 C  CB    . ARG B  1  382  ? 0.195   24.318  92.123  1.00 19.44 ? 380  ARG B CB    1 
ATOM   11801 C  CG    . ARG B  1  382  ? 1.426   23.471  91.860  1.00 29.11 ? 380  ARG B CG    1 
ATOM   11802 C  CD    . ARG B  1  382  ? 2.673   24.224  92.274  1.00 37.16 ? 380  ARG B CD    1 
ATOM   11803 N  NE    . ARG B  1  382  ? 3.490   24.591  91.129  1.00 38.77 ? 380  ARG B NE    1 
ATOM   11804 C  CZ    . ARG B  1  382  ? 4.403   25.556  91.132  1.00 41.93 ? 380  ARG B CZ    1 
ATOM   11805 N  NH1   . ARG B  1  382  ? 4.624   26.297  92.208  1.00 36.82 ? 380  ARG B NH1   1 
ATOM   11806 N  NH2   . ARG B  1  382  ? 5.107   25.789  90.024  1.00 34.70 ? 380  ARG B NH2   1 
ATOM   11807 N  N     . ALA B  1  383  ? -1.538  24.358  89.533  1.00 15.27 ? 381  ALA B N     1 
ATOM   11808 C  CA    . ALA B  1  383  ? -1.898  23.767  88.241  1.00 14.56 ? 381  ALA B CA    1 
ATOM   11809 C  C     . ALA B  1  383  ? -1.853  24.813  87.144  1.00 16.73 ? 381  ALA B C     1 
ATOM   11810 O  O     . ALA B  1  383  ? -1.398  24.540  86.030  1.00 16.88 ? 381  ALA B O     1 
ATOM   11811 C  CB    . ALA B  1  383  ? -3.284  23.141  88.324  1.00 17.68 ? 381  ALA B CB    1 
ATOM   11812 N  N     . GLN B  1  384  ? -2.292  26.030  87.457  1.00 15.83 ? 382  GLN B N     1 
ATOM   11813 C  CA    . GLN B  1  384  ? -2.216  27.108  86.486  1.00 17.21 ? 382  GLN B CA    1 
ATOM   11814 C  C     . GLN B  1  384  ? -0.774  27.460  86.176  1.00 15.20 ? 382  GLN B C     1 
ATOM   11815 O  O     . GLN B  1  384  ? -0.408  27.594  85.008  1.00 17.26 ? 382  GLN B O     1 
ATOM   11816 C  CB    . GLN B  1  384  ? -2.977  28.331  86.992  1.00 17.81 ? 382  GLN B CB    1 
ATOM   11817 C  CG    . GLN B  1  384  ? -4.480  28.143  86.909  1.00 16.57 ? 382  GLN B CG    1 
ATOM   11818 C  CD    . GLN B  1  384  ? -5.217  29.391  87.317  1.00 18.31 ? 382  GLN B CD    1 
ATOM   11819 O  OE1   . GLN B  1  384  ? -4.637  30.277  87.934  1.00 20.79 ? 382  GLN B OE1   1 
ATOM   11820 N  NE2   . GLN B  1  384  ? -6.495  29.464  86.993  1.00 18.36 ? 382  GLN B NE2   1 
ATOM   11821 N  N     . LEU B  1  385  ? 0.062   27.617  87.216  1.00 16.47 ? 383  LEU B N     1 
ATOM   11822 C  CA    . LEU B  1  385  ? 1.469   27.936  86.998  1.00 16.37 ? 383  LEU B CA    1 
ATOM   11823 C  C     . LEU B  1  385  ? 2.143   26.889  86.136  1.00 16.92 ? 383  LEU B C     1 
ATOM   11824 O  O     . LEU B  1  385  ? 2.972   27.217  85.276  1.00 17.97 ? 383  LEU B O     1 
ATOM   11825 C  CB    . LEU B  1  385  ? 2.207   28.030  88.327  1.00 18.85 ? 383  LEU B CB    1 
ATOM   11826 C  CG    . LEU B  1  385  ? 1.960   29.283  89.142  1.00 20.43 ? 383  LEU B CG    1 
ATOM   11827 C  CD1   . LEU B  1  385  ? 2.673   29.120  90.435  1.00 19.12 ? 383  LEU B CD1   1 
ATOM   11828 C  CD2   . LEU B  1  385  ? 2.516   30.465  88.387  1.00 21.38 ? 383  LEU B CD2   1 
ATOM   11829 N  N     . ASP B  1  386  ? 1.811   25.622  86.360  1.00 17.21 ? 384  ASP B N     1 
ATOM   11830 C  CA    . ASP B  1  386  ? 2.519   24.544  85.686  1.00 17.85 ? 384  ASP B CA    1 
ATOM   11831 C  C     . ASP B  1  386  ? 1.905   24.190  84.344  1.00 17.60 ? 384  ASP B C     1 
ATOM   11832 O  O     . ASP B  1  386  ? 2.423   23.305  83.654  1.00 19.41 ? 384  ASP B O     1 
ATOM   11833 C  CB    . ASP B  1  386  ? 2.577   23.311  86.605  1.00 18.97 ? 384  ASP B CB    1 
ATOM   11834 C  CG    . ASP B  1  386  ? 3.512   23.503  87.806  1.00 25.60 ? 384  ASP B CG    1 
ATOM   11835 O  OD1   . ASP B  1  386  ? 4.258   24.511  87.882  1.00 24.08 ? 384  ASP B OD1   1 
ATOM   11836 O  OD2   . ASP B  1  386  ? 3.509   22.616  88.692  1.00 24.61 ? 384  ASP B OD2   1 
ATOM   11837 N  N     . GLY B  1  387  ? 0.827   24.863  83.945  1.00 17.18 ? 385  GLY B N     1 
ATOM   11838 C  CA    . GLY B  1  387  ? 0.237   24.623  82.640  1.00 17.11 ? 385  GLY B CA    1 
ATOM   11839 C  C     . GLY B  1  387  ? -0.268  23.208  82.463  1.00 20.28 ? 385  GLY B C     1 
ATOM   11840 O  O     . GLY B  1  387  ? -0.160  22.647  81.366  1.00 19.89 ? 385  GLY B O     1 
ATOM   11841 N  N     . LEU B  1  388  ? -0.820  22.611  83.516  1.00 17.08 ? 386  LEU B N     1 
ATOM   11842 C  CA    . LEU B  1  388  ? -1.173  21.206  83.414  1.00 19.21 ? 386  LEU B CA    1 
ATOM   11843 C  C     . LEU B  1  388  ? -2.583  21.043  82.857  1.00 20.88 ? 386  LEU B C     1 
ATOM   11844 O  O     . LEU B  1  388  ? -3.331  22.007  82.674  1.00 18.81 ? 386  LEU B O     1 
ATOM   11845 C  CB    . LEU B  1  388  ? -0.998  20.514  84.761  1.00 19.38 ? 386  LEU B CB    1 
ATOM   11846 C  CG    . LEU B  1  388  ? 0.456   20.630  85.209  1.00 19.00 ? 386  LEU B CG    1 
ATOM   11847 C  CD1   . LEU B  1  388  ? 0.686   19.938  86.543  1.00 24.97 ? 386  LEU B CD1   1 
ATOM   11848 C  CD2   . LEU B  1  388  ? 1.439   20.072  84.164  1.00 20.43 ? 386  LEU B CD2   1 
ATOM   11849 N  N     . ALA B  1  389  ? -2.938  19.791  82.554  1.00 19.62 ? 387  ALA B N     1 
ATOM   11850 C  CA    . ALA B  1  389  ? -4.127  19.554  81.748  1.00 21.53 ? 387  ALA B CA    1 
ATOM   11851 C  C     . ALA B  1  389  ? -5.387  20.028  82.455  1.00 20.55 ? 387  ALA B C     1 
ATOM   11852 O  O     . ALA B  1  389  ? -6.321  20.528  81.818  1.00 23.61 ? 387  ALA B O     1 
ATOM   11853 C  CB    . ALA B  1  389  ? -4.238  18.069  81.400  1.00 25.27 ? 387  ALA B CB    1 
ATOM   11854 N  N     . ASP B  1  390  ? -5.425  19.888  83.768  1.00 22.10 ? 388  ASP B N     1 
ATOM   11855 C  CA    . ASP B  1  390  ? -6.598  20.246  84.545  1.00 19.98 ? 388  ASP B CA    1 
ATOM   11856 C  C     . ASP B  1  390  ? -6.135  20.341  85.990  1.00 17.06 ? 388  ASP B C     1 
ATOM   11857 O  O     . ASP B  1  390  ? -4.960  20.132  86.298  1.00 19.51 ? 388  ASP B O     1 
ATOM   11858 C  CB    . ASP B  1  390  ? -7.709  19.208  84.359  1.00 21.00 ? 388  ASP B CB    1 
ATOM   11859 C  CG    . ASP B  1  390  ? -9.103  19.784  84.529  1.00 25.41 ? 388  ASP B CG    1 
ATOM   11860 O  OD1   . ASP B  1  390  ? -9.320  20.558  85.486  1.00 23.30 ? 388  ASP B OD1   1 
ATOM   11861 O  OD2   . ASP B  1  390  ? -9.979  19.455  83.691  1.00 26.12 ? 388  ASP B OD2   1 
ATOM   11862 N  N     . PHE B  1  391  ? -7.058  20.641  86.861  1.00 19.02 ? 389  PHE B N     1 
ATOM   11863 C  CA    . PHE B  1  391  ? -6.760  20.664  88.278  1.00 18.74 ? 389  PHE B CA    1 
ATOM   11864 C  C     . PHE B  1  391  ? -6.830  19.261  88.864  1.00 19.34 ? 389  PHE B C     1 
ATOM   11865 O  O     . PHE B  1  391  ? -7.536  18.395  88.345  1.00 20.08 ? 389  PHE B O     1 
ATOM   11866 C  CB    . PHE B  1  391  ? -7.743  21.581  88.987  1.00 21.12 ? 389  PHE B CB    1 
ATOM   11867 C  CG    . PHE B  1  391  ? -7.727  22.964  88.425  1.00 16.23 ? 389  PHE B CG    1 
ATOM   11868 C  CD1   . PHE B  1  391  ? -6.697  23.836  88.761  1.00 18.30 ? 389  PHE B CD1   1 
ATOM   11869 C  CD2   . PHE B  1  391  ? -8.692  23.370  87.519  1.00 18.09 ? 389  PHE B CD2   1 
ATOM   11870 C  CE1   . PHE B  1  391  ? -6.639  25.102  88.218  1.00 17.06 ? 389  PHE B CE1   1 
ATOM   11871 C  CE2   . PHE B  1  391  ? -8.642  24.653  86.975  1.00 17.81 ? 389  PHE B CE2   1 
ATOM   11872 C  CZ    . PHE B  1  391  ? -7.626  25.513  87.327  1.00 18.03 ? 389  PHE B CZ    1 
ATOM   11873 N  N     . PRO B  1  392  ? -6.088  19.005  89.938  1.00 17.50 ? 390  PRO B N     1 
ATOM   11874 C  CA    . PRO B  1  392  ? -6.232  17.741  90.664  1.00 16.73 ? 390  PRO B CA    1 
ATOM   11875 C  C     . PRO B  1  392  ? -7.315  17.780  91.725  1.00 19.56 ? 390  PRO B C     1 
ATOM   11876 O  O     . PRO B  1  392  ? -7.487  16.801  92.454  1.00 20.19 ? 390  PRO B O     1 
ATOM   11877 C  CB    . PRO B  1  392  ? -4.857  17.604  91.315  1.00 19.20 ? 390  PRO B CB    1 
ATOM   11878 C  CG    . PRO B  1  392  ? -4.533  19.032  91.706  1.00 17.72 ? 390  PRO B CG    1 
ATOM   11879 C  CD    . PRO B  1  392  ? -5.055  19.867  90.542  1.00 16.20 ? 390  PRO B CD    1 
ATOM   11880 N  N     . VAL B  1  393  ? -7.995  18.913  91.836  1.00 17.81 ? 391  VAL B N     1 
ATOM   11881 C  CA    . VAL B  1  393  ? -9.088  19.112  92.771  1.00 19.01 ? 391  VAL B CA    1 
ATOM   11882 C  C     . VAL B  1  393  ? -10.268 19.642  91.971  1.00 18.51 ? 391  VAL B C     1 
ATOM   11883 O  O     . VAL B  1  393  ? -10.113 20.133  90.848  1.00 19.48 ? 391  VAL B O     1 
ATOM   11884 C  CB    . VAL B  1  393  ? -8.704  20.093  93.903  1.00 18.08 ? 391  VAL B CB    1 
ATOM   11885 C  CG1   . VAL B  1  393  ? -7.555  19.522  94.723  1.00 19.94 ? 391  VAL B CG1   1 
ATOM   11886 C  CG2   . VAL B  1  393  ? -8.299  21.436  93.311  1.00 18.46 ? 391  VAL B CG2   1 
ATOM   11887 N  N     . PHE B  1  394  ? -11.454 19.536  92.567  1.00 18.30 ? 392  PHE B N     1 
ATOM   11888 C  CA    . PHE B  1  394  ? -12.635 20.151  91.978  1.00 19.01 ? 392  PHE B CA    1 
ATOM   11889 C  C     . PHE B  1  394  ? -12.538 21.670  92.070  1.00 21.10 ? 392  PHE B C     1 
ATOM   11890 O  O     . PHE B  1  394  ? -11.772 22.225  92.868  1.00 21.75 ? 392  PHE B O     1 
ATOM   11891 C  CB    . PHE B  1  394  ? -13.898 19.631  92.664  1.00 19.94 ? 392  PHE B CB    1 
ATOM   11892 C  CG    . PHE B  1  394  ? -14.040 18.154  92.547  1.00 20.96 ? 392  PHE B CG    1 
ATOM   11893 C  CD1   . PHE B  1  394  ? -14.264 17.581  91.301  1.00 22.32 ? 392  PHE B CD1   1 
ATOM   11894 C  CD2   . PHE B  1  394  ? -13.865 17.330  93.641  1.00 22.62 ? 392  PHE B CD2   1 
ATOM   11895 C  CE1   . PHE B  1  394  ? -14.353 16.215  91.167  1.00 23.21 ? 392  PHE B CE1   1 
ATOM   11896 C  CE2   . PHE B  1  394  ? -13.962 15.956  93.515  1.00 22.76 ? 392  PHE B CE2   1 
ATOM   11897 C  CZ    . PHE B  1  394  ? -14.194 15.402  92.264  1.00 21.47 ? 392  PHE B CZ    1 
ATOM   11898 N  N     . THR B  1  395  ? -13.313 22.346  91.221  1.00 20.73 ? 393  THR B N     1 
ATOM   11899 C  CA    . THR B  1  395  ? -13.324 23.799  91.187  1.00 21.60 ? 393  THR B CA    1 
ATOM   11900 C  C     . THR B  1  395  ? -14.634 24.408  91.661  1.00 20.76 ? 393  THR B C     1 
ATOM   11901 O  O     . THR B  1  395  ? -14.679 25.621  91.869  1.00 23.40 ? 393  THR B O     1 
ATOM   11902 C  CB    . THR B  1  395  ? -13.027 24.335  89.777  1.00 20.36 ? 393  THR B CB    1 
ATOM   11903 O  OG1   . THR B  1  395  ? -14.038 23.900  88.861  1.00 22.08 ? 393  THR B OG1   1 
ATOM   11904 C  CG2   . THR B  1  395  ? -11.644 23.877  89.296  1.00 21.08 ? 393  THR B CG2   1 
ATOM   11905 N  N     . ARG B  1  396  ? -15.690 23.617  91.828  1.00 22.02 ? 394  ARG B N     1 
ATOM   11906 C  CA    . ARG B  1  396  ? -16.904 24.070  92.494  1.00 22.28 ? 394  ARG B CA    1 
ATOM   11907 C  C     . ARG B  1  396  ? -16.993 23.392  93.849  1.00 24.60 ? 394  ARG B C     1 
ATOM   11908 O  O     . ARG B  1  396  ? -16.781 22.180  93.961  1.00 23.84 ? 394  ARG B O     1 
ATOM   11909 C  CB    . ARG B  1  396  ? -18.159 23.772  91.672  1.00 21.65 ? 394  ARG B CB    1 
ATOM   11910 C  CG    . ARG B  1  396  ? -18.196 24.513  90.362  1.00 25.02 ? 394  ARG B CG    1 
ATOM   11911 C  CD    . ARG B  1  396  ? -19.543 24.286  89.684  1.00 26.49 ? 394  ARG B CD    1 
ATOM   11912 N  NE    . ARG B  1  396  ? -19.489 24.747  88.304  1.00 27.37 ? 394  ARG B NE    1 
ATOM   11913 C  CZ    . ARG B  1  396  ? -20.283 25.670  87.781  1.00 33.80 ? 394  ARG B CZ    1 
ATOM   11914 N  NH1   . ARG B  1  396  ? -21.272 26.207  88.476  1.00 38.63 ? 394  ARG B NH1   1 
ATOM   11915 N  NH2   . ARG B  1  396  ? -20.082 26.062  86.524  1.00 32.01 ? 394  ARG B NH2   1 
ATOM   11916 N  N     . LYS B  1  397  ? -17.304 24.178  94.878  1.00 26.73 ? 395  LYS B N     1 
ATOM   11917 C  CA    . LYS B  1  397  ? -17.318 23.635  96.228  1.00 26.43 ? 395  LYS B CA    1 
ATOM   11918 C  C     . LYS B  1  397  ? -18.367 22.536  96.371  1.00 24.66 ? 395  LYS B C     1 
ATOM   11919 O  O     . LYS B  1  397  ? -18.148 21.536  97.063  1.00 27.34 ? 395  LYS B O     1 
ATOM   11920 C  CB    . LYS B  1  397  ? -17.554 24.771  97.219  1.00 27.83 ? 395  LYS B CB    1 
ATOM   11921 C  CG    . LYS B  1  397  ? -17.223 24.425  98.643  1.00 26.69 ? 395  LYS B CG    1 
ATOM   11922 C  CD    . LYS B  1  397  ? -18.447 23.958  99.372  1.00 30.65 ? 395  LYS B CD    1 
ATOM   11923 C  CE    . LYS B  1  397  ? -18.148 23.660  100.828 1.00 29.27 ? 395  LYS B CE    1 
ATOM   11924 N  NZ    . LYS B  1  397  ? -19.371 23.162  101.473 1.00 26.54 ? 395  LYS B NZ    1 
ATOM   11925 N  N     . ILE B  1  398  ? -19.500 22.686  95.685  1.00 26.02 ? 396  ILE B N     1 
ATOM   11926 C  CA    . ILE B  1  398  ? -20.545 21.674  95.740  1.00 28.86 ? 396  ILE B CA    1 
ATOM   11927 C  C     . ILE B  1  398  ? -20.055 20.345  95.172  1.00 22.82 ? 396  ILE B C     1 
ATOM   11928 O  O     . ILE B  1  398  ? -20.526 19.275  95.579  1.00 24.78 ? 396  ILE B O     1 
ATOM   11929 C  CB    . ILE B  1  398  ? -21.795 22.204  95.010  1.00 31.75 ? 396  ILE B CB    1 
ATOM   11930 C  CG1   . ILE B  1  398  ? -23.014 21.387  95.376  1.00 37.52 ? 396  ILE B CG1   1 
ATOM   11931 C  CG2   . ILE B  1  398  ? -21.593 22.209  93.496  1.00 31.36 ? 396  ILE B CG2   1 
ATOM   11932 C  CD1   . ILE B  1  398  ? -24.281 22.065  94.998  1.00 41.10 ? 396  ILE B CD1   1 
ATOM   11933 N  N     . HIS B  1  399  ? -19.073 20.380  94.264  1.00 26.00 ? 397  HIS B N     1 
ATOM   11934 C  CA    . HIS B  1  399  ? -18.528 19.131  93.737  1.00 24.61 ? 397  HIS B CA    1 
ATOM   11935 C  C     . HIS B  1  399  ? -17.746 18.381  94.799  1.00 24.44 ? 397  HIS B C     1 
ATOM   11936 O  O     . HIS B  1  399  ? -17.828 17.150  94.890  1.00 26.38 ? 397  HIS B O     1 
ATOM   11937 C  CB    . HIS B  1  399  ? -17.642 19.412  92.533  1.00 24.48 ? 397  HIS B CB    1 
ATOM   11938 C  CG    . HIS B  1  399  ? -18.397 19.934  91.355  1.00 26.97 ? 397  HIS B CG    1 
ATOM   11939 N  ND1   . HIS B  1  399  ? -17.776 20.473  90.251  1.00 25.93 ? 397  HIS B ND1   1 
ATOM   11940 C  CD2   . HIS B  1  399  ? -19.728 19.995  91.111  1.00 29.19 ? 397  HIS B CD2   1 
ATOM   11941 C  CE1   . HIS B  1  399  ? -18.694 20.850  89.376  1.00 23.88 ? 397  HIS B CE1   1 
ATOM   11942 N  NE2   . HIS B  1  399  ? -19.885 20.572  89.876  1.00 24.24 ? 397  HIS B NE2   1 
ATOM   11943 N  N     . THR B  1  400  ? -16.970 19.109  95.600  1.00 25.16 ? 398  THR B N     1 
ATOM   11944 C  CA    . THR B  1  400  ? -16.276 18.483  96.716  1.00 24.48 ? 398  THR B CA    1 
ATOM   11945 C  C     . THR B  1  400  ? -17.269 17.880  97.697  1.00 21.34 ? 398  THR B C     1 
ATOM   11946 O  O     . THR B  1  400  ? -17.043 16.788  98.228  1.00 25.33 ? 398  THR B O     1 
ATOM   11947 C  CB    . THR B  1  400  ? -15.377 19.512  97.402  1.00 22.27 ? 398  THR B CB    1 
ATOM   11948 O  OG1   . THR B  1  400  ? -14.307 19.865  96.514  1.00 21.35 ? 398  THR B OG1   1 
ATOM   11949 C  CG2   . THR B  1  400  ? -14.782 18.945  98.665  1.00 23.52 ? 398  THR B CG2   1 
ATOM   11950 N  N     . ASP B  1  401  ? -18.392 18.564  97.927  1.00 27.70 ? 399  ASP B N     1 
ATOM   11951 C  CA    . ASP B  1  401  ? -19.400 18.029  98.836  1.00 29.17 ? 399  ASP B CA    1 
ATOM   11952 C  C     . ASP B  1  401  ? -19.998 16.729  98.308  1.00 25.07 ? 399  ASP B C     1 
ATOM   11953 O  O     . ASP B  1  401  ? -20.178 15.771  99.064  1.00 27.65 ? 399  ASP B O     1 
ATOM   11954 C  CB    . ASP B  1  401  ? -20.497 19.068  99.072  1.00 31.67 ? 399  ASP B CB    1 
ATOM   11955 C  CG    . ASP B  1  401  ? -20.014 20.249  99.891  1.00 37.85 ? 399  ASP B CG    1 
ATOM   11956 O  OD1   . ASP B  1  401  ? -18.997 20.110  100.620 1.00 33.66 ? 399  ASP B OD1   1 
ATOM   11957 O  OD2   . ASP B  1  401  ? -20.656 21.316  99.815  1.00 31.85 ? 399  ASP B OD2   1 
ATOM   11958 N  N     . VAL B  1  402  ? -20.321 16.678  97.011  1.00 25.66 ? 400  VAL B N     1 
ATOM   11959 C  CA    . VAL B  1  402  ? -20.824 15.438  96.425  1.00 27.73 ? 400  VAL B CA    1 
ATOM   11960 C  C     . VAL B  1  402  ? -19.760 14.352  96.501  1.00 24.10 ? 400  VAL B C     1 
ATOM   11961 O  O     . VAL B  1  402  ? -20.046 13.203  96.865  1.00 28.71 ? 400  VAL B O     1 
ATOM   11962 C  CB    . VAL B  1  402  ? -21.284 15.678  94.975  1.00 25.10 ? 400  VAL B CB    1 
ATOM   11963 C  CG1   . VAL B  1  402  ? -21.694 14.365  94.310  1.00 32.65 ? 400  VAL B CG1   1 
ATOM   11964 C  CG2   . VAL B  1  402  ? -22.420 16.690  94.948  1.00 36.04 ? 400  VAL B CG2   1 
ATOM   11965 N  N     . SER B  1  403  ? -18.513 14.707  96.165  1.00 24.64 ? 401  SER B N     1 
ATOM   11966 C  CA    . SER B  1  403  ? -17.407 13.754  96.238  1.00 28.04 ? 401  SER B CA    1 
ATOM   11967 C  C     . SER B  1  403  ? -17.282 13.164  97.638  1.00 25.58 ? 401  SER B C     1 
ATOM   11968 O  O     . SER B  1  403  ? -17.130 11.951  97.805  1.00 26.68 ? 401  SER B O     1 
ATOM   11969 C  CB    . SER B  1  403  ? -16.096 14.438  95.829  1.00 23.76 ? 401  SER B CB    1 
ATOM   11970 O  OG    . SER B  1  403  ? -14.988 13.584  96.059  1.00 27.35 ? 401  SER B OG    1 
ATOM   11971 N  N     . TYR B  1  404  ? -17.347 14.022  98.655  1.00 26.03 ? 402  TYR B N     1 
ATOM   11972 C  CA    . TYR B  1  404  ? -17.273 13.568  100.039 1.00 29.08 ? 402  TYR B CA    1 
ATOM   11973 C  C     . TYR B  1  404  ? -18.380 12.567  100.352 1.00 28.11 ? 402  TYR B C     1 
ATOM   11974 O  O     . TYR B  1  404  ? -18.129 11.492  100.909 1.00 27.52 ? 402  TYR B O     1 
ATOM   11975 C  CB    . TYR B  1  404  ? -17.354 14.779  100.969 1.00 23.82 ? 402  TYR B CB    1 
ATOM   11976 C  CG    . TYR B  1  404  ? -16.990 14.497  102.413 1.00 24.34 ? 402  TYR B CG    1 
ATOM   11977 C  CD1   . TYR B  1  404  ? -17.887 13.876  103.265 1.00 28.69 ? 402  TYR B CD1   1 
ATOM   11978 C  CD2   . TYR B  1  404  ? -15.751 14.869  102.917 1.00 26.42 ? 402  TYR B CD2   1 
ATOM   11979 C  CE1   . TYR B  1  404  ? -17.561 13.633  104.584 1.00 28.51 ? 402  TYR B CE1   1 
ATOM   11980 C  CE2   . TYR B  1  404  ? -15.417 14.626  104.231 1.00 26.65 ? 402  TYR B CE2   1 
ATOM   11981 C  CZ    . TYR B  1  404  ? -16.326 14.005  105.058 1.00 30.85 ? 402  TYR B CZ    1 
ATOM   11982 O  OH    . TYR B  1  404  ? -16.023 13.749  106.376 1.00 31.70 ? 402  TYR B OH    1 
ATOM   11983 N  N     . ILE B  1  405  ? -19.615 12.898  99.982  1.00 28.01 ? 403  ILE B N     1 
ATOM   11984 C  CA    . ILE B  1  405  ? -20.739 12.024  100.301 1.00 28.62 ? 403  ILE B CA    1 
ATOM   11985 C  C     . ILE B  1  405  ? -20.627 10.701  99.547  1.00 27.37 ? 403  ILE B C     1 
ATOM   11986 O  O     . ILE B  1  405  ? -20.876 9.626   100.110 1.00 31.06 ? 403  ILE B O     1 
ATOM   11987 C  CB    . ILE B  1  405  ? -22.061 12.761  100.017 1.00 32.30 ? 403  ILE B CB    1 
ATOM   11988 C  CG1   . ILE B  1  405  ? -22.192 13.965  100.956 1.00 36.34 ? 403  ILE B CG1   1 
ATOM   11989 C  CG2   . ILE B  1  405  ? -23.238 11.853  100.212 1.00 31.20 ? 403  ILE B CG2   1 
ATOM   11990 C  CD1   . ILE B  1  405  ? -23.387 14.845  100.687 1.00 40.39 ? 403  ILE B CD1   1 
ATOM   11991 N  N     . ALA B  1  406  ? -20.219 10.754  98.274  1.00 30.37 ? 404  ALA B N     1 
ATOM   11992 C  CA    . ALA B  1  406  ? -19.993 9.531   97.510  1.00 31.89 ? 404  ALA B CA    1 
ATOM   11993 C  C     . ALA B  1  406  ? -18.894 8.677   98.128  1.00 29.01 ? 404  ALA B C     1 
ATOM   11994 O  O     . ALA B  1  406  ? -19.014 7.447   98.197  1.00 32.07 ? 404  ALA B O     1 
ATOM   11995 C  CB    . ALA B  1  406  ? -19.638 9.883   96.063  1.00 30.12 ? 404  ALA B CB    1 
ATOM   11996 N  N     . CYS B  1  407  ? -17.806 9.308   98.573  1.00 29.34 ? 405  CYS B N     1 
ATOM   11997 C  CA    . CYS B  1  407  ? -16.727 8.552   99.192  1.00 30.10 ? 405  CYS B CA    1 
ATOM   11998 C  C     . CYS B  1  407  ? -17.131 8.046   100.569 1.00 26.73 ? 405  CYS B C     1 
ATOM   11999 O  O     . CYS B  1  407  ? -16.687 6.973   100.992 1.00 30.24 ? 405  CYS B O     1 
ATOM   12000 C  CB    . CYS B  1  407  ? -15.473 9.420   99.261  1.00 27.63 ? 405  CYS B CB    1 
ATOM   12001 S  SG    . CYS B  1  407  ? -14.785 9.734   97.604  1.00 33.13 ? 405  CYS B SG    1 
ATOM   12002 N  N     . ALA B  1  408  ? -17.985 8.792   101.267 1.00 27.98 ? 406  ALA B N     1 
ATOM   12003 C  CA    . ALA B  1  408  ? -18.551 8.287   102.510 1.00 29.65 ? 406  ALA B CA    1 
ATOM   12004 C  C     . ALA B  1  408  ? -19.343 7.006   102.269 1.00 32.90 ? 406  ALA B C     1 
ATOM   12005 O  O     . ALA B  1  408  ? -19.252 6.058   103.052 1.00 35.86 ? 406  ALA B O     1 
ATOM   12006 C  CB    . ALA B  1  408  ? -19.430 9.359   103.153 1.00 31.81 ? 406  ALA B CB    1 
ATOM   12007 N  N     . ALA B  1  409  ? -20.092 6.939   101.163 1.00 32.86 ? 407  ALA B N     1 
ATOM   12008 C  CA    . ALA B  1  409  ? -20.862 5.730   100.885 1.00 35.82 ? 407  ALA B CA    1 
ATOM   12009 C  C     . ALA B  1  409  ? -19.944 4.540   100.640 1.00 33.89 ? 407  ALA B C     1 
ATOM   12010 O  O     . ALA B  1  409  ? -20.241 3.417   101.067 1.00 36.34 ? 407  ALA B O     1 
ATOM   12011 C  CB    . ALA B  1  409  ? -21.786 5.955   99.685  1.00 30.92 ? 407  ALA B CB    1 
ATOM   12012 N  N     . LYS B  1  410  ? -18.825 4.768   99.953  1.00 29.29 ? 408  LYS B N     1 
ATOM   12013 C  CA    . LYS B  1  410  ? -17.868 3.698   99.698  1.00 30.22 ? 408  LYS B CA    1 
ATOM   12014 C  C     . LYS B  1  410  ? -17.239 3.200   100.992 1.00 37.73 ? 408  LYS B C     1 
ATOM   12015 O  O     . LYS B  1  410  ? -17.066 1.991   101.182 1.00 36.22 ? 408  LYS B O     1 
ATOM   12016 C  CB    . LYS B  1  410  ? -16.794 4.189   98.730  1.00 33.87 ? 408  LYS B CB    1 
ATOM   12017 C  CG    . LYS B  1  410  ? -15.765 3.146   98.342  1.00 31.28 ? 408  LYS B CG    1 
ATOM   12018 C  CD    . LYS B  1  410  ? -14.628 3.770   97.541  1.00 34.01 ? 408  LYS B CD    1 
ATOM   12019 C  CE    . LYS B  1  410  ? -15.092 4.252   96.170  1.00 34.18 ? 408  LYS B CE    1 
ATOM   12020 N  NZ    . LYS B  1  410  ? -15.506 3.118   95.293  1.00 37.94 ? 408  LYS B NZ    1 
ATOM   12021 N  N     . LEU B  1  411  ? -16.890 4.118   101.895 1.00 35.97 ? 409  LEU B N     1 
ATOM   12022 C  CA    . LEU B  1  411  ? -16.271 3.714   103.154 1.00 33.22 ? 409  LEU B CA    1 
ATOM   12023 C  C     . LEU B  1  411  ? -17.245 2.944   104.028 1.00 36.32 ? 409  LEU B C     1 
ATOM   12024 O  O     . LEU B  1  411  ? -16.870 1.946   104.651 1.00 35.37 ? 409  LEU B O     1 
ATOM   12025 C  CB    . LEU B  1  411  ? -15.751 4.940   103.894 1.00 30.94 ? 409  LEU B CB    1 
ATOM   12026 C  CG    . LEU B  1  411  ? -14.431 5.472   103.352 1.00 33.29 ? 409  LEU B CG    1 
ATOM   12027 C  CD1   . LEU B  1  411  ? -14.208 6.897   103.827 1.00 31.99 ? 409  LEU B CD1   1 
ATOM   12028 C  CD2   . LEU B  1  411  ? -13.281 4.561   103.764 1.00 33.92 ? 409  LEU B CD2   1 
ATOM   12029 N  N     . LEU B  1  412  ? -18.498 3.392   104.087 1.00 35.54 ? 410  LEU B N     1 
ATOM   12030 C  CA    . LEU B  1  412  ? -19.478 2.738   104.946 1.00 37.18 ? 410  LEU B CA    1 
ATOM   12031 C  C     . LEU B  1  412  ? -19.783 1.312   104.509 1.00 41.42 ? 410  LEU B C     1 
ATOM   12032 O  O     . LEU B  1  412  ? -20.359 0.552   105.289 1.00 41.52 ? 410  LEU B O     1 
ATOM   12033 C  CB    . LEU B  1  412  ? -20.761 3.566   104.987 1.00 35.29 ? 410  LEU B CB    1 
ATOM   12034 C  CG    . LEU B  1  412  ? -20.635 4.853   105.800 1.00 41.47 ? 410  LEU B CG    1 
ATOM   12035 C  CD1   . LEU B  1  412  ? -21.772 5.812   105.492 1.00 44.56 ? 410  LEU B CD1   1 
ATOM   12036 C  CD2   . LEU B  1  412  ? -20.609 4.510   107.284 1.00 45.74 ? 410  LEU B CD2   1 
ATOM   12037 N  N     . ALA B  1  413  ? -19.415 0.931   103.291 1.00 38.86 ? 411  ALA B N     1 
ATOM   12038 C  CA    . ALA B  1  413  ? -19.623 -0.430  102.819 1.00 38.57 ? 411  ALA B CA    1 
ATOM   12039 C  C     . ALA B  1  413  ? -18.418 -1.329  103.061 1.00 43.35 ? 411  ALA B C     1 
ATOM   12040 O  O     . ALA B  1  413  ? -18.489 -2.526  102.765 1.00 42.03 ? 411  ALA B O     1 
ATOM   12041 C  CB    . ALA B  1  413  ? -19.966 -0.424  101.324 1.00 38.11 ? 411  ALA B CB    1 
ATOM   12042 N  N     . ALA B  1  414  ? -17.316 -0.789  103.592 1.00 36.21 ? 412  ALA B N     1 
ATOM   12043 C  CA    . ALA B  1  414  ? -16.105 -1.567  103.818 1.00 38.92 ? 412  ALA B CA    1 
ATOM   12044 C  C     . ALA B  1  414  ? -15.649 -1.503  105.275 1.00 39.71 ? 412  ALA B C     1 
ATOM   12045 O  O     . ALA B  1  414  ? -14.460 -1.662  105.557 1.00 38.41 ? 412  ALA B O     1 
ATOM   12046 C  CB    . ALA B  1  414  ? -14.983 -1.102  102.889 1.00 38.35 ? 412  ALA B CB    1 
ATOM   12047 N  N     . THR B  1  415  ? -16.587 -1.306  106.212 1.00 43.67 ? 413  THR B N     1 
ATOM   12048 C  CA    . THR B  1  415  ? -16.219 -1.100  107.614 1.00 39.33 ? 413  THR B CA    1 
ATOM   12049 C  C     . THR B  1  415  ? -15.572 -2.320  108.262 1.00 45.03 ? 413  THR B C     1 
ATOM   12050 O  O     . THR B  1  415  ? -15.000 -2.188  109.348 1.00 39.04 ? 413  THR B O     1 
ATOM   12051 C  CB    . THR B  1  415  ? -17.432 -0.693  108.452 1.00 36.89 ? 413  THR B CB    1 
ATOM   12052 O  OG1   . THR B  1  415  ? -18.476 -1.665  108.301 1.00 42.97 ? 413  THR B OG1   1 
ATOM   12053 C  CG2   . THR B  1  415  ? -17.938 0.674   108.040 1.00 35.27 ? 413  THR B CG2   1 
ATOM   12054 N  N     . ASP B  1  416  ? -15.661 -3.503  107.655 1.00 40.87 ? 414  ASP B N     1 
ATOM   12055 C  CA    . ASP B  1  416  ? -14.885 -4.616  108.185 1.00 33.19 ? 414  ASP B CA    1 
ATOM   12056 C  C     . ASP B  1  416  ? -13.418 -4.494  107.817 1.00 48.93 ? 414  ASP B C     1 
ATOM   12057 O  O     . ASP B  1  416  ? -12.566 -5.062  108.512 1.00 48.87 ? 414  ASP B O     1 
ATOM   12058 C  CB    . ASP B  1  416  ? -15.446 -5.943  107.680 1.00 49.66 ? 414  ASP B CB    1 
ATOM   12059 N  N     . VAL B  1  417  ? -13.112 -3.739  106.759 1.00 39.21 ? 415  VAL B N     1 
ATOM   12060 C  CA    . VAL B  1  417  ? -11.757 -3.581  106.255 1.00 37.36 ? 415  VAL B CA    1 
ATOM   12061 C  C     . VAL B  1  417  ? -11.161 -2.274  106.762 1.00 29.77 ? 415  VAL B C     1 
ATOM   12062 O  O     . VAL B  1  417  ? -9.946  -2.177  106.949 1.00 41.38 ? 415  VAL B O     1 
ATOM   12063 C  CB    . VAL B  1  417  ? -11.732 -3.625  104.711 1.00 37.80 ? 415  VAL B CB    1 
ATOM   12064 N  N     . VAL B  1  418  ? -11.994 -1.245  106.953 1.00 37.40 ? 416  VAL B N     1 
ATOM   12065 C  CA    . VAL B  1  418  ? -11.496 0.090   107.281 1.00 30.72 ? 416  VAL B CA    1 
ATOM   12066 C  C     . VAL B  1  418  ? -12.377 0.742   108.337 1.00 37.99 ? 416  VAL B C     1 
ATOM   12067 O  O     . VAL B  1  418  ? -13.550 0.406   108.502 1.00 36.04 ? 416  VAL B O     1 
ATOM   12068 C  CB    . VAL B  1  418  ? -11.411 1.021   106.048 1.00 34.67 ? 416  VAL B CB    1 
ATOM   12069 C  CG1   . VAL B  1  418  ? -10.419 0.485   105.042 1.00 30.42 ? 416  VAL B CG1   1 
ATOM   12070 C  CG2   . VAL B  1  418  ? -12.788 1.198   105.414 1.00 36.78 ? 416  VAL B CG2   1 
ATOM   12071 N  N     . PHE B  1  419  ? -11.791 1.708   109.046 1.00 33.03 ? 417  PHE B N     1 
ATOM   12072 C  CA    . PHE B  1  419  ? -12.501 2.488   110.054 1.00 30.80 ? 417  PHE B CA    1 
ATOM   12073 C  C     . PHE B  1  419  ? -12.727 3.897   109.523 1.00 34.35 ? 417  PHE B C     1 
ATOM   12074 O  O     . PHE B  1  419  ? -11.814 4.741   109.589 1.00 29.61 ? 417  PHE B O     1 
ATOM   12075 C  CB    . PHE B  1  419  ? -11.702 2.521   111.363 1.00 28.66 ? 417  PHE B CB    1 
ATOM   12076 C  CG    . PHE B  1  419  ? -12.330 3.353   112.444 1.00 34.02 ? 417  PHE B CG    1 
ATOM   12077 C  CD1   . PHE B  1  419  ? -13.595 3.059   112.924 1.00 35.02 ? 417  PHE B CD1   1 
ATOM   12078 C  CD2   . PHE B  1  419  ? -11.635 4.412   113.007 1.00 27.62 ? 417  PHE B CD2   1 
ATOM   12079 C  CE1   . PHE B  1  419  ? -14.169 3.822   113.930 1.00 36.00 ? 417  PHE B CE1   1 
ATOM   12080 C  CE2   . PHE B  1  419  ? -12.200 5.172   114.019 1.00 30.76 ? 417  PHE B CE2   1 
ATOM   12081 C  CZ    . PHE B  1  419  ? -13.468 4.886   114.476 1.00 32.71 ? 417  PHE B CZ    1 
ATOM   12082 N  N     . PRO B  1  420  ? -13.912 4.204   108.990 1.00 31.09 ? 418  PRO B N     1 
ATOM   12083 C  CA    . PRO B  1  420  ? -14.145 5.532   108.409 1.00 32.31 ? 418  PRO B CA    1 
ATOM   12084 C  C     . PRO B  1  420  ? -14.209 6.596   109.491 1.00 33.16 ? 418  PRO B C     1 
ATOM   12085 O  O     . PRO B  1  420  ? -14.857 6.419   110.525 1.00 30.24 ? 418  PRO B O     1 
ATOM   12086 C  CB    . PRO B  1  420  ? -15.492 5.376   107.685 1.00 30.30 ? 418  PRO B CB    1 
ATOM   12087 C  CG    . PRO B  1  420  ? -15.708 3.901   107.564 1.00 32.63 ? 418  PRO B CG    1 
ATOM   12088 C  CD    . PRO B  1  420  ? -15.072 3.319   108.802 1.00 32.39 ? 418  PRO B CD    1 
ATOM   12089 N  N     . GLN B  1  421  ? -13.517 7.705   109.247 1.00 27.60 ? 419  GLN B N     1 
ATOM   12090 C  CA    . GLN B  1  421  ? -13.491 8.835   110.168 1.00 31.68 ? 419  GLN B CA    1 
ATOM   12091 C  C     . GLN B  1  421  ? -13.897 10.062  109.373 1.00 29.76 ? 419  GLN B C     1 
ATOM   12092 O  O     . GLN B  1  421  ? -13.126 10.546  108.540 1.00 26.84 ? 419  GLN B O     1 
ATOM   12093 C  CB    . GLN B  1  421  ? -12.103 9.000   110.784 1.00 26.16 ? 419  GLN B CB    1 
ATOM   12094 C  CG    . GLN B  1  421  ? -11.597 7.723   111.433 1.00 28.26 ? 419  GLN B CG    1 
ATOM   12095 C  CD    . GLN B  1  421  ? -10.105 7.744   111.672 1.00 28.30 ? 419  GLN B CD    1 
ATOM   12096 O  OE1   . GLN B  1  421  ? -9.317  7.800   110.735 1.00 26.12 ? 419  GLN B OE1   1 
ATOM   12097 N  NE2   . GLN B  1  421  ? -9.710  7.681   112.942 1.00 25.54 ? 419  GLN B NE2   1 
ATOM   12098 N  N     . PHE B  1  422  ? -15.101 10.559  109.610 1.00 28.71 ? 420  PHE B N     1 
ATOM   12099 C  CA    . PHE B  1  422  ? -15.672 11.602  108.759 1.00 30.16 ? 420  PHE B CA    1 
ATOM   12100 C  C     . PHE B  1  422  ? -15.375 12.959  109.387 1.00 28.23 ? 420  PHE B C     1 
ATOM   12101 O  O     . PHE B  1  422  ? -16.082 13.411  110.293 1.00 28.41 ? 420  PHE B O     1 
ATOM   12102 C  CB    . PHE B  1  422  ? -17.163 11.363  108.549 1.00 29.36 ? 420  PHE B CB    1 
ATOM   12103 C  CG    . PHE B  1  422  ? -17.470 10.045  107.889 1.00 31.47 ? 420  PHE B CG    1 
ATOM   12104 C  CD1   . PHE B  1  422  ? -17.106 9.817   106.573 1.00 31.79 ? 420  PHE B CD1   1 
ATOM   12105 C  CD2   . PHE B  1  422  ? -18.111 9.034   108.582 1.00 30.69 ? 420  PHE B CD2   1 
ATOM   12106 C  CE1   . PHE B  1  422  ? -17.376 8.607   105.959 1.00 31.77 ? 420  PHE B CE1   1 
ATOM   12107 C  CE2   . PHE B  1  422  ? -18.386 7.817   107.969 1.00 33.76 ? 420  PHE B CE2   1 
ATOM   12108 C  CZ    . PHE B  1  422  ? -18.020 7.611   106.651 1.00 32.22 ? 420  PHE B CZ    1 
ATOM   12109 N  N     . ALA B  1  423  ? -14.310 13.599  108.906 1.00 27.68 ? 421  ALA B N     1 
ATOM   12110 C  CA    . ALA B  1  423  ? -13.879 14.900  109.403 1.00 24.86 ? 421  ALA B CA    1 
ATOM   12111 C  C     . ALA B  1  423  ? -14.608 15.995  108.638 1.00 26.54 ? 421  ALA B C     1 
ATOM   12112 O  O     . ALA B  1  423  ? -14.340 16.218  107.451 1.00 28.84 ? 421  ALA B O     1 
ATOM   12113 C  CB    . ALA B  1  423  ? -12.367 15.059  109.246 1.00 25.65 ? 421  ALA B CB    1 
ATOM   12114 N  N     . THR B  1  424  ? -15.489 16.714  109.322 1.00 30.84 ? 422  THR B N     1 
ATOM   12115 C  CA    . THR B  1  424  ? -16.195 17.816  108.687 1.00 27.18 ? 422  THR B CA    1 
ATOM   12116 C  C     . THR B  1  424  ? -16.856 18.664  109.760 1.00 29.82 ? 422  THR B C     1 
ATOM   12117 O  O     . THR B  1  424  ? -17.272 18.152  110.804 1.00 30.46 ? 422  THR B O     1 
ATOM   12118 C  CB    . THR B  1  424  ? -17.248 17.310  107.684 1.00 30.79 ? 422  THR B CB    1 
ATOM   12119 O  OG1   . THR B  1  424  ? -17.884 18.435  107.072 1.00 28.42 ? 422  THR B OG1   1 
ATOM   12120 C  CG2   . THR B  1  424  ? -18.301 16.433  108.382 1.00 31.41 ? 422  THR B CG2   1 
ATOM   12121 N  N     . HIS B  1  425  ? -16.924 19.966  109.498 1.00 29.14 ? 423  HIS B N     1 
ATOM   12122 C  CA    . HIS B  1  425  ? -17.674 20.903  110.323 1.00 34.64 ? 423  HIS B CA    1 
ATOM   12123 C  C     . HIS B  1  425  ? -19.009 21.264  109.694 1.00 36.28 ? 423  HIS B C     1 
ATOM   12124 O  O     . HIS B  1  425  ? -19.709 22.146  110.199 1.00 36.72 ? 423  HIS B O     1 
ATOM   12125 C  CB    . HIS B  1  425  ? -16.851 22.168  110.562 1.00 26.86 ? 423  HIS B CB    1 
ATOM   12126 C  CG    . HIS B  1  425  ? -15.572 21.917  111.302 1.00 27.72 ? 423  HIS B CG    1 
ATOM   12127 N  ND1   . HIS B  1  425  ? -14.399 22.574  111.004 1.00 34.97 ? 423  HIS B ND1   1 
ATOM   12128 C  CD2   . HIS B  1  425  ? -15.281 21.066  112.314 1.00 31.10 ? 423  HIS B CD2   1 
ATOM   12129 C  CE1   . HIS B  1  425  ? -13.441 22.146  111.807 1.00 36.50 ? 423  HIS B CE1   1 
ATOM   12130 N  NE2   . HIS B  1  425  ? -13.951 21.234  112.614 1.00 30.71 ? 423  HIS B NE2   1 
ATOM   12131 N  N     . ASN B  1  426  ? -19.368 20.599  108.604 1.00 33.25 ? 424  ASN B N     1 
ATOM   12132 C  CA    . ASN B  1  426  ? -20.558 20.920  107.826 1.00 30.71 ? 424  ASN B CA    1 
ATOM   12133 C  C     . ASN B  1  426  ? -21.710 20.038  108.303 1.00 31.84 ? 424  ASN B C     1 
ATOM   12134 O  O     . ASN B  1  426  ? -21.699 18.821  108.091 1.00 31.68 ? 424  ASN B O     1 
ATOM   12135 C  CB    . ASN B  1  426  ? -20.246 20.719  106.344 1.00 30.03 ? 424  ASN B CB    1 
ATOM   12136 C  CG    . ASN B  1  426  ? -21.352 21.198  105.436 1.00 36.69 ? 424  ASN B CG    1 
ATOM   12137 O  OD1   . ASN B  1  426  ? -22.522 20.891  105.655 1.00 34.91 ? 424  ASN B OD1   1 
ATOM   12138 N  ND2   . ASN B  1  426  ? -20.985 21.948  104.395 1.00 35.61 ? 424  ASN B ND2   1 
ATOM   12139 N  N     . ALA B  1  427  ? -22.704 20.655  108.956 1.00 35.79 ? 425  ALA B N     1 
ATOM   12140 C  CA    . ALA B  1  427  ? -23.830 19.903  109.506 1.00 37.34 ? 425  ALA B CA    1 
ATOM   12141 C  C     . ALA B  1  427  ? -24.633 19.192  108.424 1.00 34.87 ? 425  ALA B C     1 
ATOM   12142 O  O     . ALA B  1  427  ? -25.170 18.100  108.667 1.00 34.45 ? 425  ALA B O     1 
ATOM   12143 C  CB    . ALA B  1  427  ? -24.743 20.832  110.307 1.00 41.62 ? 425  ALA B CB    1 
ATOM   12144 N  N     . GLN B  1  428  ? -24.741 19.792  107.237 1.00 37.92 ? 426  GLN B N     1 
ATOM   12145 C  CA    . GLN B  1  428  ? -25.410 19.113  106.134 1.00 37.73 ? 426  GLN B CA    1 
ATOM   12146 C  C     . GLN B  1  428  ? -24.643 17.858  105.736 1.00 35.04 ? 426  GLN B C     1 
ATOM   12147 O  O     . GLN B  1  428  ? -25.226 16.775  105.605 1.00 37.79 ? 426  GLN B O     1 
ATOM   12148 C  CB    . GLN B  1  428  ? -25.569 20.063  104.944 1.00 36.37 ? 426  GLN B CB    1 
ATOM   12149 C  CG    . GLN B  1  428  ? -26.565 19.581  103.883 1.00 36.98 ? 426  GLN B CG    1 
ATOM   12150 C  CD    . GLN B  1  428  ? -26.025 18.441  103.038 1.00 39.17 ? 426  GLN B CD    1 
ATOM   12151 O  OE1   . GLN B  1  428  ? -24.848 18.438  102.657 1.00 40.52 ? 426  GLN B OE1   1 
ATOM   12152 N  NE2   . GLN B  1  428  ? -26.875 17.459  102.752 1.00 41.97 ? 426  GLN B NE2   1 
ATOM   12153 N  N     . THR B  1  429  ? -23.323 17.986  105.545 1.00 36.00 ? 427  THR B N     1 
ATOM   12154 C  CA    . THR B  1  429  ? -22.496 16.813  105.271 1.00 37.93 ? 427  THR B CA    1 
ATOM   12155 C  C     . THR B  1  429  ? -22.652 15.767  106.367 1.00 34.88 ? 427  THR B C     1 
ATOM   12156 O  O     . THR B  1  429  ? -22.853 14.581  106.084 1.00 33.08 ? 427  THR B O     1 
ATOM   12157 C  CB    . THR B  1  429  ? -21.025 17.214  105.139 1.00 32.31 ? 427  THR B CB    1 
ATOM   12158 O  OG1   . THR B  1  429  ? -20.902 18.299  104.221 1.00 33.17 ? 427  THR B OG1   1 
ATOM   12159 C  CG2   . THR B  1  429  ? -20.209 16.044  104.639 1.00 36.30 ? 427  THR B CG2   1 
ATOM   12160 N  N     . LEU B  1  430  ? -22.541 16.195  107.630 1.00 36.60 ? 428  LEU B N     1 
ATOM   12161 C  CA    . LEU B  1  430  ? -22.659 15.276  108.758 1.00 31.93 ? 428  LEU B CA    1 
ATOM   12162 C  C     . LEU B  1  430  ? -23.989 14.531  108.729 1.00 33.23 ? 428  LEU B C     1 
ATOM   12163 O  O     . LEU B  1  430  ? -24.029 13.302  108.855 1.00 34.72 ? 428  LEU B O     1 
ATOM   12164 C  CB    . LEU B  1  430  ? -22.506 16.056  110.067 1.00 38.77 ? 428  LEU B CB    1 
ATOM   12165 C  CG    . LEU B  1  430  ? -22.313 15.393  111.440 1.00 34.29 ? 428  LEU B CG    1 
ATOM   12166 C  CD1   . LEU B  1  430  ? -22.022 16.481  112.450 1.00 34.59 ? 428  LEU B CD1   1 
ATOM   12167 C  CD2   . LEU B  1  430  ? -23.507 14.573  111.906 1.00 38.94 ? 428  LEU B CD2   1 
ATOM   12168 N  N     . ALA B  1  431  ? -25.090 15.264  108.565 1.00 38.93 ? 429  ALA B N     1 
ATOM   12169 C  CA    . ALA B  1  431  ? -26.411 14.641  108.587 1.00 38.62 ? 429  ALA B CA    1 
ATOM   12170 C  C     . ALA B  1  431  ? -26.554 13.595  107.487 1.00 39.10 ? 429  ALA B C     1 
ATOM   12171 O  O     . ALA B  1  431  ? -27.112 12.514  107.716 1.00 41.19 ? 429  ALA B O     1 
ATOM   12172 C  CB    . ALA B  1  431  ? -27.489 15.712  108.453 1.00 37.59 ? 429  ALA B CB    1 
ATOM   12173 N  N     . ALA B  1  432  ? -26.042 13.894  106.288 1.00 38.64 ? 430  ALA B N     1 
ATOM   12174 C  CA    . ALA B  1  432  ? -26.157 12.959  105.175 1.00 32.88 ? 430  ALA B CA    1 
ATOM   12175 C  C     . ALA B  1  432  ? -25.479 11.635  105.497 1.00 37.43 ? 430  ALA B C     1 
ATOM   12176 O  O     . ALA B  1  432  ? -26.024 10.563  105.209 1.00 39.24 ? 430  ALA B O     1 
ATOM   12177 C  CB    . ALA B  1  432  ? -25.557 13.577  103.907 1.00 34.46 ? 430  ALA B CB    1 
ATOM   12178 N  N     . ILE B  1  433  ? -24.292 11.689  106.107 1.00 37.32 ? 431  ILE B N     1 
ATOM   12179 C  CA    . ILE B  1  433  ? -23.573 10.463  106.439 1.00 37.30 ? 431  ILE B CA    1 
ATOM   12180 C  C     . ILE B  1  433  ? -24.208 9.777   107.639 1.00 33.31 ? 431  ILE B C     1 
ATOM   12181 O  O     . ILE B  1  433  ? -24.265 8.545   107.709 1.00 39.33 ? 431  ILE B O     1 
ATOM   12182 C  CB    . ILE B  1  433  ? -22.092 10.777  106.697 1.00 35.96 ? 431  ILE B CB    1 
ATOM   12183 C  CG1   . ILE B  1  433  ? -21.489 11.455  105.474 1.00 40.88 ? 431  ILE B CG1   1 
ATOM   12184 C  CG2   . ILE B  1  433  ? -21.323 9.509   107.037 1.00 39.20 ? 431  ILE B CG2   1 
ATOM   12185 C  CD1   . ILE B  1  433  ? -20.076 11.816  105.674 1.00 38.57 ? 431  ILE B CD1   1 
ATOM   12186 N  N     . TYR B  1  434  ? -24.665 10.561  108.610 1.00 38.17 ? 432  TYR B N     1 
ATOM   12187 C  CA    . TYR B  1  434  ? -25.294 9.981   109.789 1.00 36.44 ? 432  TYR B CA    1 
ATOM   12188 C  C     . TYR B  1  434  ? -26.461 9.079   109.397 1.00 39.89 ? 432  TYR B C     1 
ATOM   12189 O  O     . TYR B  1  434  ? -26.605 7.970   109.923 1.00 44.31 ? 432  TYR B O     1 
ATOM   12190 C  CB    . TYR B  1  434  ? -25.733 11.108  110.727 1.00 39.74 ? 432  TYR B CB    1 
ATOM   12191 C  CG    . TYR B  1  434  ? -26.661 10.686  111.834 1.00 40.46 ? 432  TYR B CG    1 
ATOM   12192 C  CD1   . TYR B  1  434  ? -26.225 9.851   112.856 1.00 43.84 ? 432  TYR B CD1   1 
ATOM   12193 C  CD2   . TYR B  1  434  ? -27.974 11.134  111.862 1.00 42.87 ? 432  TYR B CD2   1 
ATOM   12194 C  CE1   . TYR B  1  434  ? -27.082 9.467   113.877 1.00 51.18 ? 432  TYR B CE1   1 
ATOM   12195 C  CE2   . TYR B  1  434  ? -28.835 10.761  112.874 1.00 43.40 ? 432  TYR B CE2   1 
ATOM   12196 C  CZ    . TYR B  1  434  ? -28.387 9.927   113.877 1.00 51.91 ? 432  TYR B CZ    1 
ATOM   12197 O  OH    . TYR B  1  434  ? -29.253 9.559   114.881 1.00 51.49 ? 432  TYR B OH    1 
ATOM   12198 N  N     . HIS B  1  435  ? -27.262 9.507   108.426 1.00 42.30 ? 433  HIS B N     1 
ATOM   12199 C  CA    . HIS B  1  435  ? -28.395 8.697   107.999 1.00 45.91 ? 433  HIS B CA    1 
ATOM   12200 C  C     . HIS B  1  435  ? -27.997 7.629   106.988 1.00 43.11 ? 433  HIS B C     1 
ATOM   12201 O  O     . HIS B  1  435  ? -28.559 6.528   107.002 1.00 42.38 ? 433  HIS B O     1 
ATOM   12202 C  CB    . HIS B  1  435  ? -29.485 9.608   107.445 1.00 46.95 ? 433  HIS B CB    1 
ATOM   12203 C  CG    . HIS B  1  435  ? -30.226 10.350  108.511 1.00 46.80 ? 433  HIS B CG    1 
ATOM   12204 N  ND1   . HIS B  1  435  ? -31.219 9.764   109.264 1.00 42.31 ? 433  HIS B ND1   1 
ATOM   12205 C  CD2   . HIS B  1  435  ? -30.101 11.616  108.973 1.00 42.39 ? 433  HIS B CD2   1 
ATOM   12206 C  CE1   . HIS B  1  435  ? -31.684 10.640  110.135 1.00 47.84 ? 433  HIS B CE1   1 
ATOM   12207 N  NE2   . HIS B  1  435  ? -31.026 11.773  109.978 1.00 40.86 ? 433  HIS B NE2   1 
ATOM   12208 N  N     . MET B  1  436  ? -27.021 7.920   106.129 1.00 39.59 ? 434  MET B N     1 
ATOM   12209 C  CA    . MET B  1  436  ? -26.507 6.910   105.215 1.00 39.77 ? 434  MET B CA    1 
ATOM   12210 C  C     . MET B  1  436  ? -25.957 5.697   105.957 1.00 44.31 ? 434  MET B C     1 
ATOM   12211 O  O     . MET B  1  436  ? -26.023 4.573   105.446 1.00 43.70 ? 434  MET B O     1 
ATOM   12212 C  CB    . MET B  1  436  ? -25.428 7.542   104.336 1.00 41.14 ? 434  MET B CB    1 
ATOM   12213 C  CG    . MET B  1  436  ? -24.687 6.593   103.429 1.00 41.87 ? 434  MET B CG    1 
ATOM   12214 S  SD    . MET B  1  436  ? -23.365 7.500   102.595 1.00 48.04 ? 434  MET B SD    1 
ATOM   12215 C  CE    . MET B  1  436  ? -24.337 8.723   101.722 1.00 41.66 ? 434  MET B CE    1 
ATOM   12216 N  N     . ALA B  1  437  ? -25.421 5.898   107.165 1.00 39.83 ? 435  ALA B N     1 
ATOM   12217 C  CA    . ALA B  1  437  ? -24.780 4.804   107.886 1.00 42.46 ? 435  ALA B CA    1 
ATOM   12218 C  C     . ALA B  1  437  ? -25.778 3.797   108.445 1.00 45.22 ? 435  ALA B C     1 
ATOM   12219 O  O     . ALA B  1  437  ? -25.403 2.648   108.705 1.00 44.56 ? 435  ALA B O     1 
ATOM   12220 C  CB    . ALA B  1  437  ? -23.921 5.365   109.015 1.00 44.70 ? 435  ALA B CB    1 
ATOM   12221 N  N     . GLY B  1  438  ? -27.026 4.191   108.636 1.00 43.87 ? 436  GLY B N     1 
ATOM   12222 C  CA    . GLY B  1  438  ? -28.019 3.276   109.162 1.00 46.57 ? 436  GLY B CA    1 
ATOM   12223 C  C     . GLY B  1  438  ? -28.066 3.290   110.675 1.00 48.98 ? 436  GLY B C     1 
ATOM   12224 O  O     . GLY B  1  438  ? -27.510 4.164   111.347 1.00 47.77 ? 436  GLY B O     1 
ATOM   12225 N  N     . LYS B  1  439  ? -28.748 2.279   111.222 1.00 51.11 ? 437  LYS B N     1 
ATOM   12226 C  CA    . LYS B  1  439  ? -28.981 2.197   112.659 1.00 39.44 ? 437  LYS B CA    1 
ATOM   12227 C  C     . LYS B  1  439  ? -28.069 1.212   113.382 1.00 51.45 ? 437  LYS B C     1 
ATOM   12228 O  O     . LYS B  1  439  ? -27.969 1.279   114.612 1.00 54.66 ? 437  LYS B O     1 
ATOM   12229 C  CB    . LYS B  1  439  ? -30.442 1.804   112.933 1.00 47.83 ? 437  LYS B CB    1 
ATOM   12230 N  N     . ASP B  1  440  ? -27.429 0.288   112.671 1.00 48.88 ? 438  ASP B N     1 
ATOM   12231 C  CA    . ASP B  1  440  ? -26.543 -0.680  113.316 1.00 56.72 ? 438  ASP B CA    1 
ATOM   12232 C  C     . ASP B  1  440  ? -25.216 0.012   113.585 1.00 56.95 ? 438  ASP B C     1 
ATOM   12233 O  O     . ASP B  1  440  ? -24.389 0.163   112.681 1.00 59.62 ? 438  ASP B O     1 
ATOM   12234 C  CB    . ASP B  1  440  ? -26.360 -1.917  112.443 1.00 57.90 ? 438  ASP B CB    1 
ATOM   12235 N  N     . PHE B  1  441  ? -25.010 0.453   114.828 1.00 48.02 ? 439  PHE B N     1 
ATOM   12236 C  CA    . PHE B  1  441  ? -23.797 1.178   115.193 1.00 50.94 ? 439  PHE B CA    1 
ATOM   12237 C  C     . PHE B  1  441  ? -23.197 0.629   116.479 1.00 56.08 ? 439  PHE B C     1 
ATOM   12238 O  O     . PHE B  1  441  ? -23.893 0.481   117.490 1.00 49.11 ? 439  PHE B O     1 
ATOM   12239 C  CB    . PHE B  1  441  ? -24.047 2.683   115.361 1.00 45.98 ? 439  PHE B CB    1 
ATOM   12240 C  CG    . PHE B  1  441  ? -22.786 3.468   115.620 1.00 50.06 ? 439  PHE B CG    1 
ATOM   12241 C  CD1   . PHE B  1  441  ? -22.030 3.956   114.565 1.00 44.79 ? 439  PHE B CD1   1 
ATOM   12242 C  CD2   . PHE B  1  441  ? -22.342 3.695   116.915 1.00 41.48 ? 439  PHE B CD2   1 
ATOM   12243 C  CE1   . PHE B  1  441  ? -20.863 4.663   114.796 1.00 43.99 ? 439  PHE B CE1   1 
ATOM   12244 C  CE2   . PHE B  1  441  ? -21.173 4.399   117.152 1.00 45.97 ? 439  PHE B CE2   1 
ATOM   12245 C  CZ    . PHE B  1  441  ? -20.435 4.881   116.092 1.00 46.84 ? 439  PHE B CZ    1 
ATOM   12246 N  N     . HIS B  1  442  ? -21.898 0.347   116.427 1.00 48.22 ? 440  HIS B N     1 
ATOM   12247 C  CA    . HIS B  1  442  ? -21.065 0.102   117.593 1.00 46.81 ? 440  HIS B CA    1 
ATOM   12248 C  C     . HIS B  1  442  ? -19.875 1.050   117.517 1.00 45.54 ? 440  HIS B C     1 
ATOM   12249 O  O     . HIS B  1  442  ? -19.406 1.371   116.421 1.00 45.65 ? 440  HIS B O     1 
ATOM   12250 C  CB    . HIS B  1  442  ? -20.587 -1.359  117.638 1.00 51.76 ? 440  HIS B CB    1 
ATOM   12251 C  CG    . HIS B  1  442  ? -19.887 -1.810  116.390 1.00 62.87 ? 440  HIS B CG    1 
ATOM   12252 N  ND1   . HIS B  1  442  ? -18.514 -1.909  116.298 1.00 57.83 ? 440  HIS B ND1   1 
ATOM   12253 C  CD2   . HIS B  1  442  ? -20.371 -2.191  115.182 1.00 55.31 ? 440  HIS B CD2   1 
ATOM   12254 C  CE1   . HIS B  1  442  ? -18.183 -2.331  115.090 1.00 62.60 ? 440  HIS B CE1   1 
ATOM   12255 N  NE2   . HIS B  1  442  ? -19.292 -2.511  114.394 1.00 68.59 ? 440  HIS B NE2   1 
ATOM   12256 N  N     . VAL B  1  443  ? -19.405 1.532   118.670 1.00 43.07 ? 441  VAL B N     1 
ATOM   12257 C  CA    . VAL B  1  443  ? -18.153 2.280   118.664 1.00 37.64 ? 441  VAL B CA    1 
ATOM   12258 C  C     . VAL B  1  443  ? -17.087 1.388   118.053 1.00 45.33 ? 441  VAL B C     1 
ATOM   12259 O  O     . VAL B  1  443  ? -16.983 0.201   118.382 1.00 43.83 ? 441  VAL B O     1 
ATOM   12260 C  CB    . VAL B  1  443  ? -17.783 2.757   120.076 1.00 43.43 ? 441  VAL B CB    1 
ATOM   12261 C  CG1   . VAL B  1  443  ? -16.316 3.170   120.127 1.00 38.17 ? 441  VAL B CG1   1 
ATOM   12262 C  CG2   . VAL B  1  443  ? -18.660 3.938   120.471 1.00 45.73 ? 441  VAL B CG2   1 
ATOM   12263 N  N     . GLY B  1  444  ? -16.335 1.937   117.106 1.00 42.31 ? 442  GLY B N     1 
ATOM   12264 C  CA    . GLY B  1  444  ? -15.457 1.145   116.278 1.00 33.23 ? 442  GLY B CA    1 
ATOM   12265 C  C     . GLY B  1  444  ? -15.968 0.925   114.867 1.00 40.21 ? 442  GLY B C     1 
ATOM   12266 O  O     . GLY B  1  444  ? -15.198 0.479   114.012 1.00 39.47 ? 442  GLY B O     1 
ATOM   12267 N  N     . LYS B  1  445  ? -17.245 1.215   114.609 1.00 41.28 ? 443  LYS B N     1 
ATOM   12268 C  CA    . LYS B  1  445  ? -17.800 1.099   113.264 1.00 39.67 ? 443  LYS B CA    1 
ATOM   12269 C  C     . LYS B  1  445  ? -17.318 2.250   112.392 1.00 39.27 ? 443  LYS B C     1 
ATOM   12270 O  O     . LYS B  1  445  ? -16.681 2.042   111.356 1.00 39.68 ? 443  LYS B O     1 
ATOM   12271 C  CB    . LYS B  1  445  ? -19.329 1.072   113.331 1.00 43.69 ? 443  LYS B CB    1 
ATOM   12272 C  CG    . LYS B  1  445  ? -20.033 1.169   111.987 1.00 44.78 ? 443  LYS B CG    1 
ATOM   12273 C  CD    . LYS B  1  445  ? -20.740 -0.124  111.631 1.00 50.23 ? 443  LYS B CD    1 
ATOM   12274 C  CE    . LYS B  1  445  ? -21.757 0.113   110.531 1.00 57.90 ? 443  LYS B CE    1 
ATOM   12275 N  NZ    . LYS B  1  445  ? -22.739 1.166   110.928 1.00 65.35 ? 443  LYS B NZ    1 
ATOM   12276 N  N     . TYR B  1  446  ? -17.624 3.474   112.809 1.00 37.50 ? 444  TYR B N     1 
ATOM   12277 C  CA    . TYR B  1  446  ? -17.090 4.680   112.196 1.00 35.75 ? 444  TYR B CA    1 
ATOM   12278 C  C     . TYR B  1  446  ? -17.115 5.762   113.263 1.00 39.19 ? 444  TYR B C     1 
ATOM   12279 O  O     . TYR B  1  446  ? -17.686 5.580   114.342 1.00 36.27 ? 444  TYR B O     1 
ATOM   12280 C  CB    . TYR B  1  446  ? -17.889 5.089   110.947 1.00 31.38 ? 444  TYR B CB    1 
ATOM   12281 C  CG    . TYR B  1  446  ? -19.286 5.595   111.225 1.00 40.13 ? 444  TYR B CG    1 
ATOM   12282 C  CD1   . TYR B  1  446  ? -19.523 6.939   111.486 1.00 37.43 ? 444  TYR B CD1   1 
ATOM   12283 C  CD2   . TYR B  1  446  ? -20.373 4.728   111.206 1.00 39.53 ? 444  TYR B CD2   1 
ATOM   12284 C  CE1   . TYR B  1  446  ? -20.794 7.401   111.737 1.00 43.18 ? 444  TYR B CE1   1 
ATOM   12285 C  CE2   . TYR B  1  446  ? -21.645 5.180   111.460 1.00 42.16 ? 444  TYR B CE2   1 
ATOM   12286 C  CZ    . TYR B  1  446  ? -21.853 6.520   111.717 1.00 41.85 ? 444  TYR B CZ    1 
ATOM   12287 O  OH    . TYR B  1  446  ? -23.131 6.969   111.964 1.00 50.32 ? 444  TYR B OH    1 
ATOM   12288 N  N     . GLU B  1  447  ? -16.490 6.892   112.964 1.00 35.24 ? 445  GLU B N     1 
ATOM   12289 C  CA    . GLU B  1  447  ? -16.555 8.031   113.863 1.00 34.53 ? 445  GLU B CA    1 
ATOM   12290 C  C     . GLU B  1  447  ? -16.598 9.307   113.042 1.00 30.48 ? 445  GLU B C     1 
ATOM   12291 O  O     . GLU B  1  447  ? -16.335 9.313   111.835 1.00 32.19 ? 445  GLU B O     1 
ATOM   12292 C  CB    . GLU B  1  447  ? -15.370 8.047   114.841 1.00 27.92 ? 445  GLU B CB    1 
ATOM   12293 C  CG    . GLU B  1  447  ? -14.039 8.353   114.150 1.00 27.02 ? 445  GLU B CG    1 
ATOM   12294 C  CD    . GLU B  1  447  ? -12.882 8.365   115.133 1.00 30.34 ? 445  GLU B CD    1 
ATOM   12295 O  OE1   . GLU B  1  447  ? -13.091 7.977   116.302 1.00 31.28 ? 445  GLU B OE1   1 
ATOM   12296 O  OE2   . GLU B  1  447  ? -11.770 8.769   114.728 1.00 31.25 ? 445  GLU B OE2   1 
ATOM   12297 N  N     . PHE B  1  448  ? -16.961 10.395  113.699 1.00 31.42 ? 446  PHE B N     1 
ATOM   12298 C  CA    . PHE B  1  448  ? -16.764 11.717  113.130 1.00 29.62 ? 446  PHE B CA    1 
ATOM   12299 C  C     . PHE B  1  448  ? -15.503 12.340  113.716 1.00 26.60 ? 446  PHE B C     1 
ATOM   12300 O  O     . PHE B  1  448  ? -14.943 11.859  114.705 1.00 29.33 ? 446  PHE B O     1 
ATOM   12301 C  CB    . PHE B  1  448  ? -17.972 12.606  113.397 1.00 37.00 ? 446  PHE B CB    1 
ATOM   12302 C  CG    . PHE B  1  448  ? -19.214 12.155  112.702 1.00 36.85 ? 446  PHE B CG    1 
ATOM   12303 C  CD1   . PHE B  1  448  ? -19.472 12.549  111.394 1.00 36.79 ? 446  PHE B CD1   1 
ATOM   12304 C  CD2   . PHE B  1  448  ? -20.126 11.336  113.352 1.00 36.85 ? 446  PHE B CD2   1 
ATOM   12305 C  CE1   . PHE B  1  448  ? -20.620 12.132  110.747 1.00 33.26 ? 446  PHE B CE1   1 
ATOM   12306 C  CE2   . PHE B  1  448  ? -21.279 10.914  112.710 1.00 38.72 ? 446  PHE B CE2   1 
ATOM   12307 C  CZ    . PHE B  1  448  ? -21.525 11.317  111.403 1.00 34.89 ? 446  PHE B CZ    1 
ATOM   12308 N  N     . GLN B  1  449  ? -15.045 13.411  113.074 1.00 29.82 ? 447  GLN B N     1 
ATOM   12309 C  CA    . GLN B  1  449  ? -13.874 14.135  113.543 1.00 29.37 ? 447  GLN B CA    1 
ATOM   12310 C  C     . GLN B  1  449  ? -14.083 15.624  113.331 1.00 29.53 ? 447  GLN B C     1 
ATOM   12311 O  O     . GLN B  1  449  ? -14.826 16.050  112.442 1.00 29.17 ? 447  GLN B O     1 
ATOM   12312 C  CB    . GLN B  1  449  ? -12.589 13.679  112.843 1.00 25.56 ? 447  GLN B CB    1 
ATOM   12313 C  CG    . GLN B  1  449  ? -12.263 12.210  113.033 1.00 30.72 ? 447  GLN B CG    1 
ATOM   12314 C  CD    . GLN B  1  449  ? -10.796 11.924  112.813 1.00 24.74 ? 447  GLN B CD    1 
ATOM   12315 O  OE1   . GLN B  1  449  ? -10.072 12.759  112.271 1.00 30.41 ? 447  GLN B OE1   1 
ATOM   12316 N  NE2   . GLN B  1  449  ? -10.344 10.754  113.253 1.00 26.94 ? 447  GLN B NE2   1 
ATOM   12317 N  N     . CYS B  1  450  ? -13.432 16.415  114.175 1.00 26.75 ? 448  CYS B N     1 
ATOM   12318 C  CA    . CYS B  1  450  ? -13.528 17.857  114.064 1.00 26.49 ? 448  CYS B CA    1 
ATOM   12319 C  C     . CYS B  1  450  ? -12.240 18.471  114.583 1.00 25.70 ? 448  CYS B C     1 
ATOM   12320 O  O     . CYS B  1  450  ? -11.409 17.802  115.200 1.00 26.67 ? 448  CYS B O     1 
ATOM   12321 C  CB    . CYS B  1  450  ? -14.738 18.400  114.833 1.00 28.39 ? 448  CYS B CB    1 
ATOM   12322 S  SG    . CYS B  1  450  ? -14.534 18.408  116.635 1.00 30.75 ? 448  CYS B SG    1 
ATOM   12323 N  N     . LEU B  1  451  ? -12.094 19.759  114.325 1.00 27.05 ? 449  LEU B N     1 
ATOM   12324 C  CA    . LEU B  1  451  ? -10.941 20.522  114.776 1.00 28.33 ? 449  LEU B CA    1 
ATOM   12325 C  C     . LEU B  1  451  ? -11.210 21.096  116.161 1.00 29.47 ? 449  LEU B C     1 
ATOM   12326 O  O     . LEU B  1  451  ? -12.305 21.588  116.438 1.00 30.73 ? 449  LEU B O     1 
ATOM   12327 C  CB    . LEU B  1  451  ? -10.647 21.648  113.791 1.00 29.86 ? 449  LEU B CB    1 
ATOM   12328 C  CG    . LEU B  1  451  ? -9.404  22.496  114.000 1.00 38.36 ? 449  LEU B CG    1 
ATOM   12329 C  CD1   . LEU B  1  451  ? -8.155  21.635  113.893 1.00 37.98 ? 449  LEU B CD1   1 
ATOM   12330 C  CD2   . LEU B  1  451  ? -9.382  23.611  112.968 1.00 37.25 ? 449  LEU B CD2   1 
ATOM   12331 N  N     . HIS B  1  452  ? -10.207 21.010  117.034 1.00 26.50 ? 450  HIS B N     1 
ATOM   12332 C  CA    . HIS B  1  452  ? -10.298 21.629  118.347 1.00 35.51 ? 450  HIS B CA    1 
ATOM   12333 C  C     . HIS B  1  452  ? -10.689 23.097  118.232 1.00 26.47 ? 450  HIS B C     1 
ATOM   12334 O  O     . HIS B  1  452  ? -10.176 23.825  117.380 1.00 28.41 ? 450  HIS B O     1 
ATOM   12335 C  CB    . HIS B  1  452  ? -8.958  21.509  119.072 1.00 28.11 ? 450  HIS B CB    1 
ATOM   12336 C  CG    . HIS B  1  452  ? -8.866  22.370  120.291 1.00 30.85 ? 450  HIS B CG    1 
ATOM   12337 N  ND1   . HIS B  1  452  ? -9.342  21.969  121.521 1.00 31.29 ? 450  HIS B ND1   1 
ATOM   12338 C  CD2   . HIS B  1  452  ? -8.387  23.625  120.461 1.00 28.33 ? 450  HIS B CD2   1 
ATOM   12339 C  CE1   . HIS B  1  452  ? -9.149  22.936  122.400 1.00 33.35 ? 450  HIS B CE1   1 
ATOM   12340 N  NE2   . HIS B  1  452  ? -8.574  23.952  121.782 1.00 32.19 ? 450  HIS B NE2   1 
ATOM   12341 N  N     . GLY B  1  453  ? -11.605 23.526  119.099 1.00 33.00 ? 451  GLY B N     1 
ATOM   12342 C  CA    . GLY B  1  453  ? -11.969 24.931  119.160 1.00 38.55 ? 451  GLY B CA    1 
ATOM   12343 C  C     . GLY B  1  453  ? -12.653 25.456  117.923 1.00 49.46 ? 451  GLY B C     1 
ATOM   12344 O  O     . GLY B  1  453  ? -12.632 26.663  117.671 1.00 55.95 ? 451  GLY B O     1 
ATOM   12345 N  N     . MET B  1  454  ? -13.243 24.572  117.127 1.00 40.13 ? 452  MET B N     1 
ATOM   12346 C  CA    . MET B  1  454  ? -13.997 24.966  115.947 1.00 35.32 ? 452  MET B CA    1 
ATOM   12347 C  C     . MET B  1  454  ? -15.180 24.026  115.803 1.00 40.22 ? 452  MET B C     1 
ATOM   12348 O  O     . MET B  1  454  ? -16.312 24.459  115.567 1.00 42.38 ? 452  MET B O     1 
ATOM   12349 C  CB    . MET B  1  454  ? -13.116 24.925  114.695 1.00 31.91 ? 452  MET B CB    1 
ATOM   12350 C  CG    . MET B  1  454  ? -13.871 25.182  113.401 1.00 39.15 ? 452  MET B CG    1 
ATOM   12351 S  SD    . MET B  1  454  ? -14.505 26.862  113.354 1.00 57.78 ? 452  MET B SD    1 
ATOM   12352 C  CE    . MET B  1  454  ? -13.010 27.781  113.742 1.00 44.01 ? 452  MET B CE    1 
ATOM   12353 N  N     . GLY B  1  455  ? -14.919 22.731  115.964 1.00 34.84 ? 453  GLY B N     1 
ATOM   12354 C  CA    . GLY B  1  455  ? -15.923 21.706  115.777 1.00 29.88 ? 453  GLY B CA    1 
ATOM   12355 C  C     . GLY B  1  455  ? -16.747 21.346  116.984 1.00 39.36 ? 453  GLY B C     1 
ATOM   12356 O  O     . GLY B  1  455  ? -17.743 20.632  116.838 1.00 39.05 ? 453  GLY B O     1 
ATOM   12357 N  N     . GLU B  1  456  ? -16.359 21.808  118.175 1.00 45.79 ? 454  GLU B N     1 
ATOM   12358 C  CA    . GLU B  1  456  ? -17.099 21.435  119.380 1.00 45.31 ? 454  GLU B CA    1 
ATOM   12359 C  C     . GLU B  1  456  ? -18.547 21.916  119.383 1.00 37.26 ? 454  GLU B C     1 
ATOM   12360 O  O     . GLU B  1  456  ? -19.422 21.121  119.766 1.00 42.06 ? 454  GLU B O     1 
ATOM   12361 C  CB    . GLU B  1  456  ? -16.370 21.938  120.633 1.00 47.49 ? 454  GLU B CB    1 
ATOM   12362 C  CG    . GLU B  1  456  ? -15.097 21.184  120.960 1.00 53.59 ? 454  GLU B CG    1 
ATOM   12363 C  CD    . GLU B  1  456  ? -13.879 21.824  120.341 1.00 49.65 ? 454  GLU B CD    1 
ATOM   12364 O  OE1   . GLU B  1  456  ? -14.023 22.455  119.271 1.00 49.37 ? 454  GLU B OE1   1 
ATOM   12365 O  OE2   . GLU B  1  456  ? -12.782 21.710  120.931 1.00 36.67 ? 454  GLU B OE2   1 
ATOM   12366 N  N     . PRO B  1  457  ? -18.873 23.161  119.005 1.00 37.17 ? 455  PRO B N     1 
ATOM   12367 C  CA    . PRO B  1  457  ? -20.295 23.551  118.985 1.00 43.55 ? 455  PRO B CA    1 
ATOM   12368 C  C     . PRO B  1  457  ? -21.179 22.615  118.175 1.00 42.82 ? 455  PRO B C     1 
ATOM   12369 O  O     . PRO B  1  457  ? -22.305 22.323  118.595 1.00 48.83 ? 455  PRO B O     1 
ATOM   12370 C  CB    . PRO B  1  457  ? -20.255 24.960  118.382 1.00 41.71 ? 455  PRO B CB    1 
ATOM   12371 C  CG    . PRO B  1  457  ? -18.937 25.494  118.798 1.00 44.47 ? 455  PRO B CG    1 
ATOM   12372 C  CD    . PRO B  1  457  ? -17.998 24.317  118.739 1.00 43.48 ? 455  PRO B CD    1 
ATOM   12373 N  N     . LEU B  1  458  ? -20.698 22.118  117.035 1.00 44.73 ? 456  LEU B N     1 
ATOM   12374 C  CA    . LEU B  1  458  ? -21.499 21.181  116.254 1.00 39.03 ? 456  LEU B CA    1 
ATOM   12375 C  C     . LEU B  1  458  ? -21.540 19.813  116.916 1.00 37.88 ? 456  LEU B C     1 
ATOM   12376 O  O     . LEU B  1  458  ? -22.615 19.234  117.106 1.00 38.89 ? 456  LEU B O     1 
ATOM   12377 C  CB    . LEU B  1  458  ? -20.948 21.078  114.826 1.00 36.23 ? 456  LEU B CB    1 
ATOM   12378 C  CG    . LEU B  1  458  ? -21.552 20.039  113.878 1.00 40.22 ? 456  LEU B CG    1 
ATOM   12379 C  CD1   . LEU B  1  458  ? -23.066 20.179  113.788 1.00 39.15 ? 456  LEU B CD1   1 
ATOM   12380 C  CD2   . LEU B  1  458  ? -20.931 20.153  112.490 1.00 36.43 ? 456  LEU B CD2   1 
ATOM   12381 N  N     . TYR B  1  459  ? -20.380 19.284  117.299 1.00 36.54 ? 457  TYR B N     1 
ATOM   12382 C  CA    . TYR B  1  459  ? -20.347 17.905  117.758 1.00 35.41 ? 457  TYR B CA    1 
ATOM   12383 C  C     . TYR B  1  459  ? -20.807 17.738  119.198 1.00 36.00 ? 457  TYR B C     1 
ATOM   12384 O  O     . TYR B  1  459  ? -21.058 16.602  119.618 1.00 36.96 ? 457  TYR B O     1 
ATOM   12385 C  CB    . TYR B  1  459  ? -18.950 17.334  117.537 1.00 34.90 ? 457  TYR B CB    1 
ATOM   12386 C  CG    . TYR B  1  459  ? -18.791 16.977  116.085 1.00 32.72 ? 457  TYR B CG    1 
ATOM   12387 C  CD1   . TYR B  1  459  ? -19.319 15.794  115.597 1.00 34.21 ? 457  TYR B CD1   1 
ATOM   12388 C  CD2   . TYR B  1  459  ? -18.174 17.843  115.194 1.00 35.64 ? 457  TYR B CD2   1 
ATOM   12389 C  CE1   . TYR B  1  459  ? -19.219 15.465  114.270 1.00 34.80 ? 457  TYR B CE1   1 
ATOM   12390 C  CE2   . TYR B  1  459  ? -18.060 17.512  113.847 1.00 33.61 ? 457  TYR B CE2   1 
ATOM   12391 C  CZ    . TYR B  1  459  ? -18.579 16.311  113.403 1.00 30.31 ? 457  TYR B CZ    1 
ATOM   12392 O  OH    . TYR B  1  459  ? -18.485 15.953  112.070 1.00 30.50 ? 457  TYR B OH    1 
ATOM   12393 N  N     . GLU B  1  460  ? -20.953 18.833  119.944 1.00 35.73 ? 458  GLU B N     1 
ATOM   12394 C  CA    . GLU B  1  460  ? -21.739 18.778  121.172 1.00 49.40 ? 458  GLU B CA    1 
ATOM   12395 C  C     . GLU B  1  460  ? -23.117 18.186  120.912 1.00 49.45 ? 458  GLU B C     1 
ATOM   12396 O  O     . GLU B  1  460  ? -23.701 17.547  121.798 1.00 47.01 ? 458  GLU B O     1 
ATOM   12397 C  CB    . GLU B  1  460  ? -21.888 20.177  121.768 1.00 46.52 ? 458  GLU B CB    1 
ATOM   12398 C  CG    . GLU B  1  460  ? -20.752 20.617  122.650 1.00 52.41 ? 458  GLU B CG    1 
ATOM   12399 C  CD    . GLU B  1  460  ? -20.808 22.102  122.934 1.00 63.80 ? 458  GLU B CD    1 
ATOM   12400 O  OE1   . GLU B  1  460  ? -21.876 22.710  122.699 1.00 64.12 ? 458  GLU B OE1   1 
ATOM   12401 O  OE2   . GLU B  1  460  ? -19.784 22.665  123.374 1.00 72.37 ? 458  GLU B OE2   1 
ATOM   12402 N  N     . GLU B  1  461  ? -23.641 18.384  119.700 1.00 45.77 ? 459  GLU B N     1 
ATOM   12403 C  CA    . GLU B  1  461  ? -24.957 17.930  119.278 1.00 46.40 ? 459  GLU B CA    1 
ATOM   12404 C  C     . GLU B  1  461  ? -24.929 16.558  118.620 1.00 51.03 ? 459  GLU B C     1 
ATOM   12405 O  O     . GLU B  1  461  ? -25.947 16.131  118.066 1.00 47.40 ? 459  GLU B O     1 
ATOM   12406 C  CB    . GLU B  1  461  ? -25.569 18.948  118.314 1.00 46.08 ? 459  GLU B CB    1 
ATOM   12407 C  CG    . GLU B  1  461  ? -25.472 20.382  118.806 1.00 40.56 ? 459  GLU B CG    1 
ATOM   12408 C  CD    . GLU B  1  461  ? -26.190 20.572  120.133 1.00 51.66 ? 459  GLU B CD    1 
ATOM   12409 O  OE1   . GLU B  1  461  ? -27.148 19.817  120.398 1.00 54.18 ? 459  GLU B OE1   1 
ATOM   12410 O  OE2   . GLU B  1  461  ? -25.796 21.465  120.911 1.00 50.93 ? 459  GLU B OE2   1 
ATOM   12411 N  N     . VAL B  1  462  ? -23.794 15.865  118.672 1.00 38.90 ? 460  VAL B N     1 
ATOM   12412 C  CA    . VAL B  1  462  ? -23.632 14.565  118.032 1.00 45.50 ? 460  VAL B CA    1 
ATOM   12413 C  C     . VAL B  1  462  ? -23.174 13.570  119.085 1.00 49.84 ? 460  VAL B C     1 
ATOM   12414 O  O     . VAL B  1  462  ? -23.573 12.400  119.077 1.00 46.16 ? 460  VAL B O     1 
ATOM   12415 C  CB    . VAL B  1  462  ? -22.624 14.639  116.870 1.00 37.45 ? 460  VAL B CB    1 
ATOM   12416 C  CG1   . VAL B  1  462  ? -22.434 13.270  116.242 1.00 39.84 ? 460  VAL B CG1   1 
ATOM   12417 C  CG2   . VAL B  1  462  ? -23.077 15.660  115.837 1.00 36.32 ? 460  VAL B CG2   1 
ATOM   12418 N  N     . VAL B  1  463  ? -22.321 14.025  119.985 1.00 42.38 ? 461  VAL B N     1 
ATOM   12419 C  CA    . VAL B  1  463  ? -21.807 13.183  121.049 1.00 36.29 ? 461  VAL B CA    1 
ATOM   12420 C  C     . VAL B  1  463  ? -22.780 13.245  122.220 1.00 40.15 ? 461  VAL B C     1 
ATOM   12421 O  O     . VAL B  1  463  ? -23.247 14.330  122.598 1.00 47.44 ? 461  VAL B O     1 
ATOM   12422 C  CB    . VAL B  1  463  ? -20.395 13.621  121.463 1.00 35.67 ? 461  VAL B CB    1 
ATOM   12423 C  CG1   . VAL B  1  463  ? -19.855 12.708  122.548 1.00 41.27 ? 461  VAL B CG1   1 
ATOM   12424 C  CG2   . VAL B  1  463  ? -19.464 13.630  120.228 1.00 33.28 ? 461  VAL B CG2   1 
ATOM   12425 N  N     . GLY B  1  464  ? -23.104 12.089  122.772 1.00 46.77 ? 462  GLY B N     1 
ATOM   12426 C  CA    . GLY B  1  464  ? -23.981 12.007  123.931 1.00 41.94 ? 462  GLY B CA    1 
ATOM   12427 C  C     . GLY B  1  464  ? -25.293 11.336  123.583 1.00 53.23 ? 462  GLY B C     1 
ATOM   12428 O  O     . GLY B  1  464  ? -25.804 11.477  122.468 1.00 51.40 ? 462  GLY B O     1 
ATOM   12429 N  N     . ARG B  1  465  ? -25.849 10.596  124.547 1.00 54.02 ? 463  ARG B N     1 
ATOM   12430 C  CA    . ARG B  1  465  ? -27.132 9.943   124.321 1.00 48.41 ? 463  ARG B CA    1 
ATOM   12431 C  C     . ARG B  1  465  ? -28.245 10.957  124.082 1.00 56.05 ? 463  ARG B C     1 
ATOM   12432 O  O     . ARG B  1  465  ? -29.218 10.657  123.377 1.00 61.20 ? 463  ARG B O     1 
ATOM   12433 C  CB    . ARG B  1  465  ? -27.478 9.040   125.507 1.00 60.83 ? 463  ARG B CB    1 
ATOM   12434 N  N     . GLY B  1  466  ? -28.120 12.159  124.646 1.00 51.21 ? 464  GLY B N     1 
ATOM   12435 C  CA    . GLY B  1  466  ? -29.086 13.222  124.438 1.00 52.84 ? 464  GLY B CA    1 
ATOM   12436 C  C     . GLY B  1  466  ? -29.072 13.842  123.061 1.00 56.48 ? 464  GLY B C     1 
ATOM   12437 O  O     . GLY B  1  466  ? -29.807 14.805  122.821 1.00 55.67 ? 464  GLY B O     1 
ATOM   12438 N  N     . LYS B  1  467  ? -28.239 13.326  122.158 1.00 59.18 ? 465  LYS B N     1 
ATOM   12439 C  CA    . LYS B  1  467  ? -28.159 13.799  120.783 1.00 59.05 ? 465  LYS B CA    1 
ATOM   12440 C  C     . LYS B  1  467  ? -28.230 12.615  119.830 1.00 58.84 ? 465  LYS B C     1 
ATOM   12441 O  O     . LYS B  1  467  ? -28.962 11.651  120.078 1.00 57.19 ? 465  LYS B O     1 
ATOM   12442 C  CB    . LYS B  1  467  ? -26.856 14.565  120.554 1.00 60.03 ? 465  LYS B CB    1 
ATOM   12443 C  CG    . LYS B  1  467  ? -26.410 15.446  121.704 1.00 54.91 ? 465  LYS B CG    1 
ATOM   12444 C  CD    . LYS B  1  467  ? -27.300 16.661  121.848 1.00 57.73 ? 465  LYS B CD    1 
ATOM   12445 C  CE    . LYS B  1  467  ? -26.808 17.560  122.967 1.00 59.77 ? 465  LYS B CE    1 
ATOM   12446 N  NZ    . LYS B  1  467  ? -27.619 18.803  123.083 1.00 62.94 ? 465  LYS B NZ    1 
ATOM   12447 N  N     . LEU B  1  468  ? -27.474 12.681  118.738 1.00 54.97 ? 466  LEU B N     1 
ATOM   12448 C  CA    . LEU B  1  468  ? -27.104 11.466  118.033 1.00 39.01 ? 466  LEU B CA    1 
ATOM   12449 C  C     . LEU B  1  468  ? -26.162 10.684  118.930 1.00 44.46 ? 466  LEU B C     1 
ATOM   12450 O  O     . LEU B  1  468  ? -25.612 11.220  119.888 1.00 50.49 ? 466  LEU B O     1 
ATOM   12451 C  CB    . LEU B  1  468  ? -26.439 11.808  116.699 1.00 43.89 ? 466  LEU B CB    1 
ATOM   12452 C  CG    . LEU B  1  468  ? -27.039 13.043  116.023 1.00 50.07 ? 466  LEU B CG    1 
ATOM   12453 C  CD1   . LEU B  1  468  ? -26.282 13.402  114.752 1.00 50.06 ? 466  LEU B CD1   1 
ATOM   12454 C  CD2   . LEU B  1  468  ? -28.531 12.832  115.734 1.00 50.94 ? 466  LEU B CD2   1 
ATOM   12455 N  N     . ASP B  1  469  ? -25.992 9.401   118.664 1.00 49.92 ? 467  ASP B N     1 
ATOM   12456 C  CA    . ASP B  1  469  ? -25.078 8.732   119.584 1.00 51.02 ? 467  ASP B CA    1 
ATOM   12457 C  C     . ASP B  1  469  ? -23.816 8.325   118.852 1.00 41.05 ? 467  ASP B C     1 
ATOM   12458 O  O     . ASP B  1  469  ? -23.518 7.134   118.716 1.00 41.13 ? 467  ASP B O     1 
ATOM   12459 C  CB    . ASP B  1  469  ? -25.736 7.530   120.270 1.00 53.28 ? 467  ASP B CB    1 
ATOM   12460 C  CG    . ASP B  1  469  ? -25.082 7.219   121.607 1.00 61.04 ? 467  ASP B CG    1 
ATOM   12461 O  OD1   . ASP B  1  469  ? -25.026 8.130   122.458 1.00 64.27 ? 467  ASP B OD1   1 
ATOM   12462 O  OD2   . ASP B  1  469  ? -24.622 6.074   121.797 1.00 68.07 ? 467  ASP B OD2   1 
ATOM   12463 N  N     . ARG B  1  470  ? -23.064 9.324   118.392 1.00 44.35 ? 468  ARG B N     1 
ATOM   12464 C  CA    . ARG B  1  470  ? -21.959 9.118   117.478 1.00 46.17 ? 468  ARG B CA    1 
ATOM   12465 C  C     . ARG B  1  470  ? -20.705 9.763   118.053 1.00 35.89 ? 468  ARG B C     1 
ATOM   12466 O  O     . ARG B  1  470  ? -20.748 10.929  118.490 1.00 37.40 ? 468  ARG B O     1 
ATOM   12467 C  CB    . ARG B  1  470  ? -22.287 9.705   116.097 1.00 43.80 ? 468  ARG B CB    1 
ATOM   12468 C  CG    . ARG B  1  470  ? -23.519 9.083   115.460 1.00 38.71 ? 468  ARG B CG    1 
ATOM   12469 C  CD    . ARG B  1  470  ? -23.348 7.577   115.384 1.00 38.06 ? 468  ARG B CD    1 
ATOM   12470 N  NE    . ARG B  1  470  ? -24.489 6.901   114.777 1.00 41.63 ? 468  ARG B NE    1 
ATOM   12471 C  CZ    . ARG B  1  470  ? -25.351 6.147   115.445 1.00 49.65 ? 468  ARG B CZ    1 
ATOM   12472 N  NH1   . ARG B  1  470  ? -25.234 5.954   116.747 1.00 50.91 ? 468  ARG B NH1   1 
ATOM   12473 N  NH2   . ARG B  1  470  ? -26.351 5.564   114.788 1.00 47.88 ? 468  ARG B NH2   1 
ATOM   12474 N  N     . PRO B  1  471  ? -19.584 9.058   118.066 1.00 37.68 ? 469  PRO B N     1 
ATOM   12475 C  CA    . PRO B  1  471  ? -18.359 9.622   118.632 1.00 32.10 ? 469  PRO B CA    1 
ATOM   12476 C  C     . PRO B  1  471  ? -17.727 10.626  117.682 1.00 38.99 ? 469  PRO B C     1 
ATOM   12477 O  O     . PRO B  1  471  ? -17.956 10.619  116.470 1.00 33.76 ? 469  PRO B O     1 
ATOM   12478 C  CB    . PRO B  1  471  ? -17.464 8.394   118.809 1.00 36.37 ? 469  PRO B CB    1 
ATOM   12479 C  CG    . PRO B  1  471  ? -17.893 7.500   117.716 1.00 39.51 ? 469  PRO B CG    1 
ATOM   12480 C  CD    . PRO B  1  471  ? -19.381 7.681   117.592 1.00 40.10 ? 469  PRO B CD    1 
ATOM   12481 N  N     . CYS B  1  472  ? -16.933 11.514  118.264 1.00 34.33 ? 470  CYS B N     1 
ATOM   12482 C  CA    . CYS B  1  472  ? -16.177 12.490  117.501 1.00 31.33 ? 470  CYS B CA    1 
ATOM   12483 C  C     . CYS B  1  472  ? -14.756 12.531  118.037 1.00 35.28 ? 470  CYS B C     1 
ATOM   12484 O  O     . CYS B  1  472  ? -14.549 12.645  119.252 1.00 32.84 ? 470  CYS B O     1 
ATOM   12485 C  CB    . CYS B  1  472  ? -16.809 13.879  117.574 1.00 34.83 ? 470  CYS B CB    1 
ATOM   12486 S  SG    . CYS B  1  472  ? -15.945 15.082  116.555 1.00 35.41 ? 470  CYS B SG    1 
ATOM   12487 N  N     . ARG B  1  473  ? -13.786 12.429  117.136 1.00 32.80 ? 471  ARG B N     1 
ATOM   12488 C  CA    . ARG B  1  473  ? -12.385 12.598  117.489 1.00 30.97 ? 471  ARG B CA    1 
ATOM   12489 C  C     . ARG B  1  473  ? -11.971 14.030  117.200 1.00 32.82 ? 471  ARG B C     1 
ATOM   12490 O  O     . ARG B  1  473  ? -12.162 14.528  116.085 1.00 30.33 ? 471  ARG B O     1 
ATOM   12491 C  CB    . ARG B  1  473  ? -11.487 11.629  116.723 1.00 25.73 ? 471  ARG B CB    1 
ATOM   12492 C  CG    . ARG B  1  473  ? -10.023 11.678  117.192 1.00 29.33 ? 471  ARG B CG    1 
ATOM   12493 C  CD    . ARG B  1  473  ? -9.220  10.538  116.606 1.00 24.59 ? 471  ARG B CD    1 
ATOM   12494 N  NE    . ARG B  1  473  ? -9.924  9.267   116.741 1.00 28.31 ? 471  ARG B NE    1 
ATOM   12495 C  CZ    . ARG B  1  473  ? -9.812  8.445   117.776 1.00 29.59 ? 471  ARG B CZ    1 
ATOM   12496 N  NH1   . ARG B  1  473  ? -9.008  8.715   118.795 1.00 29.28 ? 471  ARG B NH1   1 
ATOM   12497 N  NH2   . ARG B  1  473  ? -10.526 7.324   117.793 1.00 31.20 ? 471  ARG B NH2   1 
ATOM   12498 N  N     . ILE B  1  474  ? -11.405 14.685  118.202 1.00 31.00 ? 472  ILE B N     1 
ATOM   12499 C  CA    . ILE B  1  474  ? -10.977 16.072  118.081 1.00 26.84 ? 472  ILE B CA    1 
ATOM   12500 C  C     . ILE B  1  474  ? -9.518  16.095  117.638 1.00 29.03 ? 472  ILE B C     1 
ATOM   12501 O  O     . ILE B  1  474  ? -8.650  15.520  118.305 1.00 28.60 ? 472  ILE B O     1 
ATOM   12502 C  CB    . ILE B  1  474  ? -11.162 16.818  119.412 1.00 29.39 ? 472  ILE B CB    1 
ATOM   12503 C  CG1   . ILE B  1  474  ? -12.634 16.804  119.832 1.00 33.03 ? 472  ILE B CG1   1 
ATOM   12504 C  CG2   . ILE B  1  474  ? -10.671 18.232  119.294 1.00 30.86 ? 472  ILE B CG2   1 
ATOM   12505 C  CD1   . ILE B  1  474  ? -12.855 17.264  121.272 1.00 30.65 ? 472  ILE B CD1   1 
ATOM   12506 N  N     . TYR B  1  475  ? -9.263  16.729  116.497 1.00 25.30 ? 473  TYR B N     1 
ATOM   12507 C  CA    . TYR B  1  475  ? -7.912  17.002  116.011 1.00 24.08 ? 473  TYR B CA    1 
ATOM   12508 C  C     . TYR B  1  475  ? -7.375  18.175  116.812 1.00 26.70 ? 473  TYR B C     1 
ATOM   12509 O  O     . TYR B  1  475  ? -7.882  19.294  116.701 1.00 28.49 ? 473  TYR B O     1 
ATOM   12510 C  CB    . TYR B  1  475  ? -7.958  17.304  114.519 1.00 25.24 ? 473  TYR B CB    1 
ATOM   12511 C  CG    . TYR B  1  475  ? -6.645  17.454  113.782 1.00 25.98 ? 473  TYR B CG    1 
ATOM   12512 C  CD1   . TYR B  1  475  ? -6.019  16.358  113.206 1.00 27.66 ? 473  TYR B CD1   1 
ATOM   12513 C  CD2   . TYR B  1  475  ? -6.055  18.699  113.632 1.00 35.87 ? 473  TYR B CD2   1 
ATOM   12514 C  CE1   . TYR B  1  475  ? -4.827  16.501  112.492 1.00 23.63 ? 473  TYR B CE1   1 
ATOM   12515 C  CE2   . TYR B  1  475  ? -4.865  18.850  112.934 1.00 38.16 ? 473  TYR B CE2   1 
ATOM   12516 C  CZ    . TYR B  1  475  ? -4.258  17.744  112.369 1.00 35.55 ? 473  TYR B CZ    1 
ATOM   12517 O  OH    . TYR B  1  475  ? -3.076  17.891  111.672 1.00 33.64 ? 473  TYR B OH    1 
ATOM   12518 N  N     . ALA B  1  476  ? -6.378  17.911  117.650 1.00 23.81 ? 474  ALA B N     1 
ATOM   12519 C  CA    . ALA B  1  476  ? -5.989  18.832  118.709 1.00 28.89 ? 474  ALA B CA    1 
ATOM   12520 C  C     . ALA B  1  476  ? -4.586  19.353  118.452 1.00 26.58 ? 474  ALA B C     1 
ATOM   12521 O  O     . ALA B  1  476  ? -3.603  18.628  118.685 1.00 25.80 ? 474  ALA B O     1 
ATOM   12522 C  CB    . ALA B  1  476  ? -6.060  18.125  120.064 1.00 27.35 ? 474  ALA B CB    1 
ATOM   12523 N  N     . PRO B  1  477  ? -4.433  20.579  117.958 1.00 26.68 ? 475  PRO B N     1 
ATOM   12524 C  CA    . PRO B  1  477  ? -3.090  21.125  117.773 1.00 25.24 ? 475  PRO B CA    1 
ATOM   12525 C  C     . PRO B  1  477  ? -2.413  21.340  119.107 1.00 25.72 ? 475  PRO B C     1 
ATOM   12526 O  O     . PRO B  1  477  ? -3.043  21.716  120.098 1.00 28.28 ? 475  PRO B O     1 
ATOM   12527 C  CB    . PRO B  1  477  ? -3.338  22.455  117.061 1.00 23.35 ? 475  PRO B CB    1 
ATOM   12528 C  CG    . PRO B  1  477  ? -4.692  22.325  116.462 1.00 30.07 ? 475  PRO B CG    1 
ATOM   12529 C  CD    . PRO B  1  477  ? -5.464  21.477  117.410 1.00 26.62 ? 475  PRO B CD    1 
ATOM   12530 N  N     . VAL B  1  478  ? -1.109  21.105  119.122 1.00 23.08 ? 476  VAL B N     1 
ATOM   12531 C  CA    . VAL B  1  478  ? -0.311  21.259  120.324 1.00 21.59 ? 476  VAL B CA    1 
ATOM   12532 C  C     . VAL B  1  478  ? 0.961   21.986  119.933 1.00 24.51 ? 476  VAL B C     1 
ATOM   12533 O  O     . VAL B  1  478  ? 1.705   21.513  119.069 1.00 30.00 ? 476  VAL B O     1 
ATOM   12534 C  CB    . VAL B  1  478  ? 0.033   19.910  120.973 1.00 23.82 ? 476  VAL B CB    1 
ATOM   12535 C  CG1   . VAL B  1  478  ? 0.855   20.140  122.229 1.00 28.46 ? 476  VAL B CG1   1 
ATOM   12536 C  CG2   . VAL B  1  478  ? -1.236  19.129  121.272 1.00 25.74 ? 476  VAL B CG2   1 
ATOM   12537 N  N     . GLY B  1  479  ? 1.217   23.126  120.557 1.00 28.13 ? 477  GLY B N     1 
ATOM   12538 C  CA    . GLY B  1  479  ? 2.431   23.844  120.242 1.00 32.77 ? 477  GLY B CA    1 
ATOM   12539 C  C     . GLY B  1  479  ? 2.404   25.253  120.787 1.00 33.91 ? 477  GLY B C     1 
ATOM   12540 O  O     . GLY B  1  479  ? 1.399   25.731  121.327 1.00 32.85 ? 477  GLY B O     1 
ATOM   12541 N  N     . THR B  1  480  ? 3.542   25.910  120.613 1.00 36.22 ? 478  THR B N     1 
ATOM   12542 C  CA    . THR B  1  480  ? 3.768   27.260  121.089 1.00 42.04 ? 478  THR B CA    1 
ATOM   12543 C  C     . THR B  1  480  ? 3.049   28.265  120.198 1.00 41.20 ? 478  THR B C     1 
ATOM   12544 O  O     . THR B  1  480  ? 2.490   27.924  119.152 1.00 41.80 ? 478  THR B O     1 
ATOM   12545 C  CB    . THR B  1  480  ? 5.262   27.563  121.109 1.00 38.39 ? 478  THR B CB    1 
ATOM   12546 O  OG1   . THR B  1  480  ? 5.763   27.504  119.766 1.00 48.29 ? 478  THR B OG1   1 
ATOM   12547 C  CG2   . THR B  1  480  ? 5.993   26.544  121.956 1.00 38.15 ? 478  THR B CG2   1 
ATOM   12548 N  N     . HIS B  1  481  ? 3.081   29.530  120.626 1.00 45.42 ? 479  HIS B N     1 
ATOM   12549 C  CA    . HIS B  1  481  ? 2.499   30.601  119.824 1.00 41.12 ? 479  HIS B CA    1 
ATOM   12550 C  C     . HIS B  1  481  ? 3.169   30.691  118.460 1.00 47.32 ? 479  HIS B C     1 
ATOM   12551 O  O     . HIS B  1  481  ? 2.493   30.812  117.432 1.00 42.13 ? 479  HIS B O     1 
ATOM   12552 C  CB    . HIS B  1  481  ? 2.609   31.932  120.564 1.00 37.66 ? 479  HIS B CB    1 
ATOM   12553 C  CG    . HIS B  1  481  ? 1.820   31.980  121.835 1.00 47.52 ? 479  HIS B CG    1 
ATOM   12554 N  ND1   . HIS B  1  481  ? 1.825   33.074  122.674 1.00 54.11 ? 479  HIS B ND1   1 
ATOM   12555 C  CD2   . HIS B  1  481  ? 0.999   31.069  122.409 1.00 42.71 ? 479  HIS B CD2   1 
ATOM   12556 C  CE1   . HIS B  1  481  ? 1.042   32.834  123.712 1.00 54.23 ? 479  HIS B CE1   1 
ATOM   12557 N  NE2   . HIS B  1  481  ? 0.527   31.624  123.574 1.00 53.38 ? 479  HIS B NE2   1 
ATOM   12558 N  N     . GLU B  1  482  ? 4.502   30.634  118.430 1.00 45.33 ? 480  GLU B N     1 
ATOM   12559 C  CA    . GLU B  1  482  ? 5.213   30.706  117.159 1.00 40.72 ? 480  GLU B CA    1 
ATOM   12560 C  C     . GLU B  1  482  ? 4.839   29.534  116.263 1.00 39.44 ? 480  GLU B C     1 
ATOM   12561 O  O     . GLU B  1  482  ? 4.539   29.715  115.077 1.00 48.53 ? 480  GLU B O     1 
ATOM   12562 C  CB    . GLU B  1  482  ? 6.723   30.747  117.401 1.00 47.92 ? 480  GLU B CB    1 
ATOM   12563 N  N     . THR B  1  483  ? 4.830   28.322  116.821 1.00 45.29 ? 481  THR B N     1 
ATOM   12564 C  CA    . THR B  1  483  ? 4.488   27.147  116.023 1.00 51.74 ? 481  THR B CA    1 
ATOM   12565 C  C     . THR B  1  483  ? 3.072   27.244  115.461 1.00 49.14 ? 481  THR B C     1 
ATOM   12566 O  O     . THR B  1  483  ? 2.837   26.911  114.292 1.00 45.17 ? 481  THR B O     1 
ATOM   12567 C  CB    . THR B  1  483  ? 4.649   25.874  116.859 1.00 50.12 ? 481  THR B CB    1 
ATOM   12568 N  N     . LEU B  1  484  ? 2.112   27.710  116.268 1.00 46.45 ? 482  LEU B N     1 
ATOM   12569 C  CA    . LEU B  1  484  ? 0.724   27.707  115.809 1.00 47.67 ? 482  LEU B CA    1 
ATOM   12570 C  C     . LEU B  1  484  ? 0.479   28.789  114.760 1.00 43.53 ? 482  LEU B C     1 
ATOM   12571 O  O     . LEU B  1  484  ? -0.244  28.562  113.783 1.00 41.57 ? 482  LEU B O     1 
ATOM   12572 C  CB    . LEU B  1  484  ? -0.236  27.857  116.997 1.00 40.90 ? 482  LEU B CB    1 
ATOM   12573 C  CG    . LEU B  1  484  ? -0.540  29.214  117.642 1.00 44.01 ? 482  LEU B CG    1 
ATOM   12574 C  CD1   . LEU B  1  484  ? -1.690  29.934  116.944 1.00 44.94 ? 482  LEU B CD1   1 
ATOM   12575 C  CD2   . LEU B  1  484  ? -0.847  29.035  119.116 1.00 44.74 ? 482  LEU B CD2   1 
ATOM   12576 N  N     . LEU B  1  485  ? 1.075   29.969  114.937 1.00 40.67 ? 483  LEU B N     1 
ATOM   12577 C  CA    . LEU B  1  485  ? 0.834   31.059  113.999 1.00 47.70 ? 483  LEU B CA    1 
ATOM   12578 C  C     . LEU B  1  485  ? 1.363   30.754  112.603 1.00 44.76 ? 483  LEU B C     1 
ATOM   12579 O  O     . LEU B  1  485  ? 0.921   31.384  111.635 1.00 44.74 ? 483  LEU B O     1 
ATOM   12580 C  CB    . LEU B  1  485  ? 1.464   32.352  114.525 1.00 49.50 ? 483  LEU B CB    1 
ATOM   12581 C  CG    . LEU B  1  485  ? 0.701   33.078  115.635 1.00 45.48 ? 483  LEU B CG    1 
ATOM   12582 C  CD1   . LEU B  1  485  ? 1.527   34.223  116.202 1.00 43.75 ? 483  LEU B CD1   1 
ATOM   12583 C  CD2   . LEU B  1  485  ? -0.636  33.584  115.119 1.00 40.52 ? 483  LEU B CD2   1 
ATOM   12584 N  N     . ALA B  1  486  ? 2.281   29.789  112.480 1.00 45.89 ? 484  ALA B N     1 
ATOM   12585 C  CA    . ALA B  1  486  ? 2.978   29.549  111.219 1.00 41.51 ? 484  ALA B CA    1 
ATOM   12586 C  C     . ALA B  1  486  ? 2.070   29.006  110.121 1.00 47.46 ? 484  ALA B C     1 
ATOM   12587 O  O     . ALA B  1  486  ? 2.403   29.147  108.939 1.00 49.87 ? 484  ALA B O     1 
ATOM   12588 C  CB    . ALA B  1  486  ? 4.146   28.588  111.442 1.00 41.84 ? 484  ALA B CB    1 
ATOM   12589 N  N     . TYR B  1  487  ? 0.944   28.377  110.473 1.00 45.56 ? 485  TYR B N     1 
ATOM   12590 C  CA    . TYR B  1  487  ? 0.017   27.889  109.458 1.00 42.34 ? 485  TYR B CA    1 
ATOM   12591 C  C     . TYR B  1  487  ? -1.432  28.117  109.868 1.00 46.10 ? 485  TYR B C     1 
ATOM   12592 O  O     . TYR B  1  487  ? -2.339  27.493  109.299 1.00 40.47 ? 485  TYR B O     1 
ATOM   12593 C  CB    . TYR B  1  487  ? 0.250   26.401  109.166 1.00 47.95 ? 485  TYR B CB    1 
ATOM   12594 N  N     . LEU B  1  488  ? -1.671  28.991  110.846 1.00 52.09 ? 486  LEU B N     1 
ATOM   12595 C  CA    . LEU B  1  488  ? -3.040  29.299  111.243 1.00 47.75 ? 486  LEU B CA    1 
ATOM   12596 C  C     . LEU B  1  488  ? -3.840  29.885  110.086 1.00 43.88 ? 486  LEU B C     1 
ATOM   12597 O  O     . LEU B  1  488  ? -5.062  29.707  110.019 1.00 36.48 ? 486  LEU B O     1 
ATOM   12598 C  CB    . LEU B  1  488  ? -3.031  30.262  112.428 1.00 40.28 ? 486  LEU B CB    1 
ATOM   12599 C  CG    . LEU B  1  488  ? -4.413  30.577  112.982 1.00 48.41 ? 486  LEU B CG    1 
ATOM   12600 C  CD1   . LEU B  1  488  ? -5.116  29.281  113.356 1.00 52.78 ? 486  LEU B CD1   1 
ATOM   12601 C  CD2   . LEU B  1  488  ? -4.301  31.504  114.174 1.00 33.52 ? 486  LEU B CD2   1 
ATOM   12602 N  N     . VAL B  1  489  ? -3.173  30.588  109.166 1.00 45.74 ? 487  VAL B N     1 
ATOM   12603 C  CA    . VAL B  1  489  ? -3.877  31.141  108.012 1.00 36.38 ? 487  VAL B CA    1 
ATOM   12604 C  C     . VAL B  1  489  ? -4.630  30.042  107.277 1.00 36.25 ? 487  VAL B C     1 
ATOM   12605 O  O     . VAL B  1  489  ? -5.843  30.135  107.056 1.00 45.85 ? 487  VAL B O     1 
ATOM   12606 C  CB    . VAL B  1  489  ? -2.895  31.873  107.084 1.00 38.73 ? 487  VAL B CB    1 
ATOM   12607 C  CG1   . VAL B  1  489  ? -3.591  32.239  105.779 1.00 44.19 ? 487  VAL B CG1   1 
ATOM   12608 C  CG2   . VAL B  1  489  ? -2.350  33.112  107.789 1.00 44.69 ? 487  VAL B CG2   1 
ATOM   12609 N  N     . ARG B  1  490  ? -3.922  28.968  106.915 1.00 41.65 ? 488  ARG B N     1 
ATOM   12610 C  CA    . ARG B  1  490  ? -4.561  27.863  106.205 1.00 46.13 ? 488  ARG B CA    1 
ATOM   12611 C  C     . ARG B  1  490  ? -5.683  27.250  107.037 1.00 43.00 ? 488  ARG B C     1 
ATOM   12612 O  O     . ARG B  1  490  ? -6.722  26.854  106.495 1.00 41.73 ? 488  ARG B O     1 
ATOM   12613 C  CB    . ARG B  1  490  ? -3.513  26.810  105.833 1.00 41.52 ? 488  ARG B CB    1 
ATOM   12614 C  CG    . ARG B  1  490  ? -3.989  25.742  104.855 1.00 39.87 ? 488  ARG B CG    1 
ATOM   12615 C  CD    . ARG B  1  490  ? -2.900  24.687  104.650 1.00 41.37 ? 488  ARG B CD    1 
ATOM   12616 N  NE    . ARG B  1  490  ? -2.568  24.011  105.902 1.00 44.37 ? 488  ARG B NE    1 
ATOM   12617 C  CZ    . ARG B  1  490  ? -1.350  23.605  106.240 1.00 44.74 ? 488  ARG B CZ    1 
ATOM   12618 N  NH1   . ARG B  1  490  ? -0.305  23.830  105.460 1.00 32.85 ? 488  ARG B NH1   1 
ATOM   12619 N  NH2   . ARG B  1  490  ? -1.175  22.972  107.398 1.00 39.95 ? 488  ARG B NH2   1 
ATOM   12620 N  N     . ARG B  1  491  ? -5.503  27.196  108.362 1.00 37.03 ? 489  ARG B N     1 
ATOM   12621 C  CA    . ARG B  1  491  ? -6.517  26.612  109.230 1.00 40.85 ? 489  ARG B CA    1 
ATOM   12622 C  C     . ARG B  1  491  ? -7.769  27.476  109.274 1.00 53.98 ? 489  ARG B C     1 
ATOM   12623 O  O     . ARG B  1  491  ? -8.890  26.955  109.311 1.00 52.14 ? 489  ARG B O     1 
ATOM   12624 C  CB    . ARG B  1  491  ? -5.952  26.420  110.640 1.00 42.31 ? 489  ARG B CB    1 
ATOM   12625 N  N     . LEU B  1  492  ? -7.595  28.802  109.259 1.00 51.87 ? 490  LEU B N     1 
ATOM   12626 C  CA    . LEU B  1  492  ? -8.731  29.712  109.368 1.00 50.22 ? 490  LEU B CA    1 
ATOM   12627 C  C     . LEU B  1  492  ? -9.537  29.762  108.076 1.00 54.60 ? 490  LEU B C     1 
ATOM   12628 O  O     . LEU B  1  492  ? -10.770 29.873  108.109 1.00 46.30 ? 490  LEU B O     1 
ATOM   12629 C  CB    . LEU B  1  492  ? -8.239  31.109  109.745 1.00 45.95 ? 490  LEU B CB    1 
ATOM   12630 C  CG    . LEU B  1  492  ? -7.628  31.253  111.136 1.00 52.14 ? 490  LEU B CG    1 
ATOM   12631 C  CD1   . LEU B  1  492  ? -6.811  32.539  111.232 1.00 46.68 ? 490  LEU B CD1   1 
ATOM   12632 C  CD2   . LEU B  1  492  ? -8.737  31.237  112.174 1.00 50.71 ? 490  LEU B CD2   1 
ATOM   12633 N  N     . LEU B  1  493  ? -8.861  29.694  106.925 1.00 53.64 ? 491  LEU B N     1 
ATOM   12634 C  CA    . LEU B  1  493  ? -9.583  29.679  105.657 1.00 42.76 ? 491  LEU B CA    1 
ATOM   12635 C  C     . LEU B  1  493  ? -10.499 28.466  105.546 1.00 54.49 ? 491  LEU B C     1 
ATOM   12636 O  O     . LEU B  1  493  ? -11.509 28.517  104.833 1.00 62.99 ? 491  LEU B O     1 
ATOM   12637 C  CB    . LEU B  1  493  ? -8.598  29.706  104.490 1.00 48.79 ? 491  LEU B CB    1 
ATOM   12638 C  CG    . LEU B  1  493  ? -8.047  31.081  104.128 1.00 48.84 ? 491  LEU B CG    1 
ATOM   12639 C  CD1   . LEU B  1  493  ? -7.172  30.979  102.892 1.00 43.82 ? 491  LEU B CD1   1 
ATOM   12640 C  CD2   . LEU B  1  493  ? -9.190  32.068  103.911 1.00 48.58 ? 491  LEU B CD2   1 
ATOM   12641 N  N     . GLU B  1  494  ? -10.173 27.381  106.249 1.00 56.20 ? 492  GLU B N     1 
ATOM   12642 C  CA    . GLU B  1  494  ? -10.926 26.128  106.175 1.00 53.65 ? 492  GLU B CA    1 
ATOM   12643 C  C     . GLU B  1  494  ? -12.402 26.310  106.507 1.00 51.42 ? 492  GLU B C     1 
ATOM   12644 O  O     . GLU B  1  494  ? -13.263 25.692  105.878 1.00 49.56 ? 492  GLU B O     1 
ATOM   12645 C  CB    . GLU B  1  494  ? -10.314 25.085  107.114 1.00 49.25 ? 492  GLU B CB    1 
ATOM   12646 N  N     . ALA B  1  497  ? -13.640 31.165  104.480 1.00 57.23 ? 495  ALA B N     1 
ATOM   12647 C  CA    . ALA B  1  497  ? -13.989 31.573  103.124 1.00 56.60 ? 495  ALA B CA    1 
ATOM   12648 C  C     . ALA B  1  497  ? -15.499 31.662  102.977 1.00 49.43 ? 495  ALA B C     1 
ATOM   12649 O  O     . ALA B  1  497  ? -16.236 31.011  103.717 1.00 59.81 ? 495  ALA B O     1 
ATOM   12650 C  CB    . ALA B  1  497  ? -13.410 30.602  102.102 1.00 41.27 ? 495  ALA B CB    1 
ATOM   12651 N  N     . ASN B  1  498  ? -15.955 32.462  102.008 1.00 52.62 ? 496  ASN B N     1 
ATOM   12652 C  CA    . ASN B  1  498  ? -17.387 32.694  101.852 1.00 53.92 ? 496  ASN B CA    1 
ATOM   12653 C  C     . ASN B  1  498  ? -18.142 31.390  101.629 1.00 54.17 ? 496  ASN B C     1 
ATOM   12654 O  O     . ASN B  1  498  ? -19.240 31.198  102.162 1.00 52.55 ? 496  ASN B O     1 
ATOM   12655 C  CB    . ASN B  1  498  ? -17.638 33.664  100.699 1.00 52.64 ? 496  ASN B CB    1 
ATOM   12656 N  N     . SER B  1  499  ? -17.563 30.475  100.856 1.00 45.75 ? 497  SER B N     1 
ATOM   12657 C  CA    . SER B  1  499  ? -18.206 29.198  100.578 1.00 41.10 ? 497  SER B CA    1 
ATOM   12658 C  C     . SER B  1  499  ? -18.140 28.228  101.748 1.00 35.97 ? 497  SER B C     1 
ATOM   12659 O  O     . SER B  1  499  ? -18.769 27.167  101.679 1.00 41.71 ? 497  SER B O     1 
ATOM   12660 C  CB    . SER B  1  499  ? -17.551 28.552  99.361  1.00 39.62 ? 497  SER B CB    1 
ATOM   12661 O  OG    . SER B  1  499  ? -16.146 28.520  99.546  1.00 46.11 ? 497  SER B OG    1 
ATOM   12662 N  N     . SER B  1  500  ? -17.380 28.542  102.795 1.00 37.08 ? 498  SER B N     1 
ATOM   12663 C  CA    . SER B  1  500  ? -17.173 27.595  103.877 1.00 38.14 ? 498  SER B CA    1 
ATOM   12664 C  C     . SER B  1  500  ? -18.357 27.610  104.837 1.00 40.58 ? 498  SER B C     1 
ATOM   12665 O  O     . SER B  1  500  ? -18.916 28.667  105.140 1.00 45.79 ? 498  SER B O     1 
ATOM   12666 C  CB    . SER B  1  500  ? -15.868 27.895  104.621 1.00 41.73 ? 498  SER B CB    1 
ATOM   12667 O  OG    . SER B  1  500  ? -15.861 29.205  105.157 1.00 54.03 ? 498  SER B OG    1 
ATOM   12668 N  N     . PHE B  1  501  ? -18.745 26.414  105.297 1.00 35.75 ? 499  PHE B N     1 
ATOM   12669 C  CA    . PHE B  1  501  ? -19.876 26.280  106.215 1.00 38.60 ? 499  PHE B CA    1 
ATOM   12670 C  C     . PHE B  1  501  ? -19.662 27.081  107.491 1.00 45.68 ? 499  PHE B C     1 
ATOM   12671 O  O     . PHE B  1  501  ? -20.628 27.596  108.067 1.00 54.80 ? 499  PHE B O     1 
ATOM   12672 C  CB    . PHE B  1  501  ? -20.104 24.801  106.547 1.00 37.29 ? 499  PHE B CB    1 
ATOM   12673 C  CG    . PHE B  1  501  ? -21.279 24.538  107.466 1.00 38.49 ? 499  PHE B CG    1 
ATOM   12674 C  CD1   . PHE B  1  501  ? -21.149 24.656  108.840 1.00 43.09 ? 499  PHE B CD1   1 
ATOM   12675 C  CD2   . PHE B  1  501  ? -22.499 24.133  106.949 1.00 38.71 ? 499  PHE B CD2   1 
ATOM   12676 C  CE1   . PHE B  1  501  ? -22.223 24.403  109.677 1.00 39.96 ? 499  PHE B CE1   1 
ATOM   12677 C  CE2   . PHE B  1  501  ? -23.576 23.872  107.781 1.00 44.06 ? 499  PHE B CE2   1 
ATOM   12678 C  CZ    . PHE B  1  501  ? -23.436 24.009  109.147 1.00 44.44 ? 499  PHE B CZ    1 
ATOM   12679 N  N     . VAL B  1  502  ? -18.414 27.186  107.952 1.00 53.87 ? 500  VAL B N     1 
ATOM   12680 C  CA    . VAL B  1  502  ? -18.120 27.946  109.165 1.00 62.49 ? 500  VAL B CA    1 
ATOM   12681 C  C     . VAL B  1  502  ? -18.539 29.402  108.989 1.00 65.47 ? 500  VAL B C     1 
ATOM   12682 O  O     . VAL B  1  502  ? -19.317 29.946  109.781 1.00 69.45 ? 500  VAL B O     1 
ATOM   12683 C  CB    . VAL B  1  502  ? -16.629 27.827  109.526 1.00 55.93 ? 500  VAL B CB    1 
ATOM   12684 N  N     . HIS B  1  503  ? -18.034 30.048  107.933 1.00 55.54 ? 501  HIS B N     1 
ATOM   12685 C  CA    . HIS B  1  503  ? -18.408 31.431  107.654 1.00 54.41 ? 501  HIS B CA    1 
ATOM   12686 C  C     . HIS B  1  503  ? -19.895 31.566  107.339 1.00 59.64 ? 501  HIS B C     1 
ATOM   12687 O  O     . HIS B  1  503  ? -20.519 32.566  107.714 1.00 56.85 ? 501  HIS B O     1 
ATOM   12688 C  CB    . HIS B  1  503  ? -17.559 31.971  106.500 1.00 59.86 ? 501  HIS B CB    1 
ATOM   12689 C  CG    . HIS B  1  503  ? -18.100 33.221  105.874 1.00 59.18 ? 501  HIS B CG    1 
ATOM   12690 N  ND1   . HIS B  1  503  ? -19.075 33.203  104.899 1.00 62.29 ? 501  HIS B ND1   1 
ATOM   12691 C  CD2   . HIS B  1  503  ? -17.790 34.525  106.071 1.00 51.42 ? 501  HIS B CD2   1 
ATOM   12692 C  CE1   . HIS B  1  503  ? -19.349 34.442  104.530 1.00 56.27 ? 501  HIS B CE1   1 
ATOM   12693 N  NE2   . HIS B  1  503  ? -18.582 35.263  105.226 1.00 57.13 ? 501  HIS B NE2   1 
ATOM   12694 N  N     . ARG B  1  504  ? -20.481 30.573  106.665 1.00 49.06 ? 502  ARG B N     1 
ATOM   12695 C  CA    . ARG B  1  504  ? -21.876 30.681  106.251 1.00 50.57 ? 502  ARG B CA    1 
ATOM   12696 C  C     . ARG B  1  504  ? -22.822 30.577  107.441 1.00 51.66 ? 502  ARG B C     1 
ATOM   12697 O  O     . ARG B  1  504  ? -23.865 31.239  107.467 1.00 52.64 ? 502  ARG B O     1 
ATOM   12698 C  CB    . ARG B  1  504  ? -22.197 29.608  105.212 1.00 45.56 ? 502  ARG B CB    1 
ATOM   12699 C  CG    . ARG B  1  504  ? -21.694 29.961  103.823 1.00 50.88 ? 502  ARG B CG    1 
ATOM   12700 C  CD    . ARG B  1  504  ? -21.695 28.767  102.880 1.00 40.60 ? 502  ARG B CD    1 
ATOM   12701 N  NE    . ARG B  1  504  ? -23.020 28.203  102.658 1.00 46.32 ? 502  ARG B NE    1 
ATOM   12702 C  CZ    . ARG B  1  504  ? -23.948 28.741  101.877 1.00 45.48 ? 502  ARG B CZ    1 
ATOM   12703 N  NH1   . ARG B  1  504  ? -23.770 29.919  101.300 1.00 49.15 ? 502  ARG B NH1   1 
ATOM   12704 N  NH2   . ARG B  1  504  ? -25.086 28.084  101.674 1.00 48.70 ? 502  ARG B NH2   1 
ATOM   12705 N  N     . ILE B  1  505  ? -22.478 29.749  108.430 1.00 49.90 ? 503  ILE B N     1 
ATOM   12706 C  CA    . ILE B  1  505  ? -23.321 29.593  109.609 1.00 50.40 ? 503  ILE B CA    1 
ATOM   12707 C  C     . ILE B  1  505  ? -23.437 30.895  110.390 1.00 53.00 ? 503  ILE B C     1 
ATOM   12708 O  O     . ILE B  1  505  ? -24.403 31.084  111.136 1.00 49.71 ? 503  ILE B O     1 
ATOM   12709 C  CB    . ILE B  1  505  ? -22.781 28.456  110.502 1.00 45.83 ? 503  ILE B CB    1 
ATOM   12710 N  N     . ASN B  1  506  ? -22.479 31.807  110.228 1.00 50.41 ? 504  ASN B N     1 
ATOM   12711 C  CA    . ASN B  1  506  ? -22.496 33.096  110.907 1.00 57.21 ? 504  ASN B CA    1 
ATOM   12712 C  C     . ASN B  1  506  ? -22.843 34.250  109.972 1.00 60.69 ? 504  ASN B C     1 
ATOM   12713 O  O     . ASN B  1  506  ? -22.625 35.411  110.332 1.00 61.24 ? 504  ASN B O     1 
ATOM   12714 C  CB    . ASN B  1  506  ? -21.147 33.357  111.581 1.00 56.51 ? 504  ASN B CB    1 
ATOM   12715 N  N     . ASP B  1  507  ? -23.366 33.964  108.779 1.00 56.67 ? 505  ASP B N     1 
ATOM   12716 C  CA    . ASP B  1  507  ? -23.859 35.011  107.898 1.00 57.07 ? 505  ASP B CA    1 
ATOM   12717 C  C     . ASP B  1  507  ? -25.374 35.051  108.000 1.00 61.44 ? 505  ASP B C     1 
ATOM   12718 O  O     . ASP B  1  507  ? -26.038 34.094  107.571 1.00 58.00 ? 505  ASP B O     1 
ATOM   12719 C  CB    . ASP B  1  507  ? -23.428 34.765  106.453 1.00 54.80 ? 505  ASP B CB    1 
ATOM   12720 N  N     . PRO B  1  508  ? -25.966 36.107  108.565 1.00 65.25 ? 506  PRO B N     1 
ATOM   12721 C  CA    . PRO B  1  508  ? -27.432 36.150  108.694 1.00 64.35 ? 506  PRO B CA    1 
ATOM   12722 C  C     . PRO B  1  508  ? -28.162 36.146  107.363 1.00 65.26 ? 506  PRO B C     1 
ATOM   12723 O  O     . PRO B  1  508  ? -29.378 35.913  107.348 1.00 62.08 ? 506  PRO B O     1 
ATOM   12724 C  CB    . PRO B  1  508  ? -27.684 37.459  109.459 1.00 68.42 ? 506  PRO B CB    1 
ATOM   12725 C  CG    . PRO B  1  508  ? -26.374 37.798  110.098 1.00 66.48 ? 506  PRO B CG    1 
ATOM   12726 C  CD    . PRO B  1  508  ? -25.321 37.287  109.165 1.00 59.37 ? 506  PRO B CD    1 
ATOM   12727 N  N     . LYS B  1  509  ? -27.461 36.393  106.252 1.00 62.76 ? 507  LYS B N     1 
ATOM   12728 C  CA    . LYS B  1  509  ? -28.104 36.382  104.944 1.00 63.56 ? 507  LYS B CA    1 
ATOM   12729 C  C     . LYS B  1  509  ? -28.414 34.965  104.475 1.00 69.51 ? 507  LYS B C     1 
ATOM   12730 O  O     . LYS B  1  509  ? -29.327 34.770  103.664 1.00 71.42 ? 507  LYS B O     1 
ATOM   12731 C  CB    . LYS B  1  509  ? -27.221 37.096  103.922 1.00 56.74 ? 507  LYS B CB    1 
ATOM   12732 N  N     . VAL B  1  510  ? -27.677 33.970  104.964 1.00 64.93 ? 508  VAL B N     1 
ATOM   12733 C  CA    . VAL B  1  510  ? -27.872 32.583  104.558 1.00 63.65 ? 508  VAL B CA    1 
ATOM   12734 C  C     . VAL B  1  510  ? -28.896 31.935  105.481 1.00 61.83 ? 508  VAL B C     1 
ATOM   12735 O  O     . VAL B  1  510  ? -28.808 32.063  106.708 1.00 68.63 ? 508  VAL B O     1 
ATOM   12736 C  CB    . VAL B  1  510  ? -26.542 31.810  104.575 1.00 55.77 ? 508  VAL B CB    1 
ATOM   12737 N  N     . SER B  1  511  ? -29.865 31.241  104.896 1.00 57.56 ? 509  SER B N     1 
ATOM   12738 C  CA    . SER B  1  511  ? -30.925 30.602  105.659 1.00 60.68 ? 509  SER B CA    1 
ATOM   12739 C  C     . SER B  1  511  ? -30.562 29.159  105.985 1.00 60.03 ? 509  SER B C     1 
ATOM   12740 O  O     . SER B  1  511  ? -29.668 28.562  105.377 1.00 61.30 ? 509  SER B O     1 
ATOM   12741 C  CB    . SER B  1  511  ? -32.241 30.625  104.884 1.00 64.00 ? 509  SER B CB    1 
ATOM   12742 O  OG    . SER B  1  511  ? -32.311 29.525  103.991 1.00 60.05 ? 509  SER B OG    1 
ATOM   12743 N  N     . ILE B  1  512  ? -31.281 28.595  106.957 1.00 54.88 ? 510  ILE B N     1 
ATOM   12744 C  CA    . ILE B  1  512  ? -31.131 27.173  107.247 1.00 57.09 ? 510  ILE B CA    1 
ATOM   12745 C  C     . ILE B  1  512  ? -31.468 26.349  106.010 1.00 57.29 ? 510  ILE B C     1 
ATOM   12746 O  O     . ILE B  1  512  ? -30.851 25.309  105.752 1.00 51.02 ? 510  ILE B O     1 
ATOM   12747 C  CB    . ILE B  1  512  ? -31.998 26.774  108.456 1.00 48.66 ? 510  ILE B CB    1 
ATOM   12748 N  N     . ASP B  1  513  ? -32.439 26.813  105.216 1.00 57.64 ? 511  ASP B N     1 
ATOM   12749 C  CA    . ASP B  1  513  ? -32.795 26.119  103.981 1.00 57.25 ? 511  ASP B CA    1 
ATOM   12750 C  C     . ASP B  1  513  ? -31.606 26.044  103.030 1.00 54.89 ? 511  ASP B C     1 
ATOM   12751 O  O     . ASP B  1  513  ? -31.317 24.984  102.462 1.00 51.96 ? 511  ASP B O     1 
ATOM   12752 C  CB    . ASP B  1  513  ? -33.978 26.815  103.305 1.00 58.34 ? 511  ASP B CB    1 
ATOM   12753 C  CG    . ASP B  1  513  ? -35.320 26.401  103.890 1.00 63.38 ? 511  ASP B CG    1 
ATOM   12754 O  OD1   . ASP B  1  513  ? -35.397 25.334  104.537 1.00 66.26 ? 511  ASP B OD1   1 
ATOM   12755 O  OD2   . ASP B  1  513  ? -36.305 27.140  103.686 1.00 71.14 ? 511  ASP B OD2   1 
ATOM   12756 N  N     . GLU B  1  514  ? -30.906 27.167  102.841 1.00 49.01 ? 512  GLU B N     1 
ATOM   12757 C  CA    . GLU B  1  514  ? -29.720 27.169  101.992 1.00 54.67 ? 512  GLU B CA    1 
ATOM   12758 C  C     . GLU B  1  514  ? -28.643 26.242  102.542 1.00 54.09 ? 512  GLU B C     1 
ATOM   12759 O  O     . GLU B  1  514  ? -27.958 25.553  101.779 1.00 47.36 ? 512  GLU B O     1 
ATOM   12760 C  CB    . GLU B  1  514  ? -29.180 28.592  101.852 1.00 49.74 ? 512  GLU B CB    1 
ATOM   12761 C  CG    . GLU B  1  514  ? -30.244 29.624  101.510 1.00 63.14 ? 512  GLU B CG    1 
ATOM   12762 C  CD    . GLU B  1  514  ? -29.723 31.049  101.570 1.00 68.06 ? 512  GLU B CD    1 
ATOM   12763 O  OE1   . GLU B  1  514  ? -28.587 31.287  101.112 1.00 69.16 ? 512  GLU B OE1   1 
ATOM   12764 O  OE2   . GLU B  1  514  ? -30.449 31.929  102.082 1.00 70.55 ? 512  GLU B OE2   1 
ATOM   12765 N  N     . LEU B  1  515  ? -28.487 26.197  103.867 1.00 46.92 ? 513  LEU B N     1 
ATOM   12766 C  CA    . LEU B  1  515  ? -27.414 25.398  104.450 1.00 45.98 ? 513  LEU B CA    1 
ATOM   12767 C  C     . LEU B  1  515  ? -27.718 23.907  104.394 1.00 48.86 ? 513  LEU B C     1 
ATOM   12768 O  O     . LEU B  1  515  ? -26.789 23.090  104.400 1.00 45.42 ? 513  LEU B O     1 
ATOM   12769 C  CB    . LEU B  1  515  ? -27.164 25.831  105.894 1.00 46.19 ? 513  LEU B CB    1 
ATOM   12770 C  CG    . LEU B  1  515  ? -26.646 27.255  106.099 1.00 39.16 ? 513  LEU B CG    1 
ATOM   12771 C  CD1   . LEU B  1  515  ? -26.580 27.572  107.590 1.00 50.52 ? 513  LEU B CD1   1 
ATOM   12772 C  CD2   . LEU B  1  515  ? -25.285 27.434  105.452 1.00 51.63 ? 513  LEU B CD2   1 
ATOM   12773 N  N     . ILE B  1  516  ? -28.998 23.529  104.350 1.00 40.34 ? 514  ILE B N     1 
ATOM   12774 C  CA    . ILE B  1  516  ? -29.389 22.124  104.277 1.00 43.85 ? 514  ILE B CA    1 
ATOM   12775 C  C     . ILE B  1  516  ? -29.701 21.697  102.849 1.00 41.59 ? 514  ILE B C     1 
ATOM   12776 O  O     . ILE B  1  516  ? -30.176 20.577  102.632 1.00 45.03 ? 514  ILE B O     1 
ATOM   12777 C  CB    . ILE B  1  516  ? -30.580 21.812  105.198 1.00 50.55 ? 514  ILE B CB    1 
ATOM   12778 C  CG1   . ILE B  1  516  ? -31.865 22.443  104.652 1.00 46.00 ? 514  ILE B CG1   1 
ATOM   12779 C  CG2   . ILE B  1  516  ? -30.294 22.270  106.622 1.00 46.66 ? 514  ILE B CG2   1 
ATOM   12780 C  CD1   . ILE B  1  516  ? -33.124 22.000  105.382 1.00 50.59 ? 514  ILE B CD1   1 
ATOM   12781 N  N     . ALA B  1  517  ? -29.463 22.569  101.872 1.00 43.62 ? 515  ALA B N     1 
ATOM   12782 C  CA    . ALA B  1  517  ? -29.566 22.180  100.472 1.00 48.05 ? 515  ALA B CA    1 
ATOM   12783 C  C     . ALA B  1  517  ? -28.691 20.965  100.200 1.00 45.04 ? 515  ALA B C     1 
ATOM   12784 O  O     . ALA B  1  517  ? -27.530 20.918  100.610 1.00 45.19 ? 515  ALA B O     1 
ATOM   12785 C  CB    . ALA B  1  517  ? -29.154 23.344  99.571  1.00 41.23 ? 515  ALA B CB    1 
ATOM   12786 N  N     . ASP B  1  518  ? -29.268 19.970  99.536  1.00 42.47 ? 516  ASP B N     1 
ATOM   12787 C  CA    . ASP B  1  518  ? -28.564 18.735  99.226  1.00 41.48 ? 516  ASP B CA    1 
ATOM   12788 C  C     . ASP B  1  518  ? -27.650 18.996  98.036  1.00 39.29 ? 516  ASP B C     1 
ATOM   12789 O  O     . ASP B  1  518  ? -28.131 19.241  96.924  1.00 40.11 ? 516  ASP B O     1 
ATOM   12790 C  CB    . ASP B  1  518  ? -29.562 17.608  98.936  1.00 36.81 ? 516  ASP B CB    1 
ATOM   12791 C  CG    . ASP B  1  518  ? -28.896 16.244  98.759  1.00 46.27 ? 516  ASP B CG    1 
ATOM   12792 O  OD1   . ASP B  1  518  ? -27.650 16.172  98.711  1.00 39.13 ? 516  ASP B OD1   1 
ATOM   12793 O  OD2   . ASP B  1  518  ? -29.630 15.230  98.665  1.00 43.24 ? 516  ASP B OD2   1 
ATOM   12794 N  N     . PRO B  1  519  ? -26.332 18.977  98.232  1.00 33.27 ? 517  PRO B N     1 
ATOM   12795 C  CA    . PRO B  1  519  ? -25.431 19.204  97.096  1.00 35.21 ? 517  PRO B CA    1 
ATOM   12796 C  C     . PRO B  1  519  ? -25.610 18.182  95.990  1.00 33.74 ? 517  PRO B C     1 
ATOM   12797 O  O     . PRO B  1  519  ? -25.424 18.513  94.813  1.00 35.97 ? 517  PRO B O     1 
ATOM   12798 C  CB    . PRO B  1  519  ? -24.034 19.122  97.734  1.00 34.77 ? 517  PRO B CB    1 
ATOM   12799 C  CG    . PRO B  1  519  ? -24.217 18.339  98.974  1.00 35.73 ? 517  PRO B CG    1 
ATOM   12800 C  CD    . PRO B  1  519  ? -25.609 18.634  99.469  1.00 36.03 ? 517  PRO B CD    1 
ATOM   12801 N  N     . VAL B  1  520  ? -25.974 16.949  96.341  1.00 32.42 ? 518  VAL B N     1 
ATOM   12802 C  CA    . VAL B  1  520  ? -26.135 15.896  95.346  1.00 35.54 ? 518  VAL B CA    1 
ATOM   12803 C  C     . VAL B  1  520  ? -27.255 16.246  94.376  1.00 39.14 ? 518  VAL B C     1 
ATOM   12804 O  O     . VAL B  1  520  ? -27.109 16.098  93.156  1.00 38.28 ? 518  VAL B O     1 
ATOM   12805 C  CB    . VAL B  1  520  ? -26.391 14.548  96.040  1.00 36.21 ? 518  VAL B CB    1 
ATOM   12806 C  CG1   . VAL B  1  520  ? -26.458 13.426  95.015  1.00 44.49 ? 518  VAL B CG1   1 
ATOM   12807 C  CG2   . VAL B  1  520  ? -25.319 14.280  97.102  1.00 34.97 ? 518  VAL B CG2   1 
ATOM   12808 N  N     . GLU B  1  521  ? -28.386 16.721  94.899  1.00 39.61 ? 519  GLU B N     1 
ATOM   12809 C  CA    . GLU B  1  521  ? -29.516 17.042  94.034  1.00 37.87 ? 519  GLU B CA    1 
ATOM   12810 C  C     . GLU B  1  521  ? -29.310 18.349  93.284  1.00 40.94 ? 519  GLU B C     1 
ATOM   12811 O  O     . GLU B  1  521  ? -29.809 18.499  92.164  1.00 41.88 ? 519  GLU B O     1 
ATOM   12812 C  CB    . GLU B  1  521  ? -30.806 17.100  94.852  1.00 39.36 ? 519  GLU B CB    1 
ATOM   12813 C  CG    . GLU B  1  521  ? -31.173 15.774  95.496  1.00 40.39 ? 519  GLU B CG    1 
ATOM   12814 C  CD    . GLU B  1  521  ? -31.292 14.633  94.488  1.00 48.78 ? 519  GLU B CD    1 
ATOM   12815 O  OE1   . GLU B  1  521  ? -31.641 14.892  93.316  1.00 50.63 ? 519  GLU B OE1   1 
ATOM   12816 O  OE2   . GLU B  1  521  ? -31.035 13.471  94.872  1.00 51.45 ? 519  GLU B OE2   1 
ATOM   12817 N  N     . VAL B  1  522  ? -28.585 19.301  93.871  1.00 36.68 ? 520  VAL B N     1 
ATOM   12818 C  CA    . VAL B  1  522  ? -28.275 20.524  93.142  1.00 37.71 ? 520  VAL B CA    1 
ATOM   12819 C  C     . VAL B  1  522  ? -27.361 20.217  91.964  1.00 41.94 ? 520  VAL B C     1 
ATOM   12820 O  O     . VAL B  1  522  ? -27.578 20.714  90.852  1.00 40.81 ? 520  VAL B O     1 
ATOM   12821 C  CB    . VAL B  1  522  ? -27.661 21.575  94.083  1.00 38.08 ? 520  VAL B CB    1 
ATOM   12822 C  CG1   . VAL B  1  522  ? -27.215 22.797  93.292  1.00 38.84 ? 520  VAL B CG1   1 
ATOM   12823 C  CG2   . VAL B  1  522  ? -28.664 21.967  95.163  1.00 46.78 ? 520  VAL B CG2   1 
ATOM   12824 N  N     . VAL B  1  523  ? -26.334 19.388  92.181  1.00 34.30 ? 521  VAL B N     1 
ATOM   12825 C  CA    . VAL B  1  523  ? -25.461 18.997  91.077  1.00 35.45 ? 521  VAL B CA    1 
ATOM   12826 C  C     . VAL B  1  523  ? -26.244 18.219  90.025  1.00 34.60 ? 521  VAL B C     1 
ATOM   12827 O  O     . VAL B  1  523  ? -26.091 18.452  88.822  1.00 35.11 ? 521  VAL B O     1 
ATOM   12828 C  CB    . VAL B  1  523  ? -24.254 18.191  91.594  1.00 34.73 ? 521  VAL B CB    1 
ATOM   12829 C  CG1   . VAL B  1  523  ? -23.503 17.562  90.436  1.00 33.98 ? 521  VAL B CG1   1 
ATOM   12830 C  CG2   . VAL B  1  523  ? -23.323 19.094  92.385  1.00 33.67 ? 521  VAL B CG2   1 
ATOM   12831 N  N     . ARG B  1  524  ? -27.093 17.284  90.460  1.00 35.43 ? 522  ARG B N     1 
ATOM   12832 C  CA    . ARG B  1  524  ? -27.844 16.468  89.508  1.00 40.79 ? 522  ARG B CA    1 
ATOM   12833 C  C     . ARG B  1  524  ? -28.709 17.319  88.585  1.00 43.00 ? 522  ARG B C     1 
ATOM   12834 O  O     . ARG B  1  524  ? -28.921 16.953  87.424  1.00 41.34 ? 522  ARG B O     1 
ATOM   12835 C  CB    . ARG B  1  524  ? -28.715 15.454  90.246  1.00 40.67 ? 522  ARG B CB    1 
ATOM   12836 C  CG    . ARG B  1  524  ? -29.388 14.447  89.324  1.00 40.28 ? 522  ARG B CG    1 
ATOM   12837 C  CD    . ARG B  1  524  ? -30.553 13.751  90.005  1.00 43.86 ? 522  ARG B CD    1 
ATOM   12838 N  NE    . ARG B  1  524  ? -30.197 13.250  91.326  1.00 42.58 ? 522  ARG B NE    1 
ATOM   12839 C  CZ    . ARG B  1  524  ? -29.530 12.124  91.544  1.00 45.60 ? 522  ARG B CZ    1 
ATOM   12840 N  NH1   . ARG B  1  524  ? -29.101 11.369  90.546  1.00 47.72 ? 522  ARG B NH1   1 
ATOM   12841 N  NH2   . ARG B  1  524  ? -29.284 11.749  92.797  1.00 46.07 ? 522  ARG B NH2   1 
ATOM   12842 N  N     . ALA B  1  525  ? -29.197 18.459  89.068  1.00 41.89 ? 523  ALA B N     1 
ATOM   12843 C  CA    . ALA B  1  525  ? -30.110 19.284  88.290  1.00 40.65 ? 523  ALA B CA    1 
ATOM   12844 C  C     . ALA B  1  525  ? -29.403 20.310  87.417  1.00 43.76 ? 523  ALA B C     1 
ATOM   12845 O  O     . ALA B  1  525  ? -30.074 21.004  86.643  1.00 41.04 ? 523  ALA B O     1 
ATOM   12846 C  CB    . ALA B  1  525  ? -31.095 20.004  89.216  1.00 43.36 ? 523  ALA B CB    1 
ATOM   12847 N  N     . MET B  1  526  ? -28.082 20.425  87.518  1.00 42.22 ? 524  MET B N     1 
ATOM   12848 C  CA    A MET B  1  526  ? -27.356 21.358  86.676  0.49 40.20 ? 524  MET B CA    1 
ATOM   12849 C  CA    B MET B  1  526  ? -27.353 21.358  86.677  0.51 40.20 ? 524  MET B CA    1 
ATOM   12850 C  C     . MET B  1  526  ? -27.468 20.936  85.212  1.00 42.80 ? 524  MET B C     1 
ATOM   12851 O  O     . MET B  1  526  ? -27.524 19.741  84.906  1.00 37.78 ? 524  MET B O     1 
ATOM   12852 C  CB    A MET B  1  526  ? -25.891 21.427  87.098  0.49 41.08 ? 524  MET B CB    1 
ATOM   12853 C  CB    B MET B  1  526  ? -25.885 21.423  87.097  0.51 41.08 ? 524  MET B CB    1 
ATOM   12854 C  CG    A MET B  1  526  ? -25.705 22.031  88.472  0.49 43.88 ? 524  MET B CG    1 
ATOM   12855 C  CG    B MET B  1  526  ? -25.533 22.629  87.959  0.51 43.67 ? 524  MET B CG    1 
ATOM   12856 S  SD    A MET B  1  526  ? -26.414 23.686  88.547  0.49 44.88 ? 524  MET B SD    1 
ATOM   12857 S  SD    B MET B  1  526  ? -24.149 22.302  89.071  0.51 45.41 ? 524  MET B SD    1 
ATOM   12858 C  CE    A MET B  1  526  ? -25.272 24.597  87.510  0.49 42.69 ? 524  MET B CE    1 
ATOM   12859 C  CE    B MET B  1  526  ? -23.511 23.954  89.338  0.51 42.15 ? 524  MET B CE    1 
ATOM   12860 N  N     . PRO B  1  527  ? -27.515 21.900  84.285  1.00 42.82 ? 525  PRO B N     1 
ATOM   12861 C  CA    . PRO B  1  527  ? -27.626 21.526  82.864  1.00 48.33 ? 525  PRO B CA    1 
ATOM   12862 C  C     . PRO B  1  527  ? -26.443 20.708  82.381  1.00 44.65 ? 525  PRO B C     1 
ATOM   12863 O  O     . PRO B  1  527  ? -26.607 19.805  81.553  1.00 39.30 ? 525  PRO B O     1 
ATOM   12864 C  CB    . PRO B  1  527  ? -27.710 22.885  82.157  1.00 51.72 ? 525  PRO B CB    1 
ATOM   12865 C  CG    . PRO B  1  527  ? -26.973 23.813  83.063  1.00 47.26 ? 525  PRO B CG    1 
ATOM   12866 C  CD    . PRO B  1  527  ? -27.312 23.349  84.458  1.00 52.40 ? 525  PRO B CD    1 
ATOM   12867 N  N     . VAL B  1  528  ? -25.250 20.999  82.885  1.00 37.23 ? 526  VAL B N     1 
ATOM   12868 C  CA    . VAL B  1  528  ? -24.046 20.243  82.571  1.00 33.86 ? 526  VAL B CA    1 
ATOM   12869 C  C     . VAL B  1  528  ? -23.493 19.759  83.904  1.00 34.45 ? 526  VAL B C     1 
ATOM   12870 O  O     . VAL B  1  528  ? -22.890 20.536  84.651  1.00 37.83 ? 526  VAL B O     1 
ATOM   12871 C  CB    . VAL B  1  528  ? -23.016 21.081  81.809  1.00 34.19 ? 526  VAL B CB    1 
ATOM   12872 C  CG1   . VAL B  1  528  ? -21.731 20.299  81.627  1.00 33.50 ? 526  VAL B CG1   1 
ATOM   12873 C  CG2   . VAL B  1  528  ? -23.576 21.509  80.460  1.00 37.68 ? 526  VAL B CG2   1 
ATOM   12874 N  N     . VAL B  1  529  ? -23.703 18.482  84.212  1.00 30.71 ? 527  VAL B N     1 
ATOM   12875 C  CA    . VAL B  1  529  ? -23.260 17.951  85.495  1.00 28.98 ? 527  VAL B CA    1 
ATOM   12876 C  C     . VAL B  1  529  ? -21.743 18.004  85.561  1.00 29.18 ? 527  VAL B C     1 
ATOM   12877 O  O     . VAL B  1  529  ? -21.045 17.495  84.673  1.00 32.32 ? 527  VAL B O     1 
ATOM   12878 C  CB    . VAL B  1  529  ? -23.779 16.529  85.700  1.00 31.12 ? 527  VAL B CB    1 
ATOM   12879 C  CG1   . VAL B  1  529  ? -23.122 15.911  86.917  1.00 30.84 ? 527  VAL B CG1   1 
ATOM   12880 C  CG2   . VAL B  1  529  ? -25.300 16.536  85.858  1.00 32.27 ? 527  VAL B CG2   1 
ATOM   12881 N  N     . GLY B  1  530  ? -21.221 18.647  86.606  1.00 26.82 ? 528  GLY B N     1 
ATOM   12882 C  CA    . GLY B  1  530  ? -19.792 18.690  86.814  1.00 27.21 ? 528  GLY B CA    1 
ATOM   12883 C  C     . GLY B  1  530  ? -19.040 19.730  86.019  1.00 26.70 ? 528  GLY B C     1 
ATOM   12884 O  O     . GLY B  1  530  ? -17.820 19.631  85.910  1.00 25.64 ? 528  GLY B O     1 
ATOM   12885 N  N     . ALA B  1  531  ? -19.723 20.723  85.448  1.00 24.27 ? 529  ALA B N     1 
ATOM   12886 C  CA    . ALA B  1  531  ? -19.017 21.798  84.764  1.00 24.39 ? 529  ALA B CA    1 
ATOM   12887 C  C     . ALA B  1  531  ? -18.065 22.516  85.714  1.00 27.86 ? 529  ALA B C     1 
ATOM   12888 O  O     . ALA B  1  531  ? -18.400 22.776  86.874  1.00 29.68 ? 529  ALA B O     1 
ATOM   12889 C  CB    . ALA B  1  531  ? -20.011 22.798  84.172  1.00 30.84 ? 529  ALA B CB    1 
ATOM   12890 N  N     . LYS B  1  532  ? -16.863 22.805  85.211  1.00 22.58 ? 530  LYS B N     1 
ATOM   12891 C  CA    . LYS B  1  532  ? -15.872 23.603  85.924  1.00 22.30 ? 530  LYS B CA    1 
ATOM   12892 C  C     . LYS B  1  532  ? -16.475 24.931  86.364  1.00 23.75 ? 530  LYS B C     1 
ATOM   12893 O  O     . LYS B  1  532  ? -17.387 25.464  85.724  1.00 25.15 ? 530  LYS B O     1 
ATOM   12894 C  CB    . LYS B  1  532  ? -14.661 23.850  85.003  1.00 24.11 ? 530  LYS B CB    1 
ATOM   12895 C  CG    . LYS B  1  532  ? -13.629 24.881  85.479  1.00 26.60 ? 530  LYS B CG    1 
ATOM   12896 C  CD    . LYS B  1  532  ? -12.570 25.143  84.408  1.00 27.56 ? 530  LYS B CD    1 
ATOM   12897 C  CE    . LYS B  1  532  ? -13.109 25.954  83.235  1.00 26.17 ? 530  LYS B CE    1 
ATOM   12898 N  NZ    . LYS B  1  532  ? -13.554 27.331  83.609  1.00 28.04 ? 530  LYS B NZ    1 
ATOM   12899 N  N     . HIS B  1  533  ? -15.963 25.464  87.470  1.00 23.56 ? 531  HIS B N     1 
ATOM   12900 C  CA    . HIS B  1  533  ? -16.352 26.796  87.906  1.00 24.93 ? 531  HIS B CA    1 
ATOM   12901 C  C     . HIS B  1  533  ? -16.171 27.795  86.768  1.00 25.52 ? 531  HIS B C     1 
ATOM   12902 O  O     . HIS B  1  533  ? -15.143 27.799  86.086  1.00 24.35 ? 531  HIS B O     1 
ATOM   12903 C  CB    . HIS B  1  533  ? -15.506 27.201  89.112  1.00 24.03 ? 531  HIS B CB    1 
ATOM   12904 C  CG    . HIS B  1  533  ? -16.057 28.356  89.884  1.00 27.96 ? 531  HIS B CG    1 
ATOM   12905 N  ND1   . HIS B  1  533  ? -16.139 29.629  89.364  1.00 26.56 ? 531  HIS B ND1   1 
ATOM   12906 C  CD2   . HIS B  1  533  ? -16.539 28.434  91.146  1.00 32.77 ? 531  HIS B CD2   1 
ATOM   12907 C  CE1   . HIS B  1  533  ? -16.657 30.440  90.268  1.00 32.79 ? 531  HIS B CE1   1 
ATOM   12908 N  NE2   . HIS B  1  533  ? -16.908 29.739  91.359  1.00 34.37 ? 531  HIS B NE2   1 
ATOM   12909 N  N     . ASP B  1  534  ? -17.186 28.643  86.567  1.00 26.62 ? 532  ASP B N     1 
ATOM   12910 C  CA    . ASP B  1  534  ? -17.158 29.605  85.469  1.00 29.16 ? 532  ASP B CA    1 
ATOM   12911 C  C     . ASP B  1  534  ? -16.046 30.633  85.622  1.00 27.92 ? 532  ASP B C     1 
ATOM   12912 O  O     . ASP B  1  534  ? -15.590 31.203  84.627  1.00 29.89 ? 532  ASP B O     1 
ATOM   12913 C  CB    . ASP B  1  534  ? -18.507 30.322  85.374  1.00 29.08 ? 532  ASP B CB    1 
ATOM   12914 C  CG    . ASP B  1  534  ? -19.573 29.466  84.734  1.00 48.99 ? 532  ASP B CG    1 
ATOM   12915 O  OD1   . ASP B  1  534  ? -19.249 28.768  83.748  1.00 51.37 ? 532  ASP B OD1   1 
ATOM   12916 O  OD2   . ASP B  1  534  ? -20.728 29.489  85.218  1.00 58.08 ? 532  ASP B OD2   1 
ATOM   12917 N  N     . ARG B  1  535  ? -15.597 30.887  86.849  1.00 25.32 ? 533  ARG B N     1 
ATOM   12918 C  CA    . ARG B  1  535  ? -14.674 31.979  87.118  1.00 25.72 ? 533  ARG B CA    1 
ATOM   12919 C  C     . ARG B  1  535  ? -13.270 31.480  87.427  1.00 25.37 ? 533  ARG B C     1 
ATOM   12920 O  O     . ARG B  1  535  ? -12.456 32.232  87.972  1.00 27.05 ? 533  ARG B O     1 
ATOM   12921 C  CB    . ARG B  1  535  ? -15.192 32.842  88.269  1.00 36.17 ? 533  ARG B CB    1 
ATOM   12922 N  N     . ILE B  1  536  ? -12.982 30.217  87.128  1.00 23.04 ? 534  ILE B N     1 
ATOM   12923 C  CA    . ILE B  1  536  ? -11.653 29.650  87.317  1.00 20.56 ? 534  ILE B CA    1 
ATOM   12924 C  C     . ILE B  1  536  ? -11.191 29.111  85.972  1.00 19.14 ? 534  ILE B C     1 
ATOM   12925 O  O     . ILE B  1  536  ? -11.828 28.215  85.403  1.00 22.10 ? 534  ILE B O     1 
ATOM   12926 C  CB    . ILE B  1  536  ? -11.644 28.553  88.388  1.00 21.86 ? 534  ILE B CB    1 
ATOM   12927 C  CG1   . ILE B  1  536  ? -12.086 29.133  89.732  1.00 25.04 ? 534  ILE B CG1   1 
ATOM   12928 C  CG2   . ILE B  1  536  ? -10.245 27.953  88.512  1.00 23.00 ? 534  ILE B CG2   1 
ATOM   12929 C  CD1   . ILE B  1  536  ? -12.158 28.122  90.828  1.00 27.36 ? 534  ILE B CD1   1 
ATOM   12930 N  N     . ALA B  1  537  ? -10.102 29.668  85.460  1.00 18.99 ? 535  ALA B N     1 
ATOM   12931 C  CA    . ALA B  1  537  ? -9.604  29.269  84.151  1.00 19.43 ? 535  ALA B CA    1 
ATOM   12932 C  C     . ALA B  1  537  ? -8.842  27.956  84.251  1.00 20.91 ? 535  ALA B C     1 
ATOM   12933 O  O     . ALA B  1  537  ? -8.000  27.785  85.140  1.00 18.31 ? 535  ALA B O     1 
ATOM   12934 C  CB    . ALA B  1  537  ? -8.697  30.356  83.575  1.00 21.09 ? 535  ALA B CB    1 
ATOM   12935 N  N     . LEU B  1  538  ? -9.126  27.033  83.336  1.00 18.53 ? 536  LEU B N     1 
ATOM   12936 C  CA    . LEU B  1  538  ? -8.195  25.938  83.126  1.00 20.07 ? 536  LEU B CA    1 
ATOM   12937 C  C     . LEU B  1  538  ? -6.823  26.517  82.800  1.00 19.54 ? 536  LEU B C     1 
ATOM   12938 O  O     . LEU B  1  538  ? -6.728  27.596  82.208  1.00 19.10 ? 536  LEU B O     1 
ATOM   12939 C  CB    . LEU B  1  538  ? -8.646  25.043  81.975  1.00 19.78 ? 536  LEU B CB    1 
ATOM   12940 C  CG    . LEU B  1  538  ? -9.807  24.096  82.234  1.00 24.75 ? 536  LEU B CG    1 
ATOM   12941 C  CD1   . LEU B  1  538  ? -10.217 23.459  80.914  1.00 25.52 ? 536  LEU B CD1   1 
ATOM   12942 C  CD2   . LEU B  1  538  ? -9.392  23.042  83.242  1.00 21.24 ? 536  LEU B CD2   1 
ATOM   12943 N  N     . PRO B  1  539  ? -5.742  25.817  83.152  1.00 16.52 ? 537  PRO B N     1 
ATOM   12944 C  CA    . PRO B  1  539  ? -4.407  26.358  82.843  1.00 16.86 ? 537  PRO B CA    1 
ATOM   12945 C  C     . PRO B  1  539  ? -4.248  26.733  81.382  1.00 17.99 ? 537  PRO B C     1 
ATOM   12946 O  O     . PRO B  1  539  ? -3.672  27.785  81.082  1.00 19.19 ? 537  PRO B O     1 
ATOM   12947 C  CB    . PRO B  1  539  ? -3.464  25.233  83.284  1.00 19.05 ? 537  PRO B CB    1 
ATOM   12948 C  CG    . PRO B  1  539  ? -4.231  24.565  84.407  1.00 16.36 ? 537  PRO B CG    1 
ATOM   12949 C  CD    . PRO B  1  539  ? -5.679  24.585  83.954  1.00 18.29 ? 537  PRO B CD    1 
ATOM   12950 N  N     . ALA B  1  540  ? -4.794  25.933  80.468  1.00 18.19 ? 538  ALA B N     1 
ATOM   12951 C  CA    . ALA B  1  540  ? -4.675  26.246  79.048  1.00 20.15 ? 538  ALA B CA    1 
ATOM   12952 C  C     . ALA B  1  540  ? -5.373  27.546  78.686  1.00 20.79 ? 538  ALA B C     1 
ATOM   12953 O  O     . ALA B  1  540  ? -5.053  28.144  77.654  1.00 19.73 ? 538  ALA B O     1 
ATOM   12954 C  CB    . ALA B  1  540  ? -5.257  25.107  78.205  1.00 20.47 ? 538  ALA B CB    1 
ATOM   12955 N  N     . GLU B  1  541  ? -6.324  27.993  79.506  1.00 21.13 ? 539  GLU B N     1 
ATOM   12956 C  CA    . GLU B  1  541  ? -7.194  29.100  79.138  1.00 20.57 ? 539  GLU B CA    1 
ATOM   12957 C  C     . GLU B  1  541  ? -6.882  30.361  79.938  1.00 20.03 ? 539  GLU B C     1 
ATOM   12958 O  O     . GLU B  1  541  ? -7.695  31.294  79.969  1.00 22.17 ? 539  GLU B O     1 
ATOM   12959 C  CB    . GLU B  1  541  ? -8.657  28.661  79.278  1.00 24.92 ? 539  GLU B CB    1 
ATOM   12960 C  CG    . GLU B  1  541  ? -8.989  27.519  78.275  1.00 26.71 ? 539  GLU B CG    1 
ATOM   12961 C  CD    . GLU B  1  541  ? -10.381 26.889  78.414  1.00 42.41 ? 539  GLU B CD    1 
ATOM   12962 O  OE1   . GLU B  1  541  ? -11.204 27.364  79.216  1.00 36.19 ? 539  GLU B OE1   1 
ATOM   12963 O  OE2   . GLU B  1  541  ? -10.653 25.899  77.699  1.00 43.48 ? 539  GLU B OE2   1 
ATOM   12964 N  N     . LEU B  1  542  ? -5.684  30.433  80.534  1.00 18.68 ? 540  LEU B N     1 
ATOM   12965 C  CA    . LEU B  1  542  ? -5.326  31.574  81.375  1.00 19.21 ? 540  LEU B CA    1 
ATOM   12966 C  C     . LEU B  1  542  ? -5.443  32.896  80.636  1.00 23.53 ? 540  LEU B C     1 
ATOM   12967 O  O     . LEU B  1  542  ? -5.714  33.929  81.261  1.00 21.52 ? 540  LEU B O     1 
ATOM   12968 C  CB    . LEU B  1  542  ? -3.894  31.441  81.887  1.00 21.93 ? 540  LEU B CB    1 
ATOM   12969 C  CG    . LEU B  1  542  ? -3.568  30.684  83.158  1.00 26.30 ? 540  LEU B CG    1 
ATOM   12970 C  CD1   . LEU B  1  542  ? -2.135  31.032  83.577  1.00 20.49 ? 540  LEU B CD1   1 
ATOM   12971 C  CD2   . LEU B  1  542  ? -4.568  30.990  84.267  1.00 24.62 ? 540  LEU B CD2   1 
ATOM   12972 N  N     . PHE B  1  543  ? -5.221  32.892  79.321  1.00 19.23 ? 541  PHE B N     1 
ATOM   12973 C  CA    . PHE B  1  543  ? -5.199  34.121  78.541  1.00 19.94 ? 541  PHE B CA    1 
ATOM   12974 C  C     . PHE B  1  543  ? -6.454  34.280  77.700  1.00 19.45 ? 541  PHE B C     1 
ATOM   12975 O  O     . PHE B  1  543  ? -6.533  35.194  76.874  1.00 21.85 ? 541  PHE B O     1 
ATOM   12976 C  CB    . PHE B  1  543  ? -3.930  34.153  77.688  1.00 17.33 ? 541  PHE B CB    1 
ATOM   12977 C  CG    . PHE B  1  543  ? -2.701  33.873  78.488  1.00 18.84 ? 541  PHE B CG    1 
ATOM   12978 C  CD1   . PHE B  1  543  ? -2.378  34.689  79.565  1.00 21.62 ? 541  PHE B CD1   1 
ATOM   12979 C  CD2   . PHE B  1  543  ? -1.909  32.776  78.221  1.00 17.33 ? 541  PHE B CD2   1 
ATOM   12980 C  CE1   . PHE B  1  543  ? -1.279  34.425  80.344  1.00 19.73 ? 541  PHE B CE1   1 
ATOM   12981 C  CE2   . PHE B  1  543  ? -0.798  32.501  79.004  1.00 19.82 ? 541  PHE B CE2   1 
ATOM   12982 C  CZ    . PHE B  1  543  ? -0.475  33.334  80.062  1.00 21.88 ? 541  PHE B CZ    1 
ATOM   12983 N  N     . GLY B  1  544  ? -7.436  33.414  77.903  1.00 20.94 ? 542  GLY B N     1 
ATOM   12984 C  CA    . GLY B  1  544  ? -8.718  33.586  77.248  1.00 21.25 ? 542  GLY B CA    1 
ATOM   12985 C  C     . GLY B  1  544  ? -8.591  33.505  75.742  1.00 22.58 ? 542  GLY B C     1 
ATOM   12986 O  O     . GLY B  1  544  ? -7.885  32.651  75.191  1.00 23.54 ? 542  GLY B O     1 
ATOM   12987 N  N     . ASP B  1  545  ? -9.278  34.421  75.060  1.00 23.00 ? 543  ASP B N     1 
ATOM   12988 C  CA    . ASP B  1  545  ? -9.309  34.397  73.605  1.00 31.58 ? 543  ASP B CA    1 
ATOM   12989 C  C     . ASP B  1  545  ? -8.007  34.863  72.967  1.00 26.00 ? 543  ASP B C     1 
ATOM   12990 O  O     . ASP B  1  545  ? -7.828  34.661  71.761  1.00 26.38 ? 543  ASP B O     1 
ATOM   12991 C  CB    . ASP B  1  545  ? -10.465 35.264  73.096  1.00 31.59 ? 543  ASP B CB    1 
ATOM   12992 C  CG    . ASP B  1  545  ? -11.822 34.709  73.484  1.00 51.49 ? 543  ASP B CG    1 
ATOM   12993 O  OD1   . ASP B  1  545  ? -11.942 33.470  73.626  1.00 48.10 ? 543  ASP B OD1   1 
ATOM   12994 O  OD2   . ASP B  1  545  ? -12.769 35.512  73.641  1.00 58.59 ? 543  ASP B OD2   1 
ATOM   12995 N  N     . ALA B  1  546  ? -7.099  35.470  73.734  1.00 22.78 ? 544  ALA B N     1 
ATOM   12996 C  CA    . ALA B  1  546  ? -5.882  36.023  73.145  1.00 21.62 ? 544  ALA B CA    1 
ATOM   12997 C  C     . ALA B  1  546  ? -4.988  34.926  72.587  1.00 21.74 ? 544  ALA B C     1 
ATOM   12998 O  O     . ALA B  1  546  ? -4.462  35.041  71.474  1.00 22.72 ? 544  ALA B O     1 
ATOM   12999 C  CB    . ALA B  1  546  ? -5.113  36.849  74.179  1.00 21.00 ? 544  ALA B CB    1 
ATOM   13000 N  N     . ARG B  1  547  ? -4.795  33.857  73.350  1.00 17.91 ? 545  ARG B N     1 
ATOM   13001 C  CA    . ARG B  1  547  ? -3.898  32.800  72.923  1.00 19.25 ? 545  ARG B CA    1 
ATOM   13002 C  C     . ARG B  1  547  ? -4.051  31.636  73.884  1.00 19.61 ? 545  ARG B C     1 
ATOM   13003 O  O     . ARG B  1  547  ? -4.597  31.774  74.981  1.00 20.22 ? 545  ARG B O     1 
ATOM   13004 C  CB    . ARG B  1  547  ? -2.442  33.269  72.890  1.00 21.25 ? 545  ARG B CB    1 
ATOM   13005 C  CG    . ARG B  1  547  ? -1.921  33.691  74.229  1.00 18.46 ? 545  ARG B CG    1 
ATOM   13006 C  CD    . ARG B  1  547  ? -0.513  34.238  74.106  1.00 20.21 ? 545  ARG B CD    1 
ATOM   13007 N  NE    . ARG B  1  547  ? -0.179  35.009  75.289  1.00 21.77 ? 545  ARG B NE    1 
ATOM   13008 C  CZ    . ARG B  1  547  ? 0.617   34.592  76.261  1.00 19.71 ? 545  ARG B CZ    1 
ATOM   13009 N  NH1   . ARG B  1  547  ? 1.230   33.423  76.197  1.00 19.23 ? 545  ARG B NH1   1 
ATOM   13010 N  NH2   . ARG B  1  547  ? 0.817   35.381  77.311  1.00 20.79 ? 545  ARG B NH2   1 
ATOM   13011 N  N     . THR B  1  548  ? -3.576  30.487  73.442  1.00 17.75 ? 546  THR B N     1 
ATOM   13012 C  CA    . THR B  1  548  ? -3.582  29.284  74.256  1.00 16.66 ? 546  THR B CA    1 
ATOM   13013 C  C     . THR B  1  548  ? -2.300  29.233  75.073  1.00 17.51 ? 546  THR B C     1 
ATOM   13014 O  O     . THR B  1  548  ? -1.206  29.393  74.534  1.00 16.60 ? 546  THR B O     1 
ATOM   13015 C  CB    . THR B  1  548  ? -3.701  28.054  73.364  1.00 18.76 ? 546  THR B CB    1 
ATOM   13016 O  OG1   . THR B  1  548  ? -4.908  28.160  72.598  1.00 23.23 ? 546  THR B OG1   1 
ATOM   13017 C  CG2   . THR B  1  548  ? -3.744  26.792  74.194  1.00 21.57 ? 546  THR B CG2   1 
ATOM   13018 N  N     . ASN B  1  549  ? -2.440  29.027  76.375  1.00 16.88 ? 547  ASN B N     1 
ATOM   13019 C  CA    . ASN B  1  549  ? -1.277  28.892  77.226  1.00 15.55 ? 547  ASN B CA    1 
ATOM   13020 C  C     . ASN B  1  549  ? -0.511  27.621  76.864  1.00 17.41 ? 547  ASN B C     1 
ATOM   13021 O  O     . ASN B  1  549  ? -1.109  26.599  76.515  1.00 18.69 ? 547  ASN B O     1 
ATOM   13022 C  CB    . ASN B  1  549  ? -1.739  28.871  78.682  1.00 16.85 ? 547  ASN B CB    1 
ATOM   13023 C  CG    . ASN B  1  549  ? -0.611  28.987  79.643  1.00 14.92 ? 547  ASN B CG    1 
ATOM   13024 O  OD1   . ASN B  1  549  ? 0.489   29.410  79.296  1.00 16.81 ? 547  ASN B OD1   1 
ATOM   13025 N  ND2   . ASN B  1  549  ? -0.881  28.622  80.895  1.00 16.16 ? 547  ASN B ND2   1 
ATOM   13026 N  N     . SER B  1  550  ? 0.814   27.697  76.919  1.00 16.68 ? 548  SER B N     1 
ATOM   13027 C  CA    . SER B  1  550  ? 1.612   26.489  76.765  1.00 16.65 ? 548  SER B CA    1 
ATOM   13028 C  C     . SER B  1  550  ? 1.275   25.502  77.871  1.00 17.97 ? 548  SER B C     1 
ATOM   13029 O  O     . SER B  1  550  ? 0.887   25.882  78.980  1.00 18.32 ? 548  SER B O     1 
ATOM   13030 C  CB    . SER B  1  550  ? 3.094   26.810  76.818  1.00 14.81 ? 548  SER B CB    1 
ATOM   13031 O  OG    . SER B  1  550  ? 3.426   27.344  78.083  1.00 17.63 ? 548  SER B OG    1 
ATOM   13032 N  N     . ALA B  1  551  ? 1.424   24.221  77.561  1.00 17.67 ? 549  ALA B N     1 
ATOM   13033 C  CA    . ALA B  1  551  ? 1.183   23.168  78.540  1.00 17.64 ? 549  ALA B CA    1 
ATOM   13034 C  C     . ALA B  1  551  ? 2.503   22.585  79.012  1.00 17.33 ? 549  ALA B C     1 
ATOM   13035 O  O     . ALA B  1  551  ? 3.445   22.437  78.230  1.00 19.01 ? 549  ALA B O     1 
ATOM   13036 C  CB    . ALA B  1  551  ? 0.317   22.064  77.951  1.00 17.69 ? 549  ALA B CB    1 
ATOM   13037 N  N     . GLY B  1  552  ? 2.566   22.248  80.290  1.00 17.93 ? 550  GLY B N     1 
ATOM   13038 C  CA    . GLY B  1  552  ? 3.703   21.578  80.852  1.00 20.47 ? 550  GLY B CA    1 
ATOM   13039 C  C     . GLY B  1  552  ? 3.479   20.085  80.935  1.00 18.11 ? 550  GLY B C     1 
ATOM   13040 O  O     . GLY B  1  552  ? 2.628   19.508  80.249  1.00 21.20 ? 550  GLY B O     1 
ATOM   13041 N  N     . LEU B  1  553  ? 4.273   19.449  81.780  1.00 20.19 ? 551  LEU B N     1 
ATOM   13042 C  CA    . LEU B  1  553  ? 4.196   18.019  82.013  1.00 21.64 ? 551  LEU B CA    1 
ATOM   13043 C  C     . LEU B  1  553  ? 4.261   17.820  83.514  1.00 18.37 ? 551  LEU B C     1 
ATOM   13044 O  O     . LEU B  1  553  ? 4.990   18.533  84.201  1.00 22.17 ? 551  LEU B O     1 
ATOM   13045 C  CB    . LEU B  1  553  ? 5.335   17.269  81.319  1.00 21.34 ? 551  LEU B CB    1 
ATOM   13046 C  CG    . LEU B  1  553  ? 5.314   17.254  79.787  1.00 23.08 ? 551  LEU B CG    1 
ATOM   13047 C  CD1   . LEU B  1  553  ? 6.616   16.719  79.241  1.00 24.55 ? 551  LEU B CD1   1 
ATOM   13048 C  CD2   . LEU B  1  553  ? 4.164   16.412  79.283  1.00 24.84 ? 551  LEU B CD2   1 
ATOM   13049 N  N     . ASP B  1  554  ? 3.485   16.865  84.013  1.00 19.07 ? 552  ASP B N     1 
ATOM   13050 C  CA    . ASP B  1  554  ? 3.365   16.637  85.451  1.00 16.64 ? 552  ASP B CA    1 
ATOM   13051 C  C     . ASP B  1  554  ? 4.369   15.563  85.856  1.00 18.89 ? 552  ASP B C     1 
ATOM   13052 O  O     . ASP B  1  554  ? 4.131   14.370  85.660  1.00 19.49 ? 552  ASP B O     1 
ATOM   13053 C  CB    . ASP B  1  554  ? 1.938   16.233  85.794  1.00 20.42 ? 552  ASP B CB    1 
ATOM   13054 C  CG    . ASP B  1  554  ? 1.730   16.031  87.279  1.00 19.84 ? 552  ASP B CG    1 
ATOM   13055 O  OD1   . ASP B  1  554  ? 2.691   16.224  88.051  1.00 23.12 ? 552  ASP B OD1   1 
ATOM   13056 O  OD2   . ASP B  1  554  ? 0.599   15.678  87.654  1.00 25.18 ? 552  ASP B OD2   1 
ATOM   13057 N  N     . LEU B  1  555  ? 5.482   15.989  86.448  1.00 20.14 ? 553  LEU B N     1 
ATOM   13058 C  CA    . LEU B  1  555  ? 6.537   15.071  86.857  1.00 19.71 ? 553  LEU B CA    1 
ATOM   13059 C  C     . LEU B  1  555  ? 6.218   14.366  88.166  1.00 21.93 ? 553  LEU B C     1 
ATOM   13060 O  O     . LEU B  1  555  ? 7.086   13.684  88.704  1.00 20.57 ? 553  LEU B O     1 
ATOM   13061 C  CB    . LEU B  1  555  ? 7.871   15.810  86.975  1.00 20.40 ? 553  LEU B CB    1 
ATOM   13062 C  CG    . LEU B  1  555  ? 8.356   16.463  85.680  1.00 21.99 ? 553  LEU B CG    1 
ATOM   13063 C  CD1   . LEU B  1  555  ? 9.747   17.055  85.872  1.00 22.18 ? 553  LEU B CD1   1 
ATOM   13064 C  CD2   . LEU B  1  555  ? 8.350   15.448  84.536  1.00 24.31 ? 553  LEU B CD2   1 
ATOM   13065 N  N     . SER B  1  556  ? 5.005   14.523  88.697  1.00 20.32 ? 554  SER B N     1 
ATOM   13066 C  CA    . SER B  1  556  ? 4.519   13.664  89.768  1.00 19.37 ? 554  SER B CA    1 
ATOM   13067 C  C     . SER B  1  556  ? 3.557   12.600  89.278  1.00 21.33 ? 554  SER B C     1 
ATOM   13068 O  O     . SER B  1  556  ? 3.101   11.782  90.080  1.00 22.16 ? 554  SER B O     1 
ATOM   13069 C  CB    . SER B  1  556  ? 3.828   14.500  90.857  1.00 22.52 ? 554  SER B CB    1 
ATOM   13070 O  OG    . SER B  1  556  ? 2.535   14.900  90.422  1.00 22.42 ? 554  SER B OG    1 
ATOM   13071 N  N     . ASN B  1  557  ? 3.249   12.580  87.983  1.00 20.27 ? 555  ASN B N     1 
ATOM   13072 C  CA    . ASN B  1  557  ? 2.321   11.624  87.402  1.00 21.55 ? 555  ASN B CA    1 
ATOM   13073 C  C     . ASN B  1  557  ? 3.118   10.431  86.878  1.00 22.68 ? 555  ASN B C     1 
ATOM   13074 O  O     . ASN B  1  557  ? 3.976   10.591  86.006  1.00 21.29 ? 555  ASN B O     1 
ATOM   13075 C  CB    . ASN B  1  557  ? 1.521   12.320  86.298  1.00 21.61 ? 555  ASN B CB    1 
ATOM   13076 C  CG    . ASN B  1  557  ? 0.510   11.412  85.640  1.00 24.70 ? 555  ASN B CG    1 
ATOM   13077 O  OD1   . ASN B  1  557  ? 0.837   10.308  85.201  1.00 24.05 ? 555  ASN B OD1   1 
ATOM   13078 N  ND2   . ASN B  1  557  ? -0.739  11.876  85.563  1.00 21.86 ? 555  ASN B ND2   1 
ATOM   13079 N  N     . GLU B  1  558  ? 2.858   9.245   87.434  1.00 21.83 ? 556  GLU B N     1 
ATOM   13080 C  CA    . GLU B  1  558  ? 3.638   8.069   87.041  1.00 24.51 ? 556  GLU B CA    1 
ATOM   13081 C  C     . GLU B  1  558  ? 3.458   7.712   85.577  1.00 26.16 ? 556  GLU B C     1 
ATOM   13082 O  O     . GLU B  1  558  ? 4.396   7.202   84.961  1.00 26.04 ? 556  GLU B O     1 
ATOM   13083 C  CB    . GLU B  1  558  ? 3.278   6.851   87.887  1.00 29.58 ? 556  GLU B CB    1 
ATOM   13084 C  CG    . GLU B  1  558  ? 3.729   6.906   89.308  1.00 27.81 ? 556  GLU B CG    1 
ATOM   13085 C  CD    . GLU B  1  558  ? 5.249   6.989   89.517  1.00 27.75 ? 556  GLU B CD    1 
ATOM   13086 O  OE1   . GLU B  1  558  ? 6.077   6.738   88.611  1.00 25.59 ? 556  GLU B OE1   1 
ATOM   13087 O  OE2   . GLU B  1  558  ? 5.609   7.312   90.645  1.00 26.73 ? 556  GLU B OE2   1 
ATOM   13088 N  N     . GLU B  1  559  ? 2.266   7.922   85.009  1.00 22.37 ? 557  GLU B N     1 
ATOM   13089 C  CA    . GLU B  1  559  ? 2.104   7.677   83.580  1.00 22.87 ? 557  GLU B CA    1 
ATOM   13090 C  C     . GLU B  1  559  ? 3.005   8.611   82.799  1.00 23.14 ? 557  GLU B C     1 
ATOM   13091 O  O     . GLU B  1  559  ? 3.679   8.204   81.849  1.00 24.79 ? 557  GLU B O     1 
ATOM   13092 C  CB    . GLU B  1  559  ? 0.660   7.892   83.126  1.00 27.76 ? 557  GLU B CB    1 
ATOM   13093 C  CG    . GLU B  1  559  ? -0.392  6.997   83.687  1.00 33.32 ? 557  GLU B CG    1 
ATOM   13094 C  CD    . GLU B  1  559  ? -1.739  7.261   83.031  1.00 42.67 ? 557  GLU B CD    1 
ATOM   13095 O  OE1   . GLU B  1  559  ? -1.754  7.642   81.840  1.00 50.85 ? 557  GLU B OE1   1 
ATOM   13096 O  OE2   . GLU B  1  559  ? -2.781  7.102   83.700  1.00 38.63 ? 557  GLU B OE2   1 
ATOM   13097 N  N     . THR B  1  560  ? 3.007   9.888   83.185  1.00 21.43 ? 558  THR B N     1 
ATOM   13098 C  CA    . THR B  1  560  ? 3.858   10.860  82.520  1.00 19.96 ? 558  THR B CA    1 
ATOM   13099 C  C     . THR B  1  560  ? 5.326   10.490  82.662  1.00 21.29 ? 558  THR B C     1 
ATOM   13100 O  O     . THR B  1  560  ? 6.080   10.562  81.691  1.00 21.30 ? 558  THR B O     1 
ATOM   13101 C  CB    . THR B  1  560  ? 3.600   12.256  83.091  1.00 19.86 ? 558  THR B CB    1 
ATOM   13102 O  OG1   . THR B  1  560  ? 2.210   12.580  82.930  1.00 22.59 ? 558  THR B OG1   1 
ATOM   13103 C  CG2   . THR B  1  560  ? 4.439   13.290  82.362  1.00 20.85 ? 558  THR B CG2   1 
ATOM   13104 N  N     . LEU B  1  561  ? 5.754   10.082  83.860  1.00 19.83 ? 559  LEU B N     1 
ATOM   13105 C  CA    . LEU B  1  561  ? 7.163   9.749   84.032  1.00 20.09 ? 559  LEU B CA    1 
ATOM   13106 C  C     . LEU B  1  561  ? 7.538   8.538   83.194  1.00 20.83 ? 559  LEU B C     1 
ATOM   13107 O  O     . LEU B  1  561  ? 8.631   8.489   82.623  1.00 21.92 ? 559  LEU B O     1 
ATOM   13108 C  CB    . LEU B  1  561  ? 7.492   9.505   85.506  1.00 20.07 ? 559  LEU B CB    1 
ATOM   13109 C  CG    . LEU B  1  561  ? 7.396   10.763  86.370  1.00 18.00 ? 559  LEU B CG    1 
ATOM   13110 C  CD1   . LEU B  1  561  ? 7.538   10.367  87.839  1.00 21.29 ? 559  LEU B CD1   1 
ATOM   13111 C  CD2   . LEU B  1  561  ? 8.472   11.751  85.971  1.00 19.58 ? 559  LEU B CD2   1 
ATOM   13112 N  N     . ALA B  1  562  ? 6.649   7.548   83.122  1.00 21.48 ? 560  ALA B N     1 
ATOM   13113 C  CA    . ALA B  1  562  ? 6.937   6.360   82.332  1.00 23.45 ? 560  ALA B CA    1 
ATOM   13114 C  C     . ALA B  1  562  ? 7.043   6.700   80.853  1.00 25.08 ? 560  ALA B C     1 
ATOM   13115 O  O     . ALA B  1  562  ? 7.963   6.237   80.168  1.00 24.26 ? 560  ALA B O     1 
ATOM   13116 C  CB    . ALA B  1  562  ? 5.858   5.302   82.566  1.00 22.76 ? 560  ALA B CB    1 
ATOM   13117 N  N     . SER B  1  563  ? 6.108   7.502   80.337  1.00 21.13 ? 561  SER B N     1 
ATOM   13118 C  CA    . SER B  1  563  ? 6.153   7.842   78.918  1.00 22.32 ? 561  SER B CA    1 
ATOM   13119 C  C     . SER B  1  563  ? 7.311   8.784   78.623  1.00 24.35 ? 561  SER B C     1 
ATOM   13120 O  O     . SER B  1  563  ? 7.967   8.661   77.582  1.00 23.97 ? 561  SER B O     1 
ATOM   13121 C  CB    . SER B  1  563  ? 4.820   8.444   78.466  1.00 26.46 ? 561  SER B CB    1 
ATOM   13122 O  OG    . SER B  1  563  ? 4.584   9.709   79.055  1.00 29.59 ? 561  SER B OG    1 
ATOM   13123 N  N     . LEU B  1  564  ? 7.586   9.724   79.535  1.00 21.36 ? 562  LEU B N     1 
ATOM   13124 C  CA    A LEU B  1  564  ? 8.713   10.627  79.342  0.70 21.07 ? 562  LEU B CA    1 
ATOM   13125 C  CA    B LEU B  1  564  ? 8.716   10.627  79.348  0.30 21.15 ? 562  LEU B CA    1 
ATOM   13126 C  C     . LEU B  1  564  ? 10.033  9.865   79.351  1.00 25.01 ? 562  LEU B C     1 
ATOM   13127 O  O     . LEU B  1  564  ? 10.910  10.122  78.521  1.00 23.78 ? 562  LEU B O     1 
ATOM   13128 C  CB    A LEU B  1  564  ? 8.692   11.715  80.417  0.70 22.56 ? 562  LEU B CB    1 
ATOM   13129 C  CB    B LEU B  1  564  ? 8.721   11.698  80.437  0.30 22.56 ? 562  LEU B CB    1 
ATOM   13130 C  CG    A LEU B  1  564  ? 9.780   12.774  80.366  0.70 21.17 ? 562  LEU B CG    1 
ATOM   13131 C  CG    B LEU B  1  564  ? 8.574   13.139  79.970  0.30 24.78 ? 562  LEU B CG    1 
ATOM   13132 C  CD1   A LEU B  1  564  ? 9.707   13.525  79.043  0.70 25.06 ? 562  LEU B CD1   1 
ATOM   13133 C  CD1   B LEU B  1  564  ? 8.713   14.072  81.161  0.30 23.43 ? 562  LEU B CD1   1 
ATOM   13134 C  CD2   A LEU B  1  564  ? 9.640   13.723  81.558  0.70 22.65 ? 562  LEU B CD2   1 
ATOM   13135 C  CD2   B LEU B  1  564  ? 9.601   13.459  78.896  0.30 24.74 ? 562  LEU B CD2   1 
ATOM   13136 N  N     . THR B  1  565  ? 10.189  8.925   80.285  1.00 23.00 ? 563  THR B N     1 
ATOM   13137 C  CA    . THR B  1  565  ? 11.376  8.077   80.307  1.00 19.68 ? 563  THR B CA    1 
ATOM   13138 C  C     . THR B  1  565  ? 11.654  7.492   78.925  1.00 23.54 ? 563  THR B C     1 
ATOM   13139 O  O     . THR B  1  565  ? 12.779  7.562   78.419  1.00 23.70 ? 563  THR B O     1 
ATOM   13140 C  CB    . THR B  1  565  ? 11.183  6.960   81.333  1.00 23.49 ? 563  THR B CB    1 
ATOM   13141 O  OG1   . THR B  1  565  ? 11.067  7.525   82.649  1.00 24.94 ? 563  THR B OG1   1 
ATOM   13142 C  CG2   . THR B  1  565  ? 12.362  6.008   81.323  1.00 24.39 ? 563  THR B CG2   1 
ATOM   13143 N  N     . GLU B  1  566  ? 10.630  6.922   78.292  1.00 23.01 ? 564  GLU B N     1 
ATOM   13144 C  CA    . GLU B  1  566  ? 10.852  6.295   76.990  1.00 22.36 ? 564  GLU B CA    1 
ATOM   13145 C  C     . GLU B  1  566  ? 11.160  7.338   75.926  1.00 22.85 ? 564  GLU B C     1 
ATOM   13146 O  O     . GLU B  1  566  ? 12.039  7.126   75.082  1.00 23.52 ? 564  GLU B O     1 
ATOM   13147 C  CB    . GLU B  1  566  ? 9.640   5.454   76.585  1.00 27.43 ? 564  GLU B CB    1 
ATOM   13148 C  CG    . GLU B  1  566  ? 9.389   4.265   77.513  1.00 33.87 ? 564  GLU B CG    1 
ATOM   13149 C  CD    . GLU B  1  566  ? 10.658  3.502   77.873  1.00 45.63 ? 564  GLU B CD    1 
ATOM   13150 O  OE1   . GLU B  1  566  ? 11.390  3.074   76.953  1.00 50.24 ? 564  GLU B OE1   1 
ATOM   13151 O  OE2   . GLU B  1  566  ? 10.922  3.328   79.084  1.00 41.79 ? 564  GLU B OE2   1 
ATOM   13152 N  N     . ALA B  1  567  ? 10.438  8.460   75.940  1.00 22.00 ? 565  ALA B N     1 
ATOM   13153 C  CA    . ALA B  1  567  ? 10.706  9.520   74.976  1.00 21.85 ? 565  ALA B CA    1 
ATOM   13154 C  C     . ALA B  1  567  ? 12.104  10.086  75.160  1.00 22.86 ? 565  ALA B C     1 
ATOM   13155 O  O     . ALA B  1  567  ? 12.780  10.433  74.180  1.00 22.16 ? 565  ALA B O     1 
ATOM   13156 C  CB    . ALA B  1  567  ? 9.666   10.634  75.113  1.00 22.06 ? 565  ALA B CB    1 
ATOM   13157 N  N     . LEU B  1  568  ? 12.556  10.193  76.406  1.00 19.01 ? 566  LEU B N     1 
ATOM   13158 C  CA    . LEU B  1  568  ? 13.884  10.738  76.650  1.00 19.31 ? 566  LEU B CA    1 
ATOM   13159 C  C     . LEU B  1  568  ? 14.955  9.767   76.177  1.00 22.71 ? 566  LEU B C     1 
ATOM   13160 O  O     . LEU B  1  568  ? 15.934  10.170  75.537  1.00 21.89 ? 566  LEU B O     1 
ATOM   13161 C  CB    . LEU B  1  568  ? 14.063  11.050  78.135  1.00 19.64 ? 566  LEU B CB    1 
ATOM   13162 C  CG    . LEU B  1  568  ? 13.204  12.184  78.702  1.00 20.51 ? 566  LEU B CG    1 
ATOM   13163 C  CD1   . LEU B  1  568  ? 13.348  12.245  80.204  1.00 24.26 ? 566  LEU B CD1   1 
ATOM   13164 C  CD2   . LEU B  1  568  ? 13.566  13.515  78.057  1.00 20.79 ? 566  LEU B CD2   1 
ATOM   13165 N  N     . ARG B  1  569  ? 14.792  8.484   76.504  1.00 21.36 ? 567  ARG B N     1 
ATOM   13166 C  CA    . ARG B  1  569  ? 15.706  7.466   76.000  1.00 22.60 ? 567  ARG B CA    1 
ATOM   13167 C  C     . ARG B  1  569  ? 15.757  7.488   74.478  1.00 24.22 ? 567  ARG B C     1 
ATOM   13168 O  O     . ARG B  1  569  ? 16.839  7.460   73.881  1.00 26.37 ? 567  ARG B O     1 
ATOM   13169 C  CB    . ARG B  1  569  ? 15.288  6.085   76.515  1.00 23.53 ? 567  ARG B CB    1 
ATOM   13170 C  CG    . ARG B  1  569  ? 15.644  5.874   77.965  1.00 31.82 ? 567  ARG B CG    1 
ATOM   13171 C  CD    . ARG B  1  569  ? 15.140  4.544   78.498  1.00 30.43 ? 567  ARG B CD    1 
ATOM   13172 N  NE    . ARG B  1  569  ? 15.270  4.504   79.950  1.00 35.72 ? 567  ARG B NE    1 
ATOM   13173 C  CZ    . ARG B  1  569  ? 14.695  3.603   80.737  1.00 35.91 ? 567  ARG B CZ    1 
ATOM   13174 N  NH1   . ARG B  1  569  ? 13.892  2.672   80.250  1.00 40.76 ? 567  ARG B NH1   1 
ATOM   13175 N  NH2   . ARG B  1  569  ? 14.922  3.648   82.048  1.00 42.89 ? 567  ARG B NH2   1 
ATOM   13176 N  N     . GLU B  1  570  ? 14.591  7.562   73.834  1.00 22.11 ? 568  GLU B N     1 
ATOM   13177 C  CA    . GLU B  1  570  ? 14.566  7.577   72.379  1.00 23.26 ? 568  GLU B CA    1 
ATOM   13178 C  C     . GLU B  1  570  ? 15.251  8.815   71.828  1.00 23.65 ? 568  GLU B C     1 
ATOM   13179 O  O     . GLU B  1  570  ? 15.904  8.745   70.784  1.00 26.00 ? 568  GLU B O     1 
ATOM   13180 C  CB    . GLU B  1  570  ? 13.125  7.489   71.886  1.00 26.09 ? 568  GLU B CB    1 
ATOM   13181 C  CG    . GLU B  1  570  ? 12.504  6.133   72.157  1.00 29.69 ? 568  GLU B CG    1 
ATOM   13182 C  CD    . GLU B  1  570  ? 10.990  6.148   72.119  1.00 41.73 ? 568  GLU B CD    1 
ATOM   13183 O  OE1   . GLU B  1  570  ? 10.403  7.197   71.776  1.00 40.49 ? 568  GLU B OE1   1 
ATOM   13184 O  OE2   . GLU B  1  570  ? 10.390  5.104   72.445  1.00 46.27 ? 568  GLU B OE2   1 
ATOM   13185 N  N     . SER B  1  571  ? 15.139  9.946   72.531  1.00 22.27 ? 569  SER B N     1 
ATOM   13186 C  CA    . SER B  1  571  ? 15.770  11.174  72.062  1.00 23.51 ? 569  SER B CA    1 
ATOM   13187 C  C     . SER B  1  571  ? 17.281  11.029  72.037  1.00 27.41 ? 569  SER B C     1 
ATOM   13188 O  O     . SER B  1  571  ? 17.951  11.575  71.155  1.00 24.66 ? 569  SER B O     1 
ATOM   13189 C  CB    . SER B  1  571  ? 15.370  12.354  72.950  1.00 23.08 ? 569  SER B CB    1 
ATOM   13190 O  OG    . SER B  1  571  ? 16.134  12.376  74.160  1.00 24.28 ? 569  SER B OG    1 
ATOM   13191 N  N     . ALA B  1  572  ? 17.833  10.293  72.998  1.00 23.05 ? 570  ALA B N     1 
ATOM   13192 C  CA    . ALA B  1  572  ? 19.271  10.095  73.046  1.00 27.01 ? 570  ALA B CA    1 
ATOM   13193 C  C     . ALA B  1  572  ? 19.765  9.177   71.938  1.00 27.31 ? 570  ALA B C     1 
ATOM   13194 O  O     . ALA B  1  572  ? 20.966  9.173   71.647  1.00 29.53 ? 570  ALA B O     1 
ATOM   13195 C  CB    . ALA B  1  572  ? 19.669  9.543   74.410  1.00 27.47 ? 570  ALA B CB    1 
ATOM   13196 N  N     . ALA B  1  573  ? 18.880  8.403   71.314  1.00 23.31 ? 571  ALA B N     1 
ATOM   13197 C  CA    . ALA B  1  573  ? 19.298  7.525   70.230  1.00 26.27 ? 571  ALA B CA    1 
ATOM   13198 C  C     . ALA B  1  573  ? 19.225  8.191   68.861  1.00 26.68 ? 571  ALA B C     1 
ATOM   13199 O  O     . ALA B  1  573  ? 19.642  7.580   67.871  1.00 28.22 ? 571  ALA B O     1 
ATOM   13200 C  CB    . ALA B  1  573  ? 18.446  6.250   70.225  1.00 28.28 ? 571  ALA B CB    1 
ATOM   13201 N  N     . MET B  1  574  ? 18.701  9.406   68.779  1.00 24.61 ? 572  MET B N     1 
ATOM   13202 C  CA    . MET B  1  574  ? 18.593  10.096  67.503  1.00 23.35 ? 572  MET B CA    1 
ATOM   13203 C  C     . MET B  1  574  ? 19.913  10.752  67.136  1.00 25.60 ? 572  MET B C     1 
ATOM   13204 O  O     . MET B  1  574  ? 20.680  11.177  68.005  1.00 25.95 ? 572  MET B O     1 
ATOM   13205 C  CB    . MET B  1  574  ? 17.505  11.166  67.566  1.00 26.30 ? 572  MET B CB    1 
ATOM   13206 C  CG    . MET B  1  574  ? 16.118  10.610  67.767  1.00 26.88 ? 572  MET B CG    1 
ATOM   13207 S  SD    . MET B  1  574  ? 15.010  11.906  68.344  1.00 30.01 ? 572  MET B SD    1 
ATOM   13208 C  CE    . MET B  1  574  ? 13.483  10.958  68.438  1.00 25.86 ? 572  MET B CE    1 
ATOM   13209 N  N     . LYS B  1  575  ? 20.164  10.864  65.833  1.00 22.20 ? 573  LYS B N     1 
ATOM   13210 C  CA    . LYS B  1  575  ? 21.337  11.603  65.370  1.00 24.72 ? 573  LYS B CA    1 
ATOM   13211 C  C     . LYS B  1  575  ? 20.994  13.089  65.334  1.00 19.88 ? 573  LYS B C     1 
ATOM   13212 O  O     . LYS B  1  575  ? 20.246  13.536  64.459  1.00 22.59 ? 573  LYS B O     1 
ATOM   13213 C  CB    . LYS B  1  575  ? 21.787  11.112  63.997  1.00 23.26 ? 573  LYS B CB    1 
ATOM   13214 C  CG    . LYS B  1  575  ? 23.049  11.802  63.501  1.00 28.45 ? 573  LYS B CG    1 
ATOM   13215 C  CD    . LYS B  1  575  ? 23.303  11.501  62.036  1.00 35.80 ? 573  LYS B CD    1 
ATOM   13216 C  CE    . LYS B  1  575  ? 24.791  11.372  61.740  1.00 48.79 ? 573  LYS B CE    1 
ATOM   13217 N  NZ    . LYS B  1  575  ? 25.587  12.512  62.287  1.00 45.65 ? 573  LYS B NZ    1 
ATOM   13218 N  N     . TRP B  1  576  ? 21.537  13.851  66.278  1.00 23.02 ? 574  TRP B N     1 
ATOM   13219 C  CA    . TRP B  1  576  ? 21.314  15.287  66.370  1.00 21.03 ? 574  TRP B CA    1 
ATOM   13220 C  C     . TRP B  1  576  ? 22.446  16.018  65.673  1.00 21.05 ? 574  TRP B C     1 
ATOM   13221 O  O     . TRP B  1  576  ? 23.623  15.794  65.986  1.00 22.54 ? 574  TRP B O     1 
ATOM   13222 C  CB    . TRP B  1  576  ? 21.238  15.738  67.823  1.00 18.98 ? 574  TRP B CB    1 
ATOM   13223 C  CG    . TRP B  1  576  ? 20.072  15.159  68.547  1.00 20.34 ? 574  TRP B CG    1 
ATOM   13224 C  CD1   . TRP B  1  576  ? 20.095  14.167  69.486  1.00 22.69 ? 574  TRP B CD1   1 
ATOM   13225 C  CD2   . TRP B  1  576  ? 18.709  15.540  68.392  1.00 18.28 ? 574  TRP B CD2   1 
ATOM   13226 N  NE1   . TRP B  1  576  ? 18.820  13.919  69.940  1.00 22.73 ? 574  TRP B NE1   1 
ATOM   13227 C  CE2   . TRP B  1  576  ? 17.951  14.745  69.276  1.00 24.03 ? 574  TRP B CE2   1 
ATOM   13228 C  CE3   . TRP B  1  576  ? 18.054  16.480  67.592  1.00 20.64 ? 574  TRP B CE3   1 
ATOM   13229 C  CZ2   . TRP B  1  576  ? 16.570  14.865  69.386  1.00 25.44 ? 574  TRP B CZ2   1 
ATOM   13230 C  CZ3   . TRP B  1  576  ? 16.682  16.603  67.709  1.00 25.00 ? 574  TRP B CZ3   1 
ATOM   13231 C  CH2   . TRP B  1  576  ? 15.954  15.798  68.597  1.00 27.17 ? 574  TRP B CH2   1 
ATOM   13232 N  N     . THR B  1  577  ? 22.089  16.869  64.720  1.00 22.50 ? 575  THR B N     1 
ATOM   13233 C  CA    . THR B  1  577  ? 23.065  17.661  63.999  1.00 19.28 ? 575  THR B CA    1 
ATOM   13234 C  C     . THR B  1  577  ? 22.626  19.115  63.966  1.00 20.99 ? 575  THR B C     1 
ATOM   13235 O  O     . THR B  1  577  ? 21.459  19.456  64.177  1.00 20.77 ? 575  THR B O     1 
ATOM   13236 C  CB    . THR B  1  577  ? 23.259  17.148  62.574  1.00 24.06 ? 575  THR B CB    1 
ATOM   13237 O  OG1   . THR B  1  577  ? 22.015  17.279  61.870  1.00 25.80 ? 575  THR B OG1   1 
ATOM   13238 C  CG2   . THR B  1  577  ? 23.691  15.697  62.588  1.00 23.91 ? 575  THR B CG2   1 
ATOM   13239 N  N     . ALA B  1  578  ? 23.595  19.981  63.698  1.00 20.36 ? 576  ALA B N     1 
ATOM   13240 C  CA    . ALA B  1  578  ? 23.334  21.390  63.459  1.00 18.99 ? 576  ALA B CA    1 
ATOM   13241 C  C     . ALA B  1  578  ? 24.281  21.802  62.355  1.00 20.34 ? 576  ALA B C     1 
ATOM   13242 O  O     . ALA B  1  578  ? 25.485  21.549  62.459  1.00 21.57 ? 576  ALA B O     1 
ATOM   13243 C  CB    . ALA B  1  578  ? 23.560  22.232  64.719  1.00 19.51 ? 576  ALA B CB    1 
ATOM   13244 N  N     . LEU B  1  579  ? 23.732  22.357  61.283  1.00 20.22 ? 577  LEU B N     1 
ATOM   13245 C  CA    . LEU B  1  579  ? 24.468  22.692  60.076  1.00 18.34 ? 577  LEU B CA    1 
ATOM   13246 C  C     . LEU B  1  579  ? 24.240  24.148  59.725  1.00 18.00 ? 577  LEU B C     1 
ATOM   13247 O  O     . LEU B  1  579  ? 23.242  24.746  60.142  1.00 18.70 ? 577  LEU B O     1 
ATOM   13248 C  CB    . LEU B  1  579  ? 24.008  21.823  58.893  1.00 21.62 ? 577  LEU B CB    1 
ATOM   13249 C  CG    . LEU B  1  579  ? 23.810  20.337  59.167  1.00 24.46 ? 577  LEU B CG    1 
ATOM   13250 C  CD1   . LEU B  1  579  ? 23.211  19.649  57.939  1.00 23.94 ? 577  LEU B CD1   1 
ATOM   13251 C  CD2   . LEU B  1  579  ? 25.126  19.724  59.516  1.00 23.95 ? 577  LEU B CD2   1 
ATOM   13252 N  N     . PRO B  1  580  ? 25.134  24.745  58.921  1.00 18.60 ? 578  PRO B N     1 
ATOM   13253 C  CA    . PRO B  1  580  ? 24.815  26.039  58.315  1.00 16.24 ? 578  PRO B CA    1 
ATOM   13254 C  C     . PRO B  1  580  ? 23.710  25.825  57.301  1.00 18.48 ? 578  PRO B C     1 
ATOM   13255 O  O     . PRO B  1  580  ? 23.954  25.332  56.197  1.00 21.71 ? 578  PRO B O     1 
ATOM   13256 C  CB    . PRO B  1  580  ? 26.134  26.475  57.661  1.00 18.97 ? 578  PRO B CB    1 
ATOM   13257 C  CG    . PRO B  1  580  ? 27.187  25.575  58.288  1.00 22.69 ? 578  PRO B CG    1 
ATOM   13258 C  CD    . PRO B  1  580  ? 26.459  24.272  58.504  1.00 19.75 ? 578  PRO B CD    1 
ATOM   13259 N  N     . GLN B  1  581  ? 22.484  26.109  57.705  1.00 17.45 ? 579  GLN B N     1 
ATOM   13260 C  CA    . GLN B  1  581  ? 21.309  25.912  56.855  1.00 19.27 ? 579  GLN B CA    1 
ATOM   13261 C  C     . GLN B  1  581  ? 21.035  27.208  56.127  1.00 22.16 ? 579  GLN B C     1 
ATOM   13262 O  O     . GLN B  1  581  ? 20.328  28.087  56.625  1.00 20.68 ? 579  GLN B O     1 
ATOM   13263 C  CB    . GLN B  1  581  ? 20.104  25.492  57.680  1.00 20.34 ? 579  GLN B CB    1 
ATOM   13264 C  CG    . GLN B  1  581  ? 20.315  24.207  58.413  1.00 20.41 ? 579  GLN B CG    1 
ATOM   13265 C  CD    . GLN B  1  581  ? 20.222  23.008  57.511  1.00 27.53 ? 579  GLN B CD    1 
ATOM   13266 O  OE1   . GLN B  1  581  ? 20.022  23.138  56.297  1.00 25.63 ? 579  GLN B OE1   1 
ATOM   13267 N  NE2   . GLN B  1  581  ? 20.350  21.825  58.098  1.00 30.48 ? 579  GLN B NE2   1 
ATOM   13268 N  N     . LEU B  1  582  ? 21.604  27.331  54.940  1.00 19.69 ? 580  LEU B N     1 
ATOM   13269 C  CA    . LEU B  1  582  ? 21.346  28.480  54.095  1.00 20.11 ? 580  LEU B CA    1 
ATOM   13270 C  C     . LEU B  1  582  ? 20.086  28.225  53.273  1.00 22.25 ? 580  LEU B C     1 
ATOM   13271 O  O     . LEU B  1  582  ? 19.534  27.120  53.265  1.00 23.17 ? 580  LEU B O     1 
ATOM   13272 C  CB    . LEU B  1  582  ? 22.556  28.765  53.201  1.00 21.97 ? 580  LEU B CB    1 
ATOM   13273 C  CG    . LEU B  1  582  ? 23.635  29.644  53.867  1.00 29.12 ? 580  LEU B CG    1 
ATOM   13274 C  CD1   . LEU B  1  582  ? 24.296  28.964  55.057  1.00 25.99 ? 580  LEU B CD1   1 
ATOM   13275 C  CD2   . LEU B  1  582  ? 24.685  30.071  52.861  1.00 30.42 ? 580  LEU B CD2   1 
ATOM   13276 N  N     . ALA B  1  583  ? 19.623  29.273  52.589  1.00 19.17 ? 581  ALA B N     1 
ATOM   13277 C  CA    . ALA B  1  583  ? 18.392  29.151  51.822  1.00 21.73 ? 581  ALA B CA    1 
ATOM   13278 C  C     . ALA B  1  583  ? 18.522  28.083  50.753  1.00 27.32 ? 581  ALA B C     1 
ATOM   13279 O  O     . ALA B  1  583  ? 17.544  27.401  50.434  1.00 29.52 ? 581  ALA B O     1 
ATOM   13280 C  CB    . ALA B  1  583  ? 18.026  30.491  51.190  1.00 22.91 ? 581  ALA B CB    1 
ATOM   13281 N  N     . THR B  1  584  ? 19.721  27.902  50.221  1.00 21.79 ? 582  THR B N     1 
ATOM   13282 C  CA    . THR B  1  584  ? 19.955  26.946  49.149  1.00 23.48 ? 582  THR B CA    1 
ATOM   13283 C  C     . THR B  1  584  ? 20.312  25.555  49.657  1.00 24.03 ? 582  THR B C     1 
ATOM   13284 O  O     . THR B  1  584  ? 20.623  24.674  48.847  1.00 24.21 ? 582  THR B O     1 
ATOM   13285 C  CB    . THR B  1  584  ? 21.075  27.462  48.249  1.00 22.90 ? 582  THR B CB    1 
ATOM   13286 O  OG1   . THR B  1  584  ? 22.173  27.874  49.080  1.00 28.02 ? 582  THR B OG1   1 
ATOM   13287 C  CG2   . THR B  1  584  ? 20.585  28.644  47.448  1.00 30.59 ? 582  THR B CG2   1 
ATOM   13288 N  N     . GLY B  1  585  ? 20.289  25.336  50.968  1.00 22.98 ? 583  GLY B N     1 
ATOM   13289 C  CA    . GLY B  1  585  ? 20.610  24.049  51.530  1.00 22.73 ? 583  GLY B CA    1 
ATOM   13290 C  C     . GLY B  1  585  ? 21.754  24.162  52.510  1.00 22.97 ? 583  GLY B C     1 
ATOM   13291 O  O     . GLY B  1  585  ? 22.352  25.234  52.679  1.00 23.75 ? 583  GLY B O     1 
ATOM   13292 N  N     . PRO B  1  586  ? 22.074  23.059  53.183  1.00 21.33 ? 584  PRO B N     1 
ATOM   13293 C  CA    . PRO B  1  586  ? 23.163  23.087  54.160  1.00 21.02 ? 584  PRO B CA    1 
ATOM   13294 C  C     . PRO B  1  586  ? 24.517  23.231  53.489  1.00 23.23 ? 584  PRO B C     1 
ATOM   13295 O  O     . PRO B  1  586  ? 24.797  22.621  52.454  1.00 25.07 ? 584  PRO B O     1 
ATOM   13296 C  CB    . PRO B  1  586  ? 23.037  21.740  54.879  1.00 25.13 ? 584  PRO B CB    1 
ATOM   13297 C  CG    . PRO B  1  586  ? 22.365  20.857  53.898  1.00 27.60 ? 584  PRO B CG    1 
ATOM   13298 C  CD    . PRO B  1  586  ? 21.415  21.745  53.128  1.00 23.50 ? 584  PRO B CD    1 
ATOM   13299 N  N     . ALA B  1  587  ? 25.361  24.054  54.098  1.00 22.04 ? 585  ALA B N     1 
ATOM   13300 C  CA    . ALA B  1  587  ? 26.698  24.326  53.601  1.00 22.22 ? 585  ALA B CA    1 
ATOM   13301 C  C     . ALA B  1  587  ? 27.709  23.492  54.366  1.00 19.11 ? 585  ALA B C     1 
ATOM   13302 O  O     . ALA B  1  587  ? 27.487  23.113  55.521  1.00 23.13 ? 585  ALA B O     1 
ATOM   13303 C  CB    . ALA B  1  587  ? 27.043  25.812  53.740  1.00 26.06 ? 585  ALA B CB    1 
ATOM   13304 N  N     . ALA B  1  588  ? 28.823  23.206  53.702  1.00 24.07 ? 586  ALA B N     1 
ATOM   13305 C  CA    . ALA B  1  588  ? 29.934  22.537  54.350  1.00 22.24 ? 586  ALA B CA    1 
ATOM   13306 C  C     . ALA B  1  588  ? 30.612  23.475  55.339  1.00 23.84 ? 586  ALA B C     1 
ATOM   13307 O  O     . ALA B  1  588  ? 30.510  24.699  55.247  1.00 26.25 ? 586  ALA B O     1 
ATOM   13308 C  CB    . ALA B  1  588  ? 30.951  22.063  53.315  1.00 24.63 ? 586  ALA B CB    1 
ATOM   13309 N  N     . GLY B  1  589  ? 31.315  22.882  56.292  1.00 25.42 ? 587  GLY B N     1 
ATOM   13310 C  CA    . GLY B  1  589  ? 32.059  23.666  57.253  1.00 23.73 ? 587  GLY B CA    1 
ATOM   13311 C  C     . GLY B  1  589  ? 32.832  22.761  58.179  1.00 29.98 ? 587  GLY B C     1 
ATOM   13312 O  O     . GLY B  1  589  ? 32.878  21.544  57.992  1.00 29.48 ? 587  GLY B O     1 
ATOM   13313 N  N     . GLU B  1  590  ? 33.438  23.374  59.195  1.00 28.55 ? 588  GLU B N     1 
ATOM   13314 C  CA    . GLU B  1  590  ? 34.215  22.622  60.171  1.00 28.17 ? 588  GLU B CA    1 
ATOM   13315 C  C     . GLU B  1  590  ? 33.272  21.963  61.172  1.00 25.49 ? 588  GLU B C     1 
ATOM   13316 O  O     . GLU B  1  590  ? 32.423  22.628  61.768  1.00 24.44 ? 588  GLU B O     1 
ATOM   13317 C  CB    . GLU B  1  590  ? 35.196  23.544  60.892  1.00 31.07 ? 588  GLU B CB    1 
ATOM   13318 N  N     . THR B  1  591  ? 33.431  20.659  61.368  1.00 28.13 ? 589  THR B N     1 
ATOM   13319 C  CA    . THR B  1  591  ? 32.511  19.884  62.187  1.00 27.92 ? 589  THR B CA    1 
ATOM   13320 C  C     . THR B  1  591  ? 33.182  19.422  63.473  1.00 28.28 ? 589  THR B C     1 
ATOM   13321 O  O     . THR B  1  591  ? 34.337  18.983  63.462  1.00 29.81 ? 589  THR B O     1 
ATOM   13322 C  CB    . THR B  1  591  ? 31.994  18.674  61.409  1.00 26.51 ? 589  THR B CB    1 
ATOM   13323 O  OG1   . THR B  1  591  ? 31.310  19.134  60.239  1.00 30.08 ? 589  THR B OG1   1 
ATOM   13324 C  CG2   . THR B  1  591  ? 31.029  17.875  62.263  1.00 28.50 ? 589  THR B CG2   1 
ATOM   13325 N  N     . ARG B  1  592  ? 32.445  19.513  64.579  1.00 26.01 ? 590  ARG B N     1 
ATOM   13326 C  CA    . ARG B  1  592  ? 32.914  18.993  65.854  1.00 29.23 ? 590  ARG B CA    1 
ATOM   13327 C  C     . ARG B  1  592  ? 31.743  18.402  66.626  1.00 28.69 ? 590  ARG B C     1 
ATOM   13328 O  O     . ARG B  1  592  ? 30.569  18.661  66.327  1.00 26.13 ? 590  ARG B O     1 
ATOM   13329 C  CB    . ARG B  1  592  ? 33.585  20.080  66.691  1.00 30.54 ? 590  ARG B CB    1 
ATOM   13330 C  CG    . ARG B  1  592  ? 32.610  21.131  67.144  1.00 32.55 ? 590  ARG B CG    1 
ATOM   13331 C  CD    . ARG B  1  592  ? 33.146  21.928  68.308  1.00 35.98 ? 590  ARG B CD    1 
ATOM   13332 N  NE    . ARG B  1  592  ? 32.305  23.087  68.567  1.00 34.66 ? 590  ARG B NE    1 
ATOM   13333 C  CZ    . ARG B  1  592  ? 31.278  23.094  69.402  1.00 36.67 ? 590  ARG B CZ    1 
ATOM   13334 N  NH1   . ARG B  1  592  ? 30.945  22.017  70.098  1.00 31.32 ? 590  ARG B NH1   1 
ATOM   13335 N  NH2   . ARG B  1  592  ? 30.567  24.210  69.543  1.00 36.19 ? 590  ARG B NH2   1 
ATOM   13336 N  N     . THR B  1  593  ? 32.079  17.623  67.652  1.00 27.65 ? 591  THR B N     1 
ATOM   13337 C  CA    . THR B  1  593  ? 31.072  17.015  68.502  1.00 26.16 ? 591  THR B CA    1 
ATOM   13338 C  C     . THR B  1  593  ? 30.563  17.995  69.545  1.00 27.16 ? 591  THR B C     1 
ATOM   13339 O  O     . THR B  1  593  ? 31.261  18.919  69.970  1.00 26.84 ? 591  THR B O     1 
ATOM   13340 C  CB    . THR B  1  593  ? 31.630  15.786  69.211  1.00 28.35 ? 591  THR B CB    1 
ATOM   13341 O  OG1   . THR B  1  593  ? 32.784  16.171  69.968  1.00 32.25 ? 591  THR B OG1   1 
ATOM   13342 C  CG2   . THR B  1  593  ? 32.007  14.729  68.190  1.00 35.61 ? 591  THR B CG2   1 
ATOM   13343 N  N     . VAL B  1  594  ? 29.325  17.770  69.960  1.00 22.38 ? 592  VAL B N     1 
ATOM   13344 C  CA    . VAL B  1  594  ? 28.687  18.502  71.041  1.00 21.87 ? 592  VAL B CA    1 
ATOM   13345 C  C     . VAL B  1  594  ? 28.576  17.529  72.198  1.00 24.94 ? 592  VAL B C     1 
ATOM   13346 O  O     . VAL B  1  594  ? 28.009  16.443  72.041  1.00 23.57 ? 592  VAL B O     1 
ATOM   13347 C  CB    . VAL B  1  594  ? 27.312  19.034  70.614  1.00 22.71 ? 592  VAL B CB    1 
ATOM   13348 C  CG1   . VAL B  1  594  ? 26.625  19.755  71.762  1.00 24.05 ? 592  VAL B CG1   1 
ATOM   13349 C  CG2   . VAL B  1  594  ? 27.454  19.945  69.398  1.00 27.91 ? 592  VAL B CG2   1 
ATOM   13350 N  N     . LEU B  1  595  ? 29.153  17.892  73.342  1.00 24.01 ? 593  LEU B N     1 
ATOM   13351 C  CA    . LEU B  1  595  ? 29.257  16.996  74.482  1.00 25.67 ? 593  LEU B CA    1 
ATOM   13352 C  C     . LEU B  1  595  ? 28.345  17.460  75.610  1.00 21.50 ? 593  LEU B C     1 
ATOM   13353 O  O     . LEU B  1  595  ? 28.118  18.657  75.800  1.00 23.62 ? 593  LEU B O     1 
ATOM   13354 C  CB    . LEU B  1  595  ? 30.699  16.918  74.993  1.00 24.05 ? 593  LEU B CB    1 
ATOM   13355 C  CG    . LEU B  1  595  ? 31.754  16.557  73.949  1.00 26.61 ? 593  LEU B CG    1 
ATOM   13356 C  CD1   . LEU B  1  595  ? 33.129  16.611  74.593  1.00 32.61 ? 593  LEU B CD1   1 
ATOM   13357 C  CD2   . LEU B  1  595  ? 31.476  15.189  73.335  1.00 24.78 ? 593  LEU B CD2   1 
ATOM   13358 N  N     . ASN B  1  596  ? 27.840  16.498  76.362  1.00 20.27 ? 594  ASN B N     1 
ATOM   13359 C  CA    . ASN B  1  596  ? 27.030  16.788  77.534  1.00 23.10 ? 594  ASN B CA    1 
ATOM   13360 C  C     . ASN B  1  596  ? 27.891  17.507  78.570  1.00 18.85 ? 594  ASN B C     1 
ATOM   13361 O  O     . ASN B  1  596  ? 28.920  16.957  78.986  1.00 20.41 ? 594  ASN B O     1 
ATOM   13362 C  CB    . ASN B  1  596  ? 26.480  15.462  78.071  1.00 21.14 ? 594  ASN B CB    1 
ATOM   13363 C  CG    . ASN B  1  596  ? 25.455  15.637  79.169  1.00 21.00 ? 594  ASN B CG    1 
ATOM   13364 O  OD1   . ASN B  1  596  ? 25.484  16.605  79.924  1.00 21.78 ? 594  ASN B OD1   1 
ATOM   13365 N  ND2   . ASN B  1  596  ? 24.542  14.673  79.274  1.00 20.76 ? 594  ASN B ND2   1 
ATOM   13366 N  N     . PRO B  1  597  ? 27.536  18.726  78.998  1.00 19.06 ? 595  PRO B N     1 
ATOM   13367 C  CA    . PRO B  1  597  ? 28.376  19.415  79.994  1.00 19.66 ? 595  PRO B CA    1 
ATOM   13368 C  C     . PRO B  1  597  ? 28.457  18.673  81.305  1.00 20.96 ? 595  PRO B C     1 
ATOM   13369 O  O     . PRO B  1  597  ? 29.428  18.862  82.043  1.00 21.37 ? 595  PRO B O     1 
ATOM   13370 C  CB    . PRO B  1  597  ? 27.695  20.785  80.165  1.00 20.74 ? 595  PRO B CB    1 
ATOM   13371 C  CG    . PRO B  1  597  ? 26.285  20.592  79.616  1.00 20.31 ? 595  PRO B CG    1 
ATOM   13372 C  CD    . PRO B  1  597  ? 26.419  19.567  78.526  1.00 19.03 ? 595  PRO B CD    1 
ATOM   13373 N  N     . GLY B  1  598  ? 27.466  17.836  81.616  1.00 19.71 ? 596  GLY B N     1 
ATOM   13374 C  CA    . GLY B  1  598  ? 27.501  17.075  82.849  1.00 19.71 ? 596  GLY B CA    1 
ATOM   13375 C  C     . GLY B  1  598  ? 28.299  15.798  82.761  1.00 22.46 ? 596  GLY B C     1 
ATOM   13376 O  O     . GLY B  1  598  ? 28.533  15.140  83.780  1.00 24.17 ? 596  GLY B O     1 
ATOM   13377 N  N     . ASP B  1  599  ? 28.732  15.438  81.559  1.00 19.92 ? 597  ASP B N     1 
ATOM   13378 C  CA    . ASP B  1  599  ? 29.491  14.215  81.360  1.00 23.49 ? 597  ASP B CA    1 
ATOM   13379 C  C     . ASP B  1  599  ? 30.019  14.234  79.938  1.00 23.76 ? 597  ASP B C     1 
ATOM   13380 O  O     . ASP B  1  599  ? 29.289  13.897  79.004  1.00 22.17 ? 597  ASP B O     1 
ATOM   13381 C  CB    . ASP B  1  599  ? 28.609  12.992  81.608  1.00 20.97 ? 597  ASP B CB    1 
ATOM   13382 C  CG    . ASP B  1  599  ? 29.371  11.696  81.551  1.00 25.92 ? 597  ASP B CG    1 
ATOM   13383 O  OD1   . ASP B  1  599  ? 30.488  11.672  80.984  1.00 25.29 ? 597  ASP B OD1   1 
ATOM   13384 O  OD2   . ASP B  1  599  ? 28.832  10.697  82.070  1.00 28.87 ? 597  ASP B OD2   1 
ATOM   13385 N  N     . HIS B  1  600  ? 31.277  14.634  79.758  1.00 21.95 ? 598  HIS B N     1 
ATOM   13386 C  CA    . HIS B  1  600  ? 31.811  14.780  78.410  1.00 23.87 ? 598  HIS B CA    1 
ATOM   13387 C  C     . HIS B  1  600  ? 31.925  13.457  77.661  1.00 22.69 ? 598  HIS B C     1 
ATOM   13388 O  O     . HIS B  1  600  ? 32.171  13.480  76.454  1.00 28.13 ? 598  HIS B O     1 
ATOM   13389 C  CB    . HIS B  1  600  ? 33.165  15.499  78.462  1.00 24.23 ? 598  HIS B CB    1 
ATOM   13390 C  CG    . HIS B  1  600  ? 33.046  16.955  78.806  1.00 26.23 ? 598  HIS B CG    1 
ATOM   13391 N  ND1   . HIS B  1  600  ? 34.137  17.789  78.926  1.00 30.14 ? 598  HIS B ND1   1 
ATOM   13392 C  CD2   . HIS B  1  600  ? 31.958  17.720  79.063  1.00 21.83 ? 598  HIS B CD2   1 
ATOM   13393 C  CE1   . HIS B  1  600  ? 33.727  19.006  79.240  1.00 30.51 ? 598  HIS B CE1   1 
ATOM   13394 N  NE2   . HIS B  1  600  ? 32.409  18.992  79.328  1.00 26.09 ? 598  HIS B NE2   1 
ATOM   13395 N  N     . ARG B  1  601  ? 31.734  12.317  78.334  1.00 24.34 ? 599  ARG B N     1 
ATOM   13396 C  CA    . ARG B  1  601  ? 31.693  11.042  77.633  1.00 23.14 ? 599  ARG B CA    1 
ATOM   13397 C  C     . ARG B  1  601  ? 30.408  10.867  76.834  1.00 27.13 ? 599  ARG B C     1 
ATOM   13398 O  O     . ARG B  1  601  ? 30.360  10.017  75.938  1.00 28.85 ? 599  ARG B O     1 
ATOM   13399 C  CB    . ARG B  1  601  ? 31.844  9.895   78.624  1.00 29.34 ? 599  ARG B CB    1 
ATOM   13400 C  CG    . ARG B  1  601  ? 33.115  9.964   79.436  1.00 29.22 ? 599  ARG B CG    1 
ATOM   13401 C  CD    . ARG B  1  601  ? 33.073  8.977   80.574  1.00 32.60 ? 599  ARG B CD    1 
ATOM   13402 N  NE    . ARG B  1  601  ? 31.953  9.238   81.467  1.00 29.14 ? 599  ARG B NE    1 
ATOM   13403 C  CZ    . ARG B  1  601  ? 31.619  8.473   82.495  1.00 32.84 ? 599  ARG B CZ    1 
ATOM   13404 N  NH1   . ARG B  1  601  ? 32.331  7.403   82.819  1.00 33.96 ? 599  ARG B NH1   1 
ATOM   13405 N  NH2   . ARG B  1  601  ? 30.545  8.785   83.216  1.00 31.92 ? 599  ARG B NH2   1 
ATOM   13406 N  N     . ASP B  1  602  ? 29.373  11.638  77.152  1.00 24.08 ? 600  ASP B N     1 
ATOM   13407 C  CA    . ASP B  1  602  ? 28.070  11.542  76.503  1.00 23.81 ? 600  ASP B CA    1 
ATOM   13408 C  C     . ASP B  1  602  ? 28.077  12.498  75.319  1.00 24.63 ? 600  ASP B C     1 
ATOM   13409 O  O     . ASP B  1  602  ? 27.957  13.714  75.487  1.00 24.49 ? 600  ASP B O     1 
ATOM   13410 C  CB    . ASP B  1  602  ? 26.966  11.863  77.505  1.00 27.08 ? 600  ASP B CB    1 
ATOM   13411 C  CG    . ASP B  1  602  ? 25.590  11.790  76.894  1.00 28.08 ? 600  ASP B CG    1 
ATOM   13412 O  OD1   . ASP B  1  602  ? 25.426  11.074  75.888  1.00 28.96 ? 600  ASP B OD1   1 
ATOM   13413 O  OD2   . ASP B  1  602  ? 24.683  12.467  77.414  1.00 27.73 ? 600  ASP B OD2   1 
ATOM   13414 N  N     . VAL B  1  603  ? 28.253  11.953  74.117  1.00 26.10 ? 601  VAL B N     1 
ATOM   13415 C  CA    . VAL B  1  603  ? 28.234  12.756  72.900  1.00 23.33 ? 601  VAL B CA    1 
ATOM   13416 C  C     . VAL B  1  603  ? 26.782  12.997  72.510  1.00 24.60 ? 601  VAL B C     1 
ATOM   13417 O  O     . VAL B  1  603  ? 26.034  12.054  72.234  1.00 27.11 ? 601  VAL B O     1 
ATOM   13418 C  CB    . VAL B  1  603  ? 29.003  12.073  71.763  1.00 24.77 ? 601  VAL B CB    1 
ATOM   13419 C  CG1   . VAL B  1  603  ? 28.899  12.907  70.492  1.00 26.45 ? 601  VAL B CG1   1 
ATOM   13420 C  CG2   . VAL B  1  603  ? 30.466  11.843  72.162  1.00 26.42 ? 601  VAL B CG2   1 
ATOM   13421 N  N     . VAL B  1  604  ? 26.377  14.258  72.494  1.00 24.24 ? 602  VAL B N     1 
ATOM   13422 C  CA    . VAL B  1  604  ? 24.985  14.565  72.200  1.00 23.36 ? 602  VAL B CA    1 
ATOM   13423 C  C     . VAL B  1  604  ? 24.749  14.649  70.703  1.00 21.43 ? 602  VAL B C     1 
ATOM   13424 O  O     . VAL B  1  604  ? 23.711  14.208  70.204  1.00 22.80 ? 602  VAL B O     1 
ATOM   13425 C  CB    . VAL B  1  604  ? 24.582  15.862  72.918  1.00 19.55 ? 602  VAL B CB    1 
ATOM   13426 C  CG1   . VAL B  1  604  ? 23.112  16.128  72.726  1.00 18.16 ? 602  VAL B CG1   1 
ATOM   13427 C  CG2   . VAL B  1  604  ? 24.924  15.762  74.406  1.00 20.99 ? 602  VAL B CG2   1 
ATOM   13428 N  N     . GLY B  1  605  ? 25.710  15.174  69.963  1.00 21.63 ? 603  GLY B N     1 
ATOM   13429 C  CA    . GLY B  1  605  ? 25.506  15.365  68.545  1.00 24.29 ? 603  GLY B CA    1 
ATOM   13430 C  C     . GLY B  1  605  ? 26.704  16.029  67.921  1.00 23.38 ? 603  GLY B C     1 
ATOM   13431 O  O     . GLY B  1  605  ? 27.790  16.046  68.495  1.00 24.48 ? 603  GLY B O     1 
ATOM   13432 N  N     . SER B  1  606  ? 26.485  16.594  66.743  1.00 22.33 ? 604  SER B N     1 
ATOM   13433 C  CA    . SER B  1  606  ? 27.566  17.113  65.926  1.00 22.51 ? 604  SER B CA    1 
ATOM   13434 C  C     . SER B  1  606  ? 27.120  18.441  65.346  1.00 23.13 ? 604  SER B C     1 
ATOM   13435 O  O     . SER B  1  606  ? 25.977  18.573  64.900  1.00 25.33 ? 604  SER B O     1 
ATOM   13436 C  CB    . SER B  1  606  ? 27.924  16.120  64.816  1.00 29.86 ? 604  SER B CB    1 
ATOM   13437 O  OG    . SER B  1  606  ? 28.616  16.752  63.761  1.00 36.02 ? 604  SER B OG    1 
ATOM   13438 N  N     . VAL B  1  607  ? 28.007  19.429  65.365  1.00 22.62 ? 605  VAL B N     1 
ATOM   13439 C  CA    . VAL B  1  607  ? 27.709  20.728  64.784  1.00 19.13 ? 605  VAL B CA    1 
ATOM   13440 C  C     . VAL B  1  607  ? 28.711  21.013  63.677  1.00 20.86 ? 605  VAL B C     1 
ATOM   13441 O  O     . VAL B  1  607  ? 29.914  20.782  63.837  1.00 22.39 ? 605  VAL B O     1 
ATOM   13442 C  CB    . VAL B  1  607  ? 27.712  21.856  65.831  1.00 21.04 ? 605  VAL B CB    1 
ATOM   13443 C  CG1   . VAL B  1  607  ? 29.037  21.902  66.616  1.00 21.88 ? 605  VAL B CG1   1 
ATOM   13444 C  CG2   . VAL B  1  607  ? 27.419  23.197  65.144  1.00 19.75 ? 605  VAL B CG2   1 
ATOM   13445 N  N     . THR B  1  608  ? 28.206  21.503  62.551  1.00 19.20 ? 606  THR B N     1 
ATOM   13446 C  CA    . THR B  1  608  ? 29.033  21.996  61.466  1.00 21.43 ? 606  THR B CA    1 
ATOM   13447 C  C     . THR B  1  608  ? 28.935  23.513  61.489  1.00 20.50 ? 606  THR B C     1 
ATOM   13448 O  O     . THR B  1  608  ? 27.836  24.075  61.406  1.00 21.35 ? 606  THR B O     1 
ATOM   13449 C  CB    . THR B  1  608  ? 28.559  21.423  60.136  1.00 23.86 ? 606  THR B CB    1 
ATOM   13450 O  OG1   . THR B  1  608  ? 28.733  20.001  60.160  1.00 24.39 ? 606  THR B OG1   1 
ATOM   13451 C  CG2   . THR B  1  608  ? 29.340  22.018  58.979  1.00 22.45 ? 606  THR B CG2   1 
ATOM   13452 N  N     . GLU B  1  609  ? 30.069  24.175  61.634  1.00 21.90 ? 607  GLU B N     1 
ATOM   13453 C  CA    . GLU B  1  609  ? 30.012  25.600  61.893  1.00 24.63 ? 607  GLU B CA    1 
ATOM   13454 C  C     . GLU B  1  609  ? 30.220  26.379  60.601  1.00 21.94 ? 607  GLU B C     1 
ATOM   13455 O  O     . GLU B  1  609  ? 30.773  25.875  59.620  1.00 24.00 ? 607  GLU B O     1 
ATOM   13456 C  CB    . GLU B  1  609  ? 31.017  25.980  62.985  1.00 25.37 ? 607  GLU B CB    1 
ATOM   13457 C  CG    . GLU B  1  609  ? 30.480  25.530  64.332  1.00 28.44 ? 607  GLU B CG    1 
ATOM   13458 C  CD    . GLU B  1  609  ? 31.409  25.788  65.498  1.00 33.38 ? 607  GLU B CD    1 
ATOM   13459 O  OE1   . GLU B  1  609  ? 32.631  25.925  65.281  1.00 36.87 ? 607  GLU B OE1   1 
ATOM   13460 O  OE2   . GLU B  1  609  ? 30.902  25.842  66.635  1.00 32.12 ? 607  GLU B OE2   1 
ATOM   13461 N  N     . THR B  1  610  ? 29.721  27.607  60.610  1.00 23.73 ? 608  THR B N     1 
ATOM   13462 C  CA    . THR B  1  610  ? 29.556  28.410  59.407  1.00 22.24 ? 608  THR B CA    1 
ATOM   13463 C  C     . THR B  1  610  ? 30.831  29.183  59.103  1.00 21.66 ? 608  THR B C     1 
ATOM   13464 O  O     . THR B  1  610  ? 31.383  29.844  59.988  1.00 23.76 ? 608  THR B O     1 
ATOM   13465 C  CB    . THR B  1  610  ? 28.403  29.397  59.586  1.00 21.85 ? 608  THR B CB    1 
ATOM   13466 O  OG1   . THR B  1  610  ? 27.233  28.723  60.075  1.00 20.57 ? 608  THR B OG1   1 
ATOM   13467 C  CG2   . THR B  1  610  ? 28.093  30.077  58.264  1.00 21.46 ? 608  THR B CG2   1 
ATOM   13468 N  N     . SER B  1  611  ? 31.286  29.124  57.856  1.00 21.49 ? 609  SER B N     1 
ATOM   13469 C  CA    . SER B  1  611  ? 32.375  30.002  57.457  1.00 24.09 ? 609  SER B CA    1 
ATOM   13470 C  C     . SER B  1  611  ? 31.889  31.442  57.396  1.00 26.55 ? 609  SER B C     1 
ATOM   13471 O  O     . SER B  1  611  ? 30.704  31.713  57.190  1.00 23.03 ? 609  SER B O     1 
ATOM   13472 C  CB    . SER B  1  611  ? 32.933  29.590  56.099  1.00 24.99 ? 609  SER B CB    1 
ATOM   13473 O  OG    . SER B  1  611  ? 32.013  29.921  55.083  1.00 25.60 ? 609  SER B OG    1 
ATOM   13474 N  N     . GLU B  1  612  ? 32.820  32.384  57.573  1.00 26.06 ? 610  GLU B N     1 
ATOM   13475 C  CA    . GLU B  1  612  ? 32.428  33.786  57.481  1.00 26.18 ? 610  GLU B CA    1 
ATOM   13476 C  C     . GLU B  1  612  ? 31.922  34.124  56.084  1.00 22.41 ? 610  GLU B C     1 
ATOM   13477 O  O     . GLU B  1  612  ? 30.983  34.918  55.941  1.00 25.38 ? 610  GLU B O     1 
ATOM   13478 C  CB    . GLU B  1  612  ? 33.598  34.692  57.879  1.00 30.16 ? 610  GLU B CB    1 
ATOM   13479 C  CG    . GLU B  1  612  ? 33.919  34.637  59.367  1.00 36.56 ? 610  GLU B CG    1 
ATOM   13480 C  CD    . GLU B  1  612  ? 35.069  35.553  59.760  1.00 46.01 ? 610  GLU B CD    1 
ATOM   13481 O  OE1   . GLU B  1  612  ? 35.176  36.664  59.195  1.00 55.12 ? 610  GLU B OE1   1 
ATOM   13482 O  OE2   . GLU B  1  612  ? 35.863  35.159  60.636  1.00 46.75 ? 610  GLU B OE2   1 
ATOM   13483 N  N     . GLU B  1  613  ? 32.500  33.500  55.054  1.00 27.84 ? 611  GLU B N     1 
ATOM   13484 C  CA    . GLU B  1  613  ? 31.994  33.678  53.697  1.00 24.50 ? 611  GLU B CA    1 
ATOM   13485 C  C     . GLU B  1  613  ? 30.541  33.224  53.590  1.00 25.70 ? 611  GLU B C     1 
ATOM   13486 O  O     . GLU B  1  613  ? 29.718  33.897  52.964  1.00 25.38 ? 611  GLU B O     1 
ATOM   13487 C  CB    . GLU B  1  613  ? 32.873  32.919  52.697  1.00 30.91 ? 611  GLU B CB    1 
ATOM   13488 N  N     . ASP B  1  614  ? 30.204  32.080  54.196  1.00 24.30 ? 612  ASP B N     1 
ATOM   13489 C  CA    . ASP B  1  614  ? 28.827  31.608  54.096  1.00 24.33 ? 612  ASP B CA    1 
ATOM   13490 C  C     . ASP B  1  614  ? 27.893  32.435  54.963  1.00 22.14 ? 612  ASP B C     1 
ATOM   13491 O  O     . ASP B  1  614  ? 26.699  32.550  54.663  1.00 21.86 ? 612  ASP B O     1 
ATOM   13492 C  CB    . ASP B  1  614  ? 28.744  30.134  54.475  1.00 23.30 ? 612  ASP B CB    1 
ATOM   13493 C  CG    . ASP B  1  614  ? 29.191  29.231  53.349  1.00 28.01 ? 612  ASP B CG    1 
ATOM   13494 O  OD1   . ASP B  1  614  ? 29.075  29.646  52.177  1.00 29.51 ? 612  ASP B OD1   1 
ATOM   13495 O  OD2   . ASP B  1  614  ? 29.660  28.115  53.632  1.00 28.99 ? 612  ASP B OD2   1 
ATOM   13496 N  N     . ALA B  1  615  ? 28.403  33.009  56.047  1.00 21.26 ? 613  ALA B N     1 
ATOM   13497 C  CA    . ALA B  1  615  ? 27.579  33.928  56.818  1.00 19.80 ? 613  ALA B CA    1 
ATOM   13498 C  C     . ALA B  1  615  ? 27.172  35.119  55.962  1.00 22.51 ? 613  ALA B C     1 
ATOM   13499 O  O     . ALA B  1  615  ? 25.996  35.507  55.928  1.00 20.25 ? 613  ALA B O     1 
ATOM   13500 C  CB    . ALA B  1  615  ? 28.325  34.378  58.073  1.00 23.10 ? 613  ALA B CB    1 
ATOM   13501 N  N     . ARG B  1  616  ? 28.134  35.696  55.236  1.00 23.17 ? 614  ARG B N     1 
ATOM   13502 C  CA    . ARG B  1  616  ? 27.817  36.807  54.349  1.00 21.90 ? 614  ARG B CA    1 
ATOM   13503 C  C     . ARG B  1  616  ? 26.868  36.373  53.244  1.00 22.19 ? 614  ARG B C     1 
ATOM   13504 O  O     . ARG B  1  616  ? 25.927  37.103  52.906  1.00 22.91 ? 614  ARG B O     1 
ATOM   13505 C  CB    . ARG B  1  616  ? 29.101  37.403  53.774  1.00 24.42 ? 614  ARG B CB    1 
ATOM   13506 C  CG    . ARG B  1  616  ? 29.807  38.298  54.788  1.00 28.60 ? 614  ARG B CG    1 
ATOM   13507 C  CD    . ARG B  1  616  ? 30.977  39.031  54.160  1.00 34.77 ? 614  ARG B CD    1 
ATOM   13508 N  NE    . ARG B  1  616  ? 32.079  38.112  53.933  1.00 40.38 ? 614  ARG B NE    1 
ATOM   13509 C  CZ    . ARG B  1  616  ? 32.926  37.722  54.874  1.00 41.42 ? 614  ARG B CZ    1 
ATOM   13510 N  NH1   . ARG B  1  616  ? 32.853  38.195  56.109  1.00 39.36 ? 614  ARG B NH1   1 
ATOM   13511 N  NH2   . ARG B  1  616  ? 33.858  36.826  54.573  1.00 36.20 ? 614  ARG B NH2   1 
ATOM   13512 N  N     . ARG B  1  617  ? 27.090  35.186  52.675  1.00 22.28 ? 615  ARG B N     1 
ATOM   13513 C  CA    . ARG B  1  617  ? 26.187  34.689  51.643  1.00 24.22 ? 615  ARG B CA    1 
ATOM   13514 C  C     . ARG B  1  617  ? 24.770  34.544  52.179  1.00 22.88 ? 615  ARG B C     1 
ATOM   13515 O  O     . ARG B  1  617  ? 23.795  34.880  51.494  1.00 21.56 ? 615  ARG B O     1 
ATOM   13516 C  CB    . ARG B  1  617  ? 26.701  33.353  51.096  1.00 25.30 ? 615  ARG B CB    1 
ATOM   13517 C  CG    . ARG B  1  617  ? 25.824  32.799  49.979  1.00 25.50 ? 615  ARG B CG    1 
ATOM   13518 C  CD    . ARG B  1  617  ? 26.548  31.749  49.157  1.00 34.15 ? 615  ARG B CD    1 
ATOM   13519 N  NE    . ARG B  1  617  ? 26.775  30.508  49.887  1.00 38.05 ? 615  ARG B NE    1 
ATOM   13520 C  CZ    . ARG B  1  617  ? 25.980  29.448  49.826  1.00 44.58 ? 615  ARG B CZ    1 
ATOM   13521 N  NH1   . ARG B  1  617  ? 24.853  29.466  49.127  1.00 42.13 ? 615  ARG B NH1   1 
ATOM   13522 N  NH2   . ARG B  1  617  ? 26.322  28.342  50.481  1.00 45.40 ? 615  ARG B NH2   1 
ATOM   13523 N  N     . ALA B  1  618  ? 24.631  34.049  53.406  1.00 20.71 ? 616  ALA B N     1 
ATOM   13524 C  CA    . ALA B  1  618  ? 23.304  33.926  54.001  1.00 19.85 ? 616  ALA B CA    1 
ATOM   13525 C  C     . ALA B  1  618  ? 22.597  35.277  54.063  1.00 18.83 ? 616  ALA B C     1 
ATOM   13526 O  O     . ALA B  1  618  ? 21.389  35.375  53.794  1.00 19.98 ? 616  ALA B O     1 
ATOM   13527 C  CB    . ALA B  1  618  ? 23.417  33.307  55.398  1.00 19.46 ? 616  ALA B CB    1 
ATOM   13528 N  N     . VAL B  1  619  ? 23.323  36.331  54.433  1.00 20.74 ? 617  VAL B N     1 
ATOM   13529 C  CA    . VAL B  1  619  ? 22.667  37.627  54.534  1.00 19.47 ? 617  VAL B CA    1 
ATOM   13530 C  C     . VAL B  1  619  ? 22.219  38.092  53.159  1.00 21.18 ? 617  VAL B C     1 
ATOM   13531 O  O     . VAL B  1  619  ? 21.124  38.634  53.006  1.00 22.15 ? 617  VAL B O     1 
ATOM   13532 C  CB    . VAL B  1  619  ? 23.576  38.658  55.229  1.00 19.82 ? 617  VAL B CB    1 
ATOM   13533 C  CG1   . VAL B  1  619  ? 22.887  40.007  55.306  1.00 22.70 ? 617  VAL B CG1   1 
ATOM   13534 C  CG2   . VAL B  1  619  ? 23.914  38.183  56.624  1.00 23.20 ? 617  VAL B CG2   1 
ATOM   13535 N  N     . ARG B  1  620  ? 23.036  37.853  52.129  1.00 22.46 ? 618  ARG B N     1 
ATOM   13536 C  CA    . ARG B  1  620  ? 22.609  38.216  50.779  1.00 22.67 ? 618  ARG B CA    1 
ATOM   13537 C  C     . ARG B  1  620  ? 21.375  37.424  50.366  1.00 20.97 ? 618  ARG B C     1 
ATOM   13538 O  O     . ARG B  1  620  ? 20.449  37.977  49.763  1.00 23.67 ? 618  ARG B O     1 
ATOM   13539 C  CB    . ARG B  1  620  ? 23.747  38.005  49.778  1.00 25.06 ? 618  ARG B CB    1 
ATOM   13540 C  CG    . ARG B  1  620  ? 24.941  38.910  49.999  1.00 31.46 ? 618  ARG B CG    1 
ATOM   13541 C  CD    . ARG B  1  620  ? 25.864  38.901  48.773  1.00 38.01 ? 618  ARG B CD    1 
ATOM   13542 N  NE    . ARG B  1  620  ? 26.226  37.549  48.362  1.00 43.71 ? 618  ARG B NE    1 
ATOM   13543 C  CZ    . ARG B  1  620  ? 27.277  36.875  48.813  1.00 40.70 ? 618  ARG B CZ    1 
ATOM   13544 N  NH1   . ARG B  1  620  ? 28.096  37.391  49.714  1.00 34.16 ? 618  ARG B NH1   1 
ATOM   13545 N  NH2   . ARG B  1  620  ? 27.512  35.651  48.346  1.00 45.55 ? 618  ARG B NH2   1 
ATOM   13546 N  N     . LEU B  1  621  ? 21.340  36.126  50.687  1.00 20.30 ? 619  LEU B N     1 
ATOM   13547 C  CA    . LEU B  1  621  ? 20.165  35.320  50.371  1.00 20.99 ? 619  LEU B CA    1 
ATOM   13548 C  C     . LEU B  1  621  ? 18.937  35.818  51.120  1.00 24.75 ? 619  LEU B C     1 
ATOM   13549 O  O     . LEU B  1  621  ? 17.819  35.798  50.582  1.00 22.93 ? 619  LEU B O     1 
ATOM   13550 C  CB    . LEU B  1  621  ? 20.421  33.851  50.706  1.00 23.77 ? 619  LEU B CB    1 
ATOM   13551 C  CG    . LEU B  1  621  ? 21.430  33.109  49.831  1.00 23.18 ? 619  LEU B CG    1 
ATOM   13552 C  CD1   . LEU B  1  621  ? 21.762  31.762  50.435  1.00 24.54 ? 619  LEU B CD1   1 
ATOM   13553 C  CD2   . LEU B  1  621  ? 20.873  32.939  48.414  1.00 29.98 ? 619  LEU B CD2   1 
ATOM   13554 N  N     . ALA B  1  622  ? 19.118  36.237  52.376  1.00 22.12 ? 620  ALA B N     1 
ATOM   13555 C  CA    . ALA B  1  622  ? 18.003  36.801  53.128  1.00 20.91 ? 620  ALA B CA    1 
ATOM   13556 C  C     . ALA B  1  622  ? 17.515  38.091  52.483  1.00 21.35 ? 620  ALA B C     1 
ATOM   13557 O  O     . ALA B  1  622  ? 16.305  38.326  52.376  1.00 20.33 ? 620  ALA B O     1 
ATOM   13558 C  CB    . ALA B  1  622  ? 18.410  37.048  54.583  1.00 21.03 ? 620  ALA B CB    1 
ATOM   13559 N  N     . ALA B  1  623  ? 18.448  38.924  52.021  1.00 20.10 ? 621  ALA B N     1 
ATOM   13560 C  CA    . ALA B  1  623  ? 18.072  40.186  51.395  1.00 22.49 ? 621  ALA B CA    1 
ATOM   13561 C  C     . ALA B  1  623  ? 17.298  39.951  50.107  1.00 21.90 ? 621  ALA B C     1 
ATOM   13562 O  O     . ALA B  1  623  ? 16.284  40.614  49.856  1.00 23.38 ? 621  ALA B O     1 
ATOM   13563 C  CB    . ALA B  1  623  ? 19.324  41.021  51.127  1.00 23.04 ? 621  ALA B CB    1 
ATOM   13564 N  N     . ASP B  1  624  ? 17.736  38.984  49.297  1.00 23.57 ? 622  ASP B N     1 
ATOM   13565 C  CA    . ASP B  1  624  ? 17.026  38.686  48.055  1.00 24.01 ? 622  ASP B CA    1 
ATOM   13566 C  C     . ASP B  1  624  ? 15.597  38.245  48.329  1.00 23.78 ? 622  ASP B C     1 
ATOM   13567 O  O     . ASP B  1  624  ? 14.675  38.600  47.584  1.00 31.68 ? 622  ASP B O     1 
ATOM   13568 C  CB    . ASP B  1  624  ? 17.762  37.598  47.267  1.00 28.90 ? 622  ASP B CB    1 
ATOM   13569 C  CG    . ASP B  1  624  ? 19.133  38.031  46.789  1.00 35.74 ? 622  ASP B CG    1 
ATOM   13570 O  OD1   . ASP B  1  624  ? 19.367  39.249  46.613  1.00 44.33 ? 622  ASP B OD1   1 
ATOM   13571 O  OD2   . ASP B  1  624  ? 19.978  37.133  46.573  1.00 40.02 ? 622  ASP B OD2   1 
ATOM   13572 N  N     . ALA B  1  625  ? 15.391  37.478  49.392  1.00 27.47 ? 623  ALA B N     1 
ATOM   13573 C  CA    . ALA B  1  625  ? 14.077  36.952  49.722  1.00 29.43 ? 623  ALA B CA    1 
ATOM   13574 C  C     . ALA B  1  625  ? 13.263  37.877  50.611  1.00 25.22 ? 623  ALA B C     1 
ATOM   13575 O  O     . ALA B  1  625  ? 12.108  37.562  50.914  1.00 27.94 ? 623  ALA B O     1 
ATOM   13576 C  CB    . ALA B  1  625  ? 14.218  35.598  50.402  1.00 36.76 ? 623  ALA B CB    1 
ATOM   13577 N  N     . ALA B  1  626  ? 13.825  38.999  51.042  1.00 22.02 ? 624  ALA B N     1 
ATOM   13578 C  CA    . ALA B  1  626  ? 13.093  39.851  51.977  1.00 21.93 ? 624  ALA B CA    1 
ATOM   13579 C  C     . ALA B  1  626  ? 11.739  40.304  51.436  1.00 20.91 ? 624  ALA B C     1 
ATOM   13580 O  O     . ALA B  1  626  ? 10.747  40.228  52.182  1.00 23.70 ? 624  ALA B O     1 
ATOM   13581 C  CB    . ALA B  1  626  ? 13.976  41.032  52.398  1.00 19.77 ? 624  ALA B CB    1 
ATOM   13582 N  N     . PRO B  1  627  ? 11.604  40.760  50.183  1.00 21.92 ? 625  PRO B N     1 
ATOM   13583 C  CA    . PRO B  1  627  ? 10.269  41.198  49.735  1.00 23.36 ? 625  PRO B CA    1 
ATOM   13584 C  C     . PRO B  1  627  ? 9.233   40.093  49.734  1.00 23.19 ? 625  PRO B C     1 
ATOM   13585 O  O     . PRO B  1  627  ? 8.059   40.360  50.025  1.00 24.16 ? 625  PRO B O     1 
ATOM   13586 C  CB    . PRO B  1  627  ? 10.529  41.726  48.315  1.00 26.10 ? 625  PRO B CB    1 
ATOM   13587 C  CG    . PRO B  1  627  ? 11.968  42.074  48.297  1.00 26.72 ? 625  PRO B CG    1 
ATOM   13588 C  CD    . PRO B  1  627  ? 12.642  41.068  49.184  1.00 27.36 ? 625  PRO B CD    1 
ATOM   13589 N  N     . ASP B  1  628  ? 9.627   38.857  49.407  1.00 22.64 ? 626  ASP B N     1 
ATOM   13590 C  CA    . ASP B  1  628  ? 8.659   37.766  49.345  1.00 27.60 ? 626  ASP B CA    1 
ATOM   13591 C  C     . ASP B  1  628  ? 8.114   37.431  50.725  1.00 23.57 ? 626  ASP B C     1 
ATOM   13592 O  O     . ASP B  1  628  ? 6.937   37.084  50.867  1.00 24.70 ? 626  ASP B O     1 
ATOM   13593 C  CB    . ASP B  1  628  ? 9.289   36.520  48.726  1.00 25.41 ? 626  ASP B CB    1 
ATOM   13594 C  CG    . ASP B  1  628  ? 9.599   36.689  47.251  1.00 33.24 ? 626  ASP B CG    1 
ATOM   13595 O  OD1   . ASP B  1  628  ? 8.988   37.570  46.606  1.00 33.19 ? 626  ASP B OD1   1 
ATOM   13596 O  OD2   . ASP B  1  628  ? 10.453  35.939  46.747  1.00 42.12 ? 626  ASP B OD2   1 
ATOM   13597 N  N     . TRP B  1  629  ? 8.957   37.510  51.753  1.00 21.44 ? 627  TRP B N     1 
ATOM   13598 C  CA    . TRP B  1  629  ? 8.474   37.225  53.093  1.00 17.96 ? 627  TRP B CA    1 
ATOM   13599 C  C     . TRP B  1  629  ? 7.668   38.401  53.635  1.00 20.04 ? 627  TRP B C     1 
ATOM   13600 O  O     . TRP B  1  629  ? 6.642   38.205  54.299  1.00 20.63 ? 627  TRP B O     1 
ATOM   13601 C  CB    . TRP B  1  629  ? 9.657   36.877  53.999  1.00 19.55 ? 627  TRP B CB    1 
ATOM   13602 C  CG    . TRP B  1  629  ? 9.240   36.589  55.398  1.00 19.97 ? 627  TRP B CG    1 
ATOM   13603 C  CD1   . TRP B  1  629  ? 9.611   37.278  56.520  1.00 19.40 ? 627  TRP B CD1   1 
ATOM   13604 C  CD2   . TRP B  1  629  ? 8.346   35.560  55.833  1.00 18.48 ? 627  TRP B CD2   1 
ATOM   13605 N  NE1   . TRP B  1  629  ? 9.012   36.731  57.621  1.00 16.76 ? 627  TRP B NE1   1 
ATOM   13606 C  CE2   . TRP B  1  629  ? 8.226   35.680  57.232  1.00 16.01 ? 627  TRP B CE2   1 
ATOM   13607 C  CE3   . TRP B  1  629  ? 7.628   34.548  55.180  1.00 17.37 ? 627  TRP B CE3   1 
ATOM   13608 C  CZ2   . TRP B  1  629  ? 7.421   34.835  57.987  1.00 18.09 ? 627  TRP B CZ2   1 
ATOM   13609 C  CZ3   . TRP B  1  629  ? 6.819   33.710  55.941  1.00 20.26 ? 627  TRP B CZ3   1 
ATOM   13610 C  CH2   . TRP B  1  629  ? 6.729   33.858  57.325  1.00 21.04 ? 627  TRP B CH2   1 
ATOM   13611 N  N     . ALA B  1  630  ? 8.102   39.627  53.339  1.00 19.86 ? 628  ALA B N     1 
ATOM   13612 C  CA    . ALA B  1  630  ? 7.319   40.784  53.754  1.00 20.37 ? 628  ALA B CA    1 
ATOM   13613 C  C     . ALA B  1  630  ? 5.917   40.730  53.171  1.00 22.29 ? 628  ALA B C     1 
ATOM   13614 O  O     . ALA B  1  630  ? 4.971   41.227  53.787  1.00 24.81 ? 628  ALA B O     1 
ATOM   13615 C  CB    . ALA B  1  630  ? 8.014   42.080  53.342  1.00 25.96 ? 628  ALA B CB    1 
ATOM   13616 N  N     . ALA B  1  631  ? 5.764   40.111  52.000  1.00 21.37 ? 629  ALA B N     1 
ATOM   13617 C  CA    . ALA B  1  631  ? 4.477   40.074  51.318  1.00 22.13 ? 629  ALA B CA    1 
ATOM   13618 C  C     . ALA B  1  631  ? 3.549   38.995  51.848  1.00 24.51 ? 629  ALA B C     1 
ATOM   13619 O  O     . ALA B  1  631  ? 2.373   38.979  51.478  1.00 22.37 ? 629  ALA B O     1 
ATOM   13620 C  CB    . ALA B  1  631  ? 4.691   39.871  49.813  1.00 22.43 ? 629  ALA B CB    1 
ATOM   13621 N  N     . VAL B  1  632  ? 4.035   38.106  52.708  1.00 21.38 ? 630  VAL B N     1 
ATOM   13622 C  CA    . VAL B  1  632  ? 3.156   37.150  53.365  1.00 19.50 ? 630  VAL B CA    1 
ATOM   13623 C  C     . VAL B  1  632  ? 2.360   37.949  54.389  1.00 21.56 ? 630  VAL B C     1 
ATOM   13624 O  O     . VAL B  1  632  ? 2.969   38.639  55.224  1.00 22.19 ? 630  VAL B O     1 
ATOM   13625 C  CB    . VAL B  1  632  ? 3.943   36.011  54.027  1.00 22.74 ? 630  VAL B CB    1 
ATOM   13626 C  CG1   . VAL B  1  632  ? 3.001   35.119  54.811  1.00 19.56 ? 630  VAL B CG1   1 
ATOM   13627 C  CG2   . VAL B  1  632  ? 4.712   35.214  52.966  1.00 21.65 ? 630  VAL B CG2   1 
ATOM   13628 N  N     . PRO B  1  633  ? 1.031   37.901  54.358  1.00 20.43 ? 631  PRO B N     1 
ATOM   13629 C  CA    . PRO B  1  633  ? 0.232   38.727  55.264  1.00 17.22 ? 631  PRO B CA    1 
ATOM   13630 C  C     . PRO B  1  633  ? 0.605   38.470  56.709  1.00 19.34 ? 631  PRO B C     1 
ATOM   13631 O  O     . PRO B  1  633  ? 0.902   37.330  57.089  1.00 21.10 ? 631  PRO B O     1 
ATOM   13632 C  CB    . PRO B  1  633  ? -1.205  38.268  54.985  1.00 21.51 ? 631  PRO B CB    1 
ATOM   13633 C  CG    . PRO B  1  633  ? -1.169  37.828  53.571  1.00 27.62 ? 631  PRO B CG    1 
ATOM   13634 C  CD    . PRO B  1  633  ? 0.187   37.178  53.390  1.00 20.13 ? 631  PRO B CD    1 
ATOM   13635 N  N     . PRO B  1  634  ? 0.568   39.501  57.542  1.00 20.34 ? 632  PRO B N     1 
ATOM   13636 C  CA    . PRO B  1  634  ? 0.899   39.307  58.963  1.00 22.30 ? 632  PRO B CA    1 
ATOM   13637 C  C     . PRO B  1  634  ? 0.129   38.176  59.614  1.00 18.10 ? 632  PRO B C     1 
ATOM   13638 O  O     . PRO B  1  634  ? 0.713   37.419  60.400  1.00 19.27 ? 632  PRO B O     1 
ATOM   13639 C  CB    . PRO B  1  634  ? 0.547   40.663  59.587  1.00 21.84 ? 632  PRO B CB    1 
ATOM   13640 C  CG    . PRO B  1  634  ? 0.713   41.644  58.473  1.00 26.20 ? 632  PRO B CG    1 
ATOM   13641 C  CD    . PRO B  1  634  ? 0.325   40.914  57.201  1.00 20.80 ? 632  PRO B CD    1 
ATOM   13642 N  N     . SER B  1  635  ? -1.157  38.030  59.314  1.00 19.79 ? 633  SER B N     1 
ATOM   13643 C  CA    . SER B  1  635  ? -1.926  36.960  59.944  1.00 22.49 ? 633  SER B CA    1 
ATOM   13644 C  C     . SER B  1  635  ? -1.420  35.589  59.517  1.00 20.39 ? 633  SER B C     1 
ATOM   13645 O  O     . SER B  1  635  ? -1.458  34.646  60.314  1.00 19.16 ? 633  SER B O     1 
ATOM   13646 C  CB    . SER B  1  635  ? -3.412  37.099  59.605  1.00 27.70 ? 633  SER B CB    1 
ATOM   13647 O  OG    . SER B  1  635  ? -3.631  36.907  58.221  1.00 31.49 ? 633  SER B OG    1 
ATOM   13648 N  N     . GLU B  1  636  ? -0.933  35.463  58.277  1.00 19.89 ? 634  GLU B N     1 
ATOM   13649 C  CA    . GLU B  1  636  ? -0.388  34.189  57.831  1.00 19.44 ? 634  GLU B CA    1 
ATOM   13650 C  C     . GLU B  1  636  ? 0.999   33.955  58.418  1.00 19.83 ? 634  GLU B C     1 
ATOM   13651 O  O     . GLU B  1  636  ? 1.346   32.816  58.748  1.00 20.05 ? 634  GLU B O     1 
ATOM   13652 C  CB    . GLU B  1  636  ? -0.346  34.127  56.302  1.00 20.53 ? 634  GLU B CB    1 
ATOM   13653 C  CG    . GLU B  1  636  ? 0.312   32.853  55.779  1.00 31.28 ? 634  GLU B CG    1 
ATOM   13654 C  CD    . GLU B  1  636  ? -0.312  31.570  56.339  1.00 39.35 ? 634  GLU B CD    1 
ATOM   13655 O  OE1   . GLU B  1  636  ? -1.560  31.495  56.449  1.00 37.69 ? 634  GLU B OE1   1 
ATOM   13656 O  OE2   . GLU B  1  636  ? 0.455   30.634  56.670  1.00 32.35 ? 634  GLU B OE2   1 
ATOM   13657 N  N     . ARG B  1  637  ? 1.803   35.017  58.560  1.00 16.85 ? 635  ARG B N     1 
ATOM   13658 C  CA    . ARG B  1  637  ? 3.067   34.856  59.268  1.00 16.19 ? 635  ARG B CA    1 
ATOM   13659 C  C     . ARG B  1  637  ? 2.810   34.415  60.702  1.00 16.85 ? 635  ARG B C     1 
ATOM   13660 O  O     . ARG B  1  637  ? 3.494   33.527  61.224  1.00 17.68 ? 635  ARG B O     1 
ATOM   13661 C  CB    . ARG B  1  637  ? 3.872   36.152  59.240  1.00 16.36 ? 635  ARG B CB    1 
ATOM   13662 C  CG    . ARG B  1  637  ? 4.149   36.662  57.824  1.00 17.37 ? 635  ARG B CG    1 
ATOM   13663 C  CD    . ARG B  1  637  ? 5.220   37.749  57.799  1.00 16.80 ? 635  ARG B CD    1 
ATOM   13664 N  NE    . ARG B  1  637  ? 4.869   38.903  58.620  1.00 17.94 ? 635  ARG B NE    1 
ATOM   13665 C  CZ    . ARG B  1  637  ? 4.595   40.114  58.150  1.00 23.31 ? 635  ARG B CZ    1 
ATOM   13666 N  NH1   . ARG B  1  637  ? 4.471   40.345  56.851  1.00 24.57 ? 635  ARG B NH1   1 
ATOM   13667 N  NH2   . ARG B  1  637  ? 4.456   41.123  59.000  1.00 20.49 ? 635  ARG B NH2   1 
ATOM   13668 N  N     . ALA B  1  638  ? 1.810   35.017  61.343  1.00 16.31 ? 636  ALA B N     1 
ATOM   13669 C  CA    . ALA B  1  638  ? 1.444   34.612  62.694  1.00 15.15 ? 636  ALA B CA    1 
ATOM   13670 C  C     . ALA B  1  638  ? 0.968   33.165  62.734  1.00 16.42 ? 636  ALA B C     1 
ATOM   13671 O  O     . ALA B  1  638  ? 1.254   32.449  63.694  1.00 17.49 ? 636  ALA B O     1 
ATOM   13672 C  CB    . ALA B  1  638  ? 0.377   35.558  63.253  1.00 17.51 ? 636  ALA B CB    1 
ATOM   13673 N  N     . ALA B  1  639  ? 0.259   32.706  61.695  1.00 17.19 ? 637  ALA B N     1 
ATOM   13674 C  CA    . ALA B  1  639  ? -0.201  31.318  61.681  1.00 19.26 ? 637  ALA B CA    1 
ATOM   13675 C  C     . ALA B  1  639  ? 0.968   30.339  61.627  1.00 16.34 ? 637  ALA B C     1 
ATOM   13676 O  O     . ALA B  1  639  ? 0.880   29.240  62.188  1.00 16.15 ? 637  ALA B O     1 
ATOM   13677 C  CB    . ALA B  1  639  ? -1.144  31.082  60.500  1.00 16.76 ? 637  ALA B CB    1 
ATOM   13678 N  N     . CYS B  1  640  ? 2.068   30.729  60.974  1.00 16.58 ? 638  CYS B N     1 
ATOM   13679 C  CA    . CYS B  1  640  ? 3.297   29.935  61.016  1.00 17.15 ? 638  CYS B CA    1 
ATOM   13680 C  C     . CYS B  1  640  ? 3.812   29.796  62.437  1.00 14.20 ? 638  CYS B C     1 
ATOM   13681 O  O     . CYS B  1  640  ? 4.181   28.702  62.872  1.00 16.35 ? 638  CYS B O     1 
ATOM   13682 C  CB    . CYS B  1  640  ? 4.386   30.576  60.160  1.00 16.32 ? 638  CYS B CB    1 
ATOM   13683 S  SG    . CYS B  1  640  ? 4.092   30.518  58.402  1.00 19.29 ? 638  CYS B SG    1 
ATOM   13684 N  N     . LEU B  1  641  ? 3.865   30.911  63.174  1.00 16.66 ? 639  LEU B N     1 
ATOM   13685 C  CA    . LEU B  1  641  ? 4.303   30.832  64.562  1.00 15.46 ? 639  LEU B CA    1 
ATOM   13686 C  C     . LEU B  1  641  ? 3.390   29.923  65.367  1.00 13.91 ? 639  LEU B C     1 
ATOM   13687 O  O     . LEU B  1  641  ? 3.868   29.107  66.171  1.00 16.19 ? 639  LEU B O     1 
ATOM   13688 C  CB    . LEU B  1  641  ? 4.347   32.227  65.189  1.00 16.00 ? 639  LEU B CB    1 
ATOM   13689 C  CG    . LEU B  1  641  ? 5.610   33.070  65.020  1.00 17.17 ? 639  LEU B CG    1 
ATOM   13690 C  CD1   . LEU B  1  641  ? 6.010   33.284  63.567  1.00 19.61 ? 639  LEU B CD1   1 
ATOM   13691 C  CD2   . LEU B  1  641  ? 5.430   34.412  65.742  1.00 16.37 ? 639  LEU B CD2   1 
ATOM   13692 N  N     . ASP B  1  642  ? 2.072   30.047  65.168  1.00 15.12 ? 640  ASP B N     1 
ATOM   13693 C  CA    . ASP B  1  642  ? 1.149   29.215  65.928  1.00 16.48 ? 640  ASP B CA    1 
ATOM   13694 C  C     . ASP B  1  642  ? 1.322   27.746  65.569  1.00 16.46 ? 640  ASP B C     1 
ATOM   13695 O  O     . ASP B  1  642  ? 1.256   26.881  66.440  1.00 17.57 ? 640  ASP B O     1 
ATOM   13696 C  CB    . ASP B  1  642  ? -0.295  29.654  65.691  1.00 16.03 ? 640  ASP B CB    1 
ATOM   13697 C  CG    . ASP B  1  642  ? -0.691  30.855  66.512  1.00 19.55 ? 640  ASP B CG    1 
ATOM   13698 O  OD1   . ASP B  1  642  ? -0.029  31.157  67.525  1.00 19.22 ? 640  ASP B OD1   1 
ATOM   13699 O  OD2   . ASP B  1  642  ? -1.696  31.487  66.139  1.00 19.57 ? 640  ASP B OD2   1 
ATOM   13700 N  N     . ARG B  1  643  ? 1.567   27.448  64.294  1.00 16.72 ? 641  ARG B N     1 
ATOM   13701 C  CA    . ARG B  1  643  ? 1.829   26.061  63.916  1.00 16.98 ? 641  ARG B CA    1 
ATOM   13702 C  C     . ARG B  1  643  ? 3.121   25.556  64.546  1.00 17.66 ? 641  ARG B C     1 
ATOM   13703 O  O     . ARG B  1  643  ? 3.183   24.410  65.009  1.00 17.05 ? 641  ARG B O     1 
ATOM   13704 C  CB    . ARG B  1  643  ? 1.885   25.924  62.396  1.00 16.49 ? 641  ARG B CB    1 
ATOM   13705 C  CG    . ARG B  1  643  ? 0.502   25.908  61.760  1.00 19.55 ? 641  ARG B CG    1 
ATOM   13706 C  CD    . ARG B  1  643  ? 0.581   25.489  60.290  1.00 22.56 ? 641  ARG B CD    1 
ATOM   13707 N  NE    . ARG B  1  643  ? 1.283   26.489  59.499  1.00 20.20 ? 641  ARG B NE    1 
ATOM   13708 C  CZ    . ARG B  1  643  ? 0.696   27.514  58.904  1.00 23.13 ? 641  ARG B CZ    1 
ATOM   13709 N  NH1   . ARG B  1  643  ? -0.611  27.703  58.990  1.00 23.21 ? 641  ARG B NH1   1 
ATOM   13710 N  NH2   . ARG B  1  643  ? 1.436   28.363  58.196  1.00 25.51 ? 641  ARG B NH2   1 
ATOM   13711 N  N     . ALA B  1  644  ? 4.159   26.395  64.582  1.00 15.45 ? 642  ALA B N     1 
ATOM   13712 C  CA    . ALA B  1  644  ? 5.399   25.985  65.232  1.00 14.69 ? 642  ALA B CA    1 
ATOM   13713 C  C     . ALA B  1  644  ? 5.172   25.693  66.703  1.00 17.57 ? 642  ALA B C     1 
ATOM   13714 O  O     . ALA B  1  644  ? 5.754   24.751  67.251  1.00 16.66 ? 642  ALA B O     1 
ATOM   13715 C  CB    . ALA B  1  644  ? 6.470   27.060  65.067  1.00 15.62 ? 642  ALA B CB    1 
ATOM   13716 N  N     . ALA B  1  645  ? 4.340   26.505  67.365  1.00 15.93 ? 643  ALA B N     1 
ATOM   13717 C  CA    . ALA B  1  645  ? 4.055   26.271  68.774  1.00 15.90 ? 643  ALA B CA    1 
ATOM   13718 C  C     . ALA B  1  645  ? 3.384   24.924  68.980  1.00 16.85 ? 643  ALA B C     1 
ATOM   13719 O  O     . ALA B  1  645  ? 3.705   24.206  69.940  1.00 18.01 ? 643  ALA B O     1 
ATOM   13720 C  CB    . ALA B  1  645  ? 3.184   27.401  69.318  1.00 17.42 ? 643  ALA B CB    1 
ATOM   13721 N  N     . GLU B  1  646  ? 2.452   24.566  68.085  1.00 16.80 ? 644  GLU B N     1 
ATOM   13722 C  CA    . GLU B  1  646  ? 1.785   23.271  68.180  1.00 18.51 ? 644  GLU B CA    1 
ATOM   13723 C  C     . GLU B  1  646  ? 2.783   22.136  68.031  1.00 17.96 ? 644  GLU B C     1 
ATOM   13724 O  O     . GLU B  1  646  ? 2.689   21.121  68.727  1.00 19.01 ? 644  GLU B O     1 
ATOM   13725 C  CB    . GLU B  1  646  ? 0.711   23.137  67.099  1.00 19.38 ? 644  GLU B CB    1 
ATOM   13726 C  CG    . GLU B  1  646  ? -0.467  24.047  67.272  1.00 25.55 ? 644  GLU B CG    1 
ATOM   13727 C  CD    . GLU B  1  646  ? -1.209  23.782  68.558  1.00 32.59 ? 644  GLU B CD    1 
ATOM   13728 O  OE1   . GLU B  1  646  ? -1.400  22.598  68.902  1.00 38.88 ? 644  GLU B OE1   1 
ATOM   13729 O  OE2   . GLU B  1  646  ? -1.587  24.759  69.235  1.00 37.88 ? 644  GLU B OE2   1 
ATOM   13730 N  N     . LEU B  1  647  ? 3.745   22.291  67.120  1.00 17.43 ? 645  LEU B N     1 
ATOM   13731 C  CA    . LEU B  1  647  ? 4.752   21.248  66.944  1.00 19.61 ? 645  LEU B CA    1 
ATOM   13732 C  C     . LEU B  1  647  ? 5.663   21.141  68.159  1.00 19.58 ? 645  LEU B C     1 
ATOM   13733 O  O     . LEU B  1  647  ? 6.006   20.033  68.590  1.00 18.95 ? 645  LEU B O     1 
ATOM   13734 C  CB    . LEU B  1  647  ? 5.578   21.521  65.694  1.00 18.22 ? 645  LEU B CB    1 
ATOM   13735 C  CG    . LEU B  1  647  ? 4.796   21.473  64.387  1.00 19.17 ? 645  LEU B CG    1 
ATOM   13736 C  CD1   . LEU B  1  647  ? 5.724   21.809  63.227  1.00 18.58 ? 645  LEU B CD1   1 
ATOM   13737 C  CD2   . LEU B  1  647  ? 4.131   20.108  64.215  1.00 22.66 ? 645  LEU B CD2   1 
ATOM   13738 N  N     . MET B  1  648  ? 6.068   22.275  68.730  1.00 16.80 ? 646  MET B N     1 
ATOM   13739 C  CA    . MET B  1  648  ? 6.917   22.215  69.914  1.00 14.86 ? 646  MET B CA    1 
ATOM   13740 C  C     . MET B  1  648  ? 6.161   21.625  71.094  1.00 17.24 ? 646  MET B C     1 
ATOM   13741 O  O     . MET B  1  648  ? 6.745   20.904  71.912  1.00 17.55 ? 646  MET B O     1 
ATOM   13742 C  CB    . MET B  1  648  ? 7.443   23.597  70.280  1.00 17.92 ? 646  MET B CB    1 
ATOM   13743 C  CG    . MET B  1  648  ? 8.431   24.157  69.305  1.00 19.01 ? 646  MET B CG    1 
ATOM   13744 S  SD    . MET B  1  648  ? 9.286   25.526  70.101  1.00 18.45 ? 646  MET B SD    1 
ATOM   13745 C  CE    . MET B  1  648  ? 10.317  26.057  68.754  1.00 21.46 ? 646  MET B CE    1 
ATOM   13746 N  N     . GLN B  1  649  ? 4.863   21.924  71.204  1.00 16.84 ? 647  GLN B N     1 
ATOM   13747 C  CA    . GLN B  1  649  ? 4.073   21.331  72.278  1.00 17.41 ? 647  GLN B CA    1 
ATOM   13748 C  C     . GLN B  1  649  ? 4.013   19.815  72.129  1.00 18.19 ? 647  GLN B C     1 
ATOM   13749 O  O     . GLN B  1  649  ? 4.240   19.072  73.092  1.00 19.61 ? 647  GLN B O     1 
ATOM   13750 C  CB    . GLN B  1  649  ? 2.667   21.932  72.282  1.00 17.88 ? 647  GLN B CB    1 
ATOM   13751 C  CG    . GLN B  1  649  ? 1.826   21.465  73.451  1.00 20.35 ? 647  GLN B CG    1 
ATOM   13752 C  CD    . GLN B  1  649  ? 2.273   22.124  74.741  1.00 18.41 ? 647  GLN B CD    1 
ATOM   13753 O  OE1   . GLN B  1  649  ? 1.958   23.292  74.995  1.00 20.62 ? 647  GLN B OE1   1 
ATOM   13754 N  NE2   . GLN B  1  649  ? 3.030   21.392  75.551  1.00 18.60 ? 647  GLN B NE2   1 
ATOM   13755 N  N     . ALA B  1  650  ? 3.729   19.341  70.915  1.00 17.73 ? 648  ALA B N     1 
ATOM   13756 C  CA    . ALA B  1  650  ? 3.570   17.909  70.681  1.00 19.19 ? 648  ALA B CA    1 
ATOM   13757 C  C     . ALA B  1  650  ? 4.886   17.171  70.837  1.00 21.76 ? 648  ALA B C     1 
ATOM   13758 O  O     . ALA B  1  650  ? 4.908   16.016  71.280  1.00 23.76 ? 648  ALA B O     1 
ATOM   13759 C  CB    . ALA B  1  650  ? 3.005   17.668  69.284  1.00 21.29 ? 648  ALA B CB    1 
ATOM   13760 N  N     . ARG B  1  651  ? 5.988   17.827  70.498  1.00 20.46 ? 649  ARG B N     1 
ATOM   13761 C  CA    . ARG B  1  651  ? 7.311   17.234  70.556  1.00 18.26 ? 649  ARG B CA    1 
ATOM   13762 C  C     . ARG B  1  651  ? 8.070   17.597  71.815  1.00 18.37 ? 649  ARG B C     1 
ATOM   13763 O  O     . ARG B  1  651  ? 9.256   17.283  71.919  1.00 20.35 ? 649  ARG B O     1 
ATOM   13764 C  CB    . ARG B  1  651  ? 8.092   17.652  69.315  1.00 18.92 ? 649  ARG B CB    1 
ATOM   13765 C  CG    . ARG B  1  651  ? 7.358   17.165  68.093  1.00 20.60 ? 649  ARG B CG    1 
ATOM   13766 C  CD    . ARG B  1  651  ? 7.982   17.651  66.810  1.00 20.81 ? 649  ARG B CD    1 
ATOM   13767 N  NE    . ARG B  1  651  ? 7.098   17.312  65.704  1.00 22.71 ? 649  ARG B NE    1 
ATOM   13768 C  CZ    . ARG B  1  651  ? 7.275   17.722  64.458  1.00 22.60 ? 649  ARG B CZ    1 
ATOM   13769 N  NH1   . ARG B  1  651  ? 8.340   18.435  64.110  1.00 20.44 ? 649  ARG B NH1   1 
ATOM   13770 N  NH2   . ARG B  1  651  ? 6.360   17.418  63.543  1.00 21.23 ? 649  ARG B NH2   1 
ATOM   13771 N  N     . MET B  1  652  ? 7.414   18.227  72.789  1.00 16.84 ? 650  MET B N     1 
ATOM   13772 C  CA    . MET B  1  652  ? 8.113   18.614  74.013  1.00 18.18 ? 650  MET B CA    1 
ATOM   13773 C  C     . MET B  1  652  ? 8.942   17.499  74.640  1.00 19.70 ? 650  MET B C     1 
ATOM   13774 O  O     . MET B  1  652  ? 10.081  17.783  75.038  1.00 20.78 ? 650  MET B O     1 
ATOM   13775 C  CB    . MET B  1  652  ? 7.112   19.166  75.036  1.00 18.93 ? 650  MET B CB    1 
ATOM   13776 C  CG    . MET B  1  652  ? 7.755   19.536  76.365  1.00 19.30 ? 650  MET B CG    1 
ATOM   13777 S  SD    . MET B  1  652  ? 6.542   20.227  77.503  1.00 21.67 ? 650  MET B SD    1 
ATOM   13778 C  CE    . MET B  1  652  ? 6.291   21.863  76.845  1.00 21.16 ? 650  MET B CE    1 
ATOM   13779 N  N     . PRO B  1  653  ? 8.478   16.246  74.749  1.00 17.93 ? 651  PRO B N     1 
ATOM   13780 C  CA    . PRO B  1  653  ? 9.326   15.243  75.414  1.00 20.37 ? 651  PRO B CA    1 
ATOM   13781 C  C     . PRO B  1  653  ? 10.657  15.040  74.725  1.00 20.10 ? 651  PRO B C     1 
ATOM   13782 O  O     . PRO B  1  653  ? 11.680  14.909  75.406  1.00 21.27 ? 651  PRO B O     1 
ATOM   13783 C  CB    . PRO B  1  653  ? 8.461   13.978  75.379  1.00 21.96 ? 651  PRO B CB    1 
ATOM   13784 C  CG    . PRO B  1  653  ? 7.064   14.498  75.412  1.00 23.70 ? 651  PRO B CG    1 
ATOM   13785 C  CD    . PRO B  1  653  ? 7.124   15.715  74.507  1.00 19.98 ? 651  PRO B CD    1 
ATOM   13786 N  N     . THR B  1  654  ? 10.671  15.017  73.389  1.00 19.13 ? 652  THR B N     1 
ATOM   13787 C  CA    . THR B  1  654  ? 11.922  14.866  72.655  1.00 20.55 ? 652  THR B CA    1 
ATOM   13788 C  C     . THR B  1  654  ? 12.804  16.102  72.813  1.00 24.02 ? 652  THR B C     1 
ATOM   13789 O  O     . THR B  1  654  ? 14.013  15.986  73.054  1.00 22.10 ? 652  THR B O     1 
ATOM   13790 C  CB    . THR B  1  654  ? 11.624  14.590  71.179  1.00 22.83 ? 652  THR B CB    1 
ATOM   13791 O  OG1   . THR B  1  654  ? 10.823  13.404  71.067  1.00 24.71 ? 652  THR B OG1   1 
ATOM   13792 C  CG2   . THR B  1  654  ? 12.914  14.400  70.388  1.00 23.77 ? 652  THR B CG2   1 
ATOM   13793 N  N     . LEU B  1  655  ? 12.215  17.294  72.712  1.00 20.40 ? 653  LEU B N     1 
ATOM   13794 C  CA    . LEU B  1  655  ? 12.977  18.521  72.931  1.00 19.09 ? 653  LEU B CA    1 
ATOM   13795 C  C     . LEU B  1  655  ? 13.590  18.555  74.323  1.00 21.68 ? 653  LEU B C     1 
ATOM   13796 O  O     . LEU B  1  655  ? 14.725  19.018  74.495  1.00 20.04 ? 653  LEU B O     1 
ATOM   13797 C  CB    . LEU B  1  655  ? 12.083  19.741  72.729  1.00 18.85 ? 653  LEU B CB    1 
ATOM   13798 C  CG    . LEU B  1  655  ? 11.436  19.852  71.352  1.00 20.31 ? 653  LEU B CG    1 
ATOM   13799 C  CD1   . LEU B  1  655  ? 10.555  21.079  71.283  1.00 20.47 ? 653  LEU B CD1   1 
ATOM   13800 C  CD2   . LEU B  1  655  ? 12.508  19.904  70.293  1.00 27.02 ? 653  LEU B CD2   1 
ATOM   13801 N  N     . LEU B  1  656  ? 12.840  18.099  75.334  1.00 21.69 ? 654  LEU B N     1 
ATOM   13802 C  CA    . LEU B  1  656  ? 13.381  18.024  76.693  1.00 22.21 ? 654  LEU B CA    1 
ATOM   13803 C  C     . LEU B  1  656  ? 14.660  17.212  76.727  1.00 21.44 ? 654  LEU B C     1 
ATOM   13804 O  O     . LEU B  1  656  ? 15.648  17.608  77.358  1.00 25.19 ? 654  LEU B O     1 
ATOM   13805 C  CB    . LEU B  1  656  ? 12.370  17.376  77.646  1.00 24.30 ? 654  LEU B CB    1 
ATOM   13806 C  CG    . LEU B  1  656  ? 11.009  18.009  77.811  1.00 26.90 ? 654  LEU B CG    1 
ATOM   13807 C  CD1   . LEU B  1  656  ? 10.227  17.292  78.886  1.00 26.76 ? 654  LEU B CD1   1 
ATOM   13808 C  CD2   . LEU B  1  656  ? 11.174  19.465  78.119  1.00 24.78 ? 654  LEU B CD2   1 
ATOM   13809 N  N     . GLY B  1  657  ? 14.639  16.041  76.094  1.00 22.50 ? 655  GLY B N     1 
ATOM   13810 C  CA    . GLY B  1  657  ? 15.803  15.182  76.129  1.00 22.39 ? 655  GLY B CA    1 
ATOM   13811 C  C     . GLY B  1  657  ? 17.021  15.879  75.578  1.00 22.12 ? 655  GLY B C     1 
ATOM   13812 O  O     . GLY B  1  657  ? 18.119  15.755  76.118  1.00 22.99 ? 655  GLY B O     1 
ATOM   13813 N  N     . LEU B  1  658  ? 16.837  16.648  74.508  1.00 19.96 ? 656  LEU B N     1 
ATOM   13814 C  CA    . LEU B  1  658  ? 17.979  17.327  73.922  1.00 21.18 ? 656  LEU B CA    1 
ATOM   13815 C  C     . LEU B  1  658  ? 18.446  18.469  74.815  1.00 23.55 ? 656  LEU B C     1 
ATOM   13816 O  O     . LEU B  1  658  ? 19.651  18.655  75.017  1.00 23.15 ? 656  LEU B O     1 
ATOM   13817 C  CB    . LEU B  1  658  ? 17.610  17.805  72.516  1.00 19.02 ? 656  LEU B CB    1 
ATOM   13818 C  CG    . LEU B  1  658  ? 18.720  18.494  71.725  1.00 21.14 ? 656  LEU B CG    1 
ATOM   13819 C  CD1   . LEU B  1  658  ? 19.937  17.591  71.586  1.00 20.07 ? 656  LEU B CD1   1 
ATOM   13820 C  CD2   . LEU B  1  658  ? 18.175  18.904  70.359  1.00 20.53 ? 656  LEU B CD2   1 
ATOM   13821 N  N     . ILE B  1  659  ? 17.511  19.226  75.391  1.00 17.81 ? 657  ILE B N     1 
ATOM   13822 C  CA    . ILE B  1  659  ? 17.901  20.353  76.228  1.00 16.08 ? 657  ILE B CA    1 
ATOM   13823 C  C     . ILE B  1  659  ? 18.594  19.867  77.487  1.00 18.71 ? 657  ILE B C     1 
ATOM   13824 O  O     . ILE B  1  659  ? 19.566  20.473  77.960  1.00 20.84 ? 657  ILE B O     1 
ATOM   13825 C  CB    . ILE B  1  659  ? 16.663  21.204  76.553  1.00 20.07 ? 657  ILE B CB    1 
ATOM   13826 C  CG1   . ILE B  1  659  ? 16.142  21.846  75.273  1.00 17.65 ? 657  ILE B CG1   1 
ATOM   13827 C  CG2   . ILE B  1  659  ? 16.977  22.246  77.619  1.00 21.01 ? 657  ILE B CG2   1 
ATOM   13828 C  CD1   . ILE B  1  659  ? 14.721  22.388  75.438  1.00 19.84 ? 657  ILE B CD1   1 
ATOM   13829 N  N     . ILE B  1  660  ? 18.100  18.774  78.060  1.00 17.74 ? 658  ILE B N     1 
ATOM   13830 C  CA    . ILE B  1  660  ? 18.725  18.230  79.261  1.00 18.05 ? 658  ILE B CA    1 
ATOM   13831 C  C     . ILE B  1  660  ? 20.185  17.888  78.990  1.00 20.77 ? 658  ILE B C     1 
ATOM   13832 O  O     . ILE B  1  660  ? 21.080  18.213  79.785  1.00 22.98 ? 658  ILE B O     1 
ATOM   13833 C  CB    . ILE B  1  660  ? 17.933  16.999  79.740  1.00 19.46 ? 658  ILE B CB    1 
ATOM   13834 C  CG1   . ILE B  1  660  ? 16.587  17.437  80.332  1.00 18.88 ? 658  ILE B CG1   1 
ATOM   13835 C  CG2   . ILE B  1  660  ? 18.764  16.166  80.716  1.00 21.41 ? 658  ILE B CG2   1 
ATOM   13836 C  CD1   . ILE B  1  660  ? 15.648  16.260  80.627  1.00 22.00 ? 658  ILE B CD1   1 
ATOM   13837 N  N     . ARG B  1  661  ? 20.449  17.225  77.867  1.00 19.99 ? 659  ARG B N     1 
ATOM   13838 C  CA    . ARG B  1  661  ? 21.785  16.697  77.621  1.00 20.46 ? 659  ARG B CA    1 
ATOM   13839 C  C     . ARG B  1  661  ? 22.704  17.730  76.987  1.00 21.23 ? 659  ARG B C     1 
ATOM   13840 O  O     . ARG B  1  661  ? 23.905  17.724  77.263  1.00 21.44 ? 659  ARG B O     1 
ATOM   13841 C  CB    . ARG B  1  661  ? 21.710  15.439  76.751  1.00 21.55 ? 659  ARG B CB    1 
ATOM   13842 C  CG    . ARG B  1  661  ? 21.140  14.258  77.497  1.00 25.21 ? 659  ARG B CG    1 
ATOM   13843 C  CD    . ARG B  1  661  ? 20.963  13.039  76.603  1.00 26.31 ? 659  ARG B CD    1 
ATOM   13844 N  NE    . ARG B  1  661  ? 22.209  12.591  75.984  1.00 25.91 ? 659  ARG B NE    1 
ATOM   13845 C  CZ    . ARG B  1  661  ? 22.384  12.486  74.673  1.00 28.27 ? 659  ARG B CZ    1 
ATOM   13846 N  NH1   . ARG B  1  661  ? 21.423  12.798  73.819  1.00 29.82 ? 659  ARG B NH1   1 
ATOM   13847 N  NH2   . ARG B  1  661  ? 23.540  12.023  74.206  1.00 27.17 ? 659  ARG B NH2   1 
ATOM   13848 N  N     . GLU B  1  662  ? 22.174  18.627  76.159  1.00 21.43 ? 660  GLU B N     1 
ATOM   13849 C  CA    . GLU B  1  662  ? 23.042  19.606  75.517  1.00 20.24 ? 660  GLU B CA    1 
ATOM   13850 C  C     . GLU B  1  662  ? 23.338  20.779  76.440  1.00 21.77 ? 660  GLU B C     1 
ATOM   13851 O  O     . GLU B  1  662  ? 24.461  21.295  76.450  1.00 22.04 ? 660  GLU B O     1 
ATOM   13852 C  CB    . GLU B  1  662  ? 22.418  20.120  74.213  1.00 22.64 ? 660  GLU B CB    1 
ATOM   13853 C  CG    . GLU B  1  662  ? 23.301  21.166  73.520  1.00 19.24 ? 660  GLU B CG    1 
ATOM   13854 C  CD    . GLU B  1  662  ? 22.739  21.648  72.186  1.00 22.31 ? 660  GLU B CD    1 
ATOM   13855 O  OE1   . GLU B  1  662  ? 21.509  21.796  72.060  1.00 21.79 ? 660  GLU B OE1   1 
ATOM   13856 O  OE2   . GLU B  1  662  ? 23.546  21.879  71.269  1.00 24.15 ? 660  GLU B OE2   1 
ATOM   13857 N  N     . ALA B  1  663  ? 22.360  21.220  77.225  1.00 19.27 ? 661  ALA B N     1 
ATOM   13858 C  CA    . ALA B  1  663  ? 22.516  22.473  77.944  1.00 20.96 ? 661  ALA B CA    1 
ATOM   13859 C  C     . ALA B  1  663  ? 22.639  22.296  79.451  1.00 20.98 ? 661  ALA B C     1 
ATOM   13860 O  O     . ALA B  1  663  ? 22.691  23.294  80.172  1.00 28.04 ? 661  ALA B O     1 
ATOM   13861 C  CB    . ALA B  1  663  ? 21.360  23.419  77.613  1.00 19.95 ? 661  ALA B CB    1 
ATOM   13862 N  N     . GLY B  1  664  ? 22.687  21.059  79.943  1.00 22.45 ? 662  GLY B N     1 
ATOM   13863 C  CA    . GLY B  1  664  ? 22.825  20.863  81.373  1.00 25.60 ? 662  GLY B CA    1 
ATOM   13864 C  C     . GLY B  1  664  ? 21.597  21.169  82.193  1.00 28.03 ? 662  GLY B C     1 
ATOM   13865 O  O     . GLY B  1  664  ? 21.713  21.440  83.390  1.00 26.59 ? 662  GLY B O     1 
ATOM   13866 N  N     . LYS B  1  665  ? 20.415  21.135  81.593  1.00 20.95 ? 663  LYS B N     1 
ATOM   13867 C  CA    A LYS B  1  665  ? 19.200  21.509  82.298  0.49 20.37 ? 663  LYS B CA    1 
ATOM   13868 C  CA    B LYS B  1  665  ? 19.195  21.506  82.290  0.51 20.36 ? 663  LYS B CA    1 
ATOM   13869 C  C     . LYS B  1  665  ? 18.545  20.296  82.938  1.00 17.40 ? 663  LYS B C     1 
ATOM   13870 O  O     . LYS B  1  665  ? 18.627  19.176  82.430  1.00 19.94 ? 663  LYS B O     1 
ATOM   13871 C  CB    A LYS B  1  665  ? 18.187  22.168  81.360  0.49 20.66 ? 663  LYS B CB    1 
ATOM   13872 C  CB    B LYS B  1  665  ? 18.187  22.141  81.335  0.51 20.65 ? 663  LYS B CB    1 
ATOM   13873 C  CG    A LYS B  1  665  ? 18.687  23.396  80.646  0.49 23.53 ? 663  LYS B CG    1 
ATOM   13874 C  CG    B LYS B  1  665  ? 18.705  23.339  80.598  0.51 23.53 ? 663  LYS B CG    1 
ATOM   13875 C  CD    A LYS B  1  665  ? 19.140  24.464  81.615  0.49 18.95 ? 663  LYS B CD    1 
ATOM   13876 C  CD    B LYS B  1  665  ? 18.097  24.607  81.131  0.51 25.55 ? 663  LYS B CD    1 
ATOM   13877 C  CE    A LYS B  1  665  ? 19.505  25.728  80.844  0.49 22.23 ? 663  LYS B CE    1 
ATOM   13878 C  CE    B LYS B  1  665  ? 18.543  25.769  80.284  0.51 23.60 ? 663  LYS B CE    1 
ATOM   13879 N  NZ    A LYS B  1  665  ? 20.099  26.787  81.702  0.49 21.76 ? 663  LYS B NZ    1 
ATOM   13880 N  NZ    B LYS B  1  665  ? 17.487  26.808  80.194  0.51 24.07 ? 663  LYS B NZ    1 
ATOM   13881 N  N     . SER B  1  666  ? 17.865  20.548  84.048  1.00 21.57 ? 664  SER B N     1 
ATOM   13882 C  CA    . SER B  1  666  ? 17.021  19.533  84.641  1.00 22.59 ? 664  SER B CA    1 
ATOM   13883 C  C     . SER B  1  666  ? 15.754  19.394  83.806  1.00 25.27 ? 664  SER B C     1 
ATOM   13884 O  O     . SER B  1  666  ? 15.432  20.253  82.984  1.00 21.22 ? 664  SER B O     1 
ATOM   13885 C  CB    . SER B  1  666  ? 16.662  19.915  86.072  1.00 23.74 ? 664  SER B CB    1 
ATOM   13886 O  OG    . SER B  1  666  ? 15.728  20.980  86.054  1.00 26.09 ? 664  SER B OG    1 
ATOM   13887 N  N     . ALA B  1  667  ? 15.029  18.294  84.022  1.00 22.88 ? 665  ALA B N     1 
ATOM   13888 C  CA    . ALA B  1  667  ? 13.771  18.099  83.306  1.00 21.13 ? 665  ALA B CA    1 
ATOM   13889 C  C     . ALA B  1  667  ? 12.794  19.234  83.578  1.00 20.75 ? 665  ALA B C     1 
ATOM   13890 O  O     . ALA B  1  667  ? 12.155  19.741  82.650  1.00 20.10 ? 665  ALA B O     1 
ATOM   13891 C  CB    . ALA B  1  667  ? 13.150  16.760  83.689  1.00 23.72 ? 665  ALA B CB    1 
ATOM   13892 N  N     . LEU B  1  668  ? 12.664  19.651  84.841  1.00 21.06 ? 666  LEU B N     1 
ATOM   13893 C  CA    A LEU B  1  668  ? 11.753  20.749  85.159  0.50 22.54 ? 666  LEU B CA    1 
ATOM   13894 C  CA    B LEU B  1  668  ? 11.756  20.746  85.165  0.50 22.54 ? 666  LEU B CA    1 
ATOM   13895 C  C     . LEU B  1  668  ? 12.148  22.016  84.420  1.00 20.34 ? 666  LEU B C     1 
ATOM   13896 O  O     . LEU B  1  668  ? 11.292  22.712  83.856  1.00 20.69 ? 666  LEU B O     1 
ATOM   13897 C  CB    A LEU B  1  668  ? 11.729  21.012  86.666  0.50 26.63 ? 666  LEU B CB    1 
ATOM   13898 C  CB    B LEU B  1  668  ? 11.751  20.984  86.675  0.50 26.64 ? 666  LEU B CB    1 
ATOM   13899 C  CG    A LEU B  1  668  ? 10.835  20.146  87.553  0.50 29.17 ? 666  LEU B CG    1 
ATOM   13900 C  CG    B LEU B  1  668  ? 10.432  21.406  87.318  0.50 27.27 ? 666  LEU B CG    1 
ATOM   13901 C  CD1   A LEU B  1  668  ? 11.114  20.458  89.015  0.50 25.83 ? 666  LEU B CD1   1 
ATOM   13902 C  CD1   B LEU B  1  668  ? 9.287   20.507  86.863  0.50 30.68 ? 666  LEU B CD1   1 
ATOM   13903 C  CD2   A LEU B  1  668  ? 9.363   20.354  87.225  0.50 30.99 ? 666  LEU B CD2   1 
ATOM   13904 C  CD2   B LEU B  1  668  ? 10.568  21.366  88.832  0.50 33.45 ? 666  LEU B CD2   1 
ATOM   13905 N  N     . ASN B  1  669  ? 13.444  22.328  84.398  1.00 19.80 ? 667  ASN B N     1 
ATOM   13906 C  CA    . ASN B  1  669  ? 13.885  23.529  83.698  1.00 18.67 ? 667  ASN B CA    1 
ATOM   13907 C  C     . ASN B  1  669  ? 13.691  23.384  82.198  1.00 21.25 ? 667  ASN B C     1 
ATOM   13908 O  O     . ASN B  1  669  ? 13.327  24.353  81.518  1.00 22.00 ? 667  ASN B O     1 
ATOM   13909 C  CB    . ASN B  1  669  ? 15.343  23.820  84.030  1.00 24.76 ? 667  ASN B CB    1 
ATOM   13910 C  CG    . ASN B  1  669  ? 15.534  24.202  85.486  1.00 27.33 ? 667  ASN B CG    1 
ATOM   13911 O  OD1   . ASN B  1  669  ? 14.659  24.802  86.100  1.00 32.60 ? 667  ASN B OD1   1 
ATOM   13912 N  ND2   . ASN B  1  669  ? 16.671  23.849  86.036  1.00 28.82 ? 667  ASN B ND2   1 
ATOM   13913 N  N     . ALA B  1  670  ? 13.914  22.181  81.665  1.00 18.13 ? 668  ALA B N     1 
ATOM   13914 C  CA    . ALA B  1  670  ? 13.734  21.986  80.236  1.00 18.89 ? 668  ALA B CA    1 
ATOM   13915 C  C     . ALA B  1  670  ? 12.273  22.127  79.841  1.00 16.08 ? 668  ALA B C     1 
ATOM   13916 O  O     . ALA B  1  670  ? 11.971  22.666  78.772  1.00 17.60 ? 668  ALA B O     1 
ATOM   13917 C  CB    . ALA B  1  670  ? 14.287  20.624  79.806  1.00 17.00 ? 668  ALA B CB    1 
ATOM   13918 N  N     . ILE B  1  671  ? 11.348  21.640  80.677  1.00 16.98 ? 669  ILE B N     1 
ATOM   13919 C  CA    . ILE B  1  671  ? 9.925   21.837  80.388  1.00 16.99 ? 669  ILE B CA    1 
ATOM   13920 C  C     . ILE B  1  671  ? 9.605   23.323  80.303  1.00 18.33 ? 669  ILE B C     1 
ATOM   13921 O  O     . ILE B  1  671  ? 8.943   23.787  79.365  1.00 18.26 ? 669  ILE B O     1 
ATOM   13922 C  CB    . ILE B  1  671  ? 9.055   21.151  81.456  1.00 18.90 ? 669  ILE B CB    1 
ATOM   13923 C  CG1   . ILE B  1  671  ? 9.156   19.635  81.333  1.00 20.66 ? 669  ILE B CG1   1 
ATOM   13924 C  CG2   . ILE B  1  671  ? 7.614   21.605  81.311  1.00 20.95 ? 669  ILE B CG2   1 
ATOM   13925 C  CD1   . ILE B  1  671  ? 8.634   18.875  82.560  1.00 22.18 ? 669  ILE B CD1   1 
ATOM   13926 N  N     . ALA B  1  672  ? 10.054  24.085  81.301  1.00 17.01 ? 670  ALA B N     1 
ATOM   13927 C  CA    . ALA B  1  672  ? 9.793   25.518  81.321  1.00 20.63 ? 670  ALA B CA    1 
ATOM   13928 C  C     . ALA B  1  672  ? 10.417  26.198  80.114  1.00 19.37 ? 670  ALA B C     1 
ATOM   13929 O  O     . ALA B  1  672  ? 9.856   27.160  79.574  1.00 18.99 ? 670  ALA B O     1 
ATOM   13930 C  CB    . ALA B  1  672  ? 10.329  26.124  82.621  1.00 22.30 ? 670  ALA B CB    1 
ATOM   13931 N  N     . GLU B  1  673  ? 11.583  25.720  79.684  1.00 16.98 ? 671  GLU B N     1 
ATOM   13932 C  CA    . GLU B  1  673  ? 12.236  26.272  78.504  1.00 17.35 ? 671  GLU B CA    1 
ATOM   13933 C  C     . GLU B  1  673  ? 11.375  26.098  77.260  1.00 18.09 ? 671  GLU B C     1 
ATOM   13934 O  O     . GLU B  1  673  ? 11.163  27.051  76.494  1.00 17.44 ? 671  GLU B O     1 
ATOM   13935 C  CB    . GLU B  1  673  ? 13.583  25.583  78.304  1.00 17.86 ? 671  GLU B CB    1 
ATOM   13936 C  CG    . GLU B  1  673  ? 14.333  26.033  77.080  1.00 19.58 ? 671  GLU B CG    1 
ATOM   13937 C  CD    . GLU B  1  673  ? 15.163  27.253  77.324  1.00 26.16 ? 671  GLU B CD    1 
ATOM   13938 O  OE1   . GLU B  1  673  ? 15.266  27.703  78.496  1.00 29.36 ? 671  GLU B OE1   1 
ATOM   13939 O  OE2   . GLU B  1  673  ? 15.721  27.771  76.336  1.00 19.99 ? 671  GLU B OE2   1 
ATOM   13940 N  N     . VAL B  1  674  ? 10.899  24.875  77.022  1.00 16.01 ? 672  VAL B N     1 
ATOM   13941 C  CA    . VAL B  1  674  ? 10.049  24.629  75.866  1.00 15.31 ? 672  VAL B CA    1 
ATOM   13942 C  C     . VAL B  1  674  ? 8.745   25.400  75.986  1.00 14.89 ? 672  VAL B C     1 
ATOM   13943 O  O     . VAL B  1  674  ? 8.258   25.972  75.004  1.00 15.70 ? 672  VAL B O     1 
ATOM   13944 C  CB    . VAL B  1  674  ? 9.802   23.122  75.686  1.00 16.15 ? 672  VAL B CB    1 
ATOM   13945 C  CG1   . VAL B  1  674  ? 8.926   22.881  74.485  1.00 16.37 ? 672  VAL B CG1   1 
ATOM   13946 C  CG2   . VAL B  1  674  ? 11.130  22.393  75.503  1.00 17.95 ? 672  VAL B CG2   1 
ATOM   13947 N  N     . ARG B  1  675  ? 8.160   25.442  77.190  1.00 14.79 ? 673  ARG B N     1 
ATOM   13948 C  CA    . ARG B  1  675  ? 6.951   26.237  77.363  1.00 16.03 ? 673  ARG B CA    1 
ATOM   13949 C  C     . ARG B  1  675  ? 7.188   27.683  76.974  1.00 15.49 ? 673  ARG B C     1 
ATOM   13950 O  O     . ARG B  1  675  ? 6.344   28.299  76.314  1.00 15.22 ? 673  ARG B O     1 
ATOM   13951 C  CB    . ARG B  1  675  ? 6.458   26.172  78.802  1.00 15.82 ? 673  ARG B CB    1 
ATOM   13952 C  CG    . ARG B  1  675  ? 5.871   24.832  79.200  1.00 16.37 ? 673  ARG B CG    1 
ATOM   13953 C  CD    . ARG B  1  675  ? 5.199   24.987  80.546  1.00 16.01 ? 673  ARG B CD    1 
ATOM   13954 N  NE    . ARG B  1  675  ? 4.041   25.861  80.437  1.00 16.84 ? 673  ARG B NE    1 
ATOM   13955 C  CZ    . ARG B  1  675  ? 3.425   26.416  81.473  1.00 17.77 ? 673  ARG B CZ    1 
ATOM   13956 N  NH1   . ARG B  1  675  ? 3.872   26.265  82.704  1.00 19.33 ? 673  ARG B NH1   1 
ATOM   13957 N  NH2   . ARG B  1  675  ? 2.339   27.149  81.262  1.00 17.22 ? 673  ARG B NH2   1 
ATOM   13958 N  N     . GLU B  1  676  ? 8.319   28.243  77.395  1.00 14.79 ? 674  GLU B N     1 
ATOM   13959 C  CA    . GLU B  1  676  ? 8.583   29.646  77.096  1.00 16.59 ? 674  GLU B CA    1 
ATOM   13960 C  C     . GLU B  1  676  ? 8.698   29.858  75.596  1.00 14.78 ? 674  GLU B C     1 
ATOM   13961 O  O     . GLU B  1  676  ? 8.195   30.851  75.068  1.00 14.59 ? 674  GLU B O     1 
ATOM   13962 C  CB    . GLU B  1  676  ? 9.851   30.114  77.813  1.00 16.58 ? 674  GLU B CB    1 
ATOM   13963 C  CG    . GLU B  1  676  ? 10.090  31.623  77.735  1.00 18.51 ? 674  GLU B CG    1 
ATOM   13964 C  CD    . GLU B  1  676  ? 9.464   32.387  78.890  1.00 31.73 ? 674  GLU B CD    1 
ATOM   13965 O  OE1   . GLU B  1  676  ? 8.396   31.966  79.383  1.00 34.65 ? 674  GLU B OE1   1 
ATOM   13966 O  OE2   . GLU B  1  676  ? 10.044  33.414  79.309  1.00 28.47 ? 674  GLU B OE2   1 
ATOM   13967 N  N     . ALA B  1  677  ? 9.316   28.912  74.888  1.00 14.21 ? 675  ALA B N     1 
ATOM   13968 C  CA    . ALA B  1  677  ? 9.396   29.027  73.435  1.00 14.70 ? 675  ALA B CA    1 
ATOM   13969 C  C     . ALA B  1  677  ? 8.006   28.999  72.803  1.00 14.59 ? 675  ALA B C     1 
ATOM   13970 O  O     . ALA B  1  677  ? 7.694   29.807  71.919  1.00 14.95 ? 675  ALA B O     1 
ATOM   13971 C  CB    . ALA B  1  677  ? 10.266  27.902  72.870  1.00 15.30 ? 675  ALA B CB    1 
ATOM   13972 N  N     . ILE B  1  678  ? 7.155   28.072  73.254  1.00 14.54 ? 676  ILE B N     1 
ATOM   13973 C  CA    . ILE B  1  678  ? 5.773   28.002  72.783  1.00 13.18 ? 676  ILE B CA    1 
ATOM   13974 C  C     . ILE B  1  678  ? 5.051   29.311  73.069  1.00 15.22 ? 676  ILE B C     1 
ATOM   13975 O  O     . ILE B  1  678  ? 4.324   29.836  72.216  1.00 15.33 ? 676  ILE B O     1 
ATOM   13976 C  CB    . ILE B  1  678  ? 5.064   26.810  73.453  1.00 14.97 ? 676  ILE B CB    1 
ATOM   13977 C  CG1   . ILE B  1  678  ? 5.643   25.498  72.929  1.00 16.64 ? 676  ILE B CG1   1 
ATOM   13978 C  CG2   . ILE B  1  678  ? 3.532   26.890  73.263  1.00 15.77 ? 676  ILE B CG2   1 
ATOM   13979 C  CD1   . ILE B  1  678  ? 5.362   24.355  73.878  1.00 15.03 ? 676  ILE B CD1   1 
ATOM   13980 N  N     . ASP B  1  679  ? 5.262   29.867  74.261  1.00 14.60 ? 677  ASP B N     1 
ATOM   13981 C  CA    . ASP B  1  679  ? 4.567   31.092  74.632  1.00 14.93 ? 677  ASP B CA    1 
ATOM   13982 C  C     . ASP B  1  679  ? 5.055   32.282  73.820  1.00 14.84 ? 677  ASP B C     1 
ATOM   13983 O  O     . ASP B  1  679  ? 4.242   33.116  73.415  1.00 15.44 ? 677  ASP B O     1 
ATOM   13984 C  CB    . ASP B  1  679  ? 4.719   31.345  76.133  1.00 15.11 ? 677  ASP B CB    1 
ATOM   13985 C  CG    . ASP B  1  679  ? 3.931   30.345  76.979  1.00 17.10 ? 677  ASP B CG    1 
ATOM   13986 O  OD1   . ASP B  1  679  ? 2.854   29.893  76.547  1.00 19.89 ? 677  ASP B OD1   1 
ATOM   13987 O  OD2   . ASP B  1  679  ? 4.399   30.030  78.091  1.00 19.94 ? 677  ASP B OD2   1 
ATOM   13988 N  N     . PHE B  1  680  ? 6.368   32.384  73.571  1.00 13.84 ? 678  PHE B N     1 
ATOM   13989 C  CA    . PHE B  1  680  ? 6.872   33.423  72.669  1.00 15.35 ? 678  PHE B CA    1 
ATOM   13990 C  C     . PHE B  1  680  ? 6.195   33.333  71.313  1.00 16.29 ? 678  PHE B C     1 
ATOM   13991 O  O     . PHE B  1  680  ? 5.733   34.337  70.761  1.00 15.27 ? 678  PHE B O     1 
ATOM   13992 C  CB    . PHE B  1  680  ? 8.382   33.303  72.478  1.00 15.35 ? 678  PHE B CB    1 
ATOM   13993 C  CG    . PHE B  1  680  ? 9.202   33.987  73.542  1.00 13.70 ? 678  PHE B CG    1 
ATOM   13994 C  CD1   . PHE B  1  680  ? 8.950   35.290  73.926  1.00 16.78 ? 678  PHE B CD1   1 
ATOM   13995 C  CD2   . PHE B  1  680  ? 10.249  33.301  74.135  1.00 14.41 ? 678  PHE B CD2   1 
ATOM   13996 C  CE1   . PHE B  1  680  ? 9.749   35.907  74.894  1.00 18.41 ? 678  PHE B CE1   1 
ATOM   13997 C  CE2   . PHE B  1  680  ? 11.041  33.903  75.098  1.00 19.04 ? 678  PHE B CE2   1 
ATOM   13998 C  CZ    . PHE B  1  680  ? 10.788  35.199  75.481  1.00 17.53 ? 678  PHE B CZ    1 
ATOM   13999 N  N     . LEU B  1  681  ? 6.155   32.128  70.747  1.00 14.40 ? 679  LEU B N     1 
ATOM   14000 C  CA    . LEU B  1  681  ? 5.515   31.951  69.449  1.00 13.94 ? 679  LEU B CA    1 
ATOM   14001 C  C     . LEU B  1  681  ? 4.076   32.439  69.474  1.00 15.36 ? 679  LEU B C     1 
ATOM   14002 O  O     . LEU B  1  681  ? 3.660   33.226  68.611  1.00 15.27 ? 679  LEU B O     1 
ATOM   14003 C  CB    . LEU B  1  681  ? 5.578   30.480  69.027  1.00 14.78 ? 679  LEU B CB    1 
ATOM   14004 C  CG    . LEU B  1  681  ? 6.993   30.001  68.703  1.00 13.08 ? 679  LEU B CG    1 
ATOM   14005 C  CD1   . LEU B  1  681  ? 7.062   28.487  68.766  1.00 14.67 ? 679  LEU B CD1   1 
ATOM   14006 C  CD2   . LEU B  1  681  ? 7.434   30.491  67.323  1.00 15.22 ? 679  LEU B CD2   1 
ATOM   14007 N  N     . ARG B  1  682  ? 3.292   31.963  70.443  1.00 14.47 ? 680  ARG B N     1 
ATOM   14008 C  CA    . ARG B  1  682  ? 1.881   32.310  70.469  1.00 14.11 ? 680  ARG B CA    1 
ATOM   14009 C  C     . ARG B  1  682  ? 1.666   33.760  70.858  1.00 15.59 ? 680  ARG B C     1 
ATOM   14010 O  O     . ARG B  1  682  ? 0.722   34.385  70.371  1.00 16.16 ? 680  ARG B O     1 
ATOM   14011 C  CB    . ARG B  1  682  ? 1.136   31.379  71.419  1.00 13.86 ? 680  ARG B CB    1 
ATOM   14012 C  CG    . ARG B  1  682  ? 1.064   29.966  70.880  1.00 15.25 ? 680  ARG B CG    1 
ATOM   14013 C  CD    . ARG B  1  682  ? 0.364   29.095  71.879  1.00 14.88 ? 680  ARG B CD    1 
ATOM   14014 N  NE    . ARG B  1  682  ? 0.147   27.754  71.354  1.00 16.18 ? 680  ARG B NE    1 
ATOM   14015 C  CZ    . ARG B  1  682  ? -0.036  26.686  72.118  1.00 16.51 ? 680  ARG B CZ    1 
ATOM   14016 N  NH1   . ARG B  1  682  ? -0.058  26.775  73.440  1.00 18.25 ? 680  ARG B NH1   1 
ATOM   14017 N  NH2   . ARG B  1  682  ? -0.167  25.497  71.539  1.00 19.07 ? 680  ARG B NH2   1 
ATOM   14018 N  N     . TYR B  1  683  ? 2.516   34.301  71.729  1.00 15.66 ? 681  TYR B N     1 
ATOM   14019 C  CA    . TYR B  1  683  ? 2.369   35.699  72.120  1.00 16.78 ? 681  TYR B CA    1 
ATOM   14020 C  C     . TYR B  1  683  ? 2.679   36.629  70.950  1.00 16.76 ? 681  TYR B C     1 
ATOM   14021 O  O     . TYR B  1  683  ? 1.906   37.544  70.648  1.00 15.62 ? 681  TYR B O     1 
ATOM   14022 C  CB    . TYR B  1  683  ? 3.275   35.997  73.313  1.00 13.84 ? 681  TYR B CB    1 
ATOM   14023 C  CG    . TYR B  1  683  ? 3.231   37.437  73.724  1.00 14.80 ? 681  TYR B CG    1 
ATOM   14024 C  CD1   . TYR B  1  683  ? 2.201   37.905  74.511  1.00 16.40 ? 681  TYR B CD1   1 
ATOM   14025 C  CD2   . TYR B  1  683  ? 4.223   38.320  73.316  1.00 14.08 ? 681  TYR B CD2   1 
ATOM   14026 C  CE1   . TYR B  1  683  ? 2.147   39.239  74.870  1.00 14.40 ? 681  TYR B CE1   1 
ATOM   14027 C  CE2   . TYR B  1  683  ? 4.184   39.648  73.680  1.00 16.09 ? 681  TYR B CE2   1 
ATOM   14028 C  CZ    . TYR B  1  683  ? 3.136   40.094  74.449  1.00 15.59 ? 681  TYR B CZ    1 
ATOM   14029 O  OH    . TYR B  1  683  ? 3.055   41.416  74.826  1.00 17.06 ? 681  TYR B OH    1 
ATOM   14030 N  N     . TYR B  1  684  ? 3.804   36.413  70.264  1.00 14.57 ? 682  TYR B N     1 
ATOM   14031 C  CA    . TYR B  1  684  ? 4.105   37.307  69.150  1.00 14.85 ? 682  TYR B CA    1 
ATOM   14032 C  C     . TYR B  1  684  ? 3.125   37.109  68.004  1.00 15.40 ? 682  TYR B C     1 
ATOM   14033 O  O     . TYR B  1  684  ? 2.835   38.062  67.281  1.00 15.94 ? 682  TYR B O     1 
ATOM   14034 C  CB    . TYR B  1  684  ? 5.545   37.120  68.675  1.00 15.34 ? 682  TYR B CB    1 
ATOM   14035 C  CG    . TYR B  1  684  ? 6.565   37.508  69.708  1.00 14.26 ? 682  TYR B CG    1 
ATOM   14036 C  CD1   . TYR B  1  684  ? 6.399   38.654  70.476  1.00 15.18 ? 682  TYR B CD1   1 
ATOM   14037 C  CD2   . TYR B  1  684  ? 7.683   36.724  69.929  1.00 14.83 ? 682  TYR B CD2   1 
ATOM   14038 C  CE1   . TYR B  1  684  ? 7.330   39.008  71.435  1.00 15.10 ? 682  TYR B CE1   1 
ATOM   14039 C  CE2   . TYR B  1  684  ? 8.624   37.072  70.891  1.00 15.06 ? 682  TYR B CE2   1 
ATOM   14040 C  CZ    . TYR B  1  684  ? 8.436   38.210  71.637  1.00 16.43 ? 682  TYR B CZ    1 
ATOM   14041 O  OH    . TYR B  1  684  ? 9.354   38.549  72.600  1.00 16.62 ? 682  TYR B OH    1 
ATOM   14042 N  N     . ALA B  1  685  ? 2.566   35.905  67.854  1.00 15.23 ? 683  ALA B N     1 
ATOM   14043 C  CA    . ALA B  1  685  ? 1.516   35.695  66.860  1.00 15.18 ? 683  ALA B CA    1 
ATOM   14044 C  C     . ALA B  1  685  ? 0.296   36.542  67.189  1.00 13.84 ? 683  ALA B C     1 
ATOM   14045 O  O     . ALA B  1  685  ? -0.249  37.233  66.320  1.00 15.56 ? 683  ALA B O     1 
ATOM   14046 C  CB    . ALA B  1  685  ? 1.155   34.209  66.784  1.00 14.86 ? 683  ALA B CB    1 
ATOM   14047 N  N     . GLU B  1  686  ? -0.138  36.513  68.449  1.00 14.07 ? 684  GLU B N     1 
ATOM   14048 C  CA    . GLU B  1  686  ? -1.293  37.314  68.822  1.00 16.71 ? 684  GLU B CA    1 
ATOM   14049 C  C     . GLU B  1  686  ? -0.987  38.799  68.733  1.00 17.19 ? 684  GLU B C     1 
ATOM   14050 O  O     . GLU B  1  686  ? -1.801  39.563  68.208  1.00 17.25 ? 684  GLU B O     1 
ATOM   14051 C  CB    . GLU B  1  686  ? -1.763  36.959  70.220  1.00 16.68 ? 684  GLU B CB    1 
ATOM   14052 C  CG    . GLU B  1  686  ? -2.895  37.886  70.702  1.00 18.34 ? 684  GLU B CG    1 
ATOM   14053 C  CD    . GLU B  1  686  ? -4.200  37.787  69.896  1.00 24.63 ? 684  GLU B CD    1 
ATOM   14054 O  OE1   . GLU B  1  686  ? -4.366  36.911  69.007  1.00 22.84 ? 684  GLU B OE1   1 
ATOM   14055 O  OE2   . GLU B  1  686  ? -5.100  38.603  70.179  1.00 25.22 ? 684  GLU B OE2   1 
ATOM   14056 N  N     . GLN B  1  687  ? 0.186   39.230  69.212  1.00 15.67 ? 685  GLN B N     1 
ATOM   14057 C  CA    . GLN B  1  687  ? 0.505   40.654  69.120  1.00 16.96 ? 685  GLN B CA    1 
ATOM   14058 C  C     . GLN B  1  687  ? 0.500   41.116  67.672  1.00 15.66 ? 685  GLN B C     1 
ATOM   14059 O  O     . GLN B  1  687  ? 0.028   42.218  67.365  1.00 18.13 ? 685  GLN B O     1 
ATOM   14060 C  CB    . GLN B  1  687  ? 1.852   40.953  69.771  1.00 18.10 ? 685  GLN B CB    1 
ATOM   14061 C  CG    . GLN B  1  687  ? 1.812   40.774  71.288  1.00 16.71 ? 685  GLN B CG    1 
ATOM   14062 C  CD    . GLN B  1  687  ? 0.775   41.652  71.940  1.00 18.77 ? 685  GLN B CD    1 
ATOM   14063 O  OE1   . GLN B  1  687  ? 0.791   42.863  71.773  1.00 18.53 ? 685  GLN B OE1   1 
ATOM   14064 N  NE2   . GLN B  1  687  ? -0.155  41.041  72.677  1.00 23.94 ? 685  GLN B NE2   1 
ATOM   14065 N  N     . THR B  1  688  ? 0.972   40.263  66.764  1.00 13.83 ? 686  THR B N     1 
ATOM   14066 C  CA    . THR B  1  688  ? 0.910   40.587  65.342  1.00 15.79 ? 686  THR B CA    1 
ATOM   14067 C  C     . THR B  1  688  ? -0.533  40.740  64.874  1.00 15.40 ? 686  THR B C     1 
ATOM   14068 O  O     . THR B  1  688  ? -0.882  41.704  64.179  1.00 18.46 ? 686  THR B O     1 
ATOM   14069 C  CB    . THR B  1  688  ? 1.618   39.494  64.542  1.00 15.42 ? 686  THR B CB    1 
ATOM   14070 O  OG1   . THR B  1  688  ? 3.007   39.529  64.849  1.00 16.50 ? 686  THR B OG1   1 
ATOM   14071 C  CG2   . THR B  1  688  ? 1.432   39.722  63.045  1.00 18.49 ? 686  THR B CG2   1 
ATOM   14072 N  N     . ARG B  1  689  ? -1.390  39.788  65.235  1.00 14.45 ? 687  ARG B N     1 
ATOM   14073 C  CA    . ARG B  1  689  ? -2.789  39.871  64.812  1.00 15.61 ? 687  ARG B CA    1 
ATOM   14074 C  C     . ARG B  1  689  ? -3.475  41.109  65.366  1.00 18.79 ? 687  ARG B C     1 
ATOM   14075 O  O     . ARG B  1  689  ? -4.440  41.601  64.772  1.00 19.83 ? 687  ARG B O     1 
ATOM   14076 C  CB    . ARG B  1  689  ? -3.539  38.622  65.254  1.00 17.78 ? 687  ARG B CB    1 
ATOM   14077 C  CG    . ARG B  1  689  ? -3.220  37.390  64.400  1.00 17.27 ? 687  ARG B CG    1 
ATOM   14078 C  CD    . ARG B  1  689  ? -4.144  36.250  64.791  1.00 19.11 ? 687  ARG B CD    1 
ATOM   14079 N  NE    . ARG B  1  689  ? -3.954  35.847  66.178  1.00 19.66 ? 687  ARG B NE    1 
ATOM   14080 C  CZ    . ARG B  1  689  ? -3.182  34.840  66.573  1.00 20.30 ? 687  ARG B CZ    1 
ATOM   14081 N  NH1   . ARG B  1  689  ? -2.509  34.101  65.703  1.00 19.97 ? 687  ARG B NH1   1 
ATOM   14082 N  NH2   . ARG B  1  689  ? -3.112  34.549  67.869  1.00 18.80 ? 687  ARG B NH2   1 
ATOM   14083 N  N     . ARG B  1  690  ? -2.987  41.630  66.492  1.00 15.98 ? 688  ARG B N     1 
ATOM   14084 C  CA    . ARG B  1  690  ? -3.550  42.839  67.079  1.00 16.45 ? 688  ARG B CA    1 
ATOM   14085 C  C     . ARG B  1  690  ? -3.023  44.124  66.458  1.00 17.44 ? 688  ARG B C     1 
ATOM   14086 O  O     . ARG B  1  690  ? -3.653  45.173  66.638  1.00 17.71 ? 688  ARG B O     1 
ATOM   14087 C  CB    . ARG B  1  690  ? -3.251  42.882  68.585  1.00 16.45 ? 688  ARG B CB    1 
ATOM   14088 C  CG    . ARG B  1  690  ? -3.914  41.778  69.381  1.00 17.77 ? 688  ARG B CG    1 
ATOM   14089 C  CD    . ARG B  1  690  ? -5.424  42.009  69.545  1.00 22.37 ? 688  ARG B CD    1 
ATOM   14090 N  NE    . ARG B  1  690  ? -5.688  43.256  70.258  1.00 24.34 ? 688  ARG B NE    1 
ATOM   14091 C  CZ    . ARG B  1  690  ? -6.290  44.308  69.725  1.00 28.31 ? 688  ARG B CZ    1 
ATOM   14092 N  NH1   . ARG B  1  690  ? -6.764  44.279  68.489  1.00 25.25 ? 688  ARG B NH1   1 
ATOM   14093 N  NH2   . ARG B  1  690  ? -6.436  45.411  70.458  1.00 21.55 ? 688  ARG B NH2   1 
ATOM   14094 N  N     . THR B  1  691  ? -1.895  44.083  65.751  1.00 17.13 ? 689  THR B N     1 
ATOM   14095 C  CA    . THR B  1  691  ? -1.245  45.354  65.415  1.00 18.41 ? 689  THR B CA    1 
ATOM   14096 C  C     . THR B  1  691  ? -0.837  45.532  63.958  1.00 20.52 ? 689  THR B C     1 
ATOM   14097 O  O     . THR B  1  691  ? -1.001  46.628  63.428  1.00 22.51 ? 689  THR B O     1 
ATOM   14098 C  CB    . THR B  1  691  ? 0.014   45.574  66.274  1.00 17.40 ? 689  THR B CB    1 
ATOM   14099 O  OG1   . THR B  1  691  ? 0.934   44.477  66.104  1.00 17.48 ? 689  THR B OG1   1 
ATOM   14100 C  CG2   . THR B  1  691  ? -0.375  45.747  67.738  1.00 20.41 ? 689  THR B CG2   1 
ATOM   14101 N  N     . LEU B  1  692  ? -0.230  44.535  63.322  1.00 16.31 ? 690  LEU B N     1 
ATOM   14102 C  CA    . LEU B  1  692  ? 0.532   44.834  62.115  1.00 17.10 ? 690  LEU B CA    1 
ATOM   14103 C  C     . LEU B  1  692  ? -0.358  44.985  60.885  1.00 20.50 ? 690  LEU B C     1 
ATOM   14104 O  O     . LEU B  1  692  ? -1.190  44.123  60.582  1.00 21.04 ? 690  LEU B O     1 
ATOM   14105 C  CB    . LEU B  1  692  ? 1.592   43.762  61.869  1.00 17.66 ? 690  LEU B CB    1 
ATOM   14106 C  CG    . LEU B  1  692  ? 2.681   43.761  62.939  1.00 17.98 ? 690  LEU B CG    1 
ATOM   14107 C  CD1   . LEU B  1  692  ? 3.806   42.804  62.557  1.00 20.25 ? 690  LEU B CD1   1 
ATOM   14108 C  CD2   . LEU B  1  692  ? 3.238   45.158  63.172  1.00 20.03 ? 690  LEU B CD2   1 
ATOM   14109 N  N     . GLY B  1  693  ? -0.148  46.084  60.172  1.00 21.55 ? 691  GLY B N     1 
ATOM   14110 C  CA    . GLY B  1  693  ? -0.871  46.391  58.964  1.00 19.59 ? 691  GLY B CA    1 
ATOM   14111 C  C     . GLY B  1  693  ? 0.098   46.807  57.881  1.00 20.46 ? 691  GLY B C     1 
ATOM   14112 O  O     . GLY B  1  693  ? 1.323   46.788  58.065  1.00 22.47 ? 691  GLY B O     1 
ATOM   14113 N  N     . PRO B  1  694  ? -0.442  47.232  56.736  1.00 23.99 ? 692  PRO B N     1 
ATOM   14114 C  CA    . PRO B  1  694  ? 0.414   47.465  55.560  1.00 26.57 ? 692  PRO B CA    1 
ATOM   14115 C  C     . PRO B  1  694  ? 1.477   48.522  55.779  1.00 25.66 ? 692  PRO B C     1 
ATOM   14116 O  O     . PRO B  1  694  ? 2.563   48.426  55.190  1.00 28.98 ? 692  PRO B O     1 
ATOM   14117 C  CB    . PRO B  1  694  ? -0.588  47.887  54.471  1.00 27.88 ? 692  PRO B CB    1 
ATOM   14118 C  CG    . PRO B  1  694  ? -1.928  47.398  54.946  1.00 30.43 ? 692  PRO B CG    1 
ATOM   14119 C  CD    . PRO B  1  694  ? -1.877  47.406  56.452  1.00 24.50 ? 692  PRO B CD    1 
ATOM   14120 N  N     . GLY B  1  695  ? 1.208   49.524  56.622  1.00 24.18 ? 693  GLY B N     1 
ATOM   14121 C  CA    . GLY B  1  695  ? 2.144   50.600  56.865  1.00 25.94 ? 693  GLY B CA    1 
ATOM   14122 C  C     . GLY B  1  695  ? 3.257   50.292  57.834  1.00 27.99 ? 693  GLY B C     1 
ATOM   14123 O  O     . GLY B  1  695  ? 4.113   51.146  58.077  1.00 25.34 ? 693  GLY B O     1 
ATOM   14124 N  N     . HIS B  1  696  ? 3.263   49.099  58.422  1.00 25.89 ? 694  HIS B N     1 
ATOM   14125 C  CA    . HIS B  1  696  ? 4.318   48.717  59.355  1.00 19.28 ? 694  HIS B CA    1 
ATOM   14126 C  C     . HIS B  1  696  ? 5.302   47.827  58.607  1.00 24.67 ? 694  HIS B C     1 
ATOM   14127 O  O     . HIS B  1  696  ? 5.299   46.603  58.723  1.00 26.06 ? 694  HIS B O     1 
ATOM   14128 C  CB    . HIS B  1  696  ? 3.723   48.029  60.578  1.00 20.76 ? 694  HIS B CB    1 
ATOM   14129 C  CG    . HIS B  1  696  ? 2.607   48.802  61.204  1.00 20.34 ? 694  HIS B CG    1 
ATOM   14130 N  ND1   . HIS B  1  696  ? 1.319   48.321  61.272  1.00 20.51 ? 694  HIS B ND1   1 
ATOM   14131 C  CD2   . HIS B  1  696  ? 2.579   50.033  61.762  1.00 23.39 ? 694  HIS B CD2   1 
ATOM   14132 C  CE1   . HIS B  1  696  ? 0.544   49.220  61.850  1.00 21.99 ? 694  HIS B CE1   1 
ATOM   14133 N  NE2   . HIS B  1  696  ? 1.284   50.268  62.159  1.00 22.21 ? 694  HIS B NE2   1 
ATOM   14134 N  N     . GLY B  1  697  ? 6.157   48.470  57.821  1.00 24.65 ? 695  GLY B N     1 
ATOM   14135 C  CA    . GLY B  1  697  ? 7.055   47.750  56.950  1.00 24.26 ? 695  GLY B CA    1 
ATOM   14136 C  C     . GLY B  1  697  ? 8.186   47.101  57.715  1.00 23.70 ? 695  GLY B C     1 
ATOM   14137 O  O     . GLY B  1  697  ? 8.635   47.600  58.745  1.00 23.53 ? 695  GLY B O     1 
ATOM   14138 N  N     . PRO B  1  698  ? 8.679   45.974  57.221  1.00 22.30 ? 696  PRO B N     1 
ATOM   14139 C  CA    . PRO B  1  698  ? 9.785   45.300  57.908  1.00 19.95 ? 696  PRO B CA    1 
ATOM   14140 C  C     . PRO B  1  698  ? 11.086  46.063  57.746  1.00 20.36 ? 696  PRO B C     1 
ATOM   14141 O  O     . PRO B  1  698  ? 11.254  46.898  56.854  1.00 22.61 ? 696  PRO B O     1 
ATOM   14142 C  CB    . PRO B  1  698  ? 9.863   43.941  57.210  1.00 26.42 ? 696  PRO B CB    1 
ATOM   14143 C  CG    . PRO B  1  698  ? 9.321   44.207  55.851  1.00 33.27 ? 696  PRO B CG    1 
ATOM   14144 C  CD    . PRO B  1  698  ? 8.208   45.212  56.055  1.00 28.13 ? 696  PRO B CD    1 
ATOM   14145 N  N     . LEU B  1  699  ? 12.018  45.761  58.647  1.00 19.42 ? 697  LEU B N     1 
ATOM   14146 C  CA    . LEU B  1  699  ? 13.353  46.328  58.525  1.00 20.51 ? 697  LEU B CA    1 
ATOM   14147 C  C     . LEU B  1  699  ? 14.118  45.688  57.378  1.00 20.12 ? 697  LEU B C     1 
ATOM   14148 O  O     . LEU B  1  699  ? 14.851  46.370  56.656  1.00 21.39 ? 697  LEU B O     1 
ATOM   14149 C  CB    . LEU B  1  699  ? 14.125  46.124  59.817  1.00 19.28 ? 697  LEU B CB    1 
ATOM   14150 C  CG    . LEU B  1  699  ? 13.520  46.739  61.069  1.00 21.46 ? 697  LEU B CG    1 
ATOM   14151 C  CD1   . LEU B  1  699  ? 14.339  46.273  62.255  1.00 21.94 ? 697  LEU B CD1   1 
ATOM   14152 C  CD2   . LEU B  1  699  ? 13.525  48.265  60.949  1.00 25.26 ? 697  LEU B CD2   1 
ATOM   14153 N  N     . GLY B  1  700  ? 13.974  44.375  57.213  1.00 19.00 ? 698  GLY B N     1 
ATOM   14154 C  CA    . GLY B  1  700  ? 14.809  43.615  56.311  1.00 18.13 ? 698  GLY B CA    1 
ATOM   14155 C  C     . GLY B  1  700  ? 15.485  42.504  57.081  1.00 18.92 ? 698  GLY B C     1 
ATOM   14156 O  O     . GLY B  1  700  ? 15.047  42.146  58.178  1.00 18.81 ? 698  GLY B O     1 
ATOM   14157 N  N     . PRO B  1  701  ? 16.569  41.954  56.543  1.00 18.77 ? 699  PRO B N     1 
ATOM   14158 C  CA    . PRO B  1  701  ? 17.282  40.875  57.242  1.00 16.24 ? 699  PRO B CA    1 
ATOM   14159 C  C     . PRO B  1  701  ? 17.673  41.253  58.663  1.00 19.54 ? 699  PRO B C     1 
ATOM   14160 O  O     . PRO B  1  701  ? 18.325  42.266  58.907  1.00 20.13 ? 699  PRO B O     1 
ATOM   14161 C  CB    . PRO B  1  701  ? 18.521  40.653  56.373  1.00 20.06 ? 699  PRO B CB    1 
ATOM   14162 C  CG    . PRO B  1  701  ? 18.098  41.135  54.999  1.00 20.15 ? 699  PRO B CG    1 
ATOM   14163 C  CD    . PRO B  1  701  ? 17.249  42.339  55.296  1.00 19.88 ? 699  PRO B CD    1 
ATOM   14164 N  N     . ILE B  1  702  ? 17.279  40.411  59.606  1.00 18.12 ? 700  ILE B N     1 
ATOM   14165 C  CA    A ILE B  1  702  ? 17.597  40.613  61.010  0.57 16.96 ? 700  ILE B CA    1 
ATOM   14166 C  CA    B ILE B  1  702  ? 17.578  40.602  61.020  0.43 16.98 ? 700  ILE B CA    1 
ATOM   14167 C  C     . ILE B  1  702  ? 18.494  39.476  61.461  1.00 19.45 ? 700  ILE B C     1 
ATOM   14168 O  O     . ILE B  1  702  ? 18.196  38.299  61.221  1.00 17.02 ? 700  ILE B O     1 
ATOM   14169 C  CB    A ILE B  1  702  ? 16.330  40.704  61.874  0.57 16.58 ? 700  ILE B CB    1 
ATOM   14170 C  CB    B ILE B  1  702  ? 16.301  40.619  61.876  0.43 16.61 ? 700  ILE B CB    1 
ATOM   14171 C  CG1   A ILE B  1  702  ? 15.648  42.051  61.632  0.57 19.36 ? 700  ILE B CG1   1 
ATOM   14172 C  CG1   B ILE B  1  702  ? 15.367  41.736  61.421  0.43 19.16 ? 700  ILE B CG1   1 
ATOM   14173 C  CG2   A ILE B  1  702  ? 16.662  40.496  63.358  0.57 19.41 ? 700  ILE B CG2   1 
ATOM   14174 C  CG2   B ILE B  1  702  ? 16.648  40.755  63.364  0.43 19.28 ? 700  ILE B CG2   1 
ATOM   14175 C  CD1   A ILE B  1  702  ? 14.387  42.253  62.421  0.57 16.02 ? 700  ILE B CD1   1 
ATOM   14176 C  CD1   B ILE B  1  702  ? 15.938  43.106  61.573  0.43 19.93 ? 700  ILE B CD1   1 
ATOM   14177 N  N     . VAL B  1  703  ? 19.588  39.836  62.103  1.00 18.16 ? 701  VAL B N     1 
ATOM   14178 C  CA    . VAL B  1  703  ? 20.517  38.884  62.684  1.00 15.54 ? 701  VAL B CA    1 
ATOM   14179 C  C     . VAL B  1  703  ? 20.096  38.654  64.127  1.00 18.00 ? 701  VAL B C     1 
ATOM   14180 O  O     . VAL B  1  703  ? 20.024  39.606  64.908  1.00 18.31 ? 701  VAL B O     1 
ATOM   14181 C  CB    . VAL B  1  703  ? 21.953  39.417  62.601  1.00 17.17 ? 701  VAL B CB    1 
ATOM   14182 C  CG1   . VAL B  1  703  ? 22.882  38.533  63.394  1.00 17.62 ? 701  VAL B CG1   1 
ATOM   14183 C  CG2   . VAL B  1  703  ? 22.372  39.506  61.155  1.00 17.65 ? 701  VAL B CG2   1 
ATOM   14184 N  N     . CYS B  1  704  ? 19.802  37.405  64.477  1.00 15.36 ? 702  CYS B N     1 
ATOM   14185 C  CA    . CYS B  1  704  ? 19.371  37.051  65.824  1.00 14.93 ? 702  CYS B CA    1 
ATOM   14186 C  C     . CYS B  1  704  ? 20.481  36.248  66.468  1.00 16.90 ? 702  CYS B C     1 
ATOM   14187 O  O     . CYS B  1  704  ? 20.790  35.145  66.012  1.00 16.46 ? 702  CYS B O     1 
ATOM   14188 C  CB    . CYS B  1  704  ? 18.072  36.249  65.804  1.00 15.56 ? 702  CYS B CB    1 
ATOM   14189 S  SG    . CYS B  1  704  ? 16.682  37.135  65.113  1.00 16.83 ? 702  CYS B SG    1 
ATOM   14190 N  N     . ILE B  1  705  ? 21.077  36.809  67.519  1.00 15.52 ? 703  ILE B N     1 
ATOM   14191 C  CA    . ILE B  1  705  ? 22.196  36.200  68.212  1.00 15.58 ? 703  ILE B CA    1 
ATOM   14192 C  C     . ILE B  1  705  ? 21.715  35.851  69.611  1.00 16.52 ? 703  ILE B C     1 
ATOM   14193 O  O     . ILE B  1  705  ? 21.249  36.731  70.344  1.00 17.16 ? 703  ILE B O     1 
ATOM   14194 C  CB    . ILE B  1  705  ? 23.408  37.141  68.231  1.00 15.57 ? 703  ILE B CB    1 
ATOM   14195 C  CG1   . ILE B  1  705  ? 23.929  37.318  66.798  1.00 18.52 ? 703  ILE B CG1   1 
ATOM   14196 C  CG2   . ILE B  1  705  ? 24.488  36.567  69.103  1.00 18.90 ? 703  ILE B CG2   1 
ATOM   14197 C  CD1   . ILE B  1  705  ? 24.937  38.435  66.664  1.00 21.17 ? 703  ILE B CD1   1 
ATOM   14198 N  N     . SER B  1  706  ? 21.817  34.576  69.975  1.00 17.19 ? 704  SER B N     1 
ATOM   14199 C  CA    . SER B  1  706  ? 21.168  34.073  71.172  1.00 19.02 ? 704  SER B CA    1 
ATOM   14200 C  C     . SER B  1  706  ? 22.175  33.446  72.121  1.00 17.80 ? 704  SER B C     1 
ATOM   14201 O  O     . SER B  1  706  ? 23.255  33.011  71.707  1.00 18.47 ? 704  SER B O     1 
ATOM   14202 C  CB    . SER B  1  706  ? 20.082  33.050  70.804  1.00 20.19 ? 704  SER B CB    1 
ATOM   14203 O  OG    . SER B  1  706  ? 20.601  32.034  69.985  1.00 18.33 ? 704  SER B OG    1 
ATOM   14204 N  N     . PRO B  1  707  ? 21.857  33.408  73.405  1.00 18.62 ? 705  PRO B N     1 
ATOM   14205 C  CA    . PRO B  1  707  ? 22.779  32.865  74.403  1.00 20.17 ? 705  PRO B CA    1 
ATOM   14206 C  C     . PRO B  1  707  ? 22.601  31.362  74.561  1.00 20.90 ? 705  PRO B C     1 
ATOM   14207 O  O     . PRO B  1  707  ? 21.630  30.767  74.092  1.00 22.58 ? 705  PRO B O     1 
ATOM   14208 C  CB    . PRO B  1  707  ? 22.349  33.596  75.680  1.00 19.61 ? 705  PRO B CB    1 
ATOM   14209 C  CG    . PRO B  1  707  ? 20.878  33.753  75.524  1.00 19.67 ? 705  PRO B CG    1 
ATOM   14210 C  CD    . PRO B  1  707  ? 20.663  34.017  74.026  1.00 22.41 ? 705  PRO B CD    1 
ATOM   14211 N  N     . TRP B  1  708  ? 23.563  30.748  75.256  1.00 18.39 ? 706  TRP B N     1 
ATOM   14212 C  CA    . TRP B  1  708  ? 23.447  29.316  75.481  1.00 18.23 ? 706  TRP B CA    1 
ATOM   14213 C  C     . TRP B  1  708  ? 22.527  28.966  76.633  1.00 20.50 ? 706  TRP B C     1 
ATOM   14214 O  O     . TRP B  1  708  ? 22.101  27.813  76.722  1.00 23.33 ? 706  TRP B O     1 
ATOM   14215 C  CB    . TRP B  1  708  ? 24.811  28.684  75.754  1.00 18.05 ? 706  TRP B CB    1 
ATOM   14216 C  CG    . TRP B  1  708  ? 25.552  29.418  76.796  1.00 23.47 ? 706  TRP B CG    1 
ATOM   14217 C  CD1   . TRP B  1  708  ? 26.452  30.409  76.587  1.00 33.36 ? 706  TRP B CD1   1 
ATOM   14218 C  CD2   . TRP B  1  708  ? 25.462  29.249  78.209  1.00 25.15 ? 706  TRP B CD2   1 
ATOM   14219 N  NE1   . TRP B  1  708  ? 26.925  30.878  77.776  1.00 30.70 ? 706  TRP B NE1   1 
ATOM   14220 C  CE2   . TRP B  1  708  ? 26.328  30.184  78.792  1.00 20.93 ? 706  TRP B CE2   1 
ATOM   14221 C  CE3   . TRP B  1  708  ? 24.737  28.402  79.037  1.00 25.21 ? 706  TRP B CE3   1 
ATOM   14222 C  CZ2   . TRP B  1  708  ? 26.487  30.303  80.176  1.00 31.55 ? 706  TRP B CZ2   1 
ATOM   14223 C  CZ3   . TRP B  1  708  ? 24.897  28.520  80.421  1.00 22.76 ? 706  TRP B CZ3   1 
ATOM   14224 C  CH2   . TRP B  1  708  ? 25.765  29.454  80.970  1.00 32.39 ? 706  TRP B CH2   1 
ATOM   14225 N  N     . ASN B  1  709  ? 22.213  29.908  77.521  1.00 16.35 ? 707  ASN B N     1 
ATOM   14226 C  CA    . ASN B  1  709  ? 21.597  29.479  78.769  1.00 17.61 ? 707  ASN B CA    1 
ATOM   14227 C  C     . ASN B  1  709  ? 20.096  29.276  78.661  1.00 19.47 ? 707  ASN B C     1 
ATOM   14228 O  O     . ASN B  1  709  ? 19.532  28.535  79.463  1.00 21.41 ? 707  ASN B O     1 
ATOM   14229 C  CB    . ASN B  1  709  ? 21.927  30.473  79.887  1.00 15.74 ? 707  ASN B CB    1 
ATOM   14230 C  CG    . ASN B  1  709  ? 21.226  31.794  79.714  1.00 18.91 ? 707  ASN B CG    1 
ATOM   14231 O  OD1   . ASN B  1  709  ? 21.319  32.431  78.669  1.00 26.03 ? 707  ASN B OD1   1 
ATOM   14232 N  ND2   . ASN B  1  709  ? 20.467  32.183  80.718  1.00 23.13 ? 707  ASN B ND2   1 
ATOM   14233 N  N     . PHE B  1  710  ? 19.441  29.901  77.688  1.00 17.35 ? 708  PHE B N     1 
ATOM   14234 C  CA    . PHE B  1  710  ? 18.060  29.598  77.326  1.00 19.15 ? 708  PHE B CA    1 
ATOM   14235 C  C     . PHE B  1  710  ? 18.099  29.259  75.839  1.00 18.10 ? 708  PHE B C     1 
ATOM   14236 O  O     . PHE B  1  710  ? 17.657  30.044  74.987  1.00 17.14 ? 708  PHE B O     1 
ATOM   14237 C  CB    . PHE B  1  710  ? 17.115  30.762  77.624  1.00 16.64 ? 708  PHE B CB    1 
ATOM   14238 C  CG    . PHE B  1  710  ? 17.081  31.183  79.084  1.00 22.79 ? 708  PHE B CG    1 
ATOM   14239 C  CD1   . PHE B  1  710  ? 16.979  30.251  80.099  1.00 29.39 ? 708  PHE B CD1   1 
ATOM   14240 C  CD2   . PHE B  1  710  ? 17.149  32.529  79.432  1.00 26.82 ? 708  PHE B CD2   1 
ATOM   14241 C  CE1   . PHE B  1  710  ? 16.946  30.649  81.434  1.00 23.41 ? 708  PHE B CE1   1 
ATOM   14242 C  CE2   . PHE B  1  710  ? 17.111  32.935  80.759  1.00 24.21 ? 708  PHE B CE2   1 
ATOM   14243 C  CZ    . PHE B  1  710  ? 17.014  31.989  81.763  1.00 25.01 ? 708  PHE B CZ    1 
ATOM   14244 N  N     . PRO B  1  711  ? 18.641  28.085  75.498  1.00 17.83 ? 709  PRO B N     1 
ATOM   14245 C  CA    . PRO B  1  711  ? 19.056  27.817  74.113  1.00 16.49 ? 709  PRO B CA    1 
ATOM   14246 C  C     . PRO B  1  711  ? 17.906  27.538  73.160  1.00 15.90 ? 709  PRO B C     1 
ATOM   14247 O  O     . PRO B  1  711  ? 18.136  27.496  71.946  1.00 18.20 ? 709  PRO B O     1 
ATOM   14248 C  CB    . PRO B  1  711  ? 19.952  26.582  74.261  1.00 19.70 ? 709  PRO B CB    1 
ATOM   14249 C  CG    . PRO B  1  711  ? 19.345  25.873  75.430  1.00 18.99 ? 709  PRO B CG    1 
ATOM   14250 C  CD    . PRO B  1  711  ? 18.966  26.964  76.399  1.00 17.68 ? 709  PRO B CD    1 
ATOM   14251 N  N     . LEU B  1  712  ? 16.692  27.325  73.665  1.00 15.84 ? 710  LEU B N     1 
ATOM   14252 C  CA    . LEU B  1  712  ? 15.508  27.282  72.815  1.00 15.84 ? 710  LEU B CA    1 
ATOM   14253 C  C     . LEU B  1  712  ? 14.595  28.473  73.026  1.00 16.16 ? 710  LEU B C     1 
ATOM   14254 O  O     . LEU B  1  712  ? 14.046  29.005  72.060  1.00 17.09 ? 710  LEU B O     1 
ATOM   14255 C  CB    . LEU B  1  712  ? 14.698  26.005  73.071  1.00 17.63 ? 710  LEU B CB    1 
ATOM   14256 C  CG    . LEU B  1  712  ? 13.481  25.828  72.142  1.00 14.09 ? 710  LEU B CG    1 
ATOM   14257 C  CD1   . LEU B  1  712  ? 13.897  25.691  70.684  1.00 16.02 ? 710  LEU B CD1   1 
ATOM   14258 C  CD2   . LEU B  1  712  ? 12.642  24.626  72.594  1.00 19.06 ? 710  LEU B CD2   1 
ATOM   14259 N  N     . ALA B  1  713  ? 14.418  28.911  74.270  1.00 17.27 ? 711  ALA B N     1 
ATOM   14260 C  CA    . ALA B  1  713  ? 13.396  29.913  74.534  1.00 16.83 ? 711  ALA B CA    1 
ATOM   14261 C  C     . ALA B  1  713  ? 13.793  31.270  73.968  1.00 15.72 ? 711  ALA B C     1 
ATOM   14262 O  O     . ALA B  1  713  ? 13.028  31.874  73.215  1.00 17.60 ? 711  ALA B O     1 
ATOM   14263 C  CB    . ALA B  1  713  ? 13.123  30.011  76.036  1.00 17.31 ? 711  ALA B CB    1 
ATOM   14264 N  N     . ILE B  1  714  ? 14.983  31.769  74.311  1.00 17.00 ? 712  ILE B N     1 
ATOM   14265 C  CA    . ILE B  1  714  ? 15.362  33.085  73.801  1.00 17.55 ? 712  ILE B CA    1 
ATOM   14266 C  C     . ILE B  1  714  ? 15.690  32.997  72.319  1.00 17.93 ? 712  ILE B C     1 
ATOM   14267 O  O     . ILE B  1  714  ? 15.356  33.897  71.535  1.00 16.79 ? 712  ILE B O     1 
ATOM   14268 C  CB    . ILE B  1  714  ? 16.516  33.668  74.630  1.00 17.49 ? 712  ILE B CB    1 
ATOM   14269 C  CG1   . ILE B  1  714  ? 15.943  33.999  76.001  1.00 18.58 ? 712  ILE B CG1   1 
ATOM   14270 C  CG2   . ILE B  1  714  ? 17.107  34.903  73.941  1.00 19.38 ? 712  ILE B CG2   1 
ATOM   14271 C  CD1   . ILE B  1  714  ? 16.787  34.930  76.814  1.00 29.12 ? 712  ILE B CD1   1 
ATOM   14272 N  N     . PHE B  1  715  ? 16.319  31.903  71.913  1.00 17.32 ? 713  PHE B N     1 
ATOM   14273 C  CA    . PHE B  1  715  ? 16.518  31.614  70.501  1.00 15.76 ? 713  PHE B CA    1 
ATOM   14274 C  C     . PHE B  1  715  ? 15.213  31.766  69.733  1.00 15.99 ? 713  PHE B C     1 
ATOM   14275 O  O     . PHE B  1  715  ? 15.129  32.536  68.763  1.00 16.05 ? 713  PHE B O     1 
ATOM   14276 C  CB    . PHE B  1  715  ? 17.074  30.200  70.360  1.00 15.39 ? 713  PHE B CB    1 
ATOM   14277 C  CG    . PHE B  1  715  ? 17.265  29.782  68.948  1.00 14.85 ? 713  PHE B CG    1 
ATOM   14278 C  CD1   . PHE B  1  715  ? 18.375  30.220  68.239  1.00 15.96 ? 713  PHE B CD1   1 
ATOM   14279 C  CD2   . PHE B  1  715  ? 16.326  28.984  68.317  1.00 16.04 ? 713  PHE B CD2   1 
ATOM   14280 C  CE1   . PHE B  1  715  ? 18.558  29.842  66.926  1.00 18.19 ? 713  PHE B CE1   1 
ATOM   14281 C  CE2   . PHE B  1  715  ? 16.507  28.605  66.995  1.00 18.50 ? 713  PHE B CE2   1 
ATOM   14282 C  CZ    . PHE B  1  715  ? 17.617  29.035  66.305  1.00 18.45 ? 713  PHE B CZ    1 
ATOM   14283 N  N     . THR B  1  716  ? 14.169  31.062  70.182  1.00 15.84 ? 714  THR B N     1 
ATOM   14284 C  CA    . THR B  1  716  ? 12.892  31.077  69.474  1.00 13.75 ? 714  THR B CA    1 
ATOM   14285 C  C     . THR B  1  716  ? 12.221  32.436  69.568  1.00 16.27 ? 714  THR B C     1 
ATOM   14286 O  O     . THR B  1  716  ? 11.666  32.925  68.578  1.00 16.23 ? 714  THR B O     1 
ATOM   14287 C  CB    . THR B  1  716  ? 11.966  29.996  70.032  1.00 15.56 ? 714  THR B CB    1 
ATOM   14288 O  OG1   . THR B  1  716  ? 12.578  28.715  69.822  1.00 17.44 ? 714  THR B OG1   1 
ATOM   14289 C  CG2   . THR B  1  716  ? 10.605  30.049  69.346  1.00 17.56 ? 714  THR B CG2   1 
ATOM   14290 N  N     . GLY B  1  717  ? 12.268  33.063  70.748  1.00 15.81 ? 715  GLY B N     1 
ATOM   14291 C  CA    . GLY B  1  717  ? 11.599  34.344  70.919  1.00 15.29 ? 715  GLY B CA    1 
ATOM   14292 C  C     . GLY B  1  717  ? 12.105  35.401  69.957  1.00 14.25 ? 715  GLY B C     1 
ATOM   14293 O  O     . GLY B  1  717  ? 11.317  36.076  69.289  1.00 16.24 ? 715  GLY B O     1 
ATOM   14294 N  N     . GLN B  1  718  ? 13.425  35.566  69.877  1.00 14.57 ? 716  GLN B N     1 
ATOM   14295 C  CA    . GLN B  1  718  ? 13.971  36.603  69.003  1.00 15.55 ? 716  GLN B CA    1 
ATOM   14296 C  C     . GLN B  1  718  ? 13.594  36.329  67.555  1.00 15.74 ? 716  GLN B C     1 
ATOM   14297 O  O     . GLN B  1  718  ? 13.118  37.217  66.838  1.00 15.75 ? 716  GLN B O     1 
ATOM   14298 C  CB    . GLN B  1  718  ? 15.493  36.698  69.150  1.00 15.25 ? 716  GLN B CB    1 
ATOM   14299 C  CG    . GLN B  1  718  ? 15.920  37.168  70.545  1.00 15.90 ? 716  GLN B CG    1 
ATOM   14300 C  CD    . GLN B  1  718  ? 17.406  37.380  70.675  1.00 17.85 ? 716  GLN B CD    1 
ATOM   14301 O  OE1   . GLN B  1  718  ? 17.842  38.336  71.335  1.00 21.01 ? 716  GLN B OE1   1 
ATOM   14302 N  NE2   . GLN B  1  718  ? 18.203  36.498  70.068  1.00 17.67 ? 716  GLN B NE2   1 
ATOM   14303 N  N     . ILE B  1  719  ? 13.768  35.083  67.128  1.00 13.98 ? 717  ILE B N     1 
ATOM   14304 C  CA    . ILE B  1  719  ? 13.537  34.725  65.737  1.00 14.53 ? 717  ILE B CA    1 
ATOM   14305 C  C     . ILE B  1  719  ? 12.072  34.873  65.393  1.00 16.18 ? 717  ILE B C     1 
ATOM   14306 O  O     . ILE B  1  719  ? 11.723  35.389  64.324  1.00 15.81 ? 717  ILE B O     1 
ATOM   14307 C  CB    . ILE B  1  719  ? 14.025  33.293  65.483  1.00 16.61 ? 717  ILE B CB    1 
ATOM   14308 C  CG1   . ILE B  1  719  ? 15.539  33.258  65.548  1.00 15.35 ? 717  ILE B CG1   1 
ATOM   14309 C  CG2   . ILE B  1  719  ? 13.537  32.793  64.154  1.00 22.03 ? 717  ILE B CG2   1 
ATOM   14310 C  CD1   . ILE B  1  719  ? 16.020  31.863  65.711  1.00 22.40 ? 717  ILE B CD1   1 
ATOM   14311 N  N     . ALA B  1  720  ? 11.193  34.420  66.290  1.00 15.16 ? 718  ALA B N     1 
ATOM   14312 C  CA    . ALA B  1  720  ? 9.765   34.467  66.025  1.00 14.50 ? 718  ALA B CA    1 
ATOM   14313 C  C     . ALA B  1  720  ? 9.308   35.897  65.857  1.00 16.17 ? 718  ALA B C     1 
ATOM   14314 O  O     . ALA B  1  720  ? 8.502   36.199  64.964  1.00 16.34 ? 718  ALA B O     1 
ATOM   14315 C  CB    . ALA B  1  720  ? 8.994   33.787  67.155  1.00 15.63 ? 718  ALA B CB    1 
ATOM   14316 N  N     . ALA B  1  721  ? 9.807   36.787  66.720  1.00 14.61 ? 719  ALA B N     1 
ATOM   14317 C  CA    . ALA B  1  721  ? 9.404   38.184  66.646  1.00 15.45 ? 719  ALA B CA    1 
ATOM   14318 C  C     . ALA B  1  721  ? 9.879   38.806  65.346  1.00 15.96 ? 719  ALA B C     1 
ATOM   14319 O  O     . ALA B  1  721  ? 9.116   39.494  64.657  1.00 16.61 ? 719  ALA B O     1 
ATOM   14320 C  CB    . ALA B  1  721  ? 9.965   38.942  67.842  1.00 16.87 ? 719  ALA B CB    1 
ATOM   14321 N  N     . ALA B  1  722  ? 11.143  38.580  64.997  1.00 15.15 ? 720  ALA B N     1 
ATOM   14322 C  CA    . ALA B  1  722  ? 11.660  39.153  63.759  1.00 16.42 ? 720  ALA B CA    1 
ATOM   14323 C  C     . ALA B  1  722  ? 10.885  38.632  62.553  1.00 17.78 ? 720  ALA B C     1 
ATOM   14324 O  O     . ALA B  1  722  ? 10.498  39.403  61.666  1.00 16.20 ? 720  ALA B O     1 
ATOM   14325 C  CB    . ALA B  1  722  ? 13.150  38.840  63.634  1.00 14.79 ? 720  ALA B CB    1 
ATOM   14326 N  N     . LEU B  1  723  ? 10.641  37.319  62.515  1.00 15.50 ? 721  LEU B N     1 
ATOM   14327 C  CA    . LEU B  1  723  ? 9.916   36.719  61.400  1.00 15.22 ? 721  LEU B CA    1 
ATOM   14328 C  C     . LEU B  1  723  ? 8.511   37.270  61.285  1.00 15.80 ? 721  LEU B C     1 
ATOM   14329 O  O     . LEU B  1  723  ? 8.059   37.633  60.191  1.00 17.41 ? 721  LEU B O     1 
ATOM   14330 C  CB    . LEU B  1  723  ? 9.834   35.207  61.575  1.00 15.50 ? 721  LEU B CB    1 
ATOM   14331 C  CG    . LEU B  1  723  ? 11.124  34.442  61.331  1.00 15.12 ? 721  LEU B CG    1 
ATOM   14332 C  CD1   . LEU B  1  723  ? 10.884  33.033  61.780  1.00 16.19 ? 721  LEU B CD1   1 
ATOM   14333 C  CD2   . LEU B  1  723  ? 11.521  34.506  59.873  1.00 18.37 ? 721  LEU B CD2   1 
ATOM   14334 N  N     . VAL B  1  724  ? 7.775   37.284  62.395  1.00 15.77 ? 722  VAL B N     1 
ATOM   14335 C  CA    . VAL B  1  724  ? 6.375   37.635  62.293  1.00 15.22 ? 722  VAL B CA    1 
ATOM   14336 C  C     . VAL B  1  724  ? 6.221   39.113  61.987  1.00 16.14 ? 722  VAL B C     1 
ATOM   14337 O  O     . VAL B  1  724  ? 5.216   39.518  61.391  1.00 17.60 ? 722  VAL B O     1 
ATOM   14338 C  CB    . VAL B  1  724  ? 5.625   37.210  63.568  1.00 15.20 ? 722  VAL B CB    1 
ATOM   14339 C  CG1   . VAL B  1  724  ? 5.818   38.223  64.702  1.00 16.92 ? 722  VAL B CG1   1 
ATOM   14340 C  CG2   . VAL B  1  724  ? 4.154   36.995  63.244  1.00 16.55 ? 722  VAL B CG2   1 
ATOM   14341 N  N     . ALA B  1  725  ? 7.226   39.922  62.322  1.00 15.58 ? 723  ALA B N     1 
ATOM   14342 C  CA    . ALA B  1  725  ? 7.208   41.315  61.904  1.00 16.19 ? 723  ALA B CA    1 
ATOM   14343 C  C     . ALA B  1  725  ? 7.552   41.479  60.428  1.00 20.96 ? 723  ALA B C     1 
ATOM   14344 O  O     . ALA B  1  725  ? 7.549   42.607  59.926  1.00 21.59 ? 723  ALA B O     1 
ATOM   14345 C  CB    . ALA B  1  725  ? 8.157   42.131  62.786  1.00 16.22 ? 723  ALA B CB    1 
ATOM   14346 N  N     . GLY B  1  726  ? 7.827   40.391  59.722  1.00 17.24 ? 724  GLY B N     1 
ATOM   14347 C  CA    . GLY B  1  726  ? 8.029   40.444  58.286  1.00 17.31 ? 724  GLY B CA    1 
ATOM   14348 C  C     . GLY B  1  726  ? 9.472   40.465  57.841  1.00 18.80 ? 724  GLY B C     1 
ATOM   14349 O  O     . GLY B  1  726  ? 9.743   40.825  56.686  1.00 21.42 ? 724  GLY B O     1 
ATOM   14350 N  N     . ASN B  1  727  ? 10.406  40.092  58.713  1.00 17.97 ? 725  ASN B N     1 
ATOM   14351 C  CA    . ASN B  1  727  ? 11.826  40.141  58.445  1.00 17.98 ? 725  ASN B CA    1 
ATOM   14352 C  C     . ASN B  1  727  ? 12.373  38.743  58.251  1.00 17.84 ? 725  ASN B C     1 
ATOM   14353 O  O     . ASN B  1  727  ? 12.104  37.868  59.081  1.00 18.24 ? 725  ASN B O     1 
ATOM   14354 C  CB    . ASN B  1  727  ? 12.575  40.793  59.607  1.00 16.37 ? 725  ASN B CB    1 
ATOM   14355 C  CG    . ASN B  1  727  ? 12.029  42.156  59.963  1.00 19.68 ? 725  ASN B CG    1 
ATOM   14356 O  OD1   . ASN B  1  727  ? 12.278  43.134  59.255  1.00 18.12 ? 725  ASN B OD1   1 
ATOM   14357 N  ND2   . ASN B  1  727  ? 11.282  42.233  61.068  1.00 18.37 ? 725  ASN B ND2   1 
ATOM   14358 N  N     . PRO B  1  728  ? 13.159  38.492  57.210  1.00 16.94 ? 726  PRO B N     1 
ATOM   14359 C  CA    . PRO B  1  728  ? 13.905  37.238  57.171  1.00 16.53 ? 726  PRO B CA    1 
ATOM   14360 C  C     . PRO B  1  728  ? 14.989  37.274  58.232  1.00 17.84 ? 726  PRO B C     1 
ATOM   14361 O  O     . PRO B  1  728  ? 15.489  38.339  58.599  1.00 18.67 ? 726  PRO B O     1 
ATOM   14362 C  CB    . PRO B  1  728  ? 14.489  37.207  55.758  1.00 19.32 ? 726  PRO B CB    1 
ATOM   14363 C  CG    . PRO B  1  728  ? 14.627  38.663  55.389  1.00 21.02 ? 726  PRO B CG    1 
ATOM   14364 C  CD    . PRO B  1  728  ? 13.581  39.441  56.164  1.00 16.99 ? 726  PRO B CD    1 
ATOM   14365 N  N     . VAL B  1  729  ? 15.336  36.092  58.736  1.00 15.73 ? 727  VAL B N     1 
ATOM   14366 C  CA    . VAL B  1  729  ? 16.196  35.968  59.902  1.00 16.58 ? 727  VAL B CA    1 
ATOM   14367 C  C     . VAL B  1  729  ? 17.436  35.152  59.589  1.00 18.50 ? 727  VAL B C     1 
ATOM   14368 O  O     . VAL B  1  729  ? 17.370  34.091  58.950  1.00 17.18 ? 727  VAL B O     1 
ATOM   14369 C  CB    . VAL B  1  729  ? 15.429  35.343  61.077  1.00 15.22 ? 727  VAL B CB    1 
ATOM   14370 C  CG1   . VAL B  1  729  ? 16.407  34.929  62.198  1.00 16.68 ? 727  VAL B CG1   1 
ATOM   14371 C  CG2   . VAL B  1  729  ? 14.404  36.331  61.572  1.00 15.80 ? 727  VAL B CG2   1 
ATOM   14372 N  N     . LEU B  1  730  ? 18.572  35.655  60.069  1.00 17.13 ? 728  LEU B N     1 
ATOM   14373 C  CA    . LEU B  1  730  ? 19.805  34.900  60.190  1.00 16.29 ? 728  LEU B CA    1 
ATOM   14374 C  C     . LEU B  1  730  ? 19.955  34.546  61.663  1.00 16.39 ? 728  LEU B C     1 
ATOM   14375 O  O     . LEU B  1  730  ? 20.189  35.425  62.493  1.00 18.25 ? 728  LEU B O     1 
ATOM   14376 C  CB    . LEU B  1  730  ? 21.004  35.712  59.711  1.00 16.54 ? 728  LEU B CB    1 
ATOM   14377 C  CG    . LEU B  1  730  ? 21.036  36.207  58.270  1.00 17.75 ? 728  LEU B CG    1 
ATOM   14378 C  CD1   . LEU B  1  730  ? 20.587  35.108  57.311  1.00 18.80 ? 728  LEU B CD1   1 
ATOM   14379 C  CD2   . LEU B  1  730  ? 20.171  37.445  58.100  1.00 17.00 ? 728  LEU B CD2   1 
ATOM   14380 N  N     . ALA B  1  731  ? 19.838  33.265  61.984  1.00 15.90 ? 729  ALA B N     1 
ATOM   14381 C  CA    . ALA B  1  731  ? 19.840  32.807  63.371  1.00 13.47 ? 729  ALA B CA    1 
ATOM   14382 C  C     . ALA B  1  731  ? 21.224  32.266  63.707  1.00 17.09 ? 729  ALA B C     1 
ATOM   14383 O  O     . ALA B  1  731  ? 21.658  31.259  63.145  1.00 16.63 ? 729  ALA B O     1 
ATOM   14384 C  CB    . ALA B  1  731  ? 18.763  31.746  63.569  1.00 16.72 ? 729  ALA B CB    1 
ATOM   14385 N  N     . LYS B  1  732  ? 21.921  32.949  64.616  1.00 16.17 ? 730  LYS B N     1 
ATOM   14386 C  CA    . LYS B  1  732  ? 23.252  32.553  65.058  1.00 17.16 ? 730  LYS B CA    1 
ATOM   14387 C  C     . LYS B  1  732  ? 23.155  32.097  66.503  1.00 17.23 ? 730  LYS B C     1 
ATOM   14388 O  O     . LYS B  1  732  ? 23.156  32.935  67.419  1.00 19.60 ? 730  LYS B O     1 
ATOM   14389 C  CB    . LYS B  1  732  ? 24.229  33.718  64.927  1.00 17.73 ? 730  LYS B CB    1 
ATOM   14390 C  CG    . LYS B  1  732  ? 25.647  33.308  64.551  1.00 18.36 ? 730  LYS B CG    1 
ATOM   14391 C  CD    . LYS B  1  732  ? 26.306  32.420  65.607  1.00 21.78 ? 730  LYS B CD    1 
ATOM   14392 C  CE    . LYS B  1  732  ? 26.541  33.155  66.925  1.00 18.76 ? 730  LYS B CE    1 
ATOM   14393 N  NZ    . LYS B  1  732  ? 27.273  32.262  67.865  1.00 21.86 ? 730  LYS B NZ    1 
ATOM   14394 N  N     . PRO B  1  733  ? 23.033  30.804  66.758  1.00 18.32 ? 731  PRO B N     1 
ATOM   14395 C  CA    . PRO B  1  733  ? 22.932  30.325  68.136  1.00 17.98 ? 731  PRO B CA    1 
ATOM   14396 C  C     . PRO B  1  733  ? 24.295  30.318  68.794  1.00 17.19 ? 731  PRO B C     1 
ATOM   14397 O  O     . PRO B  1  733  ? 25.338  30.337  68.145  1.00 17.43 ? 731  PRO B O     1 
ATOM   14398 C  CB    . PRO B  1  733  ? 22.415  28.895  67.974  1.00 18.04 ? 731  PRO B CB    1 
ATOM   14399 C  CG    . PRO B  1  733  ? 23.050  28.453  66.685  1.00 20.58 ? 731  PRO B CG    1 
ATOM   14400 C  CD    . PRO B  1  733  ? 22.972  29.695  65.793  1.00 20.07 ? 731  PRO B CD    1 
ATOM   14401 N  N     . ALA B  1  734  ? 24.254  30.291  70.117  1.00 18.44 ? 732  ALA B N     1 
ATOM   14402 C  CA    . ALA B  1  734  ? 25.481  30.171  70.892  1.00 17.23 ? 732  ALA B CA    1 
ATOM   14403 C  C     . ALA B  1  734  ? 26.278  28.945  70.458  1.00 19.73 ? 732  ALA B C     1 
ATOM   14404 O  O     . ALA B  1  734  ? 25.717  27.896  70.118  1.00 20.62 ? 732  ALA B O     1 
ATOM   14405 C  CB    . ALA B  1  734  ? 25.154  30.064  72.376  1.00 18.60 ? 732  ALA B CB    1 
ATOM   14406 N  N     . GLU B  1  735  ? 27.602  29.069  70.506  1.00 18.72 ? 733  GLU B N     1 
ATOM   14407 C  CA    . GLU B  1  735  ? 28.448  27.963  70.088  1.00 17.04 ? 733  GLU B CA    1 
ATOM   14408 C  C     . GLU B  1  735  ? 28.261  26.738  70.976  1.00 19.53 ? 733  GLU B C     1 
ATOM   14409 O  O     . GLU B  1  735  ? 28.445  25.609  70.508  1.00 19.67 ? 733  GLU B O     1 
ATOM   14410 C  CB    . GLU B  1  735  ? 29.909  28.411  70.067  1.00 23.13 ? 733  GLU B CB    1 
ATOM   14411 C  CG    . GLU B  1  735  ? 30.396  29.022  71.374  1.00 30.16 ? 733  GLU B CG    1 
ATOM   14412 C  CD    . GLU B  1  735  ? 30.268  30.555  71.437  1.00 38.29 ? 733  GLU B CD    1 
ATOM   14413 O  OE1   . GLU B  1  735  ? 29.269  31.130  70.926  1.00 28.86 ? 733  GLU B OE1   1 
ATOM   14414 O  OE2   . GLU B  1  735  ? 31.187  31.189  72.012  1.00 34.36 ? 733  GLU B OE2   1 
ATOM   14415 N  N     . GLU B  1  736  ? 27.835  26.939  72.223  1.00 20.33 ? 734  GLU B N     1 
ATOM   14416 C  CA    . GLU B  1  736  ? 27.690  25.832  73.151  1.00 19.28 ? 734  GLU B CA    1 
ATOM   14417 C  C     . GLU B  1  736  ? 26.457  24.982  72.869  1.00 21.19 ? 734  GLU B C     1 
ATOM   14418 O  O     . GLU B  1  736  ? 26.432  23.801  73.225  1.00 21.12 ? 734  GLU B O     1 
ATOM   14419 C  CB    . GLU B  1  736  ? 27.614  26.374  74.572  1.00 19.96 ? 734  GLU B CB    1 
ATOM   14420 C  CG    . GLU B  1  736  ? 28.901  27.031  75.039  1.00 22.34 ? 734  GLU B CG    1 
ATOM   14421 C  CD    . GLU B  1  736  ? 28.932  28.536  74.820  1.00 26.32 ? 734  GLU B CD    1 
ATOM   14422 O  OE1   . GLU B  1  736  ? 28.115  29.074  74.035  1.00 22.01 ? 734  GLU B OE1   1 
ATOM   14423 O  OE2   . GLU B  1  736  ? 29.794  29.185  75.449  1.00 31.72 ? 734  GLU B OE2   1 
ATOM   14424 N  N     . THR B  1  737  ? 25.412  25.557  72.271  1.00 21.07 ? 735  THR B N     1 
ATOM   14425 C  CA    . THR B  1  737  ? 24.106  24.892  72.212  1.00 18.12 ? 735  THR B CA    1 
ATOM   14426 C  C     . THR B  1  737  ? 23.488  24.973  70.819  1.00 19.83 ? 735  THR B C     1 
ATOM   14427 O  O     . THR B  1  737  ? 22.347  25.401  70.660  1.00 19.44 ? 735  THR B O     1 
ATOM   14428 C  CB    . THR B  1  737  ? 23.155  25.492  73.244  1.00 20.29 ? 735  THR B CB    1 
ATOM   14429 O  OG1   . THR B  1  737  ? 23.100  26.918  73.089  1.00 19.20 ? 735  THR B OG1   1 
ATOM   14430 C  CG2   . THR B  1  737  ? 23.610  25.160  74.642  1.00 19.99 ? 735  THR B CG2   1 
ATOM   14431 N  N     . PRO B  1  738  ? 24.200  24.519  69.791  1.00 18.70 ? 736  PRO B N     1 
ATOM   14432 C  CA    . PRO B  1  738  ? 23.641  24.608  68.434  1.00 17.07 ? 736  PRO B CA    1 
ATOM   14433 C  C     . PRO B  1  738  ? 22.573  23.572  68.138  1.00 20.57 ? 736  PRO B C     1 
ATOM   14434 O  O     . PRO B  1  738  ? 21.773  23.794  67.226  1.00 19.11 ? 736  PRO B O     1 
ATOM   14435 C  CB    . PRO B  1  738  ? 24.865  24.383  67.544  1.00 18.41 ? 736  PRO B CB    1 
ATOM   14436 C  CG    . PRO B  1  738  ? 25.671  23.387  68.344  1.00 20.58 ? 736  PRO B CG    1 
ATOM   14437 C  CD    . PRO B  1  738  ? 25.522  23.856  69.787  1.00 18.43 ? 736  PRO B CD    1 
ATOM   14438 N  N     . LEU B  1  739  ? 22.539  22.443  68.853  1.00 17.41 ? 737  LEU B N     1 
ATOM   14439 C  CA    . LEU B  1  739  ? 21.655  21.357  68.431  1.00 16.69 ? 737  LEU B CA    1 
ATOM   14440 C  C     . LEU B  1  739  ? 20.193  21.704  68.666  1.00 17.55 ? 737  LEU B C     1 
ATOM   14441 O  O     . LEU B  1  739  ? 19.348  21.476  67.791  1.00 18.43 ? 737  LEU B O     1 
ATOM   14442 C  CB    . LEU B  1  739  ? 22.019  20.065  69.153  1.00 16.01 ? 737  LEU B CB    1 
ATOM   14443 C  CG    . LEU B  1  739  ? 23.453  19.605  68.926  1.00 16.47 ? 737  LEU B CG    1 
ATOM   14444 C  CD1   . LEU B  1  739  ? 23.702  18.387  69.817  1.00 19.03 ? 737  LEU B CD1   1 
ATOM   14445 C  CD2   . LEU B  1  739  ? 23.728  19.268  67.450  1.00 17.75 ? 737  LEU B CD2   1 
ATOM   14446 N  N     . ILE B  1  740  ? 19.865  22.238  69.846  1.00 17.47 ? 738  ILE B N     1 
ATOM   14447 C  CA    . ILE B  1  740  ? 18.474  22.596  70.098  1.00 16.82 ? 738  ILE B CA    1 
ATOM   14448 C  C     . ILE B  1  740  ? 18.069  23.755  69.198  1.00 17.02 ? 738  ILE B C     1 
ATOM   14449 O  O     . ILE B  1  740  ? 16.913  23.847  68.773  1.00 18.00 ? 738  ILE B O     1 
ATOM   14450 C  CB    . ILE B  1  740  ? 18.243  22.904  71.589  1.00 21.23 ? 738  ILE B CB    1 
ATOM   14451 C  CG1   . ILE B  1  740  ? 16.745  23.097  71.876  1.00 18.63 ? 738  ILE B CG1   1 
ATOM   14452 C  CG2   . ILE B  1  740  ? 19.035  24.131  72.007  1.00 20.53 ? 738  ILE B CG2   1 
ATOM   14453 C  CD1   . ILE B  1  740  ? 15.911  21.875  71.575  1.00 22.30 ? 738  ILE B CD1   1 
ATOM   14454 N  N     . ALA B  1  741  ? 19.019  24.629  68.853  1.00 17.44 ? 739  ALA B N     1 
ATOM   14455 C  CA    . ALA B  1  741  ? 18.720  25.709  67.916  1.00 19.36 ? 739  ALA B CA    1 
ATOM   14456 C  C     . ALA B  1  741  ? 18.372  25.151  66.545  1.00 16.50 ? 739  ALA B C     1 
ATOM   14457 O  O     . ALA B  1  741  ? 17.388  25.577  65.923  1.00 18.21 ? 739  ALA B O     1 
ATOM   14458 C  CB    . ALA B  1  741  ? 19.910  26.660  67.813  1.00 18.96 ? 739  ALA B CB    1 
ATOM   14459 N  N     . ALA B  1  742  ? 19.175  24.198  66.057  1.00 17.39 ? 740  ALA B N     1 
ATOM   14460 C  CA    . ALA B  1  742  ? 18.872  23.551  64.785  1.00 17.20 ? 740  ALA B CA    1 
ATOM   14461 C  C     . ALA B  1  742  ? 17.480  22.945  64.808  1.00 17.76 ? 740  ALA B C     1 
ATOM   14462 O  O     . ALA B  1  742  ? 16.739  23.023  63.822  1.00 18.12 ? 740  ALA B O     1 
ATOM   14463 C  CB    . ALA B  1  742  ? 19.909  22.475  64.461  1.00 19.03 ? 740  ALA B CB    1 
ATOM   14464 N  N     . GLU B  1  743  ? 17.108  22.346  65.931  1.00 18.05 ? 741  GLU B N     1 
ATOM   14465 C  CA    . GLU B  1  743  ? 15.792  21.738  66.034  1.00 16.57 ? 741  GLU B CA    1 
ATOM   14466 C  C     . GLU B  1  743  ? 14.706  22.800  66.005  1.00 16.33 ? 741  GLU B C     1 
ATOM   14467 O  O     . GLU B  1  743  ? 13.675  22.617  65.348  1.00 17.73 ? 741  GLU B O     1 
ATOM   14468 C  CB    . GLU B  1  743  ? 15.727  20.889  67.306  1.00 18.71 ? 741  GLU B CB    1 
ATOM   14469 C  CG    . GLU B  1  743  ? 14.395  20.204  67.501  1.00 19.81 ? 741  GLU B CG    1 
ATOM   14470 C  CD    . GLU B  1  743  ? 14.059  19.156  66.450  1.00 24.16 ? 741  GLU B CD    1 
ATOM   14471 O  OE1   . GLU B  1  743  ? 14.930  18.756  65.640  1.00 20.76 ? 741  GLU B OE1   1 
ATOM   14472 O  OE2   . GLU B  1  743  ? 12.893  18.713  66.449  1.00 25.24 ? 741  GLU B OE2   1 
ATOM   14473 N  N     . GLY B  1  744  ? 14.928  23.931  66.681  1.00 17.86 ? 742  GLY B N     1 
ATOM   14474 C  CA    . GLY B  1  744  ? 13.996  25.037  66.568  1.00 17.57 ? 742  GLY B CA    1 
ATOM   14475 C  C     . GLY B  1  744  ? 13.785  25.484  65.135  1.00 16.58 ? 742  GLY B C     1 
ATOM   14476 O  O     . GLY B  1  744  ? 12.658  25.762  64.723  1.00 17.05 ? 742  GLY B O     1 
ATOM   14477 N  N     . VAL B  1  745  ? 14.870  25.590  64.364  1.00 16.61 ? 743  VAL B N     1 
ATOM   14478 C  CA    . VAL B  1  745  ? 14.745  26.013  62.975  1.00 16.56 ? 743  VAL B CA    1 
ATOM   14479 C  C     . VAL B  1  745  ? 14.012  24.957  62.156  1.00 17.25 ? 743  VAL B C     1 
ATOM   14480 O  O     . VAL B  1  745  ? 13.160  25.293  61.319  1.00 17.92 ? 743  VAL B O     1 
ATOM   14481 C  CB    . VAL B  1  745  ? 16.125  26.347  62.394  1.00 17.43 ? 743  VAL B CB    1 
ATOM   14482 C  CG1   . VAL B  1  745  ? 16.049  26.484  60.873  1.00 16.70 ? 743  VAL B CG1   1 
ATOM   14483 C  CG2   . VAL B  1  745  ? 16.614  27.650  63.020  1.00 20.02 ? 743  VAL B CG2   1 
ATOM   14484 N  N     . ARG B  1  746  ? 14.277  23.666  62.423  1.00 16.90 ? 744  ARG B N     1 
ATOM   14485 C  CA    . ARG B  1  746  ? 13.532  22.608  61.729  1.00 18.20 ? 744  ARG B CA    1 
ATOM   14486 C  C     . ARG B  1  746  ? 12.038  22.775  61.952  1.00 16.00 ? 744  ARG B C     1 
ATOM   14487 O  O     . ARG B  1  746  ? 11.236  22.617  61.024  1.00 17.34 ? 744  ARG B O     1 
ATOM   14488 C  CB    . ARG B  1  746  ? 13.942  21.219  62.229  1.00 17.77 ? 744  ARG B CB    1 
ATOM   14489 C  CG    . ARG B  1  746  ? 15.321  20.765  61.864  1.00 19.23 ? 744  ARG B CG    1 
ATOM   14490 C  CD    . ARG B  1  746  ? 15.542  19.339  62.406  1.00 19.17 ? 744  ARG B CD    1 
ATOM   14491 N  NE    . ARG B  1  746  ? 16.933  18.962  62.239  1.00 21.58 ? 744  ARG B NE    1 
ATOM   14492 C  CZ    . ARG B  1  746  ? 17.853  19.024  63.191  1.00 17.42 ? 744  ARG B CZ    1 
ATOM   14493 N  NH1   . ARG B  1  746  ? 17.526  19.231  64.461  1.00 20.59 ? 744  ARG B NH1   1 
ATOM   14494 N  NH2   . ARG B  1  746  ? 19.134  18.871  62.859  1.00 21.96 ? 744  ARG B NH2   1 
ATOM   14495 N  N     . ILE B  1  747  ? 11.650  23.060  63.194  1.00 16.04 ? 745  ILE B N     1 
ATOM   14496 C  CA    . ILE B  1  747  ? 10.238  23.159  63.522  1.00 15.43 ? 745  ILE B CA    1 
ATOM   14497 C  C     . ILE B  1  747  ? 9.624   24.391  62.881  1.00 17.28 ? 745  ILE B C     1 
ATOM   14498 O  O     . ILE B  1  747  ? 8.513   24.335  62.342  1.00 16.89 ? 745  ILE B O     1 
ATOM   14499 C  CB    . ILE B  1  747  ? 10.065  23.161  65.049  1.00 17.14 ? 745  ILE B CB    1 
ATOM   14500 C  CG1   . ILE B  1  747  ? 10.367  21.755  65.573  1.00 17.52 ? 745  ILE B CG1   1 
ATOM   14501 C  CG2   . ILE B  1  747  ? 8.661   23.652  65.411  1.00 17.68 ? 745  ILE B CG2   1 
ATOM   14502 C  CD1   . ILE B  1  747  ? 10.349  21.611  67.080  1.00 18.42 ? 745  ILE B CD1   1 
ATOM   14503 N  N     . LEU B  1  748  ? 10.329  25.527  62.926  1.00 15.99 ? 746  LEU B N     1 
ATOM   14504 C  CA    . LEU B  1  748  ? 9.773   26.727  62.298  1.00 15.93 ? 746  LEU B CA    1 
ATOM   14505 C  C     . LEU B  1  748  ? 9.645   26.558  60.791  1.00 15.45 ? 746  LEU B C     1 
ATOM   14506 O  O     . LEU B  1  748  ? 8.659   26.999  60.197  1.00 16.09 ? 746  LEU B O     1 
ATOM   14507 C  CB    . LEU B  1  748  ? 10.621  27.947  62.641  1.00 14.89 ? 746  LEU B CB    1 
ATOM   14508 C  CG    . LEU B  1  748  ? 10.303  28.566  64.005  1.00 21.22 ? 746  LEU B CG    1 
ATOM   14509 C  CD1   . LEU B  1  748  ? 11.509  29.402  64.458  1.00 21.12 ? 746  LEU B CD1   1 
ATOM   14510 C  CD2   . LEU B  1  748  ? 9.073   29.420  63.906  1.00 23.12 ? 746  LEU B CD2   1 
ATOM   14511 N  N     . ARG B  1  749  ? 10.628  25.916  60.152  1.00 15.45 ? 747  ARG B N     1 
ATOM   14512 C  CA    . ARG B  1  749  ? 10.500  25.649  58.725  1.00 18.67 ? 747  ARG B CA    1 
ATOM   14513 C  C     . ARG B  1  749  ? 9.347   24.697  58.449  1.00 15.59 ? 747  ARG B C     1 
ATOM   14514 O  O     . ARG B  1  749  ? 8.575   24.902  57.500  1.00 16.60 ? 747  ARG B O     1 
ATOM   14515 C  CB    . ARG B  1  749  ? 11.809  25.085  58.188  1.00 18.34 ? 747  ARG B CB    1 
ATOM   14516 C  CG    . ARG B  1  749  ? 12.878  26.137  58.018  1.00 18.54 ? 747  ARG B CG    1 
ATOM   14517 C  CD    . ARG B  1  749  ? 14.058  25.567  57.264  1.00 19.80 ? 747  ARG B CD    1 
ATOM   14518 N  NE    . ARG B  1  749  ? 15.086  26.563  56.999  1.00 19.61 ? 747  ARG B NE    1 
ATOM   14519 C  CZ    . ARG B  1  749  ? 16.114  26.336  56.195  1.00 25.61 ? 747  ARG B CZ    1 
ATOM   14520 N  NH1   . ARG B  1  749  ? 16.237  25.188  55.546  1.00 26.85 ? 747  ARG B NH1   1 
ATOM   14521 N  NH2   . ARG B  1  749  ? 17.039  27.280  56.040  1.00 24.65 ? 747  ARG B NH2   1 
ATOM   14522 N  N     . GLU B  1  750  ? 9.207   23.658  59.275  1.00 16.01 ? 748  GLU B N     1 
ATOM   14523 C  CA    . GLU B  1  750  ? 8.119   22.711  59.078  1.00 16.72 ? 748  GLU B CA    1 
ATOM   14524 C  C     . GLU B  1  750  ? 6.772   23.402  59.211  1.00 15.63 ? 748  GLU B C     1 
ATOM   14525 O  O     . GLU B  1  750  ? 5.812   23.052  58.510  1.00 18.36 ? 748  GLU B O     1 
ATOM   14526 C  CB    . GLU B  1  750  ? 8.241   21.575  60.090  1.00 16.41 ? 748  GLU B CB    1 
ATOM   14527 C  CG    . GLU B  1  750  ? 7.165   20.520  59.907  1.00 20.23 ? 748  GLU B CG    1 
ATOM   14528 C  CD    . GLU B  1  750  ? 7.358   19.346  60.839  1.00 19.51 ? 748  GLU B CD    1 
ATOM   14529 O  OE1   . GLU B  1  750  ? 8.435   19.245  61.452  1.00 21.27 ? 748  GLU B OE1   1 
ATOM   14530 O  OE2   . GLU B  1  750  ? 6.421   18.537  60.952  1.00 22.86 ? 748  GLU B OE2   1 
ATOM   14531 N  N     . ALA B  1  751  ? 6.703   24.410  60.080  1.00 16.19 ? 749  ALA B N     1 
ATOM   14532 C  CA    . ALA B  1  751  ? 5.490   25.168  60.334  1.00 16.52 ? 749  ALA B CA    1 
ATOM   14533 C  C     . ALA B  1  751  ? 5.166   26.163  59.236  1.00 19.08 ? 749  ALA B C     1 
ATOM   14534 O  O     . ALA B  1  751  ? 4.107   26.789  59.292  1.00 19.24 ? 749  ALA B O     1 
ATOM   14535 C  CB    . ALA B  1  751  ? 5.620   25.927  61.649  1.00 17.40 ? 749  ALA B CB    1 
ATOM   14536 N  N     . GLY B  1  752  ? 6.060   26.369  58.279  1.00 18.05 ? 750  GLY B N     1 
ATOM   14537 C  CA    . GLY B  1  752  ? 5.729   27.240  57.167  1.00 16.52 ? 750  GLY B CA    1 
ATOM   14538 C  C     . GLY B  1  752  ? 6.726   28.344  56.897  1.00 17.70 ? 750  GLY B C     1 
ATOM   14539 O  O     . GLY B  1  752  ? 6.602   29.056  55.899  1.00 19.11 ? 750  GLY B O     1 
ATOM   14540 N  N     . ILE B  1  753  ? 7.714   28.532  57.767  1.00 16.75 ? 751  ILE B N     1 
ATOM   14541 C  CA    . ILE B  1  753  ? 8.681   29.592  57.497  1.00 17.75 ? 751  ILE B CA    1 
ATOM   14542 C  C     . ILE B  1  753  ? 9.568   29.170  56.333  1.00 17.81 ? 751  ILE B C     1 
ATOM   14543 O  O     . ILE B  1  753  ? 10.230  28.130  56.425  1.00 19.89 ? 751  ILE B O     1 
ATOM   14544 C  CB    . ILE B  1  753  ? 9.545   29.901  58.722  1.00 14.92 ? 751  ILE B CB    1 
ATOM   14545 C  CG1   . ILE B  1  753  ? 8.672   30.244  59.935  1.00 17.90 ? 751  ILE B CG1   1 
ATOM   14546 C  CG2   . ILE B  1  753  ? 10.476  31.041  58.397  1.00 16.90 ? 751  ILE B CG2   1 
ATOM   14547 C  CD1   . ILE B  1  753  ? 7.829   31.530  59.767  1.00 17.50 ? 751  ILE B CD1   1 
ATOM   14548 N  N     . PRO B  1  754  ? 9.616   29.935  55.234  1.00 17.09 ? 752  PRO B N     1 
ATOM   14549 C  CA    . PRO B  1  754  ? 10.435  29.533  54.084  1.00 18.09 ? 752  PRO B CA    1 
ATOM   14550 C  C     . PRO B  1  754  ? 11.908  29.464  54.441  1.00 18.12 ? 752  PRO B C     1 
ATOM   14551 O  O     . PRO B  1  754  ? 12.394  30.192  55.309  1.00 18.14 ? 752  PRO B O     1 
ATOM   14552 C  CB    . PRO B  1  754  ? 10.177  30.643  53.055  1.00 21.62 ? 752  PRO B CB    1 
ATOM   14553 C  CG    . PRO B  1  754  ? 8.898   31.273  53.471  1.00 23.86 ? 752  PRO B CG    1 
ATOM   14554 C  CD    . PRO B  1  754  ? 8.814   31.138  54.962  1.00 17.43 ? 752  PRO B CD    1 
ATOM   14555 N  N     . ALA B  1  755  ? 12.629  28.585  53.734  1.00 22.31 ? 753  ALA B N     1 
ATOM   14556 C  CA    . ALA B  1  755  ? 14.052  28.420  54.010  1.00 23.62 ? 753  ALA B CA    1 
ATOM   14557 C  C     . ALA B  1  755  ? 14.814  29.725  53.816  1.00 19.54 ? 753  ALA B C     1 
ATOM   14558 O  O     . ALA B  1  755  ? 15.747  30.027  54.565  1.00 22.55 ? 753  ALA B O     1 
ATOM   14559 C  CB    . ALA B  1  755  ? 14.634  27.322  53.120  1.00 27.89 ? 753  ALA B CB    1 
ATOM   14560 N  N     . SER B  1  756  ? 14.409  30.535  52.840  1.00 19.90 ? 754  SER B N     1 
ATOM   14561 C  CA    . SER B  1  756  ? 15.080  31.810  52.635  1.00 19.22 ? 754  SER B CA    1 
ATOM   14562 C  C     . SER B  1  756  ? 14.758  32.814  53.730  1.00 21.12 ? 754  SER B C     1 
ATOM   14563 O  O     . SER B  1  756  ? 15.495  33.793  53.891  1.00 20.93 ? 754  SER B O     1 
ATOM   14564 C  CB    . SER B  1  756  ? 14.697  32.378  51.272  1.00 22.53 ? 754  SER B CB    1 
ATOM   14565 O  OG    . SER B  1  756  ? 13.303  32.604  51.228  1.00 27.17 ? 754  SER B OG    1 
ATOM   14566 N  N     . ALA B  1  757  ? 13.669  32.606  54.472  1.00 17.60 ? 755  ALA B N     1 
ATOM   14567 C  CA    . ALA B  1  757  ? 13.318  33.502  55.559  1.00 16.97 ? 755  ALA B CA    1 
ATOM   14568 C  C     . ALA B  1  757  ? 13.963  33.126  56.885  1.00 17.91 ? 755  ALA B C     1 
ATOM   14569 O  O     . ALA B  1  757  ? 13.938  33.942  57.809  1.00 18.68 ? 755  ALA B O     1 
ATOM   14570 C  CB    . ALA B  1  757  ? 11.795  33.559  55.747  1.00 18.83 ? 755  ALA B CB    1 
ATOM   14571 N  N     . LEU B  1  758  ? 14.516  31.920  57.012  1.00 17.05 ? 756  LEU B N     1 
ATOM   14572 C  CA    . LEU B  1  758  ? 15.082  31.494  58.293  1.00 17.07 ? 756  LEU B CA    1 
ATOM   14573 C  C     . LEU B  1  758  ? 16.274  30.596  57.997  1.00 18.40 ? 756  LEU B C     1 
ATOM   14574 O  O     . LEU B  1  758  ? 16.110  29.433  57.616  1.00 19.51 ? 756  LEU B O     1 
ATOM   14575 C  CB    . LEU B  1  758  ? 14.059  30.778  59.165  1.00 15.88 ? 756  LEU B CB    1 
ATOM   14576 C  CG    . LEU B  1  758  ? 14.611  30.229  60.482  1.00 16.94 ? 756  LEU B CG    1 
ATOM   14577 C  CD1   . LEU B  1  758  ? 15.210  31.350  61.322  1.00 18.71 ? 756  LEU B CD1   1 
ATOM   14578 C  CD2   . LEU B  1  758  ? 13.512  29.510  61.273  1.00 18.73 ? 756  LEU B CD2   1 
ATOM   14579 N  N     . GLN B  1  759  ? 17.462  31.151  58.165  1.00 16.51 ? 757  GLN B N     1 
ATOM   14580 C  CA    . GLN B  1  759  ? 18.698  30.428  57.954  1.00 16.37 ? 757  GLN B CA    1 
ATOM   14581 C  C     . GLN B  1  759  ? 19.405  30.296  59.289  1.00 19.09 ? 757  GLN B C     1 
ATOM   14582 O  O     . GLN B  1  759  ? 19.370  31.219  60.107  1.00 19.39 ? 757  GLN B O     1 
ATOM   14583 C  CB    . GLN B  1  759  ? 19.577  31.156  56.943  1.00 17.01 ? 757  GLN B CB    1 
ATOM   14584 C  CG    . GLN B  1  759  ? 18.935  31.190  55.558  1.00 17.61 ? 757  GLN B CG    1 
ATOM   14585 C  CD    . GLN B  1  759  ? 19.695  32.066  54.620  1.00 16.20 ? 757  GLN B CD    1 
ATOM   14586 O  OE1   . GLN B  1  759  ? 20.529  31.602  53.857  1.00 20.88 ? 757  GLN B OE1   1 
ATOM   14587 N  NE2   . GLN B  1  759  ? 19.424  33.359  54.684  1.00 16.71 ? 757  GLN B NE2   1 
ATOM   14588 N  N     . LEU B  1  760  ? 20.000  29.135  59.518  1.00 16.80 ? 758  LEU B N     1 
ATOM   14589 C  CA    . LEU B  1  760  ? 20.727  28.846  60.750  1.00 15.76 ? 758  LEU B CA    1 
ATOM   14590 C  C     . LEU B  1  760  ? 22.219  28.883  60.467  1.00 17.46 ? 758  LEU B C     1 
ATOM   14591 O  O     . LEU B  1  760  ? 22.689  28.193  59.564  1.00 18.36 ? 758  LEU B O     1 
ATOM   14592 C  CB    . LEU B  1  760  ? 20.340  27.475  61.300  1.00 17.50 ? 758  LEU B CB    1 
ATOM   14593 C  CG    . LEU B  1  760  ? 21.041  27.078  62.603  1.00 19.24 ? 758  LEU B CG    1 
ATOM   14594 C  CD1   . LEU B  1  760  ? 20.334  27.711  63.799  1.00 18.38 ? 758  LEU B CD1   1 
ATOM   14595 C  CD2   . LEU B  1  760  ? 21.103  25.555  62.722  1.00 21.35 ? 758  LEU B CD2   1 
ATOM   14596 N  N     . LEU B  1  761  ? 22.975  29.661  61.258  1.00 17.55 ? 759  LEU B N     1 
ATOM   14597 C  CA    . LEU B  1  761  ? 24.419  29.798  61.065  1.00 17.92 ? 759  LEU B CA    1 
ATOM   14598 C  C     . LEU B  1  761  ? 25.125  29.460  62.368  1.00 19.22 ? 759  LEU B C     1 
ATOM   14599 O  O     . LEU B  1  761  ? 25.454  30.350  63.163  1.00 20.06 ? 759  LEU B O     1 
ATOM   14600 C  CB    . LEU B  1  761  ? 24.806  31.204  60.591  1.00 18.79 ? 759  LEU B CB    1 
ATOM   14601 C  CG    . LEU B  1  761  ? 24.243  31.765  59.280  1.00 19.24 ? 759  LEU B CG    1 
ATOM   14602 C  CD1   . LEU B  1  761  ? 24.318  30.740  58.147  1.00 21.18 ? 759  LEU B CD1   1 
ATOM   14603 C  CD2   . LEU B  1  761  ? 22.820  32.269  59.472  1.00 21.55 ? 759  LEU B CD2   1 
ATOM   14604 N  N     . PRO B  1  762  ? 25.374  28.185  62.623  1.00 17.52 ? 760  PRO B N     1 
ATOM   14605 C  CA    . PRO B  1  762  ? 26.086  27.811  63.847  1.00 18.96 ? 760  PRO B CA    1 
ATOM   14606 C  C     . PRO B  1  762  ? 27.507  28.331  63.818  1.00 19.69 ? 760  PRO B C     1 
ATOM   14607 O  O     . PRO B  1  762  ? 28.110  28.504  62.755  1.00 20.02 ? 760  PRO B O     1 
ATOM   14608 C  CB    . PRO B  1  762  ? 26.064  26.276  63.829  1.00 18.61 ? 760  PRO B CB    1 
ATOM   14609 C  CG    . PRO B  1  762  ? 24.971  25.918  62.856  1.00 19.29 ? 760  PRO B CG    1 
ATOM   14610 C  CD    . PRO B  1  762  ? 24.999  27.012  61.824  1.00 17.79 ? 760  PRO B CD    1 
ATOM   14611 N  N     . GLY B  1  763  ? 28.042  28.590  65.001  1.00 18.27 ? 761  GLY B N     1 
ATOM   14612 C  CA    . GLY B  1  763  ? 29.441  28.942  65.120  1.00 21.33 ? 761  GLY B CA    1 
ATOM   14613 C  C     . GLY B  1  763  ? 29.653  29.858  66.304  1.00 19.74 ? 761  GLY B C     1 
ATOM   14614 O  O     . GLY B  1  763  ? 28.757  30.074  67.119  1.00 22.12 ? 761  GLY B O     1 
ATOM   14615 N  N     . ASP B  1  764  ? 30.865  30.393  66.382  1.00 25.81 ? 762  ASP B N     1 
ATOM   14616 C  CA    . ASP B  1  764  ? 31.236  31.180  67.548  1.00 25.21 ? 762  ASP B CA    1 
ATOM   14617 C  C     . ASP B  1  764  ? 30.987  32.657  67.253  1.00 30.63 ? 762  ASP B C     1 
ATOM   14618 O  O     . ASP B  1  764  ? 30.260  33.009  66.318  1.00 23.21 ? 762  ASP B O     1 
ATOM   14619 C  CB    . ASP B  1  764  ? 32.683  30.868  67.954  1.00 26.60 ? 762  ASP B CB    1 
ATOM   14620 C  CG    . ASP B  1  764  ? 33.700  31.268  66.901  1.00 31.74 ? 762  ASP B CG    1 
ATOM   14621 O  OD1   . ASP B  1  764  ? 33.396  32.101  66.021  1.00 28.65 ? 762  ASP B OD1   1 
ATOM   14622 O  OD2   . ASP B  1  764  ? 34.831  30.737  66.947  1.00 45.11 ? 762  ASP B OD2   1 
ATOM   14623 N  N     . GLY B  1  765  ? 31.593  33.543  68.045  1.00 28.13 ? 763  GLY B N     1 
ATOM   14624 C  CA    . GLY B  1  765  ? 31.308  34.954  67.890  1.00 24.59 ? 763  GLY B CA    1 
ATOM   14625 C  C     . GLY B  1  765  ? 31.798  35.539  66.586  1.00 22.89 ? 763  GLY B C     1 
ATOM   14626 O  O     . GLY B  1  765  ? 31.289  36.582  66.171  1.00 26.72 ? 763  GLY B O     1 
ATOM   14627 N  N     . ARG B  1  766  ? 32.782  34.908  65.940  1.00 25.83 ? 764  ARG B N     1 
ATOM   14628 C  CA    . ARG B  1  766  ? 33.222  35.382  64.630  1.00 25.17 ? 764  ARG B CA    1 
ATOM   14629 C  C     . ARG B  1  766  ? 32.106  35.260  63.604  1.00 24.69 ? 764  ARG B C     1 
ATOM   14630 O  O     . ARG B  1  766  ? 31.994  36.092  62.696  1.00 24.60 ? 764  ARG B O     1 
ATOM   14631 C  CB    . ARG B  1  766  ? 34.451  34.607  64.163  1.00 31.40 ? 764  ARG B CB    1 
ATOM   14632 C  CG    . ARG B  1  766  ? 35.728  34.923  64.924  1.00 34.02 ? 764  ARG B CG    1 
ATOM   14633 C  CD    . ARG B  1  766  ? 36.777  33.857  64.650  1.00 39.60 ? 764  ARG B CD    1 
ATOM   14634 N  NE    . ARG B  1  766  ? 36.188  32.528  64.770  1.00 45.61 ? 764  ARG B NE    1 
ATOM   14635 C  CZ    . ARG B  1  766  ? 36.845  31.391  64.592  1.00 54.66 ? 764  ARG B CZ    1 
ATOM   14636 N  NH1   . ARG B  1  766  ? 38.138  31.377  64.310  1.00 54.71 ? 764  ARG B NH1   1 
ATOM   14637 N  NH2   . ARG B  1  766  ? 36.187  30.239  64.695  1.00 55.79 ? 764  ARG B NH2   1 
ATOM   14638 N  N     . VAL B  1  767  ? 31.284  34.214  63.721  1.00 24.33 ? 765  VAL B N     1 
ATOM   14639 C  CA    . VAL B  1  767  ? 30.134  34.083  62.835  1.00 23.21 ? 765  VAL B CA    1 
ATOM   14640 C  C     . VAL B  1  767  ? 29.130  35.180  63.132  1.00 21.58 ? 765  VAL B C     1 
ATOM   14641 O  O     . VAL B  1  767  ? 28.595  35.822  62.216  1.00 22.95 ? 765  VAL B O     1 
ATOM   14642 C  CB    . VAL B  1  767  ? 29.502  32.687  62.969  1.00 19.75 ? 765  VAL B CB    1 
ATOM   14643 C  CG1   . VAL B  1  767  ? 28.279  32.584  62.058  1.00 20.69 ? 765  VAL B CG1   1 
ATOM   14644 C  CG2   . VAL B  1  767  ? 30.503  31.619  62.607  1.00 22.28 ? 765  VAL B CG2   1 
ATOM   14645 N  N     . GLY B  1  768  ? 28.861  35.418  64.416  1.00 20.33 ? 766  GLY B N     1 
ATOM   14646 C  CA    . GLY B  1  768  ? 27.980  36.514  64.774  1.00 19.85 ? 766  GLY B CA    1 
ATOM   14647 C  C     . GLY B  1  768  ? 28.494  37.841  64.246  1.00 19.19 ? 766  GLY B C     1 
ATOM   14648 O  O     . GLY B  1  768  ? 27.731  38.641  63.696  1.00 21.04 ? 766  GLY B O     1 
ATOM   14649 N  N     . ALA B  1  769  ? 29.791  38.091  64.414  1.00 22.09 ? 767  ALA B N     1 
ATOM   14650 C  CA    . ALA B  1  769  ? 30.358  39.360  63.968  1.00 22.09 ? 767  ALA B CA    1 
ATOM   14651 C  C     . ALA B  1  769  ? 30.243  39.516  62.456  1.00 25.73 ? 767  ALA B C     1 
ATOM   14652 O  O     . ALA B  1  769  ? 29.911  40.601  61.963  1.00 24.30 ? 767  ALA B O     1 
ATOM   14653 C  CB    . ALA B  1  769  ? 31.816  39.471  64.416  1.00 23.43 ? 767  ALA B CB    1 
ATOM   14654 N  N     . ALA B  1  770  ? 30.495  38.438  61.704  1.00 21.51 ? 768  ALA B N     1 
ATOM   14655 C  CA    . ALA B  1  770  ? 30.361  38.506  60.252  1.00 20.22 ? 768  ALA B CA    1 
ATOM   14656 C  C     . ALA B  1  770  ? 28.924  38.808  59.841  1.00 22.62 ? 768  ALA B C     1 
ATOM   14657 O  O     . ALA B  1  770  ? 28.685  39.537  58.871  1.00 22.90 ? 768  ALA B O     1 
ATOM   14658 C  CB    . ALA B  1  770  ? 30.835  37.199  59.620  1.00 23.66 ? 768  ALA B CB    1 
ATOM   14659 N  N     . LEU B  1  771  ? 27.950  38.247  60.555  1.00 20.05 ? 769  LEU B N     1 
ATOM   14660 C  CA    . LEU B  1  771  ? 26.556  38.534  60.229  1.00 19.37 ? 769  LEU B CA    1 
ATOM   14661 C  C     . LEU B  1  771  ? 26.220  39.991  60.507  1.00 21.49 ? 769  LEU B C     1 
ATOM   14662 O  O     . LEU B  1  771  ? 25.564  40.655  59.696  1.00 20.46 ? 769  LEU B O     1 
ATOM   14663 C  CB    . LEU B  1  771  ? 25.626  37.620  61.029  1.00 18.39 ? 769  LEU B CB    1 
ATOM   14664 C  CG    . LEU B  1  771  ? 25.684  36.150  60.604  1.00 17.80 ? 769  LEU B CG    1 
ATOM   14665 C  CD1   . LEU B  1  771  ? 24.891  35.290  61.576  1.00 20.56 ? 769  LEU B CD1   1 
ATOM   14666 C  CD2   . LEU B  1  771  ? 25.118  35.981  59.195  1.00 19.99 ? 769  LEU B CD2   1 
ATOM   14667 N  N     . VAL B  1  772  ? 26.622  40.481  61.680  1.00 18.10 ? 770  VAL B N     1 
ATOM   14668 C  CA    . VAL B  1  772  ? 26.325  41.853  62.090  1.00 19.65 ? 770  VAL B CA    1 
ATOM   14669 C  C     . VAL B  1  772  ? 26.923  42.857  61.110  1.00 22.85 ? 770  VAL B C     1 
ATOM   14670 O  O     . VAL B  1  772  ? 26.297  43.875  60.783  1.00 23.71 ? 770  VAL B O     1 
ATOM   14671 C  CB    . VAL B  1  772  ? 26.843  42.083  63.520  1.00 20.83 ? 770  VAL B CB    1 
ATOM   14672 C  CG1   . VAL B  1  772  ? 26.918  43.575  63.854  1.00 21.06 ? 770  VAL B CG1   1 
ATOM   14673 C  CG2   . VAL B  1  772  ? 25.972  41.330  64.524  1.00 21.04 ? 770  VAL B CG2   1 
ATOM   14674 N  N     . ALA B  1  773  ? 28.132  42.577  60.615  1.00 21.68 ? 771  ALA B N     1 
ATOM   14675 C  CA    . ALA B  1  773  ? 28.846  43.497  59.737  1.00 22.41 ? 771  ALA B CA    1 
ATOM   14676 C  C     . ALA B  1  773  ? 28.367  43.441  58.294  1.00 28.17 ? 771  ALA B C     1 
ATOM   14677 O  O     . ALA B  1  773  ? 28.727  44.327  57.511  1.00 28.11 ? 771  ALA B O     1 
ATOM   14678 C  CB    . ALA B  1  773  ? 30.345  43.202  59.791  1.00 24.47 ? 771  ALA B CB    1 
ATOM   14679 N  N     . ALA B  1  774  ? 27.575  42.437  57.926  1.00 23.24 ? 772  ALA B N     1 
ATOM   14680 C  CA    . ALA B  1  774  ? 27.152  42.288  56.537  1.00 23.44 ? 772  ALA B CA    1 
ATOM   14681 C  C     . ALA B  1  774  ? 26.323  43.486  56.084  1.00 23.60 ? 772  ALA B C     1 
ATOM   14682 O  O     . ALA B  1  774  ? 25.538  44.055  56.845  1.00 25.89 ? 772  ALA B O     1 
ATOM   14683 C  CB    . ALA B  1  774  ? 26.355  40.995  56.356  1.00 24.66 ? 772  ALA B CB    1 
ATOM   14684 N  N     . ALA B  1  775  ? 26.494  43.855  54.808  1.00 28.64 ? 773  ALA B N     1 
ATOM   14685 C  CA    . ALA B  1  775  ? 25.927  45.105  54.309  1.00 30.86 ? 773  ALA B CA    1 
ATOM   14686 C  C     . ALA B  1  775  ? 24.403  45.115  54.345  1.00 25.67 ? 773  ALA B C     1 
ATOM   14687 O  O     . ALA B  1  775  ? 23.801  46.162  54.594  1.00 29.02 ? 773  ALA B O     1 
ATOM   14688 C  CB    . ALA B  1  775  ? 26.416  45.366  52.882  1.00 31.71 ? 773  ALA B CB    1 
ATOM   14689 N  N     . GLU B  1  776  ? 23.759  43.977  54.107  1.00 22.97 ? 774  GLU B N     1 
ATOM   14690 C  CA    . GLU B  1  776  ? 22.308  43.950  54.037  1.00 19.81 ? 774  GLU B CA    1 
ATOM   14691 C  C     . GLU B  1  776  ? 21.643  43.749  55.393  1.00 21.27 ? 774  GLU B C     1 
ATOM   14692 O  O     . GLU B  1  776  ? 20.416  43.745  55.464  1.00 21.92 ? 774  GLU B O     1 
ATOM   14693 C  CB    . GLU B  1  776  ? 21.849  42.859  53.064  1.00 23.04 ? 774  GLU B CB    1 
ATOM   14694 C  CG    . GLU B  1  776  ? 22.437  42.992  51.657  1.00 29.29 ? 774  GLU B CG    1 
ATOM   14695 C  CD    . GLU B  1  776  ? 23.792  42.290  51.480  1.00 36.85 ? 774  GLU B CD    1 
ATOM   14696 O  OE1   . GLU B  1  776  ? 24.348  41.726  52.457  1.00 28.28 ? 774  GLU B OE1   1 
ATOM   14697 O  OE2   . GLU B  1  776  ? 24.313  42.307  50.343  1.00 38.44 ? 774  GLU B OE2   1 
ATOM   14698 N  N     . THR B  1  777  ? 22.407  43.580  56.466  1.00 20.04 ? 775  THR B N     1 
ATOM   14699 C  CA    . THR B  1  777  ? 21.793  43.419  57.775  1.00 18.55 ? 775  THR B CA    1 
ATOM   14700 C  C     . THR B  1  777  ? 21.058  44.690  58.179  1.00 20.57 ? 775  THR B C     1 
ATOM   14701 O  O     . THR B  1  777  ? 21.638  45.783  58.183  1.00 22.06 ? 775  THR B O     1 
ATOM   14702 C  CB    . THR B  1  777  ? 22.862  43.060  58.796  1.00 18.90 ? 775  THR B CB    1 
ATOM   14703 O  OG1   . THR B  1  777  ? 23.396  41.772  58.443  1.00 22.35 ? 775  THR B OG1   1 
ATOM   14704 C  CG2   . THR B  1  777  ? 22.272  43.022  60.196  1.00 19.77 ? 775  THR B CG2   1 
ATOM   14705 N  N     . ALA B  1  778  ? 19.776  44.537  58.514  1.00 18.09 ? 776  ALA B N     1 
ATOM   14706 C  CA    . ALA B  1  778  ? 18.886  45.661  58.766  1.00 18.48 ? 776  ALA B CA    1 
ATOM   14707 C  C     . ALA B  1  778  ? 18.519  45.806  60.233  1.00 19.75 ? 776  ALA B C     1 
ATOM   14708 O  O     . ALA B  1  778  ? 17.831  46.765  60.590  1.00 20.60 ? 776  ALA B O     1 
ATOM   14709 C  CB    . ALA B  1  778  ? 17.610  45.521  57.925  1.00 20.60 ? 776  ALA B CB    1 
ATOM   14710 N  N     . GLY B  1  779  ? 18.950  44.883  61.079  1.00 17.67 ? 777  GLY B N     1 
ATOM   14711 C  CA    . GLY B  1  779  ? 18.660  44.958  62.504  1.00 19.12 ? 777  GLY B CA    1 
ATOM   14712 C  C     . GLY B  1  779  ? 19.314  43.773  63.176  1.00 19.37 ? 777  GLY B C     1 
ATOM   14713 O  O     . GLY B  1  779  ? 19.604  42.756  62.544  1.00 18.91 ? 777  GLY B O     1 
ATOM   14714 N  N     . VAL B  1  780  ? 19.567  43.930  64.471  1.00 16.91 ? 778  VAL B N     1 
ATOM   14715 C  CA    . VAL B  1  780  ? 20.224  42.885  65.243  1.00 16.83 ? 778  VAL B CA    1 
ATOM   14716 C  C     . VAL B  1  780  ? 19.460  42.698  66.537  1.00 18.68 ? 778  VAL B C     1 
ATOM   14717 O  O     . VAL B  1  780  ? 19.103  43.674  67.209  1.00 18.06 ? 778  VAL B O     1 
ATOM   14718 C  CB    . VAL B  1  780  ? 21.705  43.201  65.531  1.00 16.92 ? 778  VAL B CB    1 
ATOM   14719 C  CG1   . VAL B  1  780  ? 22.315  42.095  66.390  1.00 18.64 ? 778  VAL B CG1   1 
ATOM   14720 C  CG2   . VAL B  1  780  ? 22.480  43.350  64.221  1.00 18.93 ? 778  VAL B CG2   1 
ATOM   14721 N  N     . MET B  1  781  ? 19.170  41.449  66.861  1.00 15.38 ? 779  MET B N     1 
ATOM   14722 C  CA    . MET B  1  781  ? 18.580  41.091  68.143  1.00 17.69 ? 779  MET B CA    1 
ATOM   14723 C  C     . MET B  1  781  ? 19.615  40.254  68.867  1.00 19.60 ? 779  MET B C     1 
ATOM   14724 O  O     . MET B  1  781  ? 20.017  39.193  68.377  1.00 18.92 ? 779  MET B O     1 
ATOM   14725 C  CB    . MET B  1  781  ? 17.263  40.339  67.955  1.00 16.11 ? 779  MET B CB    1 
ATOM   14726 C  CG    . MET B  1  781  ? 16.271  41.120  67.114  1.00 16.16 ? 779  MET B CG    1 
ATOM   14727 S  SD    . MET B  1  781  ? 14.815  40.162  66.754  1.00 18.24 ? 779  MET B SD    1 
ATOM   14728 C  CE    . MET B  1  781  ? 13.958  40.295  68.321  1.00 17.23 ? 779  MET B CE    1 
ATOM   14729 N  N     . PHE B  1  782  ? 20.111  40.774  69.981  1.00 18.13 ? 780  PHE B N     1 
ATOM   14730 C  CA    . PHE B  1  782  ? 21.196  40.159  70.706  1.00 17.24 ? 780  PHE B CA    1 
ATOM   14731 C  C     . PHE B  1  782  ? 20.779  39.954  72.146  1.00 19.80 ? 780  PHE B C     1 
ATOM   14732 O  O     . PHE B  1  782  ? 20.249  40.874  72.779  1.00 21.08 ? 780  PHE B O     1 
ATOM   14733 C  CB    . PHE B  1  782  ? 22.449  41.034  70.687  1.00 18.09 ? 780  PHE B CB    1 
ATOM   14734 C  CG    . PHE B  1  782  ? 23.540  40.505  71.551  1.00 17.48 ? 780  PHE B CG    1 
ATOM   14735 C  CD1   . PHE B  1  782  ? 24.333  39.459  71.113  1.00 19.21 ? 780  PHE B CD1   1 
ATOM   14736 C  CD2   . PHE B  1  782  ? 23.763  41.039  72.815  1.00 19.91 ? 780  PHE B CD2   1 
ATOM   14737 C  CE1   . PHE B  1  782  ? 25.329  38.960  71.893  1.00 22.66 ? 780  PHE B CE1   1 
ATOM   14738 C  CE2   . PHE B  1  782  ? 24.761  40.537  73.608  1.00 19.55 ? 780  PHE B CE2   1 
ATOM   14739 C  CZ    . PHE B  1  782  ? 25.553  39.506  73.155  1.00 22.43 ? 780  PHE B CZ    1 
ATOM   14740 N  N     . THR B  1  783  ? 21.031  38.758  72.653  1.00 16.89 ? 781  THR B N     1 
ATOM   14741 C  CA    . THR B  1  783  ? 20.908  38.465  74.071  1.00 19.61 ? 781  THR B CA    1 
ATOM   14742 C  C     . THR B  1  783  ? 22.191  37.773  74.496  1.00 20.58 ? 781  THR B C     1 
ATOM   14743 O  O     . THR B  1  783  ? 22.586  36.762  73.904  1.00 19.84 ? 781  THR B O     1 
ATOM   14744 C  CB    . THR B  1  783  ? 19.663  37.610  74.358  1.00 17.00 ? 781  THR B CB    1 
ATOM   14745 O  OG1   . THR B  1  783  ? 18.490  38.304  73.937  1.00 19.66 ? 781  THR B OG1   1 
ATOM   14746 C  CG2   . THR B  1  783  ? 19.563  37.382  75.831  1.00 21.81 ? 781  THR B CG2   1 
ATOM   14747 N  N     . GLY B  1  784  ? 22.869  38.337  75.493  1.00 18.34 ? 782  GLY B N     1 
ATOM   14748 C  CA    . GLY B  1  784  ? 24.180  37.842  75.859  1.00 19.82 ? 782  GLY B CA    1 
ATOM   14749 C  C     . GLY B  1  784  ? 24.877  38.836  76.764  1.00 21.76 ? 782  GLY B C     1 
ATOM   14750 O  O     . GLY B  1  784  ? 24.225  39.652  77.410  1.00 21.99 ? 782  GLY B O     1 
ATOM   14751 N  N     . SER B  1  785  ? 26.201  38.775  76.774  1.00 23.00 ? 783  SER B N     1 
ATOM   14752 C  CA    . SER B  1  785  ? 26.966  39.619  77.687  1.00 25.64 ? 783  SER B CA    1 
ATOM   14753 C  C     . SER B  1  785  ? 26.968  41.078  77.229  1.00 27.60 ? 783  SER B C     1 
ATOM   14754 O  O     . SER B  1  785  ? 26.904  41.389  76.034  1.00 23.24 ? 783  SER B O     1 
ATOM   14755 C  CB    . SER B  1  785  ? 28.396  39.108  77.815  1.00 23.51 ? 783  SER B CB    1 
ATOM   14756 O  OG    . SER B  1  785  ? 29.106  39.241  76.608  1.00 25.12 ? 783  SER B OG    1 
ATOM   14757 N  N     . THR B  1  786  ? 27.064  41.980  78.211  1.00 26.87 ? 784  THR B N     1 
ATOM   14758 C  CA    . THR B  1  786  ? 27.191  43.406  77.918  1.00 26.21 ? 784  THR B CA    1 
ATOM   14759 C  C     . THR B  1  786  ? 28.414  43.693  77.054  1.00 22.14 ? 784  THR B C     1 
ATOM   14760 O  O     . THR B  1  786  ? 28.350  44.513  76.130  1.00 25.58 ? 784  THR B O     1 
ATOM   14761 C  CB    . THR B  1  786  ? 27.259  44.198  79.230  1.00 26.55 ? 784  THR B CB    1 
ATOM   14762 O  OG1   . THR B  1  786  ? 26.065  43.972  79.987  1.00 31.01 ? 784  THR B OG1   1 
ATOM   14763 C  CG2   . THR B  1  786  ? 27.388  45.683  78.945  1.00 36.91 ? 784  THR B CG2   1 
ATOM   14764 N  N     . GLU B  1  787  ? 29.549  43.040  77.343  1.00 24.26 ? 785  GLU B N     1 
ATOM   14765 C  CA    . GLU B  1  787  ? 30.759  43.273  76.566  1.00 24.96 ? 785  GLU B CA    1 
ATOM   14766 C  C     . GLU B  1  787  ? 30.539  42.984  75.085  1.00 25.61 ? 785  GLU B C     1 
ATOM   14767 O  O     . GLU B  1  787  ? 30.982  43.756  74.231  1.00 23.61 ? 785  GLU B O     1 
ATOM   14768 C  CB    . GLU B  1  787  ? 31.908  42.421  77.111  1.00 32.87 ? 785  GLU B CB    1 
ATOM   14769 N  N     . VAL B  1  788  ? 29.863  41.874  74.760  1.00 23.40 ? 786  VAL B N     1 
ATOM   14770 C  CA    . VAL B  1  788  ? 29.661  41.529  73.356  1.00 23.31 ? 786  VAL B CA    1 
ATOM   14771 C  C     . VAL B  1  788  ? 28.663  42.486  72.715  1.00 19.68 ? 786  VAL B C     1 
ATOM   14772 O  O     . VAL B  1  788  ? 28.833  42.916  71.568  1.00 22.39 ? 786  VAL B O     1 
ATOM   14773 C  CB    . VAL B  1  788  ? 29.199  40.066  73.233  1.00 24.19 ? 786  VAL B CB    1 
ATOM   14774 C  CG1   . VAL B  1  788  ? 28.756  39.774  71.802  1.00 22.66 ? 786  VAL B CG1   1 
ATOM   14775 C  CG2   . VAL B  1  788  ? 30.316  39.104  73.666  1.00 25.00 ? 786  VAL B CG2   1 
ATOM   14776 N  N     . ALA B  1  789  ? 27.619  42.855  73.460  1.00 20.09 ? 787  ALA B N     1 
ATOM   14777 C  CA    . ALA B  1  789  ? 26.648  43.815  72.947  1.00 17.39 ? 787  ALA B CA    1 
ATOM   14778 C  C     . ALA B  1  789  ? 27.322  45.117  72.550  1.00 17.40 ? 787  ALA B C     1 
ATOM   14779 O  O     . ALA B  1  789  ? 26.948  45.732  71.549  1.00 20.10 ? 787  ALA B O     1 
ATOM   14780 C  CB    . ALA B  1  789  ? 25.560  44.080  73.983  1.00 17.74 ? 787  ALA B CB    1 
ATOM   14781 N  N     . ARG B  1  790  ? 28.305  45.568  73.342  1.00 18.87 ? 788  ARG B N     1 
ATOM   14782 C  CA    . ARG B  1  790  ? 29.013  46.800  72.998  1.00 20.48 ? 788  ARG B CA    1 
ATOM   14783 C  C     . ARG B  1  790  ? 29.747  46.675  71.675  1.00 22.55 ? 788  ARG B C     1 
ATOM   14784 O  O     . ARG B  1  790  ? 29.806  47.632  70.893  1.00 24.80 ? 788  ARG B O     1 
ATOM   14785 C  CB    . ARG B  1  790  ? 30.026  47.155  74.078  1.00 26.14 ? 788  ARG B CB    1 
ATOM   14786 C  CG    . ARG B  1  790  ? 29.439  47.707  75.299  1.00 28.17 ? 788  ARG B CG    1 
ATOM   14787 C  CD    . ARG B  1  790  ? 30.538  48.270  76.187  1.00 30.58 ? 788  ARG B CD    1 
ATOM   14788 N  NE    . ARG B  1  790  ? 29.994  48.427  77.521  1.00 42.94 ? 788  ARG B NE    1 
ATOM   14789 C  CZ    . ARG B  1  790  ? 29.165  49.400  77.860  1.00 49.46 ? 788  ARG B CZ    1 
ATOM   14790 N  NH1   . ARG B  1  790  ? 28.869  50.381  77.016  1.00 41.14 ? 788  ARG B NH1   1 
ATOM   14791 N  NH2   . ARG B  1  790  ? 28.605  49.380  79.065  1.00 47.17 ? 788  ARG B NH2   1 
ATOM   14792 N  N     . LEU B  1  791  ? 30.353  45.518  71.427  1.00 23.38 ? 789  LEU B N     1 
ATOM   14793 C  CA    . LEU B  1  791  ? 31.058  45.323  70.168  1.00 22.76 ? 789  LEU B CA    1 
ATOM   14794 C  C     . LEU B  1  791  ? 30.093  45.358  68.993  1.00 24.29 ? 789  LEU B C     1 
ATOM   14795 O  O     . LEU B  1  791  ? 30.397  45.932  67.945  1.00 23.55 ? 789  LEU B O     1 
ATOM   14796 C  CB    . LEU B  1  791  ? 31.806  43.996  70.201  1.00 26.51 ? 789  LEU B CB    1 
ATOM   14797 C  CG    . LEU B  1  791  ? 32.820  43.855  71.332  1.00 32.58 ? 789  LEU B CG    1 
ATOM   14798 C  CD1   . LEU B  1  791  ? 33.416  42.463  71.301  1.00 28.04 ? 789  LEU B CD1   1 
ATOM   14799 C  CD2   . LEU B  1  791  ? 33.896  44.925  71.198  1.00 30.09 ? 789  LEU B CD2   1 
ATOM   14800 N  N     . ILE B  1  792  ? 28.926  44.736  69.154  1.00 22.98 ? 790  ILE B N     1 
ATOM   14801 C  CA    . ILE B  1  792  ? 27.905  44.761  68.111  1.00 18.42 ? 790  ILE B CA    1 
ATOM   14802 C  C     . ILE B  1  792  ? 27.442  46.185  67.859  1.00 20.70 ? 790  ILE B C     1 
ATOM   14803 O  O     . ILE B  1  792  ? 27.298  46.625  66.711  1.00 22.52 ? 790  ILE B O     1 
ATOM   14804 C  CB    . ILE B  1  792  ? 26.735  43.859  68.529  1.00 17.74 ? 790  ILE B CB    1 
ATOM   14805 C  CG1   . ILE B  1  792  ? 27.233  42.418  68.550  1.00 16.55 ? 790  ILE B CG1   1 
ATOM   14806 C  CG2   . ILE B  1  792  ? 25.520  44.086  67.629  1.00 20.40 ? 790  ILE B CG2   1 
ATOM   14807 C  CD1   . ILE B  1  792  ? 26.202  41.421  69.017  1.00 19.07 ? 790  ILE B CD1   1 
ATOM   14808 N  N     . GLN B  1  793  ? 27.157  46.908  68.938  1.00 20.60 ? 791  GLN B N     1 
ATOM   14809 C  CA    . GLN B  1  793  ? 26.725  48.290  68.825  1.00 20.36 ? 791  GLN B CA    1 
ATOM   14810 C  C     . GLN B  1  793  ? 27.738  49.117  68.047  1.00 20.29 ? 791  GLN B C     1 
ATOM   14811 O  O     . GLN B  1  793  ? 27.361  49.920  67.186  1.00 23.07 ? 791  GLN B O     1 
ATOM   14812 C  CB    . GLN B  1  793  ? 26.517  48.853  70.229  1.00 23.32 ? 791  GLN B CB    1 
ATOM   14813 C  CG    . GLN B  1  793  ? 26.019  50.261  70.311  1.00 24.32 ? 791  GLN B CG    1 
ATOM   14814 C  CD    . GLN B  1  793  ? 26.375  50.876  71.646  1.00 31.91 ? 791  GLN B CD    1 
ATOM   14815 O  OE1   . GLN B  1  793  ? 27.429  50.568  72.220  1.00 31.51 ? 791  GLN B OE1   1 
ATOM   14816 N  NE2   . GLN B  1  793  ? 25.501  51.729  72.160  1.00 30.66 ? 791  GLN B NE2   1 
ATOM   14817 N  N     . ALA B  1  794  ? 29.030  48.909  68.316  1.00 22.23 ? 792  ALA B N     1 
ATOM   14818 C  CA    . ALA B  1  794  ? 30.064  49.642  67.593  1.00 26.33 ? 792  ALA B CA    1 
ATOM   14819 C  C     . ALA B  1  794  ? 30.057  49.287  66.109  1.00 28.22 ? 792  ALA B C     1 
ATOM   14820 O  O     . ALA B  1  794  ? 30.174  50.175  65.255  1.00 26.54 ? 792  ALA B O     1 
ATOM   14821 C  CB    . ALA B  1  794  ? 31.438  49.358  68.207  1.00 27.08 ? 792  ALA B CB    1 
ATOM   14822 N  N     . GLN B  1  795  ? 29.941  47.994  65.784  1.00 22.91 ? 793  GLN B N     1 
ATOM   14823 C  CA    A GLN B  1  795  ? 29.903  47.620  64.377  0.43 24.40 ? 793  GLN B CA    1 
ATOM   14824 C  CA    B GLN B  1  795  ? 29.864  47.566  64.386  0.57 24.41 ? 793  GLN B CA    1 
ATOM   14825 C  C     . GLN B  1  795  ? 28.717  48.266  63.673  1.00 23.48 ? 793  GLN B C     1 
ATOM   14826 O  O     . GLN B  1  795  ? 28.868  48.789  62.562  1.00 23.91 ? 793  GLN B O     1 
ATOM   14827 C  CB    A GLN B  1  795  ? 29.864  46.099  64.224  0.43 28.20 ? 793  GLN B CB    1 
ATOM   14828 C  CB    B GLN B  1  795  ? 29.659  46.045  64.297  0.57 28.28 ? 793  GLN B CB    1 
ATOM   14829 C  CG    A GLN B  1  795  ? 29.835  45.631  62.773  0.43 27.78 ? 793  GLN B CG    1 
ATOM   14830 C  CG    B GLN B  1  795  ? 30.839  45.132  64.631  0.57 25.45 ? 793  GLN B CG    1 
ATOM   14831 C  CD    A GLN B  1  795  ? 31.028  46.114  61.966  0.43 28.52 ? 793  GLN B CD    1 
ATOM   14832 C  CD    B GLN B  1  795  ? 30.481  43.644  64.495  0.57 31.18 ? 793  GLN B CD    1 
ATOM   14833 O  OE1   A GLN B  1  795  ? 30.893  46.956  61.078  0.43 31.86 ? 793  GLN B OE1   1 
ATOM   14834 O  OE1   B GLN B  1  795  ? 29.892  43.047  65.401  0.57 33.05 ? 793  GLN B OE1   1 
ATOM   14835 N  NE2   A GLN B  1  795  ? 32.202  45.570  62.261  0.43 26.23 ? 793  GLN B NE2   1 
ATOM   14836 N  NE2   B GLN B  1  795  ? 30.834  43.046  63.357  0.57 23.13 ? 793  GLN B NE2   1 
ATOM   14837 N  N     . LEU B  1  796  ? 27.540  48.265  64.305  1.00 20.18 ? 794  LEU B N     1 
ATOM   14838 C  CA    . LEU B  1  796  ? 26.340  48.773  63.647  1.00 19.15 ? 794  LEU B CA    1 
ATOM   14839 C  C     . LEU B  1  796  ? 26.400  50.277  63.432  1.00 24.41 ? 794  LEU B C     1 
ATOM   14840 O  O     . LEU B  1  796  ? 25.865  50.780  62.438  1.00 26.55 ? 794  LEU B O     1 
ATOM   14841 C  CB    . LEU B  1  796  ? 25.104  48.421  64.465  1.00 19.12 ? 794  LEU B CB    1 
ATOM   14842 C  CG    . LEU B  1  796  ? 24.752  46.944  64.501  1.00 22.28 ? 794  LEU B CG    1 
ATOM   14843 C  CD1   . LEU B  1  796  ? 23.510  46.759  65.363  1.00 20.29 ? 794  LEU B CD1   1 
ATOM   14844 C  CD2   . LEU B  1  796  ? 24.504  46.463  63.091  1.00 20.28 ? 794  LEU B CD2   1 
ATOM   14845 N  N     . ALA B  1  797  ? 27.042  51.005  64.346  1.00 24.80 ? 795  ALA B N     1 
ATOM   14846 C  CA    . ALA B  1  797  ? 27.071  52.457  64.247  1.00 28.00 ? 795  ALA B CA    1 
ATOM   14847 C  C     . ALA B  1  797  ? 27.915  52.934  63.078  1.00 30.41 ? 795  ALA B C     1 
ATOM   14848 O  O     . ALA B  1  797  ? 27.825  54.103  62.707  1.00 32.84 ? 795  ALA B O     1 
ATOM   14849 C  CB    . ALA B  1  797  ? 27.595  53.063  65.546  1.00 26.93 ? 795  ALA B CB    1 
ATOM   14850 N  N     . ASP B  1  798  ? 28.733  52.061  62.496  1.00 26.52 ? 796  ASP B N     1 
ATOM   14851 C  CA    . ASP B  1  798  ? 29.443  52.424  61.277  1.00 30.37 ? 796  ASP B CA    1 
ATOM   14852 C  C     . ASP B  1  798  ? 28.517  52.516  60.074  1.00 32.36 ? 796  ASP B C     1 
ATOM   14853 O  O     . ASP B  1  798  ? 28.879  53.148  59.077  1.00 35.21 ? 796  ASP B O     1 
ATOM   14854 C  CB    . ASP B  1  798  ? 30.545  51.407  60.994  1.00 27.74 ? 796  ASP B CB    1 
ATOM   14855 N  N     . ARG B  1  799  ? 27.334  51.914  60.148  1.00 30.96 ? 797  ARG B N     1 
ATOM   14856 C  CA    . ARG B  1  799  ? 26.454  51.748  59.004  1.00 34.47 ? 797  ARG B CA    1 
ATOM   14857 C  C     . ARG B  1  799  ? 25.145  52.491  59.232  1.00 32.23 ? 797  ARG B C     1 
ATOM   14858 O  O     . ARG B  1  799  ? 24.790  52.853  60.359  1.00 27.37 ? 797  ARG B O     1 
ATOM   14859 C  CB    . ARG B  1  799  ? 26.154  50.257  58.736  1.00 33.06 ? 797  ARG B CB    1 
ATOM   14860 C  CG    . ARG B  1  799  ? 27.370  49.323  58.828  1.00 42.64 ? 797  ARG B CG    1 
ATOM   14861 C  CD    . ARG B  1  799  ? 27.121  47.949  58.179  1.00 40.15 ? 797  ARG B CD    1 
ATOM   14862 N  NE    . ARG B  1  799  ? 26.352  47.028  59.016  1.00 42.82 ? 797  ARG B NE    1 
ATOM   14863 C  CZ    . ARG B  1  799  ? 25.074  46.721  58.825  1.00 43.76 ? 797  ARG B CZ    1 
ATOM   14864 N  NH1   . ARG B  1  799  ? 24.378  47.235  57.824  1.00 35.26 ? 797  ARG B NH1   1 
ATOM   14865 N  NH2   . ARG B  1  799  ? 24.477  45.871  59.657  1.00 38.88 ? 797  ARG B NH2   1 
ATOM   14866 N  N     . LEU B  1  800  ? 24.430  52.710  58.135  1.00 26.49 ? 798  LEU B N     1 
ATOM   14867 C  CA    . LEU B  1  800  ? 23.069  53.219  58.159  1.00 28.30 ? 798  LEU B CA    1 
ATOM   14868 C  C     . LEU B  1  800  ? 22.203  52.308  57.305  1.00 28.65 ? 798  LEU B C     1 
ATOM   14869 O  O     . LEU B  1  800  ? 22.696  51.613  56.414  1.00 30.84 ? 798  LEU B O     1 
ATOM   14870 C  CB    . LEU B  1  800  ? 22.982  54.652  57.621  1.00 35.80 ? 798  LEU B CB    1 
ATOM   14871 C  CG    . LEU B  1  800  ? 23.584  55.781  58.450  1.00 33.78 ? 798  LEU B CG    1 
ATOM   14872 C  CD1   . LEU B  1  800  ? 23.426  57.079  57.683  1.00 37.18 ? 798  LEU B CD1   1 
ATOM   14873 C  CD2   . LEU B  1  800  ? 22.892  55.861  59.797  1.00 27.52 ? 798  LEU B CD2   1 
ATOM   14874 N  N     . SER B  1  801  ? 20.908  52.312  57.592  1.00 28.95 ? 799  SER B N     1 
ATOM   14875 C  CA    . SER B  1  801  ? 19.953  51.577  56.774  1.00 36.68 ? 799  SER B CA    1 
ATOM   14876 C  C     . SER B  1  801  ? 19.939  52.168  55.370  1.00 42.92 ? 799  SER B C     1 
ATOM   14877 O  O     . SER B  1  801  ? 20.506  53.247  55.149  1.00 35.19 ? 799  SER B O     1 
ATOM   14878 C  CB    . SER B  1  801  ? 18.560  51.643  57.397  1.00 34.06 ? 799  SER B CB    1 
ATOM   14879 O  OG    . SER B  1  801  ? 18.028  52.948  57.273  1.00 37.57 ? 799  SER B OG    1 
ATOM   14880 N  N     . PRO B  1  802  ? 19.321  51.495  54.393  1.00 49.88 ? 800  PRO B N     1 
ATOM   14881 C  CA    . PRO B  1  802  ? 19.113  52.140  53.085  1.00 50.47 ? 800  PRO B CA    1 
ATOM   14882 C  C     . PRO B  1  802  ? 18.413  53.484  53.189  1.00 45.77 ? 800  PRO B C     1 
ATOM   14883 O  O     . PRO B  1  802  ? 18.700  54.393  52.398  1.00 48.66 ? 800  PRO B O     1 
ATOM   14884 C  CB    . PRO B  1  802  ? 18.260  51.115  52.327  1.00 56.39 ? 800  PRO B CB    1 
ATOM   14885 C  CG    . PRO B  1  802  ? 18.601  49.804  52.953  1.00 57.50 ? 800  PRO B CG    1 
ATOM   14886 C  CD    . PRO B  1  802  ? 18.880  50.087  54.398  1.00 46.34 ? 800  PRO B CD    1 
ATOM   14887 N  N     . ALA B  1  803  ? 17.508  53.635  54.155  1.00 43.62 ? 801  ALA B N     1 
ATOM   14888 C  CA    . ALA B  1  803  ? 16.794  54.882  54.393  1.00 39.47 ? 801  ALA B CA    1 
ATOM   14889 C  C     . ALA B  1  803  ? 17.614  55.912  55.163  1.00 44.77 ? 801  ALA B C     1 
ATOM   14890 O  O     . ALA B  1  803  ? 17.083  56.980  55.485  1.00 47.11 ? 801  ALA B O     1 
ATOM   14891 C  CB    . ALA B  1  803  ? 15.491  54.598  55.147  1.00 39.15 ? 801  ALA B CB    1 
ATOM   14892 N  N     . GLY B  1  804  ? 18.875  55.623  55.476  1.00 36.45 ? 802  GLY B N     1 
ATOM   14893 C  CA    . GLY B  1  804  ? 19.718  56.592  56.153  1.00 35.58 ? 802  GLY B CA    1 
ATOM   14894 C  C     . GLY B  1  804  ? 19.487  56.712  57.641  1.00 35.82 ? 802  GLY B C     1 
ATOM   14895 O  O     . GLY B  1  804  ? 19.685  57.792  58.209  1.00 32.47 ? 802  GLY B O     1 
ATOM   14896 N  N     . ARG B  1  805  ? 19.083  55.634  58.295  1.00 32.09 ? 803  ARG B N     1 
ATOM   14897 C  CA    . ARG B  1  805  ? 18.734  55.657  59.704  1.00 28.15 ? 803  ARG B CA    1 
ATOM   14898 C  C     . ARG B  1  805  ? 19.540  54.604  60.443  1.00 25.17 ? 803  ARG B C     1 
ATOM   14899 O  O     . ARG B  1  805  ? 20.043  53.655  59.832  1.00 26.85 ? 803  ARG B O     1 
ATOM   14900 C  CB    . ARG B  1  805  ? 17.232  55.412  59.910  1.00 31.34 ? 803  ARG B CB    1 
ATOM   14901 C  CG    . ARG B  1  805  ? 16.351  56.500  59.320  1.00 36.39 ? 803  ARG B CG    1 
ATOM   14902 C  CD    . ARG B  1  805  ? 16.599  57.842  60.000  1.00 43.13 ? 803  ARG B CD    1 
ATOM   14903 N  NE    . ARG B  1  805  ? 15.748  58.896  59.452  1.00 46.93 ? 803  ARG B NE    1 
ATOM   14904 C  CZ    . ARG B  1  805  ? 16.128  59.772  58.531  1.00 42.94 ? 803  ARG B CZ    1 
ATOM   14905 N  NH1   . ARG B  1  805  ? 17.356  59.768  58.034  1.00 42.33 ? 803  ARG B NH1   1 
ATOM   14906 N  NH2   . ARG B  1  805  ? 15.254  60.679  58.098  1.00 46.84 ? 803  ARG B NH2   1 
ATOM   14907 N  N     . PRO B  1  806  ? 19.715  54.760  61.751  1.00 24.47 ? 804  PRO B N     1 
ATOM   14908 C  CA    . PRO B  1  806  ? 20.488  53.763  62.493  1.00 23.51 ? 804  PRO B CA    1 
ATOM   14909 C  C     . PRO B  1  806  ? 19.867  52.382  62.374  1.00 23.05 ? 804  PRO B C     1 
ATOM   14910 O  O     . PRO B  1  806  ? 18.641  52.228  62.338  1.00 23.79 ? 804  PRO B O     1 
ATOM   14911 C  CB    . PRO B  1  806  ? 20.446  54.280  63.933  1.00 24.17 ? 804  PRO B CB    1 
ATOM   14912 C  CG    . PRO B  1  806  ? 20.279  55.758  63.771  1.00 27.67 ? 804  PRO B CG    1 
ATOM   14913 C  CD    . PRO B  1  806  ? 19.344  55.900  62.607  1.00 25.08 ? 804  PRO B CD    1 
ATOM   14914 N  N     . ILE B  1  807  ? 20.738  51.381  62.303  1.00 22.01 ? 805  ILE B N     1 
ATOM   14915 C  CA    . ILE B  1  807  ? 20.331  49.981  62.327  1.00 21.10 ? 805  ILE B CA    1 
ATOM   14916 C  C     . ILE B  1  807  ? 19.866  49.636  63.737  1.00 21.59 ? 805  ILE B C     1 
ATOM   14917 O  O     . ILE B  1  807  ? 20.649  49.776  64.687  1.00 21.23 ? 805  ILE B O     1 
ATOM   14918 C  CB    . ILE B  1  807  ? 21.486  49.062  61.908  1.00 20.17 ? 805  ILE B CB    1 
ATOM   14919 C  CG1   . ILE B  1  807  ? 22.056  49.468  60.540  1.00 27.09 ? 805  ILE B CG1   1 
ATOM   14920 C  CG2   . ILE B  1  807  ? 21.017  47.607  61.937  1.00 20.79 ? 805  ILE B CG2   1 
ATOM   14921 C  CD1   . ILE B  1  807  ? 21.102  49.256  59.407  1.00 34.29 ? 805  ILE B CD1   1 
ATOM   14922 N  N     . PRO B  1  808  ? 18.634  49.164  63.922  1.00 20.71 ? 806  PRO B N     1 
ATOM   14923 C  CA    . PRO B  1  808  ? 18.145  48.895  65.279  1.00 20.25 ? 806  PRO B CA    1 
ATOM   14924 C  C     . PRO B  1  808  ? 18.891  47.750  65.932  1.00 22.41 ? 806  PRO B C     1 
ATOM   14925 O  O     . PRO B  1  808  ? 19.197  46.735  65.298  1.00 20.01 ? 806  PRO B O     1 
ATOM   14926 C  CB    . PRO B  1  808  ? 16.674  48.525  65.060  1.00 20.63 ? 806  PRO B CB    1 
ATOM   14927 C  CG    . PRO B  1  808  ? 16.310  49.186  63.774  1.00 28.91 ? 806  PRO B CG    1 
ATOM   14928 C  CD    . PRO B  1  808  ? 17.554  49.062  62.928  1.00 21.45 ? 806  PRO B CD    1 
ATOM   14929 N  N     . LEU B  1  809  ? 19.167  47.916  67.220  1.00 18.17 ? 807  LEU B N     1 
ATOM   14930 C  CA    . LEU B  1  809  ? 19.774  46.864  68.020  1.00 18.69 ? 807  LEU B CA    1 
ATOM   14931 C  C     . LEU B  1  809  ? 18.905  46.669  69.241  1.00 17.99 ? 807  LEU B C     1 
ATOM   14932 O  O     . LEU B  1  809  ? 18.670  47.625  69.980  1.00 20.46 ? 807  LEU B O     1 
ATOM   14933 C  CB    . LEU B  1  809  ? 21.194  47.234  68.451  1.00 18.76 ? 807  LEU B CB    1 
ATOM   14934 C  CG    . LEU B  1  809  ? 21.860  46.337  69.491  1.00 20.58 ? 807  LEU B CG    1 
ATOM   14935 C  CD1   . LEU B  1  809  ? 21.997  44.905  68.958  1.00 19.89 ? 807  LEU B CD1   1 
ATOM   14936 C  CD2   . LEU B  1  809  ? 23.222  46.911  69.902  1.00 23.29 ? 807  LEU B CD2   1 
ATOM   14937 N  N     . ILE B  1  810  ? 18.421  45.448  69.450  1.00 16.53 ? 808  ILE B N     1 
ATOM   14938 C  CA    . ILE B  1  810  ? 17.818  45.075  70.723  1.00 16.75 ? 808  ILE B CA    1 
ATOM   14939 C  C     . ILE B  1  810  ? 18.868  44.255  71.438  1.00 21.31 ? 808  ILE B C     1 
ATOM   14940 O  O     . ILE B  1  810  ? 19.272  43.195  70.946  1.00 20.19 ? 808  ILE B O     1 
ATOM   14941 C  CB    . ILE B  1  810  ? 16.520  44.272  70.554  1.00 16.53 ? 808  ILE B CB    1 
ATOM   14942 C  CG1   . ILE B  1  810  ? 15.491  45.049  69.733  1.00 18.03 ? 808  ILE B CG1   1 
ATOM   14943 C  CG2   . ILE B  1  810  ? 15.947  43.949  71.924  1.00 21.05 ? 808  ILE B CG2   1 
ATOM   14944 C  CD1   . ILE B  1  810  ? 14.110  44.368  69.701  1.00 22.54 ? 808  ILE B CD1   1 
ATOM   14945 N  N     . ALA B  1  811  ? 19.353  44.752  72.571  1.00 19.66 ? 809  ALA B N     1 
ATOM   14946 C  CA    . ALA B  1  811  ? 20.441  44.089  73.274  1.00 18.83 ? 809  ALA B CA    1 
ATOM   14947 C  C     . ALA B  1  811  ? 20.000  43.894  74.709  1.00 23.33 ? 809  ALA B C     1 
ATOM   14948 O  O     . ALA B  1  811  ? 19.875  44.867  75.461  1.00 23.36 ? 809  ALA B O     1 
ATOM   14949 C  CB    . ALA B  1  811  ? 21.737  44.892  73.199  1.00 22.04 ? 809  ALA B CB    1 
ATOM   14950 N  N     . GLU B  1  812  ? 19.743  42.653  75.072  1.00 20.49 ? 810  GLU B N     1 
ATOM   14951 C  CA    . GLU B  1  812  ? 19.344  42.302  76.424  1.00 20.82 ? 810  GLU B CA    1 
ATOM   14952 C  C     . GLU B  1  812  ? 20.520  41.576  77.066  1.00 21.75 ? 810  GLU B C     1 
ATOM   14953 O  O     . GLU B  1  812  ? 20.987  40.547  76.559  1.00 22.56 ? 810  GLU B O     1 
ATOM   14954 C  CB    . GLU B  1  812  ? 18.055  41.486  76.382  1.00 24.52 ? 810  GLU B CB    1 
ATOM   14955 C  CG    . GLU B  1  812  ? 16.979  42.257  75.586  1.00 26.73 ? 810  GLU B CG    1 
ATOM   14956 C  CD    . GLU B  1  812  ? 16.500  43.548  76.283  1.00 29.50 ? 810  GLU B CD    1 
ATOM   14957 O  OE1   . GLU B  1  812  ? 15.728  43.448  77.247  1.00 29.23 ? 810  GLU B OE1   1 
ATOM   14958 O  OE2   . GLU B  1  812  ? 16.879  44.660  75.869  1.00 24.50 ? 810  GLU B OE2   1 
ATOM   14959 N  N     . THR B  1  813  ? 21.049  42.157  78.136  1.00 21.33 ? 811  THR B N     1 
ATOM   14960 C  CA    . THR B  1  813  ? 22.373  41.818  78.610  1.00 19.45 ? 811  THR B CA    1 
ATOM   14961 C  C     . THR B  1  813  ? 22.249  41.414  80.077  1.00 23.10 ? 811  THR B C     1 
ATOM   14962 O  O     . THR B  1  813  ? 21.204  40.956  80.550  1.00 23.45 ? 811  THR B O     1 
ATOM   14963 C  CB    . THR B  1  813  ? 23.335  42.981  78.314  1.00 21.51 ? 811  THR B CB    1 
ATOM   14964 O  OG1   . THR B  1  813  ? 22.743  44.224  78.715  1.00 20.93 ? 811  THR B OG1   1 
ATOM   14965 C  CG2   . THR B  1  813  ? 23.594  43.048  76.802  1.00 23.41 ? 811  THR B CG2   1 
ATOM   14966 N  N     . GLY B  1  814  ? 23.334  41.539  80.821  1.00 24.17 ? 812  GLY B N     1 
ATOM   14967 C  CA    . GLY B  1  814  ? 23.407  40.870  82.107  1.00 24.11 ? 812  GLY B CA    1 
ATOM   14968 C  C     . GLY B  1  814  ? 22.578  41.512  83.210  1.00 23.84 ? 812  GLY B C     1 
ATOM   14969 O  O     . GLY B  1  814  ? 21.848  42.485  83.030  1.00 24.20 ? 812  GLY B O     1 
ATOM   14970 N  N     . GLY B  1  815  ? 22.691  40.914  84.395  1.00 20.74 ? 813  GLY B N     1 
ATOM   14971 C  CA    . GLY B  1  815  ? 22.126  41.497  85.590  1.00 19.65 ? 813  GLY B CA    1 
ATOM   14972 C  C     . GLY B  1  815  ? 23.093  41.316  86.744  1.00 19.41 ? 813  GLY B C     1 
ATOM   14973 O  O     . GLY B  1  815  ? 24.067  40.567  86.653  1.00 24.95 ? 813  GLY B O     1 
ATOM   14974 N  N     . GLN B  1  816  ? 22.830  42.053  87.813  1.00 17.71 ? 814  GLN B N     1 
ATOM   14975 C  CA    . GLN B  1  816  ? 23.507  41.860  89.088  1.00 18.12 ? 814  GLN B CA    1 
ATOM   14976 C  C     . GLN B  1  816  ? 22.402  41.873  90.136  1.00 15.36 ? 814  GLN B C     1 
ATOM   14977 O  O     . GLN B  1  816  ? 22.240  42.833  90.889  1.00 18.92 ? 814  GLN B O     1 
ATOM   14978 C  CB    . GLN B  1  816  ? 24.562  42.935  89.333  1.00 19.85 ? 814  GLN B CB    1 
ATOM   14979 C  CG    . GLN B  1  816  ? 25.468  42.610  90.487  1.00 20.12 ? 814  GLN B CG    1 
ATOM   14980 C  CD    . GLN B  1  816  ? 26.334  41.402  90.212  1.00 22.76 ? 814  GLN B CD    1 
ATOM   14981 O  OE1   . GLN B  1  816  ? 25.883  40.264  90.337  1.00 22.05 ? 814  GLN B OE1   1 
ATOM   14982 N  NE2   . GLN B  1  816  ? 27.597  41.642  89.848  1.00 21.65 ? 814  GLN B NE2   1 
ATOM   14983 N  N     . ASN B  1  817  ? 21.607  40.815  90.144  1.00 15.88 ? 815  ASN B N     1 
ATOM   14984 C  CA    . ASN B  1  817  ? 20.254  40.890  90.676  1.00 16.34 ? 815  ASN B CA    1 
ATOM   14985 C  C     . ASN B  1  817  ? 20.254  40.662  92.173  1.00 16.28 ? 815  ASN B C     1 
ATOM   14986 O  O     . ASN B  1  817  ? 20.875  39.711  92.656  1.00 17.64 ? 815  ASN B O     1 
ATOM   14987 C  CB    . ASN B  1  817  ? 19.354  39.866  89.991  1.00 16.75 ? 815  ASN B CB    1 
ATOM   14988 C  CG    . ASN B  1  817  ? 19.491  39.913  88.491  1.00 17.21 ? 815  ASN B CG    1 
ATOM   14989 O  OD1   . ASN B  1  817  ? 19.330  40.975  87.871  1.00 16.57 ? 815  ASN B OD1   1 
ATOM   14990 N  ND2   . ASN B  1  817  ? 19.849  38.783  87.901  1.00 14.46 ? 815  ASN B ND2   1 
ATOM   14991 N  N     . ALA B  1  818  ? 19.543  41.525  92.891  1.00 16.70 ? 816  ALA B N     1 
ATOM   14992 C  CA    . ALA B  1  818  ? 19.487  41.471  94.344  1.00 15.84 ? 816  ALA B CA    1 
ATOM   14993 C  C     . ALA B  1  818  ? 18.109  41.045  94.813  1.00 15.99 ? 816  ALA B C     1 
ATOM   14994 O  O     . ALA B  1  818  ? 17.102  41.207  94.118  1.00 17.07 ? 816  ALA B O     1 
ATOM   14995 C  CB    . ALA B  1  818  ? 19.829  42.837  94.959  1.00 16.52 ? 816  ALA B CB    1 
ATOM   14996 N  N     . MET B  1  819  ? 18.076  40.489  96.011  1.00 15.90 ? 817  MET B N     1 
ATOM   14997 C  CA    . MET B  1  819  ? 16.836  40.288  96.738  1.00 16.59 ? 817  MET B CA    1 
ATOM   14998 C  C     . MET B  1  819  ? 17.041  40.890  98.116  1.00 16.50 ? 817  MET B C     1 
ATOM   14999 O  O     . MET B  1  819  ? 18.048  40.603  98.772  1.00 16.89 ? 817  MET B O     1 
ATOM   15000 C  CB    . MET B  1  819  ? 16.451  38.811  96.851  1.00 16.49 ? 817  MET B CB    1 
ATOM   15001 C  CG    . MET B  1  819  ? 15.221  38.577  97.737  1.00 17.33 ? 817  MET B CG    1 
ATOM   15002 S  SD    . MET B  1  819  ? 14.941  36.812  98.016  1.00 19.56 ? 817  MET B SD    1 
ATOM   15003 C  CE    . MET B  1  819  ? 14.402  36.301  96.382  1.00 20.16 ? 817  MET B CE    1 
ATOM   15004 N  N     . ILE B  1  820  ? 16.106  41.736  98.534  1.00 16.44 ? 818  ILE B N     1 
ATOM   15005 C  CA    . ILE B  1  820  ? 16.126  42.331  99.860  1.00 15.96 ? 818  ILE B CA    1 
ATOM   15006 C  C     . ILE B  1  820  ? 15.100  41.616  100.714 1.00 16.86 ? 818  ILE B C     1 
ATOM   15007 O  O     . ILE B  1  820  ? 13.948  41.454  100.304 1.00 17.46 ? 818  ILE B O     1 
ATOM   15008 C  CB    . ILE B  1  820  ? 15.835  43.839  99.795  1.00 17.35 ? 818  ILE B CB    1 
ATOM   15009 C  CG1   . ILE B  1  820  ? 16.946  44.535  99.006  1.00 20.34 ? 818  ILE B CG1   1 
ATOM   15010 C  CG2   . ILE B  1  820  ? 15.704  44.404  101.216 1.00 19.02 ? 818  ILE B CG2   1 
ATOM   15011 C  CD1   . ILE B  1  820  ? 16.754  46.026  98.863  1.00 21.57 ? 818  ILE B CD1   1 
ATOM   15012 N  N     . VAL B  1  821  ? 15.524  41.176  101.896 1.00 16.87 ? 819  VAL B N     1 
ATOM   15013 C  CA    . VAL B  1  821  ? 14.684  40.448  102.836 1.00 16.18 ? 819  VAL B CA    1 
ATOM   15014 C  C     . VAL B  1  821  ? 14.694  41.215  104.147 1.00 17.16 ? 819  VAL B C     1 
ATOM   15015 O  O     . VAL B  1  821  ? 15.771  41.475  104.697 1.00 19.07 ? 819  VAL B O     1 
ATOM   15016 C  CB    . VAL B  1  821  ? 15.221  39.028  103.055 1.00 16.23 ? 819  VAL B CB    1 
ATOM   15017 C  CG1   . VAL B  1  821  ? 14.345  38.271  104.051 1.00 18.05 ? 819  VAL B CG1   1 
ATOM   15018 C  CG2   . VAL B  1  821  ? 15.302  38.309  101.726 1.00 18.45 ? 819  VAL B CG2   1 
ATOM   15019 N  N     . ASP B  1  822  ? 13.515  41.569  104.655 1.00 17.65 ? 820  ASP B N     1 
ATOM   15020 C  CA    . ASP B  1  822  ? 13.495  42.222  105.959 1.00 18.94 ? 820  ASP B CA    1 
ATOM   15021 C  C     . ASP B  1  822  ? 13.058  41.229  107.032 1.00 20.73 ? 820  ASP B C     1 
ATOM   15022 O  O     . ASP B  1  822  ? 12.846  40.044  106.770 1.00 20.50 ? 820  ASP B O     1 
ATOM   15023 C  CB    . ASP B  1  822  ? 12.644  43.503  105.923 1.00 19.40 ? 820  ASP B CB    1 
ATOM   15024 C  CG    . ASP B  1  822  ? 11.142  43.266  105.873 1.00 20.62 ? 820  ASP B CG    1 
ATOM   15025 O  OD1   . ASP B  1  822  ? 10.641  42.140  106.050 1.00 19.53 ? 820  ASP B OD1   1 
ATOM   15026 O  OD2   . ASP B  1  822  ? 10.436  44.271  105.639 1.00 23.30 ? 820  ASP B OD2   1 
ATOM   15027 N  N     . SER B  1  823  ? 12.947  41.718  108.270 1.00 18.39 ? 821  SER B N     1 
ATOM   15028 C  CA    . SER B  1  823  ? 12.664  40.823  109.385 1.00 21.28 ? 821  SER B CA    1 
ATOM   15029 C  C     . SER B  1  823  ? 11.220  40.348  109.432 1.00 22.95 ? 821  SER B C     1 
ATOM   15030 O  O     . SER B  1  823  ? 10.892  39.502  110.275 1.00 23.92 ? 821  SER B O     1 
ATOM   15031 C  CB    . SER B  1  823  ? 13.032  41.504  110.701 1.00 20.63 ? 821  SER B CB    1 
ATOM   15032 O  OG    . SER B  1  823  ? 12.286  42.695  110.870 1.00 24.62 ? 821  SER B OG    1 
ATOM   15033 N  N     . SER B  1  824  ? 10.345  40.863  108.577 1.00 20.17 ? 822  SER B N     1 
ATOM   15034 C  CA    . SER B  1  824  ? 8.974   40.380  108.565 1.00 20.63 ? 822  SER B CA    1 
ATOM   15035 C  C     . SER B  1  824  ? 8.782   39.192  107.636 1.00 21.41 ? 822  SER B C     1 
ATOM   15036 O  O     . SER B  1  824  ? 7.745   38.526  107.710 1.00 23.70 ? 822  SER B O     1 
ATOM   15037 C  CB    . SER B  1  824  ? 8.009   41.499  108.158 1.00 22.36 ? 822  SER B CB    1 
ATOM   15038 O  OG    . SER B  1  824  ? 8.106   41.780  106.770 1.00 19.53 ? 822  SER B OG    1 
ATOM   15039 N  N     . ALA B  1  825  ? 9.742   38.919  106.758 1.00 18.30 ? 823  ALA B N     1 
ATOM   15040 C  CA    . ALA B  1  825  ? 9.588   37.837  105.800 1.00 19.84 ? 823  ALA B CA    1 
ATOM   15041 C  C     . ALA B  1  825  ? 9.599   36.485  106.505 1.00 21.81 ? 823  ALA B C     1 
ATOM   15042 O  O     . ALA B  1  825  ? 10.221  36.313  107.557 1.00 24.50 ? 823  ALA B O     1 
ATOM   15043 C  CB    . ALA B  1  825  ? 10.707  37.901  104.758 1.00 19.10 ? 823  ALA B CB    1 
ATOM   15044 N  N     . LEU B  1  826  ? 8.915   35.515  105.900 1.00 22.00 ? 824  LEU B N     1 
ATOM   15045 C  CA    . LEU B  1  826  ? 8.908   34.157  106.431 1.00 22.15 ? 824  LEU B CA    1 
ATOM   15046 C  C     . LEU B  1  826  ? 10.172  33.442  105.967 1.00 22.87 ? 824  LEU B C     1 
ATOM   15047 O  O     . LEU B  1  826  ? 10.387  33.271  104.762 1.00 22.94 ? 824  LEU B O     1 
ATOM   15048 C  CB    . LEU B  1  826  ? 7.660   33.410  105.973 1.00 27.45 ? 824  LEU B CB    1 
ATOM   15049 C  CG    . LEU B  1  826  ? 7.461   31.987  106.505 1.00 27.39 ? 824  LEU B CG    1 
ATOM   15050 C  CD1   . LEU B  1  826  ? 7.515   31.976  108.019 1.00 31.80 ? 824  LEU B CD1   1 
ATOM   15051 C  CD2   . LEU B  1  826  ? 6.129   31.443  106.010 1.00 33.18 ? 824  LEU B CD2   1 
ATOM   15052 N  N     . ALA B  1  827  ? 11.008  33.027  106.924 1.00 22.38 ? 825  ALA B N     1 
ATOM   15053 C  CA    . ALA B  1  827  ? 12.319  32.480  106.579 1.00 20.10 ? 825  ALA B CA    1 
ATOM   15054 C  C     . ALA B  1  827  ? 12.203  31.302  105.618 1.00 22.31 ? 825  ALA B C     1 
ATOM   15055 O  O     . ALA B  1  827  ? 12.967  31.212  104.646 1.00 20.82 ? 825  ALA B O     1 
ATOM   15056 C  CB    . ALA B  1  827  ? 13.063  32.066  107.846 1.00 23.77 ? 825  ALA B CB    1 
ATOM   15057 N  N     . GLU B  1  828  ? 11.263  30.387  105.873 1.00 21.53 ? 826  GLU B N     1 
ATOM   15058 C  CA    . GLU B  1  828  ? 11.125  29.208  105.019 1.00 23.31 ? 826  GLU B CA    1 
ATOM   15059 C  C     . GLU B  1  828  ? 10.824  29.596  103.579 1.00 23.80 ? 826  GLU B C     1 
ATOM   15060 O  O     . GLU B  1  828  ? 11.349  28.982  102.639 1.00 21.20 ? 826  GLU B O     1 
ATOM   15061 C  CB    . GLU B  1  828  ? 10.023  28.296  105.551 1.00 22.47 ? 826  GLU B CB    1 
ATOM   15062 C  CG    . GLU B  1  828  ? 10.441  27.479  106.749 1.00 30.75 ? 826  GLU B CG    1 
ATOM   15063 C  CD    . GLU B  1  828  ? 10.429  28.250  108.063 1.00 33.00 ? 826  GLU B CD    1 
ATOM   15064 O  OE1   . GLU B  1  828  ? 10.045  29.445  108.081 1.00 28.38 ? 826  GLU B OE1   1 
ATOM   15065 O  OE2   . GLU B  1  828  ? 10.810  27.645  109.089 1.00 33.56 ? 826  GLU B OE2   1 
ATOM   15066 N  N     . GLN B  1  829  ? 9.965   30.599  103.388 1.00 20.65 ? 827  GLN B N     1 
ATOM   15067 C  CA    . GLN B  1  829  ? 9.641   31.075  102.048 1.00 22.27 ? 827  GLN B CA    1 
ATOM   15068 C  C     . GLN B  1  829  ? 10.849  31.720  101.393 1.00 21.01 ? 827  GLN B C     1 
ATOM   15069 O  O     . GLN B  1  829  ? 11.128  31.483  100.212 1.00 20.20 ? 827  GLN B O     1 
ATOM   15070 C  CB    . GLN B  1  829  ? 8.503   32.094  102.108 1.00 26.14 ? 827  GLN B CB    1 
ATOM   15071 C  CG    . GLN B  1  829  ? 7.125   31.567  102.364 1.00 36.95 ? 827  GLN B CG    1 
ATOM   15072 C  CD    . GLN B  1  829  ? 6.088   32.664  102.159 1.00 44.20 ? 827  GLN B CD    1 
ATOM   15073 O  OE1   . GLN B  1  829  ? 6.411   33.857  102.230 1.00 35.32 ? 827  GLN B OE1   1 
ATOM   15074 N  NE2   . GLN B  1  829  ? 4.850   32.271  101.891 1.00 44.17 ? 827  GLN B NE2   1 
ATOM   15075 N  N     . VAL B  1  830  ? 11.559  32.571  102.142 1.00 19.36 ? 828  VAL B N     1 
ATOM   15076 C  CA    . VAL B  1  830  ? 12.779  33.184  101.631 1.00 17.98 ? 828  VAL B CA    1 
ATOM   15077 C  C     . VAL B  1  830  ? 13.746  32.108  101.175 1.00 20.82 ? 828  VAL B C     1 
ATOM   15078 O  O     . VAL B  1  830  ? 14.293  32.165  100.071 1.00 18.89 ? 828  VAL B O     1 
ATOM   15079 C  CB    . VAL B  1  830  ? 13.431  34.072  102.706 1.00 17.87 ? 828  VAL B CB    1 
ATOM   15080 C  CG1   . VAL B  1  830  ? 14.818  34.534  102.242 1.00 19.06 ? 828  VAL B CG1   1 
ATOM   15081 C  CG2   . VAL B  1  830  ? 12.544  35.242  103.032 1.00 21.09 ? 828  VAL B CG2   1 
ATOM   15082 N  N     . VAL B  1  831  ? 13.990  31.117  102.033 1.00 18.61 ? 829  VAL B N     1 
ATOM   15083 C  CA    . VAL B  1  831  ? 15.017  30.137  101.702 1.00 16.80 ? 829  VAL B CA    1 
ATOM   15084 C  C     . VAL B  1  831  ? 14.651  29.381  100.432 1.00 18.69 ? 829  VAL B C     1 
ATOM   15085 O  O     . VAL B  1  831  ? 15.495  29.186  99.549  1.00 19.61 ? 829  VAL B O     1 
ATOM   15086 C  CB    . VAL B  1  831  ? 15.250  29.197  102.895 1.00 17.28 ? 829  VAL B CB    1 
ATOM   15087 C  CG1   . VAL B  1  831  ? 16.036  27.961  102.458 1.00 21.09 ? 829  VAL B CG1   1 
ATOM   15088 C  CG2   . VAL B  1  831  ? 15.999  29.948  103.971 1.00 20.75 ? 829  VAL B CG2   1 
ATOM   15089 N  N     . GLY B  1  832  ? 13.390  28.964  100.305 1.00 17.39 ? 830  GLY B N     1 
ATOM   15090 C  CA    . GLY B  1  832  ? 12.970  28.279  99.093  1.00 17.82 ? 830  GLY B CA    1 
ATOM   15091 C  C     . GLY B  1  832  ? 13.148  29.138  97.860  1.00 21.00 ? 830  GLY B C     1 
ATOM   15092 O  O     . GLY B  1  832  ? 13.615  28.664  96.821  1.00 19.88 ? 830  GLY B O     1 
ATOM   15093 N  N     . ASP B  1  833  ? 12.796  30.417  97.962  1.00 19.33 ? 831  ASP B N     1 
ATOM   15094 C  CA    . ASP B  1  833  ? 12.928  31.300  96.809  1.00 17.44 ? 831  ASP B CA    1 
ATOM   15095 C  C     . ASP B  1  833  ? 14.380  31.670  96.542  1.00 18.13 ? 831  ASP B C     1 
ATOM   15096 O  O     . ASP B  1  833  ? 14.748  31.959  95.398  1.00 18.69 ? 831  ASP B O     1 
ATOM   15097 C  CB    . ASP B  1  833  ? 12.084  32.559  97.014  1.00 16.37 ? 831  ASP B CB    1 
ATOM   15098 C  CG    . ASP B  1  833  ? 10.597  32.261  97.002  1.00 21.26 ? 831  ASP B CG    1 
ATOM   15099 O  OD1   . ASP B  1  833  ? 10.208  31.164  96.536  1.00 22.39 ? 831  ASP B OD1   1 
ATOM   15100 O  OD2   . ASP B  1  833  ? 9.808   33.107  97.467  1.00 20.90 ? 831  ASP B OD2   1 
ATOM   15101 N  N     . VAL B  1  834  ? 15.225  31.680  97.572  1.00 17.04 ? 832  VAL B N     1 
ATOM   15102 C  CA    . VAL B  1  834  ? 16.641  31.931  97.330  1.00 16.56 ? 832  VAL B CA    1 
ATOM   15103 C  C     . VAL B  1  834  ? 17.286  30.728  96.665  1.00 18.40 ? 832  VAL B C     1 
ATOM   15104 O  O     . VAL B  1  834  ? 18.099  30.868  95.738  1.00 18.78 ? 832  VAL B O     1 
ATOM   15105 C  CB    . VAL B  1  834  ? 17.349  32.285  98.646  1.00 17.68 ? 832  VAL B CB    1 
ATOM   15106 C  CG1   . VAL B  1  834  ? 18.863  32.213  98.473  1.00 19.14 ? 832  VAL B CG1   1 
ATOM   15107 C  CG2   . VAL B  1  834  ? 16.896  33.662  99.120  1.00 18.52 ? 832  VAL B CG2   1 
ATOM   15108 N  N     . ILE B  1  835  ? 16.976  29.528  97.156  1.00 17.35 ? 833  ILE B N     1 
ATOM   15109 C  CA    . ILE B  1  835  ? 17.593  28.328  96.595  1.00 19.28 ? 833  ILE B CA    1 
ATOM   15110 C  C     . ILE B  1  835  ? 17.261  28.218  95.117  1.00 21.05 ? 833  ILE B C     1 
ATOM   15111 O  O     . ILE B  1  835  ? 18.127  27.917  94.288  1.00 23.09 ? 833  ILE B O     1 
ATOM   15112 C  CB    . ILE B  1  835  ? 17.139  27.074  97.360  1.00 21.50 ? 833  ILE B CB    1 
ATOM   15113 C  CG1   . ILE B  1  835  ? 17.644  27.102  98.802  1.00 27.31 ? 833  ILE B CG1   1 
ATOM   15114 C  CG2   . ILE B  1  835  ? 17.609  25.809  96.626  1.00 25.21 ? 833  ILE B CG2   1 
ATOM   15115 C  CD1   . ILE B  1  835  ? 18.858  26.279  99.042  1.00 33.49 ? 833  ILE B CD1   1 
ATOM   15116 N  N     . THR B  1  836  ? 16.011  28.481  94.765  1.00 19.52 ? 834  THR B N     1 
ATOM   15117 C  CA    A THR B  1  836  ? 15.609  28.478  93.365  0.56 19.34 ? 834  THR B CA    1 
ATOM   15118 C  CA    B THR B  1  836  ? 15.647  28.454  93.353  0.44 19.36 ? 834  THR B CA    1 
ATOM   15119 C  C     . THR B  1  836  ? 16.298  29.602  92.598  1.00 19.85 ? 834  THR B C     1 
ATOM   15120 O  O     . THR B  1  836  ? 16.958  29.377  91.581  1.00 22.13 ? 834  THR B O     1 
ATOM   15121 C  CB    A THR B  1  836  ? 14.086  28.609  93.292  0.56 20.90 ? 834  THR B CB    1 
ATOM   15122 C  CB    B THR B  1  836  ? 14.131  28.499  93.172  0.44 21.09 ? 834  THR B CB    1 
ATOM   15123 O  OG1   A THR B  1  836  ? 13.481  27.462  93.910  0.56 24.19 ? 834  THR B OG1   1 
ATOM   15124 O  OG1   B THR B  1  836  ? 13.606  29.665  93.806  0.44 19.34 ? 834  THR B OG1   1 
ATOM   15125 C  CG2   A THR B  1  836  ? 13.614  28.713  91.858  0.56 18.71 ? 834  THR B CG2   1 
ATOM   15126 C  CG2   B THR B  1  836  ? 13.481  27.250  93.744  0.44 23.61 ? 834  THR B CG2   1 
ATOM   15127 N  N     . SER B  1  837  ? 16.149  30.837  93.083  1.00 17.93 ? 835  SER B N     1 
ATOM   15128 C  CA    . SER B  1  837  ? 16.629  31.974  92.304  1.00 17.03 ? 835  SER B CA    1 
ATOM   15129 C  C     . SER B  1  837  ? 18.132  31.931  92.095  1.00 15.52 ? 835  SER B C     1 
ATOM   15130 O  O     . SER B  1  837  ? 18.630  32.338  91.041  1.00 17.43 ? 835  SER B O     1 
ATOM   15131 C  CB    . SER B  1  837  ? 16.248  33.290  92.978  1.00 15.85 ? 835  SER B CB    1 
ATOM   15132 O  OG    . SER B  1  837  ? 14.847  33.381  93.119  1.00 16.90 ? 835  SER B OG    1 
ATOM   15133 N  N     . ALA B  1  838  ? 18.882  31.502  93.114  1.00 16.39 ? 836  ALA B N     1 
ATOM   15134 C  CA    . ALA B  1  838  ? 20.328  31.566  93.027  1.00 17.43 ? 836  ALA B CA    1 
ATOM   15135 C  C     . ALA B  1  838  ? 20.946  30.354  92.344  1.00 16.66 ? 836  ALA B C     1 
ATOM   15136 O  O     . ALA B  1  838  ? 21.976  30.493  91.680  1.00 18.09 ? 836  ALA B O     1 
ATOM   15137 C  CB    . ALA B  1  838  ? 20.933  31.710  94.431  1.00 17.35 ? 836  ALA B CB    1 
ATOM   15138 N  N     . PHE B  1  839  ? 20.357  29.169  92.499  1.00 17.54 ? 837  PHE B N     1 
ATOM   15139 C  CA    . PHE B  1  839  ? 21.064  27.952  92.134  1.00 18.78 ? 837  PHE B CA    1 
ATOM   15140 C  C     . PHE B  1  839  ? 20.345  27.093  91.107  1.00 20.27 ? 837  PHE B C     1 
ATOM   15141 O  O     . PHE B  1  839  ? 20.974  26.188  90.544  1.00 19.37 ? 837  PHE B O     1 
ATOM   15142 C  CB    . PHE B  1  839  ? 21.363  27.122  93.390  1.00 19.04 ? 837  PHE B CB    1 
ATOM   15143 C  CG    . PHE B  1  839  ? 22.112  27.894  94.454  1.00 18.73 ? 837  PHE B CG    1 
ATOM   15144 C  CD1   . PHE B  1  839  ? 23.343  28.479  94.183  1.00 18.66 ? 837  PHE B CD1   1 
ATOM   15145 C  CD2   . PHE B  1  839  ? 21.572  28.053  95.723  1.00 21.02 ? 837  PHE B CD2   1 
ATOM   15146 C  CE1   . PHE B  1  839  ? 24.031  29.192  95.161  1.00 18.36 ? 837  PHE B CE1   1 
ATOM   15147 C  CE2   . PHE B  1  839  ? 22.262  28.770  96.714  1.00 21.78 ? 837  PHE B CE2   1 
ATOM   15148 C  CZ    . PHE B  1  839  ? 23.489  29.340  96.426  1.00 22.76 ? 837  PHE B CZ    1 
ATOM   15149 N  N     . ASP B  1  840  ? 19.064  27.346  90.839  1.00 17.66 ? 838  ASP B N     1 
ATOM   15150 C  CA    . ASP B  1  840  ? 18.408  26.732  89.695  1.00 18.55 ? 838  ASP B CA    1 
ATOM   15151 C  C     . ASP B  1  840  ? 19.250  26.956  88.450  1.00 20.04 ? 838  ASP B C     1 
ATOM   15152 O  O     . ASP B  1  840  ? 19.784  28.047  88.225  1.00 19.18 ? 838  ASP B O     1 
ATOM   15153 C  CB    . ASP B  1  840  ? 17.011  27.330  89.509  1.00 20.82 ? 838  ASP B CB    1 
ATOM   15154 C  CG    . ASP B  1  840  ? 16.287  26.773  88.314  1.00 22.62 ? 838  ASP B CG    1 
ATOM   15155 O  OD1   . ASP B  1  840  ? 16.642  27.138  87.177  1.00 24.83 ? 838  ASP B OD1   1 
ATOM   15156 O  OD2   . ASP B  1  840  ? 15.344  25.983  88.518  1.00 28.53 ? 838  ASP B OD2   1 
ATOM   15157 N  N     . SER B  1  841  ? 19.386  25.901  87.653  1.00 19.94 ? 839  SER B N     1 
ATOM   15158 C  CA    . SER B  1  841  ? 20.203  25.935  86.445  1.00 22.90 ? 839  SER B CA    1 
ATOM   15159 C  C     . SER B  1  841  ? 21.627  26.368  86.751  1.00 19.50 ? 839  SER B C     1 
ATOM   15160 O  O     . SER B  1  841  ? 22.283  27.016  85.928  1.00 19.43 ? 839  SER B O     1 
ATOM   15161 C  CB    . SER B  1  841  ? 19.577  26.839  85.381  1.00 23.34 ? 839  SER B CB    1 
ATOM   15162 O  OG    . SER B  1  841  ? 18.228  26.462  85.162  1.00 22.54 ? 839  SER B OG    1 
ATOM   15163 N  N     . ALA B  1  842  ? 22.105  26.002  87.943  1.00 18.34 ? 840  ALA B N     1 
ATOM   15164 C  CA    . ALA B  1  842  ? 23.430  26.369  88.420  1.00 18.08 ? 840  ALA B CA    1 
ATOM   15165 C  C     . ALA B  1  842  ? 23.662  27.868  88.269  1.00 18.70 ? 840  ALA B C     1 
ATOM   15166 O  O     . ALA B  1  842  ? 24.758  28.318  87.938  1.00 18.36 ? 840  ALA B O     1 
ATOM   15167 C  CB    . ALA B  1  842  ? 24.522  25.565  87.703  1.00 21.91 ? 840  ALA B CB    1 
ATOM   15168 N  N     . GLY B  1  843  ? 22.607  28.643  88.527  1.00 16.93 ? 841  GLY B N     1 
ATOM   15169 C  CA    . GLY B  1  843  ? 22.693  30.088  88.482  1.00 17.98 ? 841  GLY B CA    1 
ATOM   15170 C  C     . GLY B  1  843  ? 22.964  30.643  87.106  1.00 18.29 ? 841  GLY B C     1 
ATOM   15171 O  O     . GLY B  1  843  ? 23.384  31.796  86.982  1.00 18.50 ? 841  GLY B O     1 
ATOM   15172 N  N     . GLN B  1  844  ? 22.757  29.840  86.067  1.00 16.19 ? 842  GLN B N     1 
ATOM   15173 C  CA    . GLN B  1  844  ? 22.982  30.285  84.692  1.00 18.62 ? 842  GLN B CA    1 
ATOM   15174 C  C     . GLN B  1  844  ? 21.703  30.826  84.068  1.00 19.11 ? 842  GLN B C     1 
ATOM   15175 O  O     . GLN B  1  844  ? 21.248  30.403  83.008  1.00 22.88 ? 842  GLN B O     1 
ATOM   15176 C  CB    . GLN B  1  844  ? 23.563  29.141  83.876  1.00 16.09 ? 842  GLN B CB    1 
ATOM   15177 C  CG    . GLN B  1  844  ? 24.881  28.686  84.478  1.00 17.64 ? 842  GLN B CG    1 
ATOM   15178 C  CD    . GLN B  1  844  ? 25.427  27.423  83.882  1.00 24.03 ? 842  GLN B CD    1 
ATOM   15179 O  OE1   . GLN B  1  844  ? 26.518  27.410  83.314  1.00 18.01 ? 842  GLN B OE1   1 
ATOM   15180 N  NE2   . GLN B  1  844  ? 24.706  26.333  84.066  1.00 27.17 ? 842  GLN B NE2   1 
ATOM   15181 N  N     . ARG B  1  845  ? 21.075  31.727  84.803  1.00 16.65 ? 843  ARG B N     1 
ATOM   15182 C  CA    . ARG B  1  845  ? 19.954  32.520  84.334  1.00 16.59 ? 843  ARG B CA    1 
ATOM   15183 C  C     . ARG B  1  845  ? 20.375  33.978  84.418  1.00 17.86 ? 843  ARG B C     1 
ATOM   15184 O  O     . ARG B  1  845  ? 21.002  34.398  85.397  1.00 17.45 ? 843  ARG B O     1 
ATOM   15185 C  CB    . ARG B  1  845  ? 18.728  32.292  85.188  1.00 15.61 ? 843  ARG B CB    1 
ATOM   15186 C  CG    . ARG B  1  845  ? 18.186  30.889  85.160  1.00 17.52 ? 843  ARG B CG    1 
ATOM   15187 C  CD    . ARG B  1  845  ? 16.874  30.881  85.913  1.00 21.23 ? 843  ARG B CD    1 
ATOM   15188 N  NE    . ARG B  1  845  ? 16.244  29.569  85.903  1.00 26.09 ? 843  ARG B NE    1 
ATOM   15189 C  CZ    . ARG B  1  845  ? 15.171  29.250  85.193  1.00 23.77 ? 843  ARG B CZ    1 
ATOM   15190 N  NH1   . ARG B  1  845  ? 14.565  30.132  84.408  1.00 25.25 ? 843  ARG B NH1   1 
ATOM   15191 N  NH2   . ARG B  1  845  ? 14.682  28.019  85.283  1.00 26.55 ? 843  ARG B NH2   1 
ATOM   15192 N  N     . CYS B  1  846  ? 20.048  34.766  83.397  1.00 18.21 ? 844  CYS B N     1 
ATOM   15193 C  CA    . CYS B  1  846  ? 20.324  36.192  83.521  1.00 19.49 ? 844  CYS B CA    1 
ATOM   15194 C  C     . CYS B  1  846  ? 19.586  36.790  84.707  1.00 15.73 ? 844  CYS B C     1 
ATOM   15195 O  O     . CYS B  1  846  ? 20.055  37.767  85.296  1.00 19.06 ? 844  CYS B O     1 
ATOM   15196 C  CB    . CYS B  1  846  ? 19.911  36.920  82.251  1.00 21.14 ? 844  CYS B CB    1 
ATOM   15197 S  SG    . CYS B  1  846  ? 18.235  36.534  81.732  1.00 25.14 ? 844  CYS B SG    1 
ATOM   15198 N  N     . SER B  1  847  ? 18.439  36.208  85.051  1.00 16.65 ? 845  SER B N     1 
ATOM   15199 C  CA    . SER B  1  847  ? 17.583  36.622  86.152  1.00 16.32 ? 845  SER B CA    1 
ATOM   15200 C  C     . SER B  1  847  ? 18.052  36.120  87.510  1.00 15.92 ? 845  SER B C     1 
ATOM   15201 O  O     . SER B  1  847  ? 17.430  36.476  88.516  1.00 15.43 ? 845  SER B O     1 
ATOM   15202 C  CB    . SER B  1  847  ? 16.179  36.089  85.911  1.00 17.38 ? 845  SER B CB    1 
ATOM   15203 O  OG    . SER B  1  847  ? 16.270  34.684  85.671  1.00 17.78 ? 845  SER B OG    1 
ATOM   15204 N  N     . ALA B  1  848  ? 19.096  35.295  87.557  1.00 17.31 ? 846  ALA B N     1 
ATOM   15205 C  CA    . ALA B  1  848  ? 19.456  34.604  88.790  1.00 15.78 ? 846  ALA B CA    1 
ATOM   15206 C  C     . ALA B  1  848  ? 19.782  35.582  89.908  1.00 16.69 ? 846  ALA B C     1 
ATOM   15207 O  O     . ALA B  1  848  ? 20.329  36.664  89.687  1.00 16.36 ? 846  ALA B O     1 
ATOM   15208 C  CB    . ALA B  1  848  ? 20.665  33.692  88.565  1.00 15.91 ? 846  ALA B CB    1 
ATOM   15209 N  N     . LEU B  1  849  ? 19.441  35.178  91.129  1.00 17.33 ? 847  LEU B N     1 
ATOM   15210 C  CA    . LEU B  1  849  ? 19.786  35.959  92.309  1.00 16.28 ? 847  LEU B CA    1 
ATOM   15211 C  C     . LEU B  1  849  ? 21.294  35.935  92.559  1.00 15.87 ? 847  LEU B C     1 
ATOM   15212 O  O     . LEU B  1  849  ? 21.878  34.865  92.749  1.00 17.67 ? 847  LEU B O     1 
ATOM   15213 C  CB    . LEU B  1  849  ? 19.035  35.398  93.508  1.00 17.89 ? 847  LEU B CB    1 
ATOM   15214 C  CG    . LEU B  1  849  ? 19.424  35.993  94.856  1.00 15.61 ? 847  LEU B CG    1 
ATOM   15215 C  CD1   . LEU B  1  849  ? 19.154  37.509  94.889  1.00 17.86 ? 847  LEU B CD1   1 
ATOM   15216 C  CD2   . LEU B  1  849  ? 18.613  35.273  95.915  1.00 17.10 ? 847  LEU B CD2   1 
ATOM   15217 N  N     . ARG B  1  850  ? 21.923  37.114  92.564  1.00 15.26 ? 848  ARG B N     1 
ATOM   15218 C  CA    . ARG B  1  850  ? 23.359  37.242  92.785  1.00 16.15 ? 848  ARG B CA    1 
ATOM   15219 C  C     . ARG B  1  850  ? 23.707  37.789  94.156  1.00 16.96 ? 848  ARG B C     1 
ATOM   15220 O  O     . ARG B  1  850  ? 24.764  37.445  94.700  1.00 18.75 ? 848  ARG B O     1 
ATOM   15221 C  CB    . ARG B  1  850  ? 23.985  38.162  91.721  1.00 17.25 ? 848  ARG B CB    1 
ATOM   15222 C  CG    . ARG B  1  850  ? 23.634  37.770  90.292  1.00 17.02 ? 848  ARG B CG    1 
ATOM   15223 C  CD    . ARG B  1  850  ? 23.976  36.332  90.014  1.00 17.33 ? 848  ARG B CD    1 
ATOM   15224 N  NE    . ARG B  1  850  ? 23.780  36.017  88.600  1.00 18.70 ? 848  ARG B NE    1 
ATOM   15225 C  CZ    . ARG B  1  850  ? 23.926  34.803  88.089  1.00 19.40 ? 848  ARG B CZ    1 
ATOM   15226 N  NH1   . ARG B  1  850  ? 24.212  33.767  88.856  1.00 18.21 ? 848  ARG B NH1   1 
ATOM   15227 N  NH2   . ARG B  1  850  ? 23.759  34.623  86.777  1.00 18.08 ? 848  ARG B NH2   1 
ATOM   15228 N  N     . VAL B  1  851  ? 22.868  38.656  94.716  1.00 17.63 ? 849  VAL B N     1 
ATOM   15229 C  CA    . VAL B  1  851  ? 23.163  39.319  95.981  1.00 18.48 ? 849  VAL B CA    1 
ATOM   15230 C  C     . VAL B  1  851  ? 21.926  39.217  96.862  1.00 19.37 ? 849  VAL B C     1 
ATOM   15231 O  O     . VAL B  1  851  ? 20.903  39.845  96.571  1.00 18.61 ? 849  VAL B O     1 
ATOM   15232 C  CB    . VAL B  1  851  ? 23.566  40.788  95.794  1.00 19.95 ? 849  VAL B CB    1 
ATOM   15233 C  CG1   . VAL B  1  851  ? 24.022  41.363  97.141  1.00 21.68 ? 849  VAL B CG1   1 
ATOM   15234 C  CG2   . VAL B  1  851  ? 24.670  40.937  94.746  1.00 23.86 ? 849  VAL B CG2   1 
ATOM   15235 N  N     . LEU B  1  852  ? 22.020  38.441  97.941  1.00 17.79 ? 850  LEU B N     1 
ATOM   15236 C  CA    . LEU B  1  852  ? 20.954  38.328  98.924  1.00 19.08 ? 850  LEU B CA    1 
ATOM   15237 C  C     . LEU B  1  852  ? 21.249  39.315  100.044 1.00 17.03 ? 850  LEU B C     1 
ATOM   15238 O  O     . LEU B  1  852  ? 22.319  39.252  100.653 1.00 17.80 ? 850  LEU B O     1 
ATOM   15239 C  CB    . LEU B  1  852  ? 20.876  36.901  99.467  1.00 16.33 ? 850  LEU B CB    1 
ATOM   15240 C  CG    . LEU B  1  852  ? 19.848  36.662  100.575 1.00 17.32 ? 850  LEU B CG    1 
ATOM   15241 C  CD1   . LEU B  1  852  ? 18.418  36.951  100.102 1.00 17.78 ? 850  LEU B CD1   1 
ATOM   15242 C  CD2   . LEU B  1  852  ? 19.955  35.225  101.061 1.00 19.93 ? 850  LEU B CD2   1 
ATOM   15243 N  N     . CYS B  1  853  ? 20.317  40.231  100.301 1.00 17.50 ? 851  CYS B N     1 
ATOM   15244 C  CA    . CYS B  1  853  ? 20.486  41.275  101.310 1.00 17.76 ? 851  CYS B CA    1 
ATOM   15245 C  C     . CYS B  1  853  ? 19.550  40.974  102.468 1.00 17.38 ? 851  CYS B C     1 
ATOM   15246 O  O     . CYS B  1  853  ? 18.326  41.041  102.320 1.00 17.64 ? 851  CYS B O     1 
ATOM   15247 C  CB    . CYS B  1  853  ? 20.192  42.652  100.736 1.00 18.24 ? 851  CYS B CB    1 
ATOM   15248 S  SG    . CYS B  1  853  ? 21.066  42.961  99.197  1.00 21.06 ? 851  CYS B SG    1 
ATOM   15249 N  N     . LEU B  1  854  ? 20.125  40.652  103.621 1.00 17.11 ? 852  LEU B N     1 
ATOM   15250 C  CA    . LEU B  1  854  ? 19.359  40.179  104.763 1.00 17.54 ? 852  LEU B CA    1 
ATOM   15251 C  C     . LEU B  1  854  ? 19.408  41.207  105.879 1.00 18.29 ? 852  LEU B C     1 
ATOM   15252 O  O     . LEU B  1  854  ? 20.494  41.633  106.282 1.00 19.76 ? 852  LEU B O     1 
ATOM   15253 C  CB    . LEU B  1  854  ? 19.928  38.863  105.286 1.00 17.27 ? 852  LEU B CB    1 
ATOM   15254 C  CG    . LEU B  1  854  ? 19.942  37.703  104.308 1.00 16.92 ? 852  LEU B CG    1 
ATOM   15255 C  CD1   . LEU B  1  854  ? 20.619  36.530  104.991 1.00 18.12 ? 852  LEU B CD1   1 
ATOM   15256 C  CD2   . LEU B  1  854  ? 18.522  37.363  103.906 1.00 18.30 ? 852  LEU B CD2   1 
ATOM   15257 N  N     . GLN B  1  855  ? 18.241  41.584  106.391 1.00 18.41 ? 853  GLN B N     1 
ATOM   15258 C  CA    . GLN B  1  855  ? 18.215  42.454  107.560 1.00 17.27 ? 853  GLN B CA    1 
ATOM   15259 C  C     . GLN B  1  855  ? 19.010  41.809  108.686 1.00 21.47 ? 853  GLN B C     1 
ATOM   15260 O  O     . GLN B  1  855  ? 18.910  40.600  108.921 1.00 19.92 ? 853  GLN B O     1 
ATOM   15261 C  CB    . GLN B  1  855  ? 16.783  42.724  108.010 1.00 17.57 ? 853  GLN B CB    1 
ATOM   15262 C  CG    . GLN B  1  855  ? 16.712  43.938  108.932 1.00 20.79 ? 853  GLN B CG    1 
ATOM   15263 C  CD    . GLN B  1  855  ? 15.322  44.230  109.438 1.00 24.24 ? 853  GLN B CD    1 
ATOM   15264 O  OE1   . GLN B  1  855  ? 14.352  44.197  108.682 1.00 24.83 ? 853  GLN B OE1   1 
ATOM   15265 N  NE2   . GLN B  1  855  ? 15.218  44.532  110.730 1.00 27.43 ? 853  GLN B NE2   1 
ATOM   15266 N  N     . GLU B  1  856  ? 19.832  42.625  109.351 1.00 19.83 ? 854  GLU B N     1 
ATOM   15267 C  CA    . GLU B  1  856  ? 20.827  42.105  110.283 1.00 21.75 ? 854  GLU B CA    1 
ATOM   15268 C  C     . GLU B  1  856  ? 20.198  41.184  111.323 1.00 21.93 ? 854  GLU B C     1 
ATOM   15269 O  O     . GLU B  1  856  ? 20.771  40.144  111.675 1.00 23.21 ? 854  GLU B O     1 
ATOM   15270 C  CB    . GLU B  1  856  ? 21.550  43.279  110.953 1.00 25.20 ? 854  GLU B CB    1 
ATOM   15271 C  CG    . GLU B  1  856  ? 22.385  42.887  112.159 1.00 34.91 ? 854  GLU B CG    1 
ATOM   15272 C  CD    . GLU B  1  856  ? 23.539  41.980  111.785 1.00 41.01 ? 854  GLU B CD    1 
ATOM   15273 O  OE1   . GLU B  1  856  ? 23.940  41.994  110.599 1.00 39.91 ? 854  GLU B OE1   1 
ATOM   15274 O  OE2   . GLU B  1  856  ? 24.045  41.256  112.673 1.00 44.86 ? 854  GLU B OE2   1 
ATOM   15275 N  N     . ASP B  1  857  ? 19.001  41.535  111.799 1.00 22.74 ? 855  ASP B N     1 
ATOM   15276 C  CA    . ASP B  1  857  ? 18.379  40.812  112.905 1.00 25.51 ? 855  ASP B CA    1 
ATOM   15277 C  C     . ASP B  1  857  ? 17.976  39.393  112.539 1.00 24.99 ? 855  ASP B C     1 
ATOM   15278 O  O     . ASP B  1  857  ? 17.870  38.549  113.431 1.00 27.00 ? 855  ASP B O     1 
ATOM   15279 C  CB    . ASP B  1  857  ? 17.148  41.571  113.410 1.00 29.56 ? 855  ASP B CB    1 
ATOM   15280 N  N     . VAL B  1  858  ? 17.733  39.104  111.263 1.00 19.60 ? 856  VAL B N     1 
ATOM   15281 C  CA    . VAL B  1  858  ? 17.329  37.768  110.847 1.00 18.58 ? 856  VAL B CA    1 
ATOM   15282 C  C     . VAL B  1  858  ? 18.390  37.067  110.024 1.00 17.24 ? 856  VAL B C     1 
ATOM   15283 O  O     . VAL B  1  858  ? 18.172  35.922  109.613 1.00 20.30 ? 856  VAL B O     1 
ATOM   15284 C  CB    . VAL B  1  858  ? 15.993  37.795  110.078 1.00 20.04 ? 856  VAL B CB    1 
ATOM   15285 C  CG1   . VAL B  1  858  ? 14.857  38.225  110.999 1.00 23.66 ? 856  VAL B CG1   1 
ATOM   15286 C  CG2   . VAL B  1  858  ? 16.084  38.716  108.866 1.00 21.80 ? 856  VAL B CG2   1 
ATOM   15287 N  N     . ALA B  1  859  ? 19.536  37.705  109.779 1.00 20.84 ? 857  ALA B N     1 
ATOM   15288 C  CA    . ALA B  1  859  ? 20.492  37.164  108.814 1.00 19.74 ? 857  ALA B CA    1 
ATOM   15289 C  C     . ALA B  1  859  ? 21.030  35.803  109.249 1.00 17.72 ? 857  ALA B C     1 
ATOM   15290 O  O     . ALA B  1  859  ? 21.072  34.859  108.456 1.00 21.15 ? 857  ALA B O     1 
ATOM   15291 C  CB    . ALA B  1  859  ? 21.630  38.164  108.592 1.00 19.26 ? 857  ALA B CB    1 
ATOM   15292 N  N     . ASP B  1  860  ? 21.421  35.671  110.520 1.00 22.28 ? 858  ASP B N     1 
ATOM   15293 C  CA    . ASP B  1  860  ? 21.997  34.406  110.966 1.00 22.69 ? 858  ASP B CA    1 
ATOM   15294 C  C     . ASP B  1  860  ? 21.005  33.263  110.849 1.00 22.52 ? 858  ASP B C     1 
ATOM   15295 O  O     . ASP B  1  860  ? 21.366  32.164  110.412 1.00 21.82 ? 858  ASP B O     1 
ATOM   15296 C  CB    . ASP B  1  860  ? 22.482  34.518  112.410 1.00 21.64 ? 858  ASP B CB    1 
ATOM   15297 C  CG    . ASP B  1  860  ? 23.678  35.400  112.535 1.00 28.32 ? 858  ASP B CG    1 
ATOM   15298 O  OD1   . ASP B  1  860  ? 24.436  35.489  111.546 1.00 30.02 ? 858  ASP B OD1   1 
ATOM   15299 O  OD2   . ASP B  1  860  ? 23.855  36.009  113.611 1.00 34.82 ? 858  ASP B OD2   1 
ATOM   15300 N  N     . ARG B  1  861  ? 19.757  33.486  111.261 1.00 20.23 ? 859  ARG B N     1 
ATOM   15301 C  CA    . ARG B  1  861  ? 18.788  32.400  111.215 1.00 18.95 ? 859  ARG B CA    1 
ATOM   15302 C  C     . ARG B  1  861  ? 18.482  31.999  109.778 1.00 20.28 ? 859  ARG B C     1 
ATOM   15303 O  O     . ARG B  1  861  ? 18.412  30.806  109.459 1.00 20.87 ? 859  ARG B O     1 
ATOM   15304 C  CB    . ARG B  1  861  ? 17.509  32.801  111.945 1.00 24.08 ? 859  ARG B CB    1 
ATOM   15305 C  CG    . ARG B  1  861  ? 16.396  31.794  111.766 1.00 36.40 ? 859  ARG B CG    1 
ATOM   15306 C  CD    . ARG B  1  861  ? 15.421  31.771  112.926 1.00 45.25 ? 859  ARG B CD    1 
ATOM   15307 N  NE    . ARG B  1  861  ? 14.385  30.773  112.680 1.00 52.24 ? 859  ARG B NE    1 
ATOM   15308 C  CZ    . ARG B  1  861  ? 13.291  30.996  111.964 1.00 47.34 ? 859  ARG B CZ    1 
ATOM   15309 N  NH1   . ARG B  1  861  ? 13.022  32.193  111.467 1.00 39.42 ? 859  ARG B NH1   1 
ATOM   15310 N  NH2   . ARG B  1  861  ? 12.447  29.991  111.737 1.00 44.00 ? 859  ARG B NH2   1 
ATOM   15311 N  N     . ILE B  1  862  ? 18.324  32.978  108.889 1.00 19.39 ? 860  ILE B N     1 
ATOM   15312 C  CA    . ILE B  1  862  ? 18.081  32.645  107.491 1.00 16.87 ? 860  ILE B CA    1 
ATOM   15313 C  C     . ILE B  1  862  ? 19.288  31.939  106.882 1.00 17.15 ? 860  ILE B C     1 
ATOM   15314 O  O     . ILE B  1  862  ? 19.142  30.991  106.104 1.00 20.04 ? 860  ILE B O     1 
ATOM   15315 C  CB    . ILE B  1  862  ? 17.697  33.920  106.727 1.00 17.76 ? 860  ILE B CB    1 
ATOM   15316 C  CG1   . ILE B  1  862  ? 16.314  34.379  107.198 1.00 21.67 ? 860  ILE B CG1   1 
ATOM   15317 C  CG2   . ILE B  1  862  ? 17.669  33.665  105.241 1.00 19.53 ? 860  ILE B CG2   1 
ATOM   15318 C  CD1   . ILE B  1  862  ? 15.896  35.732  106.660 1.00 24.26 ? 860  ILE B CD1   1 
ATOM   15319 N  N     . LEU B  1  863  ? 20.498  32.383  107.212 1.00 18.42 ? 861  LEU B N     1 
ATOM   15320 C  CA    . LEU B  1  863  ? 21.677  31.743  106.631 1.00 21.19 ? 861  LEU B CA    1 
ATOM   15321 C  C     . LEU B  1  863  ? 21.816  30.299  107.096 1.00 22.99 ? 861  LEU B C     1 
ATOM   15322 O  O     . LEU B  1  863  ? 22.184  29.421  106.304 1.00 19.77 ? 861  LEU B O     1 
ATOM   15323 C  CB    . LEU B  1  863  ? 22.936  32.540  106.971 1.00 20.54 ? 861  LEU B CB    1 
ATOM   15324 C  CG    . LEU B  1  863  ? 23.090  33.828  106.171 1.00 23.71 ? 861  LEU B CG    1 
ATOM   15325 C  CD1   . LEU B  1  863  ? 24.205  34.676  106.758 1.00 25.26 ? 861  LEU B CD1   1 
ATOM   15326 C  CD2   . LEU B  1  863  ? 23.375  33.493  104.707 1.00 26.36 ? 861  LEU B CD2   1 
ATOM   15327 N  N     . THR B  1  864  ? 21.548  30.034  108.377 1.00 19.31 ? 862  THR B N     1 
ATOM   15328 C  CA    . THR B  1  864  ? 21.586  28.657  108.859 1.00 19.19 ? 862  THR B CA    1 
ATOM   15329 C  C     . THR B  1  864  ? 20.580  27.794  108.111 1.00 21.46 ? 862  THR B C     1 
ATOM   15330 O  O     . THR B  1  864  ? 20.897  26.676  107.693 1.00 22.26 ? 862  THR B O     1 
ATOM   15331 C  CB    . THR B  1  864  ? 21.316  28.631  110.367 1.00 24.94 ? 862  THR B CB    1 
ATOM   15332 O  OG1   . THR B  1  864  ? 22.365  29.336  111.027 1.00 27.42 ? 862  THR B OG1   1 
ATOM   15333 C  CG2   . THR B  1  864  ? 21.263  27.196  110.894 1.00 28.33 ? 862  THR B CG2   1 
ATOM   15334 N  N     . MET B  1  865  ? 19.362  28.306  107.921 1.00 19.08 ? 863  MET B N     1 
ATOM   15335 C  CA    . MET B  1  865  ? 18.343  27.543  107.211 1.00 19.24 ? 863  MET B CA    1 
ATOM   15336 C  C     . MET B  1  865  ? 18.726  27.358  105.750 1.00 18.58 ? 863  MET B C     1 
ATOM   15337 O  O     . MET B  1  865  ? 18.538  26.279  105.172 1.00 18.99 ? 863  MET B O     1 
ATOM   15338 C  CB    . MET B  1  865  ? 16.996  28.257  107.325 1.00 19.53 ? 863  MET B CB    1 
ATOM   15339 C  CG    . MET B  1  865  ? 15.848  27.488  106.755 1.00 22.92 ? 863  MET B CG    1 
ATOM   15340 S  SD    . MET B  1  865  ? 14.320  28.411  106.947 1.00 26.05 ? 863  MET B SD    1 
ATOM   15341 C  CE    . MET B  1  865  ? 14.407  28.841  108.688 1.00 28.08 ? 863  MET B CE    1 
ATOM   15342 N  N     . LEU B  1  866  ? 19.255  28.413  105.136 1.00 18.72 ? 864  LEU B N     1 
ATOM   15343 C  CA    . LEU B  1  866  ? 19.668  28.325  103.739 1.00 18.98 ? 864  LEU B CA    1 
ATOM   15344 C  C     . LEU B  1  866  ? 20.756  27.277  103.564 1.00 19.25 ? 864  LEU B C     1 
ATOM   15345 O  O     . LEU B  1  866  ? 20.701  26.457  102.641 1.00 19.86 ? 864  LEU B O     1 
ATOM   15346 C  CB    . LEU B  1  866  ? 20.160  29.692  103.266 1.00 21.45 ? 864  LEU B CB    1 
ATOM   15347 C  CG    . LEU B  1  866  ? 20.752  29.718  101.865 1.00 19.97 ? 864  LEU B CG    1 
ATOM   15348 C  CD1   . LEU B  1  866  ? 19.682  29.323  100.862 1.00 22.79 ? 864  LEU B CD1   1 
ATOM   15349 C  CD2   . LEU B  1  866  ? 21.262  31.128  101.582 1.00 23.65 ? 864  LEU B CD2   1 
ATOM   15350 N  N     . LYS B  1  867  ? 21.741  27.274  104.463 1.00 19.95 ? 865  LYS B N     1 
ATOM   15351 C  CA    . LYS B  1  867  ? 22.814  26.299  104.365 1.00 19.74 ? 865  LYS B CA    1 
ATOM   15352 C  C     . LYS B  1  867  ? 22.285  24.890  104.579 1.00 21.69 ? 865  LYS B C     1 
ATOM   15353 O  O     . LYS B  1  867  ? 22.690  23.962  103.872 1.00 19.91 ? 865  LYS B O     1 
ATOM   15354 C  CB    . LYS B  1  867  ? 23.921  26.647  105.365 1.00 21.09 ? 865  LYS B CB    1 
ATOM   15355 C  CG    . LYS B  1  867  ? 24.684  27.890  104.924 1.00 22.90 ? 865  LYS B CG    1 
ATOM   15356 C  CD    . LYS B  1  867  ? 25.549  28.442  106.026 1.00 27.87 ? 865  LYS B CD    1 
ATOM   15357 C  CE    . LYS B  1  867  ? 26.132  29.790  105.627 1.00 35.56 ? 865  LYS B CE    1 
ATOM   15358 N  NZ    . LYS B  1  867  ? 26.990  30.343  106.713 1.00 37.70 ? 865  LYS B NZ    1 
ATOM   15359 N  N     . GLY B  1  868  ? 21.346  24.716  105.511 1.00 19.72 ? 866  GLY B N     1 
ATOM   15360 C  CA    . GLY B  1  868  ? 20.763  23.395  105.704 1.00 20.46 ? 866  GLY B CA    1 
ATOM   15361 C  C     . GLY B  1  868  ? 19.984  22.926  104.489 1.00 20.75 ? 866  GLY B C     1 
ATOM   15362 O  O     . GLY B  1  868  ? 20.044  21.750  104.111 1.00 21.50 ? 866  GLY B O     1 
ATOM   15363 N  N     . ALA B  1  869  ? 19.257  23.845  103.850 1.00 20.64 ? 867  ALA B N     1 
ATOM   15364 C  CA    . ALA B  1  869  ? 18.537  23.519  102.627 1.00 20.68 ? 867  ALA B CA    1 
ATOM   15365 C  C     . ALA B  1  869  ? 19.496  23.178  101.497 1.00 19.98 ? 867  ALA B C     1 
ATOM   15366 O  O     . ALA B  1  869  ? 19.235  22.268  100.702 1.00 21.87 ? 867  ALA B O     1 
ATOM   15367 C  CB    . ALA B  1  869  ? 17.642  24.692  102.218 1.00 18.84 ? 867  ALA B CB    1 
ATOM   15368 N  N     . LEU B  1  870  ? 20.606  23.906  101.402 1.00 17.88 ? 868  LEU B N     1 
ATOM   15369 C  CA    . LEU B  1  870  ? 21.569  23.637  100.338 1.00 21.59 ? 868  LEU B CA    1 
ATOM   15370 C  C     . LEU B  1  870  ? 22.157  22.243  100.453 1.00 21.63 ? 868  LEU B C     1 
ATOM   15371 O  O     . LEU B  1  870  ? 22.472  21.617  99.436  1.00 22.38 ? 868  LEU B O     1 
ATOM   15372 C  CB    . LEU B  1  870  ? 22.693  24.669  100.361 1.00 20.94 ? 868  LEU B CB    1 
ATOM   15373 C  CG    . LEU B  1  870  ? 22.384  25.961  99.625  1.00 29.81 ? 868  LEU B CG    1 
ATOM   15374 C  CD1   . LEU B  1  870  ? 23.507  26.945  99.830  1.00 31.16 ? 868  LEU B CD1   1 
ATOM   15375 C  CD2   . LEU B  1  870  ? 22.182  25.637  98.142  1.00 27.54 ? 868  LEU B CD2   1 
ATOM   15376 N  N     . HIS B  1  871  ? 22.317  21.738  101.672 1.00 20.24 ? 869  HIS B N     1 
ATOM   15377 C  CA    . HIS B  1  871  ? 22.917  20.424  101.827 1.00 21.00 ? 869  HIS B CA    1 
ATOM   15378 C  C     . HIS B  1  871  ? 21.993  19.301  101.389 1.00 22.42 ? 869  HIS B C     1 
ATOM   15379 O  O     . HIS B  1  871  ? 22.449  18.162  101.267 1.00 25.76 ? 869  HIS B O     1 
ATOM   15380 C  CB    . HIS B  1  871  ? 23.376  20.233  103.270 1.00 28.22 ? 869  HIS B CB    1 
ATOM   15381 C  CG    . HIS B  1  871  ? 24.662  20.940  103.569 1.00 46.13 ? 869  HIS B CG    1 
ATOM   15382 N  ND1   . HIS B  1  871  ? 24.748  21.997  104.450 1.00 42.83 ? 869  HIS B ND1   1 
ATOM   15383 C  CD2   . HIS B  1  871  ? 25.907  20.770  103.062 1.00 46.78 ? 869  HIS B CD2   1 
ATOM   15384 C  CE1   . HIS B  1  871  ? 25.996  22.430  104.493 1.00 51.47 ? 869  HIS B CE1   1 
ATOM   15385 N  NE2   . HIS B  1  871  ? 26.719  21.703  103.660 1.00 55.33 ? 869  HIS B NE2   1 
ATOM   15386 N  N     . GLU B  1  872  ? 20.733  19.599  101.107 1.00 20.14 ? 870  GLU B N     1 
ATOM   15387 C  CA    . GLU B  1  872  ? 19.801  18.603  100.611 1.00 21.37 ? 870  GLU B CA    1 
ATOM   15388 C  C     . GLU B  1  872  ? 19.715  18.583  99.094  1.00 20.47 ? 870  GLU B C     1 
ATOM   15389 O  O     . GLU B  1  872  ? 18.937  17.794  98.546  1.00 21.42 ? 870  GLU B O     1 
ATOM   15390 C  CB    . GLU B  1  872  ? 18.414  18.850  101.208 1.00 20.49 ? 870  GLU B CB    1 
ATOM   15391 C  CG    . GLU B  1  872  ? 18.423  18.865  102.724 1.00 19.60 ? 870  GLU B CG    1 
ATOM   15392 C  CD    . GLU B  1  872  ? 18.778  17.521  103.316 1.00 22.80 ? 870  GLU B CD    1 
ATOM   15393 O  OE1   . GLU B  1  872  ? 18.564  16.497  102.627 1.00 27.46 ? 870  GLU B OE1   1 
ATOM   15394 O  OE2   . GLU B  1  872  ? 19.279  17.472  104.462 1.00 25.08 ? 870  GLU B OE2   1 
ATOM   15395 N  N     . LEU B  1  873  ? 20.479  19.429  98.406  1.00 20.33 ? 871  LEU B N     1 
ATOM   15396 C  CA    . LEU B  1  873  ? 20.435  19.458  96.953  1.00 20.73 ? 871  LEU B CA    1 
ATOM   15397 C  C     . LEU B  1  873  ? 21.290  18.350  96.367  1.00 22.97 ? 871  LEU B C     1 
ATOM   15398 O  O     . LEU B  1  873  ? 22.344  18.000  96.902  1.00 23.94 ? 871  LEU B O     1 
ATOM   15399 C  CB    . LEU B  1  873  ? 20.921  20.801  96.412  1.00 18.88 ? 871  LEU B CB    1 
ATOM   15400 C  CG    . LEU B  1  873  ? 20.059  22.015  96.753  1.00 27.53 ? 871  LEU B CG    1 
ATOM   15401 C  CD1   . LEU B  1  873  ? 20.549  23.227  95.964  1.00 25.39 ? 871  LEU B CD1   1 
ATOM   15402 C  CD2   . LEU B  1  873  ? 18.575  21.760  96.494  1.00 23.56 ? 871  LEU B CD2   1 
ATOM   15403 N  N     . HIS B  1  874  ? 20.838  17.824  95.234  1.00 21.47 ? 872  HIS B N     1 
ATOM   15404 C  CA    . HIS B  1  874  ? 21.562  16.803  94.496  1.00 24.33 ? 872  HIS B CA    1 
ATOM   15405 C  C     . HIS B  1  874  ? 22.140  17.449  93.239  1.00 19.27 ? 872  HIS B C     1 
ATOM   15406 O  O     . HIS B  1  874  ? 21.390  17.949  92.395  1.00 19.39 ? 872  HIS B O     1 
ATOM   15407 C  CB    . HIS B  1  874  ? 20.627  15.643  94.162  1.00 20.56 ? 872  HIS B CB    1 
ATOM   15408 C  CG    . HIS B  1  874  ? 21.279  14.532  93.407  1.00 22.60 ? 872  HIS B CG    1 
ATOM   15409 N  ND1   . HIS B  1  874  ? 20.583  13.422  92.979  1.00 30.38 ? 872  HIS B ND1   1 
ATOM   15410 C  CD2   . HIS B  1  874  ? 22.549  14.375  92.965  1.00 26.76 ? 872  HIS B CD2   1 
ATOM   15411 C  CE1   . HIS B  1  874  ? 21.400  12.623  92.315  1.00 29.53 ? 872  HIS B CE1   1 
ATOM   15412 N  NE2   . HIS B  1  874  ? 22.600  13.177  92.296  1.00 29.75 ? 872  HIS B NE2   1 
ATOM   15413 N  N     . ILE B  1  875  ? 23.464  17.465  93.137  1.00 21.27 ? 873  ILE B N     1 
ATOM   15414 C  CA    . ILE B  1  875  ? 24.168  18.041  91.997  1.00 20.88 ? 873  ILE B CA    1 
ATOM   15415 C  C     . ILE B  1  875  ? 24.697  16.893  91.149  1.00 22.01 ? 873  ILE B C     1 
ATOM   15416 O  O     . ILE B  1  875  ? 25.352  15.983  91.670  1.00 23.56 ? 873  ILE B O     1 
ATOM   15417 C  CB    . ILE B  1  875  ? 25.311  18.970  92.434  1.00 26.59 ? 873  ILE B CB    1 
ATOM   15418 C  CG1   . ILE B  1  875  ? 24.774  20.308  92.959  1.00 33.09 ? 873  ILE B CG1   1 
ATOM   15419 C  CG2   . ILE B  1  875  ? 26.207  19.268  91.251  1.00 23.99 ? 873  ILE B CG2   1 
ATOM   15420 C  CD1   . ILE B  1  875  ? 24.032  20.248  94.273  1.00 38.94 ? 873  ILE B CD1   1 
ATOM   15421 N  N     . GLY B  1  876  ? 24.398  16.911  89.856  1.00 18.78 ? 874  GLY B N     1 
ATOM   15422 C  CA    . GLY B  1  876  ? 24.931  15.870  89.004  1.00 21.30 ? 874  GLY B CA    1 
ATOM   15423 C  C     . GLY B  1  876  ? 24.408  15.984  87.588  1.00 19.92 ? 874  GLY B C     1 
ATOM   15424 O  O     . GLY B  1  876  ? 23.795  16.981  87.207  1.00 19.59 ? 874  GLY B O     1 
ATOM   15425 N  N     . ARG B  1  877  ? 24.696  14.943  86.812  1.00 22.38 ? 875  ARG B N     1 
ATOM   15426 C  CA    . ARG B  1  877  ? 24.219  14.876  85.440  1.00 21.28 ? 875  ARG B CA    1 
ATOM   15427 C  C     . ARG B  1  877  ? 22.694  14.868  85.434  1.00 21.72 ? 875  ARG B C     1 
ATOM   15428 O  O     . ARG B  1  877  ? 22.071  14.138  86.207  1.00 24.34 ? 875  ARG B O     1 
ATOM   15429 C  CB    . ARG B  1  877  ? 24.772  13.623  84.766  1.00 21.01 ? 875  ARG B CB    1 
ATOM   15430 C  CG    . ARG B  1  877  ? 24.702  13.688  83.254  1.00 24.65 ? 875  ARG B CG    1 
ATOM   15431 C  CD    . ARG B  1  877  ? 25.377  12.468  82.649  1.00 32.18 ? 875  ARG B CD    1 
ATOM   15432 N  NE    . ARG B  1  877  ? 24.469  11.347  82.484  1.00 28.33 ? 875  ARG B NE    1 
ATOM   15433 C  CZ    . ARG B  1  877  ? 24.797  10.230  81.850  1.00 38.69 ? 875  ARG B CZ    1 
ATOM   15434 N  NH1   . ARG B  1  877  ? 26.023  10.037  81.389  1.00 30.66 ? 875  ARG B NH1   1 
ATOM   15435 N  NH2   . ARG B  1  877  ? 23.871  9.289   81.667  1.00 34.84 ? 875  ARG B NH2   1 
ATOM   15436 N  N     . THR B  1  878  ? 22.091  15.686  84.566  1.00 18.82 ? 876  THR B N     1 
ATOM   15437 C  CA    . THR B  1  878  ? 20.691  16.069  84.717  1.00 19.95 ? 876  THR B CA    1 
ATOM   15438 C  C     . THR B  1  878  ? 19.701  15.088  84.093  1.00 21.55 ? 876  THR B C     1 
ATOM   15439 O  O     . THR B  1  878  ? 18.503  15.388  84.040  1.00 22.39 ? 876  THR B O     1 
ATOM   15440 C  CB    . THR B  1  878  ? 20.476  17.463  84.134  1.00 20.01 ? 876  THR B CB    1 
ATOM   15441 O  OG1   . THR B  1  878  ? 21.011  17.512  82.805  1.00 23.71 ? 876  THR B OG1   1 
ATOM   15442 C  CG2   . THR B  1  878  ? 21.178  18.480  84.991  1.00 20.71 ? 876  THR B CG2   1 
ATOM   15443 N  N     . ASP B  1  879  ? 20.141  13.908  83.664  1.00 22.20 ? 877  ASP B N     1 
ATOM   15444 C  CA    . ASP B  1  879  ? 19.204  12.928  83.129  1.00 22.51 ? 877  ASP B CA    1 
ATOM   15445 C  C     . ASP B  1  879  ? 18.639  12.021  84.215  1.00 21.98 ? 877  ASP B C     1 
ATOM   15446 O  O     . ASP B  1  879  ? 18.241  10.883  83.939  1.00 22.11 ? 877  ASP B O     1 
ATOM   15447 C  CB    . ASP B  1  879  ? 19.851  12.118  82.003  1.00 23.04 ? 877  ASP B CB    1 
ATOM   15448 C  CG    . ASP B  1  879  ? 21.032  11.295  82.463  1.00 27.01 ? 877  ASP B CG    1 
ATOM   15449 O  OD1   . ASP B  1  879  ? 21.762  11.708  83.392  1.00 31.61 ? 877  ASP B OD1   1 
ATOM   15450 O  OD2   . ASP B  1  879  ? 21.236  10.220  81.869  1.00 27.71 ? 877  ASP B OD2   1 
ATOM   15451 N  N     . ARG B  1  880  ? 18.567  12.526  85.443  1.00 24.60 ? 878  ARG B N     1 
ATOM   15452 C  CA    . ARG B  1  880  ? 17.888  11.871  86.554  1.00 21.55 ? 878  ARG B CA    1 
ATOM   15453 C  C     . ARG B  1  880  ? 16.950  12.887  87.184  1.00 19.82 ? 878  ARG B C     1 
ATOM   15454 O  O     . ARG B  1  880  ? 17.363  14.015  87.468  1.00 22.19 ? 878  ARG B O     1 
ATOM   15455 C  CB    . ARG B  1  880  ? 18.880  11.374  87.611  1.00 24.08 ? 878  ARG B CB    1 
ATOM   15456 C  CG    . ARG B  1  880  ? 19.632  10.107  87.254  1.00 26.85 ? 878  ARG B CG    1 
ATOM   15457 C  CD    . ARG B  1  880  ? 20.517  9.697   88.440  1.00 31.92 ? 878  ARG B CD    1 
ATOM   15458 N  NE    . ARG B  1  880  ? 20.849  8.277   88.428  1.00 53.64 ? 878  ARG B NE    1 
ATOM   15459 C  CZ    . ARG B  1  880  ? 21.933  7.765   87.860  1.00 55.57 ? 878  ARG B CZ    1 
ATOM   15460 N  NH1   . ARG B  1  880  ? 22.819  8.532   87.245  1.00 56.97 ? 878  ARG B NH1   1 
ATOM   15461 N  NH2   . ARG B  1  880  ? 22.129  6.449   87.905  1.00 58.61 ? 878  ARG B NH2   1 
ATOM   15462 N  N     . LEU B  1  881  ? 15.695  12.484  87.404  1.00 20.29 ? 879  LEU B N     1 
ATOM   15463 C  CA    . LEU B  1  881  ? 14.713  13.373  88.024  1.00 20.80 ? 879  LEU B CA    1 
ATOM   15464 C  C     . LEU B  1  881  ? 15.172  13.866  89.393  1.00 20.11 ? 879  LEU B C     1 
ATOM   15465 O  O     . LEU B  1  881  ? 14.819  14.980  89.802  1.00 21.87 ? 879  LEU B O     1 
ATOM   15466 C  CB    . LEU B  1  881  ? 13.373  12.647  88.131  1.00 20.86 ? 879  LEU B CB    1 
ATOM   15467 C  CG    . LEU B  1  881  ? 12.197  13.418  88.733  1.00 23.70 ? 879  LEU B CG    1 
ATOM   15468 C  CD1   . LEU B  1  881  ? 11.793  14.536  87.789  1.00 23.55 ? 879  LEU B CD1   1 
ATOM   15469 C  CD2   . LEU B  1  881  ? 11.031  12.467  89.024  1.00 21.49 ? 879  LEU B CD2   1 
ATOM   15470 N  N     . SER B  1  882  ? 15.978  13.070  90.101  1.00 20.02 ? 880  SER B N     1 
ATOM   15471 C  CA    . SER B  1  882  ? 16.433  13.436  91.438  1.00 18.13 ? 880  SER B CA    1 
ATOM   15472 C  C     . SER B  1  882  ? 17.484  14.530  91.448  1.00 19.65 ? 880  SER B C     1 
ATOM   15473 O  O     . SER B  1  882  ? 17.865  14.975  92.534  1.00 22.37 ? 880  SER B O     1 
ATOM   15474 C  CB    . SER B  1  882  ? 17.014  12.217  92.155  1.00 21.96 ? 880  SER B CB    1 
ATOM   15475 O  OG    . SER B  1  882  ? 18.205  11.805  91.499  1.00 24.35 ? 880  SER B OG    1 
ATOM   15476 N  N     . VAL B  1  883  ? 17.988  14.954  90.298  1.00 19.16 ? 881  VAL B N     1 
ATOM   15477 C  CA    . VAL B  1  883  ? 19.035  15.967  90.255  1.00 19.53 ? 881  VAL B CA    1 
ATOM   15478 C  C     . VAL B  1  883  ? 18.404  17.345  90.308  1.00 18.15 ? 881  VAL B C     1 
ATOM   15479 O  O     . VAL B  1  883  ? 17.504  17.666  89.522  1.00 22.89 ? 881  VAL B O     1 
ATOM   15480 C  CB    . VAL B  1  883  ? 19.910  15.804  89.006  1.00 20.71 ? 881  VAL B CB    1 
ATOM   15481 C  CG1   . VAL B  1  883  ? 20.841  17.000  88.847  1.00 22.63 ? 881  VAL B CG1   1 
ATOM   15482 C  CG2   . VAL B  1  883  ? 20.708  14.535  89.131  1.00 21.64 ? 881  VAL B CG2   1 
ATOM   15483 N  N     . ASP B  1  884  ? 18.901  18.169  91.224  1.00 19.74 ? 882  ASP B N     1 
ATOM   15484 C  CA    . ASP B  1  884  ? 18.425  19.528  91.427  1.00 20.32 ? 882  ASP B CA    1 
ATOM   15485 C  C     . ASP B  1  884  ? 19.241  20.562  90.678  1.00 22.96 ? 882  ASP B C     1 
ATOM   15486 O  O     . ASP B  1  884  ? 18.678  21.537  90.172  1.00 26.38 ? 882  ASP B O     1 
ATOM   15487 C  CB    . ASP B  1  884  ? 18.465  19.861  92.911  1.00 20.93 ? 882  ASP B CB    1 
ATOM   15488 C  CG    . ASP B  1  884  ? 17.639  18.899  93.727  1.00 21.86 ? 882  ASP B CG    1 
ATOM   15489 O  OD1   . ASP B  1  884  ? 16.440  18.765  93.408  1.00 22.66 ? 882  ASP B OD1   1 
ATOM   15490 O  OD2   . ASP B  1  884  ? 18.189  18.261  94.642  1.00 22.63 ? 882  ASP B OD2   1 
ATOM   15491 N  N     . VAL B  1  885  ? 20.558  20.380  90.627  1.00 20.39 ? 883  VAL B N     1 
ATOM   15492 C  CA    . VAL B  1  885  ? 21.476  21.371  90.076  1.00 18.94 ? 883  VAL B CA    1 
ATOM   15493 C  C     . VAL B  1  885  ? 22.403  20.638  89.122  1.00 19.08 ? 883  VAL B C     1 
ATOM   15494 O  O     . VAL B  1  885  ? 23.054  19.661  89.512  1.00 19.82 ? 883  VAL B O     1 
ATOM   15495 C  CB    . VAL B  1  885  ? 22.278  22.091  91.172  1.00 23.06 ? 883  VAL B CB    1 
ATOM   15496 C  CG1   . VAL B  1  885  ? 23.302  23.071  90.554  1.00 25.10 ? 883  VAL B CG1   1 
ATOM   15497 C  CG2   . VAL B  1  885  ? 21.344  22.833  92.119  1.00 25.87 ? 883  VAL B CG2   1 
ATOM   15498 N  N     . GLY B  1  886  ? 22.438  21.085  87.876  1.00 19.06 ? 884  GLY B N     1 
ATOM   15499 C  CA    . GLY B  1  886  ? 23.275  20.472  86.882  1.00 19.75 ? 884  GLY B CA    1 
ATOM   15500 C  C     . GLY B  1  886  ? 24.603  21.176  86.750  1.00 18.75 ? 884  GLY B C     1 
ATOM   15501 O  O     . GLY B  1  886  ? 25.031  21.951  87.614  1.00 17.61 ? 884  GLY B O     1 
ATOM   15502 N  N     . PRO B  1  887  ? 25.288  20.895  85.652  1.00 18.05 ? 885  PRO B N     1 
ATOM   15503 C  CA    . PRO B  1  887  ? 26.623  21.450  85.433  1.00 17.38 ? 885  PRO B CA    1 
ATOM   15504 C  C     . PRO B  1  887  ? 26.586  22.885  84.933  1.00 17.64 ? 885  PRO B C     1 
ATOM   15505 O  O     . PRO B  1  887  ? 25.566  23.393  84.468  1.00 18.44 ? 885  PRO B O     1 
ATOM   15506 C  CB    . PRO B  1  887  ? 27.194  20.523  84.358  1.00 17.56 ? 885  PRO B CB    1 
ATOM   15507 C  CG    . PRO B  1  887  ? 25.959  20.185  83.545  1.00 18.32 ? 885  PRO B CG    1 
ATOM   15508 C  CD    . PRO B  1  887  ? 24.874  19.990  84.567  1.00 18.97 ? 885  PRO B CD    1 
ATOM   15509 N  N     . VAL B  1  888  ? 27.746  23.530  85.024  1.00 17.32 ? 886  VAL B N     1 
ATOM   15510 C  CA    . VAL B  1  888  ? 27.948  24.754  84.263  1.00 18.02 ? 886  VAL B CA    1 
ATOM   15511 C  C     . VAL B  1  888  ? 28.325  24.384  82.833  1.00 17.90 ? 886  VAL B C     1 
ATOM   15512 O  O     . VAL B  1  888  ? 28.721  23.255  82.539  1.00 19.03 ? 886  VAL B O     1 
ATOM   15513 C  CB    . VAL B  1  888  ? 28.995  25.676  84.919  1.00 22.45 ? 886  VAL B CB    1 
ATOM   15514 C  CG1   . VAL B  1  888  ? 28.519  26.071  86.330  1.00 21.77 ? 886  VAL B CG1   1 
ATOM   15515 C  CG2   . VAL B  1  888  ? 30.343  25.033  84.979  1.00 24.54 ? 886  VAL B CG2   1 
ATOM   15516 N  N     . ILE B  1  889  ? 28.165  25.341  81.917  1.00 17.99 ? 887  ILE B N     1 
ATOM   15517 C  CA    . ILE B  1  889  ? 28.071  24.943  80.513  1.00 17.95 ? 887  ILE B CA    1 
ATOM   15518 C  C     . ILE B  1  889  ? 29.409  24.468  79.942  1.00 19.08 ? 887  ILE B C     1 
ATOM   15519 O  O     . ILE B  1  889  ? 29.431  23.586  79.076  1.00 18.41 ? 887  ILE B O     1 
ATOM   15520 C  CB    . ILE B  1  889  ? 27.477  26.103  79.695  1.00 18.42 ? 887  ILE B CB    1 
ATOM   15521 C  CG1   . ILE B  1  889  ? 27.254  25.680  78.243  1.00 18.21 ? 887  ILE B CG1   1 
ATOM   15522 C  CG2   . ILE B  1  889  ? 28.367  27.339  79.776  1.00 20.49 ? 887  ILE B CG2   1 
ATOM   15523 C  CD1   . ILE B  1  889  ? 26.273  24.532  78.099  1.00 19.36 ? 887  ILE B CD1   1 
ATOM   15524 N  N     . THR B  1  890  ? 30.536  25.030  80.394  1.00 17.27 ? 888  THR B N     1 
ATOM   15525 C  CA    . THR B  1  890  ? 31.844  24.726  79.820  1.00 20.47 ? 888  THR B CA    1 
ATOM   15526 C  C     . THR B  1  890  ? 32.902  24.784  80.905  1.00 18.03 ? 888  THR B C     1 
ATOM   15527 O  O     . THR B  1  890  ? 32.692  25.363  81.973  1.00 18.79 ? 888  THR B O     1 
ATOM   15528 C  CB    . THR B  1  890  ? 32.277  25.726  78.735  1.00 19.39 ? 888  THR B CB    1 
ATOM   15529 O  OG1   . THR B  1  890  ? 32.297  27.052  79.289  1.00 21.74 ? 888  THR B OG1   1 
ATOM   15530 C  CG2   . THR B  1  890  ? 31.332  25.699  77.542  1.00 20.56 ? 888  THR B CG2   1 
ATOM   15531 N  N     . SER B  1  891  ? 34.071  24.229  80.578  1.00 19.09 ? 889  SER B N     1 
ATOM   15532 C  CA    A SER B  1  891  ? 35.231  24.356  81.458  0.42 17.72 ? 889  SER B CA    1 
ATOM   15533 C  CA    B SER B  1  891  ? 35.221  24.356  81.470  0.58 17.66 ? 889  SER B CA    1 
ATOM   15534 C  C     . SER B  1  891  ? 35.651  25.813  81.595  1.00 21.76 ? 889  SER B C     1 
ATOM   15535 O  O     . SER B  1  891  ? 36.086  26.244  82.668  1.00 22.43 ? 889  SER B O     1 
ATOM   15536 C  CB    A SER B  1  891  ? 36.399  23.519  80.929  0.42 23.12 ? 889  SER B CB    1 
ATOM   15537 C  CB    B SER B  1  891  ? 36.382  23.491  80.976  0.58 23.12 ? 889  SER B CB    1 
ATOM   15538 O  OG    A SER B  1  891  ? 36.092  22.140  80.929  0.42 25.63 ? 889  SER B OG    1 
ATOM   15539 O  OG    B SER B  1  891  ? 36.854  23.948  79.722  0.58 26.34 ? 889  SER B OG    1 
ATOM   15540 N  N     . GLU B  1  892  ? 35.533  26.584  80.509  1.00 20.40 ? 890  GLU B N     1 
ATOM   15541 C  CA    . GLU B  1  892  ? 35.878  28.001  80.560  1.00 23.39 ? 890  GLU B CA    1 
ATOM   15542 C  C     . GLU B  1  892  ? 34.983  28.735  81.547  1.00 21.91 ? 890  GLU B C     1 
ATOM   15543 O  O     . GLU B  1  892  ? 35.463  29.541  82.353  1.00 23.54 ? 890  GLU B O     1 
ATOM   15544 C  CB    . GLU B  1  892  ? 35.759  28.631  79.170  1.00 27.73 ? 890  GLU B CB    1 
ATOM   15545 C  CG    . GLU B  1  892  ? 35.960  30.143  79.164  1.00 33.65 ? 890  GLU B CG    1 
ATOM   15546 C  CD    . GLU B  1  892  ? 35.485  30.823  77.879  1.00 57.11 ? 890  GLU B CD    1 
ATOM   15547 O  OE1   . GLU B  1  892  ? 34.507  30.346  77.259  1.00 59.87 ? 890  GLU B OE1   1 
ATOM   15548 O  OE2   . GLU B  1  892  ? 36.090  31.847  77.492  1.00 57.40 ? 890  GLU B OE2   1 
ATOM   15549 N  N     . ALA B  1  893  ? 33.677  28.467  81.503  1.00 20.90 ? 891  ALA B N     1 
ATOM   15550 C  CA    . ALA B  1  893  ? 32.765  29.090  82.454  1.00 17.97 ? 891  ALA B CA    1 
ATOM   15551 C  C     . ALA B  1  893  ? 33.120  28.681  83.870  1.00 19.79 ? 891  ALA B C     1 
ATOM   15552 O  O     . ALA B  1  893  ? 33.168  29.516  84.778  1.00 21.56 ? 891  ALA B O     1 
ATOM   15553 C  CB    . ALA B  1  893  ? 31.318  28.698  82.135  1.00 22.11 ? 891  ALA B CB    1 
ATOM   15554 N  N     . LYS B  1  894  ? 33.376  27.389  84.067  1.00 20.22 ? 892  LYS B N     1 
ATOM   15555 C  CA    . LYS B  1  894  ? 33.751  26.901  85.385  1.00 20.47 ? 892  LYS B CA    1 
ATOM   15556 C  C     . LYS B  1  894  ? 34.994  27.619  85.896  1.00 22.17 ? 892  LYS B C     1 
ATOM   15557 O  O     . LYS B  1  894  ? 35.032  28.067  87.043  1.00 21.50 ? 892  LYS B O     1 
ATOM   15558 C  CB    . LYS B  1  894  ? 33.964  25.393  85.342  1.00 21.70 ? 892  LYS B CB    1 
ATOM   15559 C  CG    . LYS B  1  894  ? 34.486  24.821  86.635  1.00 21.33 ? 892  LYS B CG    1 
ATOM   15560 C  CD    . LYS B  1  894  ? 34.628  23.316  86.537  1.00 21.15 ? 892  LYS B CD    1 
ATOM   15561 C  CE    . LYS B  1  894  ? 35.177  22.747  87.855  1.00 26.69 ? 892  LYS B CE    1 
ATOM   15562 N  NZ    . LYS B  1  894  ? 35.133  21.263  87.855  1.00 38.06 ? 892  LYS B NZ    1 
ATOM   15563 N  N     . ASP B  1  895  ? 36.003  27.782  85.038  1.00 20.49 ? 893  ASP B N     1 
ATOM   15564 C  CA    . ASP B  1  895  ? 37.219  28.475  85.462  1.00 21.16 ? 893  ASP B CA    1 
ATOM   15565 C  C     . ASP B  1  895  ? 36.938  29.927  85.823  1.00 23.75 ? 893  ASP B C     1 
ATOM   15566 O  O     . ASP B  1  895  ? 37.515  30.463  86.779  1.00 25.37 ? 893  ASP B O     1 
ATOM   15567 C  CB    . ASP B  1  895  ? 38.280  28.417  84.356  1.00 24.29 ? 893  ASP B CB    1 
ATOM   15568 C  CG    . ASP B  1  895  ? 38.825  27.031  84.139  1.00 26.92 ? 893  ASP B CG    1 
ATOM   15569 O  OD1   . ASP B  1  895  ? 38.652  26.167  85.026  1.00 31.61 ? 893  ASP B OD1   1 
ATOM   15570 O  OD2   . ASP B  1  895  ? 39.441  26.815  83.073  1.00 28.56 ? 893  ASP B OD2   1 
ATOM   15571 N  N     . ASN B  1  896  ? 36.088  30.586  85.038  1.00 21.45 ? 894  ASN B N     1 
ATOM   15572 C  CA    . ASN B  1  896  ? 35.734  31.979  85.269  1.00 21.28 ? 894  ASN B CA    1 
ATOM   15573 C  C     . ASN B  1  896  ? 35.049  32.136  86.623  1.00 24.08 ? 894  ASN B C     1 
ATOM   15574 O  O     . ASN B  1  896  ? 35.409  33.006  87.428  1.00 23.91 ? 894  ASN B O     1 
ATOM   15575 C  CB    . ASN B  1  896  ? 34.833  32.428  84.112  1.00 24.97 ? 894  ASN B CB    1 
ATOM   15576 C  CG    . ASN B  1  896  ? 34.381  33.870  84.205  1.00 31.50 ? 894  ASN B CG    1 
ATOM   15577 O  OD1   . ASN B  1  896  ? 33.779  34.297  85.185  1.00 34.11 ? 894  ASN B OD1   1 
ATOM   15578 N  ND2   . ASN B  1  896  ? 34.625  34.618  83.136  1.00 40.02 ? 894  ASN B ND2   1 
ATOM   15579 N  N     . ILE B  1  897  ? 34.079  31.265  86.897  1.00 21.62 ? 895  ILE B N     1 
ATOM   15580 C  CA    . ILE B  1  897  ? 33.377  31.286  88.174  1.00 21.14 ? 895  ILE B CA    1 
ATOM   15581 C  C     . ILE B  1  897  ? 34.351  31.019  89.316  1.00 22.46 ? 895  ILE B C     1 
ATOM   15582 O  O     . ILE B  1  897  ? 34.366  31.732  90.326  1.00 23.55 ? 895  ILE B O     1 
ATOM   15583 C  CB    . ILE B  1  897  ? 32.234  30.257  88.160  1.00 18.77 ? 895  ILE B CB    1 
ATOM   15584 C  CG1   . ILE B  1  897  ? 31.195  30.635  87.094  1.00 17.75 ? 895  ILE B CG1   1 
ATOM   15585 C  CG2   . ILE B  1  897  ? 31.595  30.160  89.539  1.00 20.24 ? 895  ILE B CG2   1 
ATOM   15586 C  CD1   . ILE B  1  897  ? 30.345  29.460  86.673  1.00 19.12 ? 895  ILE B CD1   1 
ATOM   15587 N  N     . GLU B  1  898  ? 35.174  29.986  89.171  1.00 22.62 ? 896  GLU B N     1 
ATOM   15588 C  CA    . GLU B  1  898  ? 36.101  29.628  90.238  1.00 22.25 ? 896  GLU B CA    1 
ATOM   15589 C  C     . GLU B  1  898  ? 37.150  30.709  90.458  1.00 23.68 ? 896  GLU B C     1 
ATOM   15590 O  O     . GLU B  1  898  ? 37.571  30.928  91.600  1.00 24.38 ? 896  GLU B O     1 
ATOM   15591 C  CB    . GLU B  1  898  ? 36.732  28.266  89.938  1.00 24.34 ? 896  GLU B CB    1 
ATOM   15592 C  CG    . GLU B  1  898  ? 35.691  27.136  90.064  1.00 23.46 ? 896  GLU B CG    1 
ATOM   15593 C  CD    . GLU B  1  898  ? 36.246  25.751  89.814  1.00 35.13 ? 896  GLU B CD    1 
ATOM   15594 O  OE1   . GLU B  1  898  ? 37.331  25.635  89.210  1.00 33.38 ? 896  GLU B OE1   1 
ATOM   15595 O  OE2   . GLU B  1  898  ? 35.585  24.775  90.228  1.00 39.80 ? 896  GLU B OE2   1 
ATOM   15596 N  N     . LYS B  1  899  ? 37.551  31.426  89.402  1.00 21.60 ? 897  LYS B N     1 
ATOM   15597 C  CA    . LYS B  1  899  ? 38.497  32.528  89.591  1.00 23.51 ? 897  LYS B CA    1 
ATOM   15598 C  C     . LYS B  1  899  ? 37.905  33.601  90.494  1.00 26.55 ? 897  LYS B C     1 
ATOM   15599 O  O     . LYS B  1  899  ? 38.603  34.166  91.346  1.00 26.88 ? 897  LYS B O     1 
ATOM   15600 C  CB    . LYS B  1  899  ? 38.888  33.143  88.247  1.00 26.44 ? 897  LYS B CB    1 
ATOM   15601 C  CG    . LYS B  1  899  ? 39.889  34.278  88.403  1.00 29.80 ? 897  LYS B CG    1 
ATOM   15602 C  CD    . LYS B  1  899  ? 40.394  34.803  87.071  1.00 38.89 ? 897  LYS B CD    1 
ATOM   15603 C  CE    . LYS B  1  899  ? 39.381  35.713  86.412  1.00 36.34 ? 897  LYS B CE    1 
ATOM   15604 N  NZ    . LYS B  1  899  ? 40.010  36.531  85.333  1.00 35.97 ? 897  LYS B NZ    1 
ATOM   15605 N  N     . HIS B  1  900  ? 36.619  33.894  90.321  1.00 21.61 ? 898  HIS B N     1 
ATOM   15606 C  CA    . HIS B  1  900  ? 35.955  34.845  91.202  1.00 21.71 ? 898  HIS B CA    1 
ATOM   15607 C  C     . HIS B  1  900  ? 35.889  34.308  92.621  1.00 23.94 ? 898  HIS B C     1 
ATOM   15608 O  O     . HIS B  1  900  ? 36.173  35.029  93.585  1.00 26.13 ? 898  HIS B O     1 
ATOM   15609 C  CB    . HIS B  1  900  ? 34.548  35.144  90.693  1.00 22.54 ? 898  HIS B CB    1 
ATOM   15610 C  CG    . HIS B  1  900  ? 33.699  35.857  91.691  1.00 23.42 ? 898  HIS B CG    1 
ATOM   15611 N  ND1   . HIS B  1  900  ? 33.875  37.188  91.991  1.00 26.04 ? 898  HIS B ND1   1 
ATOM   15612 C  CD2   . HIS B  1  900  ? 32.684  35.423  92.474  1.00 22.92 ? 898  HIS B CD2   1 
ATOM   15613 C  CE1   . HIS B  1  900  ? 32.987  37.553  92.900  1.00 23.18 ? 898  HIS B CE1   1 
ATOM   15614 N  NE2   . HIS B  1  900  ? 32.250  36.502  93.206  1.00 22.60 ? 898  HIS B NE2   1 
ATOM   15615 N  N     . ILE B  1  901  ? 35.501  33.041  92.766  1.00 22.62 ? 899  ILE B N     1 
ATOM   15616 C  CA    . ILE B  1  901  ? 35.367  32.463  94.097  1.00 20.95 ? 899  ILE B CA    1 
ATOM   15617 C  C     . ILE B  1  901  ? 36.702  32.535  94.819  1.00 26.91 ? 899  ILE B C     1 
ATOM   15618 O  O     . ILE B  1  901  ? 36.779  32.970  95.975  1.00 26.81 ? 899  ILE B O     1 
ATOM   15619 C  CB    . ILE B  1  901  ? 34.832  31.022  94.008  1.00 23.06 ? 899  ILE B CB    1 
ATOM   15620 C  CG1   . ILE B  1  901  ? 33.374  31.016  93.520  1.00 21.54 ? 899  ILE B CG1   1 
ATOM   15621 C  CG2   . ILE B  1  901  ? 34.930  30.339  95.361  1.00 24.48 ? 899  ILE B CG2   1 
ATOM   15622 C  CD1   . ILE B  1  901  ? 32.858  29.604  93.150  1.00 23.87 ? 899  ILE B CD1   1 
ATOM   15623 N  N     . GLU B  1  902  ? 37.783  32.191  94.120  1.00 23.85 ? 900  GLU B N     1 
ATOM   15624 C  CA    . GLU B  1  902  ? 39.097  32.199  94.757  1.00 25.44 ? 900  GLU B CA    1 
ATOM   15625 C  C     . GLU B  1  902  ? 39.598  33.614  95.016  1.00 27.32 ? 900  GLU B C     1 
ATOM   15626 O  O     . GLU B  1  902  ? 40.379  33.825  95.949  1.00 30.06 ? 900  GLU B O     1 
ATOM   15627 C  CB    . GLU B  1  902  ? 40.102  31.417  93.908  1.00 31.18 ? 900  GLU B CB    1 
ATOM   15628 C  CG    . GLU B  1  902  ? 39.812  29.920  93.876  1.00 34.88 ? 900  GLU B CG    1 
ATOM   15629 C  CD    . GLU B  1  902  ? 39.618  29.335  95.267  1.00 40.44 ? 900  GLU B CD    1 
ATOM   15630 O  OE1   . GLU B  1  902  ? 40.429  29.648  96.163  1.00 36.85 ? 900  GLU B OE1   1 
ATOM   15631 O  OE2   . GLU B  1  902  ? 38.645  28.576  95.467  1.00 38.63 ? 900  GLU B OE2   1 
ATOM   15632 N  N     . ARG B  1  903  ? 39.184  34.588  94.207  1.00 28.70 ? 901  ARG B N     1 
ATOM   15633 C  CA    . ARG B  1  903  ? 39.572  35.968  94.488  1.00 26.81 ? 901  ARG B CA    1 
ATOM   15634 C  C     . ARG B  1  903  ? 38.872  36.480  95.734  1.00 31.84 ? 901  ARG B C     1 
ATOM   15635 O  O     . ARG B  1  903  ? 39.479  37.178  96.556  1.00 32.72 ? 901  ARG B O     1 
ATOM   15636 C  CB    . ARG B  1  903  ? 39.249  36.863  93.295  1.00 32.18 ? 901  ARG B CB    1 
ATOM   15637 C  CG    . ARG B  1  903  ? 39.600  38.314  93.540  1.00 39.20 ? 901  ARG B CG    1 
ATOM   15638 C  CD    . ARG B  1  903  ? 39.339  39.173  92.321  1.00 43.71 ? 901  ARG B CD    1 
ATOM   15639 N  NE    . ARG B  1  903  ? 39.756  40.546  92.569  1.00 52.83 ? 901  ARG B NE    1 
ATOM   15640 C  CZ    . ARG B  1  903  ? 38.970  41.485  93.077  1.00 50.19 ? 901  ARG B CZ    1 
ATOM   15641 N  NH1   . ARG B  1  903  ? 37.699  41.248  93.354  1.00 42.39 ? 901  ARG B NH1   1 
ATOM   15642 N  NH2   . ARG B  1  903  ? 39.474  42.693  93.314  1.00 52.17 ? 901  ARG B NH2   1 
ATOM   15643 N  N     . MET B  1  904  ? 37.589  36.151  95.883  1.00 25.92 ? 902  MET B N     1 
ATOM   15644 C  CA    . MET B  1  904  ? 36.881  36.502  97.108  1.00 27.36 ? 902  MET B CA    1 
ATOM   15645 C  C     . MET B  1  904  ? 37.518  35.826  98.307  1.00 32.26 ? 902  MET B C     1 
ATOM   15646 O  O     . MET B  1  904  ? 37.704  36.449  99.358  1.00 30.33 ? 902  MET B O     1 
ATOM   15647 C  CB    . MET B  1  904  ? 35.409  36.116  96.990  1.00 32.11 ? 902  MET B CB    1 
ATOM   15648 C  CG    . MET B  1  904  ? 34.701  36.836  95.878  1.00 26.92 ? 902  MET B CG    1 
ATOM   15649 S  SD    . MET B  1  904  ? 34.560  38.601  96.231  1.00 34.62 ? 902  MET B SD    1 
ATOM   15650 C  CE    . MET B  1  904  ? 35.738  39.262  95.054  1.00 38.64 ? 902  MET B CE    1 
ATOM   15651 N  N     . ARG B  1  905  ? 37.871  34.551  98.162  1.00 29.30 ? 903  ARG B N     1 
ATOM   15652 C  CA    . ARG B  1  905  ? 38.544  33.847  99.246  1.00 34.71 ? 903  ARG B CA    1 
ATOM   15653 C  C     . ARG B  1  905  ? 39.875  34.513  99.581  1.00 32.88 ? 903  ARG B C     1 
ATOM   15654 O  O     . ARG B  1  905  ? 40.181  34.764  100.754 1.00 33.26 ? 903  ARG B O     1 
ATOM   15655 C  CB    . ARG B  1  905  ? 38.742  32.381  98.859  1.00 37.14 ? 903  ARG B CB    1 
ATOM   15656 C  CG    . ARG B  1  905  ? 38.725  31.420  100.025 1.00 41.79 ? 903  ARG B CG    1 
ATOM   15657 C  CD    . ARG B  1  905  ? 39.191  30.042  99.579  1.00 36.70 ? 903  ARG B CD    1 
ATOM   15658 N  NE    . ARG B  1  905  ? 38.312  29.437  98.584  1.00 40.47 ? 903  ARG B NE    1 
ATOM   15659 C  CZ    . ARG B  1  905  ? 37.252  28.694  98.873  1.00 34.06 ? 903  ARG B CZ    1 
ATOM   15660 N  NH1   . ARG B  1  905  ? 36.854  28.512  100.121 1.00 37.28 ? 903  ARG B NH1   1 
ATOM   15661 N  NH2   . ARG B  1  905  ? 36.578  28.110  97.884  1.00 40.73 ? 903  ARG B NH2   1 
ATOM   15662 N  N     . GLY B  1  906  ? 40.670  34.838  98.558  1.00 31.28 ? 904  GLY B N     1 
ATOM   15663 C  CA    . GLY B  1  906  ? 41.975  35.435  98.809  1.00 32.84 ? 904  GLY B CA    1 
ATOM   15664 C  C     . GLY B  1  906  ? 41.892  36.807  99.449  1.00 38.49 ? 904  GLY B C     1 
ATOM   15665 O  O     . GLY B  1  906  ? 42.818  37.229  100.149 1.00 39.30 ? 904  GLY B O     1 
ATOM   15666 N  N     . LEU B  1  907  ? 40.796  37.523  99.216  1.00 36.57 ? 905  LEU B N     1 
ATOM   15667 C  CA    . LEU B  1  907  ? 40.552  38.807  99.859  1.00 37.44 ? 905  LEU B CA    1 
ATOM   15668 C  C     . LEU B  1  907  ? 40.009  38.658  101.277 1.00 40.19 ? 905  LEU B C     1 
ATOM   15669 O  O     . LEU B  1  907  ? 39.680  39.668  101.911 1.00 37.86 ? 905  LEU B O     1 
ATOM   15670 C  CB    . LEU B  1  907  ? 39.586  39.642  99.017  1.00 35.36 ? 905  LEU B CB    1 
ATOM   15671 N  N     . GLY B  1  908  ? 39.907  37.433  101.783 1.00 32.36 ? 906  GLY B N     1 
ATOM   15672 C  CA    . GLY B  1  908  ? 39.475  37.192  103.139 1.00 33.14 ? 906  GLY B CA    1 
ATOM   15673 C  C     . GLY B  1  908  ? 37.981  37.081  103.346 1.00 40.67 ? 906  GLY B C     1 
ATOM   15674 O  O     . GLY B  1  908  ? 37.547  36.904  104.493 1.00 36.67 ? 906  GLY B O     1 
ATOM   15675 N  N     . ARG B  1  909  ? 37.177  37.185  102.287 1.00 31.16 ? 907  ARG B N     1 
ATOM   15676 C  CA    . ARG B  1  909  ? 35.740  37.022  102.429 1.00 30.77 ? 907  ARG B CA    1 
ATOM   15677 C  C     . ARG B  1  909  ? 35.401  35.585  102.802 1.00 31.51 ? 907  ARG B C     1 
ATOM   15678 O  O     . ARG B  1  909  ? 36.074  34.637  102.393 1.00 35.24 ? 907  ARG B O     1 
ATOM   15679 C  CB    . ARG B  1  909  ? 35.015  37.379  101.135 1.00 27.67 ? 907  ARG B CB    1 
ATOM   15680 C  CG    . ARG B  1  909  ? 35.333  38.736  100.566 1.00 37.04 ? 907  ARG B CG    1 
ATOM   15681 C  CD    . ARG B  1  909  ? 34.597  39.852  101.276 1.00 44.89 ? 907  ARG B CD    1 
ATOM   15682 N  NE    . ARG B  1  909  ? 34.734  41.086  100.512 1.00 54.18 ? 907  ARG B NE    1 
ATOM   15683 C  CZ    . ARG B  1  909  ? 35.776  41.900  100.593 1.00 53.28 ? 907  ARG B CZ    1 
ATOM   15684 N  NH1   . ARG B  1  909  ? 36.751  41.687  101.462 1.00 60.66 ? 907  ARG B NH1   1 
ATOM   15685 N  NH2   . ARG B  1  909  ? 35.848  42.947  99.775  1.00 60.20 ? 907  ARG B NH2   1 
ATOM   15686 N  N     . LYS B  1  910  ? 34.336  35.429  103.572 1.00 26.51 ? 908  LYS B N     1 
ATOM   15687 C  CA    . LYS B  1  910  ? 33.873  34.099  103.944 1.00 26.52 ? 908  LYS B CA    1 
ATOM   15688 C  C     . LYS B  1  910  ? 33.215  33.430  102.742 1.00 31.63 ? 908  LYS B C     1 
ATOM   15689 O  O     . LYS B  1  910  ? 32.257  33.965  102.170 1.00 30.17 ? 908  LYS B O     1 
ATOM   15690 C  CB    . LYS B  1  910  ? 32.899  34.186  105.113 1.00 32.96 ? 908  LYS B CB    1 
ATOM   15691 C  CG    . LYS B  1  910  ? 32.384  32.837  105.596 1.00 37.31 ? 908  LYS B CG    1 
ATOM   15692 C  CD    . LYS B  1  910  ? 31.524  33.012  106.840 1.00 45.66 ? 908  LYS B CD    1 
ATOM   15693 C  CE    . LYS B  1  910  ? 31.124  31.674  107.445 1.00 50.84 ? 908  LYS B CE    1 
ATOM   15694 N  NZ    . LYS B  1  910  ? 30.072  31.833  108.496 1.00 50.30 ? 908  LYS B NZ    1 
ATOM   15695 N  N     . VAL B  1  911  ? 33.737  32.269  102.357 1.00 24.74 ? 909  VAL B N     1 
ATOM   15696 C  CA    . VAL B  1  911  ? 33.248  31.497  101.219 1.00 27.78 ? 909  VAL B CA    1 
ATOM   15697 C  C     . VAL B  1  911  ? 32.870  30.112  101.715 1.00 26.17 ? 909  VAL B C     1 
ATOM   15698 O  O     . VAL B  1  911  ? 33.683  29.444  102.369 1.00 28.18 ? 909  VAL B O     1 
ATOM   15699 C  CB    . VAL B  1  911  ? 34.310  31.392  100.113 1.00 27.57 ? 909  VAL B CB    1 
ATOM   15700 C  CG1   . VAL B  1  911  ? 33.826  30.473  98.978  1.00 27.38 ? 909  VAL B CG1   1 
ATOM   15701 C  CG2   . VAL B  1  911  ? 34.699  32.784  99.607  1.00 31.19 ? 909  VAL B CG2   1 
ATOM   15702 N  N     . GLU B  1  912  ? 31.653  29.679  101.398 1.00 23.77 ? 910  GLU B N     1 
ATOM   15703 C  CA    . GLU B  1  912  ? 31.155  28.358  101.765 1.00 27.25 ? 910  GLU B CA    1 
ATOM   15704 C  C     . GLU B  1  912  ? 30.589  27.645  100.546 1.00 32.57 ? 910  GLU B C     1 
ATOM   15705 O  O     . GLU B  1  912  ? 29.859  28.251  99.757  1.00 27.81 ? 910  GLU B O     1 
ATOM   15706 C  CB    . GLU B  1  912  ? 30.083  28.464  102.837 1.00 29.04 ? 910  GLU B CB    1 
ATOM   15707 C  CG    . GLU B  1  912  ? 30.635  29.052  104.125 1.00 40.30 ? 910  GLU B CG    1 
ATOM   15708 C  CD    . GLU B  1  912  ? 29.574  29.259  105.173 1.00 42.18 ? 910  GLU B CD    1 
ATOM   15709 O  OE1   . GLU B  1  912  ? 29.113  28.257  105.759 1.00 51.82 ? 910  GLU B OE1   1 
ATOM   15710 O  OE2   . GLU B  1  912  ? 29.193  30.427  105.392 1.00 55.84 ? 910  GLU B OE2   1 
ATOM   15711 N  N     . GLN B  1  913  ? 30.918  26.355  100.400 1.00 25.60 ? 911  GLN B N     1 
ATOM   15712 C  CA    . GLN B  1  913  ? 30.430  25.562  99.278  1.00 27.51 ? 911  GLN B CA    1 
ATOM   15713 C  C     . GLN B  1  913  ? 29.950  24.197  99.741  1.00 35.15 ? 911  GLN B C     1 
ATOM   15714 O  O     . GLN B  1  913  ? 30.491  23.617  100.686 1.00 34.62 ? 911  GLN B O     1 
ATOM   15715 C  CB    . GLN B  1  913  ? 31.505  25.343  98.218  1.00 28.30 ? 911  GLN B CB    1 
ATOM   15716 C  CG    . GLN B  1  913  ? 32.119  26.609  97.689  1.00 30.98 ? 911  GLN B CG    1 
ATOM   15717 C  CD    . GLN B  1  913  ? 33.165  26.309  96.657  1.00 34.03 ? 911  GLN B CD    1 
ATOM   15718 O  OE1   . GLN B  1  913  ? 34.177  25.680  96.959  1.00 41.78 ? 911  GLN B OE1   1 
ATOM   15719 N  NE2   . GLN B  1  913  ? 32.922  26.729  95.425  1.00 27.78 ? 911  GLN B NE2   1 
ATOM   15720 N  N     . ILE B  1  914  ? 28.954  23.670  99.031  1.00 32.04 ? 912  ILE B N     1 
ATOM   15721 C  CA    . ILE B  1  914  ? 28.473  22.307  99.239  1.00 43.33 ? 912  ILE B CA    1 
ATOM   15722 C  C     . ILE B  1  914  ? 29.406  21.308  98.552  1.00 52.38 ? 912  ILE B C     1 
ATOM   15723 O  O     . ILE B  1  914  ? 30.251  21.685  97.730  1.00 44.08 ? 912  ILE B O     1 
ATOM   15724 C  CB    . ILE B  1  914  ? 27.026  22.156  98.738  1.00 43.58 ? 912  ILE B CB    1 
ATOM   15725 C  CG1   . ILE B  1  914  ? 26.987  21.989  97.223  1.00 41.30 ? 912  ILE B CG1   1 
ATOM   15726 C  CG2   . ILE B  1  914  ? 26.201  23.365  99.135  1.00 54.04 ? 912  ILE B CG2   1 
ATOM   15727 C  CD1   . ILE B  1  914  ? 26.504  20.625  96.787  1.00 46.26 ? 912  ILE B CD1   1 
ATOM   15728 N  N     . GLY B  1  915  ? 29.262  20.027  98.885  1.00 51.74 ? 913  GLY B N     1 
ATOM   15729 C  CA    . GLY B  1  915  ? 30.157  19.001  98.370  1.00 49.46 ? 913  GLY B CA    1 
ATOM   15730 C  C     . GLY B  1  915  ? 29.631  18.362  97.093  1.00 47.28 ? 913  GLY B C     1 
ATOM   15731 O  O     . GLY B  1  915  ? 28.432  18.146  96.936  1.00 50.02 ? 913  GLY B O     1 
ATOM   15732 N  N     . LEU B  1  916  ? 30.552  18.054  96.184  1.00 43.85 ? 914  LEU B N     1 
ATOM   15733 C  CA    . LEU B  1  916  ? 30.220  17.449  94.900  1.00 40.67 ? 914  LEU B CA    1 
ATOM   15734 C  C     . LEU B  1  916  ? 30.605  15.977  94.909  1.00 40.45 ? 914  LEU B C     1 
ATOM   15735 O  O     . LEU B  1  916  ? 31.699  15.622  95.358  1.00 40.26 ? 914  LEU B O     1 
ATOM   15736 C  CB    . LEU B  1  916  ? 30.937  18.165  93.754  1.00 38.39 ? 914  LEU B CB    1 
ATOM   15737 C  CG    . LEU B  1  916  ? 30.525  19.608  93.479  1.00 36.33 ? 914  LEU B CG    1 
ATOM   15738 C  CD1   . LEU B  1  916  ? 31.152  20.069  92.169  1.00 40.71 ? 914  LEU B CD1   1 
ATOM   15739 C  CD2   . LEU B  1  916  ? 29.008  19.736  93.449  1.00 35.63 ? 914  LEU B CD2   1 
ATOM   15740 N  N     . ALA B  1  917  ? 29.705  15.128  94.413  1.00 35.81 ? 915  ALA B N     1 
ATOM   15741 C  CA    . ALA B  1  917  ? 29.981  13.703  94.292  1.00 34.54 ? 915  ALA B CA    1 
ATOM   15742 C  C     . ALA B  1  917  ? 31.050  13.454  93.232  1.00 42.56 ? 915  ALA B C     1 
ATOM   15743 O  O     . ALA B  1  917  ? 31.251  14.255  92.315  1.00 37.67 ? 915  ALA B O     1 
ATOM   15744 C  CB    . ALA B  1  917  ? 28.706  12.937  93.934  1.00 42.72 ? 915  ALA B CB    1 
ATOM   15745 N  N     . SER B  1  918  ? 31.729  12.309  93.357  1.00 39.78 ? 916  SER B N     1 
ATOM   15746 C  CA    . SER B  1  918  ? 32.837  12.004  92.456  1.00 39.82 ? 916  SER B CA    1 
ATOM   15747 C  C     . SER B  1  918  ? 32.380  11.885  91.008  1.00 39.06 ? 916  SER B C     1 
ATOM   15748 O  O     . SER B  1  918  ? 33.175  12.116  90.090  1.00 38.52 ? 916  SER B O     1 
ATOM   15749 C  CB    . SER B  1  918  ? 33.530  10.715  92.896  1.00 40.74 ? 916  SER B CB    1 
ATOM   15750 O  OG    . SER B  1  918  ? 32.646  9.614   92.783  1.00 45.92 ? 916  SER B OG    1 
ATOM   15751 N  N     . GLU B  1  919  ? 31.107  11.537  90.781  1.00 36.29 ? 917  GLU B N     1 
ATOM   15752 C  CA    . GLU B  1  919  ? 30.605  11.390  89.419  1.00 43.12 ? 917  GLU B CA    1 
ATOM   15753 C  C     . GLU B  1  919  ? 30.626  12.701  88.652  1.00 43.81 ? 917  GLU B C     1 
ATOM   15754 O  O     . GLU B  1  919  ? 30.552  12.681  87.419  1.00 37.56 ? 917  GLU B O     1 
ATOM   15755 C  CB    . GLU B  1  919  ? 29.177  10.838  89.425  1.00 38.49 ? 917  GLU B CB    1 
ATOM   15756 N  N     . THR B  1  920  ? 30.709  13.837  89.346  1.00 37.82 ? 918  THR B N     1 
ATOM   15757 C  CA    . THR B  1  920  ? 30.745  15.124  88.665  1.00 31.61 ? 918  THR B CA    1 
ATOM   15758 C  C     . THR B  1  920  ? 32.058  15.366  87.926  1.00 30.92 ? 918  THR B C     1 
ATOM   15759 O  O     . THR B  1  920  ? 32.107  16.266  87.084  1.00 30.74 ? 918  THR B O     1 
ATOM   15760 C  CB    . THR B  1  920  ? 30.495  16.267  89.660  1.00 34.53 ? 918  THR B CB    1 
ATOM   15761 O  OG1   . THR B  1  920  ? 31.508  16.269  90.674  1.00 32.17 ? 918  THR B OG1   1 
ATOM   15762 C  CG2   . THR B  1  920  ? 29.123  16.135  90.311  1.00 31.39 ? 918  THR B CG2   1 
ATOM   15763 N  N     . GLY B  1  921  ? 33.110  14.592  88.208  1.00 29.41 ? 919  GLY B N     1 
ATOM   15764 C  CA    . GLY B  1  921  ? 34.408  14.836  87.593  1.00 31.87 ? 919  GLY B CA    1 
ATOM   15765 C  C     . GLY B  1  921  ? 34.434  14.676  86.083  1.00 32.99 ? 919  GLY B C     1 
ATOM   15766 O  O     . GLY B  1  921  ? 35.294  15.265  85.416  1.00 33.43 ? 919  GLY B O     1 
ATOM   15767 N  N     . VAL B  1  922  ? 33.518  13.885  85.523  1.00 25.63 ? 920  VAL B N     1 
ATOM   15768 C  CA    . VAL B  1  922  ? 33.455  13.736  84.071  1.00 22.86 ? 920  VAL B CA    1 
ATOM   15769 C  C     . VAL B  1  922  ? 32.789  14.918  83.388  1.00 24.06 ? 920  VAL B C     1 
ATOM   15770 O  O     . VAL B  1  922  ? 32.853  15.027  82.157  1.00 24.82 ? 920  VAL B O     1 
ATOM   15771 C  CB    . VAL B  1  922  ? 32.717  12.442  83.686  1.00 25.92 ? 920  VAL B CB    1 
ATOM   15772 C  CG1   . VAL B  1  922  ? 33.541  11.229  84.107  1.00 28.41 ? 920  VAL B CG1   1 
ATOM   15773 C  CG2   . VAL B  1  922  ? 31.343  12.407  84.337  1.00 26.44 ? 920  VAL B CG2   1 
ATOM   15774 N  N     . GLY B  1  923  ? 32.166  15.811  84.147  1.00 23.74 ? 921  GLY B N     1 
ATOM   15775 C  CA    . GLY B  1  923  ? 31.564  16.991  83.561  1.00 21.95 ? 921  GLY B CA    1 
ATOM   15776 C  C     . GLY B  1  923  ? 32.140  18.253  84.171  1.00 22.39 ? 921  GLY B C     1 
ATOM   15777 O  O     . GLY B  1  923  ? 33.164  18.198  84.856  1.00 24.76 ? 921  GLY B O     1 
ATOM   15778 N  N     . THR B  1  924  ? 31.500  19.395  83.951  1.00 19.51 ? 922  THR B N     1 
ATOM   15779 C  CA    . THR B  1  924  ? 31.984  20.666  84.483  1.00 20.40 ? 922  THR B CA    1 
ATOM   15780 C  C     . THR B  1  924  ? 30.971  21.201  85.490  1.00 21.99 ? 922  THR B C     1 
ATOM   15781 O  O     . THR B  1  924  ? 29.967  21.798  85.111  1.00 21.39 ? 922  THR B O     1 
ATOM   15782 C  CB    . THR B  1  924  ? 32.231  21.669  83.364  1.00 18.71 ? 922  THR B CB    1 
ATOM   15783 O  OG1   . THR B  1  924  ? 31.080  21.735  82.526  1.00 20.23 ? 922  THR B OG1   1 
ATOM   15784 C  CG2   . THR B  1  924  ? 33.437  21.237  82.539  1.00 23.06 ? 922  THR B CG2   1 
ATOM   15785 N  N     . PHE B  1  925  ? 31.241  20.991  86.773  1.00 20.86 ? 923  PHE B N     1 
ATOM   15786 C  CA    . PHE B  1  925  ? 30.330  21.394  87.833  1.00 18.73 ? 923  PHE B CA    1 
ATOM   15787 C  C     . PHE B  1  925  ? 30.987  22.400  88.761  1.00 20.58 ? 923  PHE B C     1 
ATOM   15788 O  O     . PHE B  1  925  ? 32.180  22.298  89.070  1.00 22.28 ? 923  PHE B O     1 
ATOM   15789 C  CB    . PHE B  1  925  ? 29.881  20.189  88.662  1.00 20.60 ? 923  PHE B CB    1 
ATOM   15790 C  CG    . PHE B  1  925  ? 29.013  19.227  87.913  1.00 20.96 ? 923  PHE B CG    1 
ATOM   15791 C  CD1   . PHE B  1  925  ? 29.571  18.266  87.088  1.00 19.33 ? 923  PHE B CD1   1 
ATOM   15792 C  CD2   . PHE B  1  925  ? 27.635  19.284  88.038  1.00 21.42 ? 923  PHE B CD2   1 
ATOM   15793 C  CE1   . PHE B  1  925  ? 28.772  17.375  86.400  1.00 20.71 ? 923  PHE B CE1   1 
ATOM   15794 C  CE2   . PHE B  1  925  ? 26.824  18.396  87.346  1.00 18.14 ? 923  PHE B CE2   1 
ATOM   15795 C  CZ    . PHE B  1  925  ? 27.391  17.437  86.540  1.00 18.95 ? 923  PHE B CZ    1 
ATOM   15796 N  N     . VAL B  1  926  ? 30.181  23.345  89.229  1.00 19.60 ? 924  VAL B N     1 
ATOM   15797 C  CA    . VAL B  1  926  ? 30.528  24.220  90.338  1.00 19.81 ? 924  VAL B CA    1 
ATOM   15798 C  C     . VAL B  1  926  ? 29.461  24.021  91.402  1.00 20.69 ? 924  VAL B C     1 
ATOM   15799 O  O     . VAL B  1  926  ? 28.269  24.107  91.094  1.00 20.51 ? 924  VAL B O     1 
ATOM   15800 C  CB    . VAL B  1  926  ? 30.597  25.700  89.920  1.00 18.83 ? 924  VAL B CB    1 
ATOM   15801 C  CG1   . VAL B  1  926  ? 30.892  26.578  91.135  1.00 20.48 ? 924  VAL B CG1   1 
ATOM   15802 C  CG2   . VAL B  1  926  ? 31.661  25.892  88.849  1.00 21.01 ? 924  VAL B CG2   1 
ATOM   15803 N  N     . PRO B  1  927  ? 29.828  23.737  92.647  1.00 22.74 ? 925  PRO B N     1 
ATOM   15804 C  CA    . PRO B  1  927  ? 28.814  23.564  93.674  1.00 21.23 ? 925  PRO B CA    1 
ATOM   15805 C  C     . PRO B  1  927  ? 28.184  24.893  94.038  1.00 21.62 ? 925  PRO B C     1 
ATOM   15806 O  O     . PRO B  1  927  ? 28.827  25.952  93.936  1.00 21.66 ? 925  PRO B O     1 
ATOM   15807 C  CB    . PRO B  1  927  ? 29.609  22.984  94.856  1.00 26.62 ? 925  PRO B CB    1 
ATOM   15808 C  CG    . PRO B  1  927  ? 30.976  23.548  94.671  1.00 24.33 ? 925  PRO B CG    1 
ATOM   15809 C  CD    . PRO B  1  927  ? 31.192  23.581  93.178  1.00 24.14 ? 925  PRO B CD    1 
ATOM   15810 N  N     . PRO B  1  928  ? 26.934  24.888  94.485  1.00 22.69 ? 926  PRO B N     1 
ATOM   15811 C  CA    . PRO B  1  928  ? 26.351  26.094  95.077  1.00 23.60 ? 926  PRO B CA    1 
ATOM   15812 C  C     . PRO B  1  928  ? 27.286  26.720  96.101  1.00 23.79 ? 926  PRO B C     1 
ATOM   15813 O  O     . PRO B  1  928  ? 27.842  26.043  96.972  1.00 26.22 ? 926  PRO B O     1 
ATOM   15814 C  CB    . PRO B  1  928  ? 25.064  25.572  95.722  1.00 26.40 ? 926  PRO B CB    1 
ATOM   15815 C  CG    . PRO B  1  928  ? 24.668  24.453  94.827  1.00 28.55 ? 926  PRO B CG    1 
ATOM   15816 C  CD    . PRO B  1  928  ? 25.944  23.810  94.332  1.00 26.49 ? 926  PRO B CD    1 
ATOM   15817 N  N     . THR B  1  929  ? 27.491  28.022  95.969  1.00 22.21 ? 927  THR B N     1 
ATOM   15818 C  CA    . THR B  1  929  ? 28.495  28.739  96.733  1.00 20.65 ? 927  THR B CA    1 
ATOM   15819 C  C     . THR B  1  929  ? 27.875  29.988  97.339  1.00 22.50 ? 927  THR B C     1 
ATOM   15820 O  O     . THR B  1  929  ? 27.080  30.668  96.686  1.00 23.76 ? 927  THR B O     1 
ATOM   15821 C  CB    . THR B  1  929  ? 29.672  29.117  95.834  1.00 23.21 ? 927  THR B CB    1 
ATOM   15822 O  OG1   . THR B  1  929  ? 30.235  27.920  95.275  1.00 21.10 ? 927  THR B OG1   1 
ATOM   15823 C  CG2   . THR B  1  929  ? 30.741  29.890  96.606  1.00 22.14 ? 927  THR B CG2   1 
ATOM   15824 N  N     . ILE B  1  930  ? 28.244  30.281  98.588  1.00 24.55 ? 928  ILE B N     1 
ATOM   15825 C  CA    . ILE B  1  930  ? 27.779  31.458  99.322  1.00 24.28 ? 928  ILE B CA    1 
ATOM   15826 C  C     . ILE B  1  930  ? 28.998  32.254  99.754  1.00 26.91 ? 928  ILE B C     1 
ATOM   15827 O  O     . ILE B  1  930  ? 29.895  31.720  100.426 1.00 24.95 ? 928  ILE B O     1 
ATOM   15828 C  CB    . ILE B  1  930  ? 26.931  31.076  100.545 1.00 24.18 ? 928  ILE B CB    1 
ATOM   15829 C  CG1   . ILE B  1  930  ? 25.723  30.250  100.122 1.00 24.63 ? 928  ILE B CG1   1 
ATOM   15830 C  CG2   . ILE B  1  930  ? 26.495  32.336  101.299 1.00 24.57 ? 928  ILE B CG2   1 
ATOM   15831 C  CD1   . ILE B  1  930  ? 24.872  29.795  101.278 1.00 33.93 ? 928  ILE B CD1   1 
ATOM   15832 N  N     . ILE B  1  931  ? 29.038  33.524  99.374  1.00 25.62 ? 929  ILE B N     1 
ATOM   15833 C  CA    . ILE B  1  931  ? 30.148  34.406  99.695  1.00 23.47 ? 929  ILE B CA    1 
ATOM   15834 C  C     . ILE B  1  931  ? 29.595  35.598  100.458 1.00 25.73 ? 929  ILE B C     1 
ATOM   15835 O  O     . ILE B  1  931  ? 28.676  36.269  99.984  1.00 23.09 ? 929  ILE B O     1 
ATOM   15836 C  CB    . ILE B  1  931  ? 30.885  34.863  98.426  1.00 23.17 ? 929  ILE B CB    1 
ATOM   15837 C  CG1   . ILE B  1  931  ? 31.342  33.643  97.608  1.00 23.57 ? 929  ILE B CG1   1 
ATOM   15838 C  CG2   . ILE B  1  931  ? 32.052  35.793  98.787  1.00 23.27 ? 929  ILE B CG2   1 
ATOM   15839 C  CD1   . ILE B  1  931  ? 32.107  34.003  96.349  1.00 26.58 ? 929  ILE B CD1   1 
ATOM   15840 N  N     . GLU B  1  932  ? 30.142  35.863  101.639 1.00 23.83 ? 930  GLU B N     1 
ATOM   15841 C  CA    . GLU B  1  932  ? 29.692  37.002  102.421 1.00 22.92 ? 930  GLU B CA    1 
ATOM   15842 C  C     . GLU B  1  932  ? 30.492  38.229  102.028 1.00 27.51 ? 930  GLU B C     1 
ATOM   15843 O  O     . GLU B  1  932  ? 31.725  38.198  102.022 1.00 29.09 ? 930  GLU B O     1 
ATOM   15844 C  CB    . GLU B  1  932  ? 29.841  36.734  103.916 1.00 28.72 ? 930  GLU B CB    1 
ATOM   15845 C  CG    . GLU B  1  932  ? 28.882  35.680  104.425 1.00 29.54 ? 930  GLU B CG    1 
ATOM   15846 C  CD    . GLU B  1  932  ? 28.871  35.607  105.935 1.00 48.19 ? 930  GLU B CD    1 
ATOM   15847 O  OE1   . GLU B  1  932  ? 29.734  36.263  106.567 1.00 46.89 ? 930  GLU B OE1   1 
ATOM   15848 O  OE2   . GLU B  1  932  ? 28.001  34.901  106.486 1.00 40.22 ? 930  GLU B OE2   1 
ATOM   15849 N  N     . LEU B  1  933  ? 29.796  39.303  101.696 1.00 22.05 ? 931  LEU B N     1 
ATOM   15850 C  CA    . LEU B  1  933  ? 30.447  40.542  101.326 1.00 24.47 ? 931  LEU B CA    1 
ATOM   15851 C  C     . LEU B  1  933  ? 30.253  41.567  102.431 1.00 28.15 ? 931  LEU B C     1 
ATOM   15852 O  O     . LEU B  1  933  ? 29.288  41.510  103.195 1.00 33.07 ? 931  LEU B O     1 
ATOM   15853 C  CB    . LEU B  1  933  ? 29.887  41.093  100.014 1.00 26.68 ? 931  LEU B CB    1 
ATOM   15854 C  CG    . LEU B  1  933  ? 29.916  40.216  98.763  1.00 29.47 ? 931  LEU B CG    1 
ATOM   15855 C  CD1   . LEU B  1  933  ? 29.289  40.982  97.622  1.00 32.22 ? 931  LEU B CD1   1 
ATOM   15856 C  CD2   . LEU B  1  933  ? 31.342  39.805  98.428  1.00 35.45 ? 931  LEU B CD2   1 
ATOM   15857 N  N     . GLU B  1  934  ? 31.184  42.514  102.500 1.00 35.40 ? 932  GLU B N     1 
ATOM   15858 C  CA    . GLU B  1  934  ? 31.009  43.659  103.379 1.00 34.00 ? 932  GLU B CA    1 
ATOM   15859 C  C     . GLU B  1  934  ? 30.180  44.749  102.723 1.00 40.43 ? 932  GLU B C     1 
ATOM   15860 O  O     . GLU B  1  934  ? 29.447  45.465  103.410 1.00 38.24 ? 932  GLU B O     1 
ATOM   15861 C  CB    . GLU B  1  934  ? 32.370  44.225  103.790 1.00 35.72 ? 932  GLU B CB    1 
ATOM   15862 N  N     . LYS B  1  935  ? 30.270  44.879  101.406 1.00 33.79 ? 933  LYS B N     1 
ATOM   15863 C  CA    . LYS B  1  935  ? 29.535  45.904  100.686 1.00 36.40 ? 933  LYS B CA    1 
ATOM   15864 C  C     . LYS B  1  935  ? 29.258  45.381  99.289  1.00 35.16 ? 933  LYS B C     1 
ATOM   15865 O  O     . LYS B  1  935  ? 30.032  44.586  98.751  1.00 29.51 ? 933  LYS B O     1 
ATOM   15866 C  CB    . LYS B  1  935  ? 30.317  47.224  100.629 1.00 37.58 ? 933  LYS B CB    1 
ATOM   15867 N  N     . LEU B  1  936  ? 28.142  45.825  98.708  1.00 31.06 ? 934  LEU B N     1 
ATOM   15868 C  CA    . LEU B  1  936  ? 27.817  45.395  97.356  1.00 34.17 ? 934  LEU B CA    1 
ATOM   15869 C  C     . LEU B  1  936  ? 28.916  45.776  96.373  1.00 34.29 ? 934  LEU B C     1 
ATOM   15870 O  O     . LEU B  1  936  ? 29.167  45.039  95.412  1.00 32.10 ? 934  LEU B O     1 
ATOM   15871 C  CB    . LEU B  1  936  ? 26.474  45.985  96.930  1.00 33.52 ? 934  LEU B CB    1 
ATOM   15872 C  CG    . LEU B  1  936  ? 25.518  45.003  96.253  1.00 34.57 ? 934  LEU B CG    1 
ATOM   15873 C  CD1   . LEU B  1  936  ? 24.077  45.438  96.469  1.00 35.63 ? 934  LEU B CD1   1 
ATOM   15874 C  CD2   . LEU B  1  936  ? 25.830  44.904  94.778  1.00 39.09 ? 934  LEU B CD2   1 
ATOM   15875 N  N     . SER B  1  937  ? 29.602  46.898  96.614  1.00 34.39 ? 935  SER B N     1 
ATOM   15876 C  CA    . SER B  1  937  ? 30.696  47.323  95.750  1.00 32.39 ? 935  SER B CA    1 
ATOM   15877 C  C     . SER B  1  937  ? 31.854  46.330  95.732  1.00 33.44 ? 935  SER B C     1 
ATOM   15878 O  O     . SER B  1  937  ? 32.712  46.436  94.848  1.00 33.57 ? 935  SER B O     1 
ATOM   15879 C  CB    . SER B  1  937  ? 31.204  48.705  96.182  1.00 32.54 ? 935  SER B CB    1 
ATOM   15880 O  OG    . SER B  1  937  ? 31.637  48.694  97.530  1.00 38.39 ? 935  SER B OG    1 
ATOM   15881 N  N     . ASP B  1  938  ? 31.905  45.381  96.677  1.00 32.82 ? 936  ASP B N     1 
ATOM   15882 C  CA    . ASP B  1  938  ? 32.887  44.301  96.608  1.00 33.56 ? 936  ASP B CA    1 
ATOM   15883 C  C     . ASP B  1  938  ? 32.698  43.432  95.371  1.00 36.95 ? 936  ASP B C     1 
ATOM   15884 O  O     . ASP B  1  938  ? 33.625  42.713  94.981  1.00 35.92 ? 936  ASP B O     1 
ATOM   15885 C  CB    . ASP B  1  938  ? 32.801  43.399  97.848  1.00 33.42 ? 936  ASP B CB    1 
ATOM   15886 C  CG    . ASP B  1  938  ? 33.133  44.127  99.149  1.00 46.10 ? 936  ASP B CG    1 
ATOM   15887 O  OD1   . ASP B  1  938  ? 33.654  45.264  99.101  1.00 40.05 ? 936  ASP B OD1   1 
ATOM   15888 O  OD2   . ASP B  1  938  ? 32.869  43.545  100.229 1.00 48.32 ? 936  ASP B OD2   1 
ATOM   15889 N  N     . LEU B  1  939  ? 31.516  43.463  94.767  1.00 31.88 ? 937  LEU B N     1 
ATOM   15890 C  CA    . LEU B  1  939  ? 31.182  42.638  93.613  1.00 32.88 ? 937  LEU B CA    1 
ATOM   15891 C  C     . LEU B  1  939  ? 31.257  43.513  92.368  1.00 28.54 ? 937  LEU B C     1 
ATOM   15892 O  O     . LEU B  1  939  ? 30.479  44.463  92.227  1.00 37.85 ? 937  LEU B O     1 
ATOM   15893 C  CB    . LEU B  1  939  ? 29.786  42.034  93.788  1.00 31.44 ? 937  LEU B CB    1 
ATOM   15894 C  CG    . LEU B  1  939  ? 29.285  41.034  92.751  1.00 31.10 ? 937  LEU B CG    1 
ATOM   15895 C  CD1   . LEU B  1  939  ? 30.241  39.851  92.645  1.00 35.32 ? 937  LEU B CD1   1 
ATOM   15896 C  CD2   . LEU B  1  939  ? 27.887  40.572  93.125  1.00 32.81 ? 937  LEU B CD2   1 
ATOM   15897 N  N     . GLN B  1  940  ? 32.192  43.197  91.469  1.00 32.43 ? 938  GLN B N     1 
ATOM   15898 C  CA    . GLN B  1  940  ? 32.524  44.076  90.354  1.00 38.84 ? 938  GLN B CA    1 
ATOM   15899 C  C     . GLN B  1  940  ? 32.057  43.576  88.993  1.00 37.28 ? 938  GLN B C     1 
ATOM   15900 O  O     . GLN B  1  940  ? 32.150  44.325  88.012  1.00 35.95 ? 938  GLN B O     1 
ATOM   15901 C  CB    . GLN B  1  940  ? 34.044  44.308  90.304  1.00 44.76 ? 938  GLN B CB    1 
ATOM   15902 N  N     . ARG B  1  941  ? 31.552  42.351  88.893  1.00 28.73 ? 939  ARG B N     1 
ATOM   15903 C  CA    . ARG B  1  941  ? 31.178  41.817  87.595  1.00 32.55 ? 939  ARG B CA    1 
ATOM   15904 C  C     . ARG B  1  941  ? 30.104  40.765  87.801  1.00 27.32 ? 939  ARG B C     1 
ATOM   15905 O  O     . ARG B  1  941  ? 30.000  40.176  88.880  1.00 27.83 ? 939  ARG B O     1 
ATOM   15906 C  CB    . ARG B  1  941  ? 32.388  41.221  86.861  1.00 33.99 ? 939  ARG B CB    1 
ATOM   15907 C  CG    . ARG B  1  941  ? 33.053  40.057  87.586  1.00 31.30 ? 939  ARG B CG    1 
ATOM   15908 C  CD    . ARG B  1  941  ? 34.307  39.616  86.836  1.00 34.26 ? 939  ARG B CD    1 
ATOM   15909 N  NE    . ARG B  1  941  ? 34.913  38.406  87.381  1.00 35.58 ? 939  ARG B NE    1 
ATOM   15910 C  CZ    . ARG B  1  941  ? 34.658  37.178  86.948  1.00 40.01 ? 939  ARG B CZ    1 
ATOM   15911 N  NH1   . ARG B  1  941  ? 33.764  36.953  85.996  1.00 34.09 ? 939  ARG B NH1   1 
ATOM   15912 N  NH2   . ARG B  1  941  ? 35.318  36.152  87.480  1.00 33.18 ? 939  ARG B NH2   1 
ATOM   15913 N  N     . GLU B  1  942  ? 29.293  40.554  86.767  1.00 28.21 ? 940  GLU B N     1 
ATOM   15914 C  CA    . GLU B  1  942  ? 28.324  39.467  86.789  1.00 27.75 ? 940  GLU B CA    1 
ATOM   15915 C  C     . GLU B  1  942  ? 29.085  38.151  86.765  1.00 27.60 ? 940  GLU B C     1 
ATOM   15916 O  O     . GLU B  1  942  ? 29.873  37.902  85.846  1.00 31.26 ? 940  GLU B O     1 
ATOM   15917 C  CB    . GLU B  1  942  ? 27.374  39.574  85.595  1.00 24.59 ? 940  GLU B CB    1 
ATOM   15918 C  CG    . GLU B  1  942  ? 26.312  38.469  85.488  1.00 27.20 ? 940  GLU B CG    1 
ATOM   15919 C  CD    . GLU B  1  942  ? 25.593  38.491  84.145  1.00 29.74 ? 940  GLU B CD    1 
ATOM   15920 O  OE1   . GLU B  1  942  ? 26.265  38.709  83.108  1.00 30.29 ? 940  GLU B OE1   1 
ATOM   15921 O  OE2   . GLU B  1  942  ? 24.360  38.282  84.114  1.00 28.23 ? 940  GLU B OE2   1 
ATOM   15922 N  N     . VAL B  1  943  ? 28.890  37.334  87.794  1.00 22.02 ? 941  VAL B N     1 
ATOM   15923 C  CA    . VAL B  1  943  ? 29.473  35.999  87.872  1.00 22.15 ? 941  VAL B CA    1 
ATOM   15924 C  C     . VAL B  1  943  ? 28.364  35.010  87.545  1.00 20.82 ? 941  VAL B C     1 
ATOM   15925 O  O     . VAL B  1  943  ? 27.445  34.795  88.343  1.00 21.13 ? 941  VAL B O     1 
ATOM   15926 C  CB    . VAL B  1  943  ? 30.088  35.731  89.249  1.00 22.62 ? 941  VAL B CB    1 
ATOM   15927 C  CG1   . VAL B  1  943  ? 30.686  34.329  89.305  1.00 24.07 ? 941  VAL B CG1   1 
ATOM   15928 C  CG2   . VAL B  1  943  ? 31.134  36.784  89.558  1.00 26.81 ? 941  VAL B CG2   1 
ATOM   15929 N  N     . PHE B  1  944  ? 28.447  34.407  86.363  1.00 19.75 ? 942  PHE B N     1 
ATOM   15930 C  CA    . PHE B  1  944  ? 27.326  33.676  85.779  1.00 19.27 ? 942  PHE B CA    1 
ATOM   15931 C  C     . PHE B  1  944  ? 27.413  32.205  86.187  1.00 21.36 ? 942  PHE B C     1 
ATOM   15932 O  O     . PHE B  1  944  ? 27.758  31.315  85.412  1.00 20.82 ? 942  PHE B O     1 
ATOM   15933 C  CB    . PHE B  1  944  ? 27.333  33.848  84.266  1.00 21.79 ? 942  PHE B CB    1 
ATOM   15934 C  CG    . PHE B  1  944  ? 26.004  33.619  83.622  1.00 21.87 ? 942  PHE B CG    1 
ATOM   15935 C  CD1   . PHE B  1  944  ? 24.991  34.556  83.747  1.00 25.05 ? 942  PHE B CD1   1 
ATOM   15936 C  CD2   . PHE B  1  944  ? 25.767  32.479  82.868  1.00 22.24 ? 942  PHE B CD2   1 
ATOM   15937 C  CE1   . PHE B  1  944  ? 23.762  34.356  83.145  1.00 21.06 ? 942  PHE B CE1   1 
ATOM   15938 C  CE2   . PHE B  1  944  ? 24.522  32.277  82.259  1.00 24.83 ? 942  PHE B CE2   1 
ATOM   15939 C  CZ    . PHE B  1  944  ? 23.528  33.223  82.408  1.00 24.10 ? 942  PHE B CZ    1 
ATOM   15940 N  N     . GLY B  1  945  ? 27.089  31.961  87.447  1.00 19.59 ? 943  GLY B N     1 
ATOM   15941 C  CA    . GLY B  1  945  ? 27.247  30.639  88.001  1.00 18.43 ? 943  GLY B CA    1 
ATOM   15942 C  C     . GLY B  1  945  ? 26.509  30.547  89.315  1.00 21.92 ? 943  GLY B C     1 
ATOM   15943 O  O     . GLY B  1  945  ? 25.816  31.480  89.721  1.00 19.27 ? 943  GLY B O     1 
ATOM   15944 N  N     . PRO B  1  946  ? 26.647  29.428  90.007  1.00 20.05 ? 944  PRO B N     1 
ATOM   15945 C  CA    . PRO B  1  946  ? 25.859  29.219  91.230  1.00 18.81 ? 944  PRO B CA    1 
ATOM   15946 C  C     . PRO B  1  946  ? 26.544  29.843  92.438  1.00 18.96 ? 944  PRO B C     1 
ATOM   15947 O  O     . PRO B  1  946  ? 26.967  29.161  93.367  1.00 20.89 ? 944  PRO B O     1 
ATOM   15948 C  CB    . PRO B  1  946  ? 25.781  27.692  91.309  1.00 19.10 ? 944  PRO B CB    1 
ATOM   15949 C  CG    . PRO B  1  946  ? 27.127  27.256  90.760  1.00 21.47 ? 944  PRO B CG    1 
ATOM   15950 C  CD    . PRO B  1  946  ? 27.391  28.223  89.611  1.00 17.50 ? 944  PRO B CD    1 
ATOM   15951 N  N     . VAL B  1  947  ? 26.691  31.162  92.404  1.00 20.20 ? 945  VAL B N     1 
ATOM   15952 C  CA    . VAL B  1  947  ? 27.453  31.882  93.412  1.00 17.59 ? 945  VAL B CA    1 
ATOM   15953 C  C     . VAL B  1  947  ? 26.556  32.974  93.982  1.00 21.91 ? 945  VAL B C     1 
ATOM   15954 O  O     . VAL B  1  947  ? 26.283  33.978  93.313  1.00 21.17 ? 945  VAL B O     1 
ATOM   15955 C  CB    . VAL B  1  947  ? 28.757  32.470  92.856  1.00 20.96 ? 945  VAL B CB    1 
ATOM   15956 C  CG1   . VAL B  1  947  ? 29.544  33.137  93.968  1.00 24.38 ? 945  VAL B CG1   1 
ATOM   15957 C  CG2   . VAL B  1  947  ? 29.595  31.376  92.184  1.00 22.15 ? 945  VAL B CG2   1 
ATOM   15958 N  N     . LEU B  1  948  ? 26.109  32.786  95.218  1.00 19.71 ? 946  LEU B N     1 
ATOM   15959 C  CA    . LEU B  1  948  ? 25.244  33.738  95.892  1.00 18.67 ? 946  LEU B CA    1 
ATOM   15960 C  C     . LEU B  1  948  ? 26.082  34.578  96.841  1.00 21.89 ? 946  LEU B C     1 
ATOM   15961 O  O     . LEU B  1  948  ? 26.827  34.037  97.660  1.00 22.08 ? 946  LEU B O     1 
ATOM   15962 C  CB    . LEU B  1  948  ? 24.147  33.009  96.661  1.00 18.78 ? 946  LEU B CB    1 
ATOM   15963 C  CG    . LEU B  1  948  ? 23.242  33.906  97.494  1.00 16.65 ? 946  LEU B CG    1 
ATOM   15964 C  CD1   . LEU B  1  948  ? 22.390  34.777  96.565  1.00 17.75 ? 946  LEU B CD1   1 
ATOM   15965 C  CD2   . LEU B  1  948  ? 22.379  33.038  98.396  1.00 22.93 ? 946  LEU B CD2   1 
ATOM   15966 N  N     . HIS B  1  949  ? 25.978  35.887  96.718  1.00 19.00 ? 947  HIS B N     1 
ATOM   15967 C  CA    . HIS B  1  949  ? 26.658  36.801  97.621  1.00 16.01 ? 947  HIS B CA    1 
ATOM   15968 C  C     . HIS B  1  949  ? 25.662  37.257  98.671  1.00 21.23 ? 947  HIS B C     1 
ATOM   15969 O  O     . HIS B  1  949  ? 24.470  37.404  98.387  1.00 22.56 ? 947  HIS B O     1 
ATOM   15970 C  CB    . HIS B  1  949  ? 27.234  37.978  96.838  1.00 20.06 ? 947  HIS B CB    1 
ATOM   15971 C  CG    . HIS B  1  949  ? 28.145  37.533  95.747  1.00 21.20 ? 947  HIS B CG    1 
ATOM   15972 N  ND1   . HIS B  1  949  ? 27.683  37.140  94.508  1.00 21.19 ? 947  HIS B ND1   1 
ATOM   15973 C  CD2   . HIS B  1  949  ? 29.481  37.317  95.739  1.00 22.72 ? 947  HIS B CD2   1 
ATOM   15974 C  CE1   . HIS B  1  949  ? 28.703  36.742  93.771  1.00 19.85 ? 947  HIS B CE1   1 
ATOM   15975 N  NE2   . HIS B  1  949  ? 29.803  36.834  94.495  1.00 20.35 ? 947  HIS B NE2   1 
ATOM   15976 N  N     . VAL B  1  950  ? 26.134  37.429  99.901  1.00 20.85 ? 948  VAL B N     1 
ATOM   15977 C  CA    . VAL B  1  950  ? 25.245  37.789  100.995 1.00 23.08 ? 948  VAL B CA    1 
ATOM   15978 C  C     . VAL B  1  950  ? 25.734  39.074  101.638 1.00 24.29 ? 948  VAL B C     1 
ATOM   15979 O  O     . VAL B  1  950  ? 26.917  39.203  101.977 1.00 24.08 ? 948  VAL B O     1 
ATOM   15980 C  CB    . VAL B  1  950  ? 25.130  36.671  102.043 1.00 24.19 ? 948  VAL B CB    1 
ATOM   15981 C  CG1   . VAL B  1  950  ? 24.290  37.172  103.227 1.00 25.66 ? 948  VAL B CG1   1 
ATOM   15982 C  CG2   . VAL B  1  950  ? 24.496  35.437  101.427 1.00 23.54 ? 948  VAL B CG2   1 
ATOM   15983 N  N     . ILE B  1  951  ? 24.815  40.015  101.805 1.00 19.06 ? 949  ILE B N     1 
ATOM   15984 C  CA    . ILE B  1  951  ? 25.042  41.286  102.478 1.00 19.64 ? 949  ILE B CA    1 
ATOM   15985 C  C     . ILE B  1  951  ? 24.063  41.369  103.637 1.00 20.13 ? 949  ILE B C     1 
ATOM   15986 O  O     . ILE B  1  951  ? 22.911  40.946  103.507 1.00 21.82 ? 949  ILE B O     1 
ATOM   15987 C  CB    . ILE B  1  951  ? 24.828  42.459  101.504 1.00 28.18 ? 949  ILE B CB    1 
ATOM   15988 C  CG1   . ILE B  1  951  ? 25.993  42.539  100.530 1.00 35.32 ? 949  ILE B CG1   1 
ATOM   15989 C  CG2   . ILE B  1  951  ? 24.639  43.788  102.244 1.00 34.92 ? 949  ILE B CG2   1 
ATOM   15990 C  CD1   . ILE B  1  951  ? 25.784  43.605  99.528  1.00 41.40 ? 949  ILE B CD1   1 
ATOM   15991 N  N     . ARG B  1  952  ? 24.519  41.894  104.768 1.00 19.38 ? 950  ARG B N     1 
ATOM   15992 C  CA    . ARG B  1  952  ? 23.645  42.175  105.894 1.00 20.82 ? 950  ARG B CA    1 
ATOM   15993 C  C     . ARG B  1  952  ? 23.426  43.678  105.964 1.00 22.48 ? 950  ARG B C     1 
ATOM   15994 O  O     . ARG B  1  952  ? 24.343  44.460  105.689 1.00 25.77 ? 950  ARG B O     1 
ATOM   15995 C  CB    . ARG B  1  952  ? 24.254  41.657  107.203 1.00 22.10 ? 950  ARG B CB    1 
ATOM   15996 C  CG    . ARG B  1  952  ? 24.714  40.222  107.088 1.00 25.63 ? 950  ARG B CG    1 
ATOM   15997 C  CD    . ARG B  1  952  ? 25.706  39.887  108.182 1.00 30.53 ? 950  ARG B CD    1 
ATOM   15998 N  NE    . ARG B  1  952  ? 25.038  39.713  109.462 1.00 37.80 ? 950  ARG B NE    1 
ATOM   15999 C  CZ    . ARG B  1  952  ? 24.834  38.539  110.044 1.00 36.45 ? 950  ARG B CZ    1 
ATOM   16000 N  NH1   . ARG B  1  952  ? 25.217  37.407  109.470 1.00 30.84 ? 950  ARG B NH1   1 
ATOM   16001 N  NH2   . ARG B  1  952  ? 24.240  38.501  111.235 1.00 35.93 ? 950  ARG B NH2   1 
ATOM   16002 N  N     . TYR B  1  953  ? 22.210  44.094  106.317 1.00 20.34 ? 951  TYR B N     1 
ATOM   16003 C  CA    . TYR B  1  953  ? 21.963  45.527  106.403 1.00 21.73 ? 951  TYR B CA    1 
ATOM   16004 C  C     . TYR B  1  953  ? 21.127  45.846  107.631 1.00 20.54 ? 951  TYR B C     1 
ATOM   16005 O  O     . TYR B  1  953  ? 20.318  45.035  108.083 1.00 20.96 ? 951  TYR B O     1 
ATOM   16006 C  CB    . TYR B  1  953  ? 21.267  46.065  105.140 1.00 22.26 ? 951  TYR B CB    1 
ATOM   16007 C  CG    . TYR B  1  953  ? 19.831  45.645  105.021 1.00 19.56 ? 951  TYR B CG    1 
ATOM   16008 C  CD1   . TYR B  1  953  ? 19.486  44.412  104.471 1.00 19.45 ? 951  TYR B CD1   1 
ATOM   16009 C  CD2   . TYR B  1  953  ? 18.810  46.482  105.440 1.00 19.82 ? 951  TYR B CD2   1 
ATOM   16010 C  CE1   . TYR B  1  953  ? 18.172  44.033  104.371 1.00 18.21 ? 951  TYR B CE1   1 
ATOM   16011 C  CE2   . TYR B  1  953  ? 17.488  46.104  105.337 1.00 21.67 ? 951  TYR B CE2   1 
ATOM   16012 C  CZ    . TYR B  1  953  ? 17.176  44.877  104.795 1.00 20.59 ? 951  TYR B CZ    1 
ATOM   16013 O  OH    . TYR B  1  953  ? 15.851  44.505  104.713 1.00 19.61 ? 951  TYR B OH    1 
ATOM   16014 N  N     . ARG B  1  954  ? 21.346  47.045  108.165 1.00 24.37 ? 952  ARG B N     1 
ATOM   16015 C  CA    . ARG B  1  954  ? 20.500  47.597  109.212 1.00 27.79 ? 952  ARG B CA    1 
ATOM   16016 C  C     . ARG B  1  954  ? 19.265  48.213  108.574 1.00 23.95 ? 952  ARG B C     1 
ATOM   16017 O  O     . ARG B  1  954  ? 19.356  48.844  107.518 1.00 21.52 ? 952  ARG B O     1 
ATOM   16018 C  CB    . ARG B  1  954  ? 21.267  48.655  110.017 1.00 28.62 ? 952  ARG B CB    1 
ATOM   16019 N  N     . ARG B  1  955  ? 18.102  48.022  109.210 1.00 27.46 ? 953  ARG B N     1 
ATOM   16020 C  CA    . ARG B  1  955  ? 16.860  48.504  108.611 1.00 29.60 ? 953  ARG B CA    1 
ATOM   16021 C  C     . ARG B  1  955  ? 16.903  50.005  108.344 1.00 26.15 ? 953  ARG B C     1 
ATOM   16022 O  O     . ARG B  1  955  ? 16.330  50.472  107.352 1.00 27.79 ? 953  ARG B O     1 
ATOM   16023 C  CB    . ARG B  1  955  ? 15.663  48.155  109.501 1.00 33.53 ? 953  ARG B CB    1 
ATOM   16024 C  CG    . ARG B  1  955  ? 14.302  48.605  108.946 1.00 41.03 ? 953  ARG B CG    1 
ATOM   16025 C  CD    . ARG B  1  955  ? 14.092  48.190  107.481 1.00 39.75 ? 953  ARG B CD    1 
ATOM   16026 N  NE    . ARG B  1  955  ? 12.799  48.618  106.953 1.00 39.33 ? 953  ARG B NE    1 
ATOM   16027 C  CZ    . ARG B  1  955  ? 12.520  49.850  106.542 1.00 45.62 ? 953  ARG B CZ    1 
ATOM   16028 N  NH1   . ARG B  1  955  ? 13.426  50.815  106.575 1.00 39.64 ? 953  ARG B NH1   1 
ATOM   16029 N  NH2   . ARG B  1  955  ? 11.300  50.120  106.083 1.00 41.97 ? 953  ARG B NH2   1 
ATOM   16030 N  N     . ASP B  1  956  ? 17.587  50.770  109.195 1.00 26.38 ? 954  ASP B N     1 
ATOM   16031 C  CA    . ASP B  1  956  ? 17.719  52.205  108.962 1.00 28.14 ? 954  ASP B CA    1 
ATOM   16032 C  C     . ASP B  1  956  ? 18.465  52.518  107.680 1.00 28.73 ? 954  ASP B C     1 
ATOM   16033 O  O     . ASP B  1  956  ? 18.356  53.640  107.171 1.00 31.28 ? 954  ASP B O     1 
ATOM   16034 C  CB    . ASP B  1  956  ? 18.456  52.881  110.121 1.00 31.13 ? 954  ASP B CB    1 
ATOM   16035 C  CG    . ASP B  1  956  ? 17.665  52.865  111.398 1.00 49.24 ? 954  ASP B CG    1 
ATOM   16036 O  OD1   . ASP B  1  956  ? 16.422  52.733  111.314 1.00 44.04 ? 954  ASP B OD1   1 
ATOM   16037 O  OD2   . ASP B  1  956  ? 18.287  52.989  112.477 1.00 54.13 ? 954  ASP B OD2   1 
ATOM   16038 N  N     . ASP B  1  957  ? 19.230  51.564  107.159 1.00 23.51 ? 955  ASP B N     1 
ATOM   16039 C  CA    . ASP B  1  957  ? 20.045  51.765  105.974 1.00 25.39 ? 955  ASP B CA    1 
ATOM   16040 C  C     . ASP B  1  957  ? 19.375  51.236  104.719 1.00 20.75 ? 955  ASP B C     1 
ATOM   16041 O  O     . ASP B  1  957  ? 20.034  51.131  103.685 1.00 24.27 ? 955  ASP B O     1 
ATOM   16042 C  CB    . ASP B  1  957  ? 21.402  51.082  106.136 1.00 26.00 ? 955  ASP B CB    1 
ATOM   16043 C  CG    . ASP B  1  957  ? 22.308  51.800  107.103 1.00 36.06 ? 955  ASP B CG    1 
ATOM   16044 O  OD1   . ASP B  1  957  ? 22.173  53.037  107.248 1.00 36.39 ? 955  ASP B OD1   1 
ATOM   16045 O  OD2   . ASP B  1  957  ? 23.158  51.119  107.714 1.00 34.03 ? 955  ASP B OD2   1 
ATOM   16046 N  N     . LEU B  1  958  ? 18.090  50.889  104.794 1.00 21.32 ? 956  LEU B N     1 
ATOM   16047 C  CA    . LEU B  1  958  ? 17.421  50.295  103.639 1.00 20.48 ? 956  LEU B CA    1 
ATOM   16048 C  C     . LEU B  1  958  ? 17.518  51.189  102.409 1.00 22.48 ? 956  LEU B C     1 
ATOM   16049 O  O     . LEU B  1  958  ? 17.794  50.706  101.305 1.00 20.28 ? 956  LEU B O     1 
ATOM   16050 C  CB    . LEU B  1  958  ? 15.964  50.018  103.978 1.00 22.47 ? 956  LEU B CB    1 
ATOM   16051 C  CG    . LEU B  1  958  ? 15.116  49.442  102.851 1.00 22.74 ? 956  LEU B CG    1 
ATOM   16052 C  CD1   . LEU B  1  958  ? 15.704  48.119  102.384 1.00 20.49 ? 956  LEU B CD1   1 
ATOM   16053 C  CD2   . LEU B  1  958  ? 13.697  49.256  103.341 1.00 22.35 ? 956  LEU B CD2   1 
ATOM   16054 N  N     . ASP B  1  959  ? 17.285  52.490  102.566 1.00 19.56 ? 957  ASP B N     1 
ATOM   16055 C  CA    . ASP B  1  959  ? 17.317  53.358  101.396 1.00 22.07 ? 957  ASP B CA    1 
ATOM   16056 C  C     . ASP B  1  959  ? 18.707  53.387  100.771 1.00 20.79 ? 957  ASP B C     1 
ATOM   16057 O  O     . ASP B  1  959  ? 18.842  53.342  99.542  1.00 21.76 ? 957  ASP B O     1 
ATOM   16058 C  CB    . ASP B  1  959  ? 16.854  54.763  101.772 1.00 21.62 ? 957  ASP B CB    1 
ATOM   16059 C  CG    . ASP B  1  959  ? 16.400  55.550  100.573 1.00 23.39 ? 957  ASP B CG    1 
ATOM   16060 O  OD1   . ASP B  1  959  ? 15.677  54.979  99.727  1.00 22.78 ? 957  ASP B OD1   1 
ATOM   16061 O  OD2   . ASP B  1  959  ? 16.759  56.736  100.477 1.00 24.59 ? 957  ASP B OD2   1 
ATOM   16062 N  N     . ARG B  1  960  ? 19.753  53.455  101.603 1.00 20.59 ? 958  ARG B N     1 
ATOM   16063 C  CA    . ARG B  1  960  ? 21.119  53.392  101.096 1.00 21.33 ? 958  ARG B CA    1 
ATOM   16064 C  C     . ARG B  1  960  ? 21.400  52.048  100.436 1.00 20.52 ? 958  ARG B C     1 
ATOM   16065 O  O     . ARG B  1  960  ? 22.142  51.974  99.451  1.00 22.32 ? 958  ARG B O     1 
ATOM   16066 C  CB    . ARG B  1  960  ? 22.111  53.652  102.234 1.00 25.09 ? 958  ARG B CB    1 
ATOM   16067 N  N     . LEU B  1  961  ? 20.834  50.970  100.979 1.00 18.18 ? 959  LEU B N     1 
ATOM   16068 C  CA    . LEU B  1  961  ? 21.019  49.667  100.355 1.00 18.89 ? 959  LEU B CA    1 
ATOM   16069 C  C     . LEU B  1  961  ? 20.414  49.640  98.962  1.00 19.69 ? 959  LEU B C     1 
ATOM   16070 O  O     . LEU B  1  961  ? 21.021  49.109  98.025  1.00 19.62 ? 959  LEU B O     1 
ATOM   16071 C  CB    . LEU B  1  961  ? 20.405  48.580  101.227 1.00 18.00 ? 959  LEU B CB    1 
ATOM   16072 C  CG    . LEU B  1  961  ? 20.405  47.178  100.617 1.00 20.46 ? 959  LEU B CG    1 
ATOM   16073 C  CD1   . LEU B  1  961  ? 21.820  46.603  100.509 1.00 22.52 ? 959  LEU B CD1   1 
ATOM   16074 C  CD2   . LEU B  1  961  ? 19.504  46.270  101.426 1.00 19.63 ? 959  LEU B CD2   1 
ATOM   16075 N  N     . VAL B  1  962  ? 19.225  50.220  98.799  1.00 17.53 ? 960  VAL B N     1 
ATOM   16076 C  CA    . VAL B  1  962  ? 18.641  50.298  97.469  1.00 17.51 ? 960  VAL B CA    1 
ATOM   16077 C  C     . VAL B  1  962  ? 19.562  51.063  96.527  1.00 22.63 ? 960  VAL B C     1 
ATOM   16078 O  O     . VAL B  1  962  ? 19.751  50.665  95.375  1.00 21.00 ? 960  VAL B O     1 
ATOM   16079 C  CB    . VAL B  1  962  ? 17.241  50.928  97.542  1.00 18.62 ? 960  VAL B CB    1 
ATOM   16080 C  CG1   . VAL B  1  962  ? 16.714  51.151  96.151  1.00 21.89 ? 960  VAL B CG1   1 
ATOM   16081 C  CG2   . VAL B  1  962  ? 16.299  50.006  98.307  1.00 19.40 ? 960  VAL B CG2   1 
ATOM   16082 N  N     . ASP B  1  963  ? 20.167  52.160  97.004  1.00 19.10 ? 961  ASP B N     1 
ATOM   16083 C  CA    . ASP B  1  963  ? 21.169  52.865  96.202  1.00 20.92 ? 961  ASP B CA    1 
ATOM   16084 C  C     . ASP B  1  963  ? 22.306  51.938  95.812  1.00 21.90 ? 961  ASP B C     1 
ATOM   16085 O  O     . ASP B  1  963  ? 22.767  51.946  94.664  1.00 23.33 ? 961  ASP B O     1 
ATOM   16086 C  CB    . ASP B  1  963  ? 21.754  54.050  96.969  1.00 23.59 ? 961  ASP B CB    1 
ATOM   16087 C  CG    . ASP B  1  963  ? 20.804  55.181  97.121  1.00 27.51 ? 961  ASP B CG    1 
ATOM   16088 O  OD1   . ASP B  1  963  ? 19.806  55.229  96.375  1.00 26.53 ? 961  ASP B OD1   1 
ATOM   16089 O  OD2   . ASP B  1  963  ? 21.083  56.044  97.990  1.00 29.53 ? 961  ASP B OD2   1 
ATOM   16090 N  N     . ASP B  1  964  ? 22.794  51.150  96.774  1.00 21.11 ? 962  ASP B N     1 
ATOM   16091 C  CA    . ASP B  1  964  ? 23.887  50.223  96.501  1.00 22.37 ? 962  ASP B CA    1 
ATOM   16092 C  C     . ASP B  1  964  ? 23.508  49.226  95.412  1.00 23.34 ? 962  ASP B C     1 
ATOM   16093 O  O     . ASP B  1  964  ? 24.325  48.909  94.539  1.00 22.39 ? 962  ASP B O     1 
ATOM   16094 C  CB    . ASP B  1  964  ? 24.281  49.486  97.781  1.00 22.46 ? 962  ASP B CB    1 
ATOM   16095 C  CG    . ASP B  1  964  ? 24.985  50.379  98.775  1.00 29.27 ? 962  ASP B CG    1 
ATOM   16096 O  OD1   . ASP B  1  964  ? 25.374  51.507  98.396  1.00 29.02 ? 962  ASP B OD1   1 
ATOM   16097 O  OD2   . ASP B  1  964  ? 25.137  49.944  99.941  1.00 33.18 ? 962  ASP B OD2   1 
ATOM   16098 N  N     . VAL B  1  965  ? 22.268  48.728  95.442  1.00 20.47 ? 963  VAL B N     1 
ATOM   16099 C  CA    . VAL B  1  965  ? 21.828  47.804  94.403  1.00 16.18 ? 963  VAL B CA    1 
ATOM   16100 C  C     . VAL B  1  965  ? 21.796  48.510  93.053  1.00 18.38 ? 963  VAL B C     1 
ATOM   16101 O  O     . VAL B  1  965  ? 22.257  47.968  92.039  1.00 21.07 ? 963  VAL B O     1 
ATOM   16102 C  CB    . VAL B  1  965  ? 20.456  47.204  94.755  1.00 19.71 ? 963  VAL B CB    1 
ATOM   16103 C  CG1   . VAL B  1  965  ? 19.938  46.386  93.567  1.00 17.78 ? 963  VAL B CG1   1 
ATOM   16104 C  CG2   . VAL B  1  965  ? 20.550  46.336  96.008  1.00 20.08 ? 963  VAL B CG2   1 
ATOM   16105 N  N     . ASN B  1  966  ? 21.237  49.724  93.016  1.00 19.85 ? 964  ASN B N     1 
ATOM   16106 C  CA    . ASN B  1  966  ? 21.168  50.460  91.752  1.00 19.69 ? 964  ASN B CA    1 
ATOM   16107 C  C     . ASN B  1  966  ? 22.553  50.841  91.245  1.00 22.99 ? 964  ASN B C     1 
ATOM   16108 O  O     . ASN B  1  966  ? 22.740  51.004  90.033  1.00 23.22 ? 964  ASN B O     1 
ATOM   16109 C  CB    . ASN B  1  966  ? 20.330  51.729  91.907  1.00 20.34 ? 964  ASN B CB    1 
ATOM   16110 C  CG    . ASN B  1  966  ? 18.857  51.450  92.135  1.00 20.71 ? 964  ASN B CG    1 
ATOM   16111 O  OD1   . ASN B  1  966  ? 18.335  50.419  91.720  1.00 21.43 ? 964  ASN B OD1   1 
ATOM   16112 N  ND2   . ASN B  1  966  ? 18.175  52.382  92.780  1.00 20.13 ? 964  ASN B ND2   1 
ATOM   16113 N  N     . ALA B  1  967  ? 23.525  50.994  92.151  1.00 20.04 ? 965  ALA B N     1 
ATOM   16114 C  CA    . ALA B  1  967  ? 24.826  51.556  91.799  1.00 23.27 ? 965  ALA B CA    1 
ATOM   16115 C  C     . ALA B  1  967  ? 25.670  50.627  90.935  1.00 23.24 ? 965  ALA B C     1 
ATOM   16116 O  O     . ALA B  1  967  ? 26.686  51.072  90.385  1.00 25.26 ? 965  ALA B O     1 
ATOM   16117 C  CB    . ALA B  1  967  ? 25.605  51.904  93.071  1.00 23.55 ? 965  ALA B CB    1 
ATOM   16118 N  N     . THR B  1  968  ? 25.315  49.344  90.833  1.00 20.59 ? 966  THR B N     1 
ATOM   16119 C  CA    . THR B  1  968  ? 26.037  48.452  89.930  1.00 19.28 ? 966  THR B CA    1 
ATOM   16120 C  C     . THR B  1  968  ? 25.886  48.871  88.476  1.00 20.24 ? 966  THR B C     1 
ATOM   16121 O  O     . THR B  1  968  ? 26.704  48.470  87.638  1.00 24.92 ? 966  THR B O     1 
ATOM   16122 C  CB    . THR B  1  968  ? 25.547  47.012  90.052  1.00 21.13 ? 966  THR B CB    1 
ATOM   16123 O  OG1   . THR B  1  968  ? 24.253  46.916  89.434  1.00 20.94 ? 966  THR B OG1   1 
ATOM   16124 C  CG2   . THR B  1  968  ? 25.446  46.584  91.501  1.00 26.57 ? 966  THR B CG2   1 
ATOM   16125 N  N     . GLY B  1  969  ? 24.848  49.643  88.161  1.00 21.62 ? 967  GLY B N     1 
ATOM   16126 C  CA    . GLY B  1  969  ? 24.532  50.010  86.801  1.00 23.15 ? 967  GLY B CA    1 
ATOM   16127 C  C     . GLY B  1  969  ? 23.629  49.035  86.086  1.00 21.44 ? 967  GLY B C     1 
ATOM   16128 O  O     . GLY B  1  969  ? 23.126  49.363  85.007  1.00 21.57 ? 967  GLY B O     1 
ATOM   16129 N  N     . TYR B  1  970  ? 23.410  47.853  86.656  1.00 18.59 ? 968  TYR B N     1 
ATOM   16130 C  CA    . TYR B  1  970  ? 22.467  46.889  86.116  1.00 17.80 ? 968  TYR B CA    1 
ATOM   16131 C  C     . TYR B  1  970  ? 21.065  47.176  86.624  1.00 21.32 ? 968  TYR B C     1 
ATOM   16132 O  O     . TYR B  1  970  ? 20.851  47.959  87.548  1.00 21.81 ? 968  TYR B O     1 
ATOM   16133 C  CB    . TYR B  1  970  ? 22.875  45.473  86.515  1.00 19.47 ? 968  TYR B CB    1 
ATOM   16134 C  CG    . TYR B  1  970  ? 24.112  44.984  85.813  1.00 22.32 ? 968  TYR B CG    1 
ATOM   16135 C  CD1   . TYR B  1  970  ? 24.027  44.459  84.536  1.00 23.64 ? 968  TYR B CD1   1 
ATOM   16136 C  CD2   . TYR B  1  970  ? 25.357  45.032  86.433  1.00 23.18 ? 968  TYR B CD2   1 
ATOM   16137 C  CE1   . TYR B  1  970  ? 25.150  43.995  83.873  1.00 29.20 ? 968  TYR B CE1   1 
ATOM   16138 C  CE2   . TYR B  1  970  ? 26.496  44.565  85.770  1.00 27.47 ? 968  TYR B CE2   1 
ATOM   16139 C  CZ    . TYR B  1  970  ? 26.374  44.049  84.495  1.00 31.12 ? 968  TYR B CZ    1 
ATOM   16140 O  OH    . TYR B  1  970  ? 27.481  43.578  83.817  1.00 42.37 ? 968  TYR B OH    1 
ATOM   16141 N  N     . GLY B  1  971  ? 20.096  46.502  86.030  1.00 17.77 ? 969  GLY B N     1 
ATOM   16142 C  CA    . GLY B  1  971  ? 18.736  46.684  86.479  1.00 18.03 ? 969  GLY B CA    1 
ATOM   16143 C  C     . GLY B  1  971  ? 17.825  45.680  85.822  1.00 17.23 ? 969  GLY B C     1 
ATOM   16144 O  O     . GLY B  1  971  ? 16.878  46.064  85.125  1.00 19.15 ? 969  GLY B O     1 
ATOM   16145 N  N     . LEU B  1  972  ? 18.100  44.390  86.041  1.00 16.51 ? 970  LEU B N     1 
ATOM   16146 C  CA    . LEU B  1  972  ? 17.324  43.351  85.381  1.00 14.87 ? 970  LEU B CA    1 
ATOM   16147 C  C     . LEU B  1  972  ? 16.232  42.845  86.320  1.00 15.12 ? 970  LEU B C     1 
ATOM   16148 O  O     . LEU B  1  972  ? 15.106  43.352  86.285  1.00 17.57 ? 970  LEU B O     1 
ATOM   16149 C  CB    . LEU B  1  972  ? 18.234  42.219  84.908  1.00 16.20 ? 970  LEU B CB    1 
ATOM   16150 C  CG    . LEU B  1  972  ? 17.575  41.190  83.987  1.00 17.23 ? 970  LEU B CG    1 
ATOM   16151 C  CD1   . LEU B  1  972  ? 16.837  41.866  82.822  1.00 20.58 ? 970  LEU B CD1   1 
ATOM   16152 C  CD2   . LEU B  1  972  ? 18.633  40.199  83.483  1.00 19.64 ? 970  LEU B CD2   1 
ATOM   16153 N  N     . THR B  1  973  ? 16.540  41.864  87.167  1.00 16.15 ? 971  THR B N     1 
ATOM   16154 C  CA    . THR B  1  973  ? 15.548  41.399  88.123  1.00 15.67 ? 971  THR B CA    1 
ATOM   16155 C  C     . THR B  1  973  ? 15.888  41.862  89.534  1.00 14.10 ? 971  THR B C     1 
ATOM   16156 O  O     . THR B  1  973  ? 17.033  42.188  89.857  1.00 16.12 ? 971  THR B O     1 
ATOM   16157 C  CB    . THR B  1  973  ? 15.411  39.875  88.105  1.00 14.67 ? 971  THR B CB    1 
ATOM   16158 O  OG1   . THR B  1  973  ? 16.653  39.270  88.477  1.00 16.26 ? 971  THR B OG1   1 
ATOM   16159 C  CG2   . THR B  1  973  ? 14.996  39.400  86.703  1.00 18.42 ? 971  THR B CG2   1 
ATOM   16160 N  N     . PHE B  1  974  ? 14.852  41.872  90.370  1.00 15.49 ? 972  PHE B N     1 
ATOM   16161 C  CA    . PHE B  1  974  ? 14.969  42.301  91.751  1.00 14.49 ? 972  PHE B CA    1 
ATOM   16162 C  C     . PHE B  1  974  ? 13.863  41.645  92.559  1.00 16.27 ? 972  PHE B C     1 
ATOM   16163 O  O     . PHE B  1  974  ? 12.709  41.625  92.131  1.00 16.38 ? 972  PHE B O     1 
ATOM   16164 C  CB    . PHE B  1  974  ? 14.848  43.822  91.878  1.00 13.70 ? 972  PHE B CB    1 
ATOM   16165 C  CG    . PHE B  1  974  ? 14.783  44.282  93.301  1.00 15.07 ? 972  PHE B CG    1 
ATOM   16166 C  CD1   . PHE B  1  974  ? 15.951  44.413  94.028  1.00 15.92 ? 972  PHE B CD1   1 
ATOM   16167 C  CD2   . PHE B  1  974  ? 13.565  44.574  93.893  1.00 16.59 ? 972  PHE B CD2   1 
ATOM   16168 C  CE1   . PHE B  1  974  ? 15.914  44.831  95.354  1.00 17.39 ? 972  PHE B CE1   1 
ATOM   16169 C  CE2   . PHE B  1  974  ? 13.507  44.987  95.200  1.00 16.91 ? 972  PHE B CE2   1 
ATOM   16170 C  CZ    . PHE B  1  974  ? 14.676  45.107  95.938  1.00 17.44 ? 972  PHE B CZ    1 
ATOM   16171 N  N     . GLY B  1  975  ? 14.212  41.161  93.748  1.00 14.73 ? 973  GLY B N     1 
ATOM   16172 C  CA    . GLY B  1  975  ? 13.247  40.550  94.641  1.00 14.67 ? 973  GLY B CA    1 
ATOM   16173 C  C     . GLY B  1  975  ? 13.167  41.272  95.974  1.00 14.31 ? 973  GLY B C     1 
ATOM   16174 O  O     . GLY B  1  975  ? 14.151  41.806  96.467  1.00 15.92 ? 973  GLY B O     1 
ATOM   16175 N  N     . LEU B  1  976  ? 11.972  41.272  96.555  1.00 15.75 ? 974  LEU B N     1 
ATOM   16176 C  CA    . LEU B  1  976  ? 11.751  41.831  97.876  1.00 16.52 ? 974  LEU B CA    1 
ATOM   16177 C  C     . LEU B  1  976  ? 10.861  40.866  98.631  1.00 17.35 ? 974  LEU B C     1 
ATOM   16178 O  O     . LEU B  1  976  ? 9.788   40.505  98.146  1.00 16.99 ? 974  LEU B O     1 
ATOM   16179 C  CB    . LEU B  1  976  ? 11.087  43.207  97.781  1.00 17.06 ? 974  LEU B CB    1 
ATOM   16180 C  CG    . LEU B  1  976  ? 10.639  43.814  99.116  1.00 18.25 ? 974  LEU B CG    1 
ATOM   16181 C  CD1   . LEU B  1  976  ? 11.836  44.156  99.998  1.00 18.97 ? 974  LEU B CD1   1 
ATOM   16182 C  CD2   . LEU B  1  976  ? 9.810   45.041  98.836  1.00 19.67 ? 974  LEU B CD2   1 
ATOM   16183 N  N     . HIS B  1  977  ? 11.314  40.440  99.804  1.00 16.30 ? 975  HIS B N     1 
ATOM   16184 C  CA    . HIS B  1  977  ? 10.510  39.626  100.706 1.00 17.47 ? 975  HIS B CA    1 
ATOM   16185 C  C     . HIS B  1  977  ? 10.212  40.454  101.943 1.00 16.53 ? 975  HIS B C     1 
ATOM   16186 O  O     . HIS B  1  977  ? 11.118  40.788  102.714 1.00 17.16 ? 975  HIS B O     1 
ATOM   16187 C  CB    . HIS B  1  977  ? 11.219  38.327  101.072 1.00 16.56 ? 975  HIS B CB    1 
ATOM   16188 C  CG    . HIS B  1  977  ? 10.931  37.205  100.129 1.00 19.19 ? 975  HIS B CG    1 
ATOM   16189 N  ND1   . HIS B  1  977  ? 10.112  36.146  100.458 1.00 26.52 ? 975  HIS B ND1   1 
ATOM   16190 C  CD2   . HIS B  1  977  ? 11.323  36.996  98.850  1.00 24.45 ? 975  HIS B CD2   1 
ATOM   16191 C  CE1   . HIS B  1  977  ? 10.036  35.320  99.431  1.00 21.19 ? 975  HIS B CE1   1 
ATOM   16192 N  NE2   . HIS B  1  977  ? 10.764  35.809  98.446  1.00 26.48 ? 975  HIS B NE2   1 
ATOM   16193 N  N     . THR B  1  978  ? 8.943   40.795  102.104 1.00 16.31 ? 976  THR B N     1 
ATOM   16194 C  CA    . THR B  1  978  ? 8.470   41.580  103.229 1.00 17.19 ? 976  THR B CA    1 
ATOM   16195 C  C     . THR B  1  978  ? 6.964   41.431  103.295 1.00 19.91 ? 976  THR B C     1 
ATOM   16196 O  O     . THR B  1  978  ? 6.296   41.255  102.274 1.00 19.14 ? 976  THR B O     1 
ATOM   16197 C  CB    . THR B  1  978  ? 8.841   43.065  103.109 1.00 17.38 ? 976  THR B CB    1 
ATOM   16198 O  OG1   . THR B  1  978  ? 8.315   43.768  104.239 1.00 18.52 ? 976  THR B OG1   1 
ATOM   16199 C  CG2   . THR B  1  978  ? 8.218   43.672  101.879 1.00 19.44 ? 976  THR B CG2   1 
ATOM   16200 N  N     . ARG B  1  979  ? 6.431   41.500  104.505 1.00 19.00 ? 977  ARG B N     1 
ATOM   16201 C  CA    . ARG B  1  979  ? 4.992   41.526  104.643 1.00 18.20 ? 977  ARG B CA    1 
ATOM   16202 C  C     . ARG B  1  979  ? 4.443   42.938  104.785 1.00 20.28 ? 977  ARG B C     1 
ATOM   16203 O  O     . ARG B  1  979  ? 3.229   43.099  104.925 1.00 21.59 ? 977  ARG B O     1 
ATOM   16204 C  CB    . ARG B  1  979  ? 4.565   40.685  105.842 1.00 23.85 ? 977  ARG B CB    1 
ATOM   16205 C  CG    . ARG B  1  979  ? 4.895   39.218  105.682 1.00 30.60 ? 977  ARG B CG    1 
ATOM   16206 C  CD    . ARG B  1  979  ? 4.636   38.484  106.971 1.00 33.48 ? 977  ARG B CD    1 
ATOM   16207 N  NE    . ARG B  1  979  ? 4.668   37.038  106.794 1.00 37.50 ? 977  ARG B NE    1 
ATOM   16208 C  CZ    . ARG B  1  979  ? 4.350   36.166  107.740 1.00 40.89 ? 977  ARG B CZ    1 
ATOM   16209 N  NH1   . ARG B  1  979  ? 3.977   36.564  108.948 1.00 33.05 ? 977  ARG B NH1   1 
ATOM   16210 N  NH2   . ARG B  1  979  ? 4.409   34.864  107.468 1.00 39.21 ? 977  ARG B NH2   1 
ATOM   16211 N  N     . LEU B  1  980  ? 5.298   43.957  104.728 1.00 17.66 ? 978  LEU B N     1 
ATOM   16212 C  CA    . LEU B  1  980  ? 4.933   45.311  105.141 1.00 16.52 ? 978  LEU B CA    1 
ATOM   16213 C  C     . LEU B  1  980  ? 4.738   46.211  103.934 1.00 17.77 ? 978  LEU B C     1 
ATOM   16214 O  O     . LEU B  1  980  ? 5.677   46.428  103.157 1.00 18.44 ? 978  LEU B O     1 
ATOM   16215 C  CB    . LEU B  1  980  ? 6.003   45.897  106.056 1.00 19.05 ? 978  LEU B CB    1 
ATOM   16216 C  CG    . LEU B  1  980  ? 6.383   44.972  107.210 1.00 20.93 ? 978  LEU B CG    1 
ATOM   16217 C  CD1   . LEU B  1  980  ? 7.537   45.595  108.002 1.00 20.41 ? 978  LEU B CD1   1 
ATOM   16218 C  CD2   . LEU B  1  980  ? 5.175   44.711  108.078 1.00 21.17 ? 978  LEU B CD2   1 
ATOM   16219 N  N     . ASP B  1  981  ? 3.532   46.773  103.812 1.00 18.22 ? 979  ASP B N     1 
ATOM   16220 C  CA    . ASP B  1  981  ? 3.210   47.597  102.650 1.00 18.28 ? 979  ASP B CA    1 
ATOM   16221 C  C     . ASP B  1  981  ? 4.112   48.818  102.543 1.00 19.07 ? 979  ASP B C     1 
ATOM   16222 O  O     . ASP B  1  981  ? 4.439   49.248  101.431 1.00 18.96 ? 979  ASP B O     1 
ATOM   16223 C  CB    . ASP B  1  981  ? 1.757   48.047  102.701 1.00 19.95 ? 979  ASP B CB    1 
ATOM   16224 C  CG    . ASP B  1  981  ? 0.793   46.950  102.343 1.00 23.60 ? 979  ASP B CG    1 
ATOM   16225 O  OD1   . ASP B  1  981  ? 1.217   45.935  101.751 1.00 23.49 ? 979  ASP B OD1   1 
ATOM   16226 O  OD2   . ASP B  1  981  ? -0.401  47.128  102.650 1.00 24.94 ? 979  ASP B OD2   1 
ATOM   16227 N  N     . GLU B  1  982  ? 4.477   49.428  103.677 1.00 19.39 ? 980  GLU B N     1 
ATOM   16228 C  CA    . GLU B  1  982  ? 5.343   50.602  103.613 1.00 20.00 ? 980  GLU B CA    1 
ATOM   16229 C  C     . GLU B  1  982  ? 6.689   50.241  103.006 1.00 19.52 ? 980  GLU B C     1 
ATOM   16230 O  O     . GLU B  1  982  ? 7.259   51.005  102.215 1.00 19.59 ? 980  GLU B O     1 
ATOM   16231 C  CB    . GLU B  1  982  ? 5.546   51.227  104.995 1.00 21.10 ? 980  GLU B CB    1 
ATOM   16232 C  CG    . GLU B  1  982  ? 6.608   52.333  104.944 1.00 24.52 ? 980  GLU B CG    1 
ATOM   16233 C  CD    . GLU B  1  982  ? 7.074   52.808  106.302 1.00 31.79 ? 980  GLU B CD    1 
ATOM   16234 O  OE1   . GLU B  1  982  ? 7.486   51.967  107.134 1.00 34.16 ? 980  GLU B OE1   1 
ATOM   16235 O  OE2   . GLU B  1  982  ? 7.042   54.031  106.529 1.00 27.21 ? 980  GLU B OE2   1 
ATOM   16236 N  N     . THR B  1  983  ? 7.217   49.072  103.366 1.00 16.75 ? 981  THR B N     1 
ATOM   16237 C  CA    . THR B  1  983  ? 8.487   48.647  102.801 1.00 17.15 ? 981  THR B CA    1 
ATOM   16238 C  C     . THR B  1  983  ? 8.349   48.327  101.320 1.00 17.47 ? 981  THR B C     1 
ATOM   16239 O  O     . THR B  1  983  ? 9.229   48.674  100.524 1.00 19.61 ? 981  THR B O     1 
ATOM   16240 C  CB    . THR B  1  983  ? 9.009   47.447  103.584 1.00 19.10 ? 981  THR B CB    1 
ATOM   16241 O  OG1   . THR B  1  983  ? 9.250   47.874  104.929 1.00 20.99 ? 981  THR B OG1   1 
ATOM   16242 C  CG2   . THR B  1  983  ? 10.286  46.924  102.971 1.00 22.14 ? 981  THR B CG2   1 
ATOM   16243 N  N     . ILE B  1  984  ? 7.233   47.702  100.932 1.00 16.56 ? 982  ILE B N     1 
ATOM   16244 C  CA    . ILE B  1  984  ? 6.991   47.429  99.518  1.00 18.32 ? 982  ILE B CA    1 
ATOM   16245 C  C     . ILE B  1  984  ? 6.950   48.727  98.729  1.00 16.87 ? 982  ILE B C     1 
ATOM   16246 O  O     . ILE B  1  984  ? 7.593   48.862  97.681  1.00 18.60 ? 982  ILE B O     1 
ATOM   16247 C  CB    . ILE B  1  984  ? 5.694   46.626  99.333  1.00 17.72 ? 982  ILE B CB    1 
ATOM   16248 C  CG1   . ILE B  1  984  ? 5.893   45.221  99.886  1.00 21.31 ? 982  ILE B CG1   1 
ATOM   16249 C  CG2   . ILE B  1  984  ? 5.331   46.540  97.850  1.00 21.87 ? 982  ILE B CG2   1 
ATOM   16250 C  CD1   . ILE B  1  984  ? 4.598   44.458  100.039 1.00 21.23 ? 982  ILE B CD1   1 
ATOM   16251 N  N     . ALA B  1  985  ? 6.205   49.709  99.229  1.00 18.52 ? 983  ALA B N     1 
ATOM   16252 C  CA    . ALA B  1  985  ? 6.100   50.974  98.508  1.00 16.86 ? 983  ALA B CA    1 
ATOM   16253 C  C     . ALA B  1  985  ? 7.450   51.668  98.436  1.00 19.91 ? 983  ALA B C     1 
ATOM   16254 O  O     . ALA B  1  985  ? 7.841   52.176  97.382  1.00 19.01 ? 983  ALA B O     1 
ATOM   16255 C  CB    . ALA B  1  985  ? 5.075   51.878  99.177  1.00 18.33 ? 983  ALA B CB    1 
ATOM   16256 N  N     . HIS B  1  986  ? 8.178   51.685  99.549  1.00 18.20 ? 984  HIS B N     1 
ATOM   16257 C  CA    . HIS B  1  986  ? 9.477   52.347  99.569  1.00 19.62 ? 984  HIS B CA    1 
ATOM   16258 C  C     . HIS B  1  986  ? 10.419  51.686  98.572  1.00 19.41 ? 984  HIS B C     1 
ATOM   16259 O  O     . HIS B  1  986  ? 10.960  52.336  97.669  1.00 19.57 ? 984  HIS B O     1 
ATOM   16260 C  CB    . HIS B  1  986  ? 10.047  52.303  100.991 1.00 20.27 ? 984  HIS B CB    1 
ATOM   16261 C  CG    . HIS B  1  986  ? 11.440  52.845  101.126 1.00 22.49 ? 984  HIS B CG    1 
ATOM   16262 N  ND1   . HIS B  1  986  ? 12.034  53.023  102.356 1.00 27.01 ? 984  HIS B ND1   1 
ATOM   16263 C  CD2   . HIS B  1  986  ? 12.354  53.240  100.207 1.00 24.31 ? 984  HIS B CD2   1 
ATOM   16264 C  CE1   . HIS B  1  986  ? 13.254  53.504  102.189 1.00 29.36 ? 984  HIS B CE1   1 
ATOM   16265 N  NE2   . HIS B  1  986  ? 13.476  53.638  100.895 1.00 25.41 ? 984  HIS B NE2   1 
ATOM   16266 N  N     . VAL B  1  987  ? 10.611  50.380  98.706  1.00 17.15 ? 985  VAL B N     1 
ATOM   16267 C  CA    . VAL B  1  987  ? 11.623  49.712  97.897  1.00 17.15 ? 985  VAL B CA    1 
ATOM   16268 C  C     . VAL B  1  987  ? 11.244  49.724  96.422  1.00 18.21 ? 985  VAL B C     1 
ATOM   16269 O  O     . VAL B  1  987  ? 12.087  49.986  95.560  1.00 20.10 ? 985  VAL B O     1 
ATOM   16270 C  CB    . VAL B  1  987  ? 11.855  48.288  98.416  1.00 18.18 ? 985  VAL B CB    1 
ATOM   16271 C  CG1   . VAL B  1  987  ? 12.728  47.531  97.448  1.00 20.55 ? 985  VAL B CG1   1 
ATOM   16272 C  CG2   . VAL B  1  987  ? 12.504  48.351  99.802  1.00 19.03 ? 985  VAL B CG2   1 
ATOM   16273 N  N     . THR B  1  988  ? 9.981   49.441  96.097  1.00 18.80 ? 986  THR B N     1 
ATOM   16274 C  CA    . THR B  1  988  ? 9.637   49.404  94.678  1.00 19.75 ? 986  THR B CA    1 
ATOM   16275 C  C     . THR B  1  988  ? 9.651   50.797  94.060  1.00 20.10 ? 986  THR B C     1 
ATOM   16276 O  O     . THR B  1  988  ? 9.867   50.919  92.851  1.00 27.07 ? 986  THR B O     1 
ATOM   16277 C  CB    . THR B  1  988  ? 8.284   48.725  94.437  1.00 22.86 ? 986  THR B CB    1 
ATOM   16278 O  OG1   . THR B  1  988  ? 7.248   49.467  95.074  1.00 23.25 ? 986  THR B OG1   1 
ATOM   16279 C  CG2   . THR B  1  988  ? 8.294   47.288  94.941  1.00 25.36 ? 986  THR B CG2   1 
ATOM   16280 N  N     . SER B  1  989  ? 9.460   51.851  94.857  1.00 20.67 ? 987  SER B N     1 
ATOM   16281 C  CA    . SER B  1  989  ? 9.556   53.199  94.305  1.00 22.45 ? 987  SER B CA    1 
ATOM   16282 C  C     . SER B  1  989  ? 10.998  53.636  94.050  1.00 25.72 ? 987  SER B C     1 
ATOM   16283 O  O     . SER B  1  989  ? 11.217  54.542  93.240  1.00 29.50 ? 987  SER B O     1 
ATOM   16284 C  CB    . SER B  1  989  ? 8.858   54.211  95.223  1.00 24.77 ? 987  SER B CB    1 
ATOM   16285 O  OG    . SER B  1  989  ? 9.596   54.476  96.402  1.00 31.67 ? 987  SER B OG    1 
ATOM   16286 N  N     . ARG B  1  990  ? 11.984  53.012  94.689  1.00 20.03 ? 988  ARG B N     1 
ATOM   16287 C  CA    . ARG B  1  990  ? 13.371  53.473  94.604  1.00 22.25 ? 988  ARG B CA    1 
ATOM   16288 C  C     . ARG B  1  990  ? 14.280  52.549  93.808  1.00 22.06 ? 988  ARG B C     1 
ATOM   16289 O  O     . ARG B  1  990  ? 15.293  53.005  93.270  1.00 21.84 ? 988  ARG B O     1 
ATOM   16290 C  CB    . ARG B  1  990  ? 13.961  53.654  96.010  1.00 22.17 ? 988  ARG B CB    1 
ATOM   16291 C  CG    . ARG B  1  990  ? 13.100  54.488  96.947  1.00 32.57 ? 988  ARG B CG    1 
ATOM   16292 C  CD    . ARG B  1  990  ? 13.290  55.966  96.713  1.00 28.50 ? 988  ARG B CD    1 
ATOM   16293 N  NE    . ARG B  1  990  ? 14.427  56.487  97.465  1.00 24.41 ? 988  ARG B NE    1 
ATOM   16294 C  CZ    . ARG B  1  990  ? 14.824  57.751  97.416  1.00 22.34 ? 988  ARG B CZ    1 
ATOM   16295 N  NH1   . ARG B  1  990  ? 14.240  58.621  96.609  1.00 28.28 ? 988  ARG B NH1   1 
ATOM   16296 N  NH2   . ARG B  1  990  ? 15.823  58.149  98.198  1.00 23.11 ? 988  ARG B NH2   1 
ATOM   16297 N  N     . ILE B  1  991  ? 13.956  51.259  93.729  1.00 18.65 ? 989  ILE B N     1 
ATOM   16298 C  CA    . ILE B  1  991  ? 14.762  50.342  92.947  1.00 19.38 ? 989  ILE B CA    1 
ATOM   16299 C  C     . ILE B  1  991  ? 14.584  50.653  91.466  1.00 19.65 ? 989  ILE B C     1 
ATOM   16300 O  O     . ILE B  1  991  ? 13.535  51.140  91.027  1.00 22.03 ? 989  ILE B O     1 
ATOM   16301 C  CB    . ILE B  1  991  ? 14.361  48.894  93.272  1.00 18.05 ? 989  ILE B CB    1 
ATOM   16302 C  CG1   . ILE B  1  991  ? 15.444  47.920  92.803  1.00 21.90 ? 989  ILE B CG1   1 
ATOM   16303 C  CG2   . ILE B  1  991  ? 12.986  48.573  92.686  1.00 22.94 ? 989  ILE B CG2   1 
ATOM   16304 C  CD1   . ILE B  1  991  ? 16.664  47.938  93.718  1.00 24.39 ? 989  ILE B CD1   1 
ATOM   16305 N  N     . LYS B  1  992  ? 15.627  50.400  90.691  1.00 17.70 ? 990  LYS B N     1 
ATOM   16306 C  CA    . LYS B  1  992  ? 15.605  50.698  89.261  1.00 18.46 ? 990  LYS B CA    1 
ATOM   16307 C  C     . LYS B  1  992  ? 15.909  49.409  88.513  1.00 19.21 ? 990  LYS B C     1 
ATOM   16308 O  O     . LYS B  1  992  ? 17.027  49.197  88.051  1.00 23.39 ? 990  LYS B O     1 
ATOM   16309 C  CB    . LYS B  1  992  ? 16.624  51.813  88.936  1.00 18.79 ? 990  LYS B CB    1 
ATOM   16310 C  CG    . LYS B  1  992  ? 16.240  53.150  89.563  1.00 22.67 ? 990  LYS B CG    1 
ATOM   16311 C  CD    . LYS B  1  992  ? 17.326  54.180  89.344  1.00 33.25 ? 990  LYS B CD    1 
ATOM   16312 C  CE    . LYS B  1  992  ? 17.574  54.427  87.867  1.00 38.37 ? 990  LYS B CE    1 
ATOM   16313 N  NZ    . LYS B  1  992  ? 18.738  55.341  87.651  1.00 45.39 ? 990  LYS B NZ    1 
ATOM   16314 N  N     . ALA B  1  993  ? 14.912  48.539  88.418  1.00 20.32 ? 991  ALA B N     1 
ATOM   16315 C  CA    . ALA B  1  993  ? 15.057  47.274  87.714  1.00 18.17 ? 991  ALA B CA    1 
ATOM   16316 C  C     . ALA B  1  993  ? 13.805  47.017  86.897  1.00 15.90 ? 991  ALA B C     1 
ATOM   16317 O  O     . ALA B  1  993  ? 12.719  47.503  87.224  1.00 18.64 ? 991  ALA B O     1 
ATOM   16318 C  CB    . ALA B  1  993  ? 15.294  46.108  88.675  1.00 19.50 ? 991  ALA B CB    1 
ATOM   16319 N  N     . GLY B  1  994  ? 13.973  46.241  85.822  1.00 17.12 ? 992  GLY B N     1 
ATOM   16320 C  CA    . GLY B  1  994  ? 12.873  46.026  84.896  1.00 17.09 ? 992  GLY B CA    1 
ATOM   16321 C  C     . GLY B  1  994  ? 11.875  44.975  85.328  1.00 15.12 ? 992  GLY B C     1 
ATOM   16322 O  O     . GLY B  1  994  ? 10.723  45.015  84.891  1.00 15.60 ? 992  GLY B O     1 
ATOM   16323 N  N     . ASN B  1  995  ? 12.286  44.032  86.166  1.00 15.88 ? 993  ASN B N     1 
ATOM   16324 C  CA    . ASN B  1  995  ? 11.429  42.933  86.588  1.00 15.08 ? 993  ASN B CA    1 
ATOM   16325 C  C     . ASN B  1  995  ? 11.515  42.816  88.097  1.00 14.10 ? 993  ASN B C     1 
ATOM   16326 O  O     . ASN B  1  995  ? 12.555  42.415  88.630  1.00 15.99 ? 993  ASN B O     1 
ATOM   16327 C  CB    . ASN B  1  995  ? 11.843  41.636  85.905  1.00 14.06 ? 993  ASN B CB    1 
ATOM   16328 C  CG    . ASN B  1  995  ? 11.300  41.552  84.496  1.00 15.06 ? 993  ASN B CG    1 
ATOM   16329 O  OD1   . ASN B  1  995  ? 11.897  42.060  83.544  1.00 15.15 ? 993  ASN B OD1   1 
ATOM   16330 N  ND2   . ASN B  1  995  ? 10.140  40.935  84.361  1.00 15.78 ? 993  ASN B ND2   1 
ATOM   16331 N  N     . LEU B  1  996  ? 10.442  43.202  88.764  1.00 15.75 ? 994  LEU B N     1 
ATOM   16332 C  CA    . LEU B  1  996  ? 10.354  43.188  90.215  1.00 14.44 ? 994  LEU B CA    1 
ATOM   16333 C  C     . LEU B  1  996  ? 9.523   41.998  90.643  1.00 17.06 ? 994  LEU B C     1 
ATOM   16334 O  O     . LEU B  1  996  ? 8.549   41.644  89.979  1.00 15.85 ? 994  LEU B O     1 
ATOM   16335 C  CB    . LEU B  1  996  ? 9.715   44.471  90.736  1.00 15.27 ? 994  LEU B CB    1 
ATOM   16336 C  CG    . LEU B  1  996  ? 10.305  45.753  90.148  1.00 15.64 ? 994  LEU B CG    1 
ATOM   16337 C  CD1   . LEU B  1  996  ? 9.574   46.942  90.798  1.00 20.03 ? 994  LEU B CD1   1 
ATOM   16338 C  CD2   . LEU B  1  996  ? 11.821  45.821  90.362  1.00 17.23 ? 994  LEU B CD2   1 
ATOM   16339 N  N     . TYR B  1  997  ? 9.899   41.397  91.769  1.00 15.07 ? 995  TYR B N     1 
ATOM   16340 C  CA    . TYR B  1  997  ? 9.220   40.216  92.283  1.00 17.16 ? 995  TYR B CA    1 
ATOM   16341 C  C     . TYR B  1  997  ? 9.047   40.373  93.779  1.00 16.40 ? 995  TYR B C     1 
ATOM   16342 O  O     . TYR B  1  997  ? 10.023  40.612  94.497  1.00 17.99 ? 995  TYR B O     1 
ATOM   16343 C  CB    . TYR B  1  997  ? 10.021  38.956  91.983  1.00 15.60 ? 995  TYR B CB    1 
ATOM   16344 C  CG    . TYR B  1  997  ? 10.177  38.699  90.507  1.00 13.43 ? 995  TYR B CG    1 
ATOM   16345 C  CD1   . TYR B  1  997  ? 9.176   38.048  89.805  1.00 19.22 ? 995  TYR B CD1   1 
ATOM   16346 C  CD2   . TYR B  1  997  ? 11.312  39.129  89.812  1.00 14.35 ? 995  TYR B CD2   1 
ATOM   16347 C  CE1   . TYR B  1  997  ? 9.293   37.799  88.456  1.00 17.51 ? 995  TYR B CE1   1 
ATOM   16348 C  CE2   . TYR B  1  997  ? 11.430  38.874  88.431  1.00 15.73 ? 995  TYR B CE2   1 
ATOM   16349 C  CZ    . TYR B  1  997  ? 10.407  38.218  87.780  1.00 16.80 ? 995  TYR B CZ    1 
ATOM   16350 O  OH    . TYR B  1  997  ? 10.459  37.935  86.430  1.00 20.81 ? 995  TYR B OH    1 
ATOM   16351 N  N     . ILE B  1  998  ? 7.816   40.250  94.243  1.00 15.04 ? 996  ILE B N     1 
ATOM   16352 C  CA    . ILE B  1  998  ? 7.492   40.494  95.641  1.00 14.82 ? 996  ILE B CA    1 
ATOM   16353 C  C     . ILE B  1  998  ? 7.039   39.177  96.252  1.00 14.56 ? 996  ILE B C     1 
ATOM   16354 O  O     . ILE B  1  998  ? 6.019   38.610  95.838  1.00 16.07 ? 996  ILE B O     1 
ATOM   16355 C  CB    . ILE B  1  998  ? 6.407   41.563  95.800  1.00 16.75 ? 996  ILE B CB    1 
ATOM   16356 C  CG1   . ILE B  1  998  ? 6.808   42.868  95.097  1.00 22.88 ? 996  ILE B CG1   1 
ATOM   16357 C  CG2   . ILE B  1  998  ? 6.163   41.828  97.278  1.00 18.23 ? 996  ILE B CG2   1 
ATOM   16358 C  CD1   . ILE B  1  998  ? 8.136   43.391  95.487  1.00 26.78 ? 996  ILE B CD1   1 
ATOM   16359 N  N     . ASN B  1  999  ? 7.794   38.707  97.251  1.00 17.00 ? 997  ASN B N     1 
ATOM   16360 C  CA    . ASN B  1  999  ? 7.420   37.529  98.036  1.00 17.00 ? 997  ASN B CA    1 
ATOM   16361 C  C     . ASN B  1  999  ? 7.356   36.271  97.174  1.00 17.04 ? 997  ASN B C     1 
ATOM   16362 O  O     . ASN B  1  999  ? 6.548   35.372  97.402  1.00 17.24 ? 997  ASN B O     1 
ATOM   16363 C  CB    . ASN B  1  999  ? 6.114   37.778  98.791  1.00 18.06 ? 997  ASN B CB    1 
ATOM   16364 C  CG    . ASN B  1  999  ? 6.299   38.797  99.900  1.00 16.03 ? 997  ASN B CG    1 
ATOM   16365 O  OD1   . ASN B  1  999  ? 7.390   38.907  100.449 1.00 17.95 ? 997  ASN B OD1   1 
ATOM   16366 N  ND2   . ASN B  1  999  ? 5.257   39.546  100.222 1.00 18.19 ? 997  ASN B ND2   1 
ATOM   16367 N  N     . ARG B  1  1000 ? 8.247   36.195  96.194  1.00 14.64 ? 998  ARG B N     1 
ATOM   16368 C  CA    . ARG B  1  1000 ? 8.389   35.013  95.356  1.00 14.12 ? 998  ARG B CA    1 
ATOM   16369 C  C     . ARG B  1  1000 ? 9.818   34.969  94.839  1.00 16.07 ? 998  ARG B C     1 
ATOM   16370 O  O     . ARG B  1  1000 ? 10.632  35.843  95.143  1.00 19.02 ? 998  ARG B O     1 
ATOM   16371 C  CB    . ARG B  1  1000 ? 7.374   35.012  94.214  1.00 17.49 ? 998  ARG B CB    1 
ATOM   16372 C  CG    . ARG B  1  1000 ? 7.290   36.331  93.472  1.00 15.14 ? 998  ARG B CG    1 
ATOM   16373 C  CD    . ARG B  1  1000 ? 6.823   36.101  92.045  1.00 15.61 ? 998  ARG B CD    1 
ATOM   16374 N  NE    . ARG B  1  1000 ? 7.828   35.363  91.302  1.00 15.97 ? 998  ARG B NE    1 
ATOM   16375 C  CZ    . ARG B  1  1000 ? 7.691   35.007  90.032  1.00 16.48 ? 998  ARG B CZ    1 
ATOM   16376 N  NH1   . ARG B  1  1000 ? 6.621   35.354  89.327  1.00 16.69 ? 998  ARG B NH1   1 
ATOM   16377 N  NH2   . ARG B  1  1000 ? 8.654   34.302  89.451  1.00 17.93 ? 998  ARG B NH2   1 
ATOM   16378 N  N     . ASN B  1  1001 ? 10.130  33.934  94.058  1.00 15.77 ? 999  ASN B N     1 
ATOM   16379 C  CA    . ASN B  1  1001 ? 11.452  33.897  93.456  1.00 15.73 ? 999  ASN B CA    1 
ATOM   16380 C  C     . ASN B  1  1001 ? 11.535  34.936  92.336  1.00 14.59 ? 999  ASN B C     1 
ATOM   16381 O  O     . ASN B  1  1001 ? 10.540  35.562  91.958  1.00 17.22 ? 999  ASN B O     1 
ATOM   16382 C  CB    . ASN B  1  1001 ? 11.793  32.478  92.975  1.00 15.23 ? 999  ASN B CB    1 
ATOM   16383 C  CG    . ASN B  1  1001 ? 10.987  32.030  91.770  1.00 18.75 ? 999  ASN B CG    1 
ATOM   16384 O  OD1   . ASN B  1  1001 ? 10.779  32.779  90.830  1.00 19.22 ? 999  ASN B OD1   1 
ATOM   16385 N  ND2   . ASN B  1  1001 ? 10.557  30.771  91.789  1.00 23.98 ? 999  ASN B ND2   1 
ATOM   16386 N  N     . ILE B  1  1002 ? 12.745  35.144  91.823  1.00 15.28 ? 1000 ILE B N     1 
ATOM   16387 C  CA    . ILE B  1  1002 ? 12.960  36.205  90.850  1.00 13.62 ? 1000 ILE B CA    1 
ATOM   16388 C  C     . ILE B  1  1002 ? 13.269  35.654  89.460  1.00 15.95 ? 1000 ILE B C     1 
ATOM   16389 O  O     . ILE B  1  1002 ? 13.764  36.395  88.608  1.00 16.72 ? 1000 ILE B O     1 
ATOM   16390 C  CB    . ILE B  1  1002 ? 14.041  37.190  91.314  1.00 15.64 ? 1000 ILE B CB    1 
ATOM   16391 C  CG1   . ILE B  1  1002 ? 15.443  36.568  91.351  1.00 14.44 ? 1000 ILE B CG1   1 
ATOM   16392 C  CG2   . ILE B  1  1002 ? 13.658  37.746  92.688  1.00 16.84 ? 1000 ILE B CG2   1 
ATOM   16393 C  CD1   . ILE B  1  1002 ? 16.517  37.598  91.646  1.00 15.09 ? 1000 ILE B CD1   1 
ATOM   16394 N  N     . ILE B  1  1003 ? 12.979  34.376  89.208  1.00 15.94 ? 1001 ILE B N     1 
ATOM   16395 C  CA    . ILE B  1  1003 ? 13.358  33.732  87.956  1.00 15.63 ? 1001 ILE B CA    1 
ATOM   16396 C  C     . ILE B  1  1003 ? 12.121  33.204  87.237  1.00 18.84 ? 1001 ILE B C     1 
ATOM   16397 O  O     . ILE B  1  1003 ? 11.008  33.217  87.756  1.00 19.09 ? 1001 ILE B O     1 
ATOM   16398 C  CB    . ILE B  1  1003 ? 14.379  32.599  88.169  1.00 17.49 ? 1001 ILE B CB    1 
ATOM   16399 C  CG1   . ILE B  1  1003 ? 13.806  31.484  89.047  1.00 19.73 ? 1001 ILE B CG1   1 
ATOM   16400 C  CG2   . ILE B  1  1003 ? 15.647  33.165  88.760  1.00 16.69 ? 1001 ILE B CG2   1 
ATOM   16401 C  CD1   . ILE B  1  1003 ? 14.670  30.213  88.975  1.00 22.08 ? 1001 ILE B CD1   1 
ATOM   16402 N  N     . GLY B  1  1004 ? 12.341  32.738  86.014  1.00 20.86 ? 1002 GLY B N     1 
ATOM   16403 C  CA    . GLY B  1  1004 ? 11.268  32.124  85.252  1.00 17.34 ? 1002 GLY B CA    1 
ATOM   16404 C  C     . GLY B  1  1004 ? 10.205  33.095  84.791  1.00 18.90 ? 1002 GLY B C     1 
ATOM   16405 O  O     . GLY B  1  1004 ? 9.014   32.777  84.867  1.00 20.01 ? 1002 GLY B O     1 
ATOM   16406 N  N     . ALA B  1  1005 ? 10.605  34.288  84.348  1.00 18.80 ? 1003 ALA B N     1 
ATOM   16407 C  CA    . ALA B  1  1005 ? 9.658   35.249  83.811  1.00 17.88 ? 1003 ALA B CA    1 
ATOM   16408 C  C     . ALA B  1  1005 ? 8.828   34.607  82.709  1.00 20.96 ? 1003 ALA B C     1 
ATOM   16409 O  O     . ALA B  1  1005 ? 9.349   33.857  81.878  1.00 23.39 ? 1003 ALA B O     1 
ATOM   16410 C  CB    . ALA B  1  1005 ? 10.391  36.473  83.262  1.00 18.95 ? 1003 ALA B CB    1 
ATOM   16411 N  N     . VAL B  1  1006 ? 7.537   34.906  82.718  1.00 15.54 ? 1004 VAL B N     1 
ATOM   16412 C  CA    . VAL B  1  1006 ? 6.559   34.263  81.853  1.00 17.17 ? 1004 VAL B CA    1 
ATOM   16413 C  C     . VAL B  1  1006 ? 6.140   35.253  80.783  1.00 17.50 ? 1004 VAL B C     1 
ATOM   16414 O  O     . VAL B  1  1006 ? 5.712   36.371  81.093  1.00 16.47 ? 1004 VAL B O     1 
ATOM   16415 C  CB    . VAL B  1  1006 ? 5.344   33.776  82.658  1.00 19.85 ? 1004 VAL B CB    1 
ATOM   16416 C  CG1   . VAL B  1  1006 ? 4.241   33.266  81.732  1.00 19.26 ? 1004 VAL B CG1   1 
ATOM   16417 C  CG2   . VAL B  1  1006 ? 5.786   32.681  83.612  1.00 20.04 ? 1004 VAL B CG2   1 
ATOM   16418 N  N     . VAL B  1  1007 ? 6.232   34.815  79.526  1.00 15.77 ? 1005 VAL B N     1 
ATOM   16419 C  CA    . VAL B  1  1007 ? 5.860   35.636  78.382  1.00 15.75 ? 1005 VAL B CA    1 
ATOM   16420 C  C     . VAL B  1  1007 ? 4.488   36.261  78.582  1.00 15.90 ? 1005 VAL B C     1 
ATOM   16421 O  O     . VAL B  1  1007 ? 3.509   35.578  78.886  1.00 16.34 ? 1005 VAL B O     1 
ATOM   16422 C  CB    . VAL B  1  1007 ? 5.883   34.767  77.117  1.00 15.75 ? 1005 VAL B CB    1 
ATOM   16423 C  CG1   . VAL B  1  1007 ? 5.399   35.574  75.925  1.00 15.97 ? 1005 VAL B CG1   1 
ATOM   16424 C  CG2   . VAL B  1  1007 ? 7.282   34.273  76.874  1.00 18.67 ? 1005 VAL B CG2   1 
ATOM   16425 N  N     . GLY B  1  1008 ? 4.408   37.572  78.367  1.00 15.50 ? 1006 GLY B N     1 
ATOM   16426 C  CA    . GLY B  1  1008 ? 3.152   38.293  78.426  1.00 15.44 ? 1006 GLY B CA    1 
ATOM   16427 C  C     . GLY B  1  1008 ? 2.538   38.423  79.803  1.00 14.46 ? 1006 GLY B C     1 
ATOM   16428 O  O     . GLY B  1  1008 ? 1.465   39.017  79.934  1.00 20.74 ? 1006 GLY B O     1 
ATOM   16429 N  N     . VAL B  1  1009 ? 3.172   37.868  80.819  1.00 15.49 ? 1007 VAL B N     1 
ATOM   16430 C  CA    . VAL B  1  1009 ? 2.725   37.973  82.197  1.00 15.84 ? 1007 VAL B CA    1 
ATOM   16431 C  C     . VAL B  1  1009 ? 3.726   38.768  83.019  1.00 14.64 ? 1007 VAL B C     1 
ATOM   16432 O  O     . VAL B  1  1009 ? 3.357   39.700  83.736  1.00 16.33 ? 1007 VAL B O     1 
ATOM   16433 C  CB    . VAL B  1  1009 ? 2.500   36.575  82.811  1.00 17.82 ? 1007 VAL B CB    1 
ATOM   16434 C  CG1   . VAL B  1  1009 ? 1.963   36.721  84.236  1.00 17.04 ? 1007 VAL B CG1   1 
ATOM   16435 C  CG2   . VAL B  1  1009 ? 1.528   35.771  81.945  1.00 19.18 ? 1007 VAL B CG2   1 
ATOM   16436 N  N     . GLN B  1  1010 ? 5.008   38.418  82.906  1.00 14.70 ? 1008 GLN B N     1 
ATOM   16437 C  CA    . GLN B  1  1010 ? 6.124   39.288  83.282  1.00 14.84 ? 1008 GLN B CA    1 
ATOM   16438 C  C     . GLN B  1  1010 ? 6.957   39.546  82.034  1.00 15.61 ? 1008 GLN B C     1 
ATOM   16439 O  O     . GLN B  1  1010 ? 8.004   38.913  81.841  1.00 17.13 ? 1008 GLN B O     1 
ATOM   16440 C  CB    . GLN B  1  1010 ? 7.000   38.685  84.380  1.00 17.23 ? 1008 GLN B CB    1 
ATOM   16441 C  CG    . GLN B  1  1010 ? 6.258   38.326  85.644  1.00 16.08 ? 1008 GLN B CG    1 
ATOM   16442 C  CD    . GLN B  1  1010 ? 5.865   36.875  85.672  1.00 17.35 ? 1008 GLN B CD    1 
ATOM   16443 O  OE1   . GLN B  1  1010 ? 6.553   36.019  85.105  1.00 18.63 ? 1008 GLN B OE1   1 
ATOM   16444 N  NE2   . GLN B  1  1010 ? 4.773   36.578  86.357  1.00 17.21 ? 1008 GLN B NE2   1 
ATOM   16445 N  N     . PRO B  1  1011 ? 6.513   40.459  81.156  1.00 16.64 ? 1009 PRO B N     1 
ATOM   16446 C  CA    . PRO B  1  1011 ? 7.405   40.957  80.096  1.00 17.29 ? 1009 PRO B CA    1 
ATOM   16447 C  C     . PRO B  1  1011 ? 8.788   41.219  80.663  1.00 15.65 ? 1009 PRO B C     1 
ATOM   16448 O  O     . PRO B  1  1011 ? 8.939   41.857  81.716  1.00 15.02 ? 1009 PRO B O     1 
ATOM   16449 C  CB    . PRO B  1  1011 ? 6.724   42.253  79.641  1.00 15.58 ? 1009 PRO B CB    1 
ATOM   16450 C  CG    . PRO B  1  1011 ? 5.281   42.040  79.953  1.00 17.69 ? 1009 PRO B CG    1 
ATOM   16451 C  CD    . PRO B  1  1011 ? 5.283   41.261  81.265  1.00 17.39 ? 1009 PRO B CD    1 
ATOM   16452 N  N     . PHE B  1  1012 ? 9.809   40.714  79.990  1.00 14.23 ? 1010 PHE B N     1 
ATOM   16453 C  CA    . PHE B  1  1012 ? 11.108  40.561  80.614  1.00 15.56 ? 1010 PHE B CA    1 
ATOM   16454 C  C     . PHE B  1  1012 ? 12.140  41.477  79.979  1.00 15.99 ? 1010 PHE B C     1 
ATOM   16455 O  O     . PHE B  1  1012 ? 12.302  41.495  78.757  1.00 15.78 ? 1010 PHE B O     1 
ATOM   16456 C  CB    . PHE B  1  1012 ? 11.585  39.111  80.529  1.00 17.07 ? 1010 PHE B CB    1 
ATOM   16457 C  CG    . PHE B  1  1012 ? 12.855  38.869  81.278  1.00 14.96 ? 1010 PHE B CG    1 
ATOM   16458 C  CD1   . PHE B  1  1012 ? 12.837  38.740  82.659  1.00 17.70 ? 1010 PHE B CD1   1 
ATOM   16459 C  CD2   . PHE B  1  1012 ? 14.074  38.812  80.613  1.00 17.12 ? 1010 PHE B CD2   1 
ATOM   16460 C  CE1   . PHE B  1  1012 ? 14.012  38.517  83.367  1.00 15.86 ? 1010 PHE B CE1   1 
ATOM   16461 C  CE2   . PHE B  1  1012 ? 15.262  38.594  81.319  1.00 20.85 ? 1010 PHE B CE2   1 
ATOM   16462 C  CZ    . PHE B  1  1012 ? 15.226  38.448  82.694  1.00 17.95 ? 1010 PHE B CZ    1 
ATOM   16463 N  N     . GLY B  1  1013 ? 12.866  42.194  80.809  1.00 15.43 ? 1011 GLY B N     1 
ATOM   16464 C  CA    . GLY B  1  1013 ? 13.992  42.961  80.317  1.00 15.54 ? 1011 GLY B CA    1 
ATOM   16465 C  C     . GLY B  1  1013 ? 14.206  44.125  81.244  1.00 17.18 ? 1011 GLY B C     1 
ATOM   16466 O  O     . GLY B  1  1013 ? 13.295  44.603  81.908  1.00 16.55 ? 1011 GLY B O     1 
ATOM   16467 N  N     . GLY B  1  1014 ? 15.436  44.604  81.262  1.00 18.73 ? 1012 GLY B N     1 
ATOM   16468 C  CA    . GLY B  1  1014 ? 15.776  45.675  82.165  1.00 19.02 ? 1012 GLY B CA    1 
ATOM   16469 C  C     . GLY B  1  1014 ? 16.394  46.865  81.485  1.00 22.52 ? 1012 GLY B C     1 
ATOM   16470 O  O     . GLY B  1  1014 ? 16.289  47.046  80.271  1.00 26.86 ? 1012 GLY B O     1 
ATOM   16471 N  N     . ARG B  1  1015 ? 17.064  47.672  82.288  1.00 20.30 ? 1013 ARG B N     1 
ATOM   16472 C  CA    . ARG B  1  1015 ? 17.553  48.979  81.914  1.00 24.00 ? 1013 ARG B CA    1 
ATOM   16473 C  C     . ARG B  1  1015 ? 19.025  49.057  82.280  1.00 21.60 ? 1013 ARG B C     1 
ATOM   16474 O  O     . ARG B  1  1015 ? 19.597  48.111  82.818  1.00 18.66 ? 1013 ARG B O     1 
ATOM   16475 C  CB    . ARG B  1  1015 ? 16.752  50.069  82.637  1.00 22.42 ? 1013 ARG B CB    1 
ATOM   16476 C  CG    . ARG B  1  1015 ? 16.730  49.873  84.150  1.00 24.28 ? 1013 ARG B CG    1 
ATOM   16477 C  CD    . ARG B  1  1015 ? 16.693  51.198  84.903  1.00 32.13 ? 1013 ARG B CD    1 
ATOM   16478 N  NE    . ARG B  1  1015 ? 17.993  51.867  84.878  1.00 31.41 ? 1013 ARG B NE    1 
ATOM   16479 C  CZ    . ARG B  1  1015 ? 19.016  51.552  85.661  1.00 28.83 ? 1013 ARG B CZ    1 
ATOM   16480 N  NH1   . ARG B  1  1015 ? 18.935  50.571  86.552  1.00 27.14 ? 1013 ARG B NH1   1 
ATOM   16481 N  NH2   . ARG B  1  1015 ? 20.152  52.234  85.546  1.00 33.72 ? 1013 ARG B NH2   1 
ATOM   16482 N  N     . GLY B  1  1016 ? 19.638  50.203  82.005  1.00 20.21 ? 1014 GLY B N     1 
ATOM   16483 C  CA    . GLY B  1  1016 ? 21.044  50.342  82.336  1.00 19.83 ? 1014 GLY B CA    1 
ATOM   16484 C  C     . GLY B  1  1016 ? 21.886  49.345  81.569  1.00 19.87 ? 1014 GLY B C     1 
ATOM   16485 O  O     . GLY B  1  1016 ? 21.671  49.108  80.374  1.00 22.07 ? 1014 GLY B O     1 
ATOM   16486 N  N     . LEU B  1  1017 ? 22.847  48.737  82.267  1.00 20.30 ? 1015 LEU B N     1 
ATOM   16487 C  CA    . LEU B  1  1017 ? 23.705  47.713  81.688  1.00 20.31 ? 1015 LEU B CA    1 
ATOM   16488 C  C     . LEU B  1  1017 ? 22.954  46.435  81.361  1.00 19.85 ? 1015 LEU B C     1 
ATOM   16489 O  O     . LEU B  1  1017 ? 23.546  45.531  80.768  1.00 20.02 ? 1015 LEU B O     1 
ATOM   16490 C  CB    . LEU B  1  1017 ? 24.859  47.378  82.641  1.00 20.07 ? 1015 LEU B CB    1 
ATOM   16491 C  CG    . LEU B  1  1017 ? 25.834  48.514  82.966  1.00 23.56 ? 1015 LEU B CG    1 
ATOM   16492 C  CD1   . LEU B  1  1017 ? 26.832  48.047  84.019  1.00 24.11 ? 1015 LEU B CD1   1 
ATOM   16493 C  CD2   . LEU B  1  1017 ? 26.568  48.963  81.710  1.00 24.94 ? 1015 LEU B CD2   1 
ATOM   16494 N  N     . SER B  1  1018 ? 21.684  46.331  81.742  1.00 17.34 ? 1016 SER B N     1 
ATOM   16495 C  CA    . SER B  1  1018 ? 20.907  45.122  81.502  1.00 17.67 ? 1016 SER B CA    1 
ATOM   16496 C  C     . SER B  1  1018 ? 20.170  45.127  80.178  1.00 17.06 ? 1016 SER B C     1 
ATOM   16497 O  O     . SER B  1  1018 ? 19.647  44.087  79.778  1.00 19.60 ? 1016 SER B O     1 
ATOM   16498 C  CB    . SER B  1  1018 ? 19.889  44.918  82.630  1.00 19.86 ? 1016 SER B CB    1 
ATOM   16499 O  OG    . SER B  1  1018 ? 20.616  44.693  83.824  1.00 19.72 ? 1016 SER B OG    1 
ATOM   16500 N  N     . GLY B  1  1019 ? 20.075  46.255  79.503  1.00 19.48 ? 1017 GLY B N     1 
ATOM   16501 C  CA    . GLY B  1  1019 ? 19.382  46.154  78.246  1.00 26.48 ? 1017 GLY B CA    1 
ATOM   16502 C  C     . GLY B  1  1019 ? 19.024  47.464  77.608  1.00 19.61 ? 1017 GLY B C     1 
ATOM   16503 O  O     . GLY B  1  1019 ? 19.003  48.505  78.261  1.00 20.14 ? 1017 GLY B O     1 
ATOM   16504 N  N     . THR B  1  1020 ? 18.731  47.400  76.310  1.00 19.17 ? 1018 THR B N     1 
ATOM   16505 C  CA    . THR B  1  1020 ? 18.146  48.516  75.592  1.00 19.54 ? 1018 THR B CA    1 
ATOM   16506 C  C     . THR B  1  1020 ? 16.638  48.538  75.696  1.00 20.74 ? 1018 THR B C     1 
ATOM   16507 O  O     . THR B  1  1020 ? 16.024  49.601  75.542  1.00 20.83 ? 1018 THR B O     1 
ATOM   16508 C  CB    . THR B  1  1020 ? 18.510  48.424  74.114  1.00 19.34 ? 1018 THR B CB    1 
ATOM   16509 O  OG1   . THR B  1  1020 ? 18.035  47.163  73.614  1.00 17.97 ? 1018 THR B OG1   1 
ATOM   16510 C  CG2   . THR B  1  1020 ? 20.015  48.489  73.936  1.00 18.85 ? 1018 THR B CG2   1 
ATOM   16511 N  N     . GLY B  1  1021 ? 16.029  47.387  75.940  1.00 20.17 ? 1019 GLY B N     1 
ATOM   16512 C  CA    . GLY B  1  1021 ? 14.626  47.243  75.677  1.00 19.98 ? 1019 GLY B CA    1 
ATOM   16513 C  C     . GLY B  1  1021 ? 14.379  47.290  74.184  1.00 20.09 ? 1019 GLY B C     1 
ATOM   16514 O  O     . GLY B  1  1021 ? 15.298  47.456  73.383  1.00 18.75 ? 1019 GLY B O     1 
ATOM   16515 N  N     . PRO B  1  1022 ? 13.135  47.131  73.783  1.00 16.75 ? 1020 PRO B N     1 
ATOM   16516 C  CA    . PRO B  1  1022 ? 11.956  46.902  74.619  1.00 17.51 ? 1020 PRO B CA    1 
ATOM   16517 C  C     . PRO B  1  1022 ? 11.966  45.481  75.174  1.00 18.78 ? 1020 PRO B C     1 
ATOM   16518 O  O     . PRO B  1  1022 ? 12.741  44.613  74.745  1.00 18.54 ? 1020 PRO B O     1 
ATOM   16519 C  CB    . PRO B  1  1022 ? 10.801  47.144  73.642  1.00 19.08 ? 1020 PRO B CB    1 
ATOM   16520 C  CG    . PRO B  1  1022 ? 11.351  46.673  72.329  1.00 20.10 ? 1020 PRO B CG    1 
ATOM   16521 C  CD    . PRO B  1  1022 ? 12.793  47.131  72.348  1.00 21.53 ? 1020 PRO B CD    1 
ATOM   16522 N  N     . LYS B  1  1023 ? 11.092  45.234  76.143  1.00 17.22 ? 1021 LYS B N     1 
ATOM   16523 C  CA    . LYS B  1  1023 ? 11.041  43.933  76.798  1.00 16.98 ? 1021 LYS B CA    1 
ATOM   16524 C  C     . LYS B  1  1023 ? 10.589  42.832  75.851  1.00 16.84 ? 1021 LYS B C     1 
ATOM   16525 O  O     . LYS B  1  1023 ? 9.573   42.961  75.165  1.00 16.96 ? 1021 LYS B O     1 
ATOM   16526 C  CB    . LYS B  1  1023 ? 10.077  43.967  77.971  1.00 15.30 ? 1021 LYS B CB    1 
ATOM   16527 C  CG    . LYS B  1  1023 ? 10.553  44.720  79.201  1.00 15.86 ? 1021 LYS B CG    1 
ATOM   16528 C  CD    . LYS B  1  1023 ? 9.396   44.766  80.177  1.00 15.58 ? 1021 LYS B CD    1 
ATOM   16529 C  CE    . LYS B  1  1023 ? 9.773   45.254  81.579  1.00 16.44 ? 1021 LYS B CE    1 
ATOM   16530 N  NZ    . LYS B  1  1023 ? 10.531  44.187  82.311  1.00 15.80 ? 1021 LYS B NZ    1 
ATOM   16531 N  N     . ALA B  1  1024 ? 11.311  41.719  75.890  1.00 18.43 ? 1022 ALA B N     1 
ATOM   16532 C  CA    . ALA B  1  1024 ? 10.845  40.493  75.264  1.00 17.92 ? 1022 ALA B CA    1 
ATOM   16533 C  C     . ALA B  1  1024 ? 9.582   40.001  75.954  1.00 16.68 ? 1022 ALA B C     1 
ATOM   16534 O  O     . ALA B  1  1024 ? 9.401   40.172  77.161  1.00 18.31 ? 1022 ALA B O     1 
ATOM   16535 C  CB    . ALA B  1  1024 ? 11.946  39.437  75.349  1.00 17.81 ? 1022 ALA B CB    1 
ATOM   16536 N  N     . GLY B  1  1025 ? 8.674   39.425  75.175  1.00 13.12 ? 1023 GLY B N     1 
ATOM   16537 C  CA    . GLY B  1  1025 ? 7.451   38.948  75.773  1.00 13.68 ? 1023 GLY B CA    1 
ATOM   16538 C  C     . GLY B  1  1025 ? 6.553   40.060  76.255  1.00 14.54 ? 1023 GLY B C     1 
ATOM   16539 O  O     . GLY B  1  1025 ? 5.699   39.831  77.107  1.00 15.77 ? 1023 GLY B O     1 
ATOM   16540 N  N     . GLY B  1  1026 ? 6.721   41.261  75.704  1.00 15.61 ? 1024 GLY B N     1 
ATOM   16541 C  CA    . GLY B  1  1026 ? 5.899   42.398  76.043  1.00 15.14 ? 1024 GLY B CA    1 
ATOM   16542 C  C     . GLY B  1  1026 ? 5.424   43.089  74.787  1.00 14.90 ? 1024 GLY B C     1 
ATOM   16543 O  O     . GLY B  1  1026 ? 5.843   42.769  73.677  1.00 15.33 ? 1024 GLY B O     1 
ATOM   16544 N  N     . PRO B  1  1027 ? 4.540   44.071  74.956  1.00 15.12 ? 1025 PRO B N     1 
ATOM   16545 C  CA    . PRO B  1  1027 ? 3.786   44.603  73.815  1.00 13.66 ? 1025 PRO B CA    1 
ATOM   16546 C  C     . PRO B  1  1027 ? 4.536   45.623  72.989  1.00 16.12 ? 1025 PRO B C     1 
ATOM   16547 O  O     . PRO B  1  1027 ? 4.037   45.996  71.926  1.00 15.92 ? 1025 PRO B O     1 
ATOM   16548 C  CB    . PRO B  1  1027 ? 2.563   45.241  74.477  1.00 18.01 ? 1025 PRO B CB    1 
ATOM   16549 C  CG    . PRO B  1  1027 ? 3.061   45.624  75.845  1.00 17.79 ? 1025 PRO B CG    1 
ATOM   16550 C  CD    . PRO B  1  1027 ? 4.028   44.547  76.248  1.00 16.79 ? 1025 PRO B CD    1 
ATOM   16551 N  N     . LEU B  1  1028 ? 5.684   46.103  73.439  1.00 17.16 ? 1026 LEU B N     1 
ATOM   16552 C  CA    . LEU B  1  1028 ? 6.459   47.039  72.634  1.00 15.57 ? 1026 LEU B CA    1 
ATOM   16553 C  C     . LEU B  1  1028 ? 7.430   46.355  71.699  1.00 16.60 ? 1026 LEU B C     1 
ATOM   16554 O  O     . LEU B  1  1028 ? 8.036   47.032  70.866  1.00 18.88 ? 1026 LEU B O     1 
ATOM   16555 C  CB    . LEU B  1  1028 ? 7.249   47.985  73.534  1.00 15.28 ? 1026 LEU B CB    1 
ATOM   16556 C  CG    . LEU B  1  1028 ? 6.375   48.850  74.426  1.00 17.74 ? 1026 LEU B CG    1 
ATOM   16557 C  CD1   . LEU B  1  1028 ? 7.258   49.780  75.235  1.00 17.88 ? 1026 LEU B CD1   1 
ATOM   16558 C  CD2   . LEU B  1  1028 ? 5.387   49.628  73.619  1.00 21.82 ? 1026 LEU B CD2   1 
ATOM   16559 N  N     . TYR B  1  1029 ? 7.612   45.046  71.837  1.00 14.61 ? 1027 TYR B N     1 
ATOM   16560 C  CA    . TYR B  1  1029 ? 8.744   44.368  71.212  1.00 14.91 ? 1027 TYR B CA    1 
ATOM   16561 C  C     . TYR B  1  1029 ? 8.654   44.396  69.694  1.00 14.96 ? 1027 TYR B C     1 
ATOM   16562 O  O     . TYR B  1  1029 ? 9.630   44.726  69.015  1.00 15.62 ? 1027 TYR B O     1 
ATOM   16563 C  CB    . TYR B  1  1029 ? 8.771   42.935  71.702  1.00 16.76 ? 1027 TYR B CB    1 
ATOM   16564 C  CG    . TYR B  1  1029 ? 10.050  42.171  71.581  1.00 17.33 ? 1027 TYR B CG    1 
ATOM   16565 C  CD1   . TYR B  1  1029 ? 11.158  42.486  72.363  1.00 15.73 ? 1027 TYR B CD1   1 
ATOM   16566 C  CD2   . TYR B  1  1029 ? 10.121  41.063  70.756  1.00 17.60 ? 1027 TYR B CD2   1 
ATOM   16567 C  CE1   . TYR B  1  1029 ? 12.318  41.729  72.295  1.00 15.27 ? 1027 TYR B CE1   1 
ATOM   16568 C  CE2   . TYR B  1  1029 ? 11.262  40.291  70.693  1.00 16.35 ? 1027 TYR B CE2   1 
ATOM   16569 C  CZ    . TYR B  1  1029 ? 12.357  40.629  71.452  1.00 17.78 ? 1027 TYR B CZ    1 
ATOM   16570 O  OH    . TYR B  1  1029 ? 13.479  39.837  71.392  1.00 19.48 ? 1027 TYR B OH    1 
ATOM   16571 N  N     . LEU B  1  1030 ? 7.505   43.981  69.146  1.00 16.03 ? 1028 LEU B N     1 
ATOM   16572 C  CA    . LEU B  1  1030 ? 7.404   43.864  67.695  1.00 15.59 ? 1028 LEU B CA    1 
ATOM   16573 C  C     . LEU B  1  1030 ? 7.594   45.208  67.019  1.00 17.32 ? 1028 LEU B C     1 
ATOM   16574 O  O     . LEU B  1  1030 ? 8.148   45.272  65.920  1.00 16.96 ? 1028 LEU B O     1 
ATOM   16575 C  CB    . LEU B  1  1030 ? 6.065   43.256  67.290  1.00 18.26 ? 1028 LEU B CB    1 
ATOM   16576 C  CG    . LEU B  1  1030 ? 5.831   41.811  67.727  1.00 19.00 ? 1028 LEU B CG    1 
ATOM   16577 C  CD1   . LEU B  1  1030 ? 4.508   41.320  67.144  1.00 20.46 ? 1028 LEU B CD1   1 
ATOM   16578 C  CD2   . LEU B  1  1030 ? 6.990   40.915  67.274  1.00 18.40 ? 1028 LEU B CD2   1 
ATOM   16579 N  N     . GLY B  1  1031 ? 7.178   46.290  67.670  1.00 17.64 ? 1029 GLY B N     1 
ATOM   16580 C  CA    . GLY B  1  1031 ? 7.298   47.601  67.057  1.00 18.97 ? 1029 GLY B CA    1 
ATOM   16581 C  C     . GLY B  1  1031 ? 8.717   48.040  66.774  1.00 18.50 ? 1029 GLY B C     1 
ATOM   16582 O  O     . GLY B  1  1031 ? 8.924   48.947  65.964  1.00 19.07 ? 1029 GLY B O     1 
ATOM   16583 N  N     . ARG B  1  1032 ? 9.705   47.435  67.434  1.00 15.58 ? 1030 ARG B N     1 
ATOM   16584 C  CA    . ARG B  1  1032 ? 11.101  47.728  67.165  1.00 16.23 ? 1030 ARG B CA    1 
ATOM   16585 C  C     . ARG B  1  1032 ? 11.586  47.069  65.886  1.00 16.96 ? 1030 ARG B C     1 
ATOM   16586 O  O     . ARG B  1  1032 ? 12.650  47.427  65.366  1.00 18.75 ? 1030 ARG B O     1 
ATOM   16587 C  CB    . ARG B  1  1032 ? 11.946  47.252  68.347  1.00 19.43 ? 1030 ARG B CB    1 
ATOM   16588 C  CG    . ARG B  1  1032 ? 13.352  47.767  68.349  1.00 20.25 ? 1030 ARG B CG    1 
ATOM   16589 C  CD    . ARG B  1  1032 ? 13.382  49.267  68.610  1.00 22.11 ? 1030 ARG B CD    1 
ATOM   16590 N  NE    . ARG B  1  1032 ? 14.754  49.704  68.800  1.00 21.69 ? 1030 ARG B NE    1 
ATOM   16591 C  CZ    . ARG B  1  1032 ? 15.367  50.634  68.079  1.00 22.80 ? 1030 ARG B CZ    1 
ATOM   16592 N  NH1   . ARG B  1  1032 ? 14.740  51.288  67.109  1.00 24.95 ? 1030 ARG B NH1   1 
ATOM   16593 N  NH2   . ARG B  1  1032 ? 16.636  50.924  68.348  1.00 23.78 ? 1030 ARG B NH2   1 
ATOM   16594 N  N     . LEU B  1  1033 ? 10.815  46.126  65.358  1.00 17.44 ? 1031 LEU B N     1 
ATOM   16595 C  CA    . LEU B  1  1033 ? 11.259  45.288  64.259  1.00 17.42 ? 1031 LEU B CA    1 
ATOM   16596 C  C     . LEU B  1  1033 ? 10.571  45.657  62.957  1.00 17.87 ? 1031 LEU B C     1 
ATOM   16597 O  O     . LEU B  1  1033 ? 10.600  44.880  61.998  1.00 18.53 ? 1031 LEU B O     1 
ATOM   16598 C  CB    . LEU B  1  1033 ? 11.010  43.825  64.610  1.00 16.32 ? 1031 LEU B CB    1 
ATOM   16599 C  CG    . LEU B  1  1033 ? 11.618  43.424  65.963  1.00 16.84 ? 1031 LEU B CG    1 
ATOM   16600 C  CD1   . LEU B  1  1033 ? 11.238  41.989  66.316  1.00 19.33 ? 1031 LEU B CD1   1 
ATOM   16601 C  CD2   . LEU B  1  1033 ? 13.130  43.593  65.982  1.00 19.94 ? 1031 LEU B CD2   1 
ATOM   16602 N  N     . VAL B  1  1034 ? 9.931   46.822  62.922  1.00 16.74 ? 1032 VAL B N     1 
ATOM   16603 C  CA    . VAL B  1  1034 ? 9.329   47.386  61.724  1.00 19.55 ? 1032 VAL B CA    1 
ATOM   16604 C  C     . VAL B  1  1034 ? 9.788   48.837  61.637  1.00 21.82 ? 1032 VAL B C     1 
ATOM   16605 O  O     . VAL B  1  1034 ? 10.271  49.412  62.613  1.00 22.20 ? 1032 VAL B O     1 
ATOM   16606 C  CB    . VAL B  1  1034 ? 7.792   47.283  61.748  1.00 17.43 ? 1032 VAL B CB    1 
ATOM   16607 C  CG1   . VAL B  1  1034 ? 7.344   45.822  61.608  1.00 20.80 ? 1032 VAL B CG1   1 
ATOM   16608 C  CG2   . VAL B  1  1034 ? 7.244   47.871  63.052  1.00 19.17 ? 1032 VAL B CG2   1 
ATOM   16609 N  N     . THR B  1  1035 ? 9.673   49.424  60.442  1.00 21.23 ? 1033 THR B N     1 
ATOM   16610 C  CA    . THR B  1  1035 ? 10.188  50.781  60.283  1.00 23.28 ? 1033 THR B CA    1 
ATOM   16611 C  C     . THR B  1  1035 ? 9.242   51.833  60.830  1.00 23.65 ? 1033 THR B C     1 
ATOM   16612 O  O     . THR B  1  1035 ? 9.681   52.951  61.125  1.00 28.72 ? 1033 THR B O     1 
ATOM   16613 C  CB    . THR B  1  1035 ? 10.497  51.080  58.816  1.00 25.29 ? 1033 THR B CB    1 
ATOM   16614 O  OG1   . THR B  1  1035 ? 9.434   50.595  57.992  1.00 32.18 ? 1033 THR B OG1   1 
ATOM   16615 C  CG2   . THR B  1  1035 ? 11.801  50.400  58.416  1.00 32.51 ? 1033 THR B CG2   1 
ATOM   16616 N  N     . THR B  1  1036 ? 7.968   51.497  60.991  1.00 20.49 ? 1034 THR B N     1 
ATOM   16617 C  CA    . THR B  1  1036 ? 6.996   52.367  61.635  1.00 21.23 ? 1034 THR B CA    1 
ATOM   16618 C  C     . THR B  1  1036 ? 6.303   51.553  62.712  1.00 21.11 ? 1034 THR B C     1 
ATOM   16619 O  O     . THR B  1  1036 ? 5.643   50.557  62.405  1.00 20.21 ? 1034 THR B O     1 
ATOM   16620 C  CB    . THR B  1  1036 ? 5.979   52.894  60.626  1.00 25.76 ? 1034 THR B CB    1 
ATOM   16621 O  OG1   . THR B  1  1036 ? 6.674   53.518  59.542  1.00 34.38 ? 1034 THR B OG1   1 
ATOM   16622 C  CG2   . THR B  1  1036 ? 5.053   53.915  61.284  1.00 29.63 ? 1034 THR B CG2   1 
ATOM   16623 N  N     . ALA B  1  1037 ? 6.454   51.967  63.968  1.00 20.16 ? 1035 ALA B N     1 
ATOM   16624 C  CA    . ALA B  1  1037 ? 5.907   51.172  65.059  1.00 21.43 ? 1035 ALA B CA    1 
ATOM   16625 C  C     . ALA B  1  1037 ? 4.386   51.310  65.115  1.00 19.74 ? 1035 ALA B C     1 
ATOM   16626 O  O     . ALA B  1  1037 ? 3.846   52.416  64.968  1.00 21.00 ? 1035 ALA B O     1 
ATOM   16627 C  CB    . ALA B  1  1037 ? 6.512   51.600  66.398  1.00 21.95 ? 1035 ALA B CB    1 
ATOM   16628 N  N     . PRO B  1  1038 ? 3.671   50.218  65.340  1.00 17.51 ? 1036 PRO B N     1 
ATOM   16629 C  CA    . PRO B  1  1038 ? 2.231   50.302  65.584  1.00 19.75 ? 1036 PRO B CA    1 
ATOM   16630 C  C     . PRO B  1  1038 ? 1.942   50.747  67.010  1.00 18.41 ? 1036 PRO B C     1 
ATOM   16631 O  O     . PRO B  1  1038 ? 2.819   50.816  67.866  1.00 18.20 ? 1036 PRO B O     1 
ATOM   16632 C  CB    . PRO B  1  1038 ? 1.751   48.865  65.367  1.00 18.62 ? 1036 PRO B CB    1 
ATOM   16633 C  CG    . PRO B  1  1038 ? 2.935   48.046  65.830  1.00 20.14 ? 1036 PRO B CG    1 
ATOM   16634 C  CD    . PRO B  1  1038 ? 4.163   48.827  65.381  1.00 18.85 ? 1036 PRO B CD    1 
ATOM   16635 N  N     . VAL B  1  1039 ? 0.670   51.030  67.253  1.00 19.60 ? 1037 VAL B N     1 
ATOM   16636 C  CA    . VAL B  1  1039 ? 0.193   51.299  68.608  1.00 17.59 ? 1037 VAL B CA    1 
ATOM   16637 C  C     . VAL B  1  1039 ? -0.075  49.949  69.257  1.00 18.28 ? 1037 VAL B C     1 
ATOM   16638 O  O     . VAL B  1  1039 ? -0.975  49.225  68.821  1.00 17.95 ? 1037 VAL B O     1 
ATOM   16639 C  CB    . VAL B  1  1039 ? -1.072  52.169  68.594  1.00 19.92 ? 1037 VAL B CB    1 
ATOM   16640 C  CG1   . VAL B  1  1039 ? -1.508  52.463  70.034  1.00 21.67 ? 1037 VAL B CG1   1 
ATOM   16641 C  CG2   . VAL B  1  1039 ? -0.815  53.460  67.835  1.00 21.01 ? 1037 VAL B CG2   1 
ATOM   16642 N  N     . PRO B  1  1040 ? 0.668   49.563  70.285  1.00 17.30 ? 1038 PRO B N     1 
ATOM   16643 C  CA    . PRO B  1  1040 ? 0.447   48.253  70.888  1.00 19.07 ? 1038 PRO B CA    1 
ATOM   16644 C  C     . PRO B  1  1040 ? -0.909  48.177  71.566  1.00 16.23 ? 1038 PRO B C     1 
ATOM   16645 O  O     . PRO B  1  1040 ? -1.504  49.207  71.938  1.00 18.11 ? 1038 PRO B O     1 
ATOM   16646 C  CB    . PRO B  1  1040 ? 1.598   48.131  71.905  1.00 18.22 ? 1038 PRO B CB    1 
ATOM   16647 C  CG    . PRO B  1  1040 ? 2.620   49.108  71.436  1.00 18.92 ? 1038 PRO B CG    1 
ATOM   16648 C  CD    . PRO B  1  1040 ? 1.835   50.252  70.855  1.00 18.40 ? 1038 PRO B CD    1 
ATOM   16649 N  N     . PRO B  1  1041 ? -1.427  46.966  71.761  1.00 16.58 ? 1039 PRO B N     1 
ATOM   16650 C  CA    . PRO B  1  1041 ? -2.640  46.789  72.560  1.00 16.59 ? 1039 PRO B CA    1 
ATOM   16651 C  C     . PRO B  1  1041 ? -2.490  47.457  73.923  1.00 17.60 ? 1039 PRO B C     1 
ATOM   16652 O  O     . PRO B  1  1041 ? -1.424  47.405  74.542  1.00 18.76 ? 1039 PRO B O     1 
ATOM   16653 C  CB    . PRO B  1  1041 ? -2.757  45.264  72.690  1.00 19.25 ? 1039 PRO B CB    1 
ATOM   16654 C  CG    . PRO B  1  1041 ? -1.917  44.719  71.539  1.00 19.46 ? 1039 PRO B CG    1 
ATOM   16655 C  CD    . PRO B  1  1041 ? -0.793  45.679  71.406  1.00 19.37 ? 1039 PRO B CD    1 
ATOM   16656 N  N     . GLN B  1  1042 ? -3.545  48.147  74.355  1.00 18.04 ? 1040 GLN B N     1 
ATOM   16657 C  CA    . GLN B  1  1042 ? -3.642  48.750  75.682  1.00 20.58 ? 1040 GLN B CA    1 
ATOM   16658 C  C     . GLN B  1  1042 ? -2.635  49.869  75.924  1.00 20.72 ? 1040 GLN B C     1 
ATOM   16659 O  O     . GLN B  1  1042 ? -2.474  50.323  77.068  1.00 18.66 ? 1040 GLN B O     1 
ATOM   16660 C  CB    . GLN B  1  1042 ? -3.485  47.690  76.778  1.00 24.23 ? 1040 GLN B CB    1 
ATOM   16661 C  CG    . GLN B  1  1042 ? -4.500  46.571  76.677  1.00 27.02 ? 1040 GLN B CG    1 
ATOM   16662 C  CD    . GLN B  1  1042 ? -4.424  45.633  77.873  1.00 30.27 ? 1040 GLN B CD    1 
ATOM   16663 O  OE1   . GLN B  1  1042 ? -5.375  45.529  78.644  1.00 43.14 ? 1040 GLN B OE1   1 
ATOM   16664 N  NE2   . GLN B  1  1042 ? -3.289  44.971  78.040  1.00 35.26 ? 1040 GLN B NE2   1 
ATOM   16665 N  N     . HIS B  1  1043 ? -1.959  50.344  74.885  1.00 17.24 ? 1041 HIS B N     1 
ATOM   16666 C  CA    . HIS B  1  1043 ? -0.843  51.273  75.056  1.00 16.82 ? 1041 HIS B CA    1 
ATOM   16667 C  C     . HIS B  1  1043 ? -1.359  52.703  74.986  1.00 19.39 ? 1041 HIS B C     1 
ATOM   16668 O  O     . HIS B  1  1043 ? -1.429  53.314  73.919  1.00 19.73 ? 1041 HIS B O     1 
ATOM   16669 C  CB    . HIS B  1  1043 ? 0.202   51.010  73.988  1.00 16.81 ? 1041 HIS B CB    1 
ATOM   16670 C  CG    . HIS B  1  1043 ? 1.409   51.891  74.081  1.00 16.60 ? 1041 HIS B CG    1 
ATOM   16671 N  ND1   . HIS B  1  1043 ? 2.495   51.586  74.875  1.00 17.32 ? 1041 HIS B ND1   1 
ATOM   16672 C  CD2   . HIS B  1  1043 ? 1.707   53.059  73.464  1.00 19.06 ? 1041 HIS B CD2   1 
ATOM   16673 C  CE1   . HIS B  1  1043 ? 3.416   52.523  74.733  1.00 18.07 ? 1041 HIS B CE1   1 
ATOM   16674 N  NE2   . HIS B  1  1043 ? 2.964   53.427  73.880  1.00 19.06 ? 1041 HIS B NE2   1 
ATOM   16675 N  N     . SER B  1  1044 ? -1.711  53.246  76.142  1.00 15.70 ? 1042 SER B N     1 
ATOM   16676 C  CA    . SER B  1  1044 ? -2.207  54.612  76.224  1.00 17.82 ? 1042 SER B CA    1 
ATOM   16677 C  C     . SER B  1  1044 ? -2.163  55.007  77.688  1.00 17.41 ? 1042 SER B C     1 
ATOM   16678 O  O     . SER B  1  1044 ? -2.010  54.163  78.569  1.00 18.65 ? 1042 SER B O     1 
ATOM   16679 C  CB    . SER B  1  1044 ? -3.626  54.740  75.669  1.00 17.72 ? 1042 SER B CB    1 
ATOM   16680 O  OG    . SER B  1  1044 ? -4.557  54.177  76.578  1.00 18.41 ? 1042 SER B OG    1 
ATOM   16681 N  N     . SER B  1  1045 ? -2.328  56.294  77.940  1.00 17.47 ? 1043 SER B N     1 
ATOM   16682 C  CA    . SER B  1  1045 ? -2.361  56.799  79.301  1.00 15.83 ? 1043 SER B CA    1 
ATOM   16683 C  C     . SER B  1  1045 ? -3.213  58.052  79.326  1.00 18.24 ? 1043 SER B C     1 
ATOM   16684 O  O     . SER B  1  1045 ? -3.148  58.850  78.388  1.00 18.44 ? 1043 SER B O     1 
ATOM   16685 C  CB    . SER B  1  1045 ? -0.946  57.115  79.774  1.00 17.95 ? 1043 SER B CB    1 
ATOM   16686 O  OG    . SER B  1  1045 ? -0.997  57.739  81.029  1.00 19.75 ? 1043 SER B OG    1 
ATOM   16687 N  N     . VAL B  1  1046 ? -4.015  58.229  80.389  1.00 17.50 ? 1044 VAL B N     1 
ATOM   16688 C  CA    . VAL B  1  1046 ? -4.800  59.462  80.506  1.00 18.70 ? 1044 VAL B CA    1 
ATOM   16689 C  C     . VAL B  1  1046 ? -3.999  60.588  81.126  1.00 18.14 ? 1044 VAL B C     1 
ATOM   16690 O  O     . VAL B  1  1046 ? -4.479  61.729  81.184  1.00 21.87 ? 1044 VAL B O     1 
ATOM   16691 C  CB    . VAL B  1  1046 ? -6.098  59.287  81.320  1.00 21.04 ? 1044 VAL B CB    1 
ATOM   16692 C  CG1   . VAL B  1  1046 ? -6.974  58.235  80.645  1.00 25.04 ? 1044 VAL B CG1   1 
ATOM   16693 C  CG2   . VAL B  1  1046 ? -5.783  58.905  82.748  1.00 21.15 ? 1044 VAL B CG2   1 
ATOM   16694 N  N     . HIS B  1  1047 ? -2.779  60.304  81.547  1.00 19.80 ? 1045 HIS B N     1 
ATOM   16695 C  CA    A HIS B  1  1047 ? -1.974  61.307  82.210  0.55 19.15 ? 1045 HIS B CA    1 
ATOM   16696 C  CA    B HIS B  1  1047 ? -1.910  61.263  82.222  0.45 19.19 ? 1045 HIS B CA    1 
ATOM   16697 C  C     . HIS B  1  1047 ? -1.158  62.104  81.203  1.00 17.66 ? 1045 HIS B C     1 
ATOM   16698 O  O     . HIS B  1  1047 ? -0.674  61.579  80.199  1.00 20.66 ? 1045 HIS B O     1 
ATOM   16699 C  CB    A HIS B  1  1047 ? -1.093  60.620  83.243  0.55 21.14 ? 1045 HIS B CB    1 
ATOM   16700 C  CB    B HIS B  1  1047 ? -0.908  60.521  83.109  0.45 20.46 ? 1045 HIS B CB    1 
ATOM   16701 C  CG    A HIS B  1  1047 ? -1.890  59.750  84.162  0.55 22.47 ? 1045 HIS B CG    1 
ATOM   16702 C  CG    B HIS B  1  1047 ? 0.279   61.340  83.518  0.45 21.13 ? 1045 HIS B CG    1 
ATOM   16703 N  ND1   A HIS B  1  1047 ? -2.793  60.267  85.065  0.55 24.84 ? 1045 HIS B ND1   1 
ATOM   16704 N  ND1   B HIS B  1  1047 ? 0.219   62.295  84.511  0.45 21.34 ? 1045 HIS B ND1   1 
ATOM   16705 C  CD2   A HIS B  1  1047 ? -1.990  58.403  84.257  0.55 22.75 ? 1045 HIS B CD2   1 
ATOM   16706 C  CD2   B HIS B  1  1047 ? 1.562   61.331  83.081  0.45 20.38 ? 1045 HIS B CD2   1 
ATOM   16707 C  CE1   A HIS B  1  1047 ? -3.383  59.275  85.708  0.55 26.05 ? 1045 HIS B CE1   1 
ATOM   16708 C  CE1   B HIS B  1  1047 ? 1.411   62.850  84.657  0.45 24.26 ? 1045 HIS B CE1   1 
ATOM   16709 N  NE2   A HIS B  1  1047 ? -2.918  58.134  85.233  0.55 21.18 ? 1045 HIS B NE2   1 
ATOM   16710 N  NE2   B HIS B  1  1047 ? 2.243   62.283  83.801  0.45 23.44 ? 1045 HIS B NE2   1 
ATOM   16711 N  N     . THR B  1  1048 ? -1.038  63.394  81.476  1.00 18.72 ? 1046 THR B N     1 
ATOM   16712 C  CA    . THR B  1  1048 ? -0.241  64.284  80.647  1.00 17.80 ? 1046 THR B CA    1 
ATOM   16713 C  C     . THR B  1  1048 ? 0.876   64.843  81.514  1.00 18.01 ? 1046 THR B C     1 
ATOM   16714 O  O     . THR B  1  1048 ? 0.618   65.380  82.596  1.00 21.30 ? 1046 THR B O     1 
ATOM   16715 C  CB    . THR B  1  1048 ? -1.080  65.428  80.082  1.00 22.25 ? 1046 THR B CB    1 
ATOM   16716 O  OG1   . THR B  1  1048 ? -2.253  64.898  79.442  1.00 22.24 ? 1046 THR B OG1   1 
ATOM   16717 C  CG2   . THR B  1  1048 ? -0.264  66.213  79.057  1.00 24.72 ? 1046 THR B CG2   1 
ATOM   16718 N  N     . ASP B  1  1049 ? 2.100   64.722  81.031  1.00 18.27 ? 1047 ASP B N     1 
ATOM   16719 C  CA    . ASP B  1  1049 ? 3.225   65.237  81.783  1.00 19.47 ? 1047 ASP B CA    1 
ATOM   16720 C  C     . ASP B  1  1049 ? 3.052   66.736  82.008  1.00 19.65 ? 1047 ASP B C     1 
ATOM   16721 O  O     . ASP B  1  1049 ? 2.769   67.477  81.059  1.00 21.53 ? 1047 ASP B O     1 
ATOM   16722 C  CB    . ASP B  1  1049 ? 4.517   64.936  81.036  1.00 19.16 ? 1047 ASP B CB    1 
ATOM   16723 C  CG    . ASP B  1  1049 ? 5.730   65.376  81.802  1.00 20.59 ? 1047 ASP B CG    1 
ATOM   16724 O  OD1   . ASP B  1  1049 ? 6.080   66.565  81.711  1.00 20.65 ? 1047 ASP B OD1   1 
ATOM   16725 O  OD2   . ASP B  1  1049 ? 6.294   64.542  82.522  1.00 21.85 ? 1047 ASP B OD2   1 
ATOM   16726 N  N     . PRO B  1  1050 ? 3.176   67.216  83.246  1.00 19.31 ? 1048 PRO B N     1 
ATOM   16727 C  CA    . PRO B  1  1050 ? 2.923   68.643  83.502  1.00 22.98 ? 1048 PRO B CA    1 
ATOM   16728 C  C     . PRO B  1  1050 ? 4.009   69.541  82.942  1.00 22.90 ? 1048 PRO B C     1 
ATOM   16729 O  O     . PRO B  1  1050 ? 3.731   70.703  82.627  1.00 23.70 ? 1048 PRO B O     1 
ATOM   16730 C  CB    . PRO B  1  1050 ? 2.857   68.712  85.034  1.00 24.20 ? 1048 PRO B CB    1 
ATOM   16731 C  CG    . PRO B  1  1050 ? 3.699   67.573  85.489  1.00 24.35 ? 1048 PRO B CG    1 
ATOM   16732 C  CD    . PRO B  1  1050 ? 3.478   66.469  84.477  1.00 21.03 ? 1048 PRO B CD    1 
ATOM   16733 N  N     . VAL B  1  1051 ? 5.236   69.034  82.811  1.00 22.58 ? 1049 VAL B N     1 
ATOM   16734 C  CA    . VAL B  1  1051 ? 6.305   69.844  82.236  1.00 20.46 ? 1049 VAL B CA    1 
ATOM   16735 C  C     . VAL B  1  1051 ? 6.122   69.954  80.733  1.00 20.31 ? 1049 VAL B C     1 
ATOM   16736 O  O     . VAL B  1  1051 ? 6.349   71.016  80.143  1.00 22.24 ? 1049 VAL B O     1 
ATOM   16737 C  CB    . VAL B  1  1051 ? 7.678   69.260  82.617  1.00 21.91 ? 1049 VAL B CB    1 
ATOM   16738 C  CG1   . VAL B  1  1051 ? 8.799   70.095  81.985  1.00 24.61 ? 1049 VAL B CG1   1 
ATOM   16739 C  CG2   . VAL B  1  1051 ? 7.832   69.239  84.138  1.00 25.56 ? 1049 VAL B CG2   1 
ATOM   16740 N  N     . LEU B  1  1052 ? 5.674   68.873  80.094  1.00 19.81 ? 1050 LEU B N     1 
ATOM   16741 C  CA    . LEU B  1  1052 ? 5.227   68.964  78.707  1.00 19.06 ? 1050 LEU B CA    1 
ATOM   16742 C  C     . LEU B  1  1052 ? 4.192   70.070  78.542  1.00 24.45 ? 1050 LEU B C     1 
ATOM   16743 O  O     . LEU B  1  1052 ? 4.280   70.881  77.619  1.00 21.09 ? 1050 LEU B O     1 
ATOM   16744 C  CB    . LEU B  1  1052 ? 4.662   67.617  78.248  1.00 19.46 ? 1050 LEU B CB    1 
ATOM   16745 C  CG    . LEU B  1  1052 ? 4.185   67.467  76.791  1.00 18.85 ? 1050 LEU B CG    1 
ATOM   16746 C  CD1   . LEU B  1  1052 ? 2.786   68.039  76.560  1.00 22.03 ? 1050 LEU B CD1   1 
ATOM   16747 C  CD2   . LEU B  1  1052 ? 5.188   68.086  75.818  1.00 20.36 ? 1050 LEU B CD2   1 
ATOM   16748 N  N     . LEU B  1  1053 ? 3.189   70.109  79.424  1.00 21.23 ? 1051 LEU B N     1 
ATOM   16749 C  CA    . LEU B  1  1053 ? 2.161   71.137  79.311  1.00 22.44 ? 1051 LEU B CA    1 
ATOM   16750 C  C     . LEU B  1  1053 ? 2.761   72.533  79.415  1.00 21.30 ? 1051 LEU B C     1 
ATOM   16751 O  O     . LEU B  1  1053 ? 2.402   73.429  78.643  1.00 25.70 ? 1051 LEU B O     1 
ATOM   16752 C  CB    . LEU B  1  1053 ? 1.092   70.937  80.388  1.00 25.36 ? 1051 LEU B CB    1 
ATOM   16753 C  CG    . LEU B  1  1053 ? 0.172   69.728  80.174  1.00 28.98 ? 1051 LEU B CG    1 
ATOM   16754 C  CD1   . LEU B  1  1053 ? -0.624  69.482  81.440  1.00 25.63 ? 1051 LEU B CD1   1 
ATOM   16755 C  CD2   . LEU B  1  1053 ? -0.757  69.942  79.001  1.00 27.47 ? 1051 LEU B CD2   1 
ATOM   16756 N  N     . ASP B  1  1054 ? 3.672   72.738  80.366  1.00 23.46 ? 1052 ASP B N     1 
ATOM   16757 C  CA    . ASP B  1  1054 ? 4.296   74.049  80.511  1.00 28.80 ? 1052 ASP B CA    1 
ATOM   16758 C  C     . ASP B  1  1054 ? 5.107   74.403  79.278  1.00 24.79 ? 1052 ASP B C     1 
ATOM   16759 O  O     . ASP B  1  1054 ? 5.133   75.564  78.854  1.00 25.50 ? 1052 ASP B O     1 
ATOM   16760 C  CB    . ASP B  1  1054 ? 5.183   74.073  81.749  1.00 25.40 ? 1052 ASP B CB    1 
ATOM   16761 C  CG    . ASP B  1  1054 ? 4.384   74.097  83.028  1.00 31.28 ? 1052 ASP B CG    1 
ATOM   16762 O  OD1   . ASP B  1  1054 ? 3.162   74.312  82.945  1.00 29.38 ? 1052 ASP B OD1   1 
ATOM   16763 O  OD2   . ASP B  1  1054 ? 4.975   73.898  84.108  1.00 35.42 ? 1052 ASP B OD2   1 
ATOM   16764 N  N     . PHE B  1  1055 ? 5.772   73.412  78.688  1.00 23.25 ? 1053 PHE B N     1 
ATOM   16765 C  CA    . PHE B  1  1055 ? 6.542   73.647  77.474  1.00 21.74 ? 1053 PHE B CA    1 
ATOM   16766 C  C     . PHE B  1  1055 ? 5.634   74.034  76.317  1.00 26.52 ? 1053 PHE B C     1 
ATOM   16767 O  O     . PHE B  1  1055 ? 5.950   74.951  75.551  1.00 24.49 ? 1053 PHE B O     1 
ATOM   16768 C  CB    . PHE B  1  1055 ? 7.360   72.403  77.147  1.00 21.60 ? 1053 PHE B CB    1 
ATOM   16769 C  CG    . PHE B  1  1055 ? 8.229   72.541  75.933  1.00 21.93 ? 1053 PHE B CG    1 
ATOM   16770 C  CD1   . PHE B  1  1055 ? 9.190   73.539  75.862  1.00 24.83 ? 1053 PHE B CD1   1 
ATOM   16771 C  CD2   . PHE B  1  1055 ? 8.096   71.664  74.872  1.00 22.02 ? 1053 PHE B CD2   1 
ATOM   16772 C  CE1   . PHE B  1  1055 ? 9.995   73.663  74.744  1.00 26.98 ? 1053 PHE B CE1   1 
ATOM   16773 C  CE2   . PHE B  1  1055 ? 8.891   71.787  73.745  1.00 22.50 ? 1053 PHE B CE2   1 
ATOM   16774 C  CZ    . PHE B  1  1055 ? 9.846   72.786  73.687  1.00 23.21 ? 1053 PHE B CZ    1 
ATOM   16775 N  N     . ALA B  1  1056 ? 4.494   73.351  76.177  1.00 23.56 ? 1054 ALA B N     1 
ATOM   16776 C  CA    . ALA B  1  1056 ? 3.546   73.710  75.127  1.00 24.23 ? 1054 ALA B CA    1 
ATOM   16777 C  C     . ALA B  1  1056 ? 3.062   75.146  75.281  1.00 24.99 ? 1054 ALA B C     1 
ATOM   16778 O  O     . ALA B  1  1056 ? 2.929   75.869  74.288  1.00 27.38 ? 1054 ALA B O     1 
ATOM   16779 C  CB    . ALA B  1  1056 ? 2.354   72.750  75.129  1.00 22.70 ? 1054 ALA B CB    1 
ATOM   16780 N  N     . LYS B  1  1057 ? 2.792   75.582  76.514  1.00 25.23 ? 1055 LYS B N     1 
ATOM   16781 C  CA    . LYS B  1  1057 ? 2.327   76.953  76.703  1.00 26.65 ? 1055 LYS B CA    1 
ATOM   16782 C  C     . LYS B  1  1057 ? 3.413   77.953  76.340  1.00 30.72 ? 1055 LYS B C     1 
ATOM   16783 O  O     . LYS B  1  1057 ? 3.133   78.996  75.731  1.00 31.36 ? 1055 LYS B O     1 
ATOM   16784 C  CB    . LYS B  1  1057 ? 1.880   77.176  78.142  1.00 29.51 ? 1055 LYS B CB    1 
ATOM   16785 C  CG    . LYS B  1  1057 ? 0.493   76.678  78.440  1.00 36.64 ? 1055 LYS B CG    1 
ATOM   16786 C  CD    . LYS B  1  1057 ? 0.130   77.008  79.863  1.00 29.72 ? 1055 LYS B CD    1 
ATOM   16787 C  CE    . LYS B  1  1057 ? 1.125   76.389  80.827  1.00 30.43 ? 1055 LYS B CE    1 
ATOM   16788 N  NZ    . LYS B  1  1057 ? 0.616   76.469  82.226  1.00 35.01 ? 1055 LYS B NZ    1 
ATOM   16789 N  N     . TRP B  1  1058 ? 4.653   77.650  76.724  1.00 29.24 ? 1056 TRP B N     1 
ATOM   16790 C  CA    . TRP B  1  1058 ? 5.793   78.483  76.355  1.00 31.42 ? 1056 TRP B CA    1 
ATOM   16791 C  C     . TRP B  1  1058 ? 5.926   78.588  74.845  1.00 30.60 ? 1056 TRP B C     1 
ATOM   16792 O  O     . TRP B  1  1058 ? 6.152   79.681  74.311  1.00 29.86 ? 1056 TRP B O     1 
ATOM   16793 C  CB    . TRP B  1  1058 ? 7.061   77.904  76.984  1.00 28.77 ? 1056 TRP B CB    1 
ATOM   16794 C  CG    . TRP B  1  1058 ? 8.326   78.636  76.670  1.00 34.23 ? 1056 TRP B CG    1 
ATOM   16795 C  CD1   . TRP B  1  1058 ? 8.772   79.796  77.246  1.00 36.05 ? 1056 TRP B CD1   1 
ATOM   16796 C  CD2   . TRP B  1  1058 ? 9.324   78.248  75.724  1.00 29.84 ? 1056 TRP B CD2   1 
ATOM   16797 N  NE1   . TRP B  1  1058 ? 9.984   80.152  76.708  1.00 36.50 ? 1056 TRP B NE1   1 
ATOM   16798 C  CE2   . TRP B  1  1058 ? 10.347  79.219  75.773  1.00 38.86 ? 1056 TRP B CE2   1 
ATOM   16799 C  CE3   . TRP B  1  1058 ? 9.458   77.172  74.842  1.00 29.74 ? 1056 TRP B CE3   1 
ATOM   16800 C  CZ2   . TRP B  1  1058 ? 11.485  79.147  74.968  1.00 34.49 ? 1056 TRP B CZ2   1 
ATOM   16801 C  CZ3   . TRP B  1  1058 ? 10.588  77.105  74.037  1.00 32.38 ? 1056 TRP B CZ3   1 
ATOM   16802 C  CH2   . TRP B  1  1058 ? 11.587  78.083  74.112  1.00 32.36 ? 1056 TRP B CH2   1 
ATOM   16803 N  N     . LEU B  1  1059 ? 5.770   77.466  74.134  1.00 27.46 ? 1057 LEU B N     1 
ATOM   16804 C  CA    . LEU B  1  1059 ? 5.808   77.502  72.675  1.00 32.61 ? 1057 LEU B CA    1 
ATOM   16805 C  C     . LEU B  1  1059 ? 4.678   78.361  72.114  1.00 35.82 ? 1057 LEU B C     1 
ATOM   16806 O  O     . LEU B  1  1059 ? 4.897   79.147  71.182  1.00 33.34 ? 1057 LEU B O     1 
ATOM   16807 C  CB    . LEU B  1  1059 ? 5.737   76.088  72.105  1.00 25.50 ? 1057 LEU B CB    1 
ATOM   16808 C  CG    . LEU B  1  1059 ? 6.941   75.187  72.390  1.00 28.03 ? 1057 LEU B CG    1 
ATOM   16809 C  CD1   . LEU B  1  1059 ? 6.640   73.771  71.952  1.00 25.51 ? 1057 LEU B CD1   1 
ATOM   16810 C  CD2   . LEU B  1  1059 ? 8.183   75.721  71.671  1.00 30.31 ? 1057 LEU B CD2   1 
ATOM   16811 N  N     . ASP B  1  1060 ? 3.461   78.214  72.661  1.00 31.95 ? 1058 ASP B N     1 
ATOM   16812 C  CA    . ASP B  1  1060 ? 2.337   79.078  72.283  1.00 34.49 ? 1058 ASP B CA    1 
ATOM   16813 C  C     . ASP B  1  1060 ? 2.712   80.551  72.386  1.00 37.37 ? 1058 ASP B C     1 
ATOM   16814 O  O     . ASP B  1  1060 ? 2.447   81.341  71.470  1.00 39.79 ? 1058 ASP B O     1 
ATOM   16815 C  CB    . ASP B  1  1060 ? 1.119   78.824  73.184  1.00 40.51 ? 1058 ASP B CB    1 
ATOM   16816 C  CG    . ASP B  1  1060 ? 0.384   77.534  72.875  1.00 40.54 ? 1058 ASP B CG    1 
ATOM   16817 O  OD1   . ASP B  1  1060 ? 0.320   77.128  71.698  1.00 36.64 ? 1058 ASP B OD1   1 
ATOM   16818 O  OD2   . ASP B  1  1060 ? -0.163  76.937  73.835  1.00 39.83 ? 1058 ASP B OD2   1 
ATOM   16819 N  N     . GLY B  1  1061 ? 3.289   80.945  73.524  1.00 33.23 ? 1059 GLY B N     1 
ATOM   16820 C  CA    . GLY B  1  1061 ? 3.641   82.341  73.730  1.00 38.05 ? 1059 GLY B CA    1 
ATOM   16821 C  C     . GLY B  1  1061 ? 4.658   82.852  72.732  1.00 43.02 ? 1059 GLY B C     1 
ATOM   16822 O  O     . GLY B  1  1061 ? 4.680   84.043  72.417  1.00 40.66 ? 1059 GLY B O     1 
ATOM   16823 N  N     . LYS B  1  1062 ? 5.504   81.965  72.215  1.00 38.95 ? 1060 LYS B N     1 
ATOM   16824 C  CA    . LYS B  1  1062 ? 6.485   82.324  71.201  1.00 40.74 ? 1060 LYS B CA    1 
ATOM   16825 C  C     . LYS B  1  1062 ? 5.919   82.320  69.794  1.00 41.72 ? 1060 LYS B C     1 
ATOM   16826 O  O     . LYS B  1  1062 ? 6.642   82.666  68.855  1.00 46.97 ? 1060 LYS B O     1 
ATOM   16827 C  CB    . LYS B  1  1062 ? 7.665   81.358  71.251  1.00 38.58 ? 1060 LYS B CB    1 
ATOM   16828 C  CG    . LYS B  1  1062 ? 8.507   81.485  72.478  1.00 44.08 ? 1060 LYS B CG    1 
ATOM   16829 C  CD    . LYS B  1  1062 ? 9.451   80.312  72.552  1.00 41.29 ? 1060 LYS B CD    1 
ATOM   16830 C  CE    . LYS B  1  1062 ? 10.174  80.099  71.234  1.00 41.30 ? 1060 LYS B CE    1 
ATOM   16831 N  NZ    . LYS B  1  1062 ? 11.370  80.970  71.092  1.00 39.59 ? 1060 LYS B NZ    1 
ATOM   16832 N  N     . GLY B  1  1063 ? 4.664   81.923  69.616  1.00 41.94 ? 1061 GLY B N     1 
ATOM   16833 C  CA    . GLY B  1  1063 ? 4.138   81.786  68.279  1.00 38.22 ? 1061 GLY B CA    1 
ATOM   16834 C  C     . GLY B  1  1063 ? 4.610   80.563  67.536  1.00 44.40 ? 1061 GLY B C     1 
ATOM   16835 O  O     . GLY B  1  1063 ? 4.333   80.439  66.339  1.00 43.12 ? 1061 GLY B O     1 
ATOM   16836 N  N     . ALA B  1  1064 ? 5.314   79.646  68.204  1.00 36.55 ? 1062 ALA B N     1 
ATOM   16837 C  CA    . ALA B  1  1064 ? 5.766   78.411  67.564  1.00 37.03 ? 1062 ALA B CA    1 
ATOM   16838 C  C     . ALA B  1  1064 ? 4.587   77.438  67.497  1.00 40.95 ? 1062 ALA B C     1 
ATOM   16839 O  O     . ALA B  1  1064 ? 4.523   76.428  68.200  1.00 32.38 ? 1062 ALA B O     1 
ATOM   16840 C  CB    . ALA B  1  1064 ? 6.952   77.824  68.317  1.00 39.97 ? 1062 ALA B CB    1 
ATOM   16841 N  N     . ARG B  1  1065 ? 3.645   77.760  66.604  1.00 36.86 ? 1063 ARG B N     1 
ATOM   16842 C  CA    . ARG B  1  1065 ? 2.338   77.101  66.609  1.00 36.58 ? 1063 ARG B CA    1 
ATOM   16843 C  C     . ARG B  1  1065 ? 2.437   75.635  66.207  1.00 35.62 ? 1063 ARG B C     1 
ATOM   16844 O  O     . ARG B  1  1065 ? 1.805   74.773  66.830  1.00 32.40 ? 1063 ARG B O     1 
ATOM   16845 C  CB    . ARG B  1  1065 ? 1.371   77.850  65.686  1.00 38.96 ? 1063 ARG B CB    1 
ATOM   16846 N  N     . ALA B  1  1066 ? 3.212   75.328  65.164  1.00 30.07 ? 1064 ALA B N     1 
ATOM   16847 C  CA    . ALA B  1  1066 ? 3.367   73.936  64.762  1.00 28.53 ? 1064 ALA B CA    1 
ATOM   16848 C  C     . ALA B  1  1066 ? 4.020   73.121  65.868  1.00 30.27 ? 1064 ALA B C     1 
ATOM   16849 O  O     . ALA B  1  1066 ? 3.619   71.981  66.129  1.00 29.93 ? 1064 ALA B O     1 
ATOM   16850 C  CB    . ALA B  1  1066 ? 4.189   73.845  63.477  1.00 36.61 ? 1064 ALA B CB    1 
ATOM   16851 N  N     . GLU B  1  1067 ? 5.029   73.693  66.530  1.00 29.03 ? 1065 GLU B N     1 
ATOM   16852 C  CA    . GLU B  1  1067 ? 5.729   72.956  67.577  1.00 26.95 ? 1065 GLU B CA    1 
ATOM   16853 C  C     . GLU B  1  1067 ? 4.848   72.774  68.809  1.00 26.62 ? 1065 GLU B C     1 
ATOM   16854 O  O     . GLU B  1  1067 ? 4.874   71.714  69.442  1.00 26.54 ? 1065 GLU B O     1 
ATOM   16855 C  CB    . GLU B  1  1067 ? 7.029   73.672  67.945  1.00 31.85 ? 1065 GLU B CB    1 
ATOM   16856 C  CG    . GLU B  1  1067 ? 8.107   73.574  66.877  1.00 26.64 ? 1065 GLU B CG    1 
ATOM   16857 C  CD    . GLU B  1  1067 ? 7.929   74.592  65.780  1.00 32.21 ? 1065 GLU B CD    1 
ATOM   16858 O  OE1   . GLU B  1  1067 ? 7.033   75.455  65.909  1.00 32.49 ? 1065 GLU B OE1   1 
ATOM   16859 O  OE2   . GLU B  1  1067 ? 8.689   74.527  64.789  1.00 31.94 ? 1065 GLU B OE2   1 
ATOM   16860 N  N     . ALA B  1  1068 ? 4.076   73.802  69.167  1.00 28.06 ? 1066 ALA B N     1 
ATOM   16861 C  CA    . ALA B  1  1068 ? 3.160   73.687  70.299  1.00 29.37 ? 1066 ALA B CA    1 
ATOM   16862 C  C     . ALA B  1  1068 ? 2.113   72.611  70.048  1.00 28.34 ? 1066 ALA B C     1 
ATOM   16863 O  O     . ALA B  1  1068 ? 1.743   71.866  70.966  1.00 24.73 ? 1066 ALA B O     1 
ATOM   16864 C  CB    . ALA B  1  1068 ? 2.491   75.032  70.568  1.00 28.54 ? 1066 ALA B CB    1 
ATOM   16865 N  N     . GLU B  1  1069 ? 1.617   72.521  68.810  1.00 27.72 ? 1067 GLU B N     1 
ATOM   16866 C  CA    . GLU B  1  1069 ? 0.680   71.461  68.457  1.00 30.40 ? 1067 GLU B CA    1 
ATOM   16867 C  C     . GLU B  1  1069 ? 1.343   70.095  68.555  1.00 29.99 ? 1067 GLU B C     1 
ATOM   16868 O  O     . GLU B  1  1069 ? 0.766   69.153  69.108  1.00 27.04 ? 1067 GLU B O     1 
ATOM   16869 C  CB    . GLU B  1  1069 ? 0.125   71.698  67.048  1.00 33.74 ? 1067 GLU B CB    1 
ATOM   16870 C  CG    . GLU B  1  1069 ? -0.764  70.583  66.509  1.00 34.54 ? 1067 GLU B CG    1 
ATOM   16871 C  CD    . GLU B  1  1069 ? -2.152  70.556  67.142  1.00 44.03 ? 1067 GLU B CD    1 
ATOM   16872 O  OE1   . GLU B  1  1069 ? -2.424  71.376  68.046  1.00 47.32 ? 1067 GLU B OE1   1 
ATOM   16873 O  OE2   . GLU B  1  1069 ? -2.977  69.712  66.729  1.00 50.11 ? 1067 GLU B OE2   1 
ATOM   16874 N  N     . ALA B  1  1070 ? 2.560   69.968  68.024  1.00 26.43 ? 1068 ALA B N     1 
ATOM   16875 C  CA    . ALA B  1  1070 ? 3.282   68.709  68.152  1.00 28.84 ? 1068 ALA B CA    1 
ATOM   16876 C  C     . ALA B  1  1070 ? 3.502   68.362  69.615  1.00 22.57 ? 1068 ALA B C     1 
ATOM   16877 O  O     . ALA B  1  1070 ? 3.425   67.188  70.000  1.00 25.46 ? 1068 ALA B O     1 
ATOM   16878 C  CB    . ALA B  1  1070 ? 4.620   68.781  67.414  1.00 33.53 ? 1068 ALA B CB    1 
ATOM   16879 N  N     . ALA B  1  1071 ? 3.764   69.369  70.447  1.00 22.45 ? 1069 ALA B N     1 
ATOM   16880 C  CA    . ALA B  1  1071 ? 3.959   69.101  71.869  1.00 20.66 ? 1069 ALA B CA    1 
ATOM   16881 C  C     . ALA B  1  1071 ? 2.681   68.567  72.505  1.00 24.87 ? 1069 ALA B C     1 
ATOM   16882 O  O     . ALA B  1  1071 ? 2.710   67.560  73.223  1.00 23.57 ? 1069 ALA B O     1 
ATOM   16883 C  CB    . ALA B  1  1071 ? 4.443   70.354  72.590  1.00 20.28 ? 1069 ALA B CB    1 
ATOM   16884 N  N     . ARG B  1  1072 ? 1.544   69.229  72.251  1.00 22.31 ? 1070 ARG B N     1 
ATOM   16885 C  CA    A ARG B  1  1072 ? 0.280   68.745  72.800  0.55 22.76 ? 1070 ARG B CA    1 
ATOM   16886 C  CA    B ARG B  1  1072 ? 0.276   68.744  72.792  0.45 22.78 ? 1070 ARG B CA    1 
ATOM   16887 C  C     . ARG B  1  1072 ? -0.033  67.340  72.304  1.00 25.15 ? 1070 ARG B C     1 
ATOM   16888 O  O     . ARG B  1  1072 ? -0.514  66.498  73.074  1.00 22.91 ? 1070 ARG B O     1 
ATOM   16889 C  CB    A ARG B  1  1072 ? -0.857  69.709  72.447  0.55 22.53 ? 1070 ARG B CB    1 
ATOM   16890 C  CB    B ARG B  1  1072 ? -0.858  69.694  72.417  0.45 22.55 ? 1070 ARG B CB    1 
ATOM   16891 C  CG    A ARG B  1  1072 ? -0.817  71.036  73.207  0.55 25.22 ? 1070 ARG B CG    1 
ATOM   16892 C  CG    B ARG B  1  1072 ? -0.717  71.022  73.092  0.45 25.35 ? 1070 ARG B CG    1 
ATOM   16893 C  CD    A ARG B  1  1072 ? -1.984  71.948  72.802  0.55 27.77 ? 1070 ARG B CD    1 
ATOM   16894 C  CD    B ARG B  1  1072 ? -1.923  71.906  72.907  0.45 27.82 ? 1070 ARG B CD    1 
ATOM   16895 N  NE    A ARG B  1  1072 ? -1.958  72.306  71.389  0.55 29.97 ? 1070 ARG B NE    1 
ATOM   16896 N  NE    B ARG B  1  1072 ? -1.883  72.916  73.949  0.45 27.93 ? 1070 ARG B NE    1 
ATOM   16897 C  CZ    A ARG B  1  1072 ? -1.542  73.475  70.918  0.55 28.98 ? 1070 ARG B CZ    1 
ATOM   16898 C  CZ    B ARG B  1  1072 ? -1.198  74.044  73.865  0.45 26.46 ? 1070 ARG B CZ    1 
ATOM   16899 N  NH1   A ARG B  1  1072 ? -1.154  74.447  71.725  0.55 26.28 ? 1070 ARG B NH1   1 
ATOM   16900 N  NH1   B ARG B  1  1072 ? -0.619  74.419  72.736  0.45 31.86 ? 1070 ARG B NH1   1 
ATOM   16901 N  NH2   A ARG B  1  1072 ? -1.507  73.670  69.602  0.55 22.95 ? 1070 ARG B NH2   1 
ATOM   16902 N  NH2   B ARG B  1  1072 ? -1.077  74.808  74.944  0.45 28.98 ? 1070 ARG B NH2   1 
ATOM   16903 N  N     . ASN B  1  1073 ? 0.225   67.070  71.020  1.00 22.50 ? 1071 ASN B N     1 
ATOM   16904 C  CA    . ASN B  1  1073 ? -0.022  65.736  70.486  1.00 21.51 ? 1071 ASN B CA    1 
ATOM   16905 C  C     . ASN B  1  1073 ? 0.881   64.704  71.142  1.00 21.89 ? 1071 ASN B C     1 
ATOM   16906 O  O     . ASN B  1  1073 ? 0.443   63.584  71.424  1.00 24.05 ? 1071 ASN B O     1 
ATOM   16907 C  CB    . ASN B  1  1073 ? 0.157   65.738  68.971  1.00 27.39 ? 1071 ASN B CB    1 
ATOM   16908 C  CG    . ASN B  1  1073 ? -0.936  66.511  68.267  1.00 31.28 ? 1071 ASN B CG    1 
ATOM   16909 O  OD1   . ASN B  1  1073 ? -1.997  66.775  68.846  1.00 34.41 ? 1071 ASN B OD1   1 
ATOM   16910 N  ND2   . ASN B  1  1073 ? -0.688  66.883  67.014  1.00 34.54 ? 1071 ASN B ND2   1 
ATOM   16911 N  N     . ALA B  1  1074 ? 2.148   65.062  71.391  1.00 22.20 ? 1072 ALA B N     1 
ATOM   16912 C  CA    . ALA B  1  1074 ? 3.037   64.162  72.119  1.00 24.22 ? 1072 ALA B CA    1 
ATOM   16913 C  C     . ALA B  1  1074 ? 2.530   63.932  73.530  1.00 18.54 ? 1072 ALA B C     1 
ATOM   16914 O  O     . ALA B  1  1074 ? 2.551   62.803  74.027  1.00 19.36 ? 1072 ALA B O     1 
ATOM   16915 C  CB    . ALA B  1  1074 ? 4.451   64.733  72.160  1.00 22.82 ? 1072 ALA B CB    1 
ATOM   16916 N  N     . GLY B  1  1075 ? 2.099   64.998  74.203  1.00 18.95 ? 1073 GLY B N     1 
ATOM   16917 C  CA    . GLY B  1  1075 ? 1.566   64.831  75.548  1.00 22.69 ? 1073 GLY B CA    1 
ATOM   16918 C  C     . GLY B  1  1075 ? 0.413   63.846  75.587  1.00 23.75 ? 1073 GLY B C     1 
ATOM   16919 O  O     . GLY B  1  1075 ? 0.302   63.033  76.513  1.00 24.18 ? 1073 GLY B O     1 
ATOM   16920 N  N     . SER B  1  1076 ? -0.434  63.872  74.559  1.00 23.59 ? 1074 SER B N     1 
ATOM   16921 C  CA    . SER B  1  1076 ? -1.589  62.984  74.544  1.00 21.25 ? 1074 SER B CA    1 
ATOM   16922 C  C     . SER B  1  1076 ? -1.214  61.562  74.159  1.00 24.82 ? 1074 SER B C     1 
ATOM   16923 O  O     . SER B  1  1076 ? -1.694  60.609  74.778  1.00 26.30 ? 1074 SER B O     1 
ATOM   16924 C  CB    . SER B  1  1076 ? -2.658  63.534  73.596  1.00 23.93 ? 1074 SER B CB    1 
ATOM   16925 O  OG    . SER B  1  1076 ? -3.258  64.687  74.166  1.00 27.47 ? 1074 SER B OG    1 
ATOM   16926 N  N     . SER B  1  1077 ? -0.351  61.388  73.158  1.00 21.97 ? 1075 SER B N     1 
ATOM   16927 C  CA    . SER B  1  1077 ? -0.101  60.035  72.678  1.00 22.92 ? 1075 SER B CA    1 
ATOM   16928 C  C     . SER B  1  1077 ? 0.908   59.296  73.548  1.00 21.90 ? 1075 SER B C     1 
ATOM   16929 O  O     . SER B  1  1077 ? 0.959   58.062  73.504  1.00 24.26 ? 1075 SER B O     1 
ATOM   16930 C  CB    . SER B  1  1077 ? 0.365   60.063  71.221  1.00 30.16 ? 1075 SER B CB    1 
ATOM   16931 O  OG    . SER B  1  1077 ? 1.703   60.482  71.124  1.00 27.43 ? 1075 SER B OG    1 
ATOM   16932 N  N     . SER B  1  1078 ? 1.683   60.020  74.352  1.00 19.13 ? 1076 SER B N     1 
ATOM   16933 C  CA    . SER B  1  1078 ? 2.561   59.376  75.320  1.00 18.44 ? 1076 SER B CA    1 
ATOM   16934 C  C     . SER B  1  1078 ? 1.768   58.408  76.184  1.00 16.10 ? 1076 SER B C     1 
ATOM   16935 O  O     . SER B  1  1078 ? 0.655   58.713  76.629  1.00 18.54 ? 1076 SER B O     1 
ATOM   16936 C  CB    . SER B  1  1078 ? 3.214   60.430  76.216  1.00 18.32 ? 1076 SER B CB    1 
ATOM   16937 O  OG    . SER B  1  1078 ? 3.907   59.818  77.302  1.00 17.63 ? 1076 SER B OG    1 
ATOM   16938 N  N     . ALA B  1  1079 ? 2.346   57.242  76.429  1.00 16.39 ? 1077 ALA B N     1 
ATOM   16939 C  CA    . ALA B  1  1079 ? 1.723   56.287  77.327  1.00 16.10 ? 1077 ALA B CA    1 
ATOM   16940 C  C     . ALA B  1  1079 ? 2.372   56.303  78.690  1.00 16.70 ? 1077 ALA B C     1 
ATOM   16941 O  O     . ALA B  1  1079 ? 2.139   55.395  79.484  1.00 17.19 ? 1077 ALA B O     1 
ATOM   16942 C  CB    . ALA B  1  1079 ? 1.763   54.878  76.732  1.00 17.51 ? 1077 ALA B CB    1 
ATOM   16943 N  N     . LEU B  1  1080 ? 3.179   57.316  78.976  1.00 16.48 ? 1078 LEU B N     1 
ATOM   16944 C  CA    . LEU B  1  1080 ? 3.716   57.487  80.317  1.00 16.52 ? 1078 LEU B CA    1 
ATOM   16945 C  C     . LEU B  1  1080 ? 2.589   57.448  81.335  1.00 14.94 ? 1078 LEU B C     1 
ATOM   16946 O  O     . LEU B  1  1080 ? 1.611   58.185  81.222  1.00 16.00 ? 1078 LEU B O     1 
ATOM   16947 C  CB    . LEU B  1  1080 ? 4.453   58.817  80.408  1.00 17.00 ? 1078 LEU B CB    1 
ATOM   16948 C  CG    . LEU B  1  1080 ? 4.856   59.258  81.810  1.00 17.99 ? 1078 LEU B CG    1 
ATOM   16949 C  CD1   . LEU B  1  1080 ? 6.019   58.392  82.281  1.00 17.54 ? 1078 LEU B CD1   1 
ATOM   16950 C  CD2   . LEU B  1  1080 ? 5.189   60.751  81.841  1.00 18.50 ? 1078 LEU B CD2   1 
ATOM   16951 N  N     . GLY B  1  1081 ? 2.737   56.599  82.356  1.00 15.76 ? 1079 GLY B N     1 
ATOM   16952 C  CA    . GLY B  1  1081 ? 1.717   56.472  83.374  1.00 16.69 ? 1079 GLY B CA    1 
ATOM   16953 C  C     . GLY B  1  1081 ? 0.803   55.280  83.193  1.00 17.04 ? 1079 GLY B C     1 
ATOM   16954 O  O     . GLY B  1  1081 ? -0.052  55.032  84.062  1.00 19.42 ? 1079 GLY B O     1 
ATOM   16955 N  N     . LEU B  1  1082 ? 0.941   54.568  82.081  1.00 17.33 ? 1080 LEU B N     1 
ATOM   16956 C  CA    A LEU B  1  1082 ? 0.219   53.320  81.887  0.48 17.41 ? 1080 LEU B CA    1 
ATOM   16957 C  CA    B LEU B  1  1082 ? 0.215   53.321  81.890  0.52 17.41 ? 1080 LEU B CA    1 
ATOM   16958 C  C     . LEU B  1  1082 ? 0.465   52.397  83.072  1.00 17.79 ? 1080 LEU B C     1 
ATOM   16959 O  O     . LEU B  1  1082 ? 1.591   52.267  83.544  1.00 18.47 ? 1080 LEU B O     1 
ATOM   16960 C  CB    A LEU B  1  1082 ? 0.681   52.660  80.587  0.48 17.39 ? 1080 LEU B CB    1 
ATOM   16961 C  CB    B LEU B  1  1082 ? 0.666   52.661  80.588  0.52 17.39 ? 1080 LEU B CB    1 
ATOM   16962 C  CG    A LEU B  1  1082 ? 0.052   51.324  80.208  0.48 17.33 ? 1080 LEU B CG    1 
ATOM   16963 C  CG    B LEU B  1  1082 ? 0.091   51.306  80.185  0.52 17.34 ? 1080 LEU B CG    1 
ATOM   16964 C  CD1   A LEU B  1  1082 ? -1.444  51.441  80.225  0.48 18.81 ? 1080 LEU B CD1   1 
ATOM   16965 C  CD1   B LEU B  1  1082 ? 0.191   51.183  78.680  0.52 17.82 ? 1080 LEU B CD1   1 
ATOM   16966 C  CD2   A LEU B  1  1082 ? 0.533   50.882  78.834  0.48 18.63 ? 1080 LEU B CD2   1 
ATOM   16967 C  CD2   B LEU B  1  1082 ? 0.845   50.161  80.861  0.52 16.03 ? 1080 LEU B CD2   1 
ATOM   16968 N  N     . ASP B  1  1083 ? -0.599  51.756  83.550  1.00 17.66 ? 1081 ASP B N     1 
ATOM   16969 C  CA    . ASP B  1  1083 ? -0.509  50.980  84.784  1.00 19.92 ? 1081 ASP B CA    1 
ATOM   16970 C  C     . ASP B  1  1083 ? -1.554  49.874  84.684  1.00 21.37 ? 1081 ASP B C     1 
ATOM   16971 O  O     . ASP B  1  1083 ? -2.726  50.099  84.992  1.00 26.95 ? 1081 ASP B O     1 
ATOM   16972 C  CB    . ASP B  1  1083 ? -0.745  51.892  85.980  1.00 22.90 ? 1081 ASP B CB    1 
ATOM   16973 C  CG    . ASP B  1  1083 ? -0.625  51.178  87.308  1.00 36.21 ? 1081 ASP B CG    1 
ATOM   16974 O  OD1   . ASP B  1  1083 ? 0.036   50.127  87.373  1.00 38.40 ? 1081 ASP B OD1   1 
ATOM   16975 O  OD2   . ASP B  1  1083 ? -1.201  51.682  88.296  1.00 41.97 ? 1081 ASP B OD2   1 
ATOM   16976 N  N     . LEU B  1  1084 ? -1.126  48.695  84.243  1.00 19.45 ? 1082 LEU B N     1 
ATOM   16977 C  CA    . LEU B  1  1084 ? -2.033  47.623  83.862  1.00 19.79 ? 1082 LEU B CA    1 
ATOM   16978 C  C     . LEU B  1  1084 ? -1.809  46.427  84.769  1.00 18.62 ? 1082 LEU B C     1 
ATOM   16979 O  O     . LEU B  1  1084 ? -0.693  46.195  85.237  1.00 20.29 ? 1082 LEU B O     1 
ATOM   16980 C  CB    . LEU B  1  1084 ? -1.798  47.178  82.415  1.00 22.04 ? 1082 LEU B CB    1 
ATOM   16981 C  CG    . LEU B  1  1084 ? -2.093  48.166  81.293  1.00 25.50 ? 1082 LEU B CG    1 
ATOM   16982 C  CD1   . LEU B  1  1084 ? -1.764  47.541  79.960  1.00 27.64 ? 1082 LEU B CD1   1 
ATOM   16983 C  CD2   . LEU B  1  1084 ? -3.545  48.633  81.340  1.00 33.28 ? 1082 LEU B CD2   1 
ATOM   16984 N  N     . GLU B  1  1085 ? -2.871  45.661  84.998  1.00 19.75 ? 1083 GLU B N     1 
ATOM   16985 C  CA    . GLU B  1  1085 ? -2.720  44.316  85.526  1.00 19.21 ? 1083 GLU B CA    1 
ATOM   16986 C  C     . GLU B  1  1085 ? -2.870  43.336  84.376  1.00 20.08 ? 1083 GLU B C     1 
ATOM   16987 O  O     . GLU B  1  1085 ? -3.861  43.386  83.636  1.00 21.72 ? 1083 GLU B O     1 
ATOM   16988 C  CB    . GLU B  1  1085 ? -3.734  43.993  86.618  1.00 19.67 ? 1083 GLU B CB    1 
ATOM   16989 C  CG    . GLU B  1  1085 ? -3.467  42.580  87.158  1.00 22.00 ? 1083 GLU B CG    1 
ATOM   16990 C  CD    . GLU B  1  1085 ? -4.208  42.246  88.426  1.00 29.49 ? 1083 GLU B CD    1 
ATOM   16991 O  OE1   . GLU B  1  1085 ? -4.813  43.156  89.032  1.00 29.95 ? 1083 GLU B OE1   1 
ATOM   16992 O  OE2   . GLU B  1  1085 ? -4.173  41.055  88.816  1.00 29.87 ? 1083 GLU B OE2   1 
ATOM   16993 N  N     . LEU B  1  1086 ? -1.907  42.461  84.231  1.00 17.48 ? 1084 LEU B N     1 
ATOM   16994 C  CA    . LEU B  1  1086 ? -1.889  41.508  83.124  1.00 17.84 ? 1084 LEU B CA    1 
ATOM   16995 C  C     . LEU B  1  1086 ? -2.523  40.191  83.559  1.00 23.74 ? 1084 LEU B C     1 
ATOM   16996 O  O     . LEU B  1  1086 ? -2.332  39.757  84.699  1.00 21.01 ? 1084 LEU B O     1 
ATOM   16997 C  CB    . LEU B  1  1086 ? -0.465  41.241  82.658  1.00 20.66 ? 1084 LEU B CB    1 
ATOM   16998 C  CG    . LEU B  1  1086 ? 0.328   42.429  82.128  1.00 20.94 ? 1084 LEU B CG    1 
ATOM   16999 C  CD1   . LEU B  1  1086 ? 1.702   42.015  81.617  1.00 19.38 ? 1084 LEU B CD1   1 
ATOM   17000 C  CD2   . LEU B  1  1086 ? -0.484  43.100  81.033  1.00 22.62 ? 1084 LEU B CD2   1 
ATOM   17001 N  N     . PRO B  1  1087 ? -3.242  39.534  82.656  1.00 19.81 ? 1085 PRO B N     1 
ATOM   17002 C  CA    . PRO B  1  1087 ? -3.842  38.237  82.992  1.00 21.37 ? 1085 PRO B CA    1 
ATOM   17003 C  C     . PRO B  1  1087 ? -2.769  37.202  83.285  1.00 18.43 ? 1085 PRO B C     1 
ATOM   17004 O  O     . PRO B  1  1087 ? -1.730  37.149  82.630  1.00 22.63 ? 1085 PRO B O     1 
ATOM   17005 C  CB    . PRO B  1  1087 ? -4.636  37.874  81.732  1.00 24.26 ? 1085 PRO B CB    1 
ATOM   17006 C  CG    . PRO B  1  1087 ? -4.868  39.164  81.035  1.00 28.53 ? 1085 PRO B CG    1 
ATOM   17007 C  CD    . PRO B  1  1087 ? -3.658  40.015  81.325  1.00 23.18 ? 1085 PRO B CD    1 
ATOM   17008 N  N     . GLY B  1  1088 ? -3.035  36.378  84.286  1.00 19.15 ? 1086 GLY B N     1 
ATOM   17009 C  CA    . GLY B  1  1088 ? -2.094  35.378  84.716  1.00 18.62 ? 1086 GLY B CA    1 
ATOM   17010 C  C     . GLY B  1  1088 ? -2.734  34.457  85.725  1.00 16.25 ? 1086 GLY B C     1 
ATOM   17011 O  O     . GLY B  1  1088 ? -3.954  34.418  85.872  1.00 19.95 ? 1086 GLY B O     1 
ATOM   17012 N  N     . PRO B  1  1089 ? -1.909  33.715  86.459  1.00 18.62 ? 1087 PRO B N     1 
ATOM   17013 C  CA    . PRO B  1  1089 ? -2.437  32.748  87.423  1.00 19.37 ? 1087 PRO B CA    1 
ATOM   17014 C  C     . PRO B  1  1089 ? -3.080  33.425  88.620  1.00 18.22 ? 1087 PRO B C     1 
ATOM   17015 O  O     . PRO B  1  1089 ? -2.762  34.561  88.983  1.00 21.64 ? 1087 PRO B O     1 
ATOM   17016 C  CB    . PRO B  1  1089 ? -1.189  31.962  87.847  1.00 20.14 ? 1087 PRO B CB    1 
ATOM   17017 C  CG    . PRO B  1  1089 ? -0.061  32.959  87.668  1.00 23.82 ? 1087 PRO B CG    1 
ATOM   17018 C  CD    . PRO B  1  1089 ? -0.437  33.774  86.463  1.00 21.17 ? 1087 PRO B CD    1 
ATOM   17019 N  N     . VAL B  1  1090 ? -3.986  32.684  89.262  1.00 17.71 ? 1088 VAL B N     1 
ATOM   17020 C  CA    . VAL B  1  1090 ? -4.515  33.142  90.542  1.00 17.13 ? 1088 VAL B CA    1 
ATOM   17021 C  C     . VAL B  1  1090 ? -3.388  33.192  91.579  1.00 18.26 ? 1088 VAL B C     1 
ATOM   17022 O  O     . VAL B  1  1090 ? -2.341  32.545  91.447  1.00 18.66 ? 1088 VAL B O     1 
ATOM   17023 C  CB    . VAL B  1  1090 ? -5.654  32.235  91.019  1.00 20.43 ? 1088 VAL B CB    1 
ATOM   17024 C  CG1   . VAL B  1  1090 ? -6.747  32.174  89.959  1.00 20.37 ? 1088 VAL B CG1   1 
ATOM   17025 C  CG2   . VAL B  1  1090 ? -5.127  30.840  91.348  1.00 22.03 ? 1088 VAL B CG2   1 
ATOM   17026 N  N     . GLY B  1  1091 ? -3.614  33.971  92.632  1.00 19.47 ? 1089 GLY B N     1 
ATOM   17027 C  CA    . GLY B  1  1091 ? -2.620  34.044  93.682  1.00 19.01 ? 1089 GLY B CA    1 
ATOM   17028 C  C     . GLY B  1  1091 ? -1.422  34.886  93.342  1.00 18.30 ? 1089 GLY B C     1 
ATOM   17029 O  O     . GLY B  1  1091 ? -0.412  34.830  94.051  1.00 17.98 ? 1089 GLY B O     1 
ATOM   17030 N  N     . GLU B  1  1092 ? -1.493  35.643  92.253  1.00 18.23 ? 1090 GLU B N     1 
ATOM   17031 C  CA    . GLU B  1  1092 ? -0.407  36.493  91.816  1.00 17.61 ? 1090 GLU B CA    1 
ATOM   17032 C  C     . GLU B  1  1092 ? -1.029  37.715  91.168  1.00 17.94 ? 1090 GLU B C     1 
ATOM   17033 O  O     . GLU B  1  1092 ? -2.072  37.609  90.522  1.00 20.27 ? 1090 GLU B O     1 
ATOM   17034 C  CB    . GLU B  1  1092 ? 0.484   35.743  90.819  1.00 20.38 ? 1090 GLU B CB    1 
ATOM   17035 C  CG    . GLU B  1  1092 ? 1.929   36.082  90.855  1.00 26.81 ? 1090 GLU B CG    1 
ATOM   17036 C  CD    . GLU B  1  1092 ? 2.711   35.143  89.955  1.00 26.66 ? 1090 GLU B CD    1 
ATOM   17037 O  OE1   . GLU B  1  1092 ? 2.493   35.198  88.732  1.00 21.74 ? 1090 GLU B OE1   1 
ATOM   17038 O  OE2   . GLU B  1  1092 ? 3.495   34.321  90.476  1.00 27.54 ? 1090 GLU B OE2   1 
ATOM   17039 N  N     . ARG B  1  1093 ? -0.421  38.874  91.379  1.00 17.08 ? 1091 ARG B N     1 
ATOM   17040 C  CA    . ARG B  1  1093 ? -0.795  40.089  90.664  1.00 16.22 ? 1091 ARG B CA    1 
ATOM   17041 C  C     . ARG B  1  1093 ? 0.393   40.483  89.815  1.00 17.70 ? 1091 ARG B C     1 
ATOM   17042 O  O     . ARG B  1  1093 ? 1.498   40.684  90.332  1.00 17.51 ? 1091 ARG B O     1 
ATOM   17043 C  CB    . ARG B  1  1093 ? -1.183  41.234  91.601  1.00 20.98 ? 1091 ARG B CB    1 
ATOM   17044 C  CG    . ARG B  1  1093 ? -2.527  41.073  92.283  1.00 29.73 ? 1091 ARG B CG    1 
ATOM   17045 C  CD    . ARG B  1  1093 ? -2.846  42.282  93.190  1.00 35.30 ? 1091 ARG B CD    1 
ATOM   17046 N  NE    . ARG B  1  1093 ? -2.991  43.526  92.440  1.00 48.28 ? 1091 ARG B NE    1 
ATOM   17047 C  CZ    . ARG B  1  1093 ? -2.210  44.590  92.585  1.00 52.93 ? 1091 ARG B CZ    1 
ATOM   17048 N  NH1   . ARG B  1  1093 ? -1.212  44.602  93.454  1.00 54.45 ? 1091 ARG B NH1   1 
ATOM   17049 N  NH2   . ARG B  1  1093 ? -2.444  45.673  91.847  1.00 52.40 ? 1091 ARG B NH2   1 
ATOM   17050 N  N     . ASN B  1  1094 ? 0.170   40.573  88.511  1.00 15.60 ? 1092 ASN B N     1 
ATOM   17051 C  CA    . ASN B  1  1094 ? 1.253   40.793  87.572  1.00 16.07 ? 1092 ASN B CA    1 
ATOM   17052 C  C     . ASN B  1  1094 ? 0.990   42.133  86.912  1.00 17.61 ? 1092 ASN B C     1 
ATOM   17053 O  O     . ASN B  1  1094 ? -0.014  42.294  86.207  1.00 18.50 ? 1092 ASN B O     1 
ATOM   17054 C  CB    . ASN B  1  1094 ? 1.325   39.636  86.588  1.00 16.21 ? 1092 ASN B CB    1 
ATOM   17055 C  CG    . ASN B  1  1094 ? 1.941   38.419  87.237  1.00 15.65 ? 1092 ASN B CG    1 
ATOM   17056 O  OD1   . ASN B  1  1094 ? 3.121   38.448  87.572  1.00 17.10 ? 1092 ASN B OD1   1 
ATOM   17057 N  ND2   . ASN B  1  1094 ? 1.140   37.379  87.479  1.00 19.05 ? 1092 ASN B ND2   1 
ATOM   17058 N  N     . LEU B  1  1095 ? 1.848   43.098  87.216  1.00 16.21 ? 1093 LEU B N     1 
ATOM   17059 C  CA    . LEU B  1  1095 ? 1.629   44.492  86.874  1.00 15.78 ? 1093 LEU B CA    1 
ATOM   17060 C  C     . LEU B  1  1095 ? 2.626   44.939  85.820  1.00 15.47 ? 1093 LEU B C     1 
ATOM   17061 O  O     . LEU B  1  1095 ? 3.768   44.476  85.778  1.00 16.88 ? 1093 LEU B O     1 
ATOM   17062 C  CB    . LEU B  1  1095 ? 1.759   45.386  88.109  1.00 16.32 ? 1093 LEU B CB    1 
ATOM   17063 C  CG    . LEU B  1  1095 ? 0.891   44.891  89.279  1.00 20.39 ? 1093 LEU B CG    1 
ATOM   17064 C  CD1   . LEU B  1  1095 ? 1.047   45.836  90.472  1.00 27.52 ? 1093 LEU B CD1   1 
ATOM   17065 C  CD2   . LEU B  1  1095 ? -0.555  44.778  88.863  1.00 22.49 ? 1093 LEU B CD2   1 
ATOM   17066 N  N     . TYR B  1  1096 ? 2.176   45.860  84.973  1.00 14.61 ? 1094 TYR B N     1 
ATOM   17067 C  CA    . TYR B  1  1096 ? 3.001   46.358  83.884  1.00 16.37 ? 1094 TYR B CA    1 
ATOM   17068 C  C     . TYR B  1  1096 ? 2.785   47.857  83.825  1.00 16.17 ? 1094 TYR B C     1 
ATOM   17069 O  O     . TYR B  1  1096 ? 1.644   48.314  83.738  1.00 17.17 ? 1094 TYR B O     1 
ATOM   17070 C  CB    . TYR B  1  1096 ? 2.613   45.677  82.572  1.00 15.58 ? 1094 TYR B CB    1 
ATOM   17071 C  CG    . TYR B  1  1096 ? 3.272   46.218  81.338  1.00 15.02 ? 1094 TYR B CG    1 
ATOM   17072 C  CD1   . TYR B  1  1096 ? 4.503   45.728  80.903  1.00 18.00 ? 1094 TYR B CD1   1 
ATOM   17073 C  CD2   . TYR B  1  1096 ? 2.636   47.174  80.575  1.00 17.66 ? 1094 TYR B CD2   1 
ATOM   17074 C  CE1   . TYR B  1  1096 ? 5.102   46.208  79.751  1.00 17.39 ? 1094 TYR B CE1   1 
ATOM   17075 C  CE2   . TYR B  1  1096 ? 3.224   47.658  79.415  1.00 18.40 ? 1094 TYR B CE2   1 
ATOM   17076 C  CZ    . TYR B  1  1096 ? 4.447   47.165  79.012  1.00 18.32 ? 1094 TYR B CZ    1 
ATOM   17077 O  OH    . TYR B  1  1096 ? 5.019   47.650  77.864  1.00 17.93 ? 1094 TYR B OH    1 
ATOM   17078 N  N     . THR B  1  1097 ? 3.872   48.614  83.917  1.00 15.65 ? 1095 THR B N     1 
ATOM   17079 C  CA    . THR B  1  1097 ? 3.770   50.059  84.073  1.00 15.46 ? 1095 THR B CA    1 
ATOM   17080 C  C     . THR B  1  1097 ? 4.808   50.732  83.195  1.00 14.90 ? 1095 THR B C     1 
ATOM   17081 O  O     . THR B  1  1097 ? 5.876   50.181  82.931  1.00 17.06 ? 1095 THR B O     1 
ATOM   17082 C  CB    . THR B  1  1097 ? 3.974   50.505  85.523  1.00 18.99 ? 1095 THR B CB    1 
ATOM   17083 O  OG1   . THR B  1  1097 ? 5.262   50.086  85.975  1.00 23.65 ? 1095 THR B OG1   1 
ATOM   17084 C  CG2   . THR B  1  1097 ? 2.947   49.870  86.401  1.00 21.08 ? 1095 THR B CG2   1 
ATOM   17085 N  N     . LEU B  1  1098 ? 4.475   51.925  82.723  1.00 16.73 ? 1096 LEU B N     1 
ATOM   17086 C  CA    . LEU B  1  1098 ? 5.389   52.686  81.882  1.00 17.06 ? 1096 LEU B CA    1 
ATOM   17087 C  C     . LEU B  1  1098 ? 5.811   53.943  82.621  1.00 16.60 ? 1096 LEU B C     1 
ATOM   17088 O  O     . LEU B  1  1098 ? 4.971   54.757  83.016  1.00 16.08 ? 1096 LEU B O     1 
ATOM   17089 C  CB    . LEU B  1  1098 ? 4.762   53.047  80.540  1.00 15.23 ? 1096 LEU B CB    1 
ATOM   17090 C  CG    . LEU B  1  1098 ? 4.407   51.850  79.661  1.00 15.09 ? 1096 LEU B CG    1 
ATOM   17091 C  CD1   . LEU B  1  1098 ? 3.779   52.394  78.365  1.00 16.08 ? 1096 LEU B CD1   1 
ATOM   17092 C  CD2   . LEU B  1  1098 ? 5.604   51.005  79.369  1.00 16.54 ? 1096 LEU B CD2   1 
ATOM   17093 N  N     . HIS B  1  1099 ? 7.115   54.098  82.774  1.00 16.40 ? 1097 HIS B N     1 
ATOM   17094 C  CA    . HIS B  1  1099 ? 7.746   55.180  83.501  1.00 16.65 ? 1097 HIS B CA    1 
ATOM   17095 C  C     . HIS B  1  1099 ? 8.598   55.985  82.536  1.00 15.30 ? 1097 HIS B C     1 
ATOM   17096 O  O     . HIS B  1  1099 ? 8.817   55.586  81.393  1.00 17.66 ? 1097 HIS B O     1 
ATOM   17097 C  CB    . HIS B  1  1099 ? 8.624   54.620  84.620  1.00 19.92 ? 1097 HIS B CB    1 
ATOM   17098 C  CG    . HIS B  1  1099 ? 7.874   53.788  85.606  1.00 22.30 ? 1097 HIS B CG    1 
ATOM   17099 N  ND1   . HIS B  1  1099 ? 7.513   54.261  86.849  1.00 24.99 ? 1097 HIS B ND1   1 
ATOM   17100 C  CD2   . HIS B  1  1099 ? 7.401   52.520  85.529  1.00 23.99 ? 1097 HIS B CD2   1 
ATOM   17101 C  CE1   . HIS B  1  1099 ? 6.859   53.314  87.502  1.00 27.31 ? 1097 HIS B CE1   1 
ATOM   17102 N  NE2   . HIS B  1  1099 ? 6.779   52.248  86.724  1.00 25.67 ? 1097 HIS B NE2   1 
ATOM   17103 N  N     . ALA B  1  1100 ? 9.098   57.115  83.015  1.00 19.79 ? 1098 ALA B N     1 
ATOM   17104 C  CA    . ALA B  1  1100 ? 10.100  57.837  82.243  1.00 19.17 ? 1098 ALA B CA    1 
ATOM   17105 C  C     . ALA B  1  1100 ? 11.353  56.986  82.096  1.00 21.28 ? 1098 ALA B C     1 
ATOM   17106 O  O     . ALA B  1  1100 ? 11.677  56.170  82.968  1.00 23.17 ? 1098 ALA B O     1 
ATOM   17107 C  CB    . ALA B  1  1100 ? 10.444  59.156  82.928  1.00 21.93 ? 1098 ALA B CB    1 
ATOM   17108 N  N     . ARG B  1  1101 ? 12.049  57.153  80.967  1.00 20.99 ? 1099 ARG B N     1 
ATOM   17109 C  CA    . ARG B  1  1101 ? 13.328  56.466  80.792  1.00 18.82 ? 1099 ARG B CA    1 
ATOM   17110 C  C     . ARG B  1  1101 ? 14.407  57.051  81.694  1.00 20.56 ? 1099 ARG B C     1 
ATOM   17111 O  O     . ARG B  1  1101 ? 15.245  56.314  82.231  1.00 22.68 ? 1099 ARG B O     1 
ATOM   17112 C  CB    . ARG B  1  1101 ? 13.774  56.522  79.329  1.00 22.69 ? 1099 ARG B CB    1 
ATOM   17113 C  CG    . ARG B  1  1101 ? 13.157  55.465  78.420  1.00 24.29 ? 1099 ARG B CG    1 
ATOM   17114 C  CD    . ARG B  1  1101 ? 14.131  54.315  78.135  1.00 26.60 ? 1099 ARG B CD    1 
ATOM   17115 N  NE    . ARG B  1  1101 ? 13.523  53.271  77.309  1.00 26.87 ? 1099 ARG B NE    1 
ATOM   17116 C  CZ    . ARG B  1  1101 ? 14.198  52.311  76.691  1.00 24.40 ? 1099 ARG B CZ    1 
ATOM   17117 N  NH1   . ARG B  1  1101 ? 15.511  52.188  76.827  1.00 25.72 ? 1099 ARG B NH1   1 
ATOM   17118 N  NH2   . ARG B  1  1101 ? 13.542  51.461  75.905  1.00 32.81 ? 1099 ARG B NH2   1 
ATOM   17119 N  N     . GLY B  1  1102 ? 14.414  58.369  81.866  1.00 20.18 ? 1100 GLY B N     1 
ATOM   17120 C  CA    . GLY B  1  1102 ? 15.464  59.035  82.607  1.00 20.70 ? 1100 GLY B CA    1 
ATOM   17121 C  C     . GLY B  1  1102 ? 15.882  60.315  81.912  1.00 20.15 ? 1100 GLY B C     1 
ATOM   17122 O  O     . GLY B  1  1102 ? 15.045  61.172  81.626  1.00 19.70 ? 1100 GLY B O     1 
ATOM   17123 N  N     . ARG B  1  1103 ? 17.170  60.473  81.630  1.00 19.09 ? 1101 ARG B N     1 
ATOM   17124 C  CA    . ARG B  1  1103 ? 17.649  61.652  80.922  1.00 19.90 ? 1101 ARG B CA    1 
ATOM   17125 C  C     . ARG B  1  1103 ? 17.989  61.267  79.490  1.00 20.85 ? 1101 ARG B C     1 
ATOM   17126 O  O     . ARG B  1  1103 ? 18.770  60.340  79.262  1.00 21.96 ? 1101 ARG B O     1 
ATOM   17127 C  CB    . ARG B  1  1103 ? 18.866  62.278  81.607  1.00 22.03 ? 1101 ARG B CB    1 
ATOM   17128 C  CG    . ARG B  1  1103 ? 19.233  63.640  80.997  1.00 22.67 ? 1101 ARG B CG    1 
ATOM   17129 C  CD    . ARG B  1  1103 ? 20.288  64.440  81.811  1.00 27.29 ? 1101 ARG B CD    1 
ATOM   17130 N  NE    . ARG B  1  1103 ? 19.858  64.745  83.174  1.00 28.85 ? 1101 ARG B NE    1 
ATOM   17131 C  CZ    . ARG B  1  1103 ? 19.294  65.883  83.570  1.00 41.85 ? 1101 ARG B CZ    1 
ATOM   17132 N  NH1   . ARG B  1  1103 ? 19.042  66.880  82.721  1.00 30.68 ? 1101 ARG B NH1   1 
ATOM   17133 N  NH2   . ARG B  1  1103 ? 18.973  66.027  84.853  1.00 31.69 ? 1101 ARG B NH2   1 
ATOM   17134 N  N     . ILE B  1  1104 ? 17.385  61.965  78.535  1.00 18.06 ? 1102 ILE B N     1 
ATOM   17135 C  CA    . ILE B  1  1104 ? 17.554  61.664  77.121  1.00 18.86 ? 1102 ILE B CA    1 
ATOM   17136 C  C     . ILE B  1  1104 ? 18.569  62.635  76.542  1.00 19.89 ? 1102 ILE B C     1 
ATOM   17137 O  O     . ILE B  1  1104 ? 18.471  63.848  76.753  1.00 19.22 ? 1102 ILE B O     1 
ATOM   17138 C  CB    . ILE B  1  1104 ? 16.214  61.760  76.376  1.00 18.65 ? 1102 ILE B CB    1 
ATOM   17139 C  CG1   . ILE B  1  1104 ? 15.153  60.890  77.086  1.00 19.41 ? 1102 ILE B CG1   1 
ATOM   17140 C  CG2   . ILE B  1  1104 ? 16.395  61.387  74.892  1.00 18.56 ? 1102 ILE B CG2   1 
ATOM   17141 C  CD1   . ILE B  1  1104 ? 15.482  59.420  77.128  1.00 20.85 ? 1102 ILE B CD1   1 
ATOM   17142 N  N     . LEU B  1  1105 ? 19.547  62.102  75.820  1.00 18.18 ? 1103 LEU B N     1 
ATOM   17143 C  CA    . LEU B  1  1105 ? 20.491  62.931  75.086  1.00 20.31 ? 1103 LEU B CA    1 
ATOM   17144 C  C     . LEU B  1  1105 ? 19.811  63.476  73.831  1.00 19.59 ? 1103 LEU B C     1 
ATOM   17145 O  O     . LEU B  1  1105 ? 19.329  62.711  72.991  1.00 19.54 ? 1103 LEU B O     1 
ATOM   17146 C  CB    . LEU B  1  1105 ? 21.726  62.105  74.728  1.00 19.09 ? 1103 LEU B CB    1 
ATOM   17147 C  CG    . LEU B  1  1105 ? 22.758  62.785  73.833  1.00 21.03 ? 1103 LEU B CG    1 
ATOM   17148 C  CD1   . LEU B  1  1105 ? 23.403  63.969  74.551  1.00 21.29 ? 1103 LEU B CD1   1 
ATOM   17149 C  CD2   . LEU B  1  1105 ? 23.795  61.753  73.408  1.00 22.01 ? 1103 LEU B CD2   1 
ATOM   17150 N  N     . LEU B  1  1106 ? 19.776  64.793  73.702  1.00 19.03 ? 1104 LEU B N     1 
ATOM   17151 C  CA    . LEU B  1  1106 ? 19.193  65.447  72.544  1.00 18.43 ? 1104 LEU B CA    1 
ATOM   17152 C  C     . LEU B  1  1106 ? 20.328  65.984  71.695  1.00 19.13 ? 1104 LEU B C     1 
ATOM   17153 O  O     . LEU B  1  1106 ? 21.168  66.740  72.191  1.00 21.60 ? 1104 LEU B O     1 
ATOM   17154 C  CB    . LEU B  1  1106 ? 18.252  66.575  72.958  1.00 21.20 ? 1104 LEU B CB    1 
ATOM   17155 C  CG    . LEU B  1  1106 ? 16.778  66.235  73.119  1.00 28.58 ? 1104 LEU B CG    1 
ATOM   17156 C  CD1   . LEU B  1  1106 ? 16.564  64.924  73.830  1.00 24.55 ? 1104 LEU B CD1   1 
ATOM   17157 C  CD2   . LEU B  1  1106 ? 16.076  67.384  73.831  1.00 20.18 ? 1104 LEU B CD2   1 
ATOM   17158 N  N     . VAL B  1  1107 ? 20.355  65.579  70.432  1.00 19.67 ? 1105 VAL B N     1 
ATOM   17159 C  CA    . VAL B  1  1107 ? 21.357  66.077  69.498  1.00 20.38 ? 1105 VAL B CA    1 
ATOM   17160 C  C     . VAL B  1  1107 ? 20.603  66.768  68.371  1.00 20.47 ? 1105 VAL B C     1 
ATOM   17161 O  O     . VAL B  1  1107 ? 20.403  66.179  67.301  1.00 21.33 ? 1105 VAL B O     1 
ATOM   17162 C  CB    . VAL B  1  1107 ? 22.256  64.948  68.976  1.00 18.48 ? 1105 VAL B CB    1 
ATOM   17163 C  CG1   . VAL B  1  1107 ? 23.438  65.543  68.223  1.00 20.53 ? 1105 VAL B CG1   1 
ATOM   17164 C  CG2   . VAL B  1  1107 ? 22.737  64.075  70.127  1.00 19.57 ? 1105 VAL B CG2   1 
ATOM   17165 N  N     . PRO B  1  1108 ? 20.156  67.998  68.570  1.00 19.98 ? 1106 PRO B N     1 
ATOM   17166 C  CA    . PRO B  1  1108 ? 19.416  68.694  67.521  1.00 22.21 ? 1106 PRO B CA    1 
ATOM   17167 C  C     . PRO B  1  1108 ? 20.346  69.327  66.502  1.00 23.92 ? 1106 PRO B C     1 
ATOM   17168 O  O     . PRO B  1  1108 ? 21.539  69.525  66.737  1.00 25.53 ? 1106 PRO B O     1 
ATOM   17169 C  CB    . PRO B  1  1108 ? 18.659  69.775  68.295  1.00 22.67 ? 1106 PRO B CB    1 
ATOM   17170 C  CG    . PRO B  1  1108 ? 19.596  70.099  69.422  1.00 23.57 ? 1106 PRO B CG    1 
ATOM   17171 C  CD    . PRO B  1  1108 ? 20.217  68.782  69.815  1.00 22.08 ? 1106 PRO B CD    1 
ATOM   17172 N  N     . ALA B  1  1109 ? 19.750  69.683  65.371  1.00 22.33 ? 1107 ALA B N     1 
ATOM   17173 C  CA    . ALA B  1  1109 ? 20.403  70.496  64.358  1.00 25.54 ? 1107 ALA B CA    1 
ATOM   17174 C  C     . ALA B  1  1109 ? 19.769  71.867  64.220  1.00 29.15 ? 1107 ALA B C     1 
ATOM   17175 O  O     . ALA B  1  1109 ? 20.470  72.855  63.978  1.00 28.19 ? 1107 ALA B O     1 
ATOM   17176 C  CB    . ALA B  1  1109 ? 20.364  69.782  63.001  1.00 24.66 ? 1107 ALA B CB    1 
ATOM   17177 N  N     . THR B  1  1110 ? 18.452  71.948  64.379  1.00 23.96 ? 1108 THR B N     1 
ATOM   17178 C  CA    . THR B  1  1110 ? 17.704  73.175  64.165  1.00 24.24 ? 1108 THR B CA    1 
ATOM   17179 C  C     . THR B  1  1110 ? 16.865  73.483  65.395  1.00 24.44 ? 1108 THR B C     1 
ATOM   17180 O  O     . THR B  1  1110 ? 16.562  72.604  66.209  1.00 22.81 ? 1108 THR B O     1 
ATOM   17181 C  CB    . THR B  1  1110 ? 16.771  73.081  62.948  1.00 28.47 ? 1108 THR B CB    1 
ATOM   17182 O  OG1   . THR B  1  1110 ? 15.807  72.043  63.164  1.00 28.11 ? 1108 THR B OG1   1 
ATOM   17183 C  CG2   . THR B  1  1110 ? 17.553  72.810  61.652  1.00 26.55 ? 1108 THR B CG2   1 
ATOM   17184 N  N     . GLU B  1  1111 ? 16.463  74.750  65.500  1.00 25.40 ? 1109 GLU B N     1 
ATOM   17185 C  CA    . GLU B  1  1111 ? 15.597  75.158  66.600  1.00 25.16 ? 1109 GLU B CA    1 
ATOM   17186 C  C     . GLU B  1  1111 ? 14.300  74.357  66.610  1.00 24.77 ? 1109 GLU B C     1 
ATOM   17187 O  O     . GLU B  1  1111 ? 13.886  73.839  67.654  1.00 23.92 ? 1109 GLU B O     1 
ATOM   17188 C  CB    . GLU B  1  1111 ? 15.306  76.650  66.507  1.00 26.61 ? 1109 GLU B CB    1 
ATOM   17189 C  CG    . GLU B  1  1111 ? 14.290  77.117  67.527  1.00 28.04 ? 1109 GLU B CG    1 
ATOM   17190 C  CD    . GLU B  1  1111 ? 14.064  78.603  67.462  1.00 31.46 ? 1109 GLU B CD    1 
ATOM   17191 O  OE1   . GLU B  1  1111 ? 14.890  79.350  68.024  1.00 31.01 ? 1109 GLU B OE1   1 
ATOM   17192 O  OE2   . GLU B  1  1111 ? 13.069  79.017  66.835  1.00 32.82 ? 1109 GLU B OE2   1 
ATOM   17193 N  N     . SER B  1  1112 ? 13.641  74.244  65.455  1.00 23.68 ? 1110 SER B N     1 
ATOM   17194 C  CA    . SER B  1  1112 ? 12.396  73.485  65.407  1.00 25.60 ? 1110 SER B CA    1 
ATOM   17195 C  C     . SER B  1  1112 ? 12.635  72.026  65.764  1.00 26.03 ? 1110 SER B C     1 
ATOM   17196 O  O     . SER B  1  1112 ? 11.826  71.411  66.469  1.00 24.31 ? 1110 SER B O     1 
ATOM   17197 C  CB    . SER B  1  1112 ? 11.753  73.598  64.028  1.00 31.45 ? 1110 SER B CB    1 
ATOM   17198 O  OG    . SER B  1  1112 ? 10.540  72.866  63.987  1.00 29.33 ? 1110 SER B OG    1 
ATOM   17199 N  N     . GLY B  1  1113 ? 13.742  71.457  65.283  1.00 23.16 ? 1111 GLY B N     1 
ATOM   17200 C  CA    . GLY B  1  1113 ? 14.073  70.087  65.644  1.00 23.13 ? 1111 GLY B CA    1 
ATOM   17201 C  C     . GLY B  1  1113 ? 14.247  69.927  67.139  1.00 22.21 ? 1111 GLY B C     1 
ATOM   17202 O  O     . GLY B  1  1113 ? 13.761  68.962  67.731  1.00 22.55 ? 1111 GLY B O     1 
ATOM   17203 N  N     . LEU B  1  1114 ? 14.927  70.885  67.773  1.00 20.63 ? 1112 LEU B N     1 
ATOM   17204 C  CA    . LEU B  1  1114 ? 15.095  70.839  69.224  1.00 21.01 ? 1112 LEU B CA    1 
ATOM   17205 C  C     . LEU B  1  1114 ? 13.754  70.904  69.941  1.00 22.93 ? 1112 LEU B C     1 
ATOM   17206 O  O     . LEU B  1  1114 ? 13.530  70.179  70.918  1.00 21.33 ? 1112 LEU B O     1 
ATOM   17207 C  CB    . LEU B  1  1114 ? 15.998  71.981  69.684  1.00 22.97 ? 1112 LEU B CB    1 
ATOM   17208 C  CG    . LEU B  1  1114 ? 16.102  72.233  71.191  1.00 23.54 ? 1112 LEU B CG    1 
ATOM   17209 C  CD1   . LEU B  1  1114 ? 16.591  70.975  71.915  1.00 21.23 ? 1112 LEU B CD1   1 
ATOM   17210 C  CD2   . LEU B  1  1114 ? 17.014  73.432  71.469  1.00 28.38 ? 1112 LEU B CD2   1 
ATOM   17211 N  N     . TYR B  1  1115 ? 12.850  71.769  69.477  1.00 22.88 ? 1113 TYR B N     1 
ATOM   17212 C  CA    . TYR B  1  1115 ? 11.542  71.856  70.125  1.00 21.25 ? 1113 TYR B CA    1 
ATOM   17213 C  C     . TYR B  1  1115 ? 10.780  70.545  69.989  1.00 20.24 ? 1113 TYR B C     1 
ATOM   17214 O  O     . TYR B  1  1115 ? 10.138  70.098  70.944  1.00 22.03 ? 1113 TYR B O     1 
ATOM   17215 C  CB    . TYR B  1  1115 ? 10.710  73.002  69.546  1.00 20.94 ? 1113 TYR B CB    1 
ATOM   17216 C  CG    . TYR B  1  1115 ? 11.221  74.403  69.809  1.00 19.93 ? 1113 TYR B CG    1 
ATOM   17217 C  CD1   . TYR B  1  1115 ? 12.193  74.658  70.763  1.00 21.51 ? 1113 TYR B CD1   1 
ATOM   17218 C  CD2   . TYR B  1  1115 ? 10.722  75.473  69.085  1.00 25.84 ? 1113 TYR B CD2   1 
ATOM   17219 C  CE1   . TYR B  1  1115 ? 12.654  75.951  70.990  1.00 26.13 ? 1113 TYR B CE1   1 
ATOM   17220 C  CE2   . TYR B  1  1115 ? 11.171  76.766  69.305  1.00 27.64 ? 1113 TYR B CE2   1 
ATOM   17221 C  CZ    . TYR B  1  1115 ? 12.138  76.996  70.258  1.00 30.85 ? 1113 TYR B CZ    1 
ATOM   17222 O  OH    . TYR B  1  1115 ? 12.598  78.275  70.475  1.00 33.78 ? 1113 TYR B OH    1 
ATOM   17223 N  N     . HIS B  1  1116 ? 10.838  69.912  68.811  1.00 20.39 ? 1114 HIS B N     1 
ATOM   17224 C  CA    . HIS B  1  1116 ? 10.193  68.611  68.644  1.00 21.08 ? 1114 HIS B CA    1 
ATOM   17225 C  C     . HIS B  1  1116 ? 10.851  67.548  69.514  1.00 21.78 ? 1114 HIS B C     1 
ATOM   17226 O  O     . HIS B  1  1116 ? 10.160  66.711  70.110  1.00 21.87 ? 1114 HIS B O     1 
ATOM   17227 C  CB    . HIS B  1  1116 ? 10.219  68.170  67.181  1.00 20.98 ? 1114 HIS B CB    1 
ATOM   17228 C  CG    . HIS B  1  1116 ? 9.165   68.804  66.329  1.00 25.91 ? 1114 HIS B CG    1 
ATOM   17229 N  ND1   . HIS B  1  1116 ? 9.337   70.026  65.717  1.00 26.83 ? 1114 HIS B ND1   1 
ATOM   17230 C  CD2   . HIS B  1  1116 ? 7.937   68.367  65.957  1.00 24.28 ? 1114 HIS B CD2   1 
ATOM   17231 C  CE1   . HIS B  1  1116 ? 8.254   70.327  65.023  1.00 27.15 ? 1114 HIS B CE1   1 
ATOM   17232 N  NE2   . HIS B  1  1116 ? 7.390   69.336  65.150  1.00 28.86 ? 1114 HIS B NE2   1 
ATOM   17233 N  N     . GLN B  1  1117 ? 12.186  67.544  69.587  1.00 19.11 ? 1115 GLN B N     1 
ATOM   17234 C  CA    . GLN B  1  1117 ? 12.858  66.575  70.446  1.00 17.80 ? 1115 GLN B CA    1 
ATOM   17235 C  C     . GLN B  1  1117 ? 12.475  66.783  71.901  1.00 20.19 ? 1115 GLN B C     1 
ATOM   17236 O  O     . GLN B  1  1117 ? 12.224  65.817  72.635  1.00 18.84 ? 1115 GLN B O     1 
ATOM   17237 C  CB    . GLN B  1  1117 ? 14.375  66.680  70.298  1.00 19.93 ? 1115 GLN B CB    1 
ATOM   17238 C  CG    . GLN B  1  1117 ? 14.892  66.235  68.959  1.00 20.25 ? 1115 GLN B CG    1 
ATOM   17239 C  CD    . GLN B  1  1117 ? 16.382  66.390  68.858  1.00 18.71 ? 1115 GLN B CD    1 
ATOM   17240 O  OE1   . GLN B  1  1117 ? 16.998  67.069  69.665  1.00 20.92 ? 1115 GLN B OE1   1 
ATOM   17241 N  NE2   . GLN B  1  1117 ? 16.979  65.741  67.861  1.00 18.25 ? 1115 GLN B NE2   1 
ATOM   17242 N  N     . LEU B  1  1118 ? 12.477  68.042  72.346  1.00 19.72 ? 1116 LEU B N     1 
ATOM   17243 C  CA    . LEU B  1  1118 ? 12.067  68.351  73.708  1.00 20.27 ? 1116 LEU B CA    1 
ATOM   17244 C  C     . LEU B  1  1118 ? 10.646  67.893  73.970  1.00 21.47 ? 1116 LEU B C     1 
ATOM   17245 O  O     . LEU B  1  1118 ? 10.360  67.320  75.027  1.00 21.95 ? 1116 LEU B O     1 
ATOM   17246 C  CB    . LEU B  1  1118 ? 12.180  69.853  73.967  1.00 22.10 ? 1116 LEU B CB    1 
ATOM   17247 C  CG    . LEU B  1  1118 ? 13.523  70.359  74.458  1.00 33.31 ? 1116 LEU B CG    1 
ATOM   17248 C  CD1   . LEU B  1  1118 ? 13.509  71.878  74.442  1.00 31.05 ? 1116 LEU B CD1   1 
ATOM   17249 C  CD2   . LEU B  1  1118 ? 13.769  69.833  75.860  1.00 31.85 ? 1116 LEU B CD2   1 
ATOM   17250 N  N     . ALA B  1  1119 ? 9.740   68.145  73.023  1.00 20.43 ? 1117 ALA B N     1 
ATOM   17251 C  CA    . ALA B  1  1119 ? 8.352   67.729  73.212  1.00 21.29 ? 1117 ALA B CA    1 
ATOM   17252 C  C     . ALA B  1  1119 ? 8.269   66.228  73.427  1.00 20.02 ? 1117 ALA B C     1 
ATOM   17253 O  O     . ALA B  1  1119 ? 7.590   65.762  74.351  1.00 21.70 ? 1117 ALA B O     1 
ATOM   17254 C  CB    . ALA B  1  1119 ? 7.493   68.145  72.018  1.00 20.69 ? 1117 ALA B CB    1 
ATOM   17255 N  N     . ALA B  1  1120 ? 8.972   65.456  72.593  1.00 19.56 ? 1118 ALA B N     1 
ATOM   17256 C  CA    . ALA B  1  1120 ? 8.926   64.002  72.713  1.00 17.00 ? 1118 ALA B CA    1 
ATOM   17257 C  C     . ALA B  1  1120 ? 9.458   63.553  74.062  1.00 19.98 ? 1118 ALA B C     1 
ATOM   17258 O  O     . ALA B  1  1120 ? 8.865   62.688  74.725  1.00 18.81 ? 1118 ALA B O     1 
ATOM   17259 C  CB    . ALA B  1  1120 ? 9.738   63.353  71.589  1.00 20.27 ? 1118 ALA B CB    1 
ATOM   17260 N  N     . ALA B  1  1121 ? 10.590  64.125  74.481  1.00 17.92 ? 1119 ALA B N     1 
ATOM   17261 C  CA    . ALA B  1  1121 ? 11.218  63.698  75.726  1.00 17.68 ? 1119 ALA B CA    1 
ATOM   17262 C  C     . ALA B  1  1121 ? 10.403  64.124  76.940  1.00 16.31 ? 1119 ALA B C     1 
ATOM   17263 O  O     . ALA B  1  1121 ? 10.242  63.343  77.889  1.00 17.05 ? 1119 ALA B O     1 
ATOM   17264 C  CB    . ALA B  1  1121 ? 12.635  64.266  75.811  1.00 20.77 ? 1119 ALA B CB    1 
ATOM   17265 N  N     . LEU B  1  1122 ? 9.901   65.360  76.941  1.00 16.81 ? 1120 LEU B N     1 
ATOM   17266 C  CA    . LEU B  1  1122 ? 9.135   65.838  78.087  1.00 17.30 ? 1120 LEU B CA    1 
ATOM   17267 C  C     . LEU B  1  1122 ? 7.807   65.106  78.194  1.00 19.04 ? 1120 LEU B C     1 
ATOM   17268 O  O     . LEU B  1  1122 ? 7.366   64.785  79.304  1.00 18.33 ? 1120 LEU B O     1 
ATOM   17269 C  CB    . LEU B  1  1122 ? 8.898   67.335  77.985  1.00 17.75 ? 1120 LEU B CB    1 
ATOM   17270 C  CG    . LEU B  1  1122 ? 10.133  68.229  78.027  1.00 20.51 ? 1120 LEU B CG    1 
ATOM   17271 C  CD1   . LEU B  1  1122 ? 9.718   69.666  77.784  1.00 22.20 ? 1120 LEU B CD1   1 
ATOM   17272 C  CD2   . LEU B  1  1122 ? 10.850  68.092  79.367  1.00 21.41 ? 1120 LEU B CD2   1 
ATOM   17273 N  N     . ALA B  1  1123 ? 7.181   64.814  77.049  1.00 17.16 ? 1121 ALA B N     1 
ATOM   17274 C  CA    . ALA B  1  1123 ? 5.885   64.139  77.050  1.00 18.09 ? 1121 ALA B CA    1 
ATOM   17275 C  C     . ALA B  1  1123 ? 5.973   62.758  77.679  1.00 20.27 ? 1121 ALA B C     1 
ATOM   17276 O  O     . ALA B  1  1123 ? 4.969   62.239  78.181  1.00 19.62 ? 1121 ALA B O     1 
ATOM   17277 C  CB    . ALA B  1  1123 ? 5.347   64.017  75.623  1.00 20.47 ? 1121 ALA B CB    1 
ATOM   17278 N  N     . THR B  1  1124 ? 7.157   62.146  77.649  1.00 16.87 ? 1122 THR B N     1 
ATOM   17279 C  CA    . THR B  1  1124 ? 7.381   60.831  78.221  1.00 16.18 ? 1122 THR B CA    1 
ATOM   17280 C  C     . THR B  1  1124 ? 8.070   60.911  79.579  1.00 16.49 ? 1122 THR B C     1 
ATOM   17281 O  O     . THR B  1  1124 ? 8.602   59.910  80.058  1.00 18.78 ? 1122 THR B O     1 
ATOM   17282 C  CB    . THR B  1  1124 ? 8.168   59.966  77.231  1.00 17.43 ? 1122 THR B CB    1 
ATOM   17283 O  OG1   . THR B  1  1124 ? 9.236   60.742  76.660  1.00 16.34 ? 1122 THR B OG1   1 
ATOM   17284 C  CG2   . THR B  1  1124 ? 7.232   59.499  76.085  1.00 17.52 ? 1122 THR B CG2   1 
ATOM   17285 N  N     . GLY B  1  1125 ? 8.073   62.089  80.195  1.00 15.63 ? 1123 GLY B N     1 
ATOM   17286 C  CA    . GLY B  1  1125 ? 8.476   62.240  81.586  1.00 15.81 ? 1123 GLY B CA    1 
ATOM   17287 C  C     . GLY B  1  1125 ? 9.959   62.418  81.797  1.00 18.65 ? 1123 GLY B C     1 
ATOM   17288 O  O     . GLY B  1  1125 ? 10.411  62.414  82.947  1.00 19.12 ? 1123 GLY B O     1 
ATOM   17289 N  N     . ASN B  1  1126 ? 10.728  62.565  80.725  1.00 17.05 ? 1124 ASN B N     1 
ATOM   17290 C  CA    . ASN B  1  1126 ? 12.178  62.551  80.809  1.00 16.99 ? 1124 ASN B CA    1 
ATOM   17291 C  C     . ASN B  1  1126 ? 12.739  63.945  81.035  1.00 16.36 ? 1124 ASN B C     1 
ATOM   17292 O  O     . ASN B  1  1126 ? 12.110  64.957  80.726  1.00 18.66 ? 1124 ASN B O     1 
ATOM   17293 C  CB    . ASN B  1  1126 ? 12.773  61.970  79.532  1.00 16.90 ? 1124 ASN B CB    1 
ATOM   17294 C  CG    . ASN B  1  1126 ? 12.293  60.576  79.269  1.00 16.11 ? 1124 ASN B CG    1 
ATOM   17295 O  OD1   . ASN B  1  1126 ? 12.656  59.653  79.985  1.00 17.56 ? 1124 ASN B OD1   1 
ATOM   17296 N  ND2   . ASN B  1  1126 ? 11.469  60.411  78.247  1.00 17.00 ? 1124 ASN B ND2   1 
ATOM   17297 N  N     . SER B  1  1127 ? 13.940  63.977  81.608  1.00 19.98 ? 1125 SER B N     1 
ATOM   17298 C  CA    . SER B  1  1127 ? 14.793  65.147  81.506  1.00 17.60 ? 1125 SER B CA    1 
ATOM   17299 C  C     . SER B  1  1127 ? 15.661  65.002  80.264  1.00 19.70 ? 1125 SER B C     1 
ATOM   17300 O  O     . SER B  1  1127 ? 15.672  63.964  79.610  1.00 18.44 ? 1125 SER B O     1 
ATOM   17301 C  CB    . SER B  1  1127 ? 15.670  65.291  82.750  1.00 20.12 ? 1125 SER B CB    1 
ATOM   17302 O  OG    . SER B  1  1127 ? 16.504  64.157  82.890  1.00 25.44 ? 1125 SER B OG    1 
ATOM   17303 N  N     . VAL B  1  1128 ? 16.391  66.059  79.927  1.00 19.49 ? 1126 VAL B N     1 
ATOM   17304 C  CA    . VAL B  1  1128 ? 17.218  66.019  78.731  1.00 18.94 ? 1126 VAL B CA    1 
ATOM   17305 C  C     . VAL B  1  1128 ? 18.578  66.621  79.014  1.00 20.02 ? 1126 VAL B C     1 
ATOM   17306 O  O     . VAL B  1  1128 ? 18.740  67.475  79.890  1.00 21.38 ? 1126 VAL B O     1 
ATOM   17307 C  CB    . VAL B  1  1128 ? 16.583  66.766  77.536  1.00 18.08 ? 1126 VAL B CB    1 
ATOM   17308 C  CG1   . VAL B  1  1128 ? 15.245  66.138  77.172  1.00 20.24 ? 1126 VAL B CG1   1 
ATOM   17309 C  CG2   . VAL B  1  1128 ? 16.434  68.254  77.847  1.00 21.89 ? 1126 VAL B CG2   1 
ATOM   17310 N  N     . ALA B  1  1129 ? 19.552  66.166  78.239  1.00 18.67 ? 1127 ALA B N     1 
ATOM   17311 C  CA    . ALA B  1  1129 ? 20.836  66.830  78.081  1.00 17.88 ? 1127 ALA B CA    1 
ATOM   17312 C  C     . ALA B  1  1129 ? 20.950  67.187  76.609  1.00 19.43 ? 1127 ALA B C     1 
ATOM   17313 O  O     . ALA B  1  1129 ? 20.907  66.295  75.751  1.00 19.28 ? 1127 ALA B O     1 
ATOM   17314 C  CB    . ALA B  1  1129 ? 21.976  65.917  78.519  1.00 20.00 ? 1127 ALA B CB    1 
ATOM   17315 N  N     . ILE B  1  1130 ? 21.033  68.480  76.312  1.00 19.24 ? 1128 ILE B N     1 
ATOM   17316 C  CA    . ILE B  1  1130 ? 21.072  68.956  74.936  1.00 20.28 ? 1128 ILE B CA    1 
ATOM   17317 C  C     . ILE B  1  1130 ? 22.519  69.167  74.547  1.00 17.78 ? 1128 ILE B C     1 
ATOM   17318 O  O     . ILE B  1  1130 ? 23.284  69.811  75.282  1.00 18.78 ? 1128 ILE B O     1 
ATOM   17319 C  CB    . ILE B  1  1130 ? 20.275  70.256  74.751  1.00 20.94 ? 1128 ILE B CB    1 
ATOM   17320 C  CG1   . ILE B  1  1130 ? 18.867  70.129  75.335  1.00 23.30 ? 1128 ILE B CG1   1 
ATOM   17321 C  CG2   . ILE B  1  1130 ? 20.189  70.607  73.267  1.00 21.21 ? 1128 ILE B CG2   1 
ATOM   17322 C  CD1   . ILE B  1  1130 ? 18.137  71.455  75.376  1.00 22.47 ? 1128 ILE B CD1   1 
ATOM   17323 N  N     . ASP B  1  1131 ? 22.888  68.641  73.384  1.00 21.10 ? 1129 ASP B N     1 
ATOM   17324 C  CA    . ASP B  1  1131 ? 24.228  68.830  72.847  1.00 20.01 ? 1129 ASP B CA    1 
ATOM   17325 C  C     . ASP B  1  1131 ? 24.571  70.309  72.719  1.00 21.89 ? 1129 ASP B C     1 
ATOM   17326 O  O     . ASP B  1  1131 ? 23.975  71.024  71.907  1.00 21.40 ? 1129 ASP B O     1 
ATOM   17327 C  CB    . ASP B  1  1131 ? 24.324  68.140  71.496  1.00 20.43 ? 1129 ASP B CB    1 
ATOM   17328 C  CG    . ASP B  1  1131 ? 25.674  68.304  70.864  1.00 21.10 ? 1129 ASP B CG    1 
ATOM   17329 O  OD1   . ASP B  1  1131 ? 26.661  68.404  71.617  1.00 21.81 ? 1129 ASP B OD1   1 
ATOM   17330 O  OD2   . ASP B  1  1131 ? 25.714  68.352  69.625  1.00 24.14 ? 1129 ASP B OD2   1 
ATOM   17331 N  N     . ALA B  1  1132 ? 25.540  70.777  73.507  1.00 21.57 ? 1130 ALA B N     1 
ATOM   17332 C  CA    . ALA B  1  1132 ? 25.914  72.189  73.440  1.00 21.59 ? 1130 ALA B CA    1 
ATOM   17333 C  C     . ALA B  1  1132 ? 26.506  72.557  72.086  1.00 23.62 ? 1130 ALA B C     1 
ATOM   17334 O  O     . ALA B  1  1132 ? 26.400  73.712  71.657  1.00 24.85 ? 1130 ALA B O     1 
ATOM   17335 C  CB    . ALA B  1  1132 ? 26.897  72.530  74.557  1.00 23.30 ? 1130 ALA B CB    1 
ATOM   17336 N  N     . ALA B  1  1133 ? 27.113  71.596  71.386  1.00 24.42 ? 1131 ALA B N     1 
ATOM   17337 C  CA    . ALA B  1  1133 ? 27.703  71.917  70.092  1.00 28.00 ? 1131 ALA B CA    1 
ATOM   17338 C  C     . ALA B  1  1133 ? 26.658  72.292  69.052  1.00 26.53 ? 1131 ALA B C     1 
ATOM   17339 O  O     . ALA B  1  1133 ? 27.024  72.811  67.992  1.00 26.95 ? 1131 ALA B O     1 
ATOM   17340 C  CB    . ALA B  1  1133 ? 28.548  70.741  69.585  1.00 26.57 ? 1131 ALA B CB    1 
ATOM   17341 N  N     . SER B  1  1134 ? 25.372  72.048  69.329  1.00 23.62 ? 1132 SER B N     1 
ATOM   17342 C  CA    . SER B  1  1134 ? 24.319  72.471  68.416  1.00 23.27 ? 1132 SER B CA    1 
ATOM   17343 C  C     . SER B  1  1134 ? 24.248  73.985  68.289  1.00 21.87 ? 1132 SER B C     1 
ATOM   17344 O  O     . SER B  1  1134 ? 23.726  74.484  67.290  1.00 25.79 ? 1132 SER B O     1 
ATOM   17345 C  CB    . SER B  1  1134 ? 22.960  71.934  68.885  1.00 24.11 ? 1132 SER B CB    1 
ATOM   17346 O  OG    . SER B  1  1134 ? 22.570  72.548  70.105  1.00 22.67 ? 1132 SER B OG    1 
ATOM   17347 N  N     . GLY B  1  1135 ? 24.738  74.719  69.285  1.00 23.00 ? 1133 GLY B N     1 
ATOM   17348 C  CA    . GLY B  1  1135 ? 24.679  76.168  69.257  1.00 26.23 ? 1133 GLY B CA    1 
ATOM   17349 C  C     . GLY B  1  1135 ? 23.289  76.748  69.372  1.00 30.31 ? 1133 GLY B C     1 
ATOM   17350 O  O     . GLY B  1  1135 ? 23.079  77.906  69.004  1.00 28.17 ? 1133 GLY B O     1 
ATOM   17351 N  N     . LEU B  1  1136 ? 22.329  75.980  69.892  1.00 25.20 ? 1134 LEU B N     1 
ATOM   17352 C  CA    . LEU B  1  1136 ? 20.936  76.404  69.942  1.00 25.17 ? 1134 LEU B CA    1 
ATOM   17353 C  C     . LEU B  1  1136 ? 20.536  76.964  71.302  1.00 28.58 ? 1134 LEU B C     1 
ATOM   17354 O  O     . LEU B  1  1136 ? 19.340  77.080  71.585  1.00 28.28 ? 1134 LEU B O     1 
ATOM   17355 C  CB    . LEU B  1  1136 ? 20.027  75.236  69.562  1.00 24.53 ? 1134 LEU B CB    1 
ATOM   17356 C  CG    . LEU B  1  1136 ? 20.193  74.753  68.123  1.00 25.73 ? 1134 LEU B CG    1 
ATOM   17357 C  CD1   . LEU B  1  1136 ? 19.456  73.449  67.882  1.00 28.64 ? 1134 LEU B CD1   1 
ATOM   17358 C  CD2   . LEU B  1  1136 ? 19.689  75.834  67.161  1.00 27.30 ? 1134 LEU B CD2   1 
ATOM   17359 N  N     . GLN B  1  1137 ? 21.511  77.336  72.136  1.00 26.53 ? 1135 GLN B N     1 
ATOM   17360 C  CA    . GLN B  1  1137 ? 21.210  77.782  73.494  1.00 26.89 ? 1135 GLN B CA    1 
ATOM   17361 C  C     . GLN B  1  1137 ? 20.218  78.940  73.505  1.00 33.88 ? 1135 GLN B C     1 
ATOM   17362 O  O     . GLN B  1  1137 ? 19.347  79.010  74.381  1.00 30.34 ? 1135 GLN B O     1 
ATOM   17363 C  CB    . GLN B  1  1137 ? 22.498  78.178  74.216  1.00 34.32 ? 1135 GLN B CB    1 
ATOM   17364 C  CG    . GLN B  1  1137 ? 23.374  77.001  74.625  1.00 30.13 ? 1135 GLN B CG    1 
ATOM   17365 C  CD    . GLN B  1  1137 ? 24.307  76.538  73.517  1.00 27.96 ? 1135 GLN B CD    1 
ATOM   17366 O  OE1   . GLN B  1  1137 ? 24.182  76.945  72.365  1.00 26.84 ? 1135 GLN B OE1   1 
ATOM   17367 N  NE2   . GLN B  1  1137 ? 25.257  75.682  73.872  1.00 27.93 ? 1135 GLN B NE2   1 
ATOM   17368 N  N     . ALA B  1  1138 ? 20.319  79.846  72.533  1.00 28.36 ? 1136 ALA B N     1 
ATOM   17369 C  CA    . ALA B  1  1138 ? 19.452  81.020  72.516  1.00 32.22 ? 1136 ALA B CA    1 
ATOM   17370 C  C     . ALA B  1  1138 ? 18.001  80.660  72.241  1.00 32.63 ? 1136 ALA B C     1 
ATOM   17371 O  O     . ALA B  1  1138 ? 17.116  81.496  72.457  1.00 33.67 ? 1136 ALA B O     1 
ATOM   17372 C  CB    . ALA B  1  1138 ? 19.933  82.021  71.468  1.00 31.91 ? 1136 ALA B CB    1 
ATOM   17373 N  N     . SER B  1  1139 ? 17.741  79.446  71.767  1.00 29.36 ? 1137 SER B N     1 
ATOM   17374 C  CA    . SER B  1  1139 ? 16.389  79.030  71.426  1.00 33.05 ? 1137 SER B CA    1 
ATOM   17375 C  C     . SER B  1  1139 ? 15.546  78.723  72.653  1.00 32.53 ? 1137 SER B C     1 
ATOM   17376 O  O     . SER B  1  1139 ? 14.320  78.646  72.538  1.00 31.23 ? 1137 SER B O     1 
ATOM   17377 C  CB    . SER B  1  1139 ? 16.437  77.798  70.518  1.00 29.83 ? 1137 SER B CB    1 
ATOM   17378 O  OG    . SER B  1  1139 ? 16.893  78.150  69.220  1.00 32.17 ? 1137 SER B OG    1 
ATOM   17379 N  N     . LEU B  1  1140 ? 16.173  78.526  73.810  1.00 29.69 ? 1138 LEU B N     1 
ATOM   17380 C  CA    . LEU B  1  1140 ? 15.471  78.244  75.055  1.00 31.16 ? 1138 LEU B CA    1 
ATOM   17381 C  C     . LEU B  1  1140 ? 15.520  79.436  76.003  1.00 35.86 ? 1138 LEU B C     1 
ATOM   17382 O  O     . LEU B  1  1140 ? 15.519  79.271  77.223  1.00 38.89 ? 1138 LEU B O     1 
ATOM   17383 C  CB    . LEU B  1  1140 ? 16.037  76.994  75.727  1.00 31.91 ? 1138 LEU B CB    1 
ATOM   17384 C  CG    . LEU B  1  1140 ? 15.872  75.709  74.916  1.00 30.91 ? 1138 LEU B CG    1 
ATOM   17385 C  CD1   . LEU B  1  1140 ? 16.329  74.492  75.708  1.00 29.95 ? 1138 LEU B CD1   1 
ATOM   17386 C  CD2   . LEU B  1  1140 ? 14.433  75.541  74.442  1.00 33.83 ? 1138 LEU B CD2   1 
ATOM   17387 N  N     . LYS B  1  1141 ? 15.568  80.642  75.452  1.00 38.59 ? 1139 LYS B N     1 
ATOM   17388 C  CA    . LYS B  1  1141 ? 15.541  81.833  76.285  1.00 36.70 ? 1139 LYS B CA    1 
ATOM   17389 C  C     . LYS B  1  1141 ? 14.174  81.971  76.939  1.00 42.10 ? 1139 LYS B C     1 
ATOM   17390 O  O     . LYS B  1  1141 ? 13.139  81.773  76.295  1.00 42.28 ? 1139 LYS B O     1 
ATOM   17391 C  CB    . LYS B  1  1141 ? 15.863  83.074  75.451  1.00 36.72 ? 1139 LYS B CB    1 
ATOM   17392 N  N     . ASN B  1  1142 ? 14.179  82.283  78.238  1.00 37.97 ? 1140 ASN B N     1 
ATOM   17393 C  CA    . ASN B  1  1142 ? 12.961  82.525  79.011  1.00 38.40 ? 1140 ASN B CA    1 
ATOM   17394 C  C     . ASN B  1  1142 ? 12.107  81.270  79.155  1.00 40.10 ? 1140 ASN B C     1 
ATOM   17395 O  O     . ASN B  1  1142 ? 10.880  81.355  79.210  1.00 37.95 ? 1140 ASN B O     1 
ATOM   17396 C  CB    . ASN B  1  1142 ? 12.125  83.661  78.411  1.00 40.37 ? 1140 ASN B CB    1 
ATOM   17397 N  N     . LEU B  1  1143 ? 12.742  80.103  79.206  1.00 38.12 ? 1141 LEU B N     1 
ATOM   17398 C  CA    . LEU B  1  1143 ? 12.013  78.876  79.493  1.00 36.16 ? 1141 LEU B CA    1 
ATOM   17399 C  C     . LEU B  1  1143 ? 11.355  78.977  80.866  1.00 28.85 ? 1141 LEU B C     1 
ATOM   17400 O  O     . LEU B  1  1143 ? 11.946  79.535  81.792  1.00 36.88 ? 1141 LEU B O     1 
ATOM   17401 C  CB    . LEU B  1  1143 ? 12.957  77.672  79.486  1.00 34.02 ? 1141 LEU B CB    1 
ATOM   17402 C  CG    . LEU B  1  1143 ? 13.055  76.673  78.345  1.00 40.22 ? 1141 LEU B CG    1 
ATOM   17403 C  CD1   . LEU B  1  1143 ? 13.820  75.473  78.865  1.00 30.21 ? 1141 LEU B CD1   1 
ATOM   17404 C  CD2   . LEU B  1  1143 ? 11.695  76.261  77.814  1.00 34.63 ? 1141 LEU B CD2   1 
ATOM   17405 N  N     . PRO B  1  1144 ? 10.150  78.437  81.041  1.00 33.87 ? 1142 PRO B N     1 
ATOM   17406 C  CA    . PRO B  1  1144 ? 9.613   78.294  82.400  1.00 36.67 ? 1142 PRO B CA    1 
ATOM   17407 C  C     . PRO B  1  1144 ? 10.562  77.471  83.256  1.00 35.54 ? 1142 PRO B C     1 
ATOM   17408 O  O     . PRO B  1  1144 ? 11.173  76.507  82.784  1.00 30.52 ? 1142 PRO B O     1 
ATOM   17409 C  CB    . PRO B  1  1144 ? 8.278   77.566  82.187  1.00 36.85 ? 1142 PRO B CB    1 
ATOM   17410 C  CG    . PRO B  1  1144 ? 7.935   77.786  80.748  1.00 39.38 ? 1142 PRO B CG    1 
ATOM   17411 C  CD    . PRO B  1  1144 ? 9.244   77.883  80.021  1.00 33.56 ? 1142 PRO B CD    1 
ATOM   17412 N  N     . GLN B  1  1145 ? 10.682  77.859  84.527  1.00 37.53 ? 1143 GLN B N     1 
ATOM   17413 C  CA    . GLN B  1  1145 ? 11.564  77.133  85.435  1.00 32.24 ? 1143 GLN B CA    1 
ATOM   17414 C  C     . GLN B  1  1145 ? 11.193  75.659  85.514  1.00 32.94 ? 1143 GLN B C     1 
ATOM   17415 O  O     . GLN B  1  1145 ? 12.072  74.811  85.686  1.00 28.35 ? 1143 GLN B O     1 
ATOM   17416 C  CB    . GLN B  1  1145 ? 11.535  77.762  86.831  1.00 36.79 ? 1143 GLN B CB    1 
ATOM   17417 N  N     . THR B  1  1146 ? 9.904   75.332  85.383  1.00 31.30 ? 1144 THR B N     1 
ATOM   17418 C  CA    . THR B  1  1146 ? 9.504   73.928  85.410  1.00 34.06 ? 1144 THR B CA    1 
ATOM   17419 C  C     . THR B  1  1146 ? 10.178  73.149  84.295  1.00 28.72 ? 1144 THR B C     1 
ATOM   17420 O  O     . THR B  1  1146 ? 10.631  72.016  84.500  1.00 32.37 ? 1144 THR B O     1 
ATOM   17421 C  CB    . THR B  1  1146 ? 7.989   73.796  85.279  1.00 33.61 ? 1144 THR B CB    1 
ATOM   17422 O  OG1   . THR B  1  1146 ? 7.547   74.584  84.169  1.00 37.32 ? 1144 THR B OG1   1 
ATOM   17423 C  CG2   . THR B  1  1146 ? 7.297   74.261  86.549  1.00 40.08 ? 1144 THR B CG2   1 
ATOM   17424 N  N     . VAL B  1  1147 ? 10.252  73.742  83.107  1.00 27.30 ? 1145 VAL B N     1 
ATOM   17425 C  CA    . VAL B  1  1147 ? 10.922  73.073  82.001  1.00 24.32 ? 1145 VAL B CA    1 
ATOM   17426 C  C     . VAL B  1  1147 ? 12.428  73.150  82.174  1.00 25.30 ? 1145 VAL B C     1 
ATOM   17427 O  O     . VAL B  1  1147 ? 13.137  72.163  81.960  1.00 26.03 ? 1145 VAL B O     1 
ATOM   17428 C  CB    . VAL B  1  1147 ? 10.480  73.676  80.657  1.00 22.54 ? 1145 VAL B CB    1 
ATOM   17429 C  CG1   . VAL B  1  1147 ? 11.045  72.844  79.497  1.00 26.99 ? 1145 VAL B CG1   1 
ATOM   17430 C  CG2   . VAL B  1  1147 ? 8.956   73.768  80.581  1.00 26.53 ? 1145 VAL B CG2   1 
ATOM   17431 N  N     . GLY B  1  1148 ? 12.937  74.321  82.569  1.00 28.30 ? 1146 GLY B N     1 
ATOM   17432 C  CA    . GLY B  1  1148 ? 14.374  74.473  82.738  1.00 27.66 ? 1146 GLY B CA    1 
ATOM   17433 C  C     . GLY B  1  1148 ? 14.973  73.470  83.703  1.00 25.95 ? 1146 GLY B C     1 
ATOM   17434 O  O     . GLY B  1  1148 ? 16.105  73.020  83.514  1.00 28.88 ? 1146 GLY B O     1 
ATOM   17435 N  N     . LEU B  1  1149 ? 14.227  73.103  84.751  1.00 27.34 ? 1147 LEU B N     1 
ATOM   17436 C  CA    . LEU B  1  1149 ? 14.714  72.118  85.711  1.00 32.86 ? 1147 LEU B CA    1 
ATOM   17437 C  C     . LEU B  1  1149 ? 14.997  70.775  85.064  1.00 28.41 ? 1147 LEU B C     1 
ATOM   17438 O  O     . LEU B  1  1149 ? 15.777  69.985  85.608  1.00 30.12 ? 1147 LEU B O     1 
ATOM   17439 C  CB    . LEU B  1  1149 ? 13.702  71.911  86.841  1.00 37.78 ? 1147 LEU B CB    1 
ATOM   17440 C  CG    . LEU B  1  1149 ? 13.456  73.066  87.809  1.00 44.62 ? 1147 LEU B CG    1 
ATOM   17441 C  CD1   . LEU B  1  1149 ? 12.659  72.578  89.015  1.00 43.47 ? 1147 LEU B CD1   1 
ATOM   17442 C  CD2   . LEU B  1  1149 ? 14.771  73.706  88.227  1.00 48.24 ? 1147 LEU B CD2   1 
ATOM   17443 N  N     . ARG B  1  1150 ? 14.365  70.494  83.930  1.00 24.13 ? 1148 ARG B N     1 
ATOM   17444 C  CA    . ARG B  1  1150 ? 14.530  69.232  83.225  1.00 26.65 ? 1148 ARG B CA    1 
ATOM   17445 C  C     . ARG B  1  1150 ? 15.557  69.307  82.115  1.00 22.30 ? 1148 ARG B C     1 
ATOM   17446 O  O     . ARG B  1  1150 ? 15.792  68.298  81.441  1.00 21.06 ? 1148 ARG B O     1 
ATOM   17447 C  CB    . ARG B  1  1150 ? 13.200  68.784  82.632  1.00 24.61 ? 1148 ARG B CB    1 
ATOM   17448 C  CG    . ARG B  1  1150 ? 12.247  68.223  83.645  1.00 26.26 ? 1148 ARG B CG    1 
ATOM   17449 C  CD    . ARG B  1  1150 ? 11.635  66.975  83.093  1.00 26.97 ? 1148 ARG B CD    1 
ATOM   17450 N  NE    . ARG B  1  1150 ? 10.431  66.605  83.819  1.00 26.28 ? 1148 ARG B NE    1 
ATOM   17451 C  CZ    . ARG B  1  1150 ? 9.363   66.072  83.248  1.00 27.01 ? 1148 ARG B CZ    1 
ATOM   17452 N  NH1   . ARG B  1  1150 ? 9.335   65.801  81.947  1.00 23.58 ? 1148 ARG B NH1   1 
ATOM   17453 N  NH2   . ARG B  1  1150 ? 8.297   65.810  83.996  1.00 22.84 ? 1148 ARG B NH2   1 
ATOM   17454 N  N     . VAL B  1  1151 ? 16.153  70.475  81.899  1.00 26.55 ? 1149 VAL B N     1 
ATOM   17455 C  CA    . VAL B  1  1151 ? 16.993  70.739  80.740  1.00 24.39 ? 1149 VAL B CA    1 
ATOM   17456 C  C     . VAL B  1  1151 ? 18.403  71.024  81.214  1.00 24.94 ? 1149 VAL B C     1 
ATOM   17457 O  O     . VAL B  1  1151 ? 18.619  71.894  82.062  1.00 27.32 ? 1149 VAL B O     1 
ATOM   17458 C  CB    . VAL B  1  1151 ? 16.467  71.923  79.911  1.00 25.24 ? 1149 VAL B CB    1 
ATOM   17459 C  CG1   . VAL B  1  1151 ? 17.509  72.346  78.854  1.00 29.09 ? 1149 VAL B CG1   1 
ATOM   17460 C  CG2   . VAL B  1  1151 ? 15.153  71.576  79.245  1.00 25.45 ? 1149 VAL B CG2   1 
ATOM   17461 N  N     . SER B  1  1152 ? 19.360  70.294  80.668  1.00 23.48 ? 1150 SER B N     1 
ATOM   17462 C  CA    A SER B  1  1152 ? 20.755  70.651  80.836  0.62 23.20 ? 1150 SER B CA    1 
ATOM   17463 C  CA    B SER B  1  1152 ? 20.770  70.593  80.842  0.38 23.28 ? 1150 SER B CA    1 
ATOM   17464 C  C     . SER B  1  1152 ? 21.401  70.679  79.462  1.00 21.58 ? 1150 SER B C     1 
ATOM   17465 O  O     . SER B  1  1152 ? 20.864  70.155  78.485  1.00 23.98 ? 1150 SER B O     1 
ATOM   17466 C  CB    A SER B  1  1152 ? 21.489  69.678  81.760  0.62 26.87 ? 1150 SER B CB    1 
ATOM   17467 C  CB    B SER B  1  1152 ? 21.480  69.529  81.695  0.38 26.69 ? 1150 SER B CB    1 
ATOM   17468 O  OG    A SER B  1  1152 ? 21.428  68.373  81.233  0.62 24.95 ? 1150 SER B OG    1 
ATOM   17469 O  OG    B SER B  1  1152 ? 20.870  69.401  82.969  0.38 24.87 ? 1150 SER B OG    1 
ATOM   17470 N  N     . TRP B  1  1153 ? 22.537  71.345  79.386  1.00 22.05 ? 1151 TRP B N     1 
ATOM   17471 C  CA    . TRP B  1  1153 ? 23.298  71.426  78.155  1.00 21.57 ? 1151 TRP B CA    1 
ATOM   17472 C  C     . TRP B  1  1153 ? 24.595  70.675  78.393  1.00 25.14 ? 1151 TRP B C     1 
ATOM   17473 O  O     . TRP B  1  1153 ? 25.207  70.813  79.458  1.00 25.98 ? 1151 TRP B O     1 
ATOM   17474 C  CB    . TRP B  1  1153 ? 23.559  72.878  77.764  1.00 24.72 ? 1151 TRP B CB    1 
ATOM   17475 C  CG    . TRP B  1  1153 ? 22.312  73.581  77.303  1.00 24.51 ? 1151 TRP B CG    1 
ATOM   17476 C  CD1   . TRP B  1  1153 ? 21.385  74.230  78.087  1.00 24.96 ? 1151 TRP B CD1   1 
ATOM   17477 C  CD2   . TRP B  1  1153 ? 21.866  73.724  75.954  1.00 24.25 ? 1151 TRP B CD2   1 
ATOM   17478 N  NE1   . TRP B  1  1153 ? 20.391  74.756  77.297  1.00 25.40 ? 1151 TRP B NE1   1 
ATOM   17479 C  CE2   . TRP B  1  1153 ? 20.662  74.460  75.985  1.00 24.47 ? 1151 TRP B CE2   1 
ATOM   17480 C  CE3   . TRP B  1  1153 ? 22.363  73.295  74.720  1.00 22.52 ? 1151 TRP B CE3   1 
ATOM   17481 C  CZ2   . TRP B  1  1153 ? 19.956  74.780  74.825  1.00 25.38 ? 1151 TRP B CZ2   1 
ATOM   17482 C  CZ3   . TRP B  1  1153 ? 21.662  73.619  73.574  1.00 24.03 ? 1151 TRP B CZ3   1 
ATOM   17483 C  CH2   . TRP B  1  1153 ? 20.468  74.349  73.637  1.00 27.50 ? 1151 TRP B CH2   1 
ATOM   17484 N  N     . SER B  1  1154 ? 24.986  69.845  77.435  1.00 20.96 ? 1152 SER B N     1 
ATOM   17485 C  CA    . SER B  1  1154 ? 26.148  68.990  77.625  1.00 22.09 ? 1152 SER B CA    1 
ATOM   17486 C  C     . SER B  1  1154 ? 27.213  69.326  76.602  1.00 22.23 ? 1152 SER B C     1 
ATOM   17487 O  O     . SER B  1  1154 ? 26.964  69.264  75.394  1.00 21.94 ? 1152 SER B O     1 
ATOM   17488 C  CB    . SER B  1  1154 ? 25.788  67.515  77.521  1.00 24.37 ? 1152 SER B CB    1 
ATOM   17489 O  OG    . SER B  1  1154 ? 26.970  66.758  77.691  1.00 23.16 ? 1152 SER B OG    1 
ATOM   17490 N  N     . LYS B  1  1155 ? 28.396  69.689  77.093  1.00 22.54 ? 1153 LYS B N     1 
ATOM   17491 C  CA    . LYS B  1  1155 ? 29.584  69.799  76.267  1.00 25.21 ? 1153 LYS B CA    1 
ATOM   17492 C  C     . LYS B  1  1155 ? 30.453  68.553  76.373  1.00 26.67 ? 1153 LYS B C     1 
ATOM   17493 O  O     . LYS B  1  1155 ? 31.585  68.547  75.882  1.00 27.16 ? 1153 LYS B O     1 
ATOM   17494 C  CB    . LYS B  1  1155 ? 30.384  71.041  76.667  1.00 28.16 ? 1153 LYS B CB    1 
ATOM   17495 N  N     . ASP B  1  1156 ? 29.943  67.502  77.009  1.00 20.28 ? 1154 ASP B N     1 
ATOM   17496 C  CA    . ASP B  1  1156 ? 30.748  66.311  77.288  1.00 21.29 ? 1154 ASP B CA    1 
ATOM   17497 C  C     . ASP B  1  1156 ? 29.752  65.174  77.538  1.00 20.50 ? 1154 ASP B C     1 
ATOM   17498 O  O     . ASP B  1  1156 ? 29.377  64.915  78.680  1.00 21.01 ? 1154 ASP B O     1 
ATOM   17499 C  CB    . ASP B  1  1156 ? 31.658  66.529  78.477  1.00 21.77 ? 1154 ASP B CB    1 
ATOM   17500 C  CG    . ASP B  1  1156 ? 32.682  65.421  78.652  1.00 19.11 ? 1154 ASP B CG    1 
ATOM   17501 O  OD1   . ASP B  1  1156 ? 32.410  64.272  78.242  1.00 21.04 ? 1154 ASP B OD1   1 
ATOM   17502 O  OD2   . ASP B  1  1156 ? 33.751  65.719  79.213  1.00 22.87 ? 1154 ASP B OD2   1 
ATOM   17503 N  N     . TRP B  1  1157 ? 29.344  64.505  76.457  1.00 17.53 ? 1155 TRP B N     1 
ATOM   17504 C  CA    . TRP B  1  1157 ? 28.278  63.513  76.578  1.00 20.51 ? 1155 TRP B CA    1 
ATOM   17505 C  C     . TRP B  1  1157 ? 28.693  62.371  77.487  1.00 23.09 ? 1155 TRP B C     1 
ATOM   17506 O  O     . TRP B  1  1157 ? 27.891  61.877  78.285  1.00 21.48 ? 1155 TRP B O     1 
ATOM   17507 C  CB    . TRP B  1  1157 ? 27.885  62.951  75.216  1.00 20.10 ? 1155 TRP B CB    1 
ATOM   17508 C  CG    . TRP B  1  1157 ? 27.431  63.943  74.196  1.00 19.99 ? 1155 TRP B CG    1 
ATOM   17509 C  CD1   . TRP B  1  1157 ? 27.179  65.272  74.376  1.00 18.89 ? 1155 TRP B CD1   1 
ATOM   17510 C  CD2   . TRP B  1  1157 ? 27.174  63.667  72.820  1.00 19.60 ? 1155 TRP B CD2   1 
ATOM   17511 N  NE1   . TRP B  1  1157 ? 26.797  65.845  73.186  1.00 21.10 ? 1155 TRP B NE1   1 
ATOM   17512 C  CE2   . TRP B  1  1157 ? 26.782  64.874  72.215  1.00 20.00 ? 1155 TRP B CE2   1 
ATOM   17513 C  CE3   . TRP B  1  1157 ? 27.248  62.504  72.031  1.00 18.44 ? 1155 TRP B CE3   1 
ATOM   17514 C  CZ2   . TRP B  1  1157 ? 26.462  64.960  70.863  1.00 22.88 ? 1155 TRP B CZ2   1 
ATOM   17515 C  CZ3   . TRP B  1  1157 ? 26.923  62.586  70.702  1.00 21.84 ? 1155 TRP B CZ3   1 
ATOM   17516 C  CH2   . TRP B  1  1157 ? 26.533  63.805  70.122  1.00 23.90 ? 1155 TRP B CH2   1 
ATOM   17517 N  N     . ALA B  1  1158 ? 29.944  61.927  77.380  1.00 20.40 ? 1156 ALA B N     1 
ATOM   17518 C  CA    . ALA B  1  1158 ? 30.328  60.769  78.167  1.00 20.89 ? 1156 ALA B CA    1 
ATOM   17519 C  C     . ALA B  1  1158 ? 30.399  61.099  79.644  1.00 22.12 ? 1156 ALA B C     1 
ATOM   17520 O  O     . ALA B  1  1158 ? 30.096  60.240  80.476  1.00 24.73 ? 1156 ALA B O     1 
ATOM   17521 C  CB    . ALA B  1  1158 ? 31.666  60.214  77.694  1.00 18.50 ? 1156 ALA B CB    1 
ATOM   17522 N  N     . ALA B  1  1159 ? 30.792  62.327  79.992  1.00 20.05 ? 1157 ALA B N     1 
ATOM   17523 C  CA    . ALA B  1  1159 ? 30.883  62.686  81.399  1.00 23.38 ? 1157 ALA B CA    1 
ATOM   17524 C  C     . ALA B  1  1159 ? 29.517  62.978  82.003  1.00 24.55 ? 1157 ALA B C     1 
ATOM   17525 O  O     . ALA B  1  1159 ? 29.335  62.818  83.211  1.00 23.32 ? 1157 ALA B O     1 
ATOM   17526 C  CB    . ALA B  1  1159 ? 31.797  63.896  81.578  1.00 22.11 ? 1157 ALA B CB    1 
ATOM   17527 N  N     . ASP B  1  1160 ? 28.552  63.385  81.186  1.00 22.22 ? 1158 ASP B N     1 
ATOM   17528 C  CA    . ASP B  1  1160 ? 27.271  63.869  81.679  1.00 22.99 ? 1158 ASP B CA    1 
ATOM   17529 C  C     . ASP B  1  1160 ? 26.200  62.792  81.713  1.00 23.54 ? 1158 ASP B C     1 
ATOM   17530 O  O     . ASP B  1  1160 ? 25.082  63.065  82.169  1.00 27.36 ? 1158 ASP B O     1 
ATOM   17531 C  CB    . ASP B  1  1160 ? 26.810  65.050  80.824  1.00 20.34 ? 1158 ASP B CB    1 
ATOM   17532 C  CG    . ASP B  1  1160 ? 27.682  66.275  81.019  1.00 24.46 ? 1158 ASP B CG    1 
ATOM   17533 O  OD1   . ASP B  1  1160 ? 28.491  66.288  81.978  1.00 29.82 ? 1158 ASP B OD1   1 
ATOM   17534 O  OD2   . ASP B  1  1160 ? 27.581  67.218  80.211  1.00 26.67 ? 1158 ASP B OD2   1 
ATOM   17535 N  N     . GLY B  1  1161 ? 26.507  61.591  81.237  1.00 19.79 ? 1159 GLY B N     1 
ATOM   17536 C  CA    . GLY B  1  1161 ? 25.595  60.478  81.327  1.00 21.12 ? 1159 GLY B CA    1 
ATOM   17537 C  C     . GLY B  1  1161 ? 25.598  59.869  82.716  1.00 27.29 ? 1159 GLY B C     1 
ATOM   17538 O  O     . GLY B  1  1161 ? 26.147  60.432  83.666  1.00 28.64 ? 1159 GLY B O     1 
ATOM   17539 N  N     . PRO B  1  1162 ? 24.994  58.690  82.859  1.00 30.07 ? 1160 PRO B N     1 
ATOM   17540 C  CA    . PRO B  1  1162 ? 24.395  57.880  81.803  1.00 23.82 ? 1160 PRO B CA    1 
ATOM   17541 C  C     . PRO B  1  1162 ? 23.068  58.443  81.344  1.00 25.09 ? 1160 PRO B C     1 
ATOM   17542 O  O     . PRO B  1  1162 ? 22.261  58.974  82.101  1.00 25.65 ? 1160 PRO B O     1 
ATOM   17543 C  CB    . PRO B  1  1162 ? 24.229  56.512  82.481  1.00 31.55 ? 1160 PRO B CB    1 
ATOM   17544 C  CG    . PRO B  1  1162 ? 23.924  56.872  83.913  1.00 28.91 ? 1160 PRO B CG    1 
ATOM   17545 C  CD    . PRO B  1  1162 ? 24.793  58.086  84.192  1.00 33.19 ? 1160 PRO B CD    1 
ATOM   17546 N  N     . PHE B  1  1163 ? 22.834  58.341  80.052  1.00 20.61 ? 1161 PHE B N     1 
ATOM   17547 C  CA    . PHE B  1  1163 ? 21.538  58.662  79.489  1.00 18.75 ? 1161 PHE B CA    1 
ATOM   17548 C  C     . PHE B  1  1163 ? 20.728  57.387  79.336  1.00 19.04 ? 1161 PHE B C     1 
ATOM   17549 O  O     . PHE B  1  1163 ? 21.210  56.278  79.583  1.00 20.42 ? 1161 PHE B O     1 
ATOM   17550 C  CB    . PHE B  1  1163 ? 21.727  59.404  78.166  1.00 20.05 ? 1161 PHE B CB    1 
ATOM   17551 C  CG    . PHE B  1  1163 ? 22.619  60.605  78.301  1.00 21.35 ? 1161 PHE B CG    1 
ATOM   17552 C  CD1   . PHE B  1  1163 ? 22.256  61.653  79.137  1.00 24.00 ? 1161 PHE B CD1   1 
ATOM   17553 C  CD2   . PHE B  1  1163 ? 23.828  60.678  77.628  1.00 21.39 ? 1161 PHE B CD2   1 
ATOM   17554 C  CE1   . PHE B  1  1163 ? 23.069  62.754  79.303  1.00 23.41 ? 1161 PHE B CE1   1 
ATOM   17555 C  CE2   . PHE B  1  1163 ? 24.650  61.795  77.776  1.00 21.42 ? 1161 PHE B CE2   1 
ATOM   17556 C  CZ    . PHE B  1  1163 ? 24.266  62.839  78.617  1.00 22.22 ? 1161 PHE B CZ    1 
ATOM   17557 N  N     . ALA B  1  1164 ? 19.463  57.555  78.974  1.00 21.17 ? 1162 ALA B N     1 
ATOM   17558 C  CA    . ALA B  1  1164 ? 18.574  56.420  78.777  1.00 21.34 ? 1162 ALA B CA    1 
ATOM   17559 C  C     . ALA B  1  1164 ? 17.985  56.392  77.376  1.00 21.98 ? 1162 ALA B C     1 
ATOM   17560 O  O     . ALA B  1  1164 ? 17.011  55.672  77.133  1.00 25.63 ? 1162 ALA B O     1 
ATOM   17561 C  CB    . ALA B  1  1164 ? 17.452  56.440  79.823  1.00 24.44 ? 1162 ALA B CB    1 
ATOM   17562 N  N     . GLY B  1  1165 ? 18.547  57.157  76.454  1.00 18.62 ? 1163 GLY B N     1 
ATOM   17563 C  CA    . GLY B  1  1165 ? 18.070  57.214  75.089  1.00 20.79 ? 1163 GLY B CA    1 
ATOM   17564 C  C     . GLY B  1  1165 ? 18.651  58.434  74.420  1.00 18.58 ? 1163 GLY B C     1 
ATOM   17565 O  O     . GLY B  1  1165 ? 19.273  59.281  75.055  1.00 18.51 ? 1163 GLY B O     1 
ATOM   17566 N  N     . ALA B  1  1166 ? 18.438  58.523  73.114  1.00 17.54 ? 1164 ALA B N     1 
ATOM   17567 C  CA    . ALA B  1  1166 ? 18.978  59.659  72.392  1.00 19.32 ? 1164 ALA B CA    1 
ATOM   17568 C  C     . ALA B  1  1166 ? 18.077  59.974  71.220  1.00 19.77 ? 1164 ALA B C     1 
ATOM   17569 O  O     . ALA B  1  1166 ? 17.554  59.068  70.571  1.00 20.07 ? 1164 ALA B O     1 
ATOM   17570 C  CB    . ALA B  1  1166 ? 20.398  59.380  71.906  1.00 18.59 ? 1164 ALA B CB    1 
ATOM   17571 N  N     . LEU B  1  1167 ? 17.869  61.264  70.983  1.00 17.47 ? 1165 LEU B N     1 
ATOM   17572 C  CA    . LEU B  1  1167 ? 17.161  61.746  69.809  1.00 17.70 ? 1165 LEU B CA    1 
ATOM   17573 C  C     . LEU B  1  1167 ? 18.142  62.565  68.991  1.00 20.40 ? 1165 LEU B C     1 
ATOM   17574 O  O     . LEU B  1  1167 ? 18.820  63.433  69.538  1.00 19.89 ? 1165 LEU B O     1 
ATOM   17575 C  CB    . LEU B  1  1167 ? 15.957  62.596  70.191  1.00 18.61 ? 1165 LEU B CB    1 
ATOM   17576 C  CG    . LEU B  1  1167 ? 14.947  61.908  71.105  1.00 16.89 ? 1165 LEU B CG    1 
ATOM   17577 C  CD1   . LEU B  1  1167 ? 13.863  62.926  71.473  1.00 19.85 ? 1165 LEU B CD1   1 
ATOM   17578 C  CD2   . LEU B  1  1167 ? 14.328  60.709  70.391  1.00 21.11 ? 1165 LEU B CD2   1 
ATOM   17579 N  N     . VAL B  1  1168 ? 18.216  62.289  67.693  1.00 17.59 ? 1166 VAL B N     1 
ATOM   17580 C  CA    . VAL B  1  1168 ? 19.223  62.886  66.825  1.00 21.45 ? 1166 VAL B CA    1 
ATOM   17581 C  C     . VAL B  1  1168 ? 18.526  63.487  65.616  1.00 20.24 ? 1166 VAL B C     1 
ATOM   17582 O  O     . VAL B  1  1168 ? 17.639  62.862  65.025  1.00 21.00 ? 1166 VAL B O     1 
ATOM   17583 C  CB    . VAL B  1  1168 ? 20.270  61.844  66.388  1.00 20.80 ? 1166 VAL B CB    1 
ATOM   17584 C  CG1   . VAL B  1  1168 ? 21.333  62.493  65.496  1.00 21.25 ? 1166 VAL B CG1   1 
ATOM   17585 C  CG2   . VAL B  1  1168 ? 20.906  61.177  67.614  1.00 21.32 ? 1166 VAL B CG2   1 
ATOM   17586 N  N     . GLU B  1  1169 ? 18.924  64.700  65.251  1.00 21.13 ? 1167 GLU B N     1 
ATOM   17587 C  CA    . GLU B  1  1169 ? 18.437  65.370  64.054  1.00 20.55 ? 1167 GLU B CA    1 
ATOM   17588 C  C     . GLU B  1  1169 ? 19.622  65.654  63.141  1.00 21.93 ? 1167 GLU B C     1 
ATOM   17589 O  O     . GLU B  1  1169 ? 20.639  66.167  63.602  1.00 24.44 ? 1167 GLU B O     1 
ATOM   17590 C  CB    . GLU B  1  1169 ? 17.739  66.681  64.403  1.00 21.56 ? 1167 GLU B CB    1 
ATOM   17591 C  CG    . GLU B  1  1169 ? 17.288  67.470  63.190  1.00 23.13 ? 1167 GLU B CG    1 
ATOM   17592 C  CD    . GLU B  1  1169 ? 16.886  68.882  63.536  1.00 26.10 ? 1167 GLU B CD    1 
ATOM   17593 O  OE1   . GLU B  1  1169 ? 17.100  69.318  64.689  1.00 22.82 ? 1167 GLU B OE1   1 
ATOM   17594 O  OE2   . GLU B  1  1169 ? 16.353  69.567  62.643  1.00 26.65 ? 1167 GLU B OE2   1 
ATOM   17595 N  N     . GLY B  1  1170 ? 19.493  65.325  61.865  1.00 24.16 ? 1168 GLY B N     1 
ATOM   17596 C  CA    . GLY B  1  1170 ? 20.541  65.656  60.920  1.00 22.72 ? 1168 GLY B CA    1 
ATOM   17597 C  C     . GLY B  1  1170 ? 20.402  64.868  59.638  1.00 24.72 ? 1168 GLY B C     1 
ATOM   17598 O  O     . GLY B  1  1170 ? 19.500  64.047  59.483  1.00 24.19 ? 1168 GLY B O     1 
ATOM   17599 N  N     . ASP B  1  1171 ? 21.315  65.158  58.703  1.00 26.68 ? 1169 ASP B N     1 
ATOM   17600 C  CA    . ASP B  1  1171 ? 21.351  64.381  57.475  1.00 26.51 ? 1169 ASP B CA    1 
ATOM   17601 C  C     . ASP B  1  1171 ? 22.068  63.060  57.737  1.00 29.82 ? 1169 ASP B C     1 
ATOM   17602 O  O     . ASP B  1  1171 ? 22.529  62.787  58.847  1.00 25.77 ? 1169 ASP B O     1 
ATOM   17603 C  CB    . ASP B  1  1171 ? 21.983  65.176  56.324  1.00 27.95 ? 1169 ASP B CB    1 
ATOM   17604 C  CG    . ASP B  1  1171 ? 23.468  65.496  56.530  1.00 34.16 ? 1169 ASP B CG    1 
ATOM   17605 O  OD1   . ASP B  1  1171 ? 24.101  65.079  57.520  1.00 29.53 ? 1169 ASP B OD1   1 
ATOM   17606 O  OD2   . ASP B  1  1171 ? 24.024  66.204  55.658  1.00 40.30 ? 1169 ASP B OD2   1 
ATOM   17607 N  N     . ALA B  1  1172 ? 22.156  62.223  56.704  1.00 27.91 ? 1170 ALA B N     1 
ATOM   17608 C  CA    . ALA B  1  1172 ? 22.683  60.875  56.894  1.00 25.71 ? 1170 ALA B CA    1 
ATOM   17609 C  C     . ALA B  1  1172 ? 24.096  60.897  57.479  1.00 28.30 ? 1170 ALA B C     1 
ATOM   17610 O  O     . ALA B  1  1172 ? 24.413  60.125  58.393  1.00 26.55 ? 1170 ALA B O     1 
ATOM   17611 C  CB    . ALA B  1  1172 ? 22.659  60.121  55.565  1.00 28.30 ? 1170 ALA B CB    1 
ATOM   17612 N  N     . GLU B  1  1173 ? 24.966  61.768  56.959  1.00 28.00 ? 1171 GLU B N     1 
ATOM   17613 C  CA    . GLU B  1  1173 ? 26.333  61.822  57.468  1.00 28.09 ? 1171 GLU B CA    1 
ATOM   17614 C  C     . GLU B  1  1173 ? 26.361  62.264  58.926  1.00 24.53 ? 1171 GLU B C     1 
ATOM   17615 O  O     . GLU B  1  1173 ? 27.112  61.713  59.738  1.00 25.57 ? 1171 GLU B O     1 
ATOM   17616 C  CB    . GLU B  1  1173 ? 27.182  62.759  56.606  1.00 35.35 ? 1171 GLU B CB    1 
ATOM   17617 N  N     . ARG B  1  1174 ? 25.548  63.260  59.273  1.00 25.91 ? 1172 ARG B N     1 
ATOM   17618 C  CA    . ARG B  1  1174 ? 25.463  63.700  60.661  1.00 23.98 ? 1172 ARG B CA    1 
ATOM   17619 C  C     . ARG B  1  1174 ? 24.954  62.582  61.562  1.00 21.68 ? 1172 ARG B C     1 
ATOM   17620 O  O     . ARG B  1  1174 ? 25.509  62.341  62.637  1.00 25.48 ? 1172 ARG B O     1 
ATOM   17621 C  CB    . ARG B  1  1174 ? 24.560  64.929  60.750  1.00 26.79 ? 1172 ARG B CB    1 
ATOM   17622 C  CG    . ARG B  1  1174 ? 24.328  65.456  62.158  1.00 24.39 ? 1172 ARG B CG    1 
ATOM   17623 C  CD    . ARG B  1  1174 ? 25.625  65.880  62.827  1.00 27.07 ? 1172 ARG B CD    1 
ATOM   17624 N  NE    . ARG B  1  1174 ? 25.382  66.395  64.171  1.00 29.30 ? 1172 ARG B NE    1 
ATOM   17625 C  CZ    . ARG B  1  1174 ? 26.305  66.501  65.119  1.00 31.58 ? 1172 ARG B CZ    1 
ATOM   17626 N  NH1   . ARG B  1  1174 ? 27.568  66.163  64.902  1.00 27.15 ? 1172 ARG B NH1   1 
ATOM   17627 N  NH2   . ARG B  1  1174 ? 25.946  66.935  66.326  1.00 26.53 ? 1172 ARG B NH2   1 
ATOM   17628 N  N     . ILE B  1  1175 ? 23.912  61.877  61.124  1.00 21.57 ? 1173 ILE B N     1 
ATOM   17629 C  CA    . ILE B  1  1175 ? 23.365  60.778  61.919  1.00 21.91 ? 1173 ILE B CA    1 
ATOM   17630 C  C     . ILE B  1  1175 ? 24.422  59.707  62.153  1.00 22.56 ? 1173 ILE B C     1 
ATOM   17631 O  O     . ILE B  1  1175 ? 24.585  59.212  63.274  1.00 21.36 ? 1173 ILE B O     1 
ATOM   17632 C  CB    . ILE B  1  1175 ? 22.115  60.204  61.234  1.00 24.66 ? 1173 ILE B CB    1 
ATOM   17633 C  CG1   . ILE B  1  1175 ? 20.971  61.215  61.306  1.00 26.01 ? 1173 ILE B CG1   1 
ATOM   17634 C  CG2   . ILE B  1  1175 ? 21.714  58.890  61.857  1.00 23.36 ? 1173 ILE B CG2   1 
ATOM   17635 C  CD1   . ILE B  1  1175 ? 19.786  60.823  60.468  1.00 26.04 ? 1173 ILE B CD1   1 
ATOM   17636 N  N     . ARG B  1  1176 ? 25.158  59.327  61.101  1.00 25.27 ? 1174 ARG B N     1 
ATOM   17637 C  CA    . ARG B  1  1176 ? 26.190  58.304  61.267  1.00 23.20 ? 1174 ARG B CA    1 
ATOM   17638 C  C     . ARG B  1  1176 ? 27.249  58.749  62.264  1.00 23.53 ? 1174 ARG B C     1 
ATOM   17639 O  O     . ARG B  1  1176 ? 27.655  57.976  63.135  1.00 23.42 ? 1174 ARG B O     1 
ATOM   17640 C  CB    . ARG B  1  1176 ? 26.843  57.964  59.923  1.00 24.65 ? 1174 ARG B CB    1 
ATOM   17641 C  CG    . ARG B  1  1176 ? 27.801  56.779  59.998  1.00 30.96 ? 1174 ARG B CG    1 
ATOM   17642 C  CD    . ARG B  1  1176 ? 28.746  56.679  58.783  1.00 35.49 ? 1174 ARG B CD    1 
ATOM   17643 N  NE    . ARG B  1  1176 ? 28.051  56.836  57.509  1.00 39.65 ? 1174 ARG B NE    1 
ATOM   17644 C  CZ    . ARG B  1  1176 ? 27.528  55.841  56.805  1.00 47.17 ? 1174 ARG B CZ    1 
ATOM   17645 N  NH1   . ARG B  1  1176 ? 27.603  54.587  57.217  1.00 41.90 ? 1174 ARG B NH1   1 
ATOM   17646 N  NH2   . ARG B  1  1176 ? 26.915  56.110  55.654  1.00 44.78 ? 1174 ARG B NH2   1 
ATOM   17647 N  N     . ALA B  1  1177 ? 27.704  59.999  62.159  1.00 23.04 ? 1175 ALA B N     1 
ATOM   17648 C  CA    . ALA B  1  1177 ? 28.731  60.485  63.072  1.00 23.05 ? 1175 ALA B CA    1 
ATOM   17649 C  C     . ALA B  1  1177 ? 28.227  60.507  64.507  1.00 20.67 ? 1175 ALA B C     1 
ATOM   17650 O  O     . ALA B  1  1177 ? 28.952  60.135  65.438  1.00 22.70 ? 1175 ALA B O     1 
ATOM   17651 C  CB    . ALA B  1  1177 ? 29.183  61.882  62.654  1.00 23.84 ? 1175 ALA B CB    1 
ATOM   17652 N  N     . VAL B  1  1178 ? 26.990  60.953  64.706  1.00 24.28 ? 1176 VAL B N     1 
ATOM   17653 C  CA    . VAL B  1  1178 ? 26.438  61.006  66.055  1.00 20.05 ? 1176 VAL B CA    1 
ATOM   17654 C  C     . VAL B  1  1178 ? 26.243  59.601  66.590  1.00 21.14 ? 1176 VAL B C     1 
ATOM   17655 O  O     . VAL B  1  1178 ? 26.574  59.304  67.745  1.00 23.87 ? 1176 VAL B O     1 
ATOM   17656 C  CB    . VAL B  1  1178 ? 25.131  61.817  66.053  1.00 23.20 ? 1176 VAL B CB    1 
ATOM   17657 C  CG1   . VAL B  1  1178 ? 24.433  61.728  67.415  1.00 21.95 ? 1176 VAL B CG1   1 
ATOM   17658 C  CG2   . VAL B  1  1178 ? 25.416  63.267  65.721  1.00 23.85 ? 1176 VAL B CG2   1 
ATOM   17659 N  N     . ASN B  1  1179 ? 25.730  58.708  65.748  1.00 22.07 ? 1177 ASN B N     1 
ATOM   17660 C  CA    . ASN B  1  1179 ? 25.505  57.332  66.170  1.00 23.34 ? 1177 ASN B CA    1 
ATOM   17661 C  C     . ASN B  1  1179 ? 26.812  56.672  66.583  1.00 24.05 ? 1177 ASN B C     1 
ATOM   17662 O  O     . ASN B  1  1179 ? 26.865  55.960  67.594  1.00 24.38 ? 1177 ASN B O     1 
ATOM   17663 C  CB    . ASN B  1  1179 ? 24.829  56.563  65.036  1.00 21.26 ? 1177 ASN B CB    1 
ATOM   17664 C  CG    . ASN B  1  1179 ? 24.093  55.335  65.517  1.00 30.00 ? 1177 ASN B CG    1 
ATOM   17665 O  OD1   . ASN B  1  1179 ? 23.591  55.288  66.644  1.00 27.75 ? 1177 ASN B OD1   1 
ATOM   17666 N  ND2   . ASN B  1  1179 ? 24.014  54.326  64.653  1.00 25.51 ? 1177 ASN B ND2   1 
ATOM   17667 N  N     . LYS B  1  1180 ? 27.888  56.924  65.827  1.00 23.54 ? 1178 LYS B N     1 
ATOM   17668 C  CA    . LYS B  1  1180 ? 29.198  56.400  66.200  1.00 21.61 ? 1178 LYS B CA    1 
ATOM   17669 C  C     . LYS B  1  1180 ? 29.649  56.955  67.545  1.00 23.52 ? 1178 LYS B C     1 
ATOM   17670 O  O     . LYS B  1  1180 ? 30.170  56.215  68.385  1.00 23.54 ? 1178 LYS B O     1 
ATOM   17671 C  CB    . LYS B  1  1180 ? 30.226  56.719  65.110  1.00 25.94 ? 1178 LYS B CB    1 
ATOM   17672 N  N     . ALA B  1  1181 ? 29.452  58.258  67.772  1.00 21.88 ? 1179 ALA B N     1 
ATOM   17673 C  CA    . ALA B  1  1181 ? 29.853  58.839  69.051  1.00 20.88 ? 1179 ALA B CA    1 
ATOM   17674 C  C     . ALA B  1  1181 ? 29.028  58.261  70.195  1.00 20.86 ? 1179 ALA B C     1 
ATOM   17675 O  O     . ALA B  1  1181 ? 29.558  58.004  71.284  1.00 21.72 ? 1179 ALA B O     1 
ATOM   17676 C  CB    . ALA B  1  1181 ? 29.715  60.361  69.010  1.00 21.89 ? 1179 ALA B CB    1 
ATOM   17677 N  N     . ILE B  1  1182 ? 27.732  58.045  69.962  1.00 21.30 ? 1180 ILE B N     1 
ATOM   17678 C  CA    . ILE B  1  1182 ? 26.881  57.486  71.006  1.00 21.35 ? 1180 ILE B CA    1 
ATOM   17679 C  C     . ILE B  1  1182 ? 27.284  56.052  71.318  1.00 20.42 ? 1180 ILE B C     1 
ATOM   17680 O  O     . ILE B  1  1182 ? 27.320  55.646  72.484  1.00 20.35 ? 1180 ILE B O     1 
ATOM   17681 C  CB    . ILE B  1  1182 ? 25.405  57.590  70.592  1.00 22.31 ? 1180 ILE B CB    1 
ATOM   17682 C  CG1   . ILE B  1  1182 ? 24.953  59.042  70.729  1.00 21.06 ? 1180 ILE B CG1   1 
ATOM   17683 C  CG2   . ILE B  1  1182 ? 24.548  56.673  71.447  1.00 23.08 ? 1180 ILE B CG2   1 
ATOM   17684 C  CD1   . ILE B  1  1182 ? 23.591  59.319  70.114  1.00 23.16 ? 1180 ILE B CD1   1 
ATOM   17685 N  N     . ALA B  1  1183 ? 27.610  55.264  70.288  1.00 23.48 ? 1181 ALA B N     1 
ATOM   17686 C  CA    . ALA B  1  1183 ? 28.034  53.893  70.541  1.00 23.96 ? 1181 ALA B CA    1 
ATOM   17687 C  C     . ALA B  1  1183 ? 29.312  53.830  71.359  1.00 24.72 ? 1181 ALA B C     1 
ATOM   17688 O  O     . ALA B  1  1183 ? 29.543  52.835  72.057  1.00 27.46 ? 1181 ALA B O     1 
ATOM   17689 C  CB    . ALA B  1  1183 ? 28.212  53.133  69.223  1.00 24.55 ? 1181 ALA B CB    1 
ATOM   17690 N  N     . ALA B  1  1184 ? 30.126  54.884  71.328  1.00 22.03 ? 1182 ALA B N     1 
ATOM   17691 C  CA    . ALA B  1  1184 ? 31.357  54.929  72.097  1.00 26.24 ? 1182 ALA B CA    1 
ATOM   17692 C  C     . ALA B  1  1184 ? 31.152  55.444  73.515  1.00 23.35 ? 1182 ALA B C     1 
ATOM   17693 O  O     . ALA B  1  1184 ? 32.115  55.500  74.279  1.00 24.48 ? 1182 ALA B O     1 
ATOM   17694 C  CB    . ALA B  1  1184 ? 32.399  55.798  71.376  1.00 26.14 ? 1182 ALA B CB    1 
ATOM   17695 N  N     . LEU B  1  1185 ? 29.936  55.829  73.892  1.00 20.87 ? 1183 LEU B N     1 
ATOM   17696 C  CA    . LEU B  1  1185 ? 29.742  56.312  75.250  1.00 20.50 ? 1183 LEU B CA    1 
ATOM   17697 C  C     . LEU B  1  1185 ? 29.853  55.150  76.230  1.00 23.01 ? 1183 LEU B C     1 
ATOM   17698 O  O     . LEU B  1  1185 ? 29.386  54.041  75.938  1.00 25.87 ? 1183 LEU B O     1 
ATOM   17699 C  CB    . LEU B  1  1185 ? 28.382  56.984  75.417  1.00 21.51 ? 1183 LEU B CB    1 
ATOM   17700 C  CG    . LEU B  1  1185 ? 28.151  58.220  74.549  1.00 18.58 ? 1183 LEU B CG    1 
ATOM   17701 C  CD1   . LEU B  1  1185 ? 26.696  58.660  74.648  1.00 20.07 ? 1183 LEU B CD1   1 
ATOM   17702 C  CD2   . LEU B  1  1185 ? 29.113  59.344  74.949  1.00 20.55 ? 1183 LEU B CD2   1 
ATOM   17703 N  N     . PRO B  1  1186 ? 30.436  55.373  77.400  1.00 23.80 ? 1184 PRO B N     1 
ATOM   17704 C  CA    . PRO B  1  1186 ? 30.474  54.318  78.410  1.00 24.72 ? 1184 PRO B CA    1 
ATOM   17705 C  C     . PRO B  1  1186 ? 29.093  54.089  78.990  1.00 22.81 ? 1184 PRO B C     1 
ATOM   17706 O  O     . PRO B  1  1186 ? 28.182  54.909  78.857  1.00 24.65 ? 1184 PRO B O     1 
ATOM   17707 C  CB    . PRO B  1  1186 ? 31.427  54.877  79.469  1.00 29.89 ? 1184 PRO B CB    1 
ATOM   17708 C  CG    . PRO B  1  1186 ? 31.215  56.371  79.372  1.00 28.61 ? 1184 PRO B CG    1 
ATOM   17709 C  CD    . PRO B  1  1186 ? 30.972  56.648  77.908  1.00 25.12 ? 1184 PRO B CD    1 
ATOM   17710 N  N     . GLY B  1  1187 ? 28.947  52.946  79.647  1.00 23.37 ? 1185 GLY B N     1 
ATOM   17711 C  CA    . GLY B  1  1187 ? 27.730  52.647  80.357  1.00 24.25 ? 1185 GLY B CA    1 
ATOM   17712 C  C     . GLY B  1  1187 ? 26.686  51.999  79.474  1.00 23.61 ? 1185 GLY B C     1 
ATOM   17713 O  O     . GLY B  1  1187 ? 26.988  51.171  78.612  1.00 26.41 ? 1185 GLY B O     1 
ATOM   17714 N  N     . PRO B  1  1188 ? 25.429  52.366  79.681  1.00 18.70 ? 1186 PRO B N     1 
ATOM   17715 C  CA    . PRO B  1  1188 ? 24.343  51.661  78.990  1.00 20.70 ? 1186 PRO B CA    1 
ATOM   17716 C  C     . PRO B  1  1188 ? 24.377  51.885  77.490  1.00 21.88 ? 1186 PRO B C     1 
ATOM   17717 O  O     . PRO B  1  1188 ? 24.823  52.923  76.995  1.00 22.30 ? 1186 PRO B O     1 
ATOM   17718 C  CB    . PRO B  1  1188 ? 23.075  52.265  79.600  1.00 25.13 ? 1186 PRO B CB    1 
ATOM   17719 C  CG    . PRO B  1  1188 ? 23.499  53.584  80.128  1.00 31.60 ? 1186 PRO B CG    1 
ATOM   17720 C  CD    . PRO B  1  1188 ? 24.927  53.424  80.569  1.00 24.15 ? 1186 PRO B CD    1 
ATOM   17721 N  N     . LEU B  1  1189 ? 23.871  50.894  76.765  1.00 20.43 ? 1187 LEU B N     1 
ATOM   17722 C  CA    . LEU B  1  1189 ? 23.699  51.016  75.322  1.00 20.75 ? 1187 LEU B CA    1 
ATOM   17723 C  C     . LEU B  1  1189 ? 22.456  51.845  75.058  1.00 23.35 ? 1187 LEU B C     1 
ATOM   17724 O  O     . LEU B  1  1189 ? 21.357  51.466  75.475  1.00 25.00 ? 1187 LEU B O     1 
ATOM   17725 C  CB    . LEU B  1  1189 ? 23.567  49.636  74.678  1.00 20.39 ? 1187 LEU B CB    1 
ATOM   17726 C  CG    . LEU B  1  1189 ? 24.852  48.861  74.418  1.00 24.75 ? 1187 LEU B CG    1 
ATOM   17727 C  CD1   . LEU B  1  1189 ? 25.413  48.319  75.720  1.00 31.73 ? 1187 LEU B CD1   1 
ATOM   17728 C  CD2   . LEU B  1  1189 ? 24.576  47.737  73.435  1.00 23.75 ? 1187 LEU B CD2   1 
ATOM   17729 N  N     . LEU B  1  1190 ? 22.619  52.977  74.385  1.00 19.57 ? 1188 LEU B N     1 
ATOM   17730 C  CA    . LEU B  1  1190 ? 21.504  53.895  74.217  1.00 19.91 ? 1188 LEU B CA    1 
ATOM   17731 C  C     . LEU B  1  1190 ? 20.649  53.514  73.018  1.00 20.09 ? 1188 LEU B C     1 
ATOM   17732 O  O     . LEU B  1  1190 ? 21.161  53.203  71.934  1.00 19.82 ? 1188 LEU B O     1 
ATOM   17733 C  CB    . LEU B  1  1190 ? 21.993  55.331  74.054  1.00 20.28 ? 1188 LEU B CB    1 
ATOM   17734 C  CG    . LEU B  1  1190 ? 22.784  55.948  75.205  1.00 19.54 ? 1188 LEU B CG    1 
ATOM   17735 C  CD1   . LEU B  1  1190 ? 22.883  57.439  74.965  1.00 20.79 ? 1188 LEU B CD1   1 
ATOM   17736 C  CD2   . LEU B  1  1190 ? 22.138  55.644  76.565  1.00 22.38 ? 1188 LEU B CD2   1 
ATOM   17737 N  N     . LEU B  1  1191 ? 19.337  53.548  73.223  1.00 21.19 ? 1189 LEU B N     1 
ATOM   17738 C  CA    . LEU B  1  1191 ? 18.385  53.429  72.133  1.00 19.60 ? 1189 LEU B CA    1 
ATOM   17739 C  C     . LEU B  1  1191 ? 18.331  54.766  71.400  1.00 21.40 ? 1189 LEU B C     1 
ATOM   17740 O  O     . LEU B  1  1191 ? 17.821  55.758  71.930  1.00 23.53 ? 1189 LEU B O     1 
ATOM   17741 C  CB    . LEU B  1  1191 ? 17.018  53.021  72.675  1.00 21.99 ? 1189 LEU B CB    1 
ATOM   17742 C  CG    . LEU B  1  1191 ? 16.074  52.314  71.696  1.00 21.51 ? 1189 LEU B CG    1 
ATOM   17743 C  CD1   . LEU B  1  1191 ? 14.927  51.676  72.469  1.00 21.76 ? 1189 LEU B CD1   1 
ATOM   17744 C  CD2   . LEU B  1  1191 ? 15.533  53.298  70.677  1.00 20.65 ? 1189 LEU B CD2   1 
ATOM   17745 N  N     . VAL B  1  1192 ? 18.873  54.788  70.190  1.00 19.58 ? 1190 VAL B N     1 
ATOM   17746 C  CA    . VAL B  1  1192 ? 19.017  56.004  69.397  1.00 19.25 ? 1190 VAL B CA    1 
ATOM   17747 C  C     . VAL B  1  1192 ? 17.881  56.081  68.388  1.00 20.84 ? 1190 VAL B C     1 
ATOM   17748 O  O     . VAL B  1  1192 ? 17.571  55.096  67.703  1.00 23.23 ? 1190 VAL B O     1 
ATOM   17749 C  CB    . VAL B  1  1192 ? 20.379  56.036  68.687  1.00 23.75 ? 1190 VAL B CB    1 
ATOM   17750 C  CG1   . VAL B  1  1192 ? 20.516  57.284  67.836  1.00 21.15 ? 1190 VAL B CG1   1 
ATOM   17751 C  CG2   . VAL B  1  1192 ? 21.516  55.945  69.720  1.00 21.75 ? 1190 VAL B CG2   1 
ATOM   17752 N  N     . GLN B  1  1193 ? 17.264  57.253  68.296  1.00 19.12 ? 1191 GLN B N     1 
ATOM   17753 C  CA    . GLN B  1  1193 ? 16.295  57.558  67.258  1.00 18.53 ? 1191 GLN B CA    1 
ATOM   17754 C  C     . GLN B  1  1193 ? 16.788  58.761  66.480  1.00 22.12 ? 1191 GLN B C     1 
ATOM   17755 O  O     . GLN B  1  1193 ? 17.151  59.780  67.077  1.00 20.28 ? 1191 GLN B O     1 
ATOM   17756 C  CB    . GLN B  1  1193 ? 14.934  57.875  67.844  1.00 19.55 ? 1191 GLN B CB    1 
ATOM   17757 C  CG    . GLN B  1  1193 ? 14.359  56.770  68.675  1.00 18.66 ? 1191 GLN B CG    1 
ATOM   17758 C  CD    . GLN B  1  1193 ? 12.903  57.021  68.923  1.00 21.51 ? 1191 GLN B CD    1 
ATOM   17759 O  OE1   . GLN B  1  1193 ? 12.092  56.969  68.001  1.00 22.40 ? 1191 GLN B OE1   1 
ATOM   17760 N  NE2   . GLN B  1  1193 ? 12.564  57.328  70.163  1.00 20.34 ? 1191 GLN B NE2   1 
ATOM   17761 N  N     . ALA B  1  1194 ? 16.776  58.657  65.157  1.00 22.57 ? 1192 ALA B N     1 
ATOM   17762 C  CA    . ALA B  1  1194 ? 17.279  59.737  64.327  1.00 22.08 ? 1192 ALA B CA    1 
ATOM   17763 C  C     . ALA B  1  1194 ? 16.242  60.124  63.287  1.00 22.98 ? 1192 ALA B C     1 
ATOM   17764 O  O     . ALA B  1  1194 ? 15.421  59.307  62.853  1.00 26.75 ? 1192 ALA B O     1 
ATOM   17765 C  CB    . ALA B  1  1194 ? 18.588  59.352  63.638  1.00 24.80 ? 1192 ALA B CB    1 
ATOM   17766 N  N     . ALA B  1  1195 ? 16.290  61.387  62.890  1.00 22.72 ? 1193 ALA B N     1 
ATOM   17767 C  CA    . ALA B  1  1195 ? 15.399  61.882  61.855  1.00 22.81 ? 1193 ALA B CA    1 
ATOM   17768 C  C     . ALA B  1  1195 ? 16.078  63.056  61.182  1.00 27.01 ? 1193 ALA B C     1 
ATOM   17769 O  O     . ALA B  1  1195 ? 16.917  63.732  61.785  1.00 23.31 ? 1193 ALA B O     1 
ATOM   17770 C  CB    . ALA B  1  1195 ? 14.043  62.317  62.420  1.00 23.50 ? 1193 ALA B CB    1 
ATOM   17771 N  N     . SER B  1  1196 ? 15.721  63.279  59.923  1.00 26.61 ? 1194 SER B N     1 
ATOM   17772 C  CA    . SER B  1  1196 ? 16.146  64.488  59.244  1.00 26.07 ? 1194 SER B CA    1 
ATOM   17773 C  C     . SER B  1  1196 ? 15.253  65.653  59.655  1.00 26.61 ? 1194 SER B C     1 
ATOM   17774 O  O     . SER B  1  1196 ? 14.133  65.470  60.141  1.00 25.70 ? 1194 SER B O     1 
ATOM   17775 C  CB    . SER B  1  1196 ? 16.087  64.299  57.728  1.00 24.71 ? 1194 SER B CB    1 
ATOM   17776 O  OG    . SER B  1  1196 ? 14.746  64.146  57.304  1.00 30.56 ? 1194 SER B OG    1 
ATOM   17777 N  N     . SER B  1  1197 ? 15.763  66.870  59.450  1.00 24.46 ? 1195 SER B N     1 
ATOM   17778 C  CA    . SER B  1  1197 ? 14.940  68.057  59.660  1.00 25.66 ? 1195 SER B CA    1 
ATOM   17779 C  C     . SER B  1  1197 ? 13.654  67.978  58.853  1.00 24.52 ? 1195 SER B C     1 
ATOM   17780 O  O     . SER B  1  1197 ? 12.574  68.335  59.343  1.00 27.37 ? 1195 SER B O     1 
ATOM   17781 C  CB    . SER B  1  1197 ? 15.718  69.311  59.274  1.00 28.61 ? 1195 SER B CB    1 
ATOM   17782 O  OG    . SER B  1  1197 ? 16.851  69.482  60.102  1.00 28.97 ? 1195 SER B OG    1 
ATOM   17783 N  N     . GLY B  1  1198 ? 13.754  67.514  57.608  1.00 28.32 ? 1196 GLY B N     1 
ATOM   17784 C  CA    . GLY B  1  1198 ? 12.568  67.381  56.785  1.00 31.68 ? 1196 GLY B CA    1 
ATOM   17785 C  C     . GLY B  1  1198 ? 11.605  66.340  57.319  1.00 33.12 ? 1196 GLY B C     1 
ATOM   17786 O  O     . GLY B  1  1198 ? 10.389  66.534  57.280  1.00 30.53 ? 1196 GLY B O     1 
ATOM   17787 N  N     . GLU B  1  1199 ? 12.135  65.221  57.825  1.00 27.24 ? 1197 GLU B N     1 
ATOM   17788 C  CA    . GLU B  1  1199 ? 11.267  64.195  58.399  1.00 29.51 ? 1197 GLU B CA    1 
ATOM   17789 C  C     . GLU B  1  1199 ? 10.537  64.724  59.623  1.00 30.49 ? 1197 GLU B C     1 
ATOM   17790 O  O     . GLU B  1  1199 ? 9.346   64.454  59.813  1.00 31.74 ? 1197 GLU B O     1 
ATOM   17791 C  CB    . GLU B  1  1199 ? 12.080  62.949  58.753  1.00 33.08 ? 1197 GLU B CB    1 
ATOM   17792 N  N     . ILE B  1  1200 ? 11.233  65.492  60.463  1.00 24.84 ? 1198 ILE B N     1 
ATOM   17793 C  CA    . ILE B  1  1200 ? 10.589  66.080  61.634  1.00 25.64 ? 1198 ILE B CA    1 
ATOM   17794 C  C     . ILE B  1  1200 ? 9.429   66.977  61.217  1.00 31.64 ? 1198 ILE B C     1 
ATOM   17795 O  O     . ILE B  1  1200 ? 8.366   66.974  61.848  1.00 27.80 ? 1198 ILE B O     1 
ATOM   17796 C  CB    . ILE B  1  1200 ? 11.630  66.842  62.474  1.00 23.96 ? 1198 ILE B CB    1 
ATOM   17797 C  CG1   . ILE B  1  1200 ? 12.618  65.858  63.099  1.00 23.92 ? 1198 ILE B CG1   1 
ATOM   17798 C  CG2   . ILE B  1  1200 ? 10.951  67.693  63.551  1.00 25.37 ? 1198 ILE B CG2   1 
ATOM   17799 C  CD1   . ILE B  1  1200 ? 13.699  66.529  63.922  1.00 25.77 ? 1198 ILE B CD1   1 
ATOM   17800 N  N     . ALA B  1  1201 ? 9.603   67.747  60.137  1.00 30.00 ? 1199 ALA B N     1 
ATOM   17801 C  CA    . ALA B  1  1201 ? 8.553   68.670  59.713  1.00 32.41 ? 1199 ALA B CA    1 
ATOM   17802 C  C     . ALA B  1  1201 ? 7.387   67.932  59.064  1.00 31.04 ? 1199 ALA B C     1 
ATOM   17803 O  O     . ALA B  1  1201 ? 6.225   68.323  59.239  1.00 36.72 ? 1199 ALA B O     1 
ATOM   17804 C  CB    . ALA B  1  1201 ? 9.124   69.711  58.748  1.00 32.28 ? 1199 ALA B CB    1 
ATOM   17805 N  N     . ARG B  1  1202 ? 7.676   66.859  58.323  1.00 33.01 ? 1200 ARG B N     1 
ATOM   17806 C  CA    . ARG B  1  1202 ? 6.670   66.102  57.584  1.00 35.58 ? 1200 ARG B CA    1 
ATOM   17807 C  C     . ARG B  1  1202 ? 5.957   65.065  58.443  1.00 39.04 ? 1200 ARG B C     1 
ATOM   17808 O  O     . ARG B  1  1202 ? 4.739   64.899  58.326  1.00 36.71 ? 1200 ARG B O     1 
ATOM   17809 C  CB    . ARG B  1  1202 ? 7.315   65.388  56.392  1.00 41.48 ? 1200 ARG B CB    1 
ATOM   17810 C  CG    . ARG B  1  1202 ? 7.982   66.308  55.375  1.00 47.97 ? 1200 ARG B CG    1 
ATOM   17811 C  CD    . ARG B  1  1202 ? 8.510   65.524  54.172  1.00 53.14 ? 1200 ARG B CD    1 
ATOM   17812 N  NE    . ARG B  1  1202 ? 9.204   64.298  54.554  1.00 49.62 ? 1200 ARG B NE    1 
ATOM   17813 C  CZ    . ARG B  1  1202 ? 10.523  64.149  54.569  1.00 48.45 ? 1200 ARG B CZ    1 
ATOM   17814 N  NH1   . ARG B  1  1202 ? 11.334  65.130  54.209  1.00 49.62 ? 1200 ARG B NH1   1 
ATOM   17815 N  NH2   . ARG B  1  1202 ? 11.040  62.985  54.954  1.00 47.13 ? 1200 ARG B NH2   1 
ATOM   17816 N  N     . ASN B  1  1203 ? 6.692   64.360  59.302  1.00 32.16 ? 1201 ASN B N     1 
ATOM   17817 C  CA    . ASN B  1  1203 ? 6.178   63.164  59.967  1.00 34.23 ? 1201 ASN B CA    1 
ATOM   17818 C  C     . ASN B  1  1203 ? 5.976   63.423  61.453  1.00 32.86 ? 1201 ASN B C     1 
ATOM   17819 O  O     . ASN B  1  1203 ? 6.963   63.502  62.203  1.00 28.50 ? 1201 ASN B O     1 
ATOM   17820 C  CB    . ASN B  1  1203 ? 7.139   61.990  59.748  1.00 33.42 ? 1201 ASN B CB    1 
ATOM   17821 C  CG    . ASN B  1  1203 ? 6.679   60.702  60.435  1.00 32.28 ? 1201 ASN B CG    1 
ATOM   17822 O  OD1   . ASN B  1  1203 ? 5.562   60.613  60.951  1.00 37.77 ? 1201 ASN B OD1   1 
ATOM   17823 N  ND2   . ASN B  1  1203 ? 7.547   59.699  60.438  1.00 35.69 ? 1201 ASN B ND2   1 
ATOM   17824 N  N     . PRO B  1  1204 ? 4.734   63.539  61.930  1.00 35.74 ? 1202 PRO B N     1 
ATOM   17825 C  CA    . PRO B  1  1204 ? 4.518   63.760  63.369  1.00 32.56 ? 1202 PRO B CA    1 
ATOM   17826 C  C     . PRO B  1  1204 ? 5.038   62.631  64.240  1.00 31.29 ? 1202 PRO B C     1 
ATOM   17827 O  O     . PRO B  1  1204 ? 5.228   62.831  65.448  1.00 34.32 ? 1202 PRO B O     1 
ATOM   17828 C  CB    . PRO B  1  1204 ? 2.992   63.899  63.478  1.00 42.95 ? 1202 PRO B CB    1 
ATOM   17829 C  CG    . PRO B  1  1204 ? 2.455   63.218  62.264  1.00 38.94 ? 1202 PRO B CG    1 
ATOM   17830 C  CD    . PRO B  1  1204 ? 3.469   63.449  61.180  1.00 40.85 ? 1202 PRO B CD    1 
ATOM   17831 N  N     . ASP B  1  1205 ? 5.280   61.451  63.673  1.00 28.12 ? 1203 ASP B N     1 
ATOM   17832 C  CA    . ASP B  1  1205 ? 5.848   60.333  64.414  1.00 34.53 ? 1203 ASP B CA    1 
ATOM   17833 C  C     . ASP B  1  1205 ? 7.316   60.108  64.076  1.00 33.27 ? 1203 ASP B C     1 
ATOM   17834 O  O     . ASP B  1  1205 ? 7.809   58.980  64.185  1.00 30.39 ? 1203 ASP B O     1 
ATOM   17835 C  CB    . ASP B  1  1205 ? 5.045   59.059  64.155  1.00 32.39 ? 1203 ASP B CB    1 
ATOM   17836 C  CG    . ASP B  1  1205 ? 3.667   59.100  64.786  1.00 40.95 ? 1203 ASP B CG    1 
ATOM   17837 O  OD1   . ASP B  1  1205 ? 3.488   59.838  65.778  1.00 35.36 ? 1203 ASP B OD1   1 
ATOM   17838 O  OD2   . ASP B  1  1205 ? 2.766   58.390  64.293  1.00 43.99 ? 1203 ASP B OD2   1 
ATOM   17839 N  N     . ALA B  1  1206 ? 8.021   61.164  63.654  1.00 29.63 ? 1204 ALA B N     1 
ATOM   17840 C  CA    . ALA B  1  1206 ? 9.441   61.034  63.335  1.00 29.17 ? 1204 ALA B CA    1 
ATOM   17841 C  C     . ALA B  1  1206 ? 10.216  60.432  64.501  1.00 28.79 ? 1204 ALA B C     1 
ATOM   17842 O  O     . ALA B  1  1206 ? 11.096  59.585  64.307  1.00 27.16 ? 1204 ALA B O     1 
ATOM   17843 C  CB    . ALA B  1  1206 ? 10.019  62.399  62.956  1.00 29.34 ? 1204 ALA B CB    1 
ATOM   17844 N  N     . TYR B  1  1207 ? 9.893   60.847  65.721  1.00 23.21 ? 1205 TYR B N     1 
ATOM   17845 C  CA    . TYR B  1  1207 ? 10.414  60.216  66.923  1.00 23.57 ? 1205 TYR B CA    1 
ATOM   17846 C  C     . TYR B  1  1207 ? 9.285   59.445  67.587  1.00 23.61 ? 1205 TYR B C     1 
ATOM   17847 O  O     . TYR B  1  1207 ? 8.194   59.983  67.786  1.00 30.81 ? 1205 TYR B O     1 
ATOM   17848 C  CB    . TYR B  1  1207 ? 10.989  61.245  67.893  1.00 22.26 ? 1205 TYR B CB    1 
ATOM   17849 C  CG    . TYR B  1  1207 ? 12.142  62.012  67.319  1.00 20.66 ? 1205 TYR B CG    1 
ATOM   17850 C  CD1   . TYR B  1  1207 ? 13.303  61.358  66.945  1.00 20.26 ? 1205 TYR B CD1   1 
ATOM   17851 C  CD2   . TYR B  1  1207 ? 12.075  63.390  67.163  1.00 20.89 ? 1205 TYR B CD2   1 
ATOM   17852 C  CE1   . TYR B  1  1207 ? 14.369  62.053  66.424  1.00 19.05 ? 1205 TYR B CE1   1 
ATOM   17853 C  CE2   . TYR B  1  1207 ? 13.141  64.099  66.637  1.00 22.99 ? 1205 TYR B CE2   1 
ATOM   17854 C  CZ    . TYR B  1  1207 ? 14.283  63.422  66.277  1.00 21.14 ? 1205 TYR B CZ    1 
ATOM   17855 O  OH    . TYR B  1  1207 ? 15.354  64.109  65.747  1.00 21.48 ? 1205 TYR B OH    1 
ATOM   17856 N  N     . CYS B  1  1208 ? 9.557   58.195  67.912  1.00 18.91 ? 1206 CYS B N     1 
ATOM   17857 C  CA    . CYS B  1  1208 ? 8.556   57.289  68.452  1.00 18.66 ? 1206 CYS B CA    1 
ATOM   17858 C  C     . CYS B  1  1208 ? 8.590   57.333  69.976  1.00 18.01 ? 1206 CYS B C     1 
ATOM   17859 O  O     . CYS B  1  1208 ? 9.636   57.094  70.588  1.00 18.25 ? 1206 CYS B O     1 
ATOM   17860 C  CB    . CYS B  1  1208 ? 8.824   55.879  67.936  1.00 23.64 ? 1206 CYS B CB    1 
ATOM   17861 S  SG    . CYS B  1  1208 ? 7.633   54.673  68.514  1.00 23.56 ? 1206 CYS B SG    1 
ATOM   17862 N  N     . LEU B  1  1209 ? 7.443   57.637  70.586  1.00 18.11 ? 1207 LEU B N     1 
ATOM   17863 C  CA    . LEU B  1  1209 ? 7.403   57.738  72.039  1.00 17.14 ? 1207 LEU B CA    1 
ATOM   17864 C  C     . LEU B  1  1209 ? 7.450   56.380  72.715  1.00 18.02 ? 1207 LEU B C     1 
ATOM   17865 O  O     . LEU B  1  1209 ? 7.690   56.323  73.924  1.00 18.16 ? 1207 LEU B O     1 
ATOM   17866 C  CB    . LEU B  1  1209 ? 6.158   58.499  72.474  1.00 15.31 ? 1207 LEU B CB    1 
ATOM   17867 C  CG    . LEU B  1  1209 ? 5.963   59.884  71.866  1.00 19.71 ? 1207 LEU B CG    1 
ATOM   17868 C  CD1   . LEU B  1  1209 ? 4.812   60.590  72.575  1.00 24.18 ? 1207 LEU B CD1   1 
ATOM   17869 C  CD2   . LEU B  1  1209 ? 7.243   60.709  71.936  1.00 22.04 ? 1207 LEU B CD2   1 
ATOM   17870 N  N     . ASN B  1  1210 ? 7.224   55.297  71.971  1.00 18.40 ? 1208 ASN B N     1 
ATOM   17871 C  CA    . ASN B  1  1210 ? 7.318   53.965  72.553  1.00 20.56 ? 1208 ASN B CA    1 
ATOM   17872 C  C     . ASN B  1  1210 ? 8.676   53.746  73.198  1.00 20.77 ? 1208 ASN B C     1 
ATOM   17873 O  O     . ASN B  1  1210 ? 8.776   53.052  74.219  1.00 20.57 ? 1208 ASN B O     1 
ATOM   17874 C  CB    . ASN B  1  1210 ? 7.085   52.882  71.484  1.00 23.41 ? 1208 ASN B CB    1 
ATOM   17875 C  CG    . ASN B  1  1210 ? 5.688   52.947  70.848  1.00 23.08 ? 1208 ASN B CG    1 
ATOM   17876 O  OD1   . ASN B  1  1210 ? 4.954   53.928  70.999  1.00 28.08 ? 1208 ASN B OD1   1 
ATOM   17877 N  ND2   . ASN B  1  1210 ? 5.340   51.907  70.095  1.00 28.62 ? 1208 ASN B ND2   1 
ATOM   17878 N  N     . TRP B  1  1211 ? 9.727   54.333  72.629  1.00 17.11 ? 1209 TRP B N     1 
ATOM   17879 C  CA    . TRP B  1  1211 ? 11.088  54.058  73.069  1.00 17.87 ? 1209 TRP B CA    1 
ATOM   17880 C  C     . TRP B  1  1211 ? 11.570  55.028  74.126  1.00 18.91 ? 1209 TRP B C     1 
ATOM   17881 O  O     . TRP B  1  1211 ? 12.702  54.892  74.595  1.00 20.98 ? 1209 TRP B O     1 
ATOM   17882 C  CB    . TRP B  1  1211 ? 12.048  54.086  71.869  1.00 23.83 ? 1209 TRP B CB    1 
ATOM   17883 C  CG    . TRP B  1  1211 ? 11.477  53.386  70.683  1.00 20.53 ? 1209 TRP B CG    1 
ATOM   17884 C  CD1   . TRP B  1  1211 ? 11.386  53.868  69.407  1.00 22.04 ? 1209 TRP B CD1   1 
ATOM   17885 C  CD2   . TRP B  1  1211 ? 10.870  52.094  70.665  1.00 18.69 ? 1209 TRP B CD2   1 
ATOM   17886 N  NE1   . TRP B  1  1211 ? 10.770  52.949  68.595  1.00 21.25 ? 1209 TRP B NE1   1 
ATOM   17887 C  CE2   . TRP B  1  1211 ? 10.444  51.851  69.346  1.00 20.86 ? 1209 TRP B CE2   1 
ATOM   17888 C  CE3   . TRP B  1  1211 ? 10.647  51.111  71.641  1.00 20.59 ? 1209 TRP B CE3   1 
ATOM   17889 C  CZ2   . TRP B  1  1211 ? 9.809   50.671  68.973  1.00 20.25 ? 1209 TRP B CZ2   1 
ATOM   17890 C  CZ3   . TRP B  1  1211 ? 10.012  49.943  71.270  1.00 20.74 ? 1209 TRP B CZ3   1 
ATOM   17891 C  CH2   . TRP B  1  1211 ? 9.604   49.732  69.946  1.00 21.47 ? 1209 TRP B CH2   1 
ATOM   17892 N  N     . LEU B  1  1212 ? 10.751  56.005  74.498  1.00 17.48 ? 1210 LEU B N     1 
ATOM   17893 C  CA    . LEU B  1  1212 ? 11.132  57.033  75.453  1.00 16.34 ? 1210 LEU B CA    1 
ATOM   17894 C  C     . LEU B  1  1212 ? 10.511  56.809  76.820  1.00 16.77 ? 1210 LEU B C     1 
ATOM   17895 O  O     . LEU B  1  1212 ? 10.636  57.661  77.699  1.00 16.55 ? 1210 LEU B O     1 
ATOM   17896 C  CB    . LEU B  1  1212 ? 10.749  58.413  74.908  1.00 15.98 ? 1210 LEU B CB    1 
ATOM   17897 C  CG    . LEU B  1  1212 ? 11.661  58.830  73.738  1.00 15.76 ? 1210 LEU B CG    1 
ATOM   17898 C  CD1   . LEU B  1  1212 ? 11.028  59.959  72.973  1.00 19.28 ? 1210 LEU B CD1   1 
ATOM   17899 C  CD2   . LEU B  1  1212 ? 13.052  59.216  74.230  1.00 17.64 ? 1210 LEU B CD2   1 
ATOM   17900 N  N     . VAL B  1  1213 ? 9.833   55.684  77.007  1.00 18.41 ? 1211 VAL B N     1 
ATOM   17901 C  CA    . VAL B  1  1213 ? 9.361   55.263  78.316  1.00 17.79 ? 1211 VAL B CA    1 
ATOM   17902 C  C     . VAL B  1  1213 ? 10.108  53.996  78.691  1.00 17.98 ? 1211 VAL B C     1 
ATOM   17903 O  O     . VAL B  1  1213 ? 10.633  53.276  77.840  1.00 19.01 ? 1211 VAL B O     1 
ATOM   17904 C  CB    . VAL B  1  1213 ? 7.840   55.023  78.325  1.00 17.51 ? 1211 VAL B CB    1 
ATOM   17905 C  CG1   . VAL B  1  1213 ? 7.107   56.342  78.205  1.00 18.93 ? 1211 VAL B CG1   1 
ATOM   17906 C  CG2   . VAL B  1  1213 ? 7.456   54.095  77.181  1.00 19.41 ? 1211 VAL B CG2   1 
ATOM   17907 N  N     . GLU B  1  1214 ? 10.149  53.723  79.991  1.00 19.32 ? 1212 GLU B N     1 
ATOM   17908 C  CA    . GLU B  1  1214 ? 10.727  52.490  80.504  1.00 21.12 ? 1212 GLU B CA    1 
ATOM   17909 C  C     . GLU B  1  1214 ? 9.614   51.574  80.982  1.00 15.55 ? 1212 GLU B C     1 
ATOM   17910 O  O     . GLU B  1  1214 ? 8.752   51.986  81.763  1.00 16.97 ? 1212 GLU B O     1 
ATOM   17911 C  CB    . GLU B  1  1214 ? 11.690  52.753  81.654  1.00 21.46 ? 1212 GLU B CB    1 
ATOM   17912 C  CG    . GLU B  1  1214 ? 12.335  51.453  82.138  1.00 24.71 ? 1212 GLU B CG    1 
ATOM   17913 C  CD    . GLU B  1  1214 ? 13.183  51.601  83.387  1.00 35.67 ? 1212 GLU B CD    1 
ATOM   17914 O  OE1   . GLU B  1  1214 ? 13.729  52.697  83.620  1.00 33.48 ? 1212 GLU B OE1   1 
ATOM   17915 O  OE2   . GLU B  1  1214 ? 13.311  50.598  84.133  1.00 39.94 ? 1212 GLU B OE2   1 
ATOM   17916 N  N     . GLU B  1  1215 ? 9.657   50.333  80.530  1.00 17.01 ? 1213 GLU B N     1 
ATOM   17917 C  CA    . GLU B  1  1215 ? 8.717   49.330  80.990  1.00 15.07 ? 1213 GLU B CA    1 
ATOM   17918 C  C     . GLU B  1  1215 ? 9.185   48.747  82.309  1.00 15.82 ? 1213 GLU B C     1 
ATOM   17919 O  O     . GLU B  1  1215 ? 10.360  48.401  82.455  1.00 16.34 ? 1213 GLU B O     1 
ATOM   17920 C  CB    . GLU B  1  1215 ? 8.639   48.201  79.977  1.00 16.08 ? 1213 GLU B CB    1 
ATOM   17921 C  CG    . GLU B  1  1215 ? 8.144   48.595  78.611  1.00 20.24 ? 1213 GLU B CG    1 
ATOM   17922 C  CD    . GLU B  1  1215 ? 8.365   47.469  77.630  1.00 17.46 ? 1213 GLU B CD    1 
ATOM   17923 O  OE1   . GLU B  1  1215 ? 9.503   47.359  77.128  1.00 16.82 ? 1213 GLU B OE1   1 
ATOM   17924 O  OE2   . GLU B  1  1215 ? 7.418   46.700  77.400  1.00 19.34 ? 1213 GLU B OE2   1 
ATOM   17925 N  N     . VAL B  1  1216 ? 8.257   48.586  83.247  1.00 15.72 ? 1214 VAL B N     1 
ATOM   17926 C  CA    . VAL B  1  1216 ? 8.550   47.879  84.487  1.00 15.28 ? 1214 VAL B CA    1 
ATOM   17927 C  C     . VAL B  1  1216 ? 7.479   46.834  84.715  1.00 15.74 ? 1214 VAL B C     1 
ATOM   17928 O  O     . VAL B  1  1216 ? 6.285   47.136  84.660  1.00 16.60 ? 1214 VAL B O     1 
ATOM   17929 C  CB    . VAL B  1  1216 ? 8.644   48.830  85.691  1.00 16.54 ? 1214 VAL B CB    1 
ATOM   17930 C  CG1   . VAL B  1  1216 ? 8.881   48.029  86.980  1.00 18.79 ? 1214 VAL B CG1   1 
ATOM   17931 C  CG2   . VAL B  1  1216 ? 9.771   49.815  85.459  1.00 18.54 ? 1214 VAL B CG2   1 
ATOM   17932 N  N     . SER B  1  1217 ? 7.917   45.606  84.973  1.00 14.56 ? 1215 SER B N     1 
ATOM   17933 C  CA    . SER B  1  1217 ? 7.047   44.498  85.313  1.00 14.27 ? 1215 SER B CA    1 
ATOM   17934 C  C     . SER B  1  1217 ? 7.200   44.211  86.796  1.00 13.70 ? 1215 SER B C     1 
ATOM   17935 O  O     . SER B  1  1217 ? 8.315   44.230  87.315  1.00 16.36 ? 1215 SER B O     1 
ATOM   17936 C  CB    . SER B  1  1217 ? 7.445   43.262  84.512  1.00 17.53 ? 1215 SER B CB    1 
ATOM   17937 O  OG    . SER B  1  1217 ? 6.936   42.078  85.089  1.00 19.55 ? 1215 SER B OG    1 
ATOM   17938 N  N     . ALA B  1  1218 ? 6.083   43.997  87.483  1.00 14.81 ? 1216 ALA B N     1 
ATOM   17939 C  CA    . ALA B  1  1218 ? 6.126   43.615  88.888  1.00 15.36 ? 1216 ALA B CA    1 
ATOM   17940 C  C     . ALA B  1  1218 ? 5.213   42.427  89.107  1.00 17.00 ? 1216 ALA B C     1 
ATOM   17941 O  O     . ALA B  1  1218 ? 4.045   42.455  88.718  1.00 19.34 ? 1216 ALA B O     1 
ATOM   17942 C  CB    . ALA B  1  1218 ? 5.701   44.770  89.791  1.00 16.44 ? 1216 ALA B CB    1 
ATOM   17943 N  N     . SER B  1  1219 ? 5.748   41.377  89.720  1.00 15.26 ? 1217 SER B N     1 
ATOM   17944 C  CA    . SER B  1  1219 ? 4.973   40.176  90.004  1.00 15.82 ? 1217 SER B CA    1 
ATOM   17945 C  C     . SER B  1  1219 ? 4.889   40.018  91.510  1.00 15.83 ? 1217 SER B C     1 
ATOM   17946 O  O     . SER B  1  1219 ? 5.915   39.832  92.166  1.00 16.29 ? 1217 SER B O     1 
ATOM   17947 C  CB    . SER B  1  1219 ? 5.630   38.956  89.377  1.00 16.03 ? 1217 SER B CB    1 
ATOM   17948 O  OG    . SER B  1  1219 ? 4.879   37.783  89.645  1.00 17.27 ? 1217 SER B OG    1 
ATOM   17949 N  N     . ILE B  1  1220 ? 3.680   40.109  92.048  1.00 17.98 ? 1218 ILE B N     1 
ATOM   17950 C  CA    . ILE B  1  1220 ? 3.460   40.045  93.486  1.00 16.78 ? 1218 ILE B CA    1 
ATOM   17951 C  C     . ILE B  1  1220 ? 2.749   38.739  93.799  1.00 18.29 ? 1218 ILE B C     1 
ATOM   17952 O  O     . ILE B  1  1220 ? 1.649   38.489  93.299  1.00 18.26 ? 1218 ILE B O     1 
ATOM   17953 C  CB    . ILE B  1  1220 ? 2.632   41.239  93.976  1.00 19.50 ? 1218 ILE B CB    1 
ATOM   17954 C  CG1   . ILE B  1  1220 ? 3.330   42.549  93.617  1.00 24.61 ? 1218 ILE B CG1   1 
ATOM   17955 C  CG2   . ILE B  1  1220 ? 2.403   41.126  95.480  1.00 21.88 ? 1218 ILE B CG2   1 
ATOM   17956 C  CD1   . ILE B  1  1220 ? 2.579   43.386  92.634  1.00 32.68 ? 1218 ILE B CD1   1 
ATOM   17957 N  N     . ASN B  1  1221 ? 3.357   37.922  94.647  1.00 16.16 ? 1219 ASN B N     1 
ATOM   17958 C  CA    . ASN B  1  1221 ? 2.710   36.707  95.133  1.00 16.75 ? 1219 ASN B CA    1 
ATOM   17959 C  C     . ASN B  1  1221 ? 1.679   37.088  96.189  1.00 18.61 ? 1219 ASN B C     1 
ATOM   17960 O  O     . ASN B  1  1221 ? 2.042   37.447  97.313  1.00 21.42 ? 1219 ASN B O     1 
ATOM   17961 C  CB    . ASN B  1  1221 ? 3.776   35.775  95.696  1.00 15.18 ? 1219 ASN B CB    1 
ATOM   17962 C  CG    . ASN B  1  1221 ? 3.198   34.535  96.347  1.00 17.54 ? 1219 ASN B CG    1 
ATOM   17963 O  OD1   . ASN B  1  1221 ? 2.008   34.262  96.258  1.00 19.19 ? 1219 ASN B OD1   1 
ATOM   17964 N  ND2   . ASN B  1  1221 ? 4.065   33.771  97.017  1.00 20.10 ? 1219 ASN B ND2   1 
ATOM   17965 N  N     . THR B  1  1222 ? 0.391   36.999  95.845  1.00 16.95 ? 1220 THR B N     1 
ATOM   17966 C  CA    . THR B  1  1222 ? -0.662  37.392  96.773  1.00 16.93 ? 1220 THR B CA    1 
ATOM   17967 C  C     . THR B  1  1222 ? -1.176  36.219  97.587  1.00 22.66 ? 1220 THR B C     1 
ATOM   17968 O  O     . THR B  1  1222 ? -2.127  36.378  98.361  1.00 28.30 ? 1220 THR B O     1 
ATOM   17969 C  CB    . THR B  1  1222 ? -1.814  38.069  96.032  1.00 21.41 ? 1220 THR B CB    1 
ATOM   17970 O  OG1   . THR B  1  1222 ? -2.333  37.183  95.029  1.00 23.13 ? 1220 THR B OG1   1 
ATOM   17971 C  CG2   . THR B  1  1222 ? -1.335  39.360  95.365  1.00 21.82 ? 1220 THR B CG2   1 
ATOM   17972 N  N     . ALA B  1  1223 ? -0.562  35.053  97.439  1.00 20.74 ? 1221 ALA B N     1 
ATOM   17973 C  CA    . ALA B  1  1223 ? -0.834  33.920  98.304  1.00 25.11 ? 1221 ALA B CA    1 
ATOM   17974 C  C     . ALA B  1  1223 ? 0.205   33.775  99.405  1.00 31.97 ? 1221 ALA B C     1 
ATOM   17975 O  O     . ALA B  1  1223 ? 0.162   32.792  100.146 1.00 35.64 ? 1221 ALA B O     1 
ATOM   17976 C  CB    . ALA B  1  1223 ? -0.902  32.634  97.479  1.00 27.91 ? 1221 ALA B CB    1 
ATOM   17977 N  N     . ALA B  1  1224 ? 1.141   34.728  99.522  1.00 32.01 ? 1222 ALA B N     1 
ATOM   17978 C  CA    . ALA B  1  1224 ? 2.312   34.527  100.374 1.00 35.94 ? 1222 ALA B CA    1 
ATOM   17979 C  C     . ALA B  1  1224 ? 1.959   34.424  101.854 1.00 45.05 ? 1222 ALA B C     1 
ATOM   17980 O  O     . ALA B  1  1224 ? 2.725   33.820  102.613 1.00 38.37 ? 1222 ALA B O     1 
ATOM   17981 C  CB    . ALA B  1  1224 ? 3.331   35.650  100.158 1.00 30.99 ? 1222 ALA B CB    1 
ATOM   17982 N  N     . ALA B  1  1225 ? 0.823   34.989  102.284 1.00 36.13 ? 1223 ALA B N     1 
ATOM   17983 C  CA    . ALA B  1  1225 ? 0.403   34.874  103.677 1.00 40.02 ? 1223 ALA B CA    1 
ATOM   17984 C  C     . ALA B  1  1225 ? -0.189  33.512  104.005 1.00 47.28 ? 1223 ALA B C     1 
ATOM   17985 O  O     . ALA B  1  1225 ? -0.532  33.272  105.168 1.00 41.08 ? 1223 ALA B O     1 
ATOM   17986 C  CB    . ALA B  1  1225 ? -0.610  35.970  104.031 1.00 41.29 ? 1223 ALA B CB    1 
ATOM   17987 N  N     . GLY B  1  1226 ? -0.319  32.624  103.024 1.00 41.03 ? 1224 GLY B N     1 
ATOM   17988 C  CA    . GLY B  1  1226 ? -0.830  31.291  103.257 1.00 38.91 ? 1224 GLY B CA    1 
ATOM   17989 C  C     . GLY B  1  1226 ? -2.185  30.994  102.656 1.00 45.87 ? 1224 GLY B C     1 
ATOM   17990 O  O     . GLY B  1  1226 ? -2.743  29.927  102.939 1.00 37.70 ? 1224 GLY B O     1 
ATOM   17991 N  N     . GLY B  1  1227 ? -2.730  31.889  101.840 1.00 34.51 ? 1225 GLY B N     1 
ATOM   17992 C  CA    . GLY B  1  1227 ? -4.031  31.666  101.234 1.00 36.77 ? 1225 GLY B CA    1 
ATOM   17993 C  C     . GLY B  1  1227 ? -4.322  32.740  100.210 1.00 43.59 ? 1225 GLY B C     1 
ATOM   17994 O  O     . GLY B  1  1227 ? -3.615  33.748  100.116 1.00 39.19 ? 1225 GLY B O     1 
ATOM   17995 N  N     . ASN B  1  1228 ? -5.391  32.515  99.447  1.00 34.32 ? 1226 ASN B N     1 
ATOM   17996 C  CA    . ASN B  1  1228 ? -5.780  33.395  98.346  1.00 38.57 ? 1226 ASN B CA    1 
ATOM   17997 C  C     . ASN B  1  1228 ? -7.077  34.105  98.724  1.00 45.80 ? 1226 ASN B C     1 
ATOM   17998 O  O     . ASN B  1  1228 ? -8.137  33.473  98.808  1.00 46.21 ? 1226 ASN B O     1 
ATOM   17999 C  CB    . ASN B  1  1228 ? -5.931  32.595  97.049  1.00 36.98 ? 1226 ASN B CB    1 
ATOM   18000 C  CG    . ASN B  1  1228 ? -6.206  33.468  95.833  1.00 43.61 ? 1226 ASN B CG    1 
ATOM   18001 O  OD1   . ASN B  1  1228 ? -6.851  34.513  95.924  1.00 45.33 ? 1226 ASN B OD1   1 
ATOM   18002 N  ND2   . ASN B  1  1228 ? -5.720  33.030  94.678  1.00 39.91 ? 1226 ASN B ND2   1 
ATOM   18003 N  N     . ALA B  1  1229 ? -6.990  35.423  98.935  1.00 43.68 ? 1227 ALA B N     1 
ATOM   18004 C  CA    . ALA B  1  1229 ? -8.170  36.209  99.289  1.00 51.29 ? 1227 ALA B CA    1 
ATOM   18005 C  C     . ALA B  1  1229 ? -9.240  36.123  98.208  1.00 50.86 ? 1227 ALA B C     1 
ATOM   18006 O  O     . ALA B  1  1229 ? -10.407 35.830  98.496  1.00 51.32 ? 1227 ALA B O     1 
ATOM   18007 C  CB    . ALA B  1  1229 ? -7.779  37.668  99.530  1.00 41.47 ? 1227 ALA B CB    1 
ATOM   18008 N  N     . SER B  1  1230 ? -8.860  36.385  96.952  1.00 48.91 ? 1228 SER B N     1 
ATOM   18009 C  CA    . SER B  1  1230 ? -9.834  36.396  95.864  1.00 47.40 ? 1228 SER B CA    1 
ATOM   18010 C  C     . SER B  1  1230 ? -10.528 35.048  95.716  1.00 52.20 ? 1228 SER B C     1 
ATOM   18011 O  O     . SER B  1  1230 ? -11.712 34.994  95.365  1.00 51.02 ? 1228 SER B O     1 
ATOM   18012 C  CB    . SER B  1  1230 ? -9.151  36.794  94.553  1.00 46.11 ? 1228 SER B CB    1 
ATOM   18013 N  N     . LEU B  1  1231 ? -9.819  33.958  95.989  1.00 49.29 ? 1229 LEU B N     1 
ATOM   18014 C  CA    . LEU B  1  1231 ? -10.396 32.624  95.903  1.00 49.55 ? 1229 LEU B CA    1 
ATOM   18015 C  C     . LEU B  1  1231 ? -10.936 32.175  97.259  1.00 53.22 ? 1229 LEU B C     1 
ATOM   18016 O  O     . LEU B  1  1231 ? -12.005 31.566  97.343  1.00 60.81 ? 1229 LEU B O     1 
ATOM   18017 C  CB    . LEU B  1  1231 ? -9.356  31.627  95.388  1.00 49.71 ? 1229 LEU B CB    1 
ATOM   18018 C  CG    . LEU B  1  1231 ? -9.298  31.277  93.900  1.00 38.77 ? 1229 LEU B CG    1 
ATOM   18019 C  CD1   . LEU B  1  1231 ? -8.960  32.498  93.062  1.00 48.23 ? 1229 LEU B CD1   1 
ATOM   18020 C  CD2   . LEU B  1  1231 ? -8.279  30.164  93.676  1.00 30.03 ? 1229 LEU B CD2   1 
HETATM 18021 P  PA    A FAD C  2  .    ? -37.631 43.542  82.617  0.48 24.18 ? 2001 FAD A PA    1 
HETATM 18022 P  PA    B FAD C  2  .    ? -37.611 43.514  82.680  0.52 24.07 ? 2001 FAD A PA    1 
HETATM 18023 O  O1A   A FAD C  2  .    ? -36.180 42.998  82.510  0.48 26.77 ? 2001 FAD A O1A   1 
HETATM 18024 O  O1A   B FAD C  2  .    ? -36.171 42.959  82.519  0.52 26.81 ? 2001 FAD A O1A   1 
HETATM 18025 O  O2A   A FAD C  2  .    ? -38.678 42.623  83.007  0.48 25.68 ? 2001 FAD A O2A   1 
HETATM 18026 O  O2A   B FAD C  2  .    ? -38.673 42.602  83.048  0.52 25.62 ? 2001 FAD A O2A   1 
HETATM 18027 O  O5B   A FAD C  2  .    ? -37.851 44.602  83.621  0.48 23.88 ? 2001 FAD A O5B   1 
HETATM 18028 O  O5B   B FAD C  2  .    ? -37.803 44.550  83.714  0.52 23.65 ? 2001 FAD A O5B   1 
HETATM 18029 C  C5B   A FAD C  2  .    ? -36.796 45.513  83.896  0.48 23.58 ? 2001 FAD A C5B   1 
HETATM 18030 C  C5B   B FAD C  2  .    ? -36.771 45.504  83.922  0.52 23.58 ? 2001 FAD A C5B   1 
HETATM 18031 C  C4B   A FAD C  2  .    ? -37.277 46.570  84.881  0.48 22.24 ? 2001 FAD A C4B   1 
HETATM 18032 C  C4B   B FAD C  2  .    ? -37.262 46.570  84.891  0.52 22.24 ? 2001 FAD A C4B   1 
HETATM 18033 O  O4B   A FAD C  2  .    ? -37.243 46.103  86.194  0.48 21.05 ? 2001 FAD A O4B   1 
HETATM 18034 O  O4B   B FAD C  2  .    ? -37.240 46.105  86.204  0.52 21.03 ? 2001 FAD A O4B   1 
HETATM 18035 C  C3B   A FAD C  2  .    ? -36.456 47.819  84.913  0.48 21.68 ? 2001 FAD A C3B   1 
HETATM 18036 C  C3B   B FAD C  2  .    ? -36.442 47.821  84.928  0.52 21.65 ? 2001 FAD A C3B   1 
HETATM 18037 O  O3B   A FAD C  2  .    ? -36.654 48.686  83.848  0.48 21.53 ? 2001 FAD A O3B   1 
HETATM 18038 O  O3B   B FAD C  2  .    ? -36.624 48.688  83.860  0.52 21.50 ? 2001 FAD A O3B   1 
HETATM 18039 C  C2B   A FAD C  2  .    ? -36.905 48.416  86.190  0.48 21.55 ? 2001 FAD A C2B   1 
HETATM 18040 C  C2B   B FAD C  2  .    ? -36.908 48.418  86.199  0.52 21.56 ? 2001 FAD A C2B   1 
HETATM 18041 O  O2B   A FAD C  2  .    ? -38.111 49.080  86.090  0.48 19.73 ? 2001 FAD A O2B   1 
HETATM 18042 O  O2B   B FAD C  2  .    ? -38.122 49.066  86.092  0.52 19.71 ? 2001 FAD A O2B   1 
HETATM 18043 C  C1B   A FAD C  2  .    ? -37.110 47.213  87.036  0.48 21.31 ? 2001 FAD A C1B   1 
HETATM 18044 C  C1B   B FAD C  2  .    ? -37.108 47.215  87.045  0.52 21.31 ? 2001 FAD A C1B   1 
HETATM 18045 N  N9A   A FAD C  2  .    ? -36.030 46.964  87.948  0.48 23.02 ? 2001 FAD A N9A   1 
HETATM 18046 N  N9A   B FAD C  2  .    ? -36.027 46.965  87.954  0.52 23.02 ? 2001 FAD A N9A   1 
HETATM 18047 C  C8A   A FAD C  2  .    ? -34.734 46.615  87.616  0.48 25.51 ? 2001 FAD A C8A   1 
HETATM 18048 C  C8A   B FAD C  2  .    ? -34.731 46.618  87.622  0.52 25.52 ? 2001 FAD A C8A   1 
HETATM 18049 N  N7A   A FAD C  2  .    ? -34.020 46.458  88.736  0.48 22.45 ? 2001 FAD A N7A   1 
HETATM 18050 N  N7A   B FAD C  2  .    ? -34.018 46.460  88.742  0.52 22.44 ? 2001 FAD A N7A   1 
HETATM 18051 C  C5A   A FAD C  2  .    ? -34.829 46.688  89.839  0.48 22.23 ? 2001 FAD A C5A   1 
HETATM 18052 C  C5A   B FAD C  2  .    ? -34.828 46.688  89.845  0.52 22.23 ? 2001 FAD A C5A   1 
HETATM 18053 C  C6A   A FAD C  2  .    ? -34.637 46.663  91.210  0.48 21.81 ? 2001 FAD A C6A   1 
HETATM 18054 C  C6A   B FAD C  2  .    ? -34.639 46.661  91.216  0.52 21.80 ? 2001 FAD A C6A   1 
HETATM 18055 N  N6A   A FAD C  2  .    ? -33.349 46.337  91.771  0.48 23.28 ? 2001 FAD A N6A   1 
HETATM 18056 N  N6A   B FAD C  2  .    ? -33.353 46.336  91.780  0.52 23.27 ? 2001 FAD A N6A   1 
HETATM 18057 N  N1A   A FAD C  2  .    ? -35.665 46.948  92.026  0.48 21.60 ? 2001 FAD A N1A   1 
HETATM 18058 N  N1A   B FAD C  2  .    ? -35.669 46.945  92.030  0.52 21.60 ? 2001 FAD A N1A   1 
HETATM 18059 C  C2A   A FAD C  2  .    ? -36.897 47.258  91.548  0.48 21.19 ? 2001 FAD A C2A   1 
HETATM 18060 C  C2A   B FAD C  2  .    ? -36.901 47.254  91.550  0.52 21.19 ? 2001 FAD A C2A   1 
HETATM 18061 N  N3A   A FAD C  2  .    ? -37.121 47.290  90.209  0.48 21.45 ? 2001 FAD A N3A   1 
HETATM 18062 N  N3A   B FAD C  2  .    ? -37.123 47.287  90.212  0.52 21.44 ? 2001 FAD A N3A   1 
HETATM 18063 C  C4A   A FAD C  2  .    ? -36.125 47.014  89.352  0.48 22.63 ? 2001 FAD A C4A   1 
HETATM 18064 C  C4A   B FAD C  2  .    ? -36.124 47.013  89.357  0.52 22.63 ? 2001 FAD A C4A   1 
HETATM 18065 N  N1    A FAD C  2  .    ? -40.514 53.780  81.295  0.48 20.21 ? 2001 FAD A N1    1 
HETATM 18066 N  N1    B FAD C  2  .    ? -40.948 53.590  81.716  0.52 16.45 ? 2001 FAD A N1    1 
HETATM 18067 C  C2    A FAD C  2  .    ? -41.024 54.828  82.125  0.48 18.68 ? 2001 FAD A C2    1 
HETATM 18068 C  C2    B FAD C  2  .    ? -41.191 54.866  82.304  0.52 18.19 ? 2001 FAD A C2    1 
HETATM 18069 O  O2    A FAD C  2  .    ? -40.450 55.056  83.308  0.48 17.10 ? 2001 FAD A O2    1 
HETATM 18070 O  O2    B FAD C  2  .    ? -40.688 55.144  83.512  0.52 18.00 ? 2001 FAD A O2    1 
HETATM 18071 N  N3    A FAD C  2  .    ? -42.004 55.677  81.668  0.48 19.09 ? 2001 FAD A N3    1 
HETATM 18072 N  N3    B FAD C  2  .    ? -41.930 55.823  81.636  0.52 19.05 ? 2001 FAD A N3    1 
HETATM 18073 C  C4    A FAD C  2  .    ? -42.586 55.447  80.452  0.48 19.62 ? 2001 FAD A C4    1 
HETATM 18074 C  C4    B FAD C  2  .    ? -42.450 55.557  80.392  0.52 19.78 ? 2001 FAD A C4    1 
HETATM 18075 O  O4    A FAD C  2  .    ? -43.563 56.303  80.044  0.48 16.08 ? 2001 FAD A O4    1 
HETATM 18076 O  O4    B FAD C  2  .    ? -43.188 56.510  79.757  0.52 19.88 ? 2001 FAD A O4    1 
HETATM 18077 C  C4X   A FAD C  2  .    ? -42.267 54.209  79.678  0.48 20.17 ? 2001 FAD A C4X   1 
HETATM 18078 C  C4X   B FAD C  2  .    ? -42.260 54.231  79.746  0.52 20.17 ? 2001 FAD A C4X   1 
HETATM 18079 N  N5    A FAD C  2  .    ? -42.987 53.795  78.560  0.48 21.16 ? 2001 FAD A N5    1 
HETATM 18080 N  N5    B FAD C  2  .    ? -42.805 53.900  78.501  0.52 20.67 ? 2001 FAD A N5    1 
HETATM 18081 C  C5X   A FAD C  2  .    ? -42.641 52.600  77.922  0.48 19.70 ? 2001 FAD A C5X   1 
HETATM 18082 C  C5X   B FAD C  2  .    ? -42.593 52.619  77.984  0.52 19.66 ? 2001 FAD A C5X   1 
HETATM 18083 C  C6    A FAD C  2  .    ? -43.351 52.176  76.791  0.48 19.54 ? 2001 FAD A C6    1 
HETATM 18084 C  C6    B FAD C  2  .    ? -43.129 52.240  76.740  0.52 19.31 ? 2001 FAD A C6    1 
HETATM 18085 C  C7    A FAD C  2  .    ? -43.017 50.990  76.150  0.48 19.61 ? 2001 FAD A C7    1 
HETATM 18086 C  C7    B FAD C  2  .    ? -42.900 50.955  76.247  0.52 19.69 ? 2001 FAD A C7    1 
HETATM 18087 C  C7M   A FAD C  2  .    ? -43.812 50.560  74.946  0.48 18.42 ? 2001 FAD A C7M   1 
HETATM 18088 C  C7M   B FAD C  2  .    ? -43.476 50.527  74.926  0.52 20.42 ? 2001 FAD A C7M   1 
HETATM 18089 C  C8    A FAD C  2  .    ? -41.976 50.206  76.617  0.48 20.01 ? 2001 FAD A C8    1 
HETATM 18090 C  C8    B FAD C  2  .    ? -42.154 50.036  76.960  0.52 19.05 ? 2001 FAD A C8    1 
HETATM 18091 C  C8M   A FAD C  2  .    ? -41.609 48.926  75.927  0.48 21.00 ? 2001 FAD A C8M   1 
HETATM 18092 C  C8M   B FAD C  2  .    ? -41.917 48.659  76.414  0.52 18.89 ? 2001 FAD A C8M   1 
HETATM 18093 C  C9    A FAD C  2  .    ? -41.259 50.614  77.740  0.48 20.94 ? 2001 FAD A C9    1 
HETATM 18094 C  C9    B FAD C  2  .    ? -41.621 50.396  78.194  0.52 21.21 ? 2001 FAD A C9    1 
HETATM 18095 C  C9A   A FAD C  2  .    ? -41.595 51.797  78.381  0.48 20.42 ? 2001 FAD A C9A   1 
HETATM 18096 C  C9A   B FAD C  2  .    ? -41.840 51.675  78.693  0.52 21.16 ? 2001 FAD A C9A   1 
HETATM 18097 N  N10   A FAD C  2  .    ? -40.860 52.195  79.524  0.48 18.58 ? 2001 FAD A N10   1 
HETATM 18098 N  N10   B FAD C  2  .    ? -41.274 52.008  79.954  0.52 21.14 ? 2001 FAD A N10   1 
HETATM 18099 C  C10   A FAD C  2  .    ? -41.196 53.388  80.176  0.48 18.67 ? 2001 FAD A C10   1 
HETATM 18100 C  C10   B FAD C  2  .    ? -41.483 53.276  80.490  0.52 18.57 ? 2001 FAD A C10   1 
HETATM 18101 C  "C1'" A FAD C  2  .    ? -39.732 51.368  80.013  0.48 22.24 ? 2001 FAD A "C1'" 1 
HETATM 18102 C  "C1'" B FAD C  2  .    ? -40.511 50.999  80.716  0.52 19.87 ? 2001 FAD A "C1'" 1 
HETATM 18103 C  "C2'" A FAD C  2  .    ? -40.164 50.297  80.996  0.48 22.19 ? 2001 FAD A "C2'" 1 
HETATM 18104 C  "C2'" B FAD C  2  .    ? -38.998 51.135  80.701  0.52 21.48 ? 2001 FAD A "C2'" 1 
HETATM 18105 O  "O2'" A FAD C  2  .    ? -40.654 50.902  82.122  0.48 20.93 ? 2001 FAD A "O2'" 1 
HETATM 18106 O  "O2'" B FAD C  2  .    ? -38.525 51.930  79.683  0.52 21.20 ? 2001 FAD A "O2'" 1 
HETATM 18107 C  "C3'" A FAD C  2  .    ? -38.991 49.359  81.342  0.48 20.59 ? 2001 FAD A "C3'" 1 
HETATM 18108 C  "C3'" B FAD C  2  .    ? -38.420 49.724  80.549  0.52 20.25 ? 2001 FAD A "C3'" 1 
HETATM 18109 O  "O3'" A FAD C  2  .    ? -37.917 50.089  81.822  0.48 20.53 ? 2001 FAD A "O3'" 1 
HETATM 18110 O  "O3'" B FAD C  2  .    ? -38.500 49.370  79.223  0.52 23.17 ? 2001 FAD A "O3'" 1 
HETATM 18111 C  "C4'" A FAD C  2  .    ? -38.487 48.501  80.190  0.48 23.96 ? 2001 FAD A "C4'" 1 
HETATM 18112 C  "C4'" B FAD C  2  .    ? -39.126 48.664  81.373  0.52 21.25 ? 2001 FAD A "C4'" 1 
HETATM 18113 O  "O4'" A FAD C  2  .    ? -39.457 48.341  79.228  0.48 23.96 ? 2001 FAD A "O4'" 1 
HETATM 18114 O  "O4'" B FAD C  2  .    ? -39.159 49.037  82.696  0.52 18.51 ? 2001 FAD A "O4'" 1 
HETATM 18115 C  "C5'" A FAD C  2  .    ? -37.993 47.133  80.654  0.48 22.71 ? 2001 FAD A "C5'" 1 
HETATM 18116 C  "C5'" B FAD C  2  .    ? -38.446 47.309  81.203  0.52 21.67 ? 2001 FAD A "C5'" 1 
HETATM 18117 O  "O5'" A FAD C  2  .    ? -39.001 46.474  81.387  0.48 24.11 ? 2001 FAD A "O5'" 1 
HETATM 18118 O  "O5'" B FAD C  2  .    ? -39.206 46.324  81.869  0.52 22.68 ? 2001 FAD A "O5'" 1 
HETATM 18119 P  P     A FAD C  2  .    ? -39.498 44.994  81.011  0.48 22.47 ? 2001 FAD A P     1 
HETATM 18120 P  P     B FAD C  2  .    ? -39.561 44.916  81.178  0.52 25.23 ? 2001 FAD A P     1 
HETATM 18121 O  O1P   A FAD C  2  .    ? -40.896 44.552  81.589  0.48 25.57 ? 2001 FAD A O1P   1 
HETATM 18122 O  O1P   B FAD C  2  .    ? -40.931 44.229  81.541  0.52 27.43 ? 2001 FAD A O1P   1 
HETATM 18123 O  O2P   A FAD C  2  .    ? -39.300 45.051  79.451  0.48 24.34 ? 2001 FAD A O2P   1 
HETATM 18124 O  O2P   B FAD C  2  .    ? -39.280 45.271  79.677  0.52 23.85 ? 2001 FAD A O2P   1 
HETATM 18125 O  O3P   A FAD C  2  .    ? -38.206 44.054  81.333  0.48 23.86 ? 2001 FAD A O3P   1 
HETATM 18126 O  O3P   B FAD C  2  .    ? -38.189 44.088  81.431  0.52 23.78 ? 2001 FAD A O3P   1 
HETATM 18127 C  C1    . PEG D  3  .    ? -2.364  61.900  96.311  1.00 34.41 ? 2002 PEG A C1    1 
HETATM 18128 O  O1    . PEG D  3  .    ? -3.028  60.721  95.907  1.00 43.50 ? 2002 PEG A O1    1 
HETATM 18129 C  C2    . PEG D  3  .    ? -0.934  61.608  96.618  1.00 26.94 ? 2002 PEG A C2    1 
HETATM 18130 O  O2    . PEG D  3  .    ? -0.267  62.808  96.890  1.00 37.75 ? 2002 PEG A O2    1 
HETATM 18131 C  C3    . PEG D  3  .    ? 1.115   62.604  97.039  1.00 32.54 ? 2002 PEG A C3    1 
HETATM 18132 C  C4    . PEG D  3  .    ? 1.659   61.837  95.866  1.00 37.96 ? 2002 PEG A C4    1 
HETATM 18133 O  O4    . PEG D  3  .    ? 2.286   60.663  96.331  1.00 45.74 ? 2002 PEG A O4    1 
HETATM 18134 C  C01   . 53E E  4  .    ? -24.961 74.073  104.662 0.83 32.82 ? 2003 53E A C01   1 
HETATM 18135 C  C02   . 53E E  4  .    ? -24.957 73.498  103.263 0.83 37.77 ? 2003 53E A C02   1 
HETATM 18136 O  O03   . 53E E  4  .    ? -24.125 74.205  102.396 0.83 32.45 ? 2003 53E A O03   1 
HETATM 18137 C  C04   . 53E E  4  .    ? -22.803 74.297  102.920 0.83 32.03 ? 2003 53E A C04   1 
HETATM 18138 C  C05   . 53E E  4  .    ? -21.697 74.412  102.054 0.83 27.61 ? 2003 53E A C05   1 
HETATM 18139 C  C06   . 53E E  4  .    ? -20.413 74.490  102.574 0.83 27.57 ? 2003 53E A C06   1 
HETATM 18140 C  C07   . 53E E  4  .    ? -20.216 74.458  103.951 0.83 34.79 ? 2003 53E A C07   1 
HETATM 18141 C  C08   . 53E E  4  .    ? -21.301 74.335  104.807 0.83 30.73 ? 2003 53E A C08   1 
HETATM 18142 C  C09   . 53E E  4  .    ? -22.604 74.264  104.293 0.83 29.46 ? 2003 53E A C09   1 
HETATM 18143 O  O10   . 53E E  4  .    ? -23.686 74.135  105.225 0.83 38.57 ? 2003 53E A O10   1 
HETATM 18144 C  C11   . 53E E  4  .    ? -21.844 74.459  100.537 0.83 22.90 ? 2003 53E A C11   1 
HETATM 18145 O  O12   . 53E E  4  .    ? -22.731 75.164  99.985  0.83 21.77 ? 2003 53E A O12   1 
HETATM 18146 O  O13   . 53E E  4  .    ? -21.047 73.773  99.844  0.83 21.22 ? 2003 53E A O13   1 
HETATM 18147 C  C     . FMT F  5  .    ? -40.329 61.475  102.886 1.00 24.29 ? 2004 FMT A C     1 
HETATM 18148 O  O1    . FMT F  5  .    ? -39.513 61.000  103.691 1.00 32.69 ? 2004 FMT A O1    1 
HETATM 18149 O  O2    . FMT F  5  .    ? -41.574 61.351  102.847 1.00 34.87 ? 2004 FMT A O2    1 
HETATM 18150 C  C1    . PEG G  3  .    ? -51.740 76.514  73.716  1.00 37.81 ? 2005 PEG A C1    1 
HETATM 18151 O  O1    . PEG G  3  .    ? -51.697 77.749  74.402  1.00 49.85 ? 2005 PEG A O1    1 
HETATM 18152 C  C2    . PEG G  3  .    ? -50.766 76.500  72.558  1.00 38.92 ? 2005 PEG A C2    1 
HETATM 18153 O  O2    . PEG G  3  .    ? -49.444 76.663  73.020  1.00 41.97 ? 2005 PEG A O2    1 
HETATM 18154 C  C3    . PEG G  3  .    ? -48.489 76.784  71.992  1.00 35.64 ? 2005 PEG A C3    1 
HETATM 18155 C  C4    . PEG G  3  .    ? -47.146 76.337  72.516  1.00 34.37 ? 2005 PEG A C4    1 
HETATM 18156 O  O4    . PEG G  3  .    ? -46.549 77.345  73.303  1.00 41.99 ? 2005 PEG A O4    1 
HETATM 18157 C  C     . FMT H  5  .    ? -63.218 62.181  97.690  1.00 36.91 ? 2006 FMT A C     1 
HETATM 18158 O  O1    . FMT H  5  .    ? -62.756 62.467  98.806  1.00 46.29 ? 2006 FMT A O1    1 
HETATM 18159 O  O2    . FMT H  5  .    ? -64.324 61.677  97.409  1.00 51.21 ? 2006 FMT A O2    1 
HETATM 18160 C  C1    . PEG I  3  .    ? -44.588 88.998  114.723 1.00 55.00 ? 2007 PEG A C1    1 
HETATM 18161 O  O1    . PEG I  3  .    ? -44.085 89.119  113.409 1.00 46.92 ? 2007 PEG A O1    1 
HETATM 18162 C  C2    . PEG I  3  .    ? -43.833 87.918  115.457 1.00 48.67 ? 2007 PEG A C2    1 
HETATM 18163 O  O2    . PEG I  3  .    ? -43.054 88.478  116.485 1.00 60.55 ? 2007 PEG A O2    1 
HETATM 18164 C  C3    . PEG I  3  .    ? -41.970 89.234  116.000 1.00 44.72 ? 2007 PEG A C3    1 
HETATM 18165 C  C4    . PEG I  3  .    ? -41.867 90.549  116.733 1.00 52.33 ? 2007 PEG A C4    1 
HETATM 18166 O  O4    . PEG I  3  .    ? -41.000 90.422  117.839 1.00 54.67 ? 2007 PEG A O4    1 
HETATM 18167 P  PA    . NAD J  6  .    ? -18.062 88.355  107.440 0.74 32.65 ? 2008 NAD A PA    1 
HETATM 18168 O  O1A   . NAD J  6  .    ? -16.519 88.427  107.379 0.74 29.81 ? 2008 NAD A O1A   1 
HETATM 18169 O  O2A   . NAD J  6  .    ? -18.828 89.531  107.055 0.74 32.21 ? 2008 NAD A O2A   1 
HETATM 18170 O  O5B   . NAD J  6  .    ? -18.713 88.049  108.737 0.74 32.92 ? 2008 NAD A O5B   1 
HETATM 18171 C  C5B   . NAD J  6  .    ? -18.463 86.833  109.416 0.74 27.44 ? 2008 NAD A C5B   1 
HETATM 18172 C  C4B   . NAD J  6  .    ? -18.329 87.063  110.919 0.74 28.38 ? 2008 NAD A C4B   1 
HETATM 18173 O  O4B   . NAD J  6  .    ? -17.199 87.860  111.236 0.74 28.63 ? 2008 NAD A O4B   1 
HETATM 18174 C  C3B   . NAD J  6  .    ? -19.533 87.680  111.566 0.74 27.46 ? 2008 NAD A C3B   1 
HETATM 18175 O  O3B   . NAD J  6  .    ? -19.936 86.957  112.670 0.74 29.25 ? 2008 NAD A O3B   1 
HETATM 18176 C  C2B   . NAD J  6  .    ? -19.075 89.035  111.938 0.74 35.32 ? 2008 NAD A C2B   1 
HETATM 18177 O  O2B   . NAD J  6  .    ? -19.729 89.511  113.052 0.74 31.12 ? 2008 NAD A O2B   1 
HETATM 18178 C  C1B   . NAD J  6  .    ? -17.640 88.786  112.200 0.74 35.69 ? 2008 NAD A C1B   1 
HETATM 18179 N  N9A   . NAD J  6  .    ? -16.762 89.942  112.211 0.74 28.80 ? 2008 NAD A N9A   1 
HETATM 18180 C  C8A   . NAD J  6  .    ? -16.804 91.054  111.392 0.74 32.72 ? 2008 NAD A C8A   1 
HETATM 18181 N  N7A   . NAD J  6  .    ? -15.789 91.868  111.698 0.74 30.80 ? 2008 NAD A N7A   1 
HETATM 18182 C  C5A   . NAD J  6  .    ? -15.044 91.311  112.728 0.74 31.58 ? 2008 NAD A C5A   1 
HETATM 18183 C  C6A   . NAD J  6  .    ? -13.922 91.696  113.429 0.74 34.67 ? 2008 NAD A C6A   1 
HETATM 18184 N  N6A   . NAD J  6  .    ? -13.286 92.941  113.113 0.74 35.18 ? 2008 NAD A N6A   1 
HETATM 18185 N  N1A   . NAD J  6  .    ? -13.430 90.914  114.395 0.74 30.86 ? 2008 NAD A N1A   1 
HETATM 18186 C  C2A   . NAD J  6  .    ? -14.000 89.727  114.720 0.74 30.37 ? 2008 NAD A C2A   1 
HETATM 18187 N  N3A   . NAD J  6  .    ? -15.110 89.315  114.054 0.74 28.86 ? 2008 NAD A N3A   1 
HETATM 18188 C  C4A   . NAD J  6  .    ? -15.643 90.073  113.069 0.74 31.13 ? 2008 NAD A C4A   1 
HETATM 18189 O  O3    . NAD J  6  .    ? -18.699 87.401  106.498 0.74 30.81 ? 2008 NAD A O3    1 
HETATM 18190 P  PN    . NAD J  6  .    ? -20.229 87.068  106.265 0.74 33.42 ? 2008 NAD A PN    1 
HETATM 18191 O  O1N   . NAD J  6  .    ? -20.823 88.134  105.393 0.74 31.92 ? 2008 NAD A O1N   1 
HETATM 18192 O  O2N   . NAD J  6  .    ? -20.980 86.872  107.547 0.74 26.79 ? 2008 NAD A O2N   1 
HETATM 18193 O  O5D   . NAD J  6  .    ? -20.220 85.727  105.432 0.74 28.34 ? 2008 NAD A O5D   1 
HETATM 18194 C  C5D   . NAD J  6  .    ? -19.898 85.796  104.076 0.74 32.77 ? 2008 NAD A C5D   1 
HETATM 18195 C  C4D   . NAD J  6  .    ? -18.483 85.314  103.858 0.74 25.82 ? 2008 NAD A C4D   1 
HETATM 18196 O  O4D   . NAD J  6  .    ? -18.285 84.085  104.496 0.74 27.81 ? 2008 NAD A O4D   1 
HETATM 18197 C  C3D   . NAD J  6  .    ? -18.177 85.145  102.413 0.74 28.55 ? 2008 NAD A C3D   1 
HETATM 18198 O  O3D   . NAD J  6  .    ? -16.986 85.739  102.087 0.74 32.47 ? 2008 NAD A O3D   1 
HETATM 18199 C  C2D   . NAD J  6  .    ? -18.101 83.681  102.278 0.74 25.96 ? 2008 NAD A C2D   1 
HETATM 18200 O  O2D   . NAD J  6  .    ? -17.370 83.235  101.185 0.74 30.16 ? 2008 NAD A O2D   1 
HETATM 18201 C  C1D   . NAD J  6  .    ? -17.553 83.305  103.604 0.74 28.61 ? 2008 NAD A C1D   1 
HETATM 18202 N  N1N   . NAD J  6  .    ? -17.850 81.941  103.911 0.74 27.80 ? 2008 NAD A N1N   1 
HETATM 18203 C  C2N   . NAD J  6  .    ? -16.851 80.949  103.860 0.74 24.28 ? 2008 NAD A C2N   1 
HETATM 18204 C  C3N   . NAD J  6  .    ? -17.222 79.647  104.176 0.74 29.02 ? 2008 NAD A C3N   1 
HETATM 18205 C  C7N   . NAD J  6  .    ? -16.221 78.552  104.139 0.74 21.50 ? 2008 NAD A C7N   1 
HETATM 18206 O  O7N   . NAD J  6  .    ? -16.502 77.496  104.672 0.74 25.93 ? 2008 NAD A O7N   1 
HETATM 18207 N  N7N   . NAD J  6  .    ? -14.976 78.746  103.460 0.74 21.40 ? 2008 NAD A N7N   1 
HETATM 18208 C  C4N   . NAD J  6  .    ? -18.551 79.347  104.536 0.74 36.89 ? 2008 NAD A C4N   1 
HETATM 18209 C  C5N   . NAD J  6  .    ? -19.543 80.350  104.582 0.74 33.68 ? 2008 NAD A C5N   1 
HETATM 18210 C  C6N   . NAD J  6  .    ? -19.180 81.648  104.268 0.74 26.48 ? 2008 NAD A C6N   1 
HETATM 18211 S  S     . SO4 K  7  .    ? -9.120  52.975  111.202 1.00 20.15 ? 2009 SO4 A S     1 
HETATM 18212 O  O1    . SO4 K  7  .    ? -8.045  53.238  110.211 1.00 22.39 ? 2009 SO4 A O1    1 
HETATM 18213 O  O2    . SO4 K  7  .    ? -10.198 52.150  110.591 1.00 23.88 ? 2009 SO4 A O2    1 
HETATM 18214 O  O3    . SO4 K  7  .    ? -8.567  52.260  112.401 1.00 20.33 ? 2009 SO4 A O3    1 
HETATM 18215 O  O4    . SO4 K  7  .    ? -9.671  54.305  111.619 1.00 25.20 ? 2009 SO4 A O4    1 
HETATM 18216 S  S     . SO4 L  7  .    ? -12.386 75.350  70.260  0.73 30.45 ? 2010 SO4 A S     1 
HETATM 18217 O  O1    . SO4 L  7  .    ? -12.082 74.135  69.437  0.73 37.57 ? 2010 SO4 A O1    1 
HETATM 18218 O  O2    . SO4 L  7  .    ? -12.680 76.507  69.354  0.73 40.44 ? 2010 SO4 A O2    1 
HETATM 18219 O  O3    . SO4 L  7  .    ? -13.608 75.073  71.078  0.73 25.38 ? 2010 SO4 A O3    1 
HETATM 18220 O  O4    . SO4 L  7  .    ? -11.204 75.653  71.118  0.73 32.83 ? 2010 SO4 A O4    1 
HETATM 18221 S  S     . SO4 M  7  .    ? 29.607  71.004  105.925 0.79 51.99 ? 2011 SO4 A S     1 
HETATM 18222 O  O1    . SO4 M  7  .    ? 30.747  70.610  105.034 0.79 61.43 ? 2011 SO4 A O1    1 
HETATM 18223 O  O2    . SO4 M  7  .    ? 28.328  70.849  105.165 0.79 52.78 ? 2011 SO4 A O2    1 
HETATM 18224 O  O3    . SO4 M  7  .    ? 29.591  70.111  107.126 0.79 53.32 ? 2011 SO4 A O3    1 
HETATM 18225 O  O4    . SO4 M  7  .    ? 29.768  72.430  106.362 0.79 52.42 ? 2011 SO4 A O4    1 
HETATM 18226 S  S     . SO4 N  7  .    ? 12.441  75.508  126.206 0.73 39.17 ? 2012 SO4 A S     1 
HETATM 18227 O  O1    . SO4 N  7  .    ? 13.584  74.551  126.316 0.73 40.91 ? 2012 SO4 A O1    1 
HETATM 18228 O  O2    . SO4 N  7  .    ? 11.217  74.797  125.722 0.73 36.26 ? 2012 SO4 A O2    1 
HETATM 18229 O  O3    . SO4 N  7  .    ? 12.150  76.099  127.555 0.73 52.08 ? 2012 SO4 A O3    1 
HETATM 18230 O  O4    . SO4 N  7  .    ? 12.795  76.626  125.274 0.73 49.54 ? 2012 SO4 A O4    1 
HETATM 18231 S  S     . SO4 O  7  .    ? -33.886 24.835  80.003  0.83 52.59 ? 2013 SO4 A S     1 
HETATM 18232 O  O1    . SO4 O  7  .    ? -33.215 25.977  79.301  0.83 50.14 ? 2013 SO4 A O1    1 
HETATM 18233 O  O2    . SO4 O  7  .    ? -34.865 24.189  79.073  0.83 41.82 ? 2013 SO4 A O2    1 
HETATM 18234 O  O3    . SO4 O  7  .    ? -32.830 23.851  80.406  0.83 67.25 ? 2013 SO4 A O3    1 
HETATM 18235 O  O4    . SO4 O  7  .    ? -34.602 25.302  81.235  0.83 43.26 ? 2013 SO4 A O4    1 
HETATM 18236 MG MG    . MG  P  8  .    ? -20.136 91.374  107.191 1.00 45.32 ? 2014 MG  A MG    1 
HETATM 18237 P  PA    A FAD Q  2  .    ? -16.961 23.081  104.292 0.63 27.10 ? 2001 FAD B PA    1 
HETATM 18238 P  PA    B FAD Q  2  .    ? -16.923 23.027  104.332 0.37 27.34 ? 2001 FAD B PA    1 
HETATM 18239 O  O1A   A FAD Q  2  .    ? -17.299 24.577  104.280 0.63 26.70 ? 2001 FAD B O1A   1 
HETATM 18240 O  O1A   B FAD Q  2  .    ? -17.287 24.523  104.231 0.37 26.67 ? 2001 FAD B O1A   1 
HETATM 18241 O  O2A   A FAD Q  2  .    ? -17.998 22.090  104.091 0.63 27.47 ? 2001 FAD B O2A   1 
HETATM 18242 O  O2A   B FAD Q  2  .    ? -17.937 22.020  104.121 0.37 27.53 ? 2001 FAD B O2A   1 
HETATM 18243 O  O5B   A FAD Q  2  .    ? -16.044 22.631  103.209 0.63 27.31 ? 2001 FAD B O5B   1 
HETATM 18244 O  O5B   B FAD Q  2  .    ? -15.930 22.518  103.358 0.37 27.87 ? 2001 FAD B O5B   1 
HETATM 18245 C  C5B   A FAD Q  2  .    ? -15.010 23.532  102.834 0.63 25.96 ? 2001 FAD B C5B   1 
HETATM 18246 C  C5B   B FAD Q  2  .    ? -14.985 23.448  102.854 0.37 26.02 ? 2001 FAD B C5B   1 
HETATM 18247 C  C4B   A FAD Q  2  .    ? -14.049 22.845  101.871 0.63 23.61 ? 2001 FAD B C4B   1 
HETATM 18248 C  C4B   B FAD Q  2  .    ? -14.040 22.758  101.880 0.37 23.58 ? 2001 FAD B C4B   1 
HETATM 18249 O  O4B   A FAD Q  2  .    ? -14.574 22.876  100.582 0.63 23.57 ? 2001 FAD B O4B   1 
HETATM 18250 O  O4B   B FAD Q  2  .    ? -14.557 22.762  100.586 0.37 23.64 ? 2001 FAD B O4B   1 
HETATM 18251 C  C3B   A FAD Q  2  .    ? -12.723 23.521  101.740 0.63 21.47 ? 2001 FAD B C3B   1 
HETATM 18252 C  C3B   B FAD Q  2  .    ? -12.718 23.441  101.771 0.37 21.60 ? 2001 FAD B C3B   1 
HETATM 18253 O  O3B   A FAD Q  2  .    ? -11.843 23.287  102.786 0.63 21.34 ? 2001 FAD B O3B   1 
HETATM 18254 O  O3B   B FAD Q  2  .    ? -11.838 23.124  102.789 0.37 21.66 ? 2001 FAD B O3B   1 
HETATM 18255 C  C2B   A FAD Q  2  .    ? -12.236 22.929  100.465 0.63 20.88 ? 2001 FAD B C2B   1 
HETATM 18256 C  C2B   B FAD Q  2  .    ? -12.223 22.928  100.472 0.37 20.94 ? 2001 FAD B C2B   1 
HETATM 18257 O  O2B   A FAD Q  2  .    ? -11.748 21.656  100.619 0.63 21.56 ? 2001 FAD B O2B   1 
HETATM 18258 O  O2B   B FAD Q  2  .    ? -11.631 21.698  100.602 0.37 21.72 ? 2001 FAD B O2B   1 
HETATM 18259 C  C1B   A FAD Q  2  .    ? -13.496 22.838  99.686  0.63 22.92 ? 2001 FAD B C1B   1 
HETATM 18260 C  C1B   B FAD Q  2  .    ? -13.477 22.781  99.692  0.37 22.91 ? 2001 FAD B C1B   1 
HETATM 18261 N  N9A   A FAD Q  2  .    ? -13.702 23.883  98.722  0.63 22.24 ? 2001 FAD B N9A   1 
HETATM 18262 N  N9A   B FAD Q  2  .    ? -13.697 23.831  98.732  0.37 22.26 ? 2001 FAD B N9A   1 
HETATM 18263 C  C8A   A FAD Q  2  .    ? -13.871 25.230  98.970  0.63 23.88 ? 2001 FAD B C8A   1 
HETATM 18264 C  C8A   B FAD Q  2  .    ? -13.875 25.174  98.998  0.37 23.87 ? 2001 FAD B C8A   1 
HETATM 18265 N  N7A   A FAD Q  2  .    ? -14.065 25.885  97.821  0.63 23.98 ? 2001 FAD B N7A   1 
HETATM 18266 N  N7A   B FAD Q  2  .    ? -14.067 25.841  97.856  0.37 23.99 ? 2001 FAD B N7A   1 
HETATM 18267 C  C5A   A FAD Q  2  .    ? -14.037 24.970  96.774  0.63 22.09 ? 2001 FAD B C5A   1 
HETATM 18268 C  C5A   B FAD Q  2  .    ? -14.027 24.946  96.794  0.37 22.11 ? 2001 FAD B C5A   1 
HETATM 18269 C  C6A   A FAD Q  2  .    ? -14.183 25.059  95.401  0.63 23.23 ? 2001 FAD B C6A   1 
HETATM 18270 C  C6A   B FAD Q  2  .    ? -14.164 25.060  95.420  0.37 23.22 ? 2001 FAD B C6A   1 
HETATM 18271 N  N6A   A FAD Q  2  .    ? -14.413 26.336  94.780  0.63 22.42 ? 2001 FAD B N6A   1 
HETATM 18272 N  N6A   B FAD Q  2  .    ? -14.403 26.349  94.823  0.37 22.44 ? 2001 FAD B N6A   1 
HETATM 18273 N  N1A   A FAD Q  2  .    ? -14.100 23.943  94.653  0.63 20.83 ? 2001 FAD B N1A   1 
HETATM 18274 N  N1A   B FAD Q  2  .    ? -14.069 23.962  94.647  0.37 20.91 ? 2001 FAD B N1A   1 
HETATM 18275 C  C2A   A FAD Q  2  .    ? -13.886 22.722  95.200  0.63 21.60 ? 2001 FAD B C2A   1 
HETATM 18276 C  C2A   B FAD Q  2  .    ? -13.847 22.734  95.176  0.37 21.60 ? 2001 FAD B C2A   1 
HETATM 18277 N  N3A   A FAD Q  2  .    ? -13.747 22.599  96.550  0.63 21.65 ? 2001 FAD B N3A   1 
HETATM 18278 N  N3A   B FAD Q  2  .    ? -13.712 22.587  96.523  0.37 21.71 ? 2001 FAD B N3A   1 
HETATM 18279 C  C4A   A FAD Q  2  .    ? -13.814 23.686  97.333  0.63 21.80 ? 2001 FAD B C4A   1 
HETATM 18280 C  C4A   B FAD Q  2  .    ? -13.794 23.655  97.334  0.37 21.83 ? 2001 FAD B C4A   1 
HETATM 18281 N  N1    A FAD Q  2  .    ? -7.441  18.529  105.014 0.63 18.10 ? 2001 FAD B N1    1 
HETATM 18282 N  N1    B FAD Q  2  .    ? -7.162  18.880  105.225 0.37 18.86 ? 2001 FAD B N1    1 
HETATM 18283 C  C2    A FAD Q  2  .    ? -6.254  18.062  104.373 0.63 19.05 ? 2001 FAD B C2    1 
HETATM 18284 C  C2    B FAD Q  2  .    ? -6.150  18.211  104.455 0.37 19.39 ? 2001 FAD B C2    1 
HETATM 18285 O  O2    A FAD Q  2  .    ? -5.990  18.486  103.115 0.63 20.73 ? 2001 FAD B O2    1 
HETATM 18286 O  O2    B FAD Q  2  .    ? -5.856  18.686  103.216 0.37 20.73 ? 2001 FAD B O2    1 
HETATM 18287 N  N3    A FAD Q  2  .    ? -5.390  17.204  105.015 0.63 18.42 ? 2001 FAD B N3    1 
HETATM 18288 N  N3    B FAD Q  2  .    ? -5.435  17.152  104.979 0.37 18.45 ? 2001 FAD B N3    1 
HETATM 18289 C  C4    A FAD Q  2  .    ? -5.630  16.768  106.301 0.63 18.58 ? 2001 FAD B C4    1 
HETATM 18290 C  C4    B FAD Q  2  .    ? -5.711  16.660  106.238 0.37 18.82 ? 2001 FAD B C4    1 
HETATM 18291 O  O4    A FAD Q  2  .    ? -4.758  15.910  106.896 0.63 21.69 ? 2001 FAD B O4    1 
HETATM 18292 O  O4    B FAD Q  2  .    ? -4.988  15.601  106.725 0.37 19.59 ? 2001 FAD B O4    1 
HETATM 18293 C  C4X   A FAD Q  2  .    ? -6.861  17.208  107.006 0.63 22.37 ? 2001 FAD B C4X   1 
HETATM 18294 C  C4X   B FAD Q  2  .    ? -6.861  17.227  107.005 0.37 22.32 ? 2001 FAD B C4X   1 
HETATM 18295 N  N5    A FAD Q  2  .    ? -7.174  16.782  108.297 0.63 21.17 ? 2001 FAD B N5    1 
HETATM 18296 N  N5    B FAD Q  2  .    ? -7.279  16.683  108.215 0.37 21.61 ? 2001 FAD B N5    1 
HETATM 18297 C  C5X   A FAD Q  2  .    ? -8.360  17.225  108.874 0.63 22.84 ? 2001 FAD B C5X   1 
HETATM 18298 C  C5X   B FAD Q  2  .    ? -8.372  17.233  108.877 0.37 22.82 ? 2001 FAD B C5X   1 
HETATM 18299 C  C6    A FAD Q  2  .    ? -8.686  16.793  110.169 0.63 21.88 ? 2001 FAD B C6    1 
HETATM 18300 C  C6    B FAD Q  2  .    ? -8.771  16.671  110.098 0.37 21.99 ? 2001 FAD B C6    1 
HETATM 18301 C  C7    A FAD Q  2  .    ? -9.869  17.244  110.744 0.63 22.11 ? 2001 FAD B C7    1 
HETATM 18302 C  C7    B FAD Q  2  .    ? -9.856  17.208  110.776 0.37 22.20 ? 2001 FAD B C7    1 
HETATM 18303 C  C7M   A FAD Q  2  .    ? -10.256 16.795  112.125 0.63 24.80 ? 2001 FAD B C7M   1 
HETATM 18304 C  C7M   B FAD Q  2  .    ? -10.284 16.590  112.083 0.37 24.42 ? 2001 FAD B C7M   1 
HETATM 18305 C  C8    A FAD Q  2  .    ? -10.721 18.093  110.070 0.63 23.79 ? 2001 FAD B C8    1 
HETATM 18306 C  C8    B FAD Q  2  .    ? -10.546 18.291  110.260 0.37 23.75 ? 2001 FAD B C8    1 
HETATM 18307 C  C8M   A FAD Q  2  .    ? -11.991 18.564  110.709 0.63 25.01 ? 2001 FAD B C8M   1 
HETATM 18308 C  C8M   B FAD Q  2  .    ? -11.717 18.878  110.986 0.37 24.64 ? 2001 FAD B C8M   1 
HETATM 18309 C  C9    A FAD Q  2  .    ? -10.405 18.526  108.783 0.63 23.95 ? 2001 FAD B C9    1 
HETATM 18310 C  C9    B FAD Q  2  .    ? -10.154 18.860  109.047 0.37 22.66 ? 2001 FAD B C9    1 
HETATM 18311 C  C9A   A FAD Q  2  .    ? -9.229  18.085  108.201 0.63 22.92 ? 2001 FAD B C9A   1 
HETATM 18312 C  C9A   B FAD Q  2  .    ? -9.070  18.327  108.362 0.37 22.13 ? 2001 FAD B C9A   1 
HETATM 18313 N  N10   A FAD Q  2  .    ? -8.910  18.541  106.889 0.63 24.36 ? 2001 FAD B N10   1 
HETATM 18314 N  N10   B FAD Q  2  .    ? -8.659  18.903  107.119 0.37 22.42 ? 2001 FAD B N10   1 
HETATM 18315 C  C10   A FAD Q  2  .    ? -7.739  18.094  106.286 0.63 21.96 ? 2001 FAD B C10   1 
HETATM 18316 C  C10   B FAD Q  2  .    ? -7.563  18.351  106.436 0.37 21.60 ? 2001 FAD B C10   1 
HETATM 18317 C  "C1'" A FAD Q  2  .    ? -9.850  19.414  106.145 0.63 23.09 ? 2001 FAD B "C1'" 1 
HETATM 18318 C  "C1'" B FAD Q  2  .    ? -9.389  20.058  106.548 0.37 24.01 ? 2001 FAD B "C1'" 1 
HETATM 18319 C  "C2'" A FAD Q  2  .    ? -9.505  20.884  106.022 0.63 25.89 ? 2001 FAD B "C2'" 1 
HETATM 18320 C  "C2'" B FAD Q  2  .    ? -10.570 19.537  105.732 0.37 22.95 ? 2001 FAD B "C2'" 1 
HETATM 18321 O  "O2'" A FAD Q  2  .    ? -8.592  21.271  106.977 0.63 22.02 ? 2001 FAD B "O2'" 1 
HETATM 18322 O  "O2'" B FAD Q  2  .    ? -10.087 18.893  104.621 0.37 26.07 ? 2001 FAD B "O2'" 1 
HETATM 18323 C  "C3'" A FAD Q  2  .    ? -10.799 21.694  106.161 0.63 25.39 ? 2001 FAD B "C3'" 1 
HETATM 18324 C  "C3'" B FAD Q  2  .    ? -11.587 20.600  105.277 0.37 26.65 ? 2001 FAD B "C3'" 1 
HETATM 18325 O  "O3'" A FAD Q  2  .    ? -11.134 21.764  107.495 0.63 23.38 ? 2001 FAD B "O3'" 1 
HETATM 18326 O  "O3'" B FAD Q  2  .    ? -11.114 21.231  104.145 0.37 28.73 ? 2001 FAD B "O3'" 1 
HETATM 18327 C  "C4'" A FAD Q  2  .    ? -11.982 21.095  105.420 0.63 27.96 ? 2001 FAD B "C4'" 1 
HETATM 18328 C  "C4'" B FAD Q  2  .    ? -11.984 21.645  106.308 0.37 29.14 ? 2001 FAD B "C4'" 1 
HETATM 18329 O  "O4'" A FAD Q  2  .    ? -11.716 21.018  104.068 0.63 27.67 ? 2001 FAD B "O4'" 1 
HETATM 18330 O  "O4'" B FAD Q  2  .    ? -12.085 21.065  107.550 0.37 28.39 ? 2001 FAD B "O4'" 1 
HETATM 18331 C  "C5'" A FAD Q  2  .    ? -13.269 21.868  105.678 0.63 25.51 ? 2001 FAD B "C5'" 1 
HETATM 18332 C  "C5'" B FAD Q  2  .    ? -13.303 22.321  105.944 0.37 26.52 ? 2001 FAD B "C5'" 1 
HETATM 18333 O  "O5'" A FAD Q  2  .    ? -14.333 21.050  105.241 0.63 26.39 ? 2001 FAD B "O5'" 1 
HETATM 18334 O  "O5'" B FAD Q  2  .    ? -14.188 21.380  105.368 0.37 27.07 ? 2001 FAD B "O5'" 1 
HETATM 18335 P  P     A FAD Q  2  .    ? -15.808 21.084  105.891 0.63 28.52 ? 2001 FAD B P     1 
HETATM 18336 P  P     B FAD Q  2  .    ? -15.675 21.141  105.931 0.37 28.43 ? 2001 FAD B P     1 
HETATM 18337 O  O1P   A FAD Q  2  .    ? -16.733 19.838  105.626 0.63 30.61 ? 2001 FAD B O1P   1 
HETATM 18338 O  O1P   B FAD Q  2  .    ? -16.369 19.763  105.606 0.37 27.20 ? 2001 FAD B O1P   1 
HETATM 18339 O  O2P   A FAD Q  2  .    ? -15.420 21.412  107.383 0.63 29.80 ? 2001 FAD B O2P   1 
HETATM 18340 O  O2P   B FAD Q  2  .    ? -15.415 21.505  107.442 0.37 29.85 ? 2001 FAD B O2P   1 
HETATM 18341 O  O3P   A FAD Q  2  .    ? -16.325 22.565  105.540 0.63 27.57 ? 2001 FAD B O3P   1 
HETATM 18342 O  O3P   B FAD Q  2  .    ? -16.424 22.533  105.634 0.37 27.57 ? 2001 FAD B O3P   1 
HETATM 18343 C  C1    . PGE R  9  .    ? 1.775   60.512  87.453  1.00 43.34 ? 2002 PGE B C1    1 
HETATM 18344 O  O1    . PGE R  9  .    ? 0.600   59.752  87.275  1.00 42.45 ? 2002 PGE B O1    1 
HETATM 18345 C  C2    . PGE R  9  .    ? 2.768   60.182  86.366  1.00 40.50 ? 2002 PGE B C2    1 
HETATM 18346 O  O2    . PGE R  9  .    ? 3.388   58.948  86.637  1.00 41.31 ? 2002 PGE B O2    1 
HETATM 18347 C  C3    . PGE R  9  .    ? 4.214   58.450  85.613  1.00 32.78 ? 2002 PGE B C3    1 
HETATM 18348 C  C4    . PGE R  9  .    ? 4.670   57.025  85.840  1.00 32.21 ? 2002 PGE B C4    1 
HETATM 18349 O  O4    . PGE R  9  .    ? 2.017   54.503  87.859  1.00 44.06 ? 2002 PGE B O4    1 
HETATM 18350 C  C6    . PGE R  9  .    ? 2.606   54.117  86.636  1.00 38.63 ? 2002 PGE B C6    1 
HETATM 18351 C  C5    . PGE R  9  .    ? 3.899   54.893  86.449  1.00 35.35 ? 2002 PGE B C5    1 
HETATM 18352 O  O3    . PGE R  9  .    ? 3.593   56.260  86.320  1.00 37.33 ? 2002 PGE B O3    1 
HETATM 18353 C  C1    . PEG S  3  .    ? -5.509  31.720  68.057  1.00 43.47 ? 2003 PEG B C1    1 
HETATM 18354 O  O1    . PEG S  3  .    ? -6.285  32.809  67.605  1.00 50.17 ? 2003 PEG B O1    1 
HETATM 18355 C  C2    . PEG S  3  .    ? -5.428  31.755  69.560  1.00 36.94 ? 2003 PEG B C2    1 
HETATM 18356 O  O2    . PEG S  3  .    ? -6.709  31.580  70.119  1.00 44.95 ? 2003 PEG B O2    1 
HETATM 18357 C  C3    . PEG S  3  .    ? -6.720  30.651  71.171  1.00 39.15 ? 2003 PEG B C3    1 
HETATM 18358 C  C4    . PEG S  3  .    ? -7.630  31.133  72.272  1.00 33.10 ? 2003 PEG B C4    1 
HETATM 18359 O  O4    . PEG S  3  .    ? -8.906  30.552  72.109  1.00 46.78 ? 2003 PEG B O4    1 
HETATM 18360 C  C01   . 53E T  4  .    ? 13.058  30.473  79.802  0.86 26.80 ? 2004 53E B C01   1 
HETATM 18361 C  C02   . 53E T  4  .    ? 12.559  30.667  81.219  0.86 34.10 ? 2004 53E B C02   1 
HETATM 18362 O  O03   . 53E T  4  .    ? 13.349  31.552  81.954  0.86 26.66 ? 2004 53E B O03   1 
HETATM 18363 C  C04   . 53E T  4  .    ? 13.529  32.772  81.246  0.86 25.23 ? 2004 53E B C04   1 
HETATM 18364 C  C05   . 53E T  4  .    ? 13.838  33.939  81.964  0.86 24.28 ? 2004 53E B C05   1 
HETATM 18365 C  C06   . 53E T  4  .    ? 14.005  35.143  81.294  0.86 23.97 ? 2004 53E B C06   1 
HETATM 18366 C  C07   . 53E T  4  .    ? 13.874  35.203  79.908  0.86 28.60 ? 2004 53E B C07   1 
HETATM 18367 C  C08   . 53E T  4  .    ? 13.565  34.049  79.193  0.86 26.73 ? 2004 53E B C08   1 
HETATM 18368 C  C09   . 53E T  4  .    ? 13.398  32.827  79.865  0.86 24.18 ? 2004 53E B C09   1 
HETATM 18369 O  O10   . 53E T  4  .    ? 13.085  31.666  79.080  0.86 28.34 ? 2004 53E B O10   1 
HETATM 18370 C  C11   . 53E T  4  .    ? 13.992  33.944  83.478  0.86 21.00 ? 2004 53E B C11   1 
HETATM 18371 O  O12   . 53E T  4  .    ? 13.450  34.886  84.106  0.86 21.23 ? 2004 53E B O12   1 
HETATM 18372 O  O13   . 53E T  4  .    ? 14.657  33.054  84.073  0.86 20.07 ? 2004 53E B O13   1 
HETATM 18373 C  C1    . PEG U  3  .    ? 7.044   28.522  81.435  1.00 37.81 ? 2005 PEG B C1    1 
HETATM 18374 O  O1    . PEG U  3  .    ? 8.344   28.856  81.047  1.00 28.60 ? 2005 PEG B O1    1 
HETATM 18375 C  C2    . PEG U  3  .    ? 7.037   28.269  82.916  1.00 37.00 ? 2005 PEG B C2    1 
HETATM 18376 O  O2    . PEG U  3  .    ? 6.370   27.056  83.122  1.00 45.90 ? 2005 PEG B O2    1 
HETATM 18377 C  C3    . PEG U  3  .    ? 7.041   26.203  84.005  1.00 41.55 ? 2005 PEG B C3    1 
HETATM 18378 C  C4    . PEG U  3  .    ? 6.337   24.875  84.029  1.00 32.86 ? 2005 PEG B C4    1 
HETATM 18379 O  O4    . PEG U  3  .    ? 7.026   23.961  83.227  1.00 35.25 ? 2005 PEG B O4    1 
HETATM 18380 C  C     . FMT V  5  .    ? -0.805  16.903  83.266  1.00 15.57 ? 2006 FMT B C     1 
HETATM 18381 O  O1    . FMT V  5  .    ? -0.977  15.673  83.432  1.00 38.98 ? 2006 FMT B O1    1 
HETATM 18382 O  O2    . FMT V  5  .    ? -1.239  17.614  82.359  1.00 34.19 ? 2006 FMT B O2    1 
HETATM 18383 C  C1    . PEG W  3  .    ? 15.738  66.640  54.302  1.00 54.42 ? 2007 PEG B C1    1 
HETATM 18384 O  O1    . PEG W  3  .    ? 15.802  67.060  55.653  1.00 37.43 ? 2007 PEG B O1    1 
HETATM 18385 C  C2    . PEG W  3  .    ? 14.412  66.002  53.968  1.00 43.45 ? 2007 PEG B C2    1 
HETATM 18386 O  O2    . PEG W  3  .    ? 14.497  64.597  54.025  1.00 48.47 ? 2007 PEG B O2    1 
HETATM 18387 C  C3    . PEG W  3  .    ? 15.527  64.080  53.216  1.00 52.74 ? 2007 PEG B C3    1 
HETATM 18388 C  C4    . PEG W  3  .    ? 15.606  62.578  53.326  1.00 46.25 ? 2007 PEG B C4    1 
HETATM 18389 O  O4    . PEG W  3  .    ? 15.662  62.199  54.681  1.00 52.31 ? 2007 PEG B O4    1 
HETATM 18390 C  C     . FMT X  5  .    ? 18.228  45.320  112.584 1.00 32.23 ? 2008 FMT B C     1 
HETATM 18391 O  O1    . FMT X  5  .    ? 17.751  44.286  112.072 1.00 33.47 ? 2008 FMT B O1    1 
HETATM 18392 O  O2    . FMT X  5  .    ? 18.424  46.429  112.049 1.00 36.54 ? 2008 FMT B O2    1 
HETATM 18393 O  O1    . PG4 Y  10 .    ? 42.365  38.049  86.126  1.00 35.96 ? 2009 PG4 B O1    1 
HETATM 18394 C  C1    . PG4 Y  10 .    ? 42.536  39.339  86.673  1.00 35.12 ? 2009 PG4 B C1    1 
HETATM 18395 C  C2    . PG4 Y  10 .    ? 41.445  40.252  86.179  1.00 36.00 ? 2009 PG4 B C2    1 
HETATM 18396 O  O2    . PG4 Y  10 .    ? 40.328  39.498  85.778  1.00 41.16 ? 2009 PG4 B O2    1 
HETATM 18397 C  C3    . PG4 Y  10 .    ? 39.126  40.034  86.272  1.00 42.28 ? 2009 PG4 B C3    1 
HETATM 18398 C  C4    . PG4 Y  10 .    ? 38.019  39.885  85.260  1.00 42.61 ? 2009 PG4 B C4    1 
HETATM 18399 O  O3    . PG4 Y  10 .    ? 37.608  38.541  85.184  1.00 47.39 ? 2009 PG4 B O3    1 
HETATM 18400 C  C5    . PG4 Y  10 .    ? 36.734  38.315  84.106  1.00 45.79 ? 2009 PG4 B C5    1 
HETATM 18401 C  C6    . PG4 Y  10 .    ? 36.848  36.884  83.652  1.00 48.21 ? 2009 PG4 B C6    1 
HETATM 18402 O  O4    . PG4 Y  10 .    ? 38.120  36.638  83.108  1.00 48.08 ? 2009 PG4 B O4    1 
HETATM 18403 C  C7    . PG4 Y  10 .    ? 38.160  35.427  82.396  1.00 43.41 ? 2009 PG4 B C7    1 
HETATM 18404 C  C8    . PG4 Y  10 .    ? 39.561  35.139  81.916  1.00 41.77 ? 2009 PG4 B C8    1 
HETATM 18405 O  O5    . PG4 Y  10 .    ? 40.273  34.446  82.915  1.00 45.68 ? 2009 PG4 B O5    1 
HETATM 18406 P  PA    . NAD Z  6  .    ? 27.625  35.761  75.281  0.75 23.71 ? 2010 NAD B PA    1 
HETATM 18407 O  O1A   . NAD Z  6  .    ? 27.761  37.295  75.183  0.75 21.49 ? 2010 NAD B O1A   1 
HETATM 18408 O  O2A   . NAD Z  6  .    ? 28.797  34.988  75.674  0.75 25.06 ? 2010 NAD B O2A   1 
HETATM 18409 O  O5B   . NAD Z  6  .    ? 27.256  35.088  74.000  0.75 24.63 ? 2010 NAD B O5B   1 
HETATM 18410 C  C5B   . NAD Z  6  .    ? 25.983  35.365  73.446  0.75 21.75 ? 2010 NAD B C5B   1 
HETATM 18411 C  C4B   . NAD Z  6  .    ? 26.000  35.259  71.920  0.75 22.24 ? 2010 NAD B C4B   1 
HETATM 18412 O  O4B   . NAD Z  6  .    ? 26.780  36.269  71.302  0.75 20.38 ? 2010 NAD B O4B   1 
HETATM 18413 C  C3B   . NAD Z  6  .    ? 26.478  33.938  71.407  0.75 20.75 ? 2010 NAD B C3B   1 
HETATM 18414 O  O3B   . NAD Z  6  .    ? 25.680  33.513  70.365  0.75 19.60 ? 2010 NAD B O3B   1 
HETATM 18415 C  C2B   . NAD Z  6  .    ? 27.852  34.251  70.951  0.75 23.13 ? 2010 NAD B C2B   1 
HETATM 18416 O  O2B   . NAD Z  6  .    ? 28.363  33.393  69.993  0.75 23.32 ? 2010 NAD B O2B   1 
HETATM 18417 C  C1B   . NAD Z  6  .    ? 27.668  35.620  70.422  0.75 22.73 ? 2010 NAD B C1B   1 
HETATM 18418 N  N9A   . NAD Z  6  .    ? 28.894  36.387  70.274  0.75 22.55 ? 2010 NAD B N9A   1 
HETATM 18419 C  C8A   . NAD Z  6  .    ? 30.063  36.293  71.011  0.75 23.87 ? 2010 NAD B C8A   1 
HETATM 18420 N  N7A   . NAD Z  6  .    ? 30.943  37.207  70.577  0.75 23.63 ? 2010 NAD B N7A   1 
HETATM 18421 C  C5A   . NAD Z  6  .    ? 30.377  37.929  69.522  0.75 20.73 ? 2010 NAD B C5A   1 
HETATM 18422 C  C6A   . NAD Z  6  .    ? 30.792  38.962  68.704  0.75 19.97 ? 2010 NAD B C6A   1 
HETATM 18423 N  N6A   . NAD Z  6  .    ? 32.109  39.515  68.868  0.75 27.28 ? 2010 NAD B N6A   1 
HETATM 18424 N  N1A   . NAD Z  6  .    ? 29.979  39.464  67.766  0.75 21.40 ? 2010 NAD B N1A   1 
HETATM 18425 C  C2A   . NAD Z  6  .    ? 28.727  38.969  67.574  0.75 20.57 ? 2010 NAD B C2A   1 
HETATM 18426 N  N3A   . NAD Z  6  .    ? 28.282  37.952  68.357  0.75 19.57 ? 2010 NAD B N3A   1 
HETATM 18427 C  C4A   . NAD Z  6  .    ? 29.064  37.421  69.320  0.75 20.28 ? 2010 NAD B C4A   1 
HETATM 18428 O  O3    . NAD Z  6  .    ? 26.602  35.236  76.224  0.75 19.94 ? 2010 NAD B O3    1 
HETATM 18429 P  PN    . NAD Z  6  .    ? 26.208  33.791  76.753  0.75 23.62 ? 2010 NAD B PN    1 
HETATM 18430 O  O1N   . NAD Z  6  .    ? 27.313  33.219  77.598  0.75 25.87 ? 2010 NAD B O1N   1 
HETATM 18431 O  O2N   . NAD Z  6  .    ? 25.849  32.906  75.583  0.75 20.06 ? 2010 NAD B O2N   1 
HETATM 18432 O  O5D   . NAD Z  6  .    ? 24.951  34.069  77.677  0.75 23.22 ? 2010 NAD B O5D   1 
HETATM 18433 C  C5D   . NAD Z  6  .    ? 25.113  34.527  78.988  0.75 24.44 ? 2010 NAD B C5D   1 
HETATM 18434 C  C4D   . NAD Z  6  .    ? 24.828  36.014  79.056  0.75 20.91 ? 2010 NAD B C4D   1 
HETATM 18435 O  O4D   . NAD Z  6  .    ? 23.561  36.248  78.512  0.75 23.99 ? 2010 NAD B O4D   1 
HETATM 18436 C  C3D   . NAD Z  6  .    ? 24.824  36.526  80.458  0.75 24.56 ? 2010 NAD B C3D   1 
HETATM 18437 O  O3D   . NAD Z  6  .    ? 25.501  37.719  80.554  0.75 25.19 ? 2010 NAD B O3D   1 
HETATM 18438 C  C2D   . NAD Z  6  .    ? 23.380  36.706  80.709  0.75 25.61 ? 2010 NAD B C2D   1 
HETATM 18439 O  O2D   . NAD Z  6  .    ? 23.050  37.587  81.728  0.75 22.24 ? 2010 NAD B O2D   1 
HETATM 18440 C  C1D   . NAD Z  6  .    ? 22.921  37.144  79.367  0.75 22.48 ? 2010 NAD B C1D   1 
HETATM 18441 N  N1N   . NAD Z  6  .    ? 21.508  36.963  79.210  0.75 21.79 ? 2010 NAD B N1N   1 
HETATM 18442 C  C2N   . NAD Z  6  .    ? 20.612  38.060  79.193  0.75 20.62 ? 2010 NAD B C2N   1 
HETATM 18443 C  C3N   . NAD Z  6  .    ? 19.253  37.794  79.031  0.75 25.48 ? 2010 NAD B C3N   1 
HETATM 18444 C  C7N   . NAD Z  6  .    ? 18.241  38.894  79.005  0.75 19.84 ? 2010 NAD B C7N   1 
HETATM 18445 O  O7N   . NAD Z  6  .    ? 17.111  38.657  78.605  0.75 21.89 ? 2010 NAD B O7N   1 
HETATM 18446 N  N7N   . NAD Z  6  .    ? 18.581  40.208  79.458  0.75 22.78 ? 2010 NAD B N7N   1 
HETATM 18447 C  C4N   . NAD Z  6  .    ? 18.811  36.461  78.868  0.75 34.78 ? 2010 NAD B C4N   1 
HETATM 18448 C  C5N   . NAD Z  6  .    ? 19.711  35.370  78.898  0.75 25.53 ? 2010 NAD B C5N   1 
HETATM 18449 C  C6N   . NAD Z  6  .    ? 21.065  35.635  79.054  0.75 19.63 ? 2010 NAD B C6N   1 
HETATM 18450 S  S     . SO4 AA 7  .    ? -7.053  47.596  73.334  1.00 18.71 ? 2011 SO4 B S     1 
HETATM 18451 O  O1    . SO4 AA 7  .    ? -5.825  46.854  72.927  1.00 22.68 ? 2011 SO4 B O1    1 
HETATM 18452 O  O2    . SO4 AA 7  .    ? -7.767  48.116  72.132  1.00 18.08 ? 2011 SO4 B O2    1 
HETATM 18453 O  O3    . SO4 AA 7  .    ? -7.953  46.680  74.078  1.00 22.24 ? 2011 SO4 B O3    1 
HETATM 18454 O  O4    . SO4 AA 7  .    ? -6.628  48.726  74.195  1.00 22.06 ? 2011 SO4 B O4    1 
HETATM 18455 S  S     . SO4 BA 7  .    ? 3.789   15.309  65.230  0.61 39.46 ? 2012 SO4 B S     1 
HETATM 18456 O  O1    . SO4 BA 7  .    ? 4.106   13.926  64.744  0.61 29.68 ? 2012 SO4 B O1    1 
HETATM 18457 O  O2    . SO4 BA 7  .    ? 3.793   16.234  64.050  0.61 37.61 ? 2012 SO4 B O2    1 
HETATM 18458 O  O3    . SO4 BA 7  .    ? 2.435   15.304  65.876  0.61 49.73 ? 2012 SO4 B O3    1 
HETATM 18459 O  O4    . SO4 BA 7  .    ? 4.797   15.738  66.254  0.61 29.23 ? 2012 SO4 B O4    1 
HETATM 18460 MG MG    . MG  CA 8  .    ? 30.263  33.543  75.401  1.00 38.74 ? 2013 MG  B MG    1 
HETATM 18461 O  O     . HOH DA 11 .    ? 14.540  76.030  124.163 1.00 33.74 ? 2101 HOH A O     1 
HETATM 18462 O  O     . HOH DA 11 .    ? -39.363 37.480  64.576  1.00 42.60 ? 2102 HOH A O     1 
HETATM 18463 O  O     . HOH DA 11 .    ? -1.201  88.819  105.781 1.00 31.61 ? 2103 HOH A O     1 
HETATM 18464 O  O     . HOH DA 11 .    ? -51.132 73.678  68.445  1.00 37.28 ? 2104 HOH A O     1 
HETATM 18465 O  O     . HOH DA 11 .    ? -30.100 95.127  91.895  1.00 40.86 ? 2105 HOH A O     1 
HETATM 18466 O  O     . HOH DA 11 .    ? -9.671  58.077  96.599  1.00 41.00 ? 2106 HOH A O     1 
HETATM 18467 O  O     . HOH DA 11 .    ? -32.063 56.136  86.240  1.00 30.36 ? 2107 HOH A O     1 
HETATM 18468 O  O     . HOH DA 11 .    ? -21.976 95.486  121.367 1.00 45.92 ? 2108 HOH A O     1 
HETATM 18469 O  O     . HOH DA 11 .    ? -57.357 67.319  61.910  1.00 31.07 ? 2109 HOH A O     1 
HETATM 18470 O  O     . HOH DA 11 .    ? -0.266  79.801  81.987  1.00 43.05 ? 2110 HOH A O     1 
HETATM 18471 O  O     . HOH DA 11 .    ? -21.097 90.404  105.507 1.00 40.16 ? 2111 HOH A O     1 
HETATM 18472 O  O     . HOH DA 11 .    ? 11.623  74.669  129.302 1.00 41.75 ? 2112 HOH A O     1 
HETATM 18473 O  O     . HOH DA 11 .    ? -41.759 80.386  70.028  1.00 41.47 ? 2113 HOH A O     1 
HETATM 18474 O  O     . HOH DA 11 .    ? -25.058 60.620  128.049 1.00 40.77 ? 2114 HOH A O     1 
HETATM 18475 O  O     . HOH DA 11 .    ? -43.896 62.069  70.561  1.00 33.20 ? 2115 HOH A O     1 
HETATM 18476 O  O     . HOH DA 11 .    ? -52.358 61.258  102.139 1.00 30.08 ? 2116 HOH A O     1 
HETATM 18477 O  O     . HOH DA 11 .    ? -32.041 79.945  99.740  1.00 30.46 ? 2117 HOH A O     1 
HETATM 18478 O  O     . HOH DA 11 .    ? -38.756 67.114  69.547  1.00 42.58 ? 2118 HOH A O     1 
HETATM 18479 O  O     . HOH DA 11 .    ? 4.961   80.637  129.513 1.00 42.61 ? 2119 HOH A O     1 
HETATM 18480 O  O     . HOH DA 11 .    ? -56.929 49.389  58.082  1.00 44.22 ? 2120 HOH A O     1 
HETATM 18481 O  O     . HOH DA 11 .    ? -16.365 75.720  106.237 1.00 28.38 ? 2121 HOH A O     1 
HETATM 18482 O  O     . HOH DA 11 .    ? -20.596 55.073  115.935 1.00 40.49 ? 2122 HOH A O     1 
HETATM 18483 O  O     . HOH DA 11 .    ? -0.458  63.707  110.100 1.00 22.93 ? 2123 HOH A O     1 
HETATM 18484 O  O     . HOH DA 11 .    ? -12.707 87.556  99.317  1.00 44.67 ? 2124 HOH A O     1 
HETATM 18485 O  O     . HOH DA 11 .    ? 14.786  55.196  111.081 1.00 38.37 ? 2125 HOH A O     1 
HETATM 18486 O  O     . HOH DA 11 .    ? -36.260 64.660  63.003  1.00 38.96 ? 2126 HOH A O     1 
HETATM 18487 O  O     . HOH DA 11 .    ? -24.952 59.164  73.824  1.00 34.18 ? 2127 HOH A O     1 
HETATM 18488 O  O     . HOH DA 11 .    ? 20.984  57.269  105.560 1.00 41.06 ? 2128 HOH A O     1 
HETATM 18489 O  O     . HOH DA 11 .    ? -31.253 58.565  115.822 1.00 43.84 ? 2129 HOH A O     1 
HETATM 18490 O  O     . HOH DA 11 .    ? -28.869 93.997  82.433  1.00 42.35 ? 2130 HOH A O     1 
HETATM 18491 O  O     . HOH DA 11 .    ? -13.090 55.548  81.793  1.00 35.22 ? 2131 HOH A O     1 
HETATM 18492 O  O     . HOH DA 11 .    ? -33.320 61.299  114.790 1.00 43.31 ? 2132 HOH A O     1 
HETATM 18493 O  O     . HOH DA 11 .    ? -37.756 48.905  76.935  1.00 37.98 ? 2133 HOH A O     1 
HETATM 18494 O  O     . HOH DA 11 .    ? 26.118  71.912  105.287 1.00 41.95 ? 2134 HOH A O     1 
HETATM 18495 O  O     . HOH DA 11 .    ? -54.926 33.616  71.596  1.00 36.94 ? 2135 HOH A O     1 
HETATM 18496 O  O     . HOH DA 11 .    ? -45.862 25.984  86.622  1.00 42.05 ? 2136 HOH A O     1 
HETATM 18497 O  O     . HOH DA 11 .    ? 8.251   89.592  120.609 1.00 29.34 ? 2137 HOH A O     1 
HETATM 18498 O  O     . HOH DA 11 .    ? -13.894 74.648  106.177 1.00 26.25 ? 2138 HOH A O     1 
HETATM 18499 O  O     . HOH DA 11 .    ? -34.174 55.350  71.500  1.00 40.24 ? 2139 HOH A O     1 
HETATM 18500 O  O     . HOH DA 11 .    ? -66.783 72.439  75.464  1.00 32.31 ? 2140 HOH A O     1 
HETATM 18501 O  O     . HOH DA 11 .    ? -34.498 67.267  125.663 1.00 39.10 ? 2141 HOH A O     1 
HETATM 18502 O  O     . HOH DA 11 .    ? -43.000 33.334  102.656 1.00 44.43 ? 2142 HOH A O     1 
HETATM 18503 O  O     . HOH DA 11 .    ? -3.905  79.258  104.106 1.00 26.07 ? 2143 HOH A O     1 
HETATM 18504 O  O     . HOH DA 11 .    ? -43.162 80.458  90.033  1.00 29.91 ? 2144 HOH A O     1 
HETATM 18505 O  O     . HOH DA 11 .    ? 21.697  68.002  116.815 1.00 35.82 ? 2145 HOH A O     1 
HETATM 18506 O  O     . HOH DA 11 .    ? -16.610 55.736  112.588 1.00 32.05 ? 2146 HOH A O     1 
HETATM 18507 O  O     . HOH DA 11 .    ? -11.791 68.667  76.795  1.00 28.43 ? 2147 HOH A O     1 
HETATM 18508 O  O     . HOH DA 11 .    ? -68.489 56.577  82.950  1.00 30.29 ? 2148 HOH A O     1 
HETATM 18509 O  O     . HOH DA 11 .    ? -7.104  50.471  76.855  1.00 29.32 ? 2149 HOH A O     1 
HETATM 18510 O  O     . HOH DA 11 .    ? -18.097 74.481  131.926 1.00 38.66 ? 2150 HOH A O     1 
HETATM 18511 O  O     . HOH DA 11 .    ? -49.190 49.732  105.007 1.00 46.06 ? 2151 HOH A O     1 
HETATM 18512 O  O     . HOH DA 11 .    ? -41.063 63.086  73.921  1.00 31.65 ? 2152 HOH A O     1 
HETATM 18513 O  O     . HOH DA 11 .    ? -38.420 38.101  88.016  1.00 37.79 ? 2153 HOH A O     1 
HETATM 18514 O  O     . HOH DA 11 .    ? -10.528 49.657  110.281 1.00 24.11 ? 2154 HOH A O     1 
HETATM 18515 O  O     . HOH DA 11 .    ? -10.570 69.202  133.787 1.00 35.41 ? 2155 HOH A O     1 
HETATM 18516 O  O     . HOH DA 11 .    ? 25.662  79.803  107.932 1.00 34.88 ? 2156 HOH A O     1 
HETATM 18517 O  O     . HOH DA 11 .    ? -22.431 96.963  79.033  1.00 33.28 ? 2157 HOH A O     1 
HETATM 18518 O  O     . HOH DA 11 .    ? -61.733 57.431  63.919  1.00 34.37 ? 2158 HOH A O     1 
HETATM 18519 O  O     . HOH DA 11 .    ? -57.646 27.997  86.174  1.00 41.11 ? 2159 HOH A O     1 
HETATM 18520 O  O     . HOH DA 11 .    ? -63.398 76.072  76.064  1.00 42.94 ? 2160 HOH A O     1 
HETATM 18521 O  O     . HOH DA 11 .    ? -58.514 37.377  65.231  1.00 48.28 ? 2161 HOH A O     1 
HETATM 18522 O  O     . HOH DA 11 .    ? -34.148 76.859  96.639  1.00 32.54 ? 2162 HOH A O     1 
HETATM 18523 O  O     . HOH DA 11 .    ? -25.543 95.969  124.326 1.00 35.30 ? 2163 HOH A O     1 
HETATM 18524 O  O     . HOH DA 11 .    ? -24.678 65.282  94.724  1.00 28.07 ? 2164 HOH A O     1 
HETATM 18525 O  O     . HOH DA 11 .    ? -14.774 64.031  99.531  1.00 26.25 ? 2165 HOH A O     1 
HETATM 18526 O  O     . HOH DA 11 .    ? -0.136  82.324  113.753 1.00 38.44 ? 2166 HOH A O     1 
HETATM 18527 O  O     . HOH DA 11 .    ? -11.500 63.213  113.474 1.00 20.20 ? 2167 HOH A O     1 
HETATM 18528 O  O     . HOH DA 11 .    ? -42.788 48.360  60.248  1.00 34.11 ? 2168 HOH A O     1 
HETATM 18529 O  O     . HOH DA 11 .    ? -49.181 66.681  94.283  1.00 22.20 ? 2169 HOH A O     1 
HETATM 18530 O  O     . HOH DA 11 .    ? -38.570 65.165  96.737  1.00 36.47 ? 2170 HOH A O     1 
HETATM 18531 O  O     . HOH DA 11 .    ? 7.770   91.243  113.959 1.00 34.01 ? 2171 HOH A O     1 
HETATM 18532 O  O     . HOH DA 11 .    ? -30.568 81.502  129.458 1.00 42.48 ? 2172 HOH A O     1 
HETATM 18533 O  O     . HOH DA 11 .    ? -42.291 38.709  85.244  1.00 29.57 ? 2173 HOH A O     1 
HETATM 18534 O  O     . HOH DA 11 .    ? -25.771 62.071  76.173  1.00 35.55 ? 2174 HOH A O     1 
HETATM 18535 O  O     . HOH DA 11 .    ? -19.400 72.802  97.845  1.00 19.46 ? 2175 HOH A O     1 
HETATM 18536 O  O     . HOH DA 11 .    ? -51.756 47.361  69.133  1.00 34.85 ? 2176 HOH A O     1 
HETATM 18537 O  O     . HOH DA 11 .    ? 17.722  78.092  120.556 1.00 39.59 ? 2177 HOH A O     1 
HETATM 18538 O  O     . HOH DA 11 .    ? -27.300 73.525  129.839 1.00 34.29 ? 2178 HOH A O     1 
HETATM 18539 O  O     . HOH DA 11 .    ? -6.497  58.454  120.235 1.00 23.30 ? 2179 HOH A O     1 
HETATM 18540 O  O     . HOH DA 11 .    ? -7.060  84.931  86.866  1.00 38.23 ? 2180 HOH A O     1 
HETATM 18541 O  O     . HOH DA 11 .    ? -10.242 81.165  91.421  1.00 24.33 ? 2181 HOH A O     1 
HETATM 18542 O  O     . HOH DA 11 .    ? -44.769 63.571  84.542  1.00 20.70 ? 2182 HOH A O     1 
HETATM 18543 O  O     . HOH DA 11 .    ? -38.897 77.702  97.558  1.00 25.71 ? 2183 HOH A O     1 
HETATM 18544 O  O     . HOH DA 11 .    ? -35.254 76.363  92.653  1.00 33.18 ? 2184 HOH A O     1 
HETATM 18545 O  O     . HOH DA 11 .    ? -45.374 89.176  106.441 1.00 36.97 ? 2185 HOH A O     1 
HETATM 18546 O  O     . HOH DA 11 .    ? -6.704  66.197  73.993  1.00 49.06 ? 2186 HOH A O     1 
HETATM 18547 O  O     . HOH DA 11 .    ? -19.848 87.761  136.233 1.00 48.43 ? 2187 HOH A O     1 
HETATM 18548 O  O     . HOH DA 11 .    ? -50.480 50.537  57.529  1.00 36.91 ? 2188 HOH A O     1 
HETATM 18549 O  O     . HOH DA 11 .    ? -44.773 85.827  100.065 1.00 40.59 ? 2189 HOH A O     1 
HETATM 18550 O  O     . HOH DA 11 .    ? -37.000 80.643  79.245  1.00 22.56 ? 2190 HOH A O     1 
HETATM 18551 O  O     . HOH DA 11 .    ? -15.018 55.442  121.898 1.00 34.36 ? 2191 HOH A O     1 
HETATM 18552 O  O     . HOH DA 11 .    ? -44.948 79.919  79.691  1.00 41.57 ? 2192 HOH A O     1 
HETATM 18553 O  O     . HOH DA 11 .    ? -1.157  77.994  114.838 1.00 27.80 ? 2193 HOH A O     1 
HETATM 18554 O  O     . HOH DA 11 .    ? -17.856 82.691  96.904  1.00 24.36 ? 2194 HOH A O     1 
HETATM 18555 O  O     . HOH DA 11 .    ? -19.754 59.637  79.364  1.00 34.16 ? 2195 HOH A O     1 
HETATM 18556 O  O     . HOH DA 11 .    ? -5.595  53.558  110.983 1.00 19.56 ? 2196 HOH A O     1 
HETATM 18557 O  O     . HOH DA 11 .    ? -48.231 82.764  111.688 1.00 33.18 ? 2197 HOH A O     1 
HETATM 18558 O  O     . HOH DA 11 .    ? -45.724 76.144  94.534  1.00 28.95 ? 2198 HOH A O     1 
HETATM 18559 O  O     . HOH DA 11 .    ? -46.742 35.002  87.265  1.00 32.79 ? 2199 HOH A O     1 
HETATM 18560 O  O     . HOH DA 11 .    ? -24.112 67.529  105.419 1.00 31.62 ? 2200 HOH A O     1 
HETATM 18561 O  O     . HOH DA 11 .    ? -3.527  70.518  117.762 1.00 26.95 ? 2201 HOH A O     1 
HETATM 18562 O  O     . HOH DA 11 .    ? -29.082 57.603  115.857 1.00 33.97 ? 2202 HOH A O     1 
HETATM 18563 O  O     . HOH DA 11 .    ? -23.223 63.862  98.101  1.00 19.85 ? 2203 HOH A O     1 
HETATM 18564 O  O     . HOH DA 11 .    ? -18.898 54.292  94.951  1.00 39.99 ? 2204 HOH A O     1 
HETATM 18565 O  O     . HOH DA 11 .    ? -32.058 86.942  76.712  1.00 35.24 ? 2205 HOH A O     1 
HETATM 18566 O  O     . HOH DA 11 .    ? -29.080 37.776  85.600  1.00 48.13 ? 2206 HOH A O     1 
HETATM 18567 O  O     . HOH DA 11 .    ? -60.348 59.575  90.654  1.00 22.90 ? 2207 HOH A O     1 
HETATM 18568 O  O     . HOH DA 11 .    ? -3.007  85.740  125.125 1.00 36.13 ? 2208 HOH A O     1 
HETATM 18569 O  O     . HOH DA 11 .    ? -60.127 51.039  62.377  1.00 37.23 ? 2209 HOH A O     1 
HETATM 18570 O  O     . HOH DA 11 .    ? -31.130 46.729  88.456  1.00 37.84 ? 2210 HOH A O     1 
HETATM 18571 O  O     . HOH DA 11 .    ? -22.992 60.440  116.077 1.00 22.58 ? 2211 HOH A O     1 
HETATM 18572 O  O     . HOH DA 11 .    ? -13.563 77.920  111.394 1.00 23.13 ? 2212 HOH A O     1 
HETATM 18573 O  O     . HOH DA 11 .    ? -37.263 63.944  67.407  1.00 29.51 ? 2213 HOH A O     1 
HETATM 18574 O  O     . HOH DA 11 .    ? -39.756 57.217  88.236  1.00 18.26 ? 2214 HOH A O     1 
HETATM 18575 O  O     . HOH DA 11 .    ? -32.246 75.766  94.761  1.00 42.41 ? 2215 HOH A O     1 
HETATM 18576 O  O     . HOH DA 11 .    ? -35.798 55.826  78.804  1.00 40.44 ? 2216 HOH A O     1 
HETATM 18577 O  O     . HOH DA 11 .    ? -8.471  80.629  74.946  1.00 31.34 ? 2217 HOH A O     1 
HETATM 18578 O  O     . HOH DA 11 .    ? -52.418 24.328  82.734  1.00 40.97 ? 2218 HOH A O     1 
HETATM 18579 O  O     . HOH DA 11 .    ? 14.746  60.922  94.867  1.00 31.49 ? 2219 HOH A O     1 
HETATM 18580 O  O     . HOH DA 11 .    ? -42.332 60.539  74.385  1.00 35.45 ? 2220 HOH A O     1 
HETATM 18581 O  O     . HOH DA 11 .    ? -58.393 38.115  76.480  1.00 33.75 ? 2221 HOH A O     1 
HETATM 18582 O  O     . HOH DA 11 .    ? 0.310   76.561  123.327 1.00 43.57 ? 2222 HOH A O     1 
HETATM 18583 O  O     . HOH DA 11 .    ? -35.013 40.477  92.367  1.00 26.13 ? 2223 HOH A O     1 
HETATM 18584 O  O     . HOH DA 11 .    ? -38.074 62.124  105.556 1.00 35.88 ? 2224 HOH A O     1 
HETATM 18585 O  O     . HOH DA 11 .    ? -26.958 89.540  77.892  1.00 28.93 ? 2225 HOH A O     1 
HETATM 18586 O  O     . HOH DA 11 .    ? -33.210 48.966  75.580  1.00 40.90 ? 2226 HOH A O     1 
HETATM 18587 O  O     . HOH DA 11 .    ? -17.190 88.275  76.187  1.00 41.38 ? 2227 HOH A O     1 
HETATM 18588 O  O     . HOH DA 11 .    ? -28.057 78.223  101.584 1.00 32.32 ? 2228 HOH A O     1 
HETATM 18589 O  O     . HOH DA 11 .    ? -12.063 77.131  103.307 1.00 27.12 ? 2229 HOH A O     1 
HETATM 18590 O  O     . HOH DA 11 .    ? -55.134 76.162  83.976  1.00 40.88 ? 2230 HOH A O     1 
HETATM 18591 O  O     . HOH DA 11 .    ? -36.519 63.337  96.269  1.00 30.47 ? 2231 HOH A O     1 
HETATM 18592 O  O     . HOH DA 11 .    ? -34.467 75.810  83.339  1.00 31.97 ? 2232 HOH A O     1 
HETATM 18593 O  O     . HOH DA 11 .    ? -16.147 64.722  66.903  1.00 38.22 ? 2233 HOH A O     1 
HETATM 18594 O  O     . HOH DA 11 .    ? -52.213 48.805  62.996  1.00 32.98 ? 2234 HOH A O     1 
HETATM 18595 O  O     . HOH DA 11 .    ? -54.845 56.504  64.995  1.00 19.23 ? 2235 HOH A O     1 
HETATM 18596 O  O     . HOH DA 11 .    ? -0.960  50.439  57.994  1.00 29.51 ? 2236 HOH A O     1 
HETATM 18597 O  O     . HOH DA 11 .    ? -0.426  77.343  117.418 1.00 27.03 ? 2237 HOH A O     1 
HETATM 18598 O  O     . HOH DA 11 .    ? -19.953 59.213  76.472  1.00 25.69 ? 2238 HOH A O     1 
HETATM 18599 O  O     . HOH DA 11 .    ? -41.314 85.777  114.069 1.00 30.04 ? 2239 HOH A O     1 
HETATM 18600 O  O     . HOH DA 11 .    ? -4.802  70.263  76.602  1.00 39.74 ? 2240 HOH A O     1 
HETATM 18601 O  O     . HOH DA 11 .    ? -6.948  80.560  128.171 1.00 38.10 ? 2241 HOH A O     1 
HETATM 18602 O  O     . HOH DA 11 .    ? -14.237 64.662  51.329  1.00 42.56 ? 2242 HOH A O     1 
HETATM 18603 O  O     . HOH DA 11 .    ? -24.973 66.926  86.435  1.00 32.39 ? 2243 HOH A O     1 
HETATM 18604 O  O     . HOH DA 11 .    ? -37.581 62.020  81.213  1.00 30.99 ? 2244 HOH A O     1 
HETATM 18605 O  O     . HOH DA 11 .    ? -63.716 47.331  74.131  1.00 40.27 ? 2245 HOH A O     1 
HETATM 18606 O  O     . HOH DA 11 .    ? -36.741 63.979  82.950  1.00 41.15 ? 2246 HOH A O     1 
HETATM 18607 O  O     . HOH DA 11 .    ? 12.673  73.999  91.899  1.00 36.02 ? 2247 HOH A O     1 
HETATM 18608 O  O     . HOH DA 11 .    ? -27.300 58.748  76.275  1.00 40.81 ? 2248 HOH A O     1 
HETATM 18609 O  O     . HOH DA 11 .    ? -45.264 86.829  112.069 1.00 44.83 ? 2249 HOH A O     1 
HETATM 18610 O  O     . HOH DA 11 .    ? -4.752  43.668  58.047  1.00 35.89 ? 2250 HOH A O     1 
HETATM 18611 O  O     . HOH DA 11 .    ? -47.672 72.257  113.334 1.00 41.93 ? 2251 HOH A O     1 
HETATM 18612 O  O     . HOH DA 11 .    ? 7.027   54.035  101.650 1.00 21.37 ? 2252 HOH A O     1 
HETATM 18613 O  O     . HOH DA 11 .    ? 0.455   85.175  112.081 1.00 31.62 ? 2253 HOH A O     1 
HETATM 18614 O  O     . HOH DA 11 .    ? 1.631   73.104  116.123 1.00 31.83 ? 2254 HOH A O     1 
HETATM 18615 O  O     . HOH DA 11 .    ? -28.520 57.200  60.220  1.00 37.45 ? 2255 HOH A O     1 
HETATM 18616 O  O     . HOH DA 11 .    ? -0.623  83.701  109.962 1.00 30.68 ? 2256 HOH A O     1 
HETATM 18617 O  O     . HOH DA 11 .    ? -44.612 30.193  96.680  1.00 41.42 ? 2257 HOH A O     1 
HETATM 18618 O  O     . HOH DA 11 .    ? -26.380 82.652  113.111 1.00 26.34 ? 2258 HOH A O     1 
HETATM 18619 O  O     . HOH DA 11 .    ? -38.785 60.817  74.782  1.00 41.34 ? 2259 HOH A O     1 
HETATM 18620 O  O     . HOH DA 11 .    ? 0.537   85.370  103.192 1.00 25.66 ? 2260 HOH A O     1 
HETATM 18621 O  O     . HOH DA 11 .    ? -31.578 84.240  99.639  1.00 24.44 ? 2261 HOH A O     1 
HETATM 18622 O  O     . HOH DA 11 .    ? -11.708 73.166  128.765 1.00 28.72 ? 2262 HOH A O     1 
HETATM 18623 O  O     . HOH DA 11 .    ? -14.206 75.861  110.068 1.00 24.90 ? 2263 HOH A O     1 
HETATM 18624 O  O     . HOH DA 11 .    ? -18.783 61.437  85.634  1.00 25.30 ? 2264 HOH A O     1 
HETATM 18625 O  O     . HOH DA 11 .    ? -44.461 58.815  55.427  1.00 32.17 ? 2265 HOH A O     1 
HETATM 18626 O  O     . HOH DA 11 .    ? -3.906  79.033  111.735 1.00 36.16 ? 2266 HOH A O     1 
HETATM 18627 O  O     . HOH DA 11 .    ? -13.109 59.302  122.700 1.00 27.48 ? 2267 HOH A O     1 
HETATM 18628 O  O     . HOH DA 11 .    ? -56.172 34.463  86.513  1.00 28.92 ? 2268 HOH A O     1 
HETATM 18629 O  O     . HOH DA 11 .    ? -35.383 73.343  83.794  1.00 26.83 ? 2269 HOH A O     1 
HETATM 18630 O  O     . HOH DA 11 .    ? -14.161 61.427  107.808 1.00 28.37 ? 2270 HOH A O     1 
HETATM 18631 O  O     . HOH DA 11 .    ? -42.638 61.264  100.371 1.00 25.66 ? 2271 HOH A O     1 
HETATM 18632 O  O     . HOH DA 11 .    ? -38.620 49.452  102.693 1.00 30.84 ? 2272 HOH A O     1 
HETATM 18633 O  O     . HOH DA 11 .    ? 20.574  58.357  111.390 1.00 38.11 ? 2273 HOH A O     1 
HETATM 18634 O  O     . HOH DA 11 .    ? -44.180 73.650  75.191  1.00 28.27 ? 2274 HOH A O     1 
HETATM 18635 O  O     . HOH DA 11 .    ? -14.724 48.812  75.944  1.00 31.64 ? 2275 HOH A O     1 
HETATM 18636 O  O     . HOH DA 11 .    ? -46.652 59.730  102.280 1.00 24.48 ? 2276 HOH A O     1 
HETATM 18637 O  O     . HOH DA 11 .    ? -49.990 32.651  91.943  1.00 37.99 ? 2277 HOH A O     1 
HETATM 18638 O  O     . HOH DA 11 .    ? -20.731 54.889  91.398  1.00 39.13 ? 2278 HOH A O     1 
HETATM 18639 O  O     . HOH DA 11 .    ? -23.565 65.280  130.171 1.00 41.11 ? 2279 HOH A O     1 
HETATM 18640 O  O     . HOH DA 11 .    ? -0.440  65.800  94.650  1.00 35.77 ? 2280 HOH A O     1 
HETATM 18641 O  O     . HOH DA 11 .    ? 1.765   64.010  119.463 1.00 41.40 ? 2281 HOH A O     1 
HETATM 18642 O  O     . HOH DA 11 .    ? -6.146  68.567  92.744  1.00 29.78 ? 2282 HOH A O     1 
HETATM 18643 O  O     . HOH DA 11 .    ? -18.832 59.225  104.577 1.00 25.73 ? 2283 HOH A O     1 
HETATM 18644 O  O     . HOH DA 11 .    ? -55.078 29.832  79.926  1.00 42.46 ? 2284 HOH A O     1 
HETATM 18645 O  O     . HOH DA 11 .    ? -21.078 55.157  95.078  1.00 34.02 ? 2285 HOH A O     1 
HETATM 18646 O  O     . HOH DA 11 .    ? -63.520 73.398  78.619  1.00 34.09 ? 2286 HOH A O     1 
HETATM 18647 O  O     . HOH DA 11 .    ? 14.415  86.848  110.528 1.00 33.23 ? 2287 HOH A O     1 
HETATM 18648 O  O     . HOH DA 11 .    ? -6.398  54.684  105.518 1.00 31.57 ? 2288 HOH A O     1 
HETATM 18649 O  O     . HOH DA 11 .    ? -25.818 50.798  105.489 1.00 36.68 ? 2289 HOH A O     1 
HETATM 18650 O  O     . HOH DA 11 .    ? -22.711 67.532  97.811  1.00 23.02 ? 2290 HOH A O     1 
HETATM 18651 O  O     . HOH DA 11 .    ? -5.771  65.097  114.525 1.00 23.07 ? 2291 HOH A O     1 
HETATM 18652 O  O     . HOH DA 11 .    ? -4.992  54.454  108.484 1.00 22.88 ? 2292 HOH A O     1 
HETATM 18653 O  O     . HOH DA 11 .    ? -60.300 61.435  92.943  1.00 25.27 ? 2293 HOH A O     1 
HETATM 18654 O  O     . HOH DA 11 .    ? -0.059  86.404  106.183 1.00 33.83 ? 2294 HOH A O     1 
HETATM 18655 O  O     . HOH DA 11 .    ? -65.605 58.826  75.979  1.00 22.66 ? 2295 HOH A O     1 
HETATM 18656 O  O     . HOH DA 11 .    ? 16.710  57.804  103.075 1.00 24.54 ? 2296 HOH A O     1 
HETATM 18657 O  O     . HOH DA 11 .    ? -59.308 54.157  74.909  1.00 21.25 ? 2297 HOH A O     1 
HETATM 18658 O  O     . HOH DA 11 .    ? 5.766   63.009  97.537  1.00 21.19 ? 2298 HOH A O     1 
HETATM 18659 O  O     . HOH DA 11 .    ? -21.147 56.854  53.687  1.00 40.64 ? 2299 HOH A O     1 
HETATM 18660 O  O     . HOH DA 11 .    ? -21.728 42.809  60.962  1.00 39.32 ? 2300 HOH A O     1 
HETATM 18661 O  O     . HOH DA 11 .    ? -19.951 78.792  70.342  1.00 26.69 ? 2301 HOH A O     1 
HETATM 18662 O  O     . HOH DA 11 .    ? -32.062 61.786  111.910 1.00 26.25 ? 2302 HOH A O     1 
HETATM 18663 O  O     . HOH DA 11 .    ? 10.967  67.434  117.005 1.00 27.52 ? 2303 HOH A O     1 
HETATM 18664 O  O     . HOH DA 11 .    ? -21.484 47.203  58.164  1.00 37.30 ? 2304 HOH A O     1 
HETATM 18665 O  O     . HOH DA 11 .    ? -44.509 77.447  70.405  1.00 41.22 ? 2305 HOH A O     1 
HETATM 18666 O  O     . HOH DA 11 .    ? -26.146 56.490  108.243 1.00 23.29 ? 2306 HOH A O     1 
HETATM 18667 O  O     . HOH DA 11 .    ? 9.331   56.902  97.833  1.00 31.14 ? 2307 HOH A O     1 
HETATM 18668 O  O     . HOH DA 11 .    ? -20.016 91.135  97.413  1.00 36.48 ? 2308 HOH A O     1 
HETATM 18669 O  O     . HOH DA 11 .    ? -65.191 47.798  85.792  1.00 38.09 ? 2309 HOH A O     1 
HETATM 18670 O  O     . HOH DA 11 .    ? -24.318 92.787  127.178 1.00 34.66 ? 2310 HOH A O     1 
HETATM 18671 O  O     . HOH DA 11 .    ? -57.522 64.702  91.246  1.00 31.87 ? 2311 HOH A O     1 
HETATM 18672 O  O     . HOH DA 11 .    ? -18.935 70.234  87.939  1.00 30.20 ? 2312 HOH A O     1 
HETATM 18673 O  O     . HOH DA 11 .    ? -0.098  92.975  104.985 1.00 32.53 ? 2313 HOH A O     1 
HETATM 18674 O  O     . HOH DA 11 .    ? -35.719 51.821  69.702  1.00 37.43 ? 2314 HOH A O     1 
HETATM 18675 O  O     . HOH DA 11 .    ? -6.268  82.672  103.535 1.00 24.42 ? 2315 HOH A O     1 
HETATM 18676 O  O     . HOH DA 11 .    ? -43.572 75.413  114.355 1.00 29.63 ? 2316 HOH A O     1 
HETATM 18677 O  O     . HOH DA 11 .    ? -32.350 59.742  109.850 1.00 31.28 ? 2317 HOH A O     1 
HETATM 18678 O  O     . HOH DA 11 .    ? -4.120  69.993  106.909 1.00 32.06 ? 2318 HOH A O     1 
HETATM 18679 O  O     . HOH DA 11 .    ? -44.539 63.324  81.649  1.00 17.26 ? 2319 HOH A O     1 
HETATM 18680 O  O     . HOH DA 11 .    ? -10.129 67.113  124.983 1.00 38.91 ? 2320 HOH A O     1 
HETATM 18681 O  O     . HOH DA 11 .    ? -0.734  58.194  110.764 1.00 34.79 ? 2321 HOH A O     1 
HETATM 18682 O  O     . HOH DA 11 .    ? -22.329 67.592  81.485  1.00 33.55 ? 2322 HOH A O     1 
HETATM 18683 O  O     . HOH DA 11 .    ? -51.305 55.225  76.028  1.00 20.50 ? 2323 HOH A O     1 
HETATM 18684 O  O     . HOH DA 11 .    ? 16.870  71.374  119.596 1.00 28.87 ? 2324 HOH A O     1 
HETATM 18685 O  O     . HOH DA 11 .    ? -20.824 70.832  75.833  1.00 26.04 ? 2325 HOH A O     1 
HETATM 18686 O  O     . HOH DA 11 .    ? -46.123 30.517  85.705  1.00 34.45 ? 2326 HOH A O     1 
HETATM 18687 O  O     . HOH DA 11 .    ? -26.973 53.858  109.981 1.00 31.13 ? 2327 HOH A O     1 
HETATM 18688 O  O     . HOH DA 11 .    ? -24.410 92.774  105.314 1.00 38.41 ? 2328 HOH A O     1 
HETATM 18689 O  O     . HOH DA 11 .    ? -11.388 84.491  136.410 1.00 51.76 ? 2329 HOH A O     1 
HETATM 18690 O  O     . HOH DA 11 .    ? 20.527  83.377  101.641 1.00 42.94 ? 2330 HOH A O     1 
HETATM 18691 O  O     . HOH DA 11 .    ? -10.114 82.272  78.617  1.00 41.73 ? 2331 HOH A O     1 
HETATM 18692 O  O     . HOH DA 11 .    ? -41.005 90.687  99.050  1.00 26.92 ? 2332 HOH A O     1 
HETATM 18693 O  O     . HOH DA 11 .    ? -18.089 57.449  97.509  1.00 20.56 ? 2333 HOH A O     1 
HETATM 18694 O  O     . HOH DA 11 .    ? -32.249 79.354  96.549  1.00 26.48 ? 2334 HOH A O     1 
HETATM 18695 O  O     . HOH DA 11 .    ? -40.850 48.895  64.109  1.00 28.60 ? 2335 HOH A O     1 
HETATM 18696 O  O     . HOH DA 11 .    ? -24.809 88.284  79.429  1.00 23.40 ? 2336 HOH A O     1 
HETATM 18697 O  O     . HOH DA 11 .    ? -39.070 35.340  85.994  1.00 35.05 ? 2337 HOH A O     1 
HETATM 18698 O  O     . HOH DA 11 .    ? -9.486  65.055  76.645  1.00 24.04 ? 2338 HOH A O     1 
HETATM 18699 O  O     . HOH DA 11 .    ? -61.872 61.776  68.332  1.00 26.94 ? 2339 HOH A O     1 
HETATM 18700 O  O     . HOH DA 11 .    ? -17.275 86.869  92.342  1.00 27.44 ? 2340 HOH A O     1 
HETATM 18701 O  O     . HOH DA 11 .    ? -64.404 59.728  92.862  1.00 37.85 ? 2341 HOH A O     1 
HETATM 18702 O  O     . HOH DA 11 .    ? -26.181 85.392  137.790 1.00 38.63 ? 2342 HOH A O     1 
HETATM 18703 O  O     . HOH DA 11 .    ? 8.421   92.849  99.330  1.00 44.26 ? 2343 HOH A O     1 
HETATM 18704 O  O     . HOH DA 11 .    ? -37.578 77.703  120.710 1.00 38.22 ? 2344 HOH A O     1 
HETATM 18705 O  O     . HOH DA 11 .    ? -50.652 69.721  100.564 1.00 22.89 ? 2345 HOH A O     1 
HETATM 18706 O  O     . HOH DA 11 .    ? -0.568  67.546  90.258  1.00 46.74 ? 2346 HOH A O     1 
HETATM 18707 O  O     . HOH DA 11 .    ? -35.749 39.483  84.816  1.00 41.21 ? 2347 HOH A O     1 
HETATM 18708 O  O     . HOH DA 11 .    ? -42.984 85.267  97.653  1.00 27.29 ? 2348 HOH A O     1 
HETATM 18709 O  O     . HOH DA 11 .    ? 18.108  57.147  105.604 1.00 33.89 ? 2349 HOH A O     1 
HETATM 18710 O  O     . HOH DA 11 .    ? -41.255 71.564  64.499  1.00 29.71 ? 2350 HOH A O     1 
HETATM 18711 O  O     . HOH DA 11 .    ? 5.147   67.145  96.269  1.00 26.91 ? 2351 HOH A O     1 
HETATM 18712 O  O     . HOH DA 11 .    ? -5.303  77.669  95.286  1.00 30.93 ? 2352 HOH A O     1 
HETATM 18713 O  O     . HOH DA 11 .    ? -44.241 41.567  104.487 1.00 35.00 ? 2353 HOH A O     1 
HETATM 18714 O  O     . HOH DA 11 .    ? -47.774 57.647  86.451  1.00 18.88 ? 2354 HOH A O     1 
HETATM 18715 O  O     . HOH DA 11 .    ? 7.087   57.422  112.620 1.00 34.81 ? 2355 HOH A O     1 
HETATM 18716 O  O     . HOH DA 11 .    ? -53.031 56.910  55.444  1.00 37.92 ? 2356 HOH A O     1 
HETATM 18717 O  O     . HOH DA 11 .    ? -32.338 60.569  73.760  1.00 35.53 ? 2357 HOH A O     1 
HETATM 18718 O  O     . HOH DA 11 .    ? 7.117   84.715  94.626  1.00 42.83 ? 2358 HOH A O     1 
HETATM 18719 O  O     . HOH DA 11 .    ? -28.124 62.047  102.413 1.00 18.84 ? 2359 HOH A O     1 
HETATM 18720 O  O     . HOH DA 11 .    ? -10.588 63.165  72.977  1.00 31.62 ? 2360 HOH A O     1 
HETATM 18721 O  O     . HOH DA 11 .    ? -39.078 52.626  105.623 1.00 39.19 ? 2361 HOH A O     1 
HETATM 18722 O  O     . HOH DA 11 .    ? -23.373 63.767  106.409 1.00 20.49 ? 2362 HOH A O     1 
HETATM 18723 O  O     . HOH DA 11 .    ? -2.267  74.559  84.599  1.00 35.89 ? 2363 HOH A O     1 
HETATM 18724 O  O     . HOH DA 11 .    ? -51.072 64.868  95.063  1.00 22.63 ? 2364 HOH A O     1 
HETATM 18725 O  O     . HOH DA 11 .    ? -46.357 54.225  89.847  1.00 20.84 ? 2365 HOH A O     1 
HETATM 18726 O  O     . HOH DA 11 .    ? 6.449   90.718  107.058 1.00 34.27 ? 2366 HOH A O     1 
HETATM 18727 O  O     . HOH DA 11 .    ? -40.600 58.415  80.300  1.00 32.44 ? 2367 HOH A O     1 
HETATM 18728 O  O     . HOH DA 11 .    ? -43.250 85.565  95.084  1.00 37.72 ? 2368 HOH A O     1 
HETATM 18729 O  O     . HOH DA 11 .    ? -17.549 72.799  111.500 1.00 20.73 ? 2369 HOH A O     1 
HETATM 18730 O  O     . HOH DA 11 .    ? -41.619 79.707  80.311  1.00 32.94 ? 2370 HOH A O     1 
HETATM 18731 O  O     . HOH DA 11 .    ? -23.905 83.187  112.386 1.00 24.07 ? 2371 HOH A O     1 
HETATM 18732 O  O     . HOH DA 11 .    ? -30.763 67.163  98.888  1.00 42.43 ? 2372 HOH A O     1 
HETATM 18733 O  O     . HOH DA 11 .    ? -12.324 40.264  68.534  1.00 41.22 ? 2373 HOH A O     1 
HETATM 18734 O  O     . HOH DA 11 .    ? 10.792  57.336  106.055 1.00 30.65 ? 2374 HOH A O     1 
HETATM 18735 O  O     . HOH DA 11 .    ? -52.898 63.604  98.554  1.00 22.92 ? 2375 HOH A O     1 
HETATM 18736 O  O     . HOH DA 11 .    ? -24.260 59.412  121.793 1.00 37.01 ? 2376 HOH A O     1 
HETATM 18737 O  O     . HOH DA 11 .    ? -50.590 51.992  64.169  1.00 22.32 ? 2377 HOH A O     1 
HETATM 18738 O  O     . HOH DA 11 .    ? -3.949  78.300  122.769 1.00 27.78 ? 2378 HOH A O     1 
HETATM 18739 O  O     . HOH DA 11 .    ? -13.808 55.600  111.878 1.00 39.66 ? 2379 HOH A O     1 
HETATM 18740 O  O     . HOH DA 11 .    ? -57.964 37.567  96.033  1.00 45.10 ? 2380 HOH A O     1 
HETATM 18741 O  O     . HOH DA 11 .    ? -26.232 68.963  99.493  1.00 42.62 ? 2381 HOH A O     1 
HETATM 18742 O  O     . HOH DA 11 .    ? -20.222 66.103  81.347  1.00 28.42 ? 2382 HOH A O     1 
HETATM 18743 O  O     . HOH DA 11 .    ? -2.752  79.990  72.668  1.00 48.58 ? 2383 HOH A O     1 
HETATM 18744 O  O     . HOH DA 11 .    ? -47.123 60.282  85.382  1.00 18.62 ? 2384 HOH A O     1 
HETATM 18745 O  O     . HOH DA 11 .    ? 4.262   73.588  116.576 1.00 31.65 ? 2385 HOH A O     1 
HETATM 18746 O  O     . HOH DA 11 .    ? -8.719  60.103  107.381 1.00 21.44 ? 2386 HOH A O     1 
HETATM 18747 O  O     . HOH DA 11 .    ? -17.012 53.398  76.424  1.00 34.09 ? 2387 HOH A O     1 
HETATM 18748 O  O     . HOH DA 11 .    ? -11.739 71.835  76.800  1.00 32.72 ? 2388 HOH A O     1 
HETATM 18749 O  O     . HOH DA 11 .    ? -4.046  73.171  117.131 1.00 27.35 ? 2389 HOH A O     1 
HETATM 18750 O  O     . HOH DA 11 .    ? -3.750  57.783  73.089  1.00 25.98 ? 2390 HOH A O     1 
HETATM 18751 O  O     . HOH DA 11 .    ? -52.348 54.036  100.505 1.00 30.60 ? 2391 HOH A O     1 
HETATM 18752 O  O     . HOH DA 11 .    ? -23.189 62.651  66.558  1.00 36.98 ? 2392 HOH A O     1 
HETATM 18753 O  O     . HOH DA 11 .    ? -51.041 69.845  94.147  1.00 24.66 ? 2393 HOH A O     1 
HETATM 18754 O  O     . HOH DA 11 .    ? -8.888  62.174  70.884  1.00 39.89 ? 2394 HOH A O     1 
HETATM 18755 O  O     . HOH DA 11 .    ? -54.267 47.466  67.501  1.00 29.71 ? 2395 HOH A O     1 
HETATM 18756 O  O     . HOH DA 11 .    ? -26.430 80.442  101.899 1.00 31.18 ? 2396 HOH A O     1 
HETATM 18757 O  O     . HOH DA 11 .    ? -58.210 65.363  94.490  1.00 30.85 ? 2397 HOH A O     1 
HETATM 18758 O  O     . HOH DA 11 .    ? -0.175  52.903  63.230  1.00 28.88 ? 2398 HOH A O     1 
HETATM 18759 O  O     . HOH DA 11 .    ? -12.458 77.269  91.272  1.00 18.99 ? 2399 HOH A O     1 
HETATM 18760 O  O     . HOH DA 11 .    ? -2.268  53.807  104.748 1.00 29.07 ? 2400 HOH A O     1 
HETATM 18761 O  O     . HOH DA 11 .    ? 4.055   57.859  105.124 1.00 22.67 ? 2401 HOH A O     1 
HETATM 18762 O  O     . HOH DA 11 .    ? -52.251 78.219  87.784  1.00 32.60 ? 2402 HOH A O     1 
HETATM 18763 O  O     . HOH DA 11 .    ? -6.845  70.577  94.310  1.00 25.98 ? 2403 HOH A O     1 
HETATM 18764 O  O     . HOH DA 11 .    ? -32.373 82.219  97.978  1.00 25.76 ? 2404 HOH A O     1 
HETATM 18765 O  O     . HOH DA 11 .    ? -34.897 64.947  66.483  1.00 32.92 ? 2405 HOH A O     1 
HETATM 18766 O  O     . HOH DA 11 .    ? -24.718 88.962  100.020 1.00 23.48 ? 2406 HOH A O     1 
HETATM 18767 O  O     . HOH DA 11 .    ? -35.007 94.996  96.657  1.00 27.91 ? 2407 HOH A O     1 
HETATM 18768 O  O     . HOH DA 11 .    ? -33.781 52.703  82.201  1.00 36.51 ? 2408 HOH A O     1 
HETATM 18769 O  O     . HOH DA 11 .    ? -9.004  45.120  55.971  1.00 34.64 ? 2409 HOH A O     1 
HETATM 18770 O  O     . HOH DA 11 .    ? -22.835 55.270  88.957  1.00 39.99 ? 2410 HOH A O     1 
HETATM 18771 O  O     . HOH DA 11 .    ? -46.865 48.877  93.339  1.00 20.40 ? 2411 HOH A O     1 
HETATM 18772 O  O     . HOH DA 11 .    ? -23.770 63.511  91.786  1.00 24.22 ? 2412 HOH A O     1 
HETATM 18773 O  O     . HOH DA 11 .    ? -13.456 55.331  103.676 1.00 33.89 ? 2413 HOH A O     1 
HETATM 18774 O  O     . HOH DA 11 .    ? -11.723 59.744  84.908  1.00 33.67 ? 2414 HOH A O     1 
HETATM 18775 O  O     . HOH DA 11 .    ? -33.872 97.666  98.585  1.00 42.88 ? 2415 HOH A O     1 
HETATM 18776 O  O     . HOH DA 11 .    ? -48.229 54.590  61.470  1.00 25.87 ? 2416 HOH A O     1 
HETATM 18777 O  O     . HOH DA 11 .    ? -16.564 76.569  108.856 1.00 22.46 ? 2417 HOH A O     1 
HETATM 18778 O  O     . HOH DA 11 .    ? -53.596 55.408  68.635  1.00 19.97 ? 2418 HOH A O     1 
HETATM 18779 O  O     . HOH DA 11 .    ? -61.746 58.080  70.305  1.00 22.58 ? 2419 HOH A O     1 
HETATM 18780 O  O     . HOH DA 11 .    ? -25.306 87.588  133.190 1.00 42.92 ? 2420 HOH A O     1 
HETATM 18781 O  O     . HOH DA 11 .    ? -37.815 40.900  71.818  1.00 30.05 ? 2421 HOH A O     1 
HETATM 18782 O  O     . HOH DA 11 .    ? -56.589 45.918  71.258  1.00 24.47 ? 2422 HOH A O     1 
HETATM 18783 O  O     . HOH DA 11 .    ? -26.669 97.066  89.357  1.00 35.19 ? 2423 HOH A O     1 
HETATM 18784 O  O     . HOH DA 11 .    ? 14.002  82.015  114.511 1.00 26.85 ? 2424 HOH A O     1 
HETATM 18785 O  O     . HOH DA 11 .    ? -2.692  55.962  99.950  1.00 30.89 ? 2425 HOH A O     1 
HETATM 18786 O  O     . HOH DA 11 .    ? -49.724 68.582  92.255  1.00 23.40 ? 2426 HOH A O     1 
HETATM 18787 O  O     . HOH DA 11 .    ? -52.139 72.697  64.501  1.00 31.86 ? 2427 HOH A O     1 
HETATM 18788 O  O     . HOH DA 11 .    ? -57.498 57.818  101.368 1.00 27.34 ? 2428 HOH A O     1 
HETATM 18789 O  O     . HOH DA 11 .    ? -17.562 80.198  134.892 1.00 41.90 ? 2429 HOH A O     1 
HETATM 18790 O  O     . HOH DA 11 .    ? -37.658 69.030  123.648 1.00 37.44 ? 2430 HOH A O     1 
HETATM 18791 O  O     . HOH DA 11 .    ? -61.126 52.999  91.388  1.00 28.68 ? 2431 HOH A O     1 
HETATM 18792 O  O     . HOH DA 11 .    ? -59.532 60.753  76.070  1.00 19.37 ? 2432 HOH A O     1 
HETATM 18793 O  O     . HOH DA 11 .    ? -55.484 36.629  76.408  1.00 31.57 ? 2433 HOH A O     1 
HETATM 18794 O  O     . HOH DA 11 .    ? -45.649 65.211  92.027  1.00 20.13 ? 2434 HOH A O     1 
HETATM 18795 O  O     . HOH DA 11 .    ? -10.857 92.033  124.810 1.00 36.33 ? 2435 HOH A O     1 
HETATM 18796 O  O     . HOH DA 11 .    ? -36.446 58.943  94.461  1.00 20.70 ? 2436 HOH A O     1 
HETATM 18797 O  O     . HOH DA 11 .    ? -61.506 70.305  83.163  1.00 23.91 ? 2437 HOH A O     1 
HETATM 18798 O  O     . HOH DA 11 .    ? -27.343 82.295  129.987 1.00 31.30 ? 2438 HOH A O     1 
HETATM 18799 O  O     . HOH DA 11 .    ? -63.679 52.780  89.995  1.00 38.01 ? 2439 HOH A O     1 
HETATM 18800 O  O     . HOH DA 11 .    ? -30.594 91.004  107.434 1.00 27.41 ? 2440 HOH A O     1 
HETATM 18801 O  O     . HOH DA 11 .    ? -46.319 67.380  59.853  1.00 27.70 ? 2441 HOH A O     1 
HETATM 18802 O  O     . HOH DA 11 .    ? -50.076 37.948  99.972  1.00 36.36 ? 2442 HOH A O     1 
HETATM 18803 O  O     . HOH DA 11 .    ? -33.083 78.267  74.504  1.00 30.01 ? 2443 HOH A O     1 
HETATM 18804 O  O     . HOH DA 11 .    ? -41.260 27.807  70.507  1.00 40.66 ? 2444 HOH A O     1 
HETATM 18805 O  O     . HOH DA 11 .    ? -48.526 81.182  85.164  1.00 36.79 ? 2445 HOH A O     1 
HETATM 18806 O  O     . HOH DA 11 .    ? -3.358  66.249  77.339  1.00 32.14 ? 2446 HOH A O     1 
HETATM 18807 O  O     . HOH DA 11 .    ? -26.853 69.406  103.946 1.00 33.88 ? 2447 HOH A O     1 
HETATM 18808 O  O     . HOH DA 11 .    ? -47.995 66.079  58.076  1.00 29.82 ? 2448 HOH A O     1 
HETATM 18809 O  O     . HOH DA 11 .    ? -35.392 51.772  85.544  1.00 19.41 ? 2449 HOH A O     1 
HETATM 18810 O  O     . HOH DA 11 .    ? -44.017 55.716  95.237  1.00 18.93 ? 2450 HOH A O     1 
HETATM 18811 O  O     . HOH DA 11 .    ? -46.470 34.720  101.128 1.00 43.09 ? 2451 HOH A O     1 
HETATM 18812 O  O     . HOH DA 11 .    ? -17.650 59.059  86.633  1.00 36.00 ? 2452 HOH A O     1 
HETATM 18813 O  O     . HOH DA 11 .    ? -8.140  60.129  94.388  1.00 36.75 ? 2453 HOH A O     1 
HETATM 18814 O  O     . HOH DA 11 .    ? -5.943  76.154  111.392 1.00 19.67 ? 2454 HOH A O     1 
HETATM 18815 O  O     . HOH DA 11 .    ? -56.043 55.720  95.164  1.00 21.63 ? 2455 HOH A O     1 
HETATM 18816 O  O     . HOH DA 11 .    ? -51.763 72.958  105.809 1.00 34.89 ? 2456 HOH A O     1 
HETATM 18817 O  O     . HOH DA 11 .    ? 23.069  77.025  101.592 1.00 42.82 ? 2457 HOH A O     1 
HETATM 18818 O  O     . HOH DA 11 .    ? -8.568  65.120  114.158 1.00 20.51 ? 2458 HOH A O     1 
HETATM 18819 O  O     . HOH DA 11 .    ? -22.395 95.765  130.092 1.00 44.29 ? 2459 HOH A O     1 
HETATM 18820 O  O     . HOH DA 11 .    ? -1.090  83.816  118.188 1.00 28.96 ? 2460 HOH A O     1 
HETATM 18821 O  O     . HOH DA 11 .    ? -23.316 54.440  101.560 1.00 28.19 ? 2461 HOH A O     1 
HETATM 18822 O  O     . HOH DA 11 .    ? -3.101  77.912  101.618 1.00 31.85 ? 2462 HOH A O     1 
HETATM 18823 O  O     . HOH DA 11 .    ? -32.765 92.124  126.747 1.00 44.82 ? 2463 HOH A O     1 
HETATM 18824 O  O     . HOH DA 11 .    ? -37.883 65.380  88.551  1.00 35.21 ? 2464 HOH A O     1 
HETATM 18825 O  O     . HOH DA 11 .    ? -4.064  55.039  61.720  1.00 38.85 ? 2465 HOH A O     1 
HETATM 18826 O  O     . HOH DA 11 .    ? 14.473  87.828  106.331 1.00 37.36 ? 2466 HOH A O     1 
HETATM 18827 O  O     . HOH DA 11 .    ? -28.593 84.078  104.497 1.00 31.58 ? 2467 HOH A O     1 
HETATM 18828 O  O     . HOH DA 11 .    ? -37.139 45.474  104.286 1.00 31.36 ? 2468 HOH A O     1 
HETATM 18829 O  O     . HOH DA 11 .    ? -49.655 48.979  100.034 1.00 24.74 ? 2469 HOH A O     1 
HETATM 18830 O  O     . HOH DA 11 .    ? -27.123 64.901  100.487 1.00 25.52 ? 2470 HOH A O     1 
HETATM 18831 O  O     . HOH DA 11 .    ? -25.788 63.760  105.012 1.00 24.93 ? 2471 HOH A O     1 
HETATM 18832 O  O     . HOH DA 11 .    ? -2.040  85.355  113.505 1.00 32.67 ? 2472 HOH A O     1 
HETATM 18833 O  O     . HOH DA 11 .    ? -8.966  77.635  132.219 1.00 37.76 ? 2473 HOH A O     1 
HETATM 18834 O  O     . HOH DA 11 .    ? -12.164 79.288  94.724  1.00 19.39 ? 2474 HOH A O     1 
HETATM 18835 O  O     . HOH DA 11 .    ? -40.785 68.895  63.562  1.00 39.86 ? 2475 HOH A O     1 
HETATM 18836 O  O     . HOH DA 11 .    ? -30.037 63.089  92.055  1.00 36.02 ? 2476 HOH A O     1 
HETATM 18837 O  O     . HOH DA 11 .    ? -31.767 82.588  75.545  1.00 23.28 ? 2477 HOH A O     1 
HETATM 18838 O  O     . HOH DA 11 .    ? -34.607 66.527  101.909 1.00 23.38 ? 2478 HOH A O     1 
HETATM 18839 O  O     . HOH DA 11 .    ? -39.462 78.288  100.349 1.00 26.60 ? 2479 HOH A O     1 
HETATM 18840 O  O     . HOH DA 11 .    ? -31.392 60.011  105.784 1.00 26.36 ? 2480 HOH A O     1 
HETATM 18841 O  O     . HOH DA 11 .    ? -10.646 67.796  108.299 1.00 18.58 ? 2481 HOH A O     1 
HETATM 18842 O  O     . HOH DA 11 .    ? -33.362 45.743  84.868  1.00 33.90 ? 2482 HOH A O     1 
HETATM 18843 O  O     . HOH DA 11 .    ? -6.771  42.108  66.421  1.00 28.40 ? 2483 HOH A O     1 
HETATM 18844 O  O     . HOH DA 11 .    ? -31.400 71.781  82.677  1.00 38.58 ? 2484 HOH A O     1 
HETATM 18845 O  O     . HOH DA 11 .    ? -36.780 68.270  83.530  1.00 32.13 ? 2485 HOH A O     1 
HETATM 18846 O  O     . HOH DA 11 .    ? -32.234 48.466  84.333  1.00 36.60 ? 2486 HOH A O     1 
HETATM 18847 O  O     . HOH DA 11 .    ? -42.229 47.562  81.303  1.00 22.13 ? 2487 HOH A O     1 
HETATM 18848 O  O     . HOH DA 11 .    ? -45.713 78.257  96.324  1.00 22.01 ? 2488 HOH A O     1 
HETATM 18849 O  O     . HOH DA 11 .    ? -12.747 89.996  102.120 1.00 39.11 ? 2489 HOH A O     1 
HETATM 18850 O  O     . HOH DA 11 .    ? -64.454 44.772  78.361  1.00 38.25 ? 2490 HOH A O     1 
HETATM 18851 O  O     . HOH DA 11 .    ? -21.979 54.486  86.590  1.00 37.89 ? 2491 HOH A O     1 
HETATM 18852 O  O     . HOH DA 11 .    ? 25.175  77.238  109.893 1.00 37.04 ? 2492 HOH A O     1 
HETATM 18853 O  O     . HOH DA 11 .    ? -0.929  73.442  88.953  1.00 34.35 ? 2493 HOH A O     1 
HETATM 18854 O  O     . HOH DA 11 .    ? -40.526 81.727  111.087 1.00 29.16 ? 2494 HOH A O     1 
HETATM 18855 O  O     . HOH DA 11 .    ? -2.936  62.530  77.862  1.00 26.11 ? 2495 HOH A O     1 
HETATM 18856 O  O     . HOH DA 11 .    ? -28.423 61.940  117.071 1.00 23.59 ? 2496 HOH A O     1 
HETATM 18857 O  O     . HOH DA 11 .    ? -45.971 29.327  89.545  1.00 41.63 ? 2497 HOH A O     1 
HETATM 18858 O  O     . HOH DA 11 .    ? -18.243 60.961  67.122  1.00 31.67 ? 2498 HOH A O     1 
HETATM 18859 O  O     . HOH DA 11 .    ? -61.038 55.381  67.673  1.00 21.78 ? 2499 HOH A O     1 
HETATM 18860 O  O     . HOH DA 11 .    ? -57.014 60.165  61.222  1.00 21.69 ? 2500 HOH A O     1 
HETATM 18861 O  O     . HOH DA 11 .    ? -18.796 97.659  127.298 1.00 45.11 ? 2501 HOH A O     1 
HETATM 18862 O  O     . HOH DA 11 .    ? -32.330 92.966  104.194 1.00 27.61 ? 2502 HOH A O     1 
HETATM 18863 O  O     . HOH DA 11 .    ? -56.619 31.721  80.526  1.00 39.11 ? 2503 HOH A O     1 
HETATM 18864 O  O     . HOH DA 11 .    ? -15.852 47.245  53.875  1.00 33.77 ? 2504 HOH A O     1 
HETATM 18865 O  O     . HOH DA 11 .    ? -20.033 86.793  91.726  1.00 23.55 ? 2505 HOH A O     1 
HETATM 18866 O  O     . HOH DA 11 .    ? -6.816  93.659  113.622 1.00 32.24 ? 2506 HOH A O     1 
HETATM 18867 O  O     . HOH DA 11 .    ? -26.254 50.307  96.793  1.00 28.04 ? 2507 HOH A O     1 
HETATM 18868 O  O     . HOH DA 11 .    ? 17.053  69.102  118.182 1.00 28.11 ? 2508 HOH A O     1 
HETATM 18869 O  O     . HOH DA 11 .    ? -18.858 59.672  70.181  1.00 24.89 ? 2509 HOH A O     1 
HETATM 18870 O  O     . HOH DA 11 .    ? -31.414 67.584  66.032  1.00 46.88 ? 2510 HOH A O     1 
HETATM 18871 O  O     . HOH DA 11 .    ? -41.397 64.165  103.835 1.00 23.29 ? 2511 HOH A O     1 
HETATM 18872 O  O     . HOH DA 11 .    ? -26.421 39.086  77.894  1.00 46.31 ? 2512 HOH A O     1 
HETATM 18873 O  O     . HOH DA 11 .    ? -25.737 70.039  131.573 1.00 41.55 ? 2513 HOH A O     1 
HETATM 18874 O  O     . HOH DA 11 .    ? -0.618  70.203  96.324  1.00 38.42 ? 2514 HOH A O     1 
HETATM 18875 O  O     . HOH DA 11 .    ? -38.474 73.287  90.456  1.00 33.39 ? 2515 HOH A O     1 
HETATM 18876 O  O     . HOH DA 11 .    ? -31.857 88.578  95.469  1.00 22.77 ? 2516 HOH A O     1 
HETATM 18877 O  O     . HOH DA 11 .    ? -33.502 98.135  93.600  1.00 47.15 ? 2517 HOH A O     1 
HETATM 18878 O  O     . HOH DA 11 .    ? -47.656 59.113  82.997  1.00 16.98 ? 2518 HOH A O     1 
HETATM 18879 O  O     . HOH DA 11 .    ? -31.815 89.105  108.960 1.00 30.90 ? 2519 HOH A O     1 
HETATM 18880 O  O     . HOH DA 11 .    ? -1.483  58.177  96.775  1.00 35.66 ? 2520 HOH A O     1 
HETATM 18881 O  O     . HOH DA 11 .    ? -32.147 75.075  126.689 1.00 32.10 ? 2521 HOH A O     1 
HETATM 18882 O  O     . HOH DA 11 .    ? -54.995 47.600  70.111  1.00 24.90 ? 2522 HOH A O     1 
HETATM 18883 O  O     . HOH DA 11 .    ? 15.224  83.013  111.581 1.00 26.71 ? 2523 HOH A O     1 
HETATM 18884 O  O     . HOH DA 11 .    ? -23.435 64.159  70.985  1.00 43.23 ? 2524 HOH A O     1 
HETATM 18885 O  O     . HOH DA 11 .    ? -47.737 64.198  96.986  1.00 24.53 ? 2525 HOH A O     1 
HETATM 18886 O  O     . HOH DA 11 .    ? -31.648 59.163  63.321  1.00 33.05 ? 2526 HOH A O     1 
HETATM 18887 O  O     . HOH DA 11 .    ? -32.299 98.227  124.349 1.00 44.49 ? 2527 HOH A O     1 
HETATM 18888 O  O     . HOH DA 11 .    ? -45.235 62.627  92.840  1.00 20.60 ? 2528 HOH A O     1 
HETATM 18889 O  O     . HOH DA 11 .    ? -57.904 57.781  63.220  1.00 22.65 ? 2529 HOH A O     1 
HETATM 18890 O  O     . HOH DA 11 .    ? -33.208 70.206  100.701 1.00 33.92 ? 2530 HOH A O     1 
HETATM 18891 O  O     . HOH DA 11 .    ? -7.105  62.409  107.339 1.00 22.66 ? 2531 HOH A O     1 
HETATM 18892 O  O     . HOH DA 11 .    ? -21.971 67.436  74.124  1.00 39.47 ? 2532 HOH A O     1 
HETATM 18893 O  O     . HOH DA 11 .    ? -9.482  39.986  61.414  1.00 43.45 ? 2533 HOH A O     1 
HETATM 18894 O  O     . HOH DA 11 .    ? -11.212 58.617  125.818 1.00 40.58 ? 2534 HOH A O     1 
HETATM 18895 O  O     . HOH DA 11 .    ? 23.288  65.653  115.127 1.00 29.60 ? 2535 HOH A O     1 
HETATM 18896 O  O     . HOH DA 11 .    ? -40.638 80.196  87.873  1.00 20.80 ? 2536 HOH A O     1 
HETATM 18897 O  O     . HOH DA 11 .    ? -41.085 71.569  114.617 1.00 28.24 ? 2537 HOH A O     1 
HETATM 18898 O  O     . HOH DA 11 .    ? -49.383 78.187  77.743  1.00 32.08 ? 2538 HOH A O     1 
HETATM 18899 O  O     . HOH DA 11 .    ? -60.120 47.065  88.830  1.00 29.46 ? 2539 HOH A O     1 
HETATM 18900 O  O     . HOH DA 11 .    ? -8.083  87.608  93.453  1.00 44.93 ? 2540 HOH A O     1 
HETATM 18901 O  O     . HOH DA 11 .    ? -46.618 81.209  93.522  1.00 41.22 ? 2541 HOH A O     1 
HETATM 18902 O  O     . HOH DA 11 .    ? -3.131  90.006  109.202 1.00 30.31 ? 2542 HOH A O     1 
HETATM 18903 O  O     . HOH DA 11 .    ? -19.559 54.980  107.265 1.00 32.07 ? 2543 HOH A O     1 
HETATM 18904 O  O     . HOH DA 11 .    ? -47.377 49.084  96.128  1.00 22.23 ? 2544 HOH A O     1 
HETATM 18905 O  O     . HOH DA 11 .    ? -34.689 80.522  120.713 1.00 25.55 ? 2545 HOH A O     1 
HETATM 18906 O  O     . HOH DA 11 .    ? -25.261 62.516  110.336 1.00 24.50 ? 2546 HOH A O     1 
HETATM 18907 O  O     . HOH DA 11 .    ? -24.113 48.150  99.112  1.00 46.40 ? 2547 HOH A O     1 
HETATM 18908 O  O     . HOH DA 11 .    ? 9.197   55.148  105.141 1.00 30.90 ? 2548 HOH A O     1 
HETATM 18909 O  O     . HOH DA 11 .    ? -67.262 59.973  69.921  1.00 31.58 ? 2549 HOH A O     1 
HETATM 18910 O  O     . HOH DA 11 .    ? -46.076 55.982  87.588  1.00 18.41 ? 2550 HOH A O     1 
HETATM 18911 O  O     . HOH DA 11 .    ? -34.060 69.328  76.446  1.00 39.94 ? 2551 HOH A O     1 
HETATM 18912 O  O     . HOH DA 11 .    ? -23.783 61.229  63.814  1.00 36.55 ? 2552 HOH A O     1 
HETATM 18913 O  O     . HOH DA 11 .    ? -25.926 61.031  58.735  1.00 45.75 ? 2553 HOH A O     1 
HETATM 18914 O  O     . HOH DA 11 .    ? -9.660  74.411  104.372 1.00 27.66 ? 2554 HOH A O     1 
HETATM 18915 O  O     . HOH DA 11 .    ? -59.080 51.855  66.234  1.00 22.88 ? 2555 HOH A O     1 
HETATM 18916 O  O     . HOH DA 11 .    ? -28.634 75.020  102.212 1.00 30.42 ? 2556 HOH A O     1 
HETATM 18917 O  O     . HOH DA 11 .    ? -47.739 85.043  102.144 1.00 39.04 ? 2557 HOH A O     1 
HETATM 18918 O  O     . HOH DA 11 .    ? -62.950 53.963  72.328  1.00 28.51 ? 2558 HOH A O     1 
HETATM 18919 O  O     . HOH DA 11 .    ? -53.640 43.274  65.662  1.00 46.89 ? 2559 HOH A O     1 
HETATM 18920 O  O     . HOH DA 11 .    ? 17.363  80.479  97.185  1.00 34.91 ? 2560 HOH A O     1 
HETATM 18921 O  O     . HOH DA 11 .    ? 12.403  75.667  95.204  1.00 37.21 ? 2561 HOH A O     1 
HETATM 18922 O  O     . HOH DA 11 .    ? -46.750 82.288  101.724 1.00 27.68 ? 2562 HOH A O     1 
HETATM 18923 O  O     . HOH DA 11 .    ? -4.407  59.253  118.582 1.00 23.42 ? 2563 HOH A O     1 
HETATM 18924 O  O     . HOH DA 11 .    ? -18.276 79.460  127.518 1.00 27.94 ? 2564 HOH A O     1 
HETATM 18925 O  O     . HOH DA 11 .    ? -65.977 54.859  75.691  1.00 43.12 ? 2565 HOH A O     1 
HETATM 18926 O  O     . HOH DA 11 .    ? -33.461 93.468  86.467  1.00 40.37 ? 2566 HOH A O     1 
HETATM 18927 O  O     . HOH DA 11 .    ? 1.195   74.710  107.641 1.00 30.29 ? 2567 HOH A O     1 
HETATM 18928 O  O     . HOH DA 11 .    ? -41.505 70.895  95.593  1.00 28.18 ? 2568 HOH A O     1 
HETATM 18929 O  O     . HOH DA 11 .    ? -8.206  93.092  106.149 1.00 28.88 ? 2569 HOH A O     1 
HETATM 18930 O  O     . HOH DA 11 .    ? -41.862 55.165  105.118 1.00 37.52 ? 2570 HOH A O     1 
HETATM 18931 O  O     . HOH DA 11 .    ? -11.563 88.786  129.069 1.00 35.56 ? 2571 HOH A O     1 
HETATM 18932 O  O     . HOH DA 11 .    ? -66.656 68.065  72.167  1.00 39.82 ? 2572 HOH A O     1 
HETATM 18933 O  O     . HOH DA 11 .    ? -45.770 72.539  64.437  1.00 20.62 ? 2573 HOH A O     1 
HETATM 18934 O  O     . HOH DA 11 .    ? 10.737  67.098  112.264 1.00 34.32 ? 2574 HOH A O     1 
HETATM 18935 O  O     . HOH DA 11 .    ? -14.876 67.282  73.323  1.00 23.04 ? 2575 HOH A O     1 
HETATM 18936 O  O     . HOH DA 11 .    ? -7.490  42.590  62.192  1.00 28.34 ? 2576 HOH A O     1 
HETATM 18937 O  O     . HOH DA 11 .    ? -1.317  79.287  100.112 1.00 29.76 ? 2577 HOH A O     1 
HETATM 18938 O  O     . HOH DA 11 .    ? 18.174  58.788  95.913  1.00 33.44 ? 2578 HOH A O     1 
HETATM 18939 O  O     . HOH DA 11 .    ? -22.735 83.457  91.785  1.00 19.99 ? 2579 HOH A O     1 
HETATM 18940 O  O     . HOH DA 11 .    ? -64.334 42.956  86.507  1.00 35.92 ? 2580 HOH A O     1 
HETATM 18941 O  O     . HOH DA 11 .    ? 12.898  67.159  93.649  1.00 34.28 ? 2581 HOH A O     1 
HETATM 18942 O  O     . HOH DA 11 .    ? -1.653  77.740  121.458 1.00 29.27 ? 2582 HOH A O     1 
HETATM 18943 O  O     . HOH DA 11 .    ? -43.696 25.073  76.381  1.00 45.10 ? 2583 HOH A O     1 
HETATM 18944 O  O     . HOH DA 11 .    ? -49.862 72.377  101.347 1.00 24.23 ? 2584 HOH A O     1 
HETATM 18945 O  O     . HOH DA 11 .    ? -20.824 100.982 90.022  1.00 37.14 ? 2585 HOH A O     1 
HETATM 18946 O  O     . HOH DA 11 .    ? -54.312 37.475  89.442  1.00 32.43 ? 2586 HOH A O     1 
HETATM 18947 O  O     . HOH DA 11 .    ? 2.303   85.690  118.407 1.00 29.01 ? 2587 HOH A O     1 
HETATM 18948 O  O     . HOH DA 11 .    ? -36.780 60.476  96.585  1.00 21.73 ? 2588 HOH A O     1 
HETATM 18949 O  O     . HOH DA 11 .    ? -9.511  63.976  96.354  1.00 22.79 ? 2589 HOH A O     1 
HETATM 18950 O  O     . HOH DA 11 .    ? -52.218 61.979  94.951  1.00 23.48 ? 2590 HOH A O     1 
HETATM 18951 O  O     . HOH DA 11 .    ? -30.969 60.960  90.757  1.00 24.19 ? 2591 HOH A O     1 
HETATM 18952 O  O     . HOH DA 11 .    ? -18.034 39.541  68.481  1.00 45.86 ? 2592 HOH A O     1 
HETATM 18953 O  O     . HOH DA 11 .    ? -9.596  55.956  82.788  1.00 33.37 ? 2593 HOH A O     1 
HETATM 18954 O  O     . HOH DA 11 .    ? 19.275  81.959  113.622 1.00 32.01 ? 2594 HOH A O     1 
HETATM 18955 O  O     . HOH DA 11 .    ? -69.541 65.150  73.973  1.00 31.08 ? 2595 HOH A O     1 
HETATM 18956 O  O     . HOH DA 11 .    ? -30.550 72.993  98.993  1.00 38.05 ? 2596 HOH A O     1 
HETATM 18957 O  O     . HOH DA 11 .    ? 0.018   73.772  96.426  1.00 44.81 ? 2597 HOH A O     1 
HETATM 18958 O  O     . HOH DA 11 .    ? -49.027 47.645  97.570  1.00 24.60 ? 2598 HOH A O     1 
HETATM 18959 O  O     . HOH DA 11 .    ? -46.510 66.528  94.102  1.00 20.81 ? 2599 HOH A O     1 
HETATM 18960 O  O     . HOH DA 11 .    ? -38.322 32.315  97.388  1.00 39.98 ? 2600 HOH A O     1 
HETATM 18961 O  O     . HOH DA 11 .    ? -42.014 24.135  74.334  1.00 47.85 ? 2601 HOH A O     1 
HETATM 18962 O  O     . HOH DA 11 .    ? -65.303 71.420  80.660  1.00 29.91 ? 2602 HOH A O     1 
HETATM 18963 O  O     . HOH DA 11 .    ? -30.360 81.131  123.431 1.00 29.51 ? 2603 HOH A O     1 
HETATM 18964 O  O     . HOH DA 11 .    ? -19.623 85.202  75.714  1.00 31.99 ? 2604 HOH A O     1 
HETATM 18965 O  O     . HOH DA 11 .    ? -70.100 60.946  85.294  1.00 45.27 ? 2605 HOH A O     1 
HETATM 18966 O  O     . HOH DA 11 .    ? -16.357 60.343  106.705 1.00 25.93 ? 2606 HOH A O     1 
HETATM 18967 O  O     . HOH DA 11 .    ? -27.684 56.049  90.760  1.00 30.07 ? 2607 HOH A O     1 
HETATM 18968 O  O     . HOH DA 11 .    ? -49.013 83.296  109.290 1.00 35.04 ? 2608 HOH A O     1 
HETATM 18969 O  O     . HOH DA 11 .    ? 1.407   62.289  111.486 1.00 28.26 ? 2609 HOH A O     1 
HETATM 18970 O  O     . HOH DA 11 .    ? -41.823 67.861  91.340  1.00 21.18 ? 2610 HOH A O     1 
HETATM 18971 O  O     . HOH DA 11 .    ? 15.892  61.438  116.414 1.00 40.69 ? 2611 HOH A O     1 
HETATM 18972 O  O     . HOH DA 11 .    ? -60.788 68.536  68.715  1.00 25.98 ? 2612 HOH A O     1 
HETATM 18973 O  O     . HOH DA 11 .    ? -39.207 76.668  93.389  1.00 24.05 ? 2613 HOH A O     1 
HETATM 18974 O  O     . HOH DA 11 .    ? -2.103  62.791  113.532 1.00 37.06 ? 2614 HOH A O     1 
HETATM 18975 O  O     . HOH DA 11 .    ? 6.750   60.988  103.427 1.00 19.99 ? 2615 HOH A O     1 
HETATM 18976 O  O     . HOH DA 11 .    ? 20.713  61.925  99.311  1.00 27.43 ? 2616 HOH A O     1 
HETATM 18977 O  O     . HOH DA 11 .    ? 8.239   67.853  114.865 1.00 32.81 ? 2617 HOH A O     1 
HETATM 18978 O  O     . HOH DA 11 .    ? -4.260  71.285  127.002 1.00 44.11 ? 2618 HOH A O     1 
HETATM 18979 O  O     . HOH DA 11 .    ? -50.186 66.360  106.614 1.00 31.06 ? 2619 HOH A O     1 
HETATM 18980 O  O     . HOH DA 11 .    ? -7.025  38.323  63.735  1.00 36.90 ? 2620 HOH A O     1 
HETATM 18981 O  O     . HOH DA 11 .    ? -34.243 82.517  118.856 1.00 24.28 ? 2621 HOH A O     1 
HETATM 18982 O  O     . HOH DA 11 .    ? -44.118 31.554  84.385  1.00 31.20 ? 2622 HOH A O     1 
HETATM 18983 O  O     . HOH DA 11 .    ? -6.255  71.343  103.807 1.00 33.32 ? 2623 HOH A O     1 
HETATM 18984 O  O     . HOH DA 11 .    ? -49.627 75.915  101.766 1.00 25.54 ? 2624 HOH A O     1 
HETATM 18985 O  O     . HOH DA 11 .    ? -39.181 88.818  91.036  1.00 32.88 ? 2625 HOH A O     1 
HETATM 18986 O  O     . HOH DA 11 .    ? -2.087  78.087  75.999  1.00 31.06 ? 2626 HOH A O     1 
HETATM 18987 O  O     . HOH DA 11 .    ? -48.219 75.158  95.788  1.00 23.61 ? 2627 HOH A O     1 
HETATM 18988 O  O     . HOH DA 11 .    ? -63.553 70.939  70.978  1.00 28.50 ? 2628 HOH A O     1 
HETATM 18989 O  O     . HOH DA 11 .    ? -6.971  64.584  94.622  1.00 40.81 ? 2629 HOH A O     1 
HETATM 18990 O  O     A HOH DA 11 .    ? 4.182   60.439  101.282 0.65 23.27 ? 2630 HOH A O     1 
HETATM 18991 O  O     . HOH DA 11 .    ? -38.255 61.553  92.104  1.00 20.44 ? 2631 HOH A O     1 
HETATM 18992 O  O     . HOH DA 11 .    ? -39.605 61.542  94.755  1.00 24.22 ? 2632 HOH A O     1 
HETATM 18993 O  O     . HOH DA 11 .    ? -1.451  76.874  87.997  1.00 31.31 ? 2633 HOH A O     1 
HETATM 18994 O  O     . HOH DA 11 .    ? 2.564   83.916  126.991 1.00 40.39 ? 2634 HOH A O     1 
HETATM 18995 O  O     . HOH DA 11 .    ? 18.793  73.086  118.498 1.00 26.38 ? 2635 HOH A O     1 
HETATM 18996 O  O     . HOH DA 11 .    ? 10.154  63.110  113.287 1.00 35.35 ? 2636 HOH A O     1 
HETATM 18997 O  O     . HOH DA 11 .    ? -62.269 54.933  63.361  1.00 38.18 ? 2637 HOH A O     1 
HETATM 18998 O  O     . HOH DA 11 .    ? -3.120  57.549  68.402  1.00 36.68 ? 2638 HOH A O     1 
HETATM 18999 O  O     . HOH DA 11 .    ? -20.162 90.857  109.492 1.00 41.03 ? 2639 HOH A O     1 
HETATM 19000 O  O     . HOH DA 11 .    ? -31.037 70.201  129.658 1.00 43.67 ? 2640 HOH A O     1 
HETATM 19001 O  O     . HOH DA 11 .    ? -28.965 76.565  72.975  1.00 32.14 ? 2641 HOH A O     1 
HETATM 19002 O  O     . HOH DA 11 .    ? -38.254 50.489  98.602  1.00 26.76 ? 2642 HOH A O     1 
HETATM 19003 O  O     . HOH DA 11 .    ? 14.180  78.293  121.290 1.00 32.61 ? 2643 HOH A O     1 
HETATM 19004 O  O     . HOH DA 11 .    ? -22.778 58.931  76.222  1.00 33.43 ? 2644 HOH A O     1 
HETATM 19005 O  O     . HOH DA 11 .    ? -30.583 95.948  105.285 1.00 29.62 ? 2645 HOH A O     1 
HETATM 19006 O  O     . HOH DA 11 .    ? -34.355 77.614  85.268  1.00 23.31 ? 2646 HOH A O     1 
HETATM 19007 O  O     . HOH DA 11 .    ? -27.937 60.284  125.258 1.00 41.51 ? 2647 HOH A O     1 
HETATM 19008 O  O     . HOH DA 11 .    ? -8.049  77.241  92.241  1.00 24.06 ? 2648 HOH A O     1 
HETATM 19009 O  O     . HOH DA 11 .    ? -27.674 71.036  90.169  1.00 26.94 ? 2649 HOH A O     1 
HETATM 19010 O  O     . HOH DA 11 .    ? -48.526 61.633  57.013  1.00 24.72 ? 2650 HOH A O     1 
HETATM 19011 O  O     . HOH DA 11 .    ? 5.250   55.133  97.088  1.00 27.49 ? 2651 HOH A O     1 
HETATM 19012 O  O     . HOH DA 11 .    ? -20.708 81.415  116.219 1.00 22.63 ? 2652 HOH A O     1 
HETATM 19013 O  O     . HOH DA 11 .    ? -64.696 45.181  82.905  1.00 38.11 ? 2653 HOH A O     1 
HETATM 19014 O  O     . HOH DA 11 .    ? -31.062 41.341  98.616  1.00 37.34 ? 2654 HOH A O     1 
HETATM 19015 O  O     . HOH DA 11 .    ? -15.500 92.923  131.655 1.00 43.31 ? 2655 HOH A O     1 
HETATM 19016 O  O     . HOH DA 11 .    ? -42.526 66.085  63.784  1.00 33.55 ? 2656 HOH A O     1 
HETATM 19017 O  O     . HOH DA 11 .    ? 25.749  64.277  103.011 1.00 31.60 ? 2657 HOH A O     1 
HETATM 19018 O  O     . HOH DA 11 .    ? -38.009 36.432  82.839  1.00 35.39 ? 2658 HOH A O     1 
HETATM 19019 O  O     . HOH DA 11 .    ? -58.171 45.707  92.103  1.00 41.55 ? 2659 HOH A O     1 
HETATM 19020 O  O     . HOH DA 11 .    ? -53.316 39.650  66.215  1.00 39.14 ? 2660 HOH A O     1 
HETATM 19021 O  O     . HOH DA 11 .    ? -44.566 61.052  85.730  1.00 19.24 ? 2661 HOH A O     1 
HETATM 19022 O  O     . HOH DA 11 .    ? -42.416 77.870  76.124  1.00 29.40 ? 2662 HOH A O     1 
HETATM 19023 O  O     . HOH DA 11 .    ? -48.412 78.291  75.215  1.00 32.26 ? 2663 HOH A O     1 
HETATM 19024 O  O     . HOH DA 11 .    ? -9.449  91.721  118.184 1.00 30.80 ? 2664 HOH A O     1 
HETATM 19025 O  O     . HOH DA 11 .    ? -35.148 63.264  116.336 1.00 37.61 ? 2665 HOH A O     1 
HETATM 19026 O  O     . HOH DA 11 .    ? -26.814 51.900  98.949  1.00 22.79 ? 2666 HOH A O     1 
HETATM 19027 O  O     . HOH DA 11 .    ? -34.076 90.592  122.636 1.00 30.90 ? 2667 HOH A O     1 
HETATM 19028 O  O     . HOH DA 11 .    ? -6.584  53.782  100.350 1.00 41.36 ? 2668 HOH A O     1 
HETATM 19029 O  O     . HOH DA 11 .    ? -66.117 61.493  75.878  1.00 20.19 ? 2669 HOH A O     1 
HETATM 19030 O  O     . HOH DA 11 .    ? -25.683 94.173  78.460  1.00 29.75 ? 2670 HOH A O     1 
HETATM 19031 O  O     . HOH DA 11 .    ? -12.578 65.946  112.994 1.00 20.34 ? 2671 HOH A O     1 
HETATM 19032 O  O     . HOH DA 11 .    ? -49.917 27.261  77.541  1.00 36.05 ? 2672 HOH A O     1 
HETATM 19033 O  O     . HOH DA 11 .    ? -45.068 65.402  53.162  1.00 37.36 ? 2673 HOH A O     1 
HETATM 19034 O  O     . HOH DA 11 .    ? -42.538 77.635  78.594  1.00 26.78 ? 2674 HOH A O     1 
HETATM 19035 O  O     . HOH DA 11 .    ? -15.864 68.169  96.906  1.00 17.55 ? 2675 HOH A O     1 
HETATM 19036 O  O     . HOH DA 11 .    ? -36.602 69.251  119.543 1.00 31.86 ? 2676 HOH A O     1 
HETATM 19037 O  O     . HOH DA 11 .    ? -27.906 61.162  84.642  1.00 36.28 ? 2677 HOH A O     1 
HETATM 19038 O  O     . HOH DA 11 .    ? 9.634   68.003  94.252  1.00 36.09 ? 2678 HOH A O     1 
HETATM 19039 O  O     . HOH DA 11 .    ? 12.385  65.243  119.060 1.00 33.88 ? 2679 HOH A O     1 
HETATM 19040 O  O     . HOH DA 11 .    ? -19.315 91.091  77.115  1.00 28.94 ? 2680 HOH A O     1 
HETATM 19041 O  O     . HOH DA 11 .    ? 2.632   84.022  101.955 1.00 24.47 ? 2681 HOH A O     1 
HETATM 19042 O  O     . HOH DA 11 .    ? -19.831 89.032  75.235  1.00 31.63 ? 2682 HOH A O     1 
HETATM 19043 O  O     . HOH DA 11 .    ? 22.822  76.053  115.191 1.00 29.78 ? 2683 HOH A O     1 
HETATM 19044 O  O     . HOH DA 11 .    ? -44.984 57.500  102.414 1.00 29.33 ? 2684 HOH A O     1 
HETATM 19045 O  O     . HOH DA 11 .    ? 10.403  81.280  125.636 1.00 34.39 ? 2685 HOH A O     1 
HETATM 19046 O  O     . HOH DA 11 .    ? -39.678 84.760  104.162 1.00 32.12 ? 2686 HOH A O     1 
HETATM 19047 O  O     . HOH DA 11 .    ? -47.122 22.396  77.747  1.00 53.79 ? 2687 HOH A O     1 
HETATM 19048 O  O     . HOH DA 11 .    ? -31.479 94.362  127.725 1.00 38.82 ? 2688 HOH A O     1 
HETATM 19049 O  O     . HOH DA 11 .    ? -36.340 95.185  94.253  1.00 30.50 ? 2689 HOH A O     1 
HETATM 19050 O  O     . HOH DA 11 .    ? -25.010 79.318  95.300  1.00 21.10 ? 2690 HOH A O     1 
HETATM 19051 O  O     . HOH DA 11 .    ? -6.100  70.924  106.364 1.00 31.96 ? 2691 HOH A O     1 
HETATM 19052 O  O     . HOH DA 11 .    ? -43.927 69.265  109.262 1.00 37.50 ? 2692 HOH A O     1 
HETATM 19053 O  O     . HOH DA 11 .    ? -47.393 70.613  111.481 1.00 35.94 ? 2693 HOH A O     1 
HETATM 19054 O  O     . HOH DA 11 .    ? -14.305 85.206  77.266  1.00 33.70 ? 2694 HOH A O     1 
HETATM 19055 O  O     . HOH DA 11 .    ? -45.294 63.565  105.574 1.00 43.87 ? 2695 HOH A O     1 
HETATM 19056 O  O     . HOH DA 11 .    ? -36.789 51.619  61.156  1.00 34.19 ? 2696 HOH A O     1 
HETATM 19057 O  O     . HOH DA 11 .    ? -3.197  87.852  105.044 1.00 40.82 ? 2697 HOH A O     1 
HETATM 19058 O  O     . HOH DA 11 .    ? -7.835  72.485  100.702 1.00 31.85 ? 2698 HOH A O     1 
HETATM 19059 O  O     . HOH DA 11 .    ? -35.855 37.310  83.814  1.00 33.82 ? 2699 HOH A O     1 
HETATM 19060 O  O     . HOH DA 11 .    ? -20.867 58.252  97.543  1.00 21.71 ? 2700 HOH A O     1 
HETATM 19061 O  O     . HOH DA 11 .    ? -54.900 26.475  92.033  1.00 37.57 ? 2701 HOH A O     1 
HETATM 19062 O  O     . HOH DA 11 .    ? -18.213 68.922  104.835 1.00 25.70 ? 2702 HOH A O     1 
HETATM 19063 O  O     . HOH DA 11 .    ? -32.036 44.857  103.607 1.00 42.90 ? 2703 HOH A O     1 
HETATM 19064 O  O     . HOH DA 11 .    ? -26.408 84.469  74.236  1.00 33.17 ? 2704 HOH A O     1 
HETATM 19065 O  O     . HOH DA 11 .    ? -46.156 31.941  70.774  1.00 37.92 ? 2705 HOH A O     1 
HETATM 19066 O  O     . HOH DA 11 .    ? -31.950 52.385  86.271  1.00 30.74 ? 2706 HOH A O     1 
HETATM 19067 O  O     . HOH DA 11 .    ? -30.715 66.300  127.051 1.00 39.32 ? 2707 HOH A O     1 
HETATM 19068 O  O     . HOH DA 11 .    ? -35.377 66.316  94.845  1.00 43.78 ? 2708 HOH A O     1 
HETATM 19069 O  O     . HOH DA 11 .    ? -3.225  82.332  97.673  1.00 29.44 ? 2709 HOH A O     1 
HETATM 19070 O  O     . HOH DA 11 .    ? -23.334 86.674  73.866  1.00 33.64 ? 2710 HOH A O     1 
HETATM 19071 O  O     . HOH DA 11 .    ? -39.508 88.745  119.610 1.00 35.08 ? 2711 HOH A O     1 
HETATM 19072 O  O     . HOH DA 11 .    ? -58.920 58.371  77.060  1.00 19.49 ? 2712 HOH A O     1 
HETATM 19073 O  O     . HOH DA 11 .    ? -53.310 49.330  60.419  1.00 29.76 ? 2713 HOH A O     1 
HETATM 19074 O  O     . HOH DA 11 .    ? -1.779  77.911  105.522 1.00 23.98 ? 2714 HOH A O     1 
HETATM 19075 O  O     . HOH DA 11 .    ? -28.204 69.462  86.096  1.00 31.47 ? 2715 HOH A O     1 
HETATM 19076 O  O     . HOH DA 11 .    ? -31.103 91.509  80.753  1.00 28.92 ? 2716 HOH A O     1 
HETATM 19077 O  O     . HOH DA 11 .    ? -50.065 56.863  71.909  1.00 28.09 ? 2717 HOH A O     1 
HETATM 19078 O  O     . HOH DA 11 .    ? -25.401 88.569  116.539 1.00 25.41 ? 2718 HOH A O     1 
HETATM 19079 O  O     . HOH DA 11 .    ? -65.097 54.384  91.001  1.00 35.07 ? 2719 HOH A O     1 
HETATM 19080 O  O     . HOH DA 11 .    ? -28.771 54.825  111.833 1.00 38.49 ? 2720 HOH A O     1 
HETATM 19081 O  O     . HOH DA 11 .    ? -22.551 98.637  100.578 1.00 35.91 ? 2721 HOH A O     1 
HETATM 19082 O  O     . HOH DA 11 .    ? -19.635 76.649  67.364  1.00 38.84 ? 2722 HOH A O     1 
HETATM 19083 O  O     . HOH DA 11 .    ? 2.681   64.753  113.327 1.00 30.69 ? 2723 HOH A O     1 
HETATM 19084 O  O     . HOH DA 11 .    ? -33.171 92.337  107.219 1.00 38.05 ? 2724 HOH A O     1 
HETATM 19085 O  O     . HOH DA 11 .    ? -45.311 89.498  109.724 1.00 46.18 ? 2725 HOH A O     1 
HETATM 19086 O  O     . HOH DA 11 .    ? 9.023   64.953  94.601  1.00 32.27 ? 2726 HOH A O     1 
HETATM 19087 O  O     . HOH DA 11 .    ? -12.636 53.660  110.698 1.00 39.48 ? 2727 HOH A O     1 
HETATM 19088 O  O     . HOH DA 11 .    ? -32.260 64.546  122.272 1.00 31.66 ? 2728 HOH A O     1 
HETATM 19089 O  O     . HOH DA 11 .    ? -49.412 35.339  88.006  1.00 35.11 ? 2729 HOH A O     1 
HETATM 19090 O  O     . HOH DA 11 .    ? -7.359  50.886  53.203  1.00 30.79 ? 2730 HOH A O     1 
HETATM 19091 O  O     . HOH DA 11 .    ? -8.374  82.028  105.197 1.00 27.34 ? 2731 HOH A O     1 
HETATM 19092 O  O     . HOH DA 11 .    ? 20.771  75.562  100.589 1.00 39.97 ? 2732 HOH A O     1 
HETATM 19093 O  O     . HOH DA 11 .    ? -19.903 52.267  78.513  1.00 31.07 ? 2733 HOH A O     1 
HETATM 19094 O  O     A HOH DA 11 .    ? 5.935   58.452  97.563  0.65 27.42 ? 2734 HOH A O     1 
HETATM 19095 O  O     . HOH DA 11 .    ? -48.047 56.803  56.198  1.00 33.90 ? 2735 HOH A O     1 
HETATM 19096 O  O     . HOH DA 11 .    ? -33.578 83.789  123.663 1.00 32.52 ? 2736 HOH A O     1 
HETATM 19097 O  O     . HOH DA 11 .    ? -17.065 55.068  78.647  1.00 38.31 ? 2737 HOH A O     1 
HETATM 19098 O  O     . HOH DA 11 .    ? -41.656 88.862  97.118  1.00 27.52 ? 2738 HOH A O     1 
HETATM 19099 O  O     . HOH DA 11 .    ? -62.366 67.560  66.595  1.00 29.90 ? 2739 HOH A O     1 
HETATM 19100 O  O     . HOH DA 11 .    ? -12.170 64.177  129.966 1.00 32.40 ? 2740 HOH A O     1 
HETATM 19101 O  O     . HOH DA 11 .    ? 13.770  86.693  121.069 1.00 37.79 ? 2741 HOH A O     1 
HETATM 19102 O  O     . HOH DA 11 .    ? -35.524 43.519  79.622  1.00 30.60 ? 2742 HOH A O     1 
HETATM 19103 O  O     . HOH DA 11 .    ? -53.555 68.727  93.610  1.00 26.88 ? 2743 HOH A O     1 
HETATM 19104 O  O     . HOH DA 11 .    ? -31.785 82.415  110.109 1.00 36.38 ? 2744 HOH A O     1 
HETATM 19105 O  O     . HOH DA 11 .    ? -3.928  76.322  124.774 1.00 30.22 ? 2745 HOH A O     1 
HETATM 19106 O  O     . HOH DA 11 .    ? -37.793 75.554  98.379  1.00 36.57 ? 2746 HOH A O     1 
HETATM 19107 O  O     . HOH DA 11 .    ? -21.763 89.012  109.411 1.00 37.92 ? 2747 HOH A O     1 
HETATM 19108 O  O     . HOH DA 11 .    ? -59.359 62.887  77.776  1.00 24.06 ? 2748 HOH A O     1 
HETATM 19109 O  O     . HOH DA 11 .    ? -13.840 41.974  71.316  1.00 31.87 ? 2749 HOH A O     1 
HETATM 19110 O  O     . HOH DA 11 .    ? -53.122 37.136  61.437  1.00 50.75 ? 2750 HOH A O     1 
HETATM 19111 O  O     . HOH DA 11 .    ? -16.074 53.822  100.847 1.00 35.66 ? 2751 HOH A O     1 
HETATM 19112 O  O     . HOH DA 11 .    ? -1.518  80.222  88.422  1.00 38.54 ? 2752 HOH A O     1 
HETATM 19113 O  O     . HOH DA 11 .    ? -36.983 88.299  83.377  1.00 36.90 ? 2753 HOH A O     1 
HETATM 19114 O  O     . HOH DA 11 .    ? -26.948 80.051  70.286  1.00 42.65 ? 2754 HOH A O     1 
HETATM 19115 O  O     . HOH DA 11 .    ? 18.769  62.104  94.799  1.00 35.57 ? 2755 HOH A O     1 
HETATM 19116 O  O     . HOH DA 11 .    ? -24.717 69.343  74.701  1.00 32.97 ? 2756 HOH A O     1 
HETATM 19117 O  O     . HOH DA 11 .    ? 21.709  72.760  116.241 1.00 30.54 ? 2757 HOH A O     1 
HETATM 19118 O  O     . HOH DA 11 .    ? -53.309 72.228  68.296  1.00 26.97 ? 2758 HOH A O     1 
HETATM 19119 O  O     . HOH DA 11 .    ? -0.213  67.881  117.894 1.00 32.45 ? 2759 HOH A O     1 
HETATM 19120 O  O     . HOH DA 11 .    ? -55.785 36.776  92.928  1.00 43.02 ? 2760 HOH A O     1 
HETATM 19121 O  O     . HOH DA 11 .    ? -56.448 73.515  96.661  1.00 35.75 ? 2761 HOH A O     1 
HETATM 19122 O  O     . HOH DA 11 .    ? -22.268 76.961  70.396  1.00 25.77 ? 2762 HOH A O     1 
HETATM 19123 O  O     . HOH DA 11 .    ? -37.936 67.660  98.392  1.00 28.96 ? 2763 HOH A O     1 
HETATM 19124 O  O     . HOH DA 11 .    ? -10.205 64.253  125.424 1.00 41.32 ? 2764 HOH A O     1 
HETATM 19125 O  O     . HOH DA 11 .    ? -4.421  50.966  56.812  1.00 39.62 ? 2765 HOH A O     1 
HETATM 19126 O  O     . HOH DA 11 .    ? -4.148  73.014  77.289  1.00 31.48 ? 2766 HOH A O     1 
HETATM 19127 O  O     . HOH DA 11 .    ? -54.099 79.403  81.725  1.00 37.05 ? 2767 HOH A O     1 
HETATM 19128 O  O     . HOH DA 11 .    ? -25.281 59.317  114.723 1.00 26.35 ? 2768 HOH A O     1 
HETATM 19129 O  O     . HOH DA 11 .    ? -4.927  55.717  101.301 1.00 32.96 ? 2769 HOH A O     1 
HETATM 19130 O  O     . HOH DA 11 .    ? -25.796 69.965  95.957  1.00 31.52 ? 2770 HOH A O     1 
HETATM 19131 O  O     . HOH DA 11 .    ? -36.701 49.838  100.923 1.00 30.68 ? 2771 HOH A O     1 
HETATM 19132 O  O     . HOH DA 11 .    ? -38.346 70.470  82.078  1.00 28.10 ? 2772 HOH A O     1 
HETATM 19133 O  O     . HOH DA 11 .    ? 2.751   77.898  98.389  1.00 25.83 ? 2773 HOH A O     1 
HETATM 19134 O  O     . HOH DA 11 .    ? -59.481 38.351  82.981  1.00 38.99 ? 2774 HOH A O     1 
HETATM 19135 O  O     . HOH DA 11 .    ? -30.342 86.635  102.435 1.00 26.54 ? 2775 HOH A O     1 
HETATM 19136 O  O     . HOH DA 11 .    ? -5.284  67.935  78.026  1.00 33.95 ? 2776 HOH A O     1 
HETATM 19137 O  O     . HOH DA 11 .    ? -11.528 53.489  103.143 1.00 45.14 ? 2777 HOH A O     1 
HETATM 19138 O  O     . HOH DA 11 .    ? -48.730 29.403  74.137  1.00 41.90 ? 2778 HOH A O     1 
HETATM 19139 O  O     . HOH DA 11 .    ? -42.069 56.756  89.669  1.00 19.19 ? 2779 HOH A O     1 
HETATM 19140 O  O     . HOH DA 11 .    ? -27.330 62.047  89.249  1.00 23.08 ? 2780 HOH A O     1 
HETATM 19141 O  O     . HOH DA 11 .    ? -56.988 53.462  96.408  1.00 25.58 ? 2781 HOH A O     1 
HETATM 19142 O  O     . HOH DA 11 .    ? 2.387   76.354  117.226 1.00 27.31 ? 2782 HOH A O     1 
HETATM 19143 O  O     . HOH DA 11 .    ? -25.456 68.159  90.996  1.00 27.63 ? 2783 HOH A O     1 
HETATM 19144 O  O     . HOH DA 11 .    ? -35.205 97.918  116.389 1.00 38.86 ? 2784 HOH A O     1 
HETATM 19145 O  O     . HOH DA 11 .    ? -49.732 72.989  63.128  1.00 24.38 ? 2785 HOH A O     1 
HETATM 19146 O  O     . HOH DA 11 .    ? -31.397 38.620  99.655  1.00 49.50 ? 2786 HOH A O     1 
HETATM 19147 O  O     . HOH DA 11 .    ? 8.706   90.606  103.697 1.00 44.35 ? 2787 HOH A O     1 
HETATM 19148 O  O     . HOH DA 11 .    ? -40.183 64.704  62.624  1.00 33.67 ? 2788 HOH A O     1 
HETATM 19149 O  O     . HOH DA 11 .    ? -23.222 78.539  135.134 1.00 40.66 ? 2789 HOH A O     1 
HETATM 19150 O  O     . HOH DA 11 .    ? -10.628 91.606  114.717 1.00 41.10 ? 2790 HOH A O     1 
HETATM 19151 O  O     . HOH DA 11 .    ? -42.820 49.816  56.020  1.00 36.79 ? 2791 HOH A O     1 
HETATM 19152 O  O     . HOH DA 11 .    ? -20.009 69.189  70.917  1.00 47.06 ? 2792 HOH A O     1 
HETATM 19153 O  O     . HOH DA 11 .    ? -28.574 32.946  75.378  1.00 45.12 ? 2793 HOH A O     1 
HETATM 19154 O  O     . HOH DA 11 .    ? -13.006 69.137  74.109  1.00 36.47 ? 2794 HOH A O     1 
HETATM 19155 O  O     . HOH DA 11 .    ? -13.492 54.210  77.470  1.00 28.76 ? 2795 HOH A O     1 
HETATM 19156 O  O     . HOH DA 11 .    ? -27.989 88.232  74.932  1.00 42.97 ? 2796 HOH A O     1 
HETATM 19157 O  O     . HOH DA 11 .    ? -1.467  80.368  112.202 1.00 29.18 ? 2797 HOH A O     1 
HETATM 19158 O  O     . HOH DA 11 .    ? -43.961 31.002  69.561  1.00 40.17 ? 2798 HOH A O     1 
HETATM 19159 O  O     . HOH DA 11 .    ? 22.996  72.857  98.737  1.00 37.47 ? 2799 HOH A O     1 
HETATM 19160 O  O     . HOH DA 11 .    ? -38.559 71.159  84.558  1.00 29.33 ? 2800 HOH A O     1 
HETATM 19161 O  O     . HOH DA 11 .    ? -23.346 101.331 84.479  1.00 43.47 ? 2801 HOH A O     1 
HETATM 19162 O  O     . HOH DA 11 .    ? -28.686 95.106  89.397  1.00 31.67 ? 2802 HOH A O     1 
HETATM 19163 O  O     . HOH DA 11 .    ? -21.821 52.757  104.558 1.00 37.07 ? 2803 HOH A O     1 
HETATM 19164 O  O     . HOH DA 11 .    ? -30.964 83.907  123.703 1.00 26.28 ? 2804 HOH A O     1 
HETATM 19165 O  O     . HOH DA 11 .    ? -12.396 81.819  72.874  1.00 39.96 ? 2805 HOH A O     1 
HETATM 19166 O  O     . HOH DA 11 .    ? -22.229 54.627  97.539  1.00 32.98 ? 2806 HOH A O     1 
HETATM 19167 O  O     . HOH DA 11 .    ? -34.200 56.486  105.663 1.00 27.01 ? 2807 HOH A O     1 
HETATM 19168 O  O     . HOH DA 11 .    ? -19.900 79.054  115.199 1.00 21.43 ? 2808 HOH A O     1 
HETATM 19169 O  O     . HOH DA 11 .    ? -28.068 64.866  64.470  1.00 40.78 ? 2809 HOH A O     1 
HETATM 19170 O  O     . HOH DA 11 .    ? -43.765 59.417  87.739  1.00 18.22 ? 2810 HOH A O     1 
HETATM 19171 O  O     . HOH DA 11 .    ? -41.597 29.457  89.691  1.00 40.28 ? 2811 HOH A O     1 
HETATM 19172 O  O     . HOH DA 11 .    ? 4.644   85.986  101.218 1.00 28.40 ? 2812 HOH A O     1 
HETATM 19173 O  O     . HOH DA 11 .    ? -1.841  90.908  105.860 1.00 34.58 ? 2813 HOH A O     1 
HETATM 19174 O  O     . HOH DA 11 .    ? -3.477  56.250  95.935  1.00 41.99 ? 2814 HOH A O     1 
HETATM 19175 O  O     . HOH DA 11 .    ? -27.241 90.509  116.129 1.00 28.31 ? 2815 HOH A O     1 
HETATM 19176 O  O     . HOH DA 11 .    ? -30.506 50.227  105.027 1.00 30.02 ? 2816 HOH A O     1 
HETATM 19177 O  O     . HOH DA 11 .    ? 24.996  58.283  110.063 1.00 45.55 ? 2817 HOH A O     1 
HETATM 19178 O  O     . HOH DA 11 .    ? -22.685 53.835  92.902  1.00 31.74 ? 2818 HOH A O     1 
HETATM 19179 O  O     . HOH DA 11 .    ? -46.014 65.039  107.437 1.00 42.86 ? 2819 HOH A O     1 
HETATM 19180 O  O     . HOH DA 11 .    ? -36.192 80.786  76.038  1.00 27.64 ? 2820 HOH A O     1 
HETATM 19181 O  O     . HOH DA 11 .    ? -10.690 87.193  91.745  1.00 36.67 ? 2821 HOH A O     1 
HETATM 19182 O  O     . HOH DA 11 .    ? -54.021 45.056  92.222  1.00 36.31 ? 2822 HOH A O     1 
HETATM 19183 O  O     . HOH DA 11 .    ? -45.922 24.166  82.895  1.00 40.54 ? 2823 HOH A O     1 
HETATM 19184 O  O     . HOH DA 11 .    ? -44.169 91.631  111.603 1.00 37.56 ? 2824 HOH A O     1 
HETATM 19185 O  O     . HOH DA 11 .    ? -24.906 82.900  72.822  1.00 32.64 ? 2825 HOH A O     1 
HETATM 19186 O  O     . HOH DA 11 .    ? -16.893 54.768  117.413 1.00 40.93 ? 2826 HOH A O     1 
HETATM 19187 O  O     . HOH DA 11 .    ? -61.866 68.102  89.543  1.00 44.55 ? 2827 HOH A O     1 
HETATM 19188 O  O     . HOH DA 11 .    ? 18.620  75.358  96.989  1.00 37.09 ? 2828 HOH A O     1 
HETATM 19189 O  O     . HOH DA 11 .    ? -41.553 88.649  94.142  1.00 33.89 ? 2829 HOH A O     1 
HETATM 19190 O  O     . HOH DA 11 .    ? -11.094 54.055  100.618 1.00 27.54 ? 2830 HOH A O     1 
HETATM 19191 O  O     . HOH DA 11 .    ? -54.065 76.323  94.470  1.00 44.24 ? 2831 HOH A O     1 
HETATM 19192 O  O     . HOH DA 11 .    ? -7.963  75.201  70.518  1.00 33.93 ? 2832 HOH A O     1 
HETATM 19193 O  O     . HOH DA 11 .    ? -32.479 92.498  110.600 1.00 35.38 ? 2833 HOH A O     1 
HETATM 19194 O  O     . HOH DA 11 .    ? -63.246 44.886  68.077  1.00 40.12 ? 2834 HOH A O     1 
HETATM 19195 O  O     . HOH DA 11 .    ? -42.530 28.663  86.802  1.00 39.53 ? 2835 HOH A O     1 
HETATM 19196 O  O     . HOH DA 11 .    ? 1.409   57.230  107.894 1.00 20.87 ? 2836 HOH A O     1 
HETATM 19197 O  O     . HOH DA 11 .    ? -25.340 89.977  133.644 1.00 49.50 ? 2837 HOH A O     1 
HETATM 19198 O  O     . HOH DA 11 .    ? 1.345   66.322  96.767  1.00 23.74 ? 2838 HOH A O     1 
HETATM 19199 O  O     . HOH DA 11 .    ? -37.301 66.157  109.795 1.00 37.56 ? 2839 HOH A O     1 
HETATM 19200 O  O     . HOH DA 11 .    ? -58.879 42.417  89.635  1.00 34.69 ? 2840 HOH A O     1 
HETATM 19201 O  O     . HOH DA 11 .    ? 16.331  65.064  120.145 1.00 29.87 ? 2841 HOH A O     1 
HETATM 19202 O  O     . HOH DA 11 .    ? -64.321 70.872  83.425  1.00 40.09 ? 2842 HOH A O     1 
HETATM 19203 O  O     . HOH DA 11 .    ? -38.950 78.641  70.076  1.00 33.37 ? 2843 HOH A O     1 
HETATM 19204 O  O     . HOH DA 11 .    ? -17.726 85.688  77.624  1.00 26.22 ? 2844 HOH A O     1 
HETATM 19205 O  O     . HOH DA 11 .    ? -14.736 59.127  126.838 1.00 30.20 ? 2845 HOH A O     1 
HETATM 19206 O  O     . HOH DA 11 .    ? -36.555 76.734  95.633  1.00 33.76 ? 2846 HOH A O     1 
HETATM 19207 O  O     . HOH DA 11 .    ? -32.665 77.987  93.228  1.00 37.31 ? 2847 HOH A O     1 
HETATM 19208 O  O     . HOH DA 11 .    ? -64.071 58.062  67.370  1.00 40.38 ? 2848 HOH A O     1 
HETATM 19209 O  O     . HOH DA 11 .    ? -1.163  70.090  116.602 1.00 26.21 ? 2849 HOH A O     1 
HETATM 19210 O  O     . HOH DA 11 .    ? -65.621 72.493  72.111  1.00 43.42 ? 2850 HOH A O     1 
HETATM 19211 O  O     . HOH DA 11 .    ? 11.087  61.021  115.527 1.00 33.54 ? 2851 HOH A O     1 
HETATM 19212 O  O     . HOH DA 11 .    ? 15.065  76.068  94.325  1.00 43.48 ? 2852 HOH A O     1 
HETATM 19213 O  O     . HOH DA 11 .    ? -33.019 84.073  128.270 1.00 41.18 ? 2853 HOH A O     1 
HETATM 19214 O  O     . HOH DA 11 .    ? -1.468  95.961  117.800 1.00 44.22 ? 2854 HOH A O     1 
HETATM 19215 O  O     . HOH DA 11 .    ? -21.388 59.269  122.617 1.00 29.53 ? 2855 HOH A O     1 
HETATM 19216 O  O     . HOH DA 11 .    ? -45.437 54.952  92.331  1.00 18.10 ? 2856 HOH A O     1 
HETATM 19217 O  O     . HOH DA 11 .    ? -43.634 90.582  100.392 1.00 32.16 ? 2857 HOH A O     1 
HETATM 19218 O  O     . HOH DA 11 .    ? -54.922 41.822  97.025  1.00 35.59 ? 2858 HOH A O     1 
HETATM 19219 O  O     . HOH DA 11 .    ? -37.599 39.597  100.306 1.00 43.14 ? 2859 HOH A O     1 
HETATM 19220 O  O     . HOH DA 11 .    ? -38.889 66.733  94.686  1.00 31.01 ? 2860 HOH A O     1 
HETATM 19221 O  O     . HOH DA 11 .    ? -52.139 87.179  104.103 1.00 47.34 ? 2861 HOH A O     1 
HETATM 19222 O  O     . HOH DA 11 .    ? -14.777 53.182  75.896  1.00 35.40 ? 2862 HOH A O     1 
HETATM 19223 O  O     . HOH DA 11 .    ? 2.463   86.433  126.443 1.00 43.91 ? 2863 HOH A O     1 
HETATM 19224 O  O     . HOH DA 11 .    ? 21.460  71.219  95.476  1.00 42.22 ? 2864 HOH A O     1 
HETATM 19225 O  O     . HOH DA 11 .    ? -5.397  90.590  120.363 1.00 39.42 ? 2865 HOH A O     1 
HETATM 19226 O  O     . HOH DA 11 .    ? -52.792 66.382  102.239 1.00 34.79 ? 2866 HOH A O     1 
HETATM 19227 O  O     . HOH DA 11 .    ? -51.260 79.612  78.973  1.00 39.60 ? 2867 HOH A O     1 
HETATM 19228 O  O     . HOH DA 11 .    ? -46.851 77.226  92.334  1.00 27.04 ? 2868 HOH A O     1 
HETATM 19229 O  O     . HOH DA 11 .    ? -33.169 53.184  109.211 1.00 43.00 ? 2869 HOH A O     1 
HETATM 19230 O  O     . HOH DA 11 .    ? 7.197   55.194  99.058  1.00 21.59 ? 2870 HOH A O     1 
HETATM 19231 O  O     . HOH DA 11 .    ? -47.881 53.672  104.752 1.00 44.07 ? 2871 HOH A O     1 
HETATM 19232 O  O     . HOH DA 11 .    ? -8.816  51.834  107.720 1.00 34.04 ? 2872 HOH A O     1 
HETATM 19233 O  O     . HOH DA 11 .    ? -2.797  76.027  77.559  1.00 23.56 ? 2873 HOH A O     1 
HETATM 19234 O  O     . HOH DA 11 .    ? -66.083 68.773  84.186  1.00 34.06 ? 2874 HOH A O     1 
HETATM 19235 O  O     . HOH DA 11 .    ? -14.877 55.439  51.206  1.00 43.62 ? 2875 HOH A O     1 
HETATM 19236 O  O     . HOH DA 11 .    ? 11.167  85.044  124.998 1.00 32.35 ? 2876 HOH A O     1 
HETATM 19237 O  O     . HOH DA 11 .    ? -39.537 39.318  98.898  1.00 40.41 ? 2877 HOH A O     1 
HETATM 19238 O  O     . HOH DA 11 .    ? 8.076   89.007  127.307 1.00 38.31 ? 2878 HOH A O     1 
HETATM 19239 O  O     . HOH DA 11 .    ? -40.752 70.420  93.130  1.00 30.20 ? 2879 HOH A O     1 
HETATM 19240 O  O     . HOH DA 11 .    ? -29.412 73.320  96.337  1.00 39.21 ? 2880 HOH A O     1 
HETATM 19241 O  O     . HOH DA 11 .    ? -3.513  82.350  110.247 1.00 35.13 ? 2881 HOH A O     1 
HETATM 19242 O  O     . HOH DA 11 .    ? -11.266 43.556  74.340  1.00 30.30 ? 2882 HOH A O     1 
HETATM 19243 O  O     . HOH DA 11 .    ? -16.204 43.260  72.124  1.00 39.97 ? 2883 HOH A O     1 
HETATM 19244 O  O     . HOH DA 11 .    ? 13.095  88.740  116.581 1.00 35.94 ? 2884 HOH A O     1 
HETATM 19245 O  O     . HOH DA 11 .    ? -47.702 80.080  96.089  1.00 37.35 ? 2885 HOH A O     1 
HETATM 19246 O  O     . HOH DA 11 .    ? -14.002 95.615  120.373 1.00 40.48 ? 2886 HOH A O     1 
HETATM 19247 O  O     . HOH DA 11 .    ? -9.237  60.517  84.585  1.00 26.74 ? 2887 HOH A O     1 
HETATM 19248 O  O     . HOH DA 11 .    ? -32.937 57.420  72.850  1.00 41.14 ? 2888 HOH A O     1 
HETATM 19249 O  O     . HOH DA 11 .    ? -56.145 68.825  100.286 1.00 37.66 ? 2889 HOH A O     1 
HETATM 19250 O  O     . HOH DA 11 .    ? -18.848 59.751  108.564 1.00 36.79 ? 2890 HOH A O     1 
HETATM 19251 O  O     . HOH DA 11 .    ? -1.578  54.428  101.922 1.00 27.42 ? 2891 HOH A O     1 
HETATM 19252 O  O     . HOH DA 11 .    ? -67.500 64.241  85.527  1.00 33.53 ? 2892 HOH A O     1 
HETATM 19253 O  O     . HOH DA 11 .    ? -13.784 86.477  101.100 1.00 35.38 ? 2893 HOH A O     1 
HETATM 19254 O  O     . HOH DA 11 .    ? -1.615  83.476  115.736 1.00 34.04 ? 2894 HOH A O     1 
HETATM 19255 O  O     . HOH DA 11 .    ? -22.829 94.776  118.763 1.00 42.91 ? 2895 HOH A O     1 
HETATM 19256 O  O     . HOH DA 11 .    ? 0.486   64.217  107.494 1.00 20.47 ? 2896 HOH A O     1 
HETATM 19257 O  O     . HOH DA 11 .    ? -39.421 86.389  89.512  1.00 30.29 ? 2897 HOH A O     1 
HETATM 19258 O  O     . HOH DA 11 .    ? -10.853 66.671  127.661 1.00 37.32 ? 2898 HOH A O     1 
HETATM 19259 O  O     . HOH DA 11 .    ? -61.892 67.199  60.898  1.00 39.64 ? 2899 HOH A O     1 
HETATM 19260 O  O     . HOH DA 11 .    ? 0.057   79.389  95.346  1.00 48.56 ? 2900 HOH A O     1 
HETATM 19261 O  O     . HOH DA 11 .    ? -49.337 54.296  74.168  1.00 21.97 ? 2901 HOH A O     1 
HETATM 19262 O  O     . HOH DA 11 .    ? -61.835 59.903  96.073  1.00 28.72 ? 2902 HOH A O     1 
HETATM 19263 O  O     . HOH DA 11 .    ? -30.858 59.619  60.619  1.00 40.95 ? 2903 HOH A O     1 
HETATM 19264 O  O     . HOH DA 11 .    ? -28.133 42.078  93.150  1.00 48.42 ? 2904 HOH A O     1 
HETATM 19265 O  O     . HOH DA 11 .    ? 2.840   74.323  109.648 1.00 26.84 ? 2905 HOH A O     1 
HETATM 19266 O  O     . HOH DA 11 .    ? -25.919 58.614  53.482  1.00 50.98 ? 2906 HOH A O     1 
HETATM 19267 O  O     . HOH DA 11 .    ? -42.872 56.314  92.264  1.00 19.28 ? 2907 HOH A O     1 
HETATM 19268 O  O     . HOH DA 11 .    ? 10.946  64.803  114.871 1.00 36.37 ? 2908 HOH A O     1 
HETATM 19269 O  O     . HOH DA 11 .    ? -26.978 72.879  101.169 1.00 32.12 ? 2909 HOH A O     1 
HETATM 19270 O  O     . HOH DA 11 .    ? -10.254 63.775  115.829 1.00 22.78 ? 2910 HOH A O     1 
HETATM 19271 O  O     . HOH DA 11 .    ? -37.354 86.165  102.193 1.00 28.50 ? 2911 HOH A O     1 
HETATM 19272 O  O     . HOH DA 11 .    ? -64.198 47.665  76.453  1.00 42.19 ? 2912 HOH A O     1 
HETATM 19273 O  O     . HOH DA 11 .    ? -48.763 65.390  54.372  1.00 32.75 ? 2913 HOH A O     1 
HETATM 19274 O  O     . HOH DA 11 .    ? -26.812 62.881  86.671  1.00 24.50 ? 2914 HOH A O     1 
HETATM 19275 O  O     . HOH DA 11 .    ? -52.936 79.166  100.172 1.00 45.77 ? 2915 HOH A O     1 
HETATM 19276 O  O     . HOH DA 11 .    ? -36.296 71.253  121.525 1.00 34.04 ? 2916 HOH A O     1 
HETATM 19277 O  O     . HOH DA 11 .    ? -37.675 40.309  74.526  1.00 34.69 ? 2917 HOH A O     1 
HETATM 19278 O  O     . HOH DA 11 .    ? -5.671  79.357  71.061  1.00 47.19 ? 2918 HOH A O     1 
HETATM 19279 O  O     . HOH DA 11 .    ? -64.570 55.137  80.876  1.00 29.78 ? 2919 HOH A O     1 
HETATM 19280 O  O     . HOH DA 11 .    ? -36.510 38.206  102.923 1.00 42.67 ? 2920 HOH A O     1 
HETATM 19281 O  O     . HOH DA 11 .    ? -32.233 98.690  99.774  1.00 44.43 ? 2921 HOH A O     1 
HETATM 19282 O  O     . HOH DA 11 .    ? -39.422 47.107  104.140 1.00 31.70 ? 2922 HOH A O     1 
HETATM 19283 O  O     . HOH DA 11 .    ? -13.171 43.496  76.727  1.00 52.35 ? 2923 HOH A O     1 
HETATM 19284 O  O     . HOH DA 11 .    ? -38.065 72.847  87.867  1.00 30.64 ? 2924 HOH A O     1 
HETATM 19285 O  O     . HOH DA 11 .    ? -15.591 43.927  77.189  1.00 50.90 ? 2925 HOH A O     1 
HETATM 19286 O  O     . HOH DA 11 .    ? -56.192 40.356  67.941  1.00 41.54 ? 2926 HOH A O     1 
HETATM 19287 O  O     . HOH DA 11 .    ? 12.740  63.549  120.938 1.00 38.75 ? 2927 HOH A O     1 
HETATM 19288 O  O     . HOH DA 11 .    ? -9.060  83.952  81.181  1.00 41.60 ? 2928 HOH A O     1 
HETATM 19289 O  O     . HOH DA 11 .    ? -8.862  41.158  69.393  1.00 39.70 ? 2929 HOH A O     1 
HETATM 19290 O  O     . HOH DA 11 .    ? -20.916 50.402  108.702 1.00 41.39 ? 2930 HOH A O     1 
HETATM 19291 O  O     . HOH DA 11 .    ? -65.918 64.347  88.311  1.00 31.88 ? 2931 HOH A O     1 
HETATM 19292 O  O     . HOH DA 11 .    ? -39.731 37.848  85.431  1.00 31.88 ? 2932 HOH A O     1 
HETATM 19293 O  O     . HOH DA 11 .    ? -39.972 47.412  107.024 1.00 39.61 ? 2933 HOH A O     1 
HETATM 19294 O  O     . HOH DA 11 .    ? -0.101  67.040  86.584  1.00 40.31 ? 2934 HOH A O     1 
HETATM 19295 O  O     . HOH DA 11 .    ? -64.519 59.180  99.476  1.00 47.55 ? 2935 HOH A O     1 
HETATM 19296 O  O     . HOH DA 11 .    ? -21.307 53.073  88.966  1.00 42.87 ? 2936 HOH A O     1 
HETATM 19297 O  O     . HOH DA 11 .    ? -30.659 91.404  111.741 1.00 39.22 ? 2937 HOH A O     1 
HETATM 19298 O  O     . HOH DA 11 .    ? -28.544 57.453  88.785  1.00 33.39 ? 2938 HOH A O     1 
HETATM 19299 O  O     . HOH DA 11 .    ? 2.896   66.252  120.774 1.00 40.44 ? 2939 HOH A O     1 
HETATM 19300 O  O     . HOH DA 11 .    ? -4.537  82.366  125.492 1.00 41.59 ? 2940 HOH A O     1 
HETATM 19301 O  O     . HOH DA 11 .    ? 2.206   57.818  95.234  1.00 47.51 ? 2941 HOH A O     1 
HETATM 19302 O  O     . HOH DA 11 .    ? -44.019 76.537  74.810  1.00 34.78 ? 2942 HOH A O     1 
HETATM 19303 O  O     . HOH DA 11 .    ? -3.299  75.318  102.329 1.00 35.54 ? 2943 HOH A O     1 
HETATM 19304 O  O     . HOH DA 11 .    ? -31.247 74.562  87.820  1.00 30.79 ? 2944 HOH A O     1 
HETATM 19305 O  O     . HOH DA 11 .    ? -36.628 82.661  121.238 1.00 33.76 ? 2945 HOH A O     1 
HETATM 19306 O  O     . HOH DA 11 .    ? -14.089 58.109  110.118 1.00 35.91 ? 2946 HOH A O     1 
HETATM 19307 O  O     . HOH DA 11 .    ? -52.002 29.775  73.261  1.00 47.99 ? 2947 HOH A O     1 
HETATM 19308 O  O     . HOH DA 11 .    ? -17.024 64.898  134.745 1.00 43.96 ? 2948 HOH A O     1 
HETATM 19309 O  O     . HOH DA 11 .    ? -67.172 57.533  90.392  1.00 42.68 ? 2949 HOH A O     1 
HETATM 19310 O  O     . HOH DA 11 .    ? -20.281 54.797  99.192  1.00 30.70 ? 2950 HOH A O     1 
HETATM 19311 O  O     . HOH DA 11 .    ? 15.749  73.561  128.242 1.00 40.35 ? 2951 HOH A O     1 
HETATM 19312 O  O     . HOH DA 11 .    ? -5.663  75.118  103.448 1.00 30.64 ? 2952 HOH A O     1 
HETATM 19313 O  O     . HOH DA 11 .    ? -29.455 58.689  79.451  1.00 37.55 ? 2953 HOH A O     1 
HETATM 19314 O  O     . HOH DA 11 .    ? 0.229   65.132  117.443 1.00 39.92 ? 2954 HOH A O     1 
HETATM 19315 O  O     . HOH DA 11 .    ? -56.645 32.185  87.989  1.00 31.25 ? 2955 HOH A O     1 
HETATM 19316 O  O     . HOH DA 11 .    ? -46.151 51.820  72.284  1.00 32.37 ? 2956 HOH A O     1 
HETATM 19317 O  O     . HOH DA 11 .    ? -26.427 96.302  79.769  1.00 47.77 ? 2957 HOH A O     1 
HETATM 19318 O  O     . HOH DA 11 .    ? -34.695 75.453  126.471 1.00 37.34 ? 2958 HOH A O     1 
HETATM 19319 O  O     . HOH DA 11 .    ? -0.950  77.332  127.005 1.00 45.51 ? 2959 HOH A O     1 
HETATM 19320 O  O     . HOH DA 11 .    ? -39.264 96.967  113.824 1.00 50.77 ? 2960 HOH A O     1 
HETATM 19321 O  O     . HOH DA 11 .    ? -5.209  47.071  55.858  1.00 42.81 ? 2961 HOH A O     1 
HETATM 19322 O  O     . HOH DA 11 .    ? -18.221 92.410  107.951 1.00 45.53 ? 2962 HOH A O     1 
HETATM 19323 O  O     . HOH DA 11 .    ? 17.074  86.971  112.227 1.00 45.61 ? 2963 HOH A O     1 
HETATM 19324 O  O     . HOH DA 11 .    ? -7.156  86.085  82.815  1.00 42.03 ? 2964 HOH A O     1 
HETATM 19325 O  O     . HOH DA 11 .    ? 0.091   87.375  124.780 1.00 35.88 ? 2965 HOH A O     1 
HETATM 19326 O  O     . HOH DA 11 .    ? 14.960  82.470  119.631 1.00 31.99 ? 2966 HOH A O     1 
HETATM 19327 O  O     . HOH DA 11 .    ? -26.797 48.077  102.372 1.00 41.58 ? 2967 HOH A O     1 
HETATM 19328 O  O     . HOH DA 11 .    ? -65.510 69.167  69.210  1.00 39.25 ? 2968 HOH A O     1 
HETATM 19329 O  O     . HOH DA 11 .    ? -14.814 48.628  51.677  1.00 41.28 ? 2969 HOH A O     1 
HETATM 19330 O  O     . HOH DA 11 .    ? -0.470  52.676  59.140  1.00 37.15 ? 2970 HOH A O     1 
HETATM 19331 O  O     . HOH DA 11 .    ? -26.467 92.111  132.665 1.00 42.65 ? 2971 HOH A O     1 
HETATM 19332 O  O     . HOH DA 11 .    ? 19.322  71.306  92.518  1.00 43.42 ? 2972 HOH A O     1 
HETATM 19333 O  O     . HOH DA 11 .    ? 11.053  89.614  105.172 1.00 38.41 ? 2973 HOH A O     1 
HETATM 19334 O  O     . HOH DA 11 .    ? -23.191 75.899  133.783 1.00 33.17 ? 2974 HOH A O     1 
HETATM 19335 O  O     . HOH DA 11 .    ? -43.861 65.952  107.483 1.00 45.62 ? 2975 HOH A O     1 
HETATM 19336 O  O     . HOH DA 11 .    ? 7.882   79.584  125.842 1.00 44.58 ? 2976 HOH A O     1 
HETATM 19337 O  O     . HOH DA 11 .    ? -44.582 93.033  89.165  1.00 47.11 ? 2977 HOH A O     1 
HETATM 19338 O  O     . HOH DA 11 .    ? -42.384 85.426  105.796 1.00 39.87 ? 2978 HOH A O     1 
HETATM 19339 O  O     . HOH DA 11 .    ? -22.547 67.590  130.153 1.00 41.36 ? 2979 HOH A O     1 
HETATM 19340 O  O     . HOH DA 11 .    ? -9.906  66.808  74.733  1.00 33.24 ? 2980 HOH A O     1 
HETATM 19341 O  O     . HOH DA 11 .    ? -50.217 23.907  81.464  1.00 44.92 ? 2981 HOH A O     1 
HETATM 19342 O  O     . HOH DA 11 .    ? -30.456 59.563  81.997  1.00 43.90 ? 2982 HOH A O     1 
HETATM 19343 O  O     . HOH DA 11 .    ? -38.891 54.367  77.725  1.00 40.99 ? 2983 HOH A O     1 
HETATM 19344 O  O     . HOH DA 11 .    ? -31.173 78.251  91.106  1.00 30.98 ? 2984 HOH A O     1 
HETATM 19345 O  O     . HOH DA 11 .    ? -10.743 63.082  69.127  1.00 30.97 ? 2985 HOH A O     1 
HETATM 19346 O  O     . HOH DA 11 .    ? -50.232 54.602  105.093 1.00 43.89 ? 2986 HOH A O     1 
HETATM 19347 O  O     . HOH DA 11 .    ? -19.993 98.171  123.938 1.00 49.45 ? 2987 HOH A O     1 
HETATM 19348 O  O     . HOH DA 11 .    ? -9.026  73.156  132.016 1.00 43.79 ? 2988 HOH A O     1 
HETATM 19349 O  O     . HOH DA 11 .    ? -34.061 59.055  106.502 1.00 30.27 ? 2989 HOH A O     1 
HETATM 19350 O  O     . HOH DA 11 .    ? 19.662  64.363  93.524  1.00 36.13 ? 2990 HOH A O     1 
HETATM 19351 O  O     . HOH DA 11 .    ? -47.411 97.869  104.041 1.00 47.50 ? 2991 HOH A O     1 
HETATM 19352 O  O     . HOH DA 11 .    ? -45.775 78.425  90.263  1.00 26.14 ? 2992 HOH A O     1 
HETATM 19353 O  O     . HOH DA 11 .    ? 15.972  64.382  117.340 1.00 43.85 ? 2993 HOH A O     1 
HETATM 19354 O  O     . HOH DA 11 .    ? -60.392 59.565  62.316  1.00 35.52 ? 2994 HOH A O     1 
HETATM 19355 O  O     . HOH DA 11 .    ? -52.032 31.585  97.511  1.00 47.64 ? 2995 HOH A O     1 
HETATM 19356 O  O     . HOH DA 11 .    ? -1.631  80.022  97.542  1.00 33.24 ? 2996 HOH A O     1 
HETATM 19357 O  O     . HOH DA 11 .    ? -33.899 50.332  83.822  1.00 36.31 ? 2997 HOH A O     1 
HETATM 19358 O  O     . HOH DA 11 .    ? 1.142   69.855  87.913  1.00 39.78 ? 2998 HOH A O     1 
HETATM 19359 O  O     . HOH DA 11 .    ? -60.799 41.361  67.104  1.00 47.31 ? 2999 HOH A O     1 
HETATM 19360 O  O     . HOH DA 11 .    ? -25.728 74.576  133.212 1.00 38.00 ? 3000 HOH A O     1 
HETATM 19361 O  O     . HOH DA 11 .    ? -21.418 93.073  107.726 1.00 47.83 ? 3001 HOH A O     1 
HETATM 19362 O  O     . HOH DA 11 .    ? -19.358 92.227  105.370 1.00 48.04 ? 3002 HOH A O     1 
HETATM 19363 O  O     . HOH DA 11 .    ? -51.572 55.166  70.541  1.00 25.50 ? 3003 HOH A O     1 
HETATM 19364 O  O     . HOH DA 11 .    ? -47.391 63.914  56.283  1.00 34.28 ? 3004 HOH A O     1 
HETATM 19365 O  O     . HOH DA 11 .    ? 8.045   69.581  125.465 1.00 46.57 ? 3005 HOH A O     1 
HETATM 19366 O  O     . HOH DA 11 .    ? -27.306 51.252  109.831 1.00 38.75 ? 3006 HOH A O     1 
HETATM 19367 O  O     . HOH DA 11 .    ? -60.759 68.733  92.181  1.00 42.97 ? 3007 HOH A O     1 
HETATM 19368 O  O     . HOH DA 11 .    ? -19.019 54.616  118.626 1.00 40.74 ? 3008 HOH A O     1 
HETATM 19369 O  O     . HOH DA 11 .    ? -47.349 33.114  85.797  1.00 42.40 ? 3009 HOH A O     1 
HETATM 19370 O  O     . HOH DA 11 .    ? -41.583 75.652  121.205 1.00 48.79 ? 3010 HOH A O     1 
HETATM 19371 O  O     . HOH DA 11 .    ? -26.808 60.508  122.886 1.00 37.10 ? 3011 HOH A O     1 
HETATM 19372 O  O     . HOH DA 11 .    ? -52.354 41.517  101.780 1.00 45.39 ? 3012 HOH A O     1 
HETATM 19373 O  O     . HOH DA 11 .    ? -35.952 98.825  97.414  1.00 48.50 ? 3013 HOH A O     1 
HETATM 19374 O  O     . HOH DA 11 .    ? -59.750 64.205  92.392  1.00 31.36 ? 3014 HOH A O     1 
HETATM 19375 O  O     . HOH DA 11 .    ? -34.913 70.571  82.907  1.00 41.04 ? 3015 HOH A O     1 
HETATM 19376 O  O     . HOH DA 11 .    ? 22.708  65.080  93.434  1.00 42.47 ? 3016 HOH A O     1 
HETATM 19377 O  O     . HOH DA 11 .    ? -27.094 92.190  77.146  1.00 38.45 ? 3017 HOH A O     1 
HETATM 19378 O  O     . HOH DA 11 .    ? -48.131 27.059  75.249  1.00 44.12 ? 3018 HOH A O     1 
HETATM 19379 O  O     . HOH DA 11 .    ? -64.241 63.212  68.801  1.00 35.00 ? 3019 HOH A O     1 
HETATM 19380 O  O     . HOH DA 11 .    ? 12.607  64.306  116.827 1.00 40.56 ? 3020 HOH A O     1 
HETATM 19381 O  O     . HOH DA 11 .    ? -23.896 100.340 101.270 1.00 41.13 ? 3021 HOH A O     1 
HETATM 19382 O  O     . HOH DA 11 .    ? -18.030 53.939  99.156  1.00 38.43 ? 3022 HOH A O     1 
HETATM 19383 O  O     . HOH DA 11 .    ? -54.192 62.207  103.864 1.00 42.53 ? 3023 HOH A O     1 
HETATM 19384 O  O     . HOH DA 11 .    ? 5.422   71.214  96.436  1.00 43.75 ? 3024 HOH A O     1 
HETATM 19385 O  O     . HOH DA 11 .    ? -46.600 80.485  75.499  1.00 53.05 ? 3025 HOH A O     1 
HETATM 19386 O  O     . HOH DA 11 .    ? -63.939 51.179  73.505  1.00 38.93 ? 3026 HOH A O     1 
HETATM 19387 O  O     . HOH DA 11 .    ? 27.668  58.974  109.874 1.00 49.48 ? 3027 HOH A O     1 
HETATM 19388 O  O     . HOH DA 11 .    ? -26.856 65.442  103.163 1.00 29.04 ? 3028 HOH A O     1 
HETATM 19389 O  O     . HOH DA 11 .    ? -28.354 67.368  93.635  1.00 44.59 ? 3029 HOH A O     1 
HETATM 19390 O  O     . HOH DA 11 .    ? -52.445 56.808  74.006  1.00 31.44 ? 3030 HOH A O     1 
HETATM 19391 O  O     . HOH DA 11 .    ? -39.822 67.850  89.407  1.00 30.04 ? 3031 HOH A O     1 
HETATM 19392 O  O     . HOH DA 11 .    ? -22.641 74.152  70.004  1.00 32.93 ? 3032 HOH A O     1 
HETATM 19393 O  O     . HOH DA 11 .    ? -21.401 63.031  81.348  1.00 46.23 ? 3033 HOH A O     1 
HETATM 19394 O  O     . HOH DA 11 .    ? -30.423 49.146  86.718  1.00 39.57 ? 3034 HOH A O     1 
HETATM 19395 O  O     . HOH DA 11 .    ? -9.318  62.324  94.345  1.00 38.58 ? 3035 HOH A O     1 
HETATM 19396 O  O     . HOH DA 11 .    ? -44.493 69.577  111.760 1.00 43.23 ? 3036 HOH A O     1 
HETATM 19397 O  O     . HOH DA 11 .    ? -18.482 59.709  111.209 1.00 33.11 ? 3037 HOH A O     1 
HETATM 19398 O  O     . HOH DA 11 .    ? -22.831 71.413  74.218  1.00 35.87 ? 3038 HOH A O     1 
HETATM 19399 O  O     . HOH DA 11 .    ? -38.899 76.185  122.503 1.00 43.88 ? 3039 HOH A O     1 
HETATM 19400 O  O     . HOH DA 11 .    ? -16.033 98.510  127.525 1.00 47.74 ? 3040 HOH A O     1 
HETATM 19401 O  O     . HOH DA 11 .    ? -32.027 68.043  101.834 1.00 36.81 ? 3041 HOH A O     1 
HETATM 19402 O  O     . HOH DA 11 .    ? -26.046 67.857  94.442  1.00 38.86 ? 3042 HOH A O     1 
HETATM 19403 O  O     . HOH DA 11 .    ? -10.801 41.045  57.723  1.00 45.18 ? 3043 HOH A O     1 
HETATM 19404 O  O     . HOH DA 11 .    ? -40.072 56.383  78.284  1.00 36.40 ? 3044 HOH A O     1 
HETATM 19405 O  O     . HOH DA 11 .    ? -34.551 39.107  95.102  1.00 35.42 ? 3045 HOH A O     1 
HETATM 19406 O  O     . HOH DA 11 .    ? -32.986 84.385  77.206  1.00 26.96 ? 3046 HOH A O     1 
HETATM 19407 O  O     . HOH DA 11 .    ? 12.586  88.420  119.238 1.00 39.48 ? 3047 HOH A O     1 
HETATM 19408 O  O     . HOH DA 11 .    ? -21.892 74.128  134.795 1.00 41.34 ? 3048 HOH A O     1 
HETATM 19409 O  O     . HOH DA 11 .    ? -58.567 30.433  86.772  1.00 37.01 ? 3049 HOH A O     1 
HETATM 19410 O  O     . HOH DA 11 .    ? -55.136 57.615  102.545 1.00 33.92 ? 3050 HOH A O     1 
HETATM 19411 O  O     . HOH DA 11 .    ? -11.403 59.902  106.702 1.00 33.20 ? 3051 HOH A O     1 
HETATM 19412 O  O     . HOH DA 11 .    ? -38.995 35.637  88.996  1.00 34.91 ? 3052 HOH A O     1 
HETATM 19413 O  O     . HOH DA 11 .    ? -11.171 64.081  51.328  1.00 45.18 ? 3053 HOH A O     1 
HETATM 19414 O  O     . HOH DA 11 .    ? -45.759 56.768  54.750  1.00 39.82 ? 3054 HOH A O     1 
HETATM 19415 O  O     . HOH DA 11 .    ? -45.096 28.751  87.130  1.00 36.48 ? 3055 HOH A O     1 
HETATM 19416 O  O     . HOH DA 11 .    ? -7.081  65.900  92.747  1.00 39.17 ? 3056 HOH A O     1 
HETATM 19417 O  O     . HOH DA 11 .    ? -21.245 99.266  98.171  1.00 44.47 ? 3057 HOH A O     1 
HETATM 19418 O  O     . HOH DA 11 .    ? -27.993 82.536  102.161 1.00 32.65 ? 3058 HOH A O     1 
HETATM 19419 O  O     . HOH DA 11 .    ? 7.533   62.420  112.750 1.00 39.13 ? 3059 HOH A O     1 
HETATM 19420 O  O     . HOH DA 11 .    ? -30.050 82.852  101.215 1.00 41.16 ? 3060 HOH A O     1 
HETATM 19421 O  O     . HOH DA 11 .    ? -8.994  67.215  129.676 1.00 37.59 ? 3061 HOH A O     1 
HETATM 19422 O  O     . HOH DA 11 .    ? -15.381 57.800  106.492 1.00 31.10 ? 3062 HOH A O     1 
HETATM 19423 O  O     . HOH DA 11 .    ? -24.092 77.739  68.762  1.00 42.48 ? 3063 HOH A O     1 
HETATM 19424 O  O     . HOH DA 11 .    ? -53.351 50.685  101.755 1.00 44.32 ? 3064 HOH A O     1 
HETATM 19425 O  O     . HOH DA 11 .    ? -34.594 76.490  87.597  1.00 27.57 ? 3065 HOH A O     1 
HETATM 19426 O  O     . HOH DA 11 .    ? -9.465  55.142  96.603  1.00 47.87 ? 3066 HOH A O     1 
HETATM 19427 O  O     . HOH DA 11 .    ? -52.103 80.573  96.177  1.00 51.64 ? 3067 HOH A O     1 
HETATM 19428 O  O     A HOH DA 11 .    ? 5.109   60.665  98.518  0.65 21.54 ? 3068 HOH A O     1 
HETATM 19429 O  O     . HOH DA 11 .    ? -6.820  55.103  82.856  1.00 33.15 ? 3069 HOH A O     1 
HETATM 19430 O  O     . HOH DA 11 .    ? -55.020 27.653  81.927  1.00 43.34 ? 3070 HOH A O     1 
HETATM 19431 O  O     . HOH DA 11 .    ? -62.751 61.038  93.707  1.00 35.77 ? 3071 HOH A O     1 
HETATM 19432 O  O     . HOH DA 11 .    ? -35.211 73.758  86.899  1.00 31.61 ? 3072 HOH A O     1 
HETATM 19433 O  O     . HOH DA 11 .    ? -40.531 47.073  59.943  1.00 41.78 ? 3073 HOH A O     1 
HETATM 19434 O  O     . HOH DA 11 .    ? -27.708 63.936  90.808  1.00 33.82 ? 3074 HOH A O     1 
HETATM 19435 O  O     . HOH DA 11 .    ? -25.065 100.706 91.430  1.00 39.73 ? 3075 HOH A O     1 
HETATM 19436 O  O     . HOH DA 11 .    ? 17.111  84.216  113.143 1.00 41.14 ? 3076 HOH A O     1 
HETATM 19437 O  O     . HOH DA 11 .    ? -8.541  52.867  104.702 1.00 44.84 ? 3077 HOH A O     1 
HETATM 19438 O  O     . HOH DA 11 .    ? -9.774  67.095  132.544 1.00 39.03 ? 3078 HOH A O     1 
HETATM 19439 O  O     . HOH DA 11 .    ? 7.024   59.834  94.542  1.00 44.29 ? 3079 HOH A O     1 
HETATM 19440 O  O     . HOH DA 11 .    ? -29.008 60.780  121.166 1.00 40.67 ? 3080 HOH A O     1 
HETATM 19441 O  O     . HOH DA 11 .    ? -53.106 40.461  63.544  1.00 44.16 ? 3081 HOH A O     1 
HETATM 19442 O  O     . HOH DA 11 .    ? -23.091 55.385  52.551  1.00 49.67 ? 3082 HOH A O     1 
HETATM 19443 O  O     . HOH DA 11 .    ? -52.528 51.092  104.083 1.00 48.57 ? 3083 HOH A O     1 
HETATM 19444 O  O     . HOH DA 11 .    ? -52.381 64.129  101.020 1.00 33.08 ? 3084 HOH A O     1 
HETATM 19445 O  O     . HOH DA 11 .    ? -36.030 66.734  69.526  1.00 47.44 ? 3085 HOH A O     1 
HETATM 19446 O  O     . HOH DA 11 .    ? -3.561  68.395  93.384  1.00 42.07 ? 3086 HOH A O     1 
HETATM 19447 O  O     . HOH DA 11 .    ? -36.032 63.267  90.656  1.00 36.80 ? 3087 HOH A O     1 
HETATM 19448 O  O     . HOH DA 11 .    ? -58.381 74.557  95.058  1.00 47.87 ? 3088 HOH A O     1 
HETATM 19449 O  O     . HOH DA 11 .    ? -52.354 48.424  58.086  1.00 39.56 ? 3089 HOH A O     1 
HETATM 19450 O  O     . HOH DA 11 .    ? -65.488 54.449  78.607  1.00 36.24 ? 3090 HOH A O     1 
HETATM 19451 O  O     . HOH DA 11 .    ? -5.917  85.678  85.006  1.00 42.93 ? 3091 HOH A O     1 
HETATM 19452 O  O     . HOH DA 11 .    ? -33.820 60.978  86.634  1.00 39.41 ? 3092 HOH A O     1 
HETATM 19453 O  O     . HOH DA 11 .    ? 22.744  79.200  100.382 1.00 44.61 ? 3093 HOH A O     1 
HETATM 19454 O  O     . HOH DA 11 .    ? -39.034 69.793  118.736 1.00 41.52 ? 3094 HOH A O     1 
HETATM 19455 O  O     . HOH DA 11 .    ? -57.834 46.437  64.113  1.00 45.46 ? 3095 HOH A O     1 
HETATM 19456 O  O     . HOH DA 11 .    ? -44.673 88.329  99.515  1.00 43.36 ? 3096 HOH A O     1 
HETATM 19457 O  O     . HOH DA 11 .    ? -52.126 74.109  62.210  1.00 26.05 ? 3097 HOH A O     1 
HETATM 19458 O  O     . HOH DA 11 .    ? -23.985 51.151  103.918 1.00 48.26 ? 3098 HOH A O     1 
HETATM 19459 O  O     . HOH DA 11 .    ? -56.402 44.300  92.694  1.00 38.95 ? 3099 HOH A O     1 
HETATM 19460 O  O     . HOH DA 11 .    ? 16.108  83.115  116.846 1.00 39.95 ? 3100 HOH A O     1 
HETATM 19461 O  O     . HOH DA 11 .    ? -2.539  56.901  70.953  1.00 35.30 ? 3101 HOH A O     1 
HETATM 19462 O  O     . HOH DA 11 .    ? -10.504 78.710  92.531  1.00 22.54 ? 3102 HOH A O     1 
HETATM 19463 O  O     . HOH DA 11 .    ? 2.897   74.541  87.586  1.00 48.90 ? 3103 HOH A O     1 
HETATM 19464 O  O     . HOH DA 11 .    ? -14.696 57.981  124.197 1.00 39.30 ? 3104 HOH A O     1 
HETATM 19465 O  O     . HOH DA 11 .    ? -16.789 57.465  110.615 1.00 44.15 ? 3105 HOH A O     1 
HETATM 19466 O  O     . HOH DA 11 .    ? -44.636 82.647  89.129  1.00 43.18 ? 3106 HOH A O     1 
HETATM 19467 O  O     . HOH DA 11 .    ? -53.700 42.393  60.725  1.00 49.55 ? 3107 HOH A O     1 
HETATM 19468 O  O     . HOH DA 11 .    ? -24.694 65.956  97.332  1.00 26.71 ? 3108 HOH A O     1 
HETATM 19469 O  O     . HOH DA 11 .    ? -34.892 54.749  107.715 1.00 33.64 ? 3109 HOH A O     1 
HETATM 19470 O  O     . HOH DA 11 .    ? -50.512 81.206  84.002  1.00 38.72 ? 3110 HOH A O     1 
HETATM 19471 O  O     . HOH DA 11 .    ? -52.620 66.392  105.074 1.00 38.80 ? 3111 HOH A O     1 
HETATM 19472 O  O     . HOH DA 11 .    ? -57.764 32.118  90.453  1.00 30.39 ? 3112 HOH A O     1 
HETATM 19473 O  O     . HOH DA 11 .    ? -3.617  69.737  95.266  1.00 45.59 ? 3113 HOH A O     1 
HETATM 19474 O  O     . HOH DA 11 .    ? -41.909 64.015  106.514 1.00 39.02 ? 3114 HOH A O     1 
HETATM 19475 O  O     . HOH DA 11 .    ? -59.901 52.610  96.433  1.00 42.17 ? 3115 HOH A O     1 
HETATM 19476 O  O     . HOH DA 11 .    ? -66.740 66.039  83.567  1.00 26.88 ? 3116 HOH A O     1 
HETATM 19477 O  O     . HOH DA 11 .    ? -53.081 45.393  94.757  1.00 33.99 ? 3117 HOH A O     1 
HETATM 19478 O  O     . HOH DA 11 .    ? -2.012  74.369  118.618 1.00 38.95 ? 3118 HOH A O     1 
HETATM 19479 O  O     . HOH DA 11 .    ? -44.854 29.762  99.132  1.00 46.81 ? 3119 HOH A O     1 
HETATM 19480 O  O     . HOH DA 11 .    ? -8.173  61.485  86.994  1.00 42.11 ? 3120 HOH A O     1 
HETATM 19481 O  O     . HOH DA 11 .    ? 16.534  66.514  90.552  1.00 41.47 ? 3121 HOH A O     1 
HETATM 19482 O  O     . HOH DA 11 .    ? -19.808 52.789  105.790 1.00 37.80 ? 3122 HOH A O     1 
HETATM 19483 O  O     . HOH DA 11 .    ? -44.375 83.297  86.721  1.00 42.77 ? 3123 HOH A O     1 
HETATM 19484 O  O     . HOH DA 11 .    ? 2.246   83.862  129.871 1.00 44.95 ? 3124 HOH A O     1 
HETATM 19485 O  O     . HOH DA 11 .    ? -26.640 40.819  76.339  1.00 52.11 ? 3125 HOH A O     1 
HETATM 19486 O  O     . HOH DA 11 .    ? -33.622 81.141  122.850 1.00 37.40 ? 3126 HOH A O     1 
HETATM 19487 O  O     . HOH DA 11 .    ? -54.527 78.040  85.884  1.00 43.04 ? 3127 HOH A O     1 
HETATM 19488 O  O     . HOH DA 11 .    ? -61.196 72.614  82.484  1.00 43.81 ? 3128 HOH A O     1 
HETATM 19489 O  O     . HOH DA 11 .    ? -66.461 72.835  78.080  1.00 44.68 ? 3129 HOH A O     1 
HETATM 19490 O  O     . HOH DA 11 .    ? -37.281 63.159  114.476 1.00 37.82 ? 3130 HOH A O     1 
HETATM 19491 O  O     . HOH DA 11 .    ? -30.273 79.711  126.076 1.00 38.00 ? 3131 HOH A O     1 
HETATM 19492 O  O     . HOH DA 11 .    ? 24.875  66.841  113.524 1.00 37.70 ? 3132 HOH A O     1 
HETATM 19493 O  O     . HOH DA 11 .    ? -35.104 39.070  90.057  1.00 43.66 ? 3133 HOH A O     1 
HETATM 19494 O  O     . HOH DA 11 .    ? -10.094 90.704  127.853 1.00 42.31 ? 3134 HOH A O     1 
HETATM 19495 O  O     . HOH DA 11 .    ? -26.931 59.300  116.578 1.00 37.33 ? 3135 HOH A O     1 
HETATM 19496 O  O     . HOH DA 11 .    ? -22.587 91.570  103.753 1.00 37.65 ? 3136 HOH A O     1 
HETATM 19497 O  O     . HOH DA 11 .    ? -37.841 74.297  93.362  1.00 35.87 ? 3137 HOH A O     1 
HETATM 19498 O  O     . HOH DA 11 .    ? -25.813 83.307  70.000  1.00 43.34 ? 3138 HOH A O     1 
HETATM 19499 O  O     . HOH DA 11 .    ? -22.288 46.490  55.771  1.00 47.87 ? 3139 HOH A O     1 
HETATM 19500 O  O     . HOH DA 11 .    ? -33.595 80.980  74.756  1.00 30.51 ? 3140 HOH A O     1 
HETATM 19501 O  O     . HOH DA 11 .    ? 2.075   74.972  119.604 1.00 41.38 ? 3141 HOH A O     1 
HETATM 19502 O  O     . HOH DA 11 .    ? -56.359 74.593  79.583  1.00 34.36 ? 3142 HOH A O     1 
HETATM 19503 O  O     . HOH DA 11 .    ? -63.869 65.177  66.907  1.00 37.50 ? 3143 HOH A O     1 
HETATM 19504 O  O     . HOH DA 11 .    ? 6.679   81.472  127.446 1.00 40.14 ? 3144 HOH A O     1 
HETATM 19505 O  O     . HOH DA 11 .    ? -18.651 47.310  53.216  1.00 39.55 ? 3145 HOH A O     1 
HETATM 19506 O  O     . HOH DA 11 .    ? -5.778  62.407  93.618  1.00 44.53 ? 3146 HOH A O     1 
HETATM 19507 O  O     . HOH DA 11 .    ? -53.386 71.115  106.936 1.00 45.11 ? 3147 HOH A O     1 
HETATM 19508 O  O     . HOH DA 11 .    ? -25.636 65.221  92.085  1.00 33.20 ? 3148 HOH A O     1 
HETATM 19509 O  O     . HOH DA 11 .    ? -16.755 50.507  77.255  1.00 45.14 ? 3149 HOH A O     1 
HETATM 19510 O  O     . HOH DA 11 .    ? -63.463 48.678  72.069  1.00 40.89 ? 3150 HOH A O     1 
HETATM 19511 O  O     . HOH DA 11 .    ? -22.684 90.082  101.280 1.00 37.89 ? 3151 HOH A O     1 
HETATM 19512 O  O     . HOH DA 11 .    ? 20.565  61.645  96.648  1.00 35.30 ? 3152 HOH A O     1 
HETATM 19513 O  O     . HOH DA 11 .    ? -51.955 38.706  102.055 1.00 46.13 ? 3153 HOH A O     1 
HETATM 19514 O  O     . HOH DA 11 .    ? -25.018 97.552  126.420 1.00 43.86 ? 3154 HOH A O     1 
HETATM 19515 O  O     . HOH DA 11 .    ? 0.749   63.896  93.142  1.00 48.77 ? 3155 HOH A O     1 
HETATM 19516 O  O     . HOH DA 11 .    ? -41.508 48.680  108.418 1.00 45.48 ? 3156 HOH A O     1 
HETATM 19517 O  O     . HOH DA 11 .    ? -25.340 62.154  102.566 1.00 28.27 ? 3157 HOH A O     1 
HETATM 19518 O  O     . HOH DA 11 .    ? -18.444 74.553  109.594 1.00 27.00 ? 3158 HOH A O     1 
HETATM 19519 O  O     . HOH DA 11 .    ? -0.710  61.095  112.760 1.00 34.50 ? 3159 HOH A O     1 
HETATM 19520 O  O     . HOH DA 11 .    ? 17.489  59.789  117.495 1.00 44.94 ? 3160 HOH A O     1 
HETATM 19521 O  O     . HOH DA 11 .    ? -46.594 80.759  90.076  1.00 41.07 ? 3161 HOH A O     1 
HETATM 19522 O  O     . HOH DA 11 .    ? -9.131  73.772  129.454 1.00 37.50 ? 3162 HOH A O     1 
HETATM 19523 O  O     . HOH DA 11 .    ? -24.262 97.223  121.931 1.00 43.30 ? 3163 HOH A O     1 
HETATM 19524 O  O     . HOH DA 11 .    ? -12.802 51.519  103.396 1.00 50.89 ? 3164 HOH A O     1 
HETATM 19525 O  O     . HOH DA 11 .    ? -66.356 47.748  73.573  1.00 37.35 ? 3165 HOH A O     1 
HETATM 19526 O  O     . HOH DA 11 .    ? 10.916  79.739  129.004 1.00 40.57 ? 3166 HOH A O     1 
HETATM 19527 O  O     . HOH DA 11 .    ? -58.695 55.359  100.951 1.00 42.14 ? 3167 HOH A O     1 
HETATM 19528 O  O     . HOH DA 11 .    ? -10.557 66.032  72.733  1.00 43.12 ? 3168 HOH A O     1 
HETATM 19529 O  O     . HOH DA 11 .    ? -53.112 69.010  101.002 1.00 31.39 ? 3169 HOH A O     1 
HETATM 19530 O  O     . HOH DA 11 .    ? -48.937 77.435  94.180  1.00 39.43 ? 3170 HOH A O     1 
HETATM 19531 O  O     . HOH DA 11 .    ? -69.513 61.688  72.684  1.00 30.56 ? 3171 HOH A O     1 
HETATM 19532 O  O     . HOH DA 11 .    ? -35.938 90.523  124.167 1.00 36.51 ? 3172 HOH A O     1 
HETATM 19533 O  O     . HOH DA 11 .    ? -6.685  86.936  88.398  1.00 49.30 ? 3173 HOH A O     1 
HETATM 19534 O  O     . HOH DA 11 .    ? -31.515 70.204  98.796  1.00 38.95 ? 3174 HOH A O     1 
HETATM 19535 O  O     . HOH DA 11 .    ? -20.618 89.748  138.190 1.00 44.31 ? 3175 HOH A O     1 
HETATM 19536 O  O     . HOH DA 11 .    ? -33.292 62.316  89.576  1.00 46.87 ? 3176 HOH A O     1 
HETATM 19537 O  O     . HOH DA 11 .    ? -28.512 77.901  70.518  1.00 35.52 ? 3177 HOH A O     1 
HETATM 19538 O  O     . HOH DA 11 .    ? 10.334  68.456  114.625 1.00 34.35 ? 3178 HOH A O     1 
HETATM 19539 O  O     . HOH DA 11 .    ? -51.998 73.143  102.939 1.00 32.37 ? 3179 HOH A O     1 
HETATM 19540 O  O     . HOH DA 11 .    ? -34.777 83.482  126.352 1.00 46.06 ? 3180 HOH A O     1 
HETATM 19541 O  O     . HOH DA 11 .    ? -9.516  63.761  91.805  1.00 47.13 ? 3181 HOH A O     1 
HETATM 19542 O  O     . HOH DA 11 .    ? -31.279 54.610  111.188 1.00 45.63 ? 3182 HOH A O     1 
HETATM 19543 O  O     . HOH DA 11 .    ? -10.335 62.307  89.904  1.00 51.75 ? 3183 HOH A O     1 
HETATM 19544 O  O     . HOH DA 11 .    ? 16.345  59.923  92.942  1.00 48.08 ? 3184 HOH A O     1 
HETATM 19545 O  O     . HOH DA 11 .    ? -50.584 81.952  113.176 1.00 44.11 ? 3185 HOH A O     1 
HETATM 19546 O  O     . HOH DA 11 .    ? -6.144  42.259  59.650  1.00 43.57 ? 3186 HOH A O     1 
HETATM 19547 O  O     . HOH DA 11 .    ? -31.959 75.575  85.368  1.00 31.08 ? 3187 HOH A O     1 
HETATM 19548 O  O     . HOH DA 11 .    ? -40.917 82.585  68.873  1.00 36.55 ? 3188 HOH A O     1 
HETATM 19549 O  O     . HOH DA 11 .    ? -26.865 66.643  98.554  1.00 27.31 ? 3189 HOH A O     1 
HETATM 19550 O  O     . HOH DA 11 .    ? -4.068  80.059  125.136 1.00 35.35 ? 3190 HOH A O     1 
HETATM 19551 O  O     . HOH DA 11 .    ? 13.028  61.824  116.701 1.00 44.66 ? 3191 HOH A O     1 
HETATM 19552 O  O     . HOH DA 11 .    ? 20.820  70.788  119.136 1.00 37.16 ? 3192 HOH A O     1 
HETATM 19553 O  O     . HOH DA 11 .    ? -27.738 71.305  99.498  1.00 36.05 ? 3193 HOH A O     1 
HETATM 19554 O  O     . HOH DA 11 .    ? -32.425 58.423  84.918  1.00 42.35 ? 3194 HOH A O     1 
HETATM 19555 O  O     . HOH DA 11 .    ? -32.124 65.703  124.996 1.00 35.00 ? 3195 HOH A O     1 
HETATM 19556 O  O     . HOH DA 11 .    ? -8.769  57.709  84.679  1.00 39.24 ? 3196 HOH A O     1 
HETATM 19557 O  O     . HOH DA 11 .    ? 3.257   64.100  94.007  1.00 41.94 ? 3197 HOH A O     1 
HETATM 19558 O  O     . HOH DA 11 .    ? -30.773 84.228  73.646  1.00 36.28 ? 3198 HOH A O     1 
HETATM 19559 O  O     . HOH DA 11 .    ? -18.550 70.921  69.408  1.00 38.53 ? 3199 HOH A O     1 
HETATM 19560 O  O     . HOH DA 11 .    ? -64.625 67.405  89.500  1.00 46.23 ? 3200 HOH A O     1 
HETATM 19561 O  O     . HOH DA 11 .    ? -2.052  91.765  98.564  1.00 41.61 ? 3201 HOH A O     1 
HETATM 19562 O  O     . HOH DA 11 .    ? -26.898 93.837  109.989 1.00 48.48 ? 3202 HOH A O     1 
HETATM 19563 O  O     . HOH DA 11 .    ? -36.972 82.732  77.626  1.00 40.57 ? 3203 HOH A O     1 
HETATM 19564 O  O     . HOH DA 11 .    ? -62.492 53.699  65.992  1.00 41.01 ? 3204 HOH A O     1 
HETATM 19565 O  O     . HOH DA 11 .    ? -8.211  77.147  129.638 1.00 41.72 ? 3205 HOH A O     1 
HETATM 19566 O  O     . HOH DA 11 .    ? 6.872   62.673  95.028  1.00 30.35 ? 3206 HOH A O     1 
HETATM 19567 O  O     . HOH DA 11 .    ? -33.035 58.495  113.872 1.00 44.97 ? 3207 HOH A O     1 
HETATM 19568 O  O     . HOH DA 11 .    ? -7.708  49.130  51.713  1.00 46.71 ? 3208 HOH A O     1 
HETATM 19569 O  O     . HOH DA 11 .    ? -33.152 76.353  90.076  1.00 42.79 ? 3209 HOH A O     1 
HETATM 19570 O  O     . HOH DA 11 .    ? 3.983   64.741  96.530  1.00 30.27 ? 3210 HOH A O     1 
HETATM 19571 O  O     . HOH DA 11 .    ? -16.659 93.287  106.524 1.00 40.38 ? 3211 HOH A O     1 
HETATM 19572 O  O     . HOH DA 11 .    ? -29.448 92.566  109.123 1.00 35.97 ? 3212 HOH A O     1 
HETATM 19573 O  O     . HOH DA 11 .    ? -42.044 42.059  107.986 1.00 45.93 ? 3213 HOH A O     1 
HETATM 19574 O  O     . HOH DA 11 .    ? -9.793  49.272  107.301 1.00 42.65 ? 3214 HOH A O     1 
HETATM 19575 O  O     . HOH DA 11 .    ? -7.045  69.405  130.159 1.00 44.55 ? 3215 HOH A O     1 
HETATM 19576 O  O     . HOH DA 11 .    ? -54.402 54.915  102.579 1.00 43.84 ? 3216 HOH A O     1 
HETATM 19577 O  O     . HOH DA 11 .    ? -11.579 57.155  86.163  1.00 46.66 ? 3217 HOH A O     1 
HETATM 19578 O  O     . HOH DA 11 .    ? -63.235 57.466  96.620  1.00 37.60 ? 3218 HOH A O     1 
HETATM 19579 O  O     . HOH DA 11 .    ? -29.892 60.141  86.138  1.00 37.34 ? 3219 HOH A O     1 
HETATM 19580 O  O     . HOH DA 11 .    ? -47.563 37.308  100.747 1.00 37.62 ? 3220 HOH A O     1 
HETATM 19581 O  O     . HOH DA 11 .    ? -24.436 52.220  100.432 1.00 33.16 ? 3221 HOH A O     1 
HETATM 19582 O  O     . HOH DA 11 .    ? -35.268 39.475  72.846  1.00 48.87 ? 3222 HOH A O     1 
HETATM 19583 O  O     . HOH DA 11 .    ? -58.844 73.986  82.417  1.00 46.19 ? 3223 HOH A O     1 
HETATM 19584 O  O     . HOH DA 11 .    ? -19.096 57.750  106.940 1.00 29.97 ? 3224 HOH A O     1 
HETATM 19585 O  O     . HOH DA 11 .    ? -20.712 52.896  101.590 1.00 38.34 ? 3225 HOH A O     1 
HETATM 19586 O  O     . HOH DA 11 .    ? -56.387 76.270  77.113  1.00 32.78 ? 3226 HOH A O     1 
HETATM 19587 O  O     . HOH DA 11 .    ? 23.229  70.199  116.232 1.00 34.28 ? 3227 HOH A O     1 
HETATM 19588 O  O     . HOH DA 11 .    ? -61.565 50.871  66.553  1.00 36.70 ? 3228 HOH A O     1 
HETATM 19589 O  O     . HOH DA 11 .    ? -8.745  52.671  101.570 1.00 46.21 ? 3229 HOH A O     1 
HETATM 19590 O  O     . HOH DA 11 .    ? -58.202 59.356  103.264 1.00 42.97 ? 3230 HOH A O     1 
HETATM 19591 O  O     . HOH DA 11 .    ? 2.893   71.282  95.566  1.00 46.91 ? 3231 HOH A O     1 
HETATM 19592 O  O     . HOH DA 11 .    ? -54.977 41.634  99.896  1.00 45.64 ? 3232 HOH A O     1 
HETATM 19593 O  O     . HOH DA 11 .    ? -62.529 55.391  69.999  1.00 30.72 ? 3233 HOH A O     1 
HETATM 19594 O  O     . HOH DA 11 .    ? -30.610 86.926  74.656  1.00 42.66 ? 3234 HOH A O     1 
HETATM 19595 O  O     . HOH DA 11 .    ? 3.168   68.559  94.808  1.00 46.69 ? 3235 HOH A O     1 
HETATM 19596 O  O     . HOH DA 11 .    ? -18.538 74.017  106.656 1.00 31.41 ? 3236 HOH A O     1 
HETATM 19597 O  O     . HOH DA 11 .    ? -23.985 50.357  95.591  1.00 37.76 ? 3237 HOH A O     1 
HETATM 19598 O  O     . HOH DA 11 .    ? -29.231 60.162  88.876  1.00 22.88 ? 3238 HOH A O     1 
HETATM 19599 O  O     . HOH DA 11 .    ? -1.930  87.919  126.070 1.00 47.08 ? 3239 HOH A O     1 
HETATM 19600 O  O     . HOH DA 11 .    ? -8.347  70.892  132.668 1.00 47.29 ? 3240 HOH A O     1 
HETATM 19601 O  O     . HOH DA 11 .    ? -41.901 26.327  85.357  1.00 47.07 ? 3241 HOH A O     1 
HETATM 19602 O  O     . HOH DA 11 .    ? -61.541 70.616  85.810  1.00 37.81 ? 3242 HOH A O     1 
HETATM 19603 O  O     . HOH DA 11 .    ? 3.563   69.389  88.671  1.00 35.83 ? 3243 HOH A O     1 
HETATM 19604 O  O     . HOH DA 11 .    ? -21.745 68.666  132.450 1.00 41.07 ? 3244 HOH A O     1 
HETATM 19605 O  O     . HOH DA 11 .    ? -1.800  75.143  121.132 1.00 41.29 ? 3245 HOH A O     1 
HETATM 19606 O  O     . HOH DA 11 .    ? -56.799 27.953  92.624  1.00 43.56 ? 3246 HOH A O     1 
HETATM 19607 O  O     . HOH DA 11 .    ? -8.764  43.319  58.014  1.00 39.06 ? 3247 HOH A O     1 
HETATM 19608 O  O     . HOH DA 11 .    ? -56.641 52.321  98.919  1.00 36.85 ? 3248 HOH A O     1 
HETATM 19609 O  O     . HOH DA 11 .    ? 12.721  62.546  93.534  1.00 38.30 ? 3249 HOH A O     1 
HETATM 19610 O  O     . HOH DA 11 .    ? -61.549 52.780  94.084  1.00 40.47 ? 3250 HOH A O     1 
HETATM 19611 O  O     . HOH DA 11 .    ? -2.449  84.919  96.848  1.00 38.93 ? 3251 HOH A O     1 
HETATM 19612 O  O     . HOH DA 11 .    ? -54.721 80.018  84.408  1.00 48.67 ? 3252 HOH A O     1 
HETATM 19613 O  O     . HOH DA 11 .    ? -3.314  83.305  112.515 1.00 35.97 ? 3253 HOH A O     1 
HETATM 19614 O  O     . HOH DA 11 .    ? -51.707 47.203  96.829  1.00 31.21 ? 3254 HOH A O     1 
HETATM 19615 O  O     . HOH DA 11 .    ? -22.817 52.142  97.871  1.00 41.19 ? 3255 HOH A O     1 
HETATM 19616 O  O     . HOH DA 11 .    ? -55.486 46.088  65.329  1.00 38.39 ? 3256 HOH A O     1 
HETATM 19617 O  O     . HOH DA 11 .    ? -12.222 61.878  105.289 1.00 33.29 ? 3257 HOH A O     1 
HETATM 19618 O  O     . HOH DA 11 .    ? -54.736 42.186  63.292  1.00 48.88 ? 3258 HOH A O     1 
HETATM 19619 O  O     . HOH DA 11 .    ? -23.056 102.211 90.553  1.00 43.04 ? 3259 HOH A O     1 
HETATM 19620 O  O     . HOH DA 11 .    ? -54.756 52.833  100.811 1.00 34.31 ? 3260 HOH A O     1 
HETATM 19621 O  O     . HOH DA 11 .    ? -29.303 52.564  113.555 1.00 53.98 ? 3261 HOH A O     1 
HETATM 19622 O  O     . HOH DA 11 .    ? -45.854 39.168  104.839 1.00 37.66 ? 3262 HOH A O     1 
HETATM 19623 O  O     . HOH DA 11 .    ? -56.463 76.237  81.169  1.00 42.59 ? 3263 HOH A O     1 
HETATM 19624 O  O     . HOH DA 11 .    ? -61.720 55.417  98.082  1.00 49.97 ? 3264 HOH A O     1 
HETATM 19625 O  O     . HOH DA 11 .    ? -39.188 71.954  96.038  1.00 34.64 ? 3265 HOH A O     1 
HETATM 19626 O  O     . HOH DA 11 .    ? -24.875 62.916  100.107 1.00 29.45 ? 3266 HOH A O     1 
HETATM 19627 O  O     . HOH DA 11 .    ? -28.160 92.578  74.562  1.00 49.42 ? 3267 HOH A O     1 
HETATM 19628 O  O     . HOH DA 11 .    ? -37.826 69.450  96.158  1.00 44.43 ? 3268 HOH A O     1 
HETATM 19629 O  O     . HOH DA 11 .    ? -0.207  57.160  68.039  1.00 34.54 ? 3269 HOH A O     1 
HETATM 19630 O  O     . HOH DA 11 .    ? -39.739 83.422  76.870  1.00 45.44 ? 3270 HOH A O     1 
HETATM 19631 O  O     . HOH DA 11 .    ? -14.864 39.272  70.813  1.00 51.06 ? 3271 HOH A O     1 
HETATM 19632 O  O     . HOH DA 11 .    ? -34.740 63.874  122.080 1.00 39.72 ? 3272 HOH A O     1 
HETATM 19633 O  O     . HOH DA 11 .    ? -31.629 61.601  122.201 1.00 39.01 ? 3273 HOH A O     1 
HETATM 19634 O  O     . HOH DA 11 .    ? 11.456  64.802  93.427  1.00 41.70 ? 3274 HOH A O     1 
HETATM 19635 O  O     . HOH DA 11 .    ? -56.758 71.330  100.758 1.00 47.42 ? 3275 HOH A O     1 
HETATM 19636 O  O     . HOH DA 11 .    ? -33.105 78.542  71.420  1.00 45.29 ? 3276 HOH A O     1 
HETATM 19637 O  O     . HOH DA 11 .    ? -32.954 57.286  111.263 1.00 33.18 ? 3277 HOH A O     1 
HETATM 19638 O  O     . HOH DA 11 .    ? 14.081  65.930  90.951  1.00 40.15 ? 3278 HOH A O     1 
HETATM 19639 O  O     . HOH DA 11 .    ? -54.217 78.549  95.330  1.00 55.33 ? 3279 HOH A O     1 
HETATM 19640 O  O     . HOH DA 11 .    ? -37.068 34.355  90.222  1.00 39.42 ? 3280 HOH A O     1 
HETATM 19641 O  O     . HOH DA 11 .    ? -36.100 81.268  70.430  1.00 45.26 ? 3281 HOH A O     1 
HETATM 19642 O  O     . HOH DA 11 .    ? -66.035 66.824  66.437  1.00 46.31 ? 3282 HOH A O     1 
HETATM 19643 O  O     . HOH DA 11 .    ? -47.463 37.736  102.997 1.00 41.31 ? 3283 HOH A O     1 
HETATM 19644 O  O     . HOH DA 11 .    ? -55.851 78.751  77.626  1.00 35.90 ? 3284 HOH A O     1 
HETATM 19645 O  O     . HOH DA 11 .    ? -68.182 70.463  69.612  1.00 37.01 ? 3285 HOH A O     1 
HETATM 19646 O  O     . HOH DA 11 .    ? -36.301 32.283  91.156  1.00 40.40 ? 3286 HOH A O     1 
HETATM 19647 O  O     . HOH DA 11 .    ? -53.538 47.581  98.764  1.00 37.16 ? 3287 HOH A O     1 
HETATM 19648 O  O     . HOH DA 11 .    ? -53.964 71.545  102.736 1.00 39.16 ? 3288 HOH A O     1 
HETATM 19649 O  O     . HOH DA 11 .    ? -35.258 56.628  110.109 1.00 45.12 ? 3289 HOH A O     1 
HETATM 19650 O  O     . HOH DA 11 .    ? -33.884 81.403  71.810  1.00 38.06 ? 3290 HOH A O     1 
HETATM 19651 O  O     . HOH DA 11 .    ? 13.857  63.178  91.042  1.00 40.14 ? 3291 HOH A O     1 
HETATM 19652 O  O     . HOH EA 11 .    ? 6.421   31.945  79.319  1.00 29.75 ? 2101 HOH B O     1 
HETATM 19653 O  O     . HOH EA 11 .    ? -11.073 27.667  81.288  1.00 27.75 ? 2102 HOH B O     1 
HETATM 19654 O  O     . HOH EA 11 .    ? -2.900  29.495  99.270  1.00 39.44 ? 2103 HOH B O     1 
HETATM 19655 O  O     . HOH EA 11 .    ? 5.200   31.281  113.716 1.00 44.76 ? 2104 HOH B O     1 
HETATM 19656 O  O     . HOH EA 11 .    ? 15.608  27.021  81.294  1.00 33.44 ? 2105 HOH B O     1 
HETATM 19657 O  O     . HOH EA 11 .    ? 18.532  23.290  85.023  1.00 29.14 ? 2106 HOH B O     1 
HETATM 19658 O  O     . HOH EA 11 .    ? -4.140  26.788  99.860  1.00 31.18 ? 2107 HOH B O     1 
HETATM 19659 O  O     . HOH EA 11 .    ? 0.429   77.741  69.585  1.00 38.96 ? 2108 HOH B O     1 
HETATM 19660 O  O     . HOH EA 11 .    ? -0.191  -10.117 115.276 1.00 39.18 ? 2109 HOH B O     1 
HETATM 19661 O  O     . HOH EA 11 .    ? -7.417  34.394  66.460  1.00 44.81 ? 2110 HOH B O     1 
HETATM 19662 O  O     . HOH EA 11 .    ? 5.896   25.777  86.894  1.00 40.36 ? 2111 HOH B O     1 
HETATM 19663 O  O     . HOH EA 11 .    ? 6.539   15.246  124.711 1.00 38.05 ? 2112 HOH B O     1 
HETATM 19664 O  O     . HOH EA 11 .    ? 27.849  32.795  105.467 1.00 43.30 ? 2113 HOH B O     1 
HETATM 19665 O  O     . HOH EA 11 .    ? -0.036  18.691  80.638  1.00 28.31 ? 2114 HOH B O     1 
HETATM 19666 O  O     . HOH EA 11 .    ? -1.002  -8.785  102.365 1.00 35.64 ? 2115 HOH B O     1 
HETATM 19667 O  O     . HOH EA 11 .    ? -22.589 9.829   122.252 1.00 43.50 ? 2116 HOH B O     1 
HETATM 19668 O  O     . HOH EA 11 .    ? 2.507   17.300  112.584 1.00 33.14 ? 2117 HOH B O     1 
HETATM 19669 O  O     . HOH EA 11 .    ? -7.947  24.302  116.691 1.00 41.15 ? 2118 HOH B O     1 
HETATM 19670 O  O     . HOH EA 11 .    ? 21.166  40.122  47.911  1.00 41.82 ? 2119 HOH B O     1 
HETATM 19671 O  O     . HOH EA 11 .    ? 5.004   32.492  90.108  1.00 30.93 ? 2120 HOH B O     1 
HETATM 19672 O  O     . HOH EA 11 .    ? 16.902  14.479  109.464 1.00 32.54 ? 2121 HOH B O     1 
HETATM 19673 O  O     . HOH EA 11 .    ? 15.198  38.834  77.142  1.00 23.75 ? 2122 HOH B O     1 
HETATM 19674 O  O     . HOH EA 11 .    ? -7.157  -1.062  120.076 1.00 36.91 ? 2123 HOH B O     1 
HETATM 19675 O  O     . HOH EA 11 .    ? -0.833  47.864  87.544  1.00 37.77 ? 2124 HOH B O     1 
HETATM 19676 O  O     . HOH EA 11 .    ? -22.503 18.988  102.321 1.00 36.92 ? 2125 HOH B O     1 
HETATM 19677 O  O     . HOH EA 11 .    ? -10.072 -2.529  115.930 1.00 37.87 ? 2126 HOH B O     1 
HETATM 19678 O  O     . HOH EA 11 .    ? -4.265  23.300  107.499 1.00 42.84 ? 2127 HOH B O     1 
HETATM 19679 O  O     . HOH EA 11 .    ? 29.411  32.375  76.689  1.00 33.63 ? 2128 HOH B O     1 
HETATM 19680 O  O     . HOH EA 11 .    ? -1.117  22.469  71.320  1.00 34.75 ? 2129 HOH B O     1 
HETATM 19681 O  O     . HOH EA 11 .    ? 1.042   -10.206 111.039 1.00 35.93 ? 2130 HOH B O     1 
HETATM 19682 O  O     . HOH EA 11 .    ? 14.352  41.420  77.215  1.00 25.77 ? 2131 HOH B O     1 
HETATM 19683 O  O     . HOH EA 11 .    ? 29.494  42.302  84.420  1.00 35.46 ? 2132 HOH B O     1 
HETATM 19684 O  O     . HOH EA 11 .    ? 10.057  49.272  56.014  1.00 36.67 ? 2133 HOH B O     1 
HETATM 19685 O  O     . HOH EA 11 .    ? 5.635   -5.622  117.052 1.00 49.45 ? 2134 HOH B O     1 
HETATM 19686 O  O     . HOH EA 11 .    ? 12.547  55.926  65.810  1.00 37.11 ? 2135 HOH B O     1 
HETATM 19687 O  O     . HOH EA 11 .    ? 5.519   51.315  109.942 1.00 40.56 ? 2136 HOH B O     1 
HETATM 19688 O  O     . HOH EA 11 .    ? 20.108  15.851  111.501 1.00 42.91 ? 2137 HOH B O     1 
HETATM 19689 O  O     . HOH EA 11 .    ? -3.661  24.774  70.582  1.00 43.53 ? 2138 HOH B O     1 
HETATM 19690 O  O     . HOH EA 11 .    ? 38.316  33.725  102.916 1.00 40.23 ? 2139 HOH B O     1 
HETATM 19691 O  O     . HOH EA 11 .    ? -16.872 15.360  79.861  1.00 44.00 ? 2140 HOH B O     1 
HETATM 19692 O  O     . HOH EA 11 .    ? 11.015  79.954  67.861  1.00 44.94 ? 2141 HOH B O     1 
HETATM 19693 O  O     . HOH EA 11 .    ? 2.875   11.870  65.398  1.00 43.34 ? 2142 HOH B O     1 
HETATM 19694 O  O     . HOH EA 11 .    ? 33.696  12.408  74.803  1.00 36.57 ? 2143 HOH B O     1 
HETATM 19695 O  O     . HOH EA 11 .    ? 25.614  8.694   75.174  1.00 44.49 ? 2144 HOH B O     1 
HETATM 19696 O  O     . HOH EA 11 .    ? 5.203   22.706  122.877 1.00 37.05 ? 2145 HOH B O     1 
HETATM 19697 O  O     . HOH EA 11 .    ? -8.635  45.309  109.147 1.00 37.42 ? 2146 HOH B O     1 
HETATM 19698 O  O     . HOH EA 11 .    ? 9.541   26.063  55.211  1.00 25.54 ? 2147 HOH B O     1 
HETATM 19699 O  O     . HOH EA 11 .    ? 4.161   72.451  85.971  1.00 40.79 ? 2148 HOH B O     1 
HETATM 19700 O  O     . HOH EA 11 .    ? 18.915  24.995  54.421  1.00 27.68 ? 2149 HOH B O     1 
HETATM 19701 O  O     . HOH EA 11 .    ? 18.852  13.077  95.577  1.00 31.81 ? 2150 HOH B O     1 
HETATM 19702 O  O     . HOH EA 11 .    ? 18.936  31.435  73.344  1.00 28.68 ? 2151 HOH B O     1 
HETATM 19703 O  O     . HOH EA 11 .    ? 28.412  26.024  104.860 1.00 41.02 ? 2152 HOH B O     1 
HETATM 19704 O  O     . HOH EA 11 .    ? 3.339   18.390  89.136  1.00 32.23 ? 2153 HOH B O     1 
HETATM 19705 O  O     . HOH EA 11 .    ? -2.505  29.545  57.720  1.00 34.95 ? 2154 HOH B O     1 
HETATM 19706 O  O     . HOH EA 11 .    ? -6.323  12.353  125.578 1.00 32.72 ? 2155 HOH B O     1 
HETATM 19707 O  O     . HOH EA 11 .    ? 2.842   22.041  130.172 1.00 36.66 ? 2156 HOH B O     1 
HETATM 19708 O  O     . HOH EA 11 .    ? -10.858 27.391  110.813 1.00 48.31 ? 2157 HOH B O     1 
HETATM 19709 O  O     . HOH EA 11 .    ? -10.864 20.007  122.801 1.00 34.05 ? 2158 HOH B O     1 
HETATM 19710 O  O     . HOH EA 11 .    ? 3.501   21.326  102.826 1.00 40.00 ? 2159 HOH B O     1 
HETATM 19711 O  O     . HOH EA 11 .    ? 8.725   22.924  84.768  1.00 31.73 ? 2160 HOH B O     1 
HETATM 19712 O  O     . HOH EA 11 .    ? 10.613  24.629  103.957 1.00 33.40 ? 2161 HOH B O     1 
HETATM 19713 O  O     . HOH EA 11 .    ? 34.293  62.599  78.432  1.00 20.22 ? 2162 HOH B O     1 
HETATM 19714 O  O     . HOH EA 11 .    ? 7.067   51.413  57.638  1.00 35.65 ? 2163 HOH B O     1 
HETATM 19715 O  O     . HOH EA 11 .    ? -1.097  14.717  86.038  1.00 23.97 ? 2164 HOH B O     1 
HETATM 19716 O  O     . HOH EA 11 .    ? 7.415   32.764  98.224  1.00 32.84 ? 2165 HOH B O     1 
HETATM 19717 O  O     . HOH EA 11 .    ? 13.183  51.185  86.594  1.00 33.99 ? 2166 HOH B O     1 
HETATM 19718 O  O     . HOH EA 11 .    ? 23.518  18.151  80.472  1.00 33.82 ? 2167 HOH B O     1 
HETATM 19719 O  O     . HOH EA 11 .    ? 22.928  35.011  115.752 1.00 30.87 ? 2168 HOH B O     1 
HETATM 19720 O  O     . HOH EA 11 .    ? 12.091  70.342  60.820  1.00 39.20 ? 2169 HOH B O     1 
HETATM 19721 O  O     . HOH EA 11 .    ? 18.012  12.797  117.361 1.00 28.78 ? 2170 HOH B O     1 
HETATM 19722 O  O     . HOH EA 11 .    ? 33.207  29.693  61.756  1.00 32.94 ? 2171 HOH B O     1 
HETATM 19723 O  O     . HOH EA 11 .    ? 5.224   36.253  49.178  1.00 35.75 ? 2172 HOH B O     1 
HETATM 19724 O  O     . HOH EA 11 .    ? 22.521  9.998   69.805  1.00 43.06 ? 2173 HOH B O     1 
HETATM 19725 O  O     . HOH EA 11 .    ? 15.422  21.618  88.502  1.00 35.45 ? 2174 HOH B O     1 
HETATM 19726 O  O     . HOH EA 11 .    ? 1.407   15.087  116.173 1.00 32.51 ? 2175 HOH B O     1 
HETATM 19727 O  O     . HOH EA 11 .    ? 18.815  50.181  70.036  1.00 32.32 ? 2176 HOH B O     1 
HETATM 19728 O  O     . HOH EA 11 .    ? 15.635  52.818  58.178  1.00 36.78 ? 2177 HOH B O     1 
HETATM 19729 O  O     . HOH EA 11 .    ? 10.146  50.627  90.320  1.00 30.11 ? 2178 HOH B O     1 
HETATM 19730 O  O     . HOH EA 11 .    ? 8.726   -1.000  107.175 1.00 41.33 ? 2179 HOH B O     1 
HETATM 19731 O  O     . HOH EA 11 .    ? -8.710  24.330  77.121  1.00 39.37 ? 2180 HOH B O     1 
HETATM 19732 O  O     . HOH EA 11 .    ? -4.592  6.813   81.907  1.00 46.15 ? 2181 HOH B O     1 
HETATM 19733 O  O     . HOH EA 11 .    ? -5.730  37.450  77.797  1.00 31.52 ? 2182 HOH B O     1 
HETATM 19734 O  O     . HOH EA 11 .    ? 5.913   44.118  58.526  1.00 33.60 ? 2183 HOH B O     1 
HETATM 19735 O  O     . HOH EA 11 .    ? -14.303 9.570   118.763 1.00 39.14 ? 2184 HOH B O     1 
HETATM 19736 O  O     . HOH EA 11 .    ? 13.663  10.425  91.475  1.00 28.76 ? 2185 HOH B O     1 
HETATM 19737 O  O     . HOH EA 11 .    ? 21.647  79.848  69.895  1.00 41.26 ? 2186 HOH B O     1 
HETATM 19738 O  O     . HOH EA 11 .    ? 23.656  52.933  70.830  1.00 36.26 ? 2187 HOH B O     1 
HETATM 19739 O  O     . HOH EA 11 .    ? -4.212  64.291  81.219  1.00 19.28 ? 2188 HOH B O     1 
HETATM 19740 O  O     . HOH EA 11 .    ? 8.186   8.066   72.759  1.00 41.58 ? 2189 HOH B O     1 
HETATM 19741 O  O     . HOH EA 11 .    ? -13.979 54.249  118.293 1.00 31.51 ? 2190 HOH B O     1 
HETATM 19742 O  O     . HOH EA 11 .    ? 9.866   30.925  110.187 1.00 42.98 ? 2191 HOH B O     1 
HETATM 19743 O  O     . HOH EA 11 .    ? -25.570 6.129   111.865 1.00 38.77 ? 2192 HOH B O     1 
HETATM 19744 O  O     . HOH EA 11 .    ? -31.071 15.592  102.436 1.00 38.31 ? 2193 HOH B O     1 
HETATM 19745 O  O     . HOH EA 11 .    ? -4.732  27.105  70.246  1.00 32.21 ? 2194 HOH B O     1 
HETATM 19746 O  O     . HOH EA 11 .    ? -1.131  15.721  131.282 1.00 37.28 ? 2195 HOH B O     1 
HETATM 19747 O  O     . HOH EA 11 .    ? 42.378  34.737  84.390  1.00 38.03 ? 2196 HOH B O     1 
HETATM 19748 O  O     . HOH EA 11 .    ? 2.661   44.137  70.516  1.00 18.77 ? 2197 HOH B O     1 
HETATM 19749 O  O     . HOH EA 11 .    ? 4.291   21.413  119.176 1.00 37.85 ? 2198 HOH B O     1 
HETATM 19750 O  O     . HOH EA 11 .    ? -13.881 -0.052  97.147  1.00 43.99 ? 2199 HOH B O     1 
HETATM 19751 O  O     . HOH EA 11 .    ? 11.040  46.522  106.773 1.00 30.97 ? 2200 HOH B O     1 
HETATM 19752 O  O     . HOH EA 11 .    ? 3.770   -3.543  92.813  1.00 44.30 ? 2201 HOH B O     1 
HETATM 19753 O  O     . HOH EA 11 .    ? 29.016  69.361  79.938  1.00 26.18 ? 2202 HOH B O     1 
HETATM 19754 O  O     . HOH EA 11 .    ? 6.854   5.810   92.354  1.00 26.61 ? 2203 HOH B O     1 
HETATM 19755 O  O     . HOH EA 11 .    ? 11.057  18.340  64.655  1.00 27.52 ? 2204 HOH B O     1 
HETATM 19756 O  O     . HOH EA 11 .    ? 5.723   -8.524  114.735 1.00 42.06 ? 2205 HOH B O     1 
HETATM 19757 O  O     . HOH EA 11 .    ? 30.373  50.080  71.538  1.00 33.76 ? 2206 HOH B O     1 
HETATM 19758 O  O     . HOH EA 11 .    ? 9.193   23.332  109.131 1.00 35.79 ? 2207 HOH B O     1 
HETATM 19759 O  O     . HOH EA 11 .    ? -4.646  37.771  94.008  1.00 41.87 ? 2208 HOH B O     1 
HETATM 19760 O  O     . HOH EA 11 .    ? 1.410   20.597  104.731 1.00 36.39 ? 2209 HOH B O     1 
HETATM 19761 O  O     . HOH EA 11 .    ? 18.124  52.743  66.748  1.00 28.11 ? 2210 HOH B O     1 
HETATM 19762 O  O     . HOH EA 11 .    ? 32.666  18.953  57.955  1.00 33.37 ? 2211 HOH B O     1 
HETATM 19763 O  O     . HOH EA 11 .    ? 29.921  27.332  56.098  1.00 25.83 ? 2212 HOH B O     1 
HETATM 19764 O  O     . HOH EA 11 .    ? -12.642 49.289  130.256 1.00 45.84 ? 2213 HOH B O     1 
HETATM 19765 O  O     . HOH EA 11 .    ? 38.805  32.612  84.034  1.00 36.90 ? 2214 HOH B O     1 
HETATM 19766 O  O     . HOH EA 11 .    ? -5.549  -6.397  112.368 1.00 37.96 ? 2215 HOH B O     1 
HETATM 19767 O  O     . HOH EA 11 .    ? 12.743  36.743  86.054  1.00 17.29 ? 2216 HOH B O     1 
HETATM 19768 O  O     . HOH EA 11 .    ? 3.577   33.875  86.768  1.00 21.28 ? 2217 HOH B O     1 
HETATM 19769 O  O     . HOH EA 11 .    ? 12.509  13.057  110.627 1.00 32.36 ? 2218 HOH B O     1 
HETATM 19770 O  O     . HOH EA 11 .    ? 27.408  16.150  93.731  1.00 35.50 ? 2219 HOH B O     1 
HETATM 19771 O  O     . HOH EA 11 .    ? 7.764   65.422  63.852  1.00 30.37 ? 2220 HOH B O     1 
HETATM 19772 O  O     . HOH EA 11 .    ? -10.505 46.561  74.592  1.00 21.89 ? 2221 HOH B O     1 
HETATM 19773 O  O     . HOH EA 11 .    ? 28.231  39.808  50.683  1.00 45.12 ? 2222 HOH B O     1 
HETATM 19774 O  O     . HOH EA 11 .    ? 21.656  30.097  71.376  1.00 20.53 ? 2223 HOH B O     1 
HETATM 19775 O  O     . HOH EA 11 .    ? 25.414  54.914  62.129  1.00 24.06 ? 2224 HOH B O     1 
HETATM 19776 O  O     . HOH EA 11 .    ? 4.177   -8.683  104.532 1.00 32.38 ? 2225 HOH B O     1 
HETATM 19777 O  O     . HOH EA 11 .    ? 15.875  55.540  93.063  1.00 31.43 ? 2226 HOH B O     1 
HETATM 19778 O  O     . HOH EA 11 .    ? 10.233  50.904  64.839  1.00 26.82 ? 2227 HOH B O     1 
HETATM 19779 O  O     . HOH EA 11 .    ? 1.669   57.302  87.742  1.00 38.90 ? 2228 HOH B O     1 
HETATM 19780 O  O     . HOH EA 11 .    ? 31.970  38.440  84.388  1.00 34.91 ? 2229 HOH B O     1 
HETATM 19781 O  O     . HOH EA 11 .    ? -16.719 4.875   116.662 1.00 34.61 ? 2230 HOH B O     1 
HETATM 19782 O  O     . HOH EA 11 .    ? 17.333  40.887  71.559  1.00 21.80 ? 2231 HOH B O     1 
HETATM 19783 O  O     . HOH EA 11 .    ? 1.103   38.831  108.402 1.00 27.89 ? 2232 HOH B O     1 
HETATM 19784 O  O     . HOH EA 11 .    ? 3.799   7.985   92.410  1.00 23.31 ? 2233 HOH B O     1 
HETATM 19785 O  O     . HOH EA 11 .    ? -14.261 39.969  125.041 1.00 43.83 ? 2234 HOH B O     1 
HETATM 19786 O  O     . HOH EA 11 .    ? -18.797 23.695  115.271 1.00 36.12 ? 2235 HOH B O     1 
HETATM 19787 O  O     . HOH EA 11 .    ? 18.172  23.835  110.662 1.00 28.33 ? 2236 HOH B O     1 
HETATM 19788 O  O     . HOH EA 11 .    ? 17.973  68.891  84.696  1.00 37.64 ? 2237 HOH B O     1 
HETATM 19789 O  O     . HOH EA 11 .    ? -6.837  35.342  69.436  1.00 35.34 ? 2238 HOH B O     1 
HETATM 19790 O  O     . HOH EA 11 .    ? 27.884  67.634  68.344  1.00 31.83 ? 2239 HOH B O     1 
HETATM 19791 O  O     . HOH EA 11 .    ? 4.829   35.643  117.635 1.00 46.33 ? 2240 HOH B O     1 
HETATM 19792 O  O     . HOH EA 11 .    ? -5.146  39.969  72.416  1.00 27.68 ? 2241 HOH B O     1 
HETATM 19793 O  O     . HOH EA 11 .    ? -9.461  5.981   87.214  1.00 31.04 ? 2242 HOH B O     1 
HETATM 19794 O  O     . HOH EA 11 .    ? 19.934  19.642  105.783 1.00 21.50 ? 2243 HOH B O     1 
HETATM 19795 O  O     . HOH EA 11 .    ? -4.512  -1.925  97.148  1.00 28.85 ? 2244 HOH B O     1 
HETATM 19796 O  O     . HOH EA 11 .    ? 11.264  5.955   121.978 1.00 35.77 ? 2245 HOH B O     1 
HETATM 19797 O  O     . HOH EA 11 .    ? 22.859  48.631  78.083  1.00 22.83 ? 2246 HOH B O     1 
HETATM 19798 O  O     . HOH EA 11 .    ? -9.398  19.174  81.147  1.00 38.27 ? 2247 HOH B O     1 
HETATM 19799 O  O     . HOH EA 11 .    ? 25.936  55.250  77.483  1.00 28.73 ? 2248 HOH B O     1 
HETATM 19800 O  O     . HOH EA 11 .    ? -32.143 17.390  91.698  1.00 43.43 ? 2249 HOH B O     1 
HETATM 19801 O  O     . HOH EA 11 .    ? 10.912  52.932  104.731 1.00 33.94 ? 2250 HOH B O     1 
HETATM 19802 O  O     . HOH EA 11 .    ? 3.958   55.629  72.845  1.00 27.56 ? 2251 HOH B O     1 
HETATM 19803 O  O     . HOH EA 11 .    ? -13.490 18.013  105.729 1.00 28.50 ? 2252 HOH B O     1 
HETATM 19804 O  O     . HOH EA 11 .    ? -4.047  18.784  98.242  1.00 18.39 ? 2253 HOH B O     1 
HETATM 19805 O  O     . HOH EA 11 .    ? -6.788  8.356   111.192 1.00 27.27 ? 2254 HOH B O     1 
HETATM 19806 O  O     . HOH EA 11 .    ? 22.394  45.591  90.739  1.00 20.54 ? 2255 HOH B O     1 
HETATM 19807 O  O     . HOH EA 11 .    ? -2.146  48.973  63.755  1.00 19.52 ? 2256 HOH B O     1 
HETATM 19808 O  O     . HOH EA 11 .    ? -2.320  4.963   85.161  1.00 34.78 ? 2257 HOH B O     1 
HETATM 19809 O  O     . HOH EA 11 .    ? 15.115  55.940  74.669  1.00 29.47 ? 2258 HOH B O     1 
HETATM 19810 O  O     . HOH EA 11 .    ? 17.221  43.125  79.428  1.00 24.91 ? 2259 HOH B O     1 
HETATM 19811 O  O     . HOH EA 11 .    ? -5.400  5.286   122.272 1.00 29.77 ? 2260 HOH B O     1 
HETATM 19812 O  O     . HOH EA 11 .    ? 6.447   5.805   86.175  1.00 22.61 ? 2261 HOH B O     1 
HETATM 19813 O  O     . HOH EA 11 .    ? 19.830  51.093  77.590  1.00 24.31 ? 2262 HOH B O     1 
HETATM 19814 O  O     . HOH EA 11 .    ? 1.812   13.694  104.901 1.00 20.42 ? 2263 HOH B O     1 
HETATM 19815 O  O     . HOH EA 11 .    ? 6.467   -4.032  104.633 1.00 36.23 ? 2264 HOH B O     1 
HETATM 19816 O  O     . HOH EA 11 .    ? 15.542  53.656  81.963  1.00 29.80 ? 2265 HOH B O     1 
HETATM 19817 O  O     . HOH EA 11 .    ? -6.135  0.374   86.323  1.00 30.40 ? 2266 HOH B O     1 
HETATM 19818 O  O     . HOH EA 11 .    ? -12.525 20.022  84.094  1.00 25.13 ? 2267 HOH B O     1 
HETATM 19819 O  O     . HOH EA 11 .    ? 19.640  5.382   76.874  1.00 33.88 ? 2268 HOH B O     1 
HETATM 19820 O  O     . HOH EA 11 .    ? 30.141  35.311  50.775  1.00 35.17 ? 2269 HOH B O     1 
HETATM 19821 O  O     . HOH EA 11 .    ? 1.811   13.343  102.047 1.00 23.43 ? 2270 HOH B O     1 
HETATM 19822 O  O     . HOH EA 11 .    ? 33.454  19.268  87.434  1.00 27.03 ? 2271 HOH B O     1 
HETATM 19823 O  O     . HOH EA 11 .    ? -1.089  38.303  80.342  1.00 24.93 ? 2272 HOH B O     1 
HETATM 19824 O  O     . HOH EA 11 .    ? 25.270  13.921  65.116  1.00 32.61 ? 2273 HOH B O     1 
HETATM 19825 O  O     . HOH EA 11 .    ? 6.219   50.012  88.436  1.00 39.60 ? 2274 HOH B O     1 
HETATM 19826 O  O     . HOH EA 11 .    ? 13.934  81.230  69.615  1.00 39.89 ? 2275 HOH B O     1 
HETATM 19827 O  O     . HOH EA 11 .    ? 26.410  66.341  57.761  1.00 43.77 ? 2276 HOH B O     1 
HETATM 19828 O  O     . HOH EA 11 .    ? 12.033  11.116  71.603  1.00 25.46 ? 2277 HOH B O     1 
HETATM 19829 O  O     . HOH EA 11 .    ? -12.632 8.891   124.557 1.00 42.58 ? 2278 HOH B O     1 
HETATM 19830 O  O     . HOH EA 11 .    ? -24.890 10.348  87.684  1.00 35.51 ? 2279 HOH B O     1 
HETATM 19831 O  O     . HOH EA 11 .    ? -17.671 54.568  121.458 1.00 41.02 ? 2280 HOH B O     1 
HETATM 19832 O  O     . HOH EA 11 .    ? 26.998  52.653  75.515  1.00 32.08 ? 2281 HOH B O     1 
HETATM 19833 O  O     . HOH EA 11 .    ? 4.367   42.218  84.476  1.00 22.99 ? 2282 HOH B O     1 
HETATM 19834 O  O     . HOH EA 11 .    ? 15.226  40.480  73.271  1.00 20.80 ? 2283 HOH B O     1 
HETATM 19835 O  O     . HOH EA 11 .    ? 2.670   39.515  98.839  1.00 22.78 ? 2284 HOH B O     1 
HETATM 19836 O  O     . HOH EA 11 .    ? 9.133   3.998   80.958  1.00 30.00 ? 2285 HOH B O     1 
HETATM 19837 O  O     . HOH EA 11 .    ? 11.082  19.312  61.466  1.00 27.69 ? 2286 HOH B O     1 
HETATM 19838 O  O     . HOH EA 11 .    ? -2.111  35.640  101.198 1.00 40.01 ? 2287 HOH B O     1 
HETATM 19839 O  O     . HOH EA 11 .    ? -2.276  42.063  61.845  1.00 25.89 ? 2288 HOH B O     1 
HETATM 19840 O  O     . HOH EA 11 .    ? -0.178  56.075  86.494  1.00 38.26 ? 2289 HOH B O     1 
HETATM 19841 O  O     . HOH EA 11 .    ? 18.812  38.583  115.907 1.00 31.86 ? 2290 HOH B O     1 
HETATM 19842 O  O     . HOH EA 11 .    ? -26.756 14.639  100.679 1.00 41.78 ? 2291 HOH B O     1 
HETATM 19843 O  O     . HOH EA 11 .    ? 23.353  52.066  62.442  1.00 24.67 ? 2292 HOH B O     1 
HETATM 19844 O  O     . HOH EA 11 .    ? -2.250  39.590  87.345  1.00 19.79 ? 2293 HOH B O     1 
HETATM 19845 O  O     . HOH EA 11 .    ? -4.565  50.702  78.656  1.00 31.53 ? 2294 HOH B O     1 
HETATM 19846 O  O     . HOH EA 11 .    ? -4.850  30.839  77.453  1.00 19.43 ? 2295 HOH B O     1 
HETATM 19847 O  O     . HOH EA 11 .    ? -1.036  -2.678  119.090 1.00 42.86 ? 2296 HOH B O     1 
HETATM 19848 O  O     . HOH EA 11 .    ? 4.934   49.489  68.772  1.00 25.18 ? 2297 HOH B O     1 
HETATM 19849 O  O     . HOH EA 11 .    ? -29.031 22.880  90.341  1.00 47.18 ? 2298 HOH B O     1 
HETATM 19850 O  O     . HOH EA 11 .    ? 11.349  38.242  96.039  1.00 30.06 ? 2299 HOH B O     1 
HETATM 19851 O  O     . HOH EA 11 .    ? -6.217  51.132  73.139  1.00 16.80 ? 2300 HOH B O     1 
HETATM 19852 O  O     . HOH EA 11 .    ? -5.031  42.781  72.791  1.00 33.52 ? 2301 HOH B O     1 
HETATM 19853 O  O     . HOH EA 11 .    ? 22.882  37.391  86.139  1.00 21.05 ? 2302 HOH B O     1 
HETATM 19854 O  O     . HOH EA 11 .    ? 33.742  67.888  80.755  1.00 22.88 ? 2303 HOH B O     1 
HETATM 19855 O  O     . HOH EA 11 .    ? 0.375   36.185  109.053 1.00 35.75 ? 2304 HOH B O     1 
HETATM 19856 O  O     . HOH EA 11 .    ? -18.333 8.291   122.274 1.00 38.77 ? 2305 HOH B O     1 
HETATM 19857 O  O     . HOH EA 11 .    ? 21.473  50.552  87.736  1.00 28.80 ? 2306 HOH B O     1 
HETATM 19858 O  O     . HOH EA 11 .    ? 15.166  20.954  92.587  1.00 31.89 ? 2307 HOH B O     1 
HETATM 19859 O  O     . HOH EA 11 .    ? 1.061   42.256  76.378  1.00 26.45 ? 2308 HOH B O     1 
HETATM 19860 O  O     . HOH EA 11 .    ? 11.798  16.592  67.630  1.00 36.40 ? 2309 HOH B O     1 
HETATM 19861 O  O     . HOH EA 11 .    ? -10.113 32.441  89.222  1.00 24.44 ? 2310 HOH B O     1 
HETATM 19862 O  O     . HOH EA 11 .    ? -5.046  -1.708  123.846 1.00 40.16 ? 2311 HOH B O     1 
HETATM 19863 O  O     . HOH EA 11 .    ? 31.028  25.962  52.864  1.00 38.92 ? 2312 HOH B O     1 
HETATM 19864 O  O     . HOH EA 11 .    ? -2.328  43.075  58.413  1.00 36.51 ? 2313 HOH B O     1 
HETATM 19865 O  O     . HOH EA 11 .    ? 3.634   14.277  72.847  1.00 40.49 ? 2314 HOH B O     1 
HETATM 19866 O  O     . HOH EA 11 .    ? -2.290  24.210  76.551  1.00 27.53 ? 2315 HOH B O     1 
HETATM 19867 O  O     . HOH EA 11 .    ? -10.105 39.867  127.623 1.00 44.35 ? 2316 HOH B O     1 
HETATM 19868 O  O     . HOH EA 11 .    ? 26.738  22.077  75.302  1.00 28.25 ? 2317 HOH B O     1 
HETATM 19869 O  O     . HOH EA 11 .    ? 21.948  53.283  67.274  1.00 29.18 ? 2318 HOH B O     1 
HETATM 19870 O  O     . HOH EA 11 .    ? 6.060   48.082  110.826 1.00 33.77 ? 2319 HOH B O     1 
HETATM 19871 O  O     . HOH EA 11 .    ? 31.282  28.957  77.717  1.00 29.57 ? 2320 HOH B O     1 
HETATM 19872 O  O     . HOH EA 11 .    ? -7.967  27.213  100.013 1.00 32.02 ? 2321 HOH B O     1 
HETATM 19873 O  O     . HOH EA 11 .    ? -7.735  20.204  79.575  1.00 41.17 ? 2322 HOH B O     1 
HETATM 19874 O  O     . HOH EA 11 .    ? -5.008  9.817   115.228 1.00 29.81 ? 2323 HOH B O     1 
HETATM 19875 O  O     . HOH EA 11 .    ? 15.447  16.820  87.967  1.00 26.60 ? 2324 HOH B O     1 
HETATM 19876 O  O     . HOH EA 11 .    ? -5.472  55.407  78.769  1.00 27.47 ? 2325 HOH B O     1 
HETATM 19877 O  O     . HOH EA 11 .    ? 3.861   56.380  62.908  1.00 42.68 ? 2326 HOH B O     1 
HETATM 19878 O  O     . HOH EA 11 .    ? 32.688  21.244  96.717  1.00 46.75 ? 2327 HOH B O     1 
HETATM 19879 O  O     . HOH EA 11 .    ? -0.501  24.057  74.264  1.00 20.82 ? 2328 HOH B O     1 
HETATM 19880 O  O     . HOH EA 11 .    ? 17.327  27.469  82.851  1.00 30.85 ? 2329 HOH B O     1 
HETATM 19881 O  O     . HOH EA 11 .    ? -4.617  43.961  81.133  1.00 36.44 ? 2330 HOH B O     1 
HETATM 19882 O  O     . HOH EA 11 .    ? 12.022  38.239  47.610  1.00 35.62 ? 2331 HOH B O     1 
HETATM 19883 O  O     . HOH EA 11 .    ? -10.854 1.943   121.895 1.00 30.69 ? 2332 HOH B O     1 
HETATM 19884 O  O     . HOH EA 11 .    ? -2.391  45.339  102.793 1.00 37.11 ? 2333 HOH B O     1 
HETATM 19885 O  O     . HOH EA 11 .    ? -5.772  39.350  106.901 1.00 31.88 ? 2334 HOH B O     1 
HETATM 19886 O  O     . HOH EA 11 .    ? 7.807   56.755  87.786  1.00 35.52 ? 2335 HOH B O     1 
HETATM 19887 O  O     . HOH EA 11 .    ? 7.268   33.953  86.656  1.00 20.98 ? 2336 HOH B O     1 
HETATM 19888 O  O     . HOH EA 11 .    ? -17.535 26.143  83.135  1.00 44.96 ? 2337 HOH B O     1 
HETATM 19889 O  O     . HOH EA 11 .    ? -10.408 25.527  103.125 1.00 42.46 ? 2338 HOH B O     1 
HETATM 19890 O  O     . HOH EA 11 .    ? 26.998  49.011  94.731  1.00 34.26 ? 2339 HOH B O     1 
HETATM 19891 O  O     . HOH EA 11 .    ? -5.082  51.714  75.653  1.00 22.92 ? 2340 HOH B O     1 
HETATM 19892 O  O     . HOH EA 11 .    ? 19.218  79.366  68.653  1.00 34.76 ? 2341 HOH B O     1 
HETATM 19893 O  O     . HOH EA 11 .    ? 33.345  26.352  59.015  1.00 27.94 ? 2342 HOH B O     1 
HETATM 19894 O  O     . HOH EA 11 .    ? 9.917   43.840  110.335 1.00 29.42 ? 2343 HOH B O     1 
HETATM 19895 O  O     . HOH EA 11 .    ? 20.709  27.559  71.180  1.00 18.80 ? 2344 HOH B O     1 
HETATM 19896 O  O     . HOH EA 11 .    ? -0.276  75.778  68.198  1.00 40.32 ? 2345 HOH B O     1 
HETATM 19897 O  O     . HOH EA 11 .    ? 26.649  20.568  55.710  1.00 34.30 ? 2346 HOH B O     1 
HETATM 19898 O  O     . HOH EA 11 .    ? -11.666 18.290  126.776 1.00 30.43 ? 2347 HOH B O     1 
HETATM 19899 O  O     . HOH EA 11 .    ? 23.223  10.342  85.186  1.00 42.50 ? 2348 HOH B O     1 
HETATM 19900 O  O     . HOH EA 11 .    ? 24.223  19.118  98.464  1.00 33.46 ? 2349 HOH B O     1 
HETATM 19901 O  O     . HOH EA 11 .    ? 18.106  23.402  88.264  1.00 27.81 ? 2350 HOH B O     1 
HETATM 19902 O  O     . HOH EA 11 .    ? -2.753  -2.284  94.750  1.00 31.56 ? 2351 HOH B O     1 
HETATM 19903 O  O     . HOH EA 11 .    ? -4.468  10.912  100.547 1.00 21.80 ? 2352 HOH B O     1 
HETATM 19904 O  O     . HOH EA 11 .    ? -1.494  31.566  125.635 1.00 41.12 ? 2353 HOH B O     1 
HETATM 19905 O  O     . HOH EA 11 .    ? 9.818   71.417  61.838  1.00 32.73 ? 2354 HOH B O     1 
HETATM 19906 O  O     . HOH EA 11 .    ? 18.912  45.362  53.926  1.00 32.58 ? 2355 HOH B O     1 
HETATM 19907 O  O     . HOH EA 11 .    ? 17.330  54.998  97.404  1.00 29.28 ? 2356 HOH B O     1 
HETATM 19908 O  O     . HOH EA 11 .    ? -1.343  32.793  69.211  1.00 17.01 ? 2357 HOH B O     1 
HETATM 19909 O  O     . HOH EA 11 .    ? 0.094   4.396   88.627  1.00 26.61 ? 2358 HOH B O     1 
HETATM 19910 O  O     . HOH EA 11 .    ? 26.176  47.482  100.274 1.00 37.69 ? 2359 HOH B O     1 
HETATM 19911 O  O     . HOH EA 11 .    ? 2.860   11.793  94.567  1.00 21.05 ? 2360 HOH B O     1 
HETATM 19912 O  O     . HOH EA 11 .    ? 1.694   6.254   91.893  1.00 23.10 ? 2361 HOH B O     1 
HETATM 19913 O  O     . HOH EA 11 .    ? 20.117  43.550  87.932  1.00 16.72 ? 2362 HOH B O     1 
HETATM 19914 O  O     . HOH EA 11 .    ? 8.215   30.232  85.240  1.00 36.64 ? 2363 HOH B O     1 
HETATM 19915 O  O     . HOH EA 11 .    ? 1.251   10.677  129.595 1.00 30.84 ? 2364 HOH B O     1 
HETATM 19916 O  O     . HOH EA 11 .    ? -7.786  30.080  75.991  1.00 26.84 ? 2365 HOH B O     1 
HETATM 19917 O  O     . HOH EA 11 .    ? 16.879  53.126  64.168  1.00 33.73 ? 2366 HOH B O     1 
HETATM 19918 O  O     . HOH EA 11 .    ? 1.140   55.644  110.597 1.00 30.20 ? 2367 HOH B O     1 
HETATM 19919 O  O     . HOH EA 11 .    ? 18.345  43.759  91.611  1.00 17.16 ? 2368 HOH B O     1 
HETATM 19920 O  O     . HOH EA 11 .    ? 2.653   30.727  80.219  1.00 20.59 ? 2369 HOH B O     1 
HETATM 19921 O  O     . HOH EA 11 .    ? -7.900  12.493  97.258  1.00 19.93 ? 2370 HOH B O     1 
HETATM 19922 O  O     . HOH EA 11 .    ? 31.775  59.268  72.155  1.00 28.56 ? 2371 HOH B O     1 
HETATM 19923 O  O     . HOH EA 11 .    ? 7.694   49.136  106.734 1.00 23.81 ? 2372 HOH B O     1 
HETATM 19924 O  O     . HOH EA 11 .    ? -3.254  10.750  84.517  1.00 28.86 ? 2373 HOH B O     1 
HETATM 19925 O  O     . HOH EA 11 .    ? 23.415  48.568  106.878 1.00 34.79 ? 2374 HOH B O     1 
HETATM 19926 O  O     . HOH EA 11 .    ? -1.747  2.593   125.975 1.00 31.32 ? 2375 HOH B O     1 
HETATM 19927 O  O     . HOH EA 11 .    ? 7.690   45.056  75.278  1.00 17.97 ? 2376 HOH B O     1 
HETATM 19928 O  O     . HOH EA 11 .    ? -6.559  52.601  107.317 1.00 34.20 ? 2377 HOH B O     1 
HETATM 19929 O  O     . HOH EA 11 .    ? 25.962  8.728   78.854  1.00 38.40 ? 2378 HOH B O     1 
HETATM 19930 O  O     . HOH EA 11 .    ? 3.999   29.644  84.690  1.00 21.94 ? 2379 HOH B O     1 
HETATM 19931 O  O     . HOH EA 11 .    ? 18.759  7.552   100.769 1.00 37.40 ? 2380 HOH B O     1 
HETATM 19932 O  O     . HOH EA 11 .    ? -11.276 20.497  88.273  1.00 25.98 ? 2381 HOH B O     1 
HETATM 19933 O  O     . HOH EA 11 .    ? 17.315  49.030  59.212  1.00 26.12 ? 2382 HOH B O     1 
HETATM 19934 O  O     . HOH EA 11 .    ? 4.090   65.117  66.329  1.00 44.90 ? 2383 HOH B O     1 
HETATM 19935 O  O     . HOH EA 11 .    ? 23.838  26.142  50.613  1.00 29.23 ? 2384 HOH B O     1 
HETATM 19936 O  O     . HOH EA 11 .    ? 31.206  21.429  79.844  1.00 22.73 ? 2385 HOH B O     1 
HETATM 19937 O  O     . HOH EA 11 .    ? 23.520  65.270  82.224  1.00 41.02 ? 2386 HOH B O     1 
HETATM 19938 O  O     . HOH EA 11 .    ? 22.395  12.017  71.421  1.00 29.92 ? 2387 HOH B O     1 
HETATM 19939 O  O     . HOH EA 11 .    ? 23.480  56.036  99.239  1.00 34.06 ? 2388 HOH B O     1 
HETATM 19940 O  O     . HOH EA 11 .    ? 31.612  53.981  67.898  1.00 28.80 ? 2389 HOH B O     1 
HETATM 19941 O  O     . HOH EA 11 .    ? 0.211   28.114  122.268 1.00 43.24 ? 2390 HOH B O     1 
HETATM 19942 O  O     . HOH EA 11 .    ? 10.509  51.508  75.606  1.00 27.70 ? 2391 HOH B O     1 
HETATM 19943 O  O     . HOH EA 11 .    ? 6.593   16.471  121.575 1.00 35.14 ? 2392 HOH B O     1 
HETATM 19944 O  O     . HOH EA 11 .    ? 28.432  18.724  57.795  1.00 36.55 ? 2393 HOH B O     1 
HETATM 19945 O  O     . HOH EA 11 .    ? 31.656  60.201  65.416  1.00 31.04 ? 2394 HOH B O     1 
HETATM 19946 O  O     . HOH EA 11 .    ? -0.416  27.119  68.621  1.00 19.74 ? 2395 HOH B O     1 
HETATM 19947 O  O     . HOH EA 11 .    ? 5.769   55.716  104.838 1.00 25.83 ? 2396 HOH B O     1 
HETATM 19948 O  O     . HOH EA 11 .    ? 11.539  24.970  108.468 1.00 36.10 ? 2397 HOH B O     1 
HETATM 19949 O  O     . HOH EA 11 .    ? 2.793   32.984  78.606  1.00 17.73 ? 2398 HOH B O     1 
HETATM 19950 O  O     . HOH EA 11 .    ? 18.593  13.484  74.377  1.00 29.69 ? 2399 HOH B O     1 
HETATM 19951 O  O     . HOH EA 11 .    ? 7.771   74.570  62.243  1.00 42.79 ? 2400 HOH B O     1 
HETATM 19952 O  O     . HOH EA 11 .    ? 0.168   40.229  77.890  1.00 28.17 ? 2401 HOH B O     1 
HETATM 19953 O  O     . HOH EA 11 .    ? 7.056   42.853  49.695  1.00 29.20 ? 2402 HOH B O     1 
HETATM 19954 O  O     . HOH EA 11 .    ? 14.709  25.741  110.602 1.00 42.58 ? 2403 HOH B O     1 
HETATM 19955 O  O     . HOH EA 11 .    ? 16.474  46.409  54.489  1.00 38.38 ? 2404 HOH B O     1 
HETATM 19956 O  O     . HOH EA 11 .    ? 12.415  21.564  101.661 1.00 29.78 ? 2405 HOH B O     1 
HETATM 19957 O  O     . HOH EA 11 .    ? 7.932   65.934  68.780  1.00 34.30 ? 2406 HOH B O     1 
HETATM 19958 O  O     . HOH EA 11 .    ? -1.722  11.315  101.473 1.00 22.06 ? 2407 HOH B O     1 
HETATM 19959 O  O     . HOH EA 11 .    ? 6.898   7.930   75.202  1.00 31.27 ? 2408 HOH B O     1 
HETATM 19960 O  O     . HOH EA 11 .    ? -0.217  16.491  112.080 1.00 36.76 ? 2409 HOH B O     1 
HETATM 19961 O  O     . HOH EA 11 .    ? -4.293  59.998  125.603 1.00 31.72 ? 2410 HOH B O     1 
HETATM 19962 O  O     . HOH EA 11 .    ? 32.972  46.086  67.112  1.00 33.63 ? 2411 HOH B O     1 
HETATM 19963 O  O     . HOH EA 11 .    ? -5.834  40.379  62.794  1.00 36.17 ? 2412 HOH B O     1 
HETATM 19964 O  O     . HOH EA 11 .    ? 22.400  24.663  108.712 1.00 28.97 ? 2413 HOH B O     1 
HETATM 19965 O  O     . HOH EA 11 .    ? -2.436  21.511  91.740  1.00 18.90 ? 2414 HOH B O     1 
HETATM 19966 O  O     . HOH EA 11 .    ? -21.033 15.504  82.833  1.00 33.36 ? 2415 HOH B O     1 
HETATM 19967 O  O     . HOH EA 11 .    ? 3.739   33.759  93.117  1.00 21.26 ? 2416 HOH B O     1 
HETATM 19968 O  O     . HOH EA 11 .    ? 19.084  70.719  59.188  1.00 42.49 ? 2417 HOH B O     1 
HETATM 19969 O  O     . HOH EA 11 .    ? 20.849  5.158   68.043  1.00 38.35 ? 2418 HOH B O     1 
HETATM 19970 O  O     . HOH EA 11 .    ? 8.200   13.846  71.601  1.00 26.14 ? 2419 HOH B O     1 
HETATM 19971 O  O     . HOH EA 11 .    ? 1.017   30.924  74.837  1.00 20.19 ? 2420 HOH B O     1 
HETATM 19972 O  O     . HOH EA 11 .    ? 16.165  43.252  50.486  1.00 31.45 ? 2421 HOH B O     1 
HETATM 19973 O  O     . HOH EA 11 .    ? 12.641  2.110   111.416 1.00 33.55 ? 2422 HOH B O     1 
HETATM 19974 O  O     . HOH EA 11 .    ? 29.388  58.492  82.430  1.00 43.99 ? 2423 HOH B O     1 
HETATM 19975 O  O     . HOH EA 11 .    ? 27.395  38.026  90.050  1.00 23.74 ? 2424 HOH B O     1 
HETATM 19976 O  O     . HOH EA 11 .    ? -13.820 -7.922  103.453 1.00 42.09 ? 2425 HOH B O     1 
HETATM 19977 O  O     . HOH EA 11 .    ? 14.799  22.579  101.989 1.00 25.46 ? 2426 HOH B O     1 
HETATM 19978 O  O     . HOH EA 11 .    ? -2.351  18.464  106.046 1.00 30.88 ? 2427 HOH B O     1 
HETATM 19979 O  O     . HOH EA 11 .    ? 12.914  50.115  65.046  1.00 28.95 ? 2428 HOH B O     1 
HETATM 19980 O  O     . HOH EA 11 .    ? 2.588   70.194  64.354  1.00 38.16 ? 2429 HOH B O     1 
HETATM 19981 O  O     . HOH EA 11 .    ? 24.101  68.929  67.510  1.00 26.17 ? 2430 HOH B O     1 
HETATM 19982 O  O     . HOH EA 11 .    ? 18.908  34.671  46.120  1.00 39.85 ? 2431 HOH B O     1 
HETATM 19983 O  O     . HOH EA 11 .    ? 0.213   -7.192  107.223 1.00 33.89 ? 2432 HOH B O     1 
HETATM 19984 O  O     . HOH EA 11 .    ? 11.165  20.244  120.735 1.00 35.65 ? 2433 HOH B O     1 
HETATM 19985 O  O     . HOH EA 11 .    ? -0.966  55.572  72.468  1.00 31.23 ? 2434 HOH B O     1 
HETATM 19986 O  O     . HOH EA 11 .    ? 25.671  33.315  110.465 1.00 42.98 ? 2435 HOH B O     1 
HETATM 19987 O  O     . HOH EA 11 .    ? 10.165  2.627   117.559 1.00 35.11 ? 2436 HOH B O     1 
HETATM 19988 O  O     . HOH EA 11 .    ? 2.806   3.782   84.794  1.00 40.07 ? 2437 HOH B O     1 
HETATM 19989 O  O     . HOH EA 11 .    ? 16.145  69.746  55.349  1.00 49.75 ? 2438 HOH B O     1 
HETATM 19990 O  O     . HOH EA 11 .    ? 25.417  30.079  108.923 1.00 44.14 ? 2439 HOH B O     1 
HETATM 19991 O  O     . HOH EA 11 .    ? -14.588 6.161   117.677 1.00 31.89 ? 2440 HOH B O     1 
HETATM 19992 O  O     . HOH EA 11 .    ? 2.839   46.030  53.920  1.00 40.96 ? 2441 HOH B O     1 
HETATM 19993 O  O     . HOH EA 11 .    ? -7.173  15.783  81.745  1.00 35.57 ? 2442 HOH B O     1 
HETATM 19994 O  O     . HOH EA 11 .    ? -1.329  67.284  75.555  1.00 29.16 ? 2443 HOH B O     1 
HETATM 19995 O  O     . HOH EA 11 .    ? 20.409  50.722  67.234  1.00 34.56 ? 2444 HOH B O     1 
HETATM 19996 O  O     . HOH EA 11 .    ? 0.272   12.450  93.875  1.00 18.33 ? 2445 HOH B O     1 
HETATM 19997 O  O     . HOH EA 11 .    ? 28.189  29.664  83.284  1.00 21.09 ? 2446 HOH B O     1 
HETATM 19998 O  O     . HOH EA 11 .    ? 11.829  37.417  72.417  1.00 17.75 ? 2447 HOH B O     1 
HETATM 19999 O  O     . HOH EA 11 .    ? 20.499  75.355  62.887  1.00 45.69 ? 2448 HOH B O     1 
HETATM 20000 O  O     . HOH EA 11 .    ? 13.214  25.982  96.511  1.00 31.85 ? 2449 HOH B O     1 
HETATM 20001 O  O     . HOH EA 11 .    ? 19.852  33.004  67.422  1.00 17.67 ? 2450 HOH B O     1 
HETATM 20002 O  O     . HOH EA 11 .    ? 29.009  22.876  76.474  1.00 22.90 ? 2451 HOH B O     1 
HETATM 20003 O  O     . HOH EA 11 .    ? 0.367   20.301  69.909  1.00 28.47 ? 2452 HOH B O     1 
HETATM 20004 O  O     . HOH EA 11 .    ? 18.677  9.158   91.982  1.00 43.51 ? 2453 HOH B O     1 
HETATM 20005 O  O     . HOH EA 11 .    ? 3.852   19.305  60.428  1.00 36.52 ? 2454 HOH B O     1 
HETATM 20006 O  O     . HOH EA 11 .    ? 25.505  53.940  73.765  1.00 25.20 ? 2455 HOH B O     1 
HETATM 20007 O  O     . HOH EA 11 .    ? 16.130  16.004  85.246  1.00 26.04 ? 2456 HOH B O     1 
HETATM 20008 O  O     . HOH EA 11 .    ? 26.475  22.657  50.298  1.00 39.04 ? 2457 HOH B O     1 
HETATM 20009 O  O     . HOH EA 11 .    ? -1.234  5.481   92.244  1.00 21.57 ? 2458 HOH B O     1 
HETATM 20010 O  O     . HOH EA 11 .    ? 0.279   47.823  76.638  1.00 21.54 ? 2459 HOH B O     1 
HETATM 20011 O  O     . HOH EA 11 .    ? 4.979   63.053  84.400  1.00 21.94 ? 2460 HOH B O     1 
HETATM 20012 O  O     . HOH EA 11 .    ? 28.380  13.409  85.927  1.00 30.97 ? 2461 HOH B O     1 
HETATM 20013 O  O     . HOH EA 11 .    ? -23.565 23.186  84.593  1.00 41.90 ? 2462 HOH B O     1 
HETATM 20014 O  O     . HOH EA 11 .    ? 22.034  25.171  82.764  1.00 32.09 ? 2463 HOH B O     1 
HETATM 20015 O  O     . HOH EA 11 .    ? -5.587  -7.313  116.067 1.00 36.92 ? 2464 HOH B O     1 
HETATM 20016 O  O     . HOH EA 11 .    ? 41.320  34.477  91.459  1.00 30.16 ? 2465 HOH B O     1 
HETATM 20017 O  O     . HOH EA 11 .    ? 22.850  23.559  84.766  1.00 22.98 ? 2466 HOH B O     1 
HETATM 20018 O  O     . HOH EA 11 .    ? 13.965  72.434  61.177  1.00 30.64 ? 2467 HOH B O     1 
HETATM 20019 O  O     . HOH EA 11 .    ? 2.592   53.829  69.616  1.00 31.74 ? 2468 HOH B O     1 
HETATM 20020 O  O     . HOH EA 11 .    ? 30.261  33.356  73.408  1.00 35.99 ? 2469 HOH B O     1 
HETATM 20021 O  O     . HOH EA 11 .    ? 12.257  7.891   90.506  1.00 26.01 ? 2470 HOH B O     1 
HETATM 20022 O  O     . HOH EA 11 .    ? 37.555  31.208  81.761  1.00 31.95 ? 2471 HOH B O     1 
HETATM 20023 O  O     . HOH EA 11 .    ? -9.191  10.028  123.197 1.00 28.82 ? 2472 HOH B O     1 
HETATM 20024 O  O     . HOH EA 11 .    ? 6.614   82.035  75.635  1.00 36.10 ? 2473 HOH B O     1 
HETATM 20025 O  O     . HOH EA 11 .    ? 11.397  41.533  54.618  1.00 23.29 ? 2474 HOH B O     1 
HETATM 20026 O  O     . HOH EA 11 .    ? 30.688  40.478  57.253  1.00 28.93 ? 2475 HOH B O     1 
HETATM 20027 O  O     . HOH EA 11 .    ? 26.489  37.148  106.911 1.00 37.80 ? 2476 HOH B O     1 
HETATM 20028 O  O     . HOH EA 11 .    ? 5.406   3.546   93.145  1.00 26.23 ? 2477 HOH B O     1 
HETATM 20029 O  O     . HOH EA 11 .    ? 23.046  72.881  64.917  1.00 36.87 ? 2478 HOH B O     1 
HETATM 20030 O  O     . HOH EA 11 .    ? -8.772  24.063  101.014 1.00 21.68 ? 2479 HOH B O     1 
HETATM 20031 O  O     . HOH EA 11 .    ? 9.905   -0.160  90.343  1.00 40.72 ? 2480 HOH B O     1 
HETATM 20032 O  O     . HOH EA 11 .    ? 1.846   20.753  89.827  1.00 24.74 ? 2481 HOH B O     1 
HETATM 20033 O  O     . HOH EA 11 .    ? 30.064  20.284  76.845  1.00 31.23 ? 2482 HOH B O     1 
HETATM 20034 O  O     . HOH EA 11 .    ? -17.856 1.785   95.772  1.00 45.32 ? 2483 HOH B O     1 
HETATM 20035 O  O     . HOH EA 11 .    ? 21.463  53.830  83.739  1.00 30.74 ? 2484 HOH B O     1 
HETATM 20036 O  O     . HOH EA 11 .    ? 3.613   41.066  117.320 1.00 30.92 ? 2485 HOH B O     1 
HETATM 20037 O  O     . HOH EA 11 .    ? 13.833  26.845  82.552  1.00 30.46 ? 2486 HOH B O     1 
HETATM 20038 O  O     . HOH EA 11 .    ? 11.719  34.638  52.172  1.00 32.99 ? 2487 HOH B O     1 
HETATM 20039 O  O     . HOH EA 11 .    ? 15.896  4.053   98.707  1.00 35.11 ? 2488 HOH B O     1 
HETATM 20040 O  O     . HOH EA 11 .    ? 19.068  5.917   74.316  1.00 29.92 ? 2489 HOH B O     1 
HETATM 20041 O  O     . HOH EA 11 .    ? 10.875  9.138   69.892  1.00 34.12 ? 2490 HOH B O     1 
HETATM 20042 O  O     . HOH EA 11 .    ? 33.119  58.053  74.157  1.00 33.33 ? 2491 HOH B O     1 
HETATM 20043 O  O     . HOH EA 11 .    ? 16.622  21.777  100.015 1.00 25.67 ? 2492 HOH B O     1 
HETATM 20044 O  O     . HOH EA 11 .    ? -7.604  24.055  125.309 1.00 42.37 ? 2493 HOH B O     1 
HETATM 20045 O  O     . HOH EA 11 .    ? -4.701  37.230  98.805  1.00 38.88 ? 2494 HOH B O     1 
HETATM 20046 O  O     . HOH EA 11 .    ? -1.040  51.077  65.103  1.00 20.71 ? 2495 HOH B O     1 
HETATM 20047 O  O     . HOH EA 11 .    ? 12.695  37.413  108.026 1.00 24.52 ? 2496 HOH B O     1 
HETATM 20048 O  O     . HOH EA 11 .    ? -4.721  37.091  90.003  1.00 31.70 ? 2497 HOH B O     1 
HETATM 20049 O  O     . HOH EA 11 .    ? 7.171   -7.998  107.365 1.00 39.72 ? 2498 HOH B O     1 
HETATM 20050 O  O     . HOH EA 11 .    ? -1.215  66.823  84.051  1.00 30.07 ? 2499 HOH B O     1 
HETATM 20051 O  O     . HOH EA 11 .    ? 27.127  59.253  78.590  1.00 22.72 ? 2500 HOH B O     1 
HETATM 20052 O  O     . HOH EA 11 .    ? 39.810  29.485  87.936  1.00 27.95 ? 2501 HOH B O     1 
HETATM 20053 O  O     . HOH EA 11 .    ? -6.119  34.497  83.921  1.00 25.27 ? 2502 HOH B O     1 
HETATM 20054 O  O     . HOH EA 11 .    ? 16.338  10.710  112.612 1.00 45.66 ? 2503 HOH B O     1 
HETATM 20055 O  O     . HOH EA 11 .    ? 8.524   40.830  86.957  1.00 18.14 ? 2504 HOH B O     1 
HETATM 20056 O  O     . HOH EA 11 .    ? 4.373   19.677  97.335  1.00 40.86 ? 2505 HOH B O     1 
HETATM 20057 O  O     . HOH EA 11 .    ? -2.564  62.947  85.644  1.00 26.85 ? 2506 HOH B O     1 
HETATM 20058 O  O     . HOH EA 11 .    ? 19.723  19.180  66.322  1.00 18.50 ? 2507 HOH B O     1 
HETATM 20059 O  O     . HOH EA 11 .    ? -7.910  2.473   92.495  1.00 25.84 ? 2508 HOH B O     1 
HETATM 20060 O  O     . HOH EA 11 .    ? 23.570  11.853  90.087  1.00 40.94 ? 2509 HOH B O     1 
HETATM 20061 O  O     . HOH EA 11 .    ? 1.411   38.792  105.653 1.00 32.70 ? 2510 HOH B O     1 
HETATM 20062 O  O     . HOH EA 11 .    ? 34.973  64.716  81.466  1.00 22.52 ? 2511 HOH B O     1 
HETATM 20063 O  O     . HOH EA 11 .    ? 1.579   49.425  89.542  1.00 39.86 ? 2512 HOH B O     1 
HETATM 20064 O  O     . HOH EA 11 .    ? 2.271   62.136  68.998  1.00 38.54 ? 2513 HOH B O     1 
HETATM 20065 O  O     . HOH EA 11 .    ? 21.164  37.622  112.707 1.00 23.82 ? 2514 HOH B O     1 
HETATM 20066 O  O     . HOH EA 11 .    ? 2.940   44.599  58.486  1.00 33.15 ? 2515 HOH B O     1 
HETATM 20067 O  O     . HOH EA 11 .    ? 19.945  24.396  46.192  1.00 24.78 ? 2516 HOH B O     1 
HETATM 20068 O  O     . HOH EA 11 .    ? -0.057  39.538  131.540 1.00 40.74 ? 2517 HOH B O     1 
HETATM 20069 O  O     . HOH EA 11 .    ? 2.295   41.777  54.142  1.00 29.06 ? 2518 HOH B O     1 
HETATM 20070 O  O     . HOH EA 11 .    ? 7.391   37.868  103.001 1.00 26.56 ? 2519 HOH B O     1 
HETATM 20071 O  O     . HOH EA 11 .    ? 20.756  22.781  86.502  1.00 28.41 ? 2520 HOH B O     1 
HETATM 20072 O  O     . HOH EA 11 .    ? 11.335  49.356  76.628  1.00 34.93 ? 2521 HOH B O     1 
HETATM 20073 O  O     . HOH EA 11 .    ? 1.012   28.921  83.054  1.00 16.68 ? 2522 HOH B O     1 
HETATM 20074 O  O     . HOH EA 11 .    ? 18.763  62.244  57.533  1.00 37.09 ? 2523 HOH B O     1 
HETATM 20075 O  O     . HOH EA 11 .    ? 25.666  69.415  81.789  1.00 37.98 ? 2524 HOH B O     1 
HETATM 20076 O  O     . HOH EA 11 .    ? 15.344  54.090  66.425  1.00 33.64 ? 2525 HOH B O     1 
HETATM 20077 O  O     . HOH EA 11 .    ? 19.571  54.861  93.652  1.00 26.34 ? 2526 HOH B O     1 
HETATM 20078 O  O     . HOH EA 11 .    ? -13.502 11.884  91.379  1.00 22.72 ? 2527 HOH B O     1 
HETATM 20079 O  O     . HOH EA 11 .    ? -14.444 15.481  78.741  1.00 37.34 ? 2528 HOH B O     1 
HETATM 20080 O  O     . HOH EA 11 .    ? 11.980  49.723  88.684  1.00 23.30 ? 2529 HOH B O     1 
HETATM 20081 O  O     . HOH EA 11 .    ? 22.834  67.420  64.709  1.00 26.06 ? 2530 HOH B O     1 
HETATM 20082 O  O     . HOH EA 11 .    ? -2.908  31.127  63.686  1.00 27.72 ? 2531 HOH B O     1 
HETATM 20083 O  O     . HOH EA 11 .    ? 1.574   15.254  82.466  1.00 22.22 ? 2532 HOH B O     1 
HETATM 20084 O  O     . HOH EA 11 .    ? -30.812 20.832  83.989  1.00 44.25 ? 2533 HOH B O     1 
HETATM 20085 O  O     . HOH EA 11 .    ? -5.974  41.696  84.182  1.00 36.96 ? 2534 HOH B O     1 
HETATM 20086 O  O     . HOH EA 11 .    ? -3.257  -11.165 101.060 1.00 30.14 ? 2535 HOH B O     1 
HETATM 20087 O  O     . HOH EA 11 .    ? 12.714  2.353   92.209  1.00 41.49 ? 2536 HOH B O     1 
HETATM 20088 O  O     . HOH EA 11 .    ? 17.591  28.716  111.067 1.00 32.04 ? 2537 HOH B O     1 
HETATM 20089 O  O     . HOH EA 11 .    ? 5.754   7.368   94.352  1.00 25.74 ? 2538 HOH B O     1 
HETATM 20090 O  O     . HOH EA 11 .    ? -2.848  10.987  103.934 1.00 20.48 ? 2539 HOH B O     1 
HETATM 20091 O  O     . HOH EA 11 .    ? 2.459   63.338  78.547  1.00 20.02 ? 2540 HOH B O     1 
HETATM 20092 O  O     . HOH EA 11 .    ? -7.570  25.630  103.975 1.00 37.36 ? 2541 HOH B O     1 
HETATM 20093 O  O     . HOH EA 11 .    ? -6.540  14.326  91.632  1.00 21.56 ? 2542 HOH B O     1 
HETATM 20094 O  O     . HOH EA 11 .    ? 36.606  20.889  78.517  1.00 45.11 ? 2543 HOH B O     1 
HETATM 20095 O  O     . HOH EA 11 .    ? -1.157  60.608  77.615  1.00 26.03 ? 2544 HOH B O     1 
HETATM 20096 O  O     . HOH EA 11 .    ? 33.846  18.659  70.921  1.00 42.24 ? 2545 HOH B O     1 
HETATM 20097 O  O     . HOH EA 11 .    ? -5.992  12.759  99.383  1.00 20.59 ? 2546 HOH B O     1 
HETATM 20098 O  O     . HOH EA 11 .    ? -2.650  26.488  60.412  1.00 40.34 ? 2547 HOH B O     1 
HETATM 20099 O  O     . HOH EA 11 .    ? -10.074 18.189  131.038 1.00 41.84 ? 2548 HOH B O     1 
HETATM 20100 O  O     . HOH EA 11 .    ? 20.413  52.541  69.351  1.00 25.44 ? 2549 HOH B O     1 
HETATM 20101 O  O     . HOH EA 11 .    ? 11.197  16.265  121.969 1.00 38.00 ? 2550 HOH B O     1 
HETATM 20102 O  O     . HOH EA 11 .    ? 22.805  11.886  87.644  1.00 30.81 ? 2551 HOH B O     1 
HETATM 20103 O  O     . HOH EA 11 .    ? 1.643   46.567  99.087  1.00 32.60 ? 2552 HOH B O     1 
HETATM 20104 O  O     . HOH EA 11 .    ? 15.722  10.094  89.598  1.00 22.50 ? 2553 HOH B O     1 
HETATM 20105 O  O     . HOH EA 11 .    ? 10.894  29.424  94.490  1.00 25.44 ? 2554 HOH B O     1 
HETATM 20106 O  O     . HOH EA 11 .    ? 2.277   20.444  92.575  1.00 34.82 ? 2555 HOH B O     1 
HETATM 20107 O  O     . HOH EA 11 .    ? 22.529  26.005  79.612  1.00 31.45 ? 2556 HOH B O     1 
HETATM 20108 O  O     . HOH EA 11 .    ? -13.449 12.574  93.985  1.00 22.46 ? 2557 HOH B O     1 
HETATM 20109 O  O     . HOH EA 11 .    ? 27.181  35.376  91.090  1.00 21.41 ? 2558 HOH B O     1 
HETATM 20110 O  O     . HOH EA 11 .    ? 11.990  21.009  58.891  1.00 22.02 ? 2559 HOH B O     1 
HETATM 20111 O  O     . HOH EA 11 .    ? 19.477  16.084  63.671  1.00 20.27 ? 2560 HOH B O     1 
HETATM 20112 O  O     . HOH EA 11 .    ? 18.326  66.968  58.384  1.00 32.97 ? 2561 HOH B O     1 
HETATM 20113 O  O     . HOH EA 11 .    ? -2.815  54.964  83.776  1.00 35.99 ? 2562 HOH B O     1 
HETATM 20114 O  O     . HOH EA 11 .    ? 9.157   62.132  85.411  1.00 27.57 ? 2563 HOH B O     1 
HETATM 20115 O  O     . HOH EA 11 .    ? 2.075   30.735  96.060  1.00 22.20 ? 2564 HOH B O     1 
HETATM 20116 O  O     . HOH EA 11 .    ? -0.655  55.972  121.881 1.00 33.49 ? 2565 HOH B O     1 
HETATM 20117 O  O     . HOH EA 11 .    ? -4.357  2.051   124.164 1.00 31.77 ? 2566 HOH B O     1 
HETATM 20118 O  O     . HOH EA 11 .    ? -14.974 18.774  80.272  1.00 38.26 ? 2567 HOH B O     1 
HETATM 20119 O  O     . HOH EA 11 .    ? -4.384  35.659  96.508  1.00 40.43 ? 2568 HOH B O     1 
HETATM 20120 O  O     . HOH EA 11 .    ? 19.047  30.701  88.619  1.00 20.86 ? 2569 HOH B O     1 
HETATM 20121 O  O     . HOH EA 11 .    ? -5.420  12.658  84.558  1.00 28.30 ? 2570 HOH B O     1 
HETATM 20122 O  O     . HOH EA 11 .    ? 6.728   57.148  61.192  1.00 45.07 ? 2571 HOH B O     1 
HETATM 20123 O  O     . HOH EA 11 .    ? 10.452  70.428  86.779  1.00 43.47 ? 2572 HOH B O     1 
HETATM 20124 O  O     . HOH EA 11 .    ? -6.477  6.449   118.774 1.00 26.38 ? 2573 HOH B O     1 
HETATM 20125 O  O     . HOH EA 11 .    ? -14.385 7.219   120.442 1.00 36.46 ? 2574 HOH B O     1 
HETATM 20126 O  O     . HOH EA 11 .    ? 37.062  27.847  93.296  1.00 34.97 ? 2575 HOH B O     1 
HETATM 20127 O  O     . HOH EA 11 .    ? 19.271  8.262   84.100  1.00 30.15 ? 2576 HOH B O     1 
HETATM 20128 O  O     . HOH EA 11 .    ? 12.648  6.097   84.579  1.00 25.56 ? 2577 HOH B O     1 
HETATM 20129 O  O     . HOH EA 11 .    ? 15.787  38.283  74.610  1.00 19.07 ? 2578 HOH B O     1 
HETATM 20130 O  O     . HOH EA 11 .    ? -7.723  35.823  80.890  1.00 36.79 ? 2579 HOH B O     1 
HETATM 20131 O  O     . HOH EA 11 .    ? 8.755   15.030  90.483  1.00 25.93 ? 2580 HOH B O     1 
HETATM 20132 O  O     . HOH EA 11 .    ? 24.117  31.752  110.575 1.00 35.12 ? 2581 HOH B O     1 
HETATM 20133 O  O     . HOH EA 11 .    ? 12.035  12.007  121.572 1.00 30.76 ? 2582 HOH B O     1 
HETATM 20134 O  O     . HOH EA 11 .    ? 14.609  45.780  78.443  1.00 28.05 ? 2583 HOH B O     1 
HETATM 20135 O  O     . HOH EA 11 .    ? -10.381 1.718   91.514  1.00 28.95 ? 2584 HOH B O     1 
HETATM 20136 O  O     . HOH EA 11 .    ? 27.363  23.086  88.636  1.00 20.49 ? 2585 HOH B O     1 
HETATM 20137 O  O     . HOH EA 11 .    ? 7.727   20.667  102.349 1.00 32.13 ? 2586 HOH B O     1 
HETATM 20138 O  O     . HOH EA 11 .    ? 12.281  0.713   94.135  1.00 41.80 ? 2587 HOH B O     1 
HETATM 20139 O  O     . HOH EA 11 .    ? 21.065  47.756  56.296  1.00 33.60 ? 2588 HOH B O     1 
HETATM 20140 O  O     . HOH EA 11 .    ? 14.949  16.833  92.056  1.00 24.07 ? 2589 HOH B O     1 
HETATM 20141 O  O     . HOH EA 11 .    ? 43.827  36.812  88.156  1.00 35.24 ? 2590 HOH B O     1 
HETATM 20142 O  O     . HOH EA 11 .    ? 4.808   30.864  54.757  1.00 36.95 ? 2591 HOH B O     1 
HETATM 20143 O  O     . HOH EA 11 .    ? 6.029   15.291  94.820  1.00 19.47 ? 2592 HOH B O     1 
HETATM 20144 O  O     . HOH EA 11 .    ? 16.110  48.498  70.922  1.00 18.58 ? 2593 HOH B O     1 
HETATM 20145 O  O     . HOH EA 11 .    ? 26.445  39.946  52.939  1.00 30.10 ? 2594 HOH B O     1 
HETATM 20146 O  O     . HOH EA 11 .    ? 27.199  18.291  61.911  1.00 26.43 ? 2595 HOH B O     1 
HETATM 20147 O  O     . HOH EA 11 .    ? 28.722  46.570  87.980  1.00 32.70 ? 2596 HOH B O     1 
HETATM 20148 O  O     . HOH EA 11 .    ? -10.309 10.902  130.110 1.00 40.55 ? 2597 HOH B O     1 
HETATM 20149 O  O     . HOH EA 11 .    ? 17.212  34.350  56.074  1.00 18.54 ? 2598 HOH B O     1 
HETATM 20150 O  O     . HOH EA 11 .    ? -10.359 31.943  80.507  1.00 31.22 ? 2599 HOH B O     1 
HETATM 20151 O  O     . HOH EA 11 .    ? 4.804   46.771  69.353  1.00 17.17 ? 2600 HOH B O     1 
HETATM 20152 O  O     . HOH EA 11 .    ? 23.591  32.969  91.617  1.00 20.60 ? 2601 HOH B O     1 
HETATM 20153 O  O     . HOH EA 11 .    ? 17.082  33.954  48.615  1.00 32.84 ? 2602 HOH B O     1 
HETATM 20154 O  O     . HOH EA 11 .    ? 2.830   5.948   80.433  1.00 31.70 ? 2603 HOH B O     1 
HETATM 20155 O  O     . HOH EA 11 .    ? 27.352  42.344  105.033 1.00 33.34 ? 2604 HOH B O     1 
HETATM 20156 O  O     . HOH EA 11 .    ? 29.351  68.201  72.355  1.00 38.67 ? 2605 HOH B O     1 
HETATM 20157 O  O     . HOH EA 11 .    ? 13.558  58.331  64.746  1.00 34.80 ? 2606 HOH B O     1 
HETATM 20158 O  O     . HOH EA 11 .    ? 0.894   -7.798  109.563 1.00 35.30 ? 2607 HOH B O     1 
HETATM 20159 O  O     . HOH EA 11 .    ? -4.233  53.940  130.896 1.00 36.85 ? 2608 HOH B O     1 
HETATM 20160 O  O     . HOH EA 11 .    ? 27.848  31.853  73.843  1.00 27.93 ? 2609 HOH B O     1 
HETATM 20161 O  O     . HOH EA 11 .    ? 4.040   10.629  92.451  1.00 22.20 ? 2610 HOH B O     1 
HETATM 20162 O  O     . HOH EA 11 .    ? -1.690  49.257  101.369 1.00 36.29 ? 2611 HOH B O     1 
HETATM 20163 O  O     . HOH EA 11 .    ? -16.878 16.068  131.396 1.00 48.31 ? 2612 HOH B O     1 
HETATM 20164 O  O     . HOH EA 11 .    ? 10.864  36.062  78.915  1.00 31.42 ? 2613 HOH B O     1 
HETATM 20165 O  O     . HOH EA 11 .    ? 4.916   22.045  83.877  1.00 23.64 ? 2614 HOH B O     1 
HETATM 20166 O  O     . HOH EA 11 .    ? 3.109   35.524  121.280 1.00 33.61 ? 2615 HOH B O     1 
HETATM 20167 O  O     . HOH EA 11 .    ? 28.295  25.553  67.624  1.00 21.52 ? 2616 HOH B O     1 
HETATM 20168 O  O     . HOH EA 11 .    ? 0.456   27.029  94.899  1.00 22.22 ? 2617 HOH B O     1 
HETATM 20169 O  O     . HOH EA 11 .    ? 25.154  23.901  81.742  1.00 26.88 ? 2618 HOH B O     1 
HETATM 20170 O  O     . HOH EA 11 .    ? -15.212 47.197  114.143 1.00 32.82 ? 2619 HOH B O     1 
HETATM 20171 O  O     . HOH EA 11 .    ? 24.938  57.607  78.347  1.00 24.20 ? 2620 HOH B O     1 
HETATM 20172 O  O     . HOH EA 11 .    ? -2.883  33.909  62.617  1.00 24.12 ? 2621 HOH B O     1 
HETATM 20173 O  O     . HOH EA 11 .    ? -5.544  35.673  87.818  1.00 29.90 ? 2622 HOH B O     1 
HETATM 20174 O  O     . HOH EA 11 .    ? 4.819   18.905  124.116 1.00 30.26 ? 2623 HOH B O     1 
HETATM 20175 O  O     . HOH EA 11 .    ? 1.322   9.549   89.774  1.00 25.84 ? 2624 HOH B O     1 
HETATM 20176 O  O     . HOH EA 11 .    ? 5.744   11.931  77.786  1.00 33.46 ? 2625 HOH B O     1 
HETATM 20177 O  O     . HOH EA 11 .    ? 28.439  9.182   73.684  1.00 38.28 ? 2626 HOH B O     1 
HETATM 20178 O  O     . HOH EA 11 .    ? 11.788  26.231  102.263 1.00 32.48 ? 2627 HOH B O     1 
HETATM 20179 O  O     . HOH EA 11 .    ? 9.084   6.090   85.145  1.00 25.80 ? 2628 HOH B O     1 
HETATM 20180 O  O     . HOH EA 11 .    ? 28.613  59.320  56.311  1.00 36.02 ? 2629 HOH B O     1 
HETATM 20181 O  O     . HOH EA 11 .    ? -5.147  -2.226  117.273 1.00 36.43 ? 2630 HOH B O     1 
HETATM 20182 O  O     . HOH EA 11 .    ? -6.605  34.783  129.279 1.00 41.01 ? 2631 HOH B O     1 
HETATM 20183 O  O     . HOH EA 11 .    ? 19.175  14.786  105.299 1.00 39.50 ? 2632 HOH B O     1 
HETATM 20184 O  O     . HOH EA 11 .    ? 34.008  37.821  61.757  1.00 35.07 ? 2633 HOH B O     1 
HETATM 20185 O  O     . HOH EA 11 .    ? 7.851   62.833  66.472  1.00 36.88 ? 2634 HOH B O     1 
HETATM 20186 O  O     . HOH EA 11 .    ? -9.316  0.745   112.806 1.00 32.76 ? 2635 HOH B O     1 
HETATM 20187 O  O     . HOH EA 11 .    ? 26.417  27.592  67.073  1.00 21.89 ? 2636 HOH B O     1 
HETATM 20188 O  O     . HOH EA 11 .    ? 1.392   -0.710  92.891  1.00 30.72 ? 2637 HOH B O     1 
HETATM 20189 O  O     . HOH EA 11 .    ? 14.296  34.627  112.090 1.00 43.19 ? 2638 HOH B O     1 
HETATM 20190 O  O     . HOH EA 11 .    ? -1.006  20.854  89.642  1.00 18.21 ? 2639 HOH B O     1 
HETATM 20191 O  O     . HOH EA 11 .    ? -0.343  3.765   130.749 1.00 45.88 ? 2640 HOH B O     1 
HETATM 20192 O  O     . HOH EA 11 .    ? 29.533  60.474  58.991  1.00 32.19 ? 2641 HOH B O     1 
HETATM 20193 O  O     . HOH EA 11 .    ? -6.183  48.179  79.174  1.00 37.46 ? 2642 HOH B O     1 
HETATM 20194 O  O     . HOH EA 11 .    ? 2.702   49.137  76.260  1.00 20.89 ? 2643 HOH B O     1 
HETATM 20195 O  O     . HOH EA 11 .    ? 23.247  12.429  68.060  1.00 25.37 ? 2644 HOH B O     1 
HETATM 20196 O  O     . HOH EA 11 .    ? 24.749  50.989  67.067  1.00 26.31 ? 2645 HOH B O     1 
HETATM 20197 O  O     . HOH EA 11 .    ? 24.860  16.253  95.273  1.00 29.89 ? 2646 HOH B O     1 
HETATM 20198 O  O     . HOH EA 11 .    ? -0.219  18.015  91.628  1.00 22.99 ? 2647 HOH B O     1 
HETATM 20199 O  O     . HOH EA 11 .    ? -1.685  25.481  80.078  1.00 24.36 ? 2648 HOH B O     1 
HETATM 20200 O  O     . HOH EA 11 .    ? 20.206  54.302  81.335  1.00 30.92 ? 2649 HOH B O     1 
HETATM 20201 O  O     . HOH EA 11 .    ? 15.516  49.002  57.440  1.00 29.14 ? 2650 HOH B O     1 
HETATM 20202 O  O     . HOH EA 11 .    ? 3.991   -4.359  98.322  1.00 46.38 ? 2651 HOH B O     1 
HETATM 20203 O  O     . HOH EA 11 .    ? 9.555   19.207  103.870 1.00 26.63 ? 2652 HOH B O     1 
HETATM 20204 O  O     . HOH EA 11 .    ? -4.197  -0.218  110.671 1.00 26.31 ? 2653 HOH B O     1 
HETATM 20205 O  O     . HOH EA 11 .    ? 33.100  45.531  74.843  1.00 30.78 ? 2654 HOH B O     1 
HETATM 20206 O  O     . HOH EA 11 .    ? 4.560   77.820  80.465  1.00 31.90 ? 2655 HOH B O     1 
HETATM 20207 O  O     . HOH EA 11 .    ? -13.229 54.099  122.859 1.00 36.06 ? 2656 HOH B O     1 
HETATM 20208 O  O     . HOH EA 11 .    ? -4.323  55.845  81.887  1.00 34.43 ? 2657 HOH B O     1 
HETATM 20209 O  O     . HOH EA 11 .    ? 28.941  24.163  51.038  1.00 33.61 ? 2658 HOH B O     1 
HETATM 20210 O  O     . HOH EA 11 .    ? 2.135   40.456  114.595 1.00 26.27 ? 2659 HOH B O     1 
HETATM 20211 O  O     . HOH EA 11 .    ? 33.109  25.524  101.999 1.00 39.55 ? 2660 HOH B O     1 
HETATM 20212 O  O     . HOH EA 11 .    ? 18.477  66.121  55.757  1.00 36.28 ? 2661 HOH B O     1 
HETATM 20213 O  O     . HOH EA 11 .    ? -22.339 20.594  88.452  1.00 34.61 ? 2662 HOH B O     1 
HETATM 20214 O  O     . HOH EA 11 .    ? 23.621  51.960  83.976  1.00 32.22 ? 2663 HOH B O     1 
HETATM 20215 O  O     . HOH EA 11 .    ? 18.589  15.138  97.607  1.00 26.52 ? 2664 HOH B O     1 
HETATM 20216 O  O     . HOH EA 11 .    ? 11.756  18.215  95.253  1.00 39.18 ? 2665 HOH B O     1 
HETATM 20217 O  O     . HOH EA 11 .    ? 6.246   51.974  94.188  1.00 40.96 ? 2666 HOH B O     1 
HETATM 20218 O  O     . HOH EA 11 .    ? 31.250  52.799  65.444  1.00 34.01 ? 2667 HOH B O     1 
HETATM 20219 O  O     . HOH EA 11 .    ? 32.626  29.134  64.540  1.00 29.70 ? 2668 HOH B O     1 
HETATM 20220 O  O     . HOH EA 11 .    ? 31.672  62.411  75.173  1.00 22.48 ? 2669 HOH B O     1 
HETATM 20221 O  O     . HOH EA 11 .    ? 30.659  20.298  73.540  1.00 35.97 ? 2670 HOH B O     1 
HETATM 20222 O  O     . HOH EA 11 .    ? -4.006  30.788  95.046  1.00 29.75 ? 2671 HOH B O     1 
HETATM 20223 O  O     . HOH EA 11 .    ? 5.309   42.830  70.881  1.00 15.47 ? 2672 HOH B O     1 
HETATM 20224 O  O     . HOH EA 11 .    ? 34.684  13.303  80.821  1.00 37.07 ? 2673 HOH B O     1 
HETATM 20225 O  O     . HOH EA 11 .    ? 0.193   19.612  94.094  1.00 23.06 ? 2674 HOH B O     1 
HETATM 20226 O  O     . HOH EA 11 .    ? 4.982   18.013  91.358  1.00 27.26 ? 2675 HOH B O     1 
HETATM 20227 O  O     . HOH EA 11 .    ? 5.365   76.569  85.021  1.00 40.19 ? 2676 HOH B O     1 
HETATM 20228 O  O     . HOH EA 11 .    ? -4.486  44.698  108.818 1.00 34.62 ? 2677 HOH B O     1 
HETATM 20229 O  O     . HOH EA 11 .    ? -3.402  45.983  106.978 1.00 24.33 ? 2678 HOH B O     1 
HETATM 20230 O  O     . HOH EA 11 .    ? 1.775   10.177  79.194  1.00 37.29 ? 2679 HOH B O     1 
HETATM 20231 O  O     . HOH EA 11 .    ? 22.671  61.849  83.085  1.00 37.45 ? 2680 HOH B O     1 
HETATM 20232 O  O     . HOH EA 11 .    ? -2.404  60.221  120.159 1.00 29.59 ? 2681 HOH B O     1 
HETATM 20233 O  O     . HOH EA 11 .    ? 12.416  53.738  90.664  1.00 41.91 ? 2682 HOH B O     1 
HETATM 20234 O  O     . HOH EA 11 .    ? 33.570  23.102  64.336  1.00 35.84 ? 2683 HOH B O     1 
HETATM 20235 O  O     . HOH EA 11 .    ? 3.995   17.627  75.539  1.00 34.91 ? 2684 HOH B O     1 
HETATM 20236 O  O     . HOH EA 11 .    ? 22.641  54.350  93.132  1.00 30.98 ? 2685 HOH B O     1 
HETATM 20237 O  O     . HOH EA 11 .    ? -4.878  16.448  96.994  1.00 20.91 ? 2686 HOH B O     1 
HETATM 20238 O  O     . HOH EA 11 .    ? 6.759   16.925  115.379 1.00 33.43 ? 2687 HOH B O     1 
HETATM 20239 O  O     . HOH EA 11 .    ? 35.110  32.342  55.022  1.00 31.35 ? 2688 HOH B O     1 
HETATM 20240 O  O     . HOH EA 11 .    ? 2.450   30.174  54.679  1.00 36.89 ? 2689 HOH B O     1 
HETATM 20241 O  O     . HOH EA 11 .    ? 14.782  6.826   68.991  1.00 34.87 ? 2690 HOH B O     1 
HETATM 20242 O  O     . HOH EA 11 .    ? -7.757  45.972  76.838  1.00 41.57 ? 2691 HOH B O     1 
HETATM 20243 O  O     . HOH EA 11 .    ? 35.608  25.592  77.746  1.00 28.33 ? 2692 HOH B O     1 
HETATM 20244 O  O     . HOH EA 11 .    ? 9.557   29.304  98.604  1.00 32.16 ? 2693 HOH B O     1 
HETATM 20245 O  O     . HOH EA 11 .    ? -15.204 10.301  90.011  1.00 23.81 ? 2694 HOH B O     1 
HETATM 20246 O  O     . HOH EA 11 .    ? 32.898  28.403  52.829  1.00 33.20 ? 2695 HOH B O     1 
HETATM 20247 O  O     . HOH EA 11 .    ? -10.555 52.372  128.617 1.00 38.72 ? 2696 HOH B O     1 
HETATM 20248 O  O     . HOH EA 11 .    ? 13.211  48.209  82.334  1.00 27.20 ? 2697 HOH B O     1 
HETATM 20249 O  O     . HOH EA 11 .    ? 18.598  48.023  90.133  1.00 22.68 ? 2698 HOH B O     1 
HETATM 20250 O  O     . HOH EA 11 .    ? 39.614  26.781  87.923  1.00 39.42 ? 2699 HOH B O     1 
HETATM 20251 O  O     . HOH EA 11 .    ? -1.663  36.803  87.461  1.00 22.20 ? 2700 HOH B O     1 
HETATM 20252 O  O     . HOH EA 11 .    ? -2.404  14.629  98.884  1.00 19.76 ? 2701 HOH B O     1 
HETATM 20253 O  O     . HOH EA 11 .    ? 19.205  52.167  79.969  1.00 27.05 ? 2702 HOH B O     1 
HETATM 20254 O  O     . HOH EA 11 .    ? 4.945   60.758  68.063  1.00 38.10 ? 2703 HOH B O     1 
HETATM 20255 O  O     . HOH EA 11 .    ? 20.161  22.439  74.504  1.00 34.05 ? 2704 HOH B O     1 
HETATM 20256 O  O     . HOH EA 11 .    ? 34.602  25.630  93.381  1.00 39.68 ? 2705 HOH B O     1 
HETATM 20257 O  O     . HOH EA 11 .    ? 6.581   12.103  126.727 1.00 22.98 ? 2706 HOH B O     1 
HETATM 20258 O  O     . HOH EA 11 .    ? 18.204  23.368  61.383  1.00 24.84 ? 2707 HOH B O     1 
HETATM 20259 O  O     . HOH EA 11 .    ? 4.937   47.535  87.241  1.00 21.94 ? 2708 HOH B O     1 
HETATM 20260 O  O     . HOH EA 11 .    ? 26.542  13.086  87.979  1.00 31.06 ? 2709 HOH B O     1 
HETATM 20261 O  O     . HOH EA 11 .    ? 20.686  22.011  60.939  1.00 19.22 ? 2710 HOH B O     1 
HETATM 20262 O  O     . HOH EA 11 .    ? 10.499  66.685  86.684  1.00 41.96 ? 2711 HOH B O     1 
HETATM 20263 O  O     . HOH EA 11 .    ? 28.425  44.387  89.854  1.00 31.20 ? 2712 HOH B O     1 
HETATM 20264 O  O     . HOH EA 11 .    ? 5.014   57.967  69.097  1.00 22.49 ? 2713 HOH B O     1 
HETATM 20265 O  O     . HOH EA 11 .    ? 18.378  49.986  111.839 1.00 37.44 ? 2714 HOH B O     1 
HETATM 20266 O  O     . HOH EA 11 .    ? 21.666  7.139   83.627  1.00 39.16 ? 2715 HOH B O     1 
HETATM 20267 O  O     . HOH EA 11 .    ? 8.660   35.712  102.896 1.00 31.23 ? 2716 HOH B O     1 
HETATM 20268 O  O     . HOH EA 11 .    ? 32.877  47.433  92.161  1.00 43.89 ? 2717 HOH B O     1 
HETATM 20269 O  O     . HOH EA 11 .    ? 31.078  51.035  79.882  1.00 35.78 ? 2718 HOH B O     1 
HETATM 20270 O  O     . HOH EA 11 .    ? 10.362  22.301  102.964 1.00 40.80 ? 2719 HOH B O     1 
HETATM 20271 O  O     . HOH EA 11 .    ? -0.355  73.419  77.831  1.00 30.73 ? 2720 HOH B O     1 
HETATM 20272 O  O     . HOH EA 11 .    ? 8.194   31.827  93.785  1.00 30.30 ? 2721 HOH B O     1 
HETATM 20273 O  O     . HOH EA 11 .    ? 24.247  50.374  102.642 1.00 44.84 ? 2722 HOH B O     1 
HETATM 20274 O  O     . HOH EA 11 .    ? 34.833  16.820  67.444  1.00 34.05 ? 2723 HOH B O     1 
HETATM 20275 O  O     . HOH EA 11 .    ? -7.125  27.923  74.417  1.00 31.21 ? 2724 HOH B O     1 
HETATM 20276 O  O     . HOH EA 11 .    ? 10.736  33.720  109.704 1.00 27.12 ? 2725 HOH B O     1 
HETATM 20277 O  O     . HOH EA 11 .    ? 0.958   0.162   96.319  1.00 29.71 ? 2726 HOH B O     1 
HETATM 20278 O  O     . HOH EA 11 .    ? 34.164  22.633  78.183  1.00 26.45 ? 2727 HOH B O     1 
HETATM 20279 O  O     . HOH EA 11 .    ? -4.756  8.393   131.701 1.00 43.50 ? 2728 HOH B O     1 
HETATM 20280 O  O     . HOH EA 11 .    ? 8.050   58.203  85.467  1.00 24.30 ? 2729 HOH B O     1 
HETATM 20281 O  O     . HOH EA 11 .    ? 26.289  20.250  53.127  1.00 29.50 ? 2730 HOH B O     1 
HETATM 20282 O  O     . HOH EA 11 .    ? 2.965   23.238  58.913  1.00 34.05 ? 2731 HOH B O     1 
HETATM 20283 O  O     . HOH EA 11 .    ? -24.893 16.794  82.202  1.00 35.58 ? 2732 HOH B O     1 
HETATM 20284 O  O     . HOH EA 11 .    ? 18.049  53.992  82.931  1.00 32.03 ? 2733 HOH B O     1 
HETATM 20285 O  O     . HOH EA 11 .    ? 30.852  34.382  84.774  1.00 30.50 ? 2734 HOH B O     1 
HETATM 20286 O  O     . HOH EA 11 .    ? 16.319  53.616  105.038 1.00 29.59 ? 2735 HOH B O     1 
HETATM 20287 O  O     . HOH EA 11 .    ? 27.596  56.908  80.851  1.00 41.07 ? 2736 HOH B O     1 
HETATM 20288 O  O     . HOH EA 11 .    ? -4.354  42.359  108.270 1.00 37.32 ? 2737 HOH B O     1 
HETATM 20289 O  O     . HOH EA 11 .    ? 10.049  18.532  101.265 1.00 29.85 ? 2738 HOH B O     1 
HETATM 20290 O  O     . HOH EA 11 .    ? 16.733  51.375  60.350  1.00 34.98 ? 2739 HOH B O     1 
HETATM 20291 O  O     . HOH EA 11 .    ? 27.966  10.797  84.822  1.00 29.76 ? 2740 HOH B O     1 
HETATM 20292 O  O     . HOH EA 11 .    ? -11.280 -2.034  96.742  1.00 35.09 ? 2741 HOH B O     1 
HETATM 20293 O  O     . HOH EA 11 .    ? -22.955 25.421  103.431 1.00 43.31 ? 2742 HOH B O     1 
HETATM 20294 O  O     . HOH EA 11 .    ? -14.516 24.145  108.583 1.00 32.13 ? 2743 HOH B O     1 
HETATM 20295 O  O     . HOH EA 11 .    ? -17.022 -4.580  105.344 1.00 36.64 ? 2744 HOH B O     1 
HETATM 20296 O  O     . HOH EA 11 .    ? -5.494  46.566  84.179  1.00 27.79 ? 2745 HOH B O     1 
HETATM 20297 O  O     . HOH EA 11 .    ? -12.082 7.959   127.243 1.00 36.88 ? 2746 HOH B O     1 
HETATM 20298 O  O     . HOH EA 11 .    ? -5.433  23.074  80.762  1.00 22.38 ? 2747 HOH B O     1 
HETATM 20299 O  O     . HOH EA 11 .    ? -0.756  13.627  100.894 1.00 20.69 ? 2748 HOH B O     1 
HETATM 20300 O  O     . HOH EA 11 .    ? 33.152  37.815  104.715 1.00 37.27 ? 2749 HOH B O     1 
HETATM 20301 O  O     . HOH EA 11 .    ? -3.288  52.502  82.765  1.00 27.79 ? 2750 HOH B O     1 
HETATM 20302 O  O     . HOH EA 11 .    ? -9.274  45.726  131.223 1.00 36.78 ? 2751 HOH B O     1 
HETATM 20303 O  O     . HOH EA 11 .    ? 32.735  9.124   74.530  1.00 43.67 ? 2752 HOH B O     1 
HETATM 20304 O  O     . HOH EA 11 .    ? -10.749 36.470  76.495  1.00 43.66 ? 2753 HOH B O     1 
HETATM 20305 O  O     . HOH EA 11 .    ? 13.456  3.373   84.538  1.00 43.72 ? 2754 HOH B O     1 
HETATM 20306 O  O     . HOH EA 11 .    ? -7.259  13.212  94.668  1.00 21.00 ? 2755 HOH B O     1 
HETATM 20307 O  O     . HOH EA 11 .    ? 11.849  25.524  86.214  1.00 39.42 ? 2756 HOH B O     1 
HETATM 20308 O  O     . HOH EA 11 .    ? 18.583  53.408  76.024  1.00 24.27 ? 2757 HOH B O     1 
HETATM 20309 O  O     . HOH EA 11 .    ? 7.774   54.470  64.625  1.00 27.22 ? 2758 HOH B O     1 
HETATM 20310 O  O     . HOH EA 11 .    ? 29.649  32.501  103.408 1.00 33.76 ? 2759 HOH B O     1 
HETATM 20311 O  O     . HOH EA 11 .    ? -6.686  44.068  73.935  1.00 34.34 ? 2760 HOH B O     1 
HETATM 20312 O  O     . HOH EA 11 .    ? -1.981  57.778  75.372  1.00 19.94 ? 2761 HOH B O     1 
HETATM 20313 O  O     . HOH EA 11 .    ? -2.505  30.639  70.738  1.00 20.15 ? 2762 HOH B O     1 
HETATM 20314 O  O     . HOH EA 11 .    ? 12.008  49.521  79.015  1.00 32.09 ? 2763 HOH B O     1 
HETATM 20315 O  O     . HOH EA 11 .    ? 42.552  32.186  96.991  1.00 42.00 ? 2764 HOH B O     1 
HETATM 20316 O  O     . HOH EA 11 .    ? -20.404 25.246  94.622  1.00 29.96 ? 2765 HOH B O     1 
HETATM 20317 O  O     . HOH EA 11 .    ? 24.804  63.343  54.509  1.00 37.93 ? 2766 HOH B O     1 
HETATM 20318 O  O     . HOH EA 11 .    ? 3.080   45.146  67.965  1.00 19.41 ? 2767 HOH B O     1 
HETATM 20319 O  O     . HOH EA 11 .    ? 4.797   0.460   86.868  1.00 35.64 ? 2768 HOH B O     1 
HETATM 20320 O  O     . HOH EA 11 .    ? 1.379   22.640  63.549  1.00 27.27 ? 2769 HOH B O     1 
HETATM 20321 O  O     . HOH EA 11 .    ? -13.563 48.920  110.779 1.00 35.41 ? 2770 HOH B O     1 
HETATM 20322 O  O     . HOH EA 11 .    ? -1.797  28.259  62.817  1.00 31.24 ? 2771 HOH B O     1 
HETATM 20323 O  O     . HOH EA 11 .    ? 8.509   37.595  79.285  1.00 22.85 ? 2772 HOH B O     1 
HETATM 20324 O  O     . HOH EA 11 .    ? -16.291 21.974  82.471  1.00 30.44 ? 2773 HOH B O     1 
HETATM 20325 O  O     . HOH EA 11 .    ? 5.177   43.133  55.990  1.00 32.21 ? 2774 HOH B O     1 
HETATM 20326 O  O     . HOH EA 11 .    ? -11.861 21.985  85.710  1.00 26.75 ? 2775 HOH B O     1 
HETATM 20327 O  O     . HOH EA 11 .    ? 29.199  9.941   92.318  1.00 43.84 ? 2776 HOH B O     1 
HETATM 20328 O  O     . HOH EA 11 .    ? 7.242   35.963  109.025 1.00 42.10 ? 2777 HOH B O     1 
HETATM 20329 O  O     . HOH EA 11 .    ? 11.254  26.656  52.017  1.00 32.41 ? 2778 HOH B O     1 
HETATM 20330 O  O     . HOH EA 11 .    ? -0.466  -7.731  99.799  1.00 34.40 ? 2779 HOH B O     1 
HETATM 20331 O  O     . HOH EA 11 .    ? 11.579  18.636  97.976  1.00 35.00 ? 2780 HOH B O     1 
HETATM 20332 O  O     . HOH EA 11 .    ? 23.920  17.186  82.740  1.00 26.44 ? 2781 HOH B O     1 
HETATM 20333 O  O     . HOH EA 11 .    ? 8.021   41.270  122.248 1.00 43.72 ? 2782 HOH B O     1 
HETATM 20334 O  O     . HOH EA 11 .    ? 17.580  34.109  68.454  1.00 16.27 ? 2783 HOH B O     1 
HETATM 20335 O  O     . HOH EA 11 .    ? -16.414 25.243  107.053 1.00 34.80 ? 2784 HOH B O     1 
HETATM 20336 O  O     . HOH EA 11 .    ? -37.351 13.865  95.124  1.00 56.18 ? 2785 HOH B O     1 
HETATM 20337 O  O     . HOH EA 11 .    ? -30.517 5.549   100.136 1.00 42.60 ? 2786 HOH B O     1 
HETATM 20338 O  O     . HOH EA 11 .    ? -8.500  31.602  87.004  1.00 21.43 ? 2787 HOH B O     1 
HETATM 20339 O  O     . HOH EA 11 .    ? -18.076 6.088   95.773  1.00 36.27 ? 2788 HOH B O     1 
HETATM 20340 O  O     . HOH EA 11 .    ? 15.944  56.123  63.935  1.00 27.32 ? 2789 HOH B O     1 
HETATM 20341 O  O     . HOH EA 11 .    ? -6.419  11.383  127.913 1.00 38.45 ? 2790 HOH B O     1 
HETATM 20342 O  O     . HOH EA 11 .    ? 5.021   55.103  64.859  1.00 39.54 ? 2791 HOH B O     1 
HETATM 20343 O  O     . HOH EA 11 .    ? 20.241  18.998  60.143  1.00 24.07 ? 2792 HOH B O     1 
HETATM 20344 O  O     . HOH EA 11 .    ? 17.819  76.679  63.751  1.00 33.21 ? 2793 HOH B O     1 
HETATM 20345 O  O     . HOH EA 11 .    ? 3.254   31.377  98.511  1.00 26.80 ? 2794 HOH B O     1 
HETATM 20346 O  O     . HOH EA 11 .    ? 3.021   54.258  67.101  1.00 35.48 ? 2795 HOH B O     1 
HETATM 20347 O  O     . HOH EA 11 .    ? -14.095 9.479   87.562  1.00 27.63 ? 2796 HOH B O     1 
HETATM 20348 O  O     . HOH EA 11 .    ? 7.021   19.418  116.771 1.00 36.92 ? 2797 HOH B O     1 
HETATM 20349 O  O     . HOH EA 11 .    ? 29.967  41.746  79.951  1.00 36.66 ? 2798 HOH B O     1 
HETATM 20350 O  O     . HOH EA 11 .    ? -1.557  -0.897  109.246 1.00 34.73 ? 2799 HOH B O     1 
HETATM 20351 O  O     . HOH EA 11 .    ? -14.711 26.859  101.508 1.00 35.94 ? 2800 HOH B O     1 
HETATM 20352 O  O     . HOH EA 11 .    ? 10.080  53.380  65.765  1.00 27.42 ? 2801 HOH B O     1 
HETATM 20353 O  O     . HOH EA 11 .    ? 23.016  51.458  65.180  1.00 24.46 ? 2802 HOH B O     1 
HETATM 20354 O  O     . HOH EA 11 .    ? 5.631   23.956  119.910 1.00 45.23 ? 2803 HOH B O     1 
HETATM 20355 O  O     . HOH EA 11 .    ? -5.604  15.535  94.547  1.00 20.48 ? 2804 HOH B O     1 
HETATM 20356 O  O     . HOH EA 11 .    ? 22.268  46.406  76.791  1.00 27.61 ? 2805 HOH B O     1 
HETATM 20357 O  O     . HOH EA 11 .    ? 0.456   11.224  80.987  1.00 38.07 ? 2806 HOH B O     1 
HETATM 20358 O  O     . HOH EA 11 .    ? 18.247  76.223  78.695  1.00 36.09 ? 2807 HOH B O     1 
HETATM 20359 O  O     . HOH EA 11 .    ? -4.153  52.666  79.937  1.00 36.82 ? 2808 HOH B O     1 
HETATM 20360 O  O     . HOH EA 11 .    ? 31.162  67.389  82.579  1.00 34.76 ? 2809 HOH B O     1 
HETATM 20361 O  O     . HOH EA 11 .    ? -2.706  64.610  83.585  1.00 21.02 ? 2810 HOH B O     1 
HETATM 20362 O  O     . HOH EA 11 .    ? 23.436  2.436   82.085  1.00 44.58 ? 2811 HOH B O     1 
HETATM 20363 O  O     . HOH EA 11 .    ? 32.593  70.464  73.877  1.00 36.51 ? 2812 HOH B O     1 
HETATM 20364 O  O     . HOH EA 11 .    ? 31.356  46.169  78.851  1.00 38.47 ? 2813 HOH B O     1 
HETATM 20365 O  O     . HOH EA 11 .    ? 8.193   26.890  110.231 1.00 44.45 ? 2814 HOH B O     1 
HETATM 20366 O  O     . HOH EA 11 .    ? 5.846   18.739  87.463  1.00 25.53 ? 2815 HOH B O     1 
HETATM 20367 O  O     . HOH EA 11 .    ? 31.061  5.331   84.499  1.00 52.13 ? 2816 HOH B O     1 
HETATM 20368 O  O     . HOH EA 11 .    ? 8.917   -0.690  98.817  1.00 45.58 ? 2817 HOH B O     1 
HETATM 20369 O  O     . HOH EA 11 .    ? -12.772 31.471  83.767  1.00 44.43 ? 2818 HOH B O     1 
HETATM 20370 O  O     . HOH EA 11 .    ? 36.213  38.733  91.039  1.00 39.64 ? 2819 HOH B O     1 
HETATM 20371 O  O     . HOH EA 11 .    ? -2.841  40.080  58.002  1.00 25.44 ? 2820 HOH B O     1 
HETATM 20372 O  O     . HOH EA 11 .    ? 9.509   30.824  88.649  1.00 30.47 ? 2821 HOH B O     1 
HETATM 20373 O  O     . HOH EA 11 .    ? 19.080  35.650  113.168 1.00 24.12 ? 2822 HOH B O     1 
HETATM 20374 O  O     . HOH EA 11 .    ? 29.046  22.529  72.314  1.00 33.59 ? 2823 HOH B O     1 
HETATM 20375 O  O     . HOH EA 11 .    ? -7.973  48.149  76.772  1.00 36.53 ? 2824 HOH B O     1 
HETATM 20376 O  O     . HOH EA 11 .    ? 4.123   77.580  63.466  1.00 43.51 ? 2825 HOH B O     1 
HETATM 20377 O  O     . HOH EA 11 .    ? 23.157  73.125  81.675  1.00 32.65 ? 2826 HOH B O     1 
HETATM 20378 O  O     . HOH EA 11 .    ? -2.128  -7.449  110.805 1.00 27.26 ? 2827 HOH B O     1 
HETATM 20379 O  O     . HOH EA 11 .    ? 20.486  20.489  109.333 1.00 23.65 ? 2828 HOH B O     1 
HETATM 20380 O  O     . HOH EA 11 .    ? 15.127  19.437  89.625  1.00 35.33 ? 2829 HOH B O     1 
HETATM 20381 O  O     . HOH EA 11 .    ? -29.647 17.806  103.749 1.00 38.85 ? 2830 HOH B O     1 
HETATM 20382 O  O     . HOH EA 11 .    ? 8.619   15.995  92.786  1.00 32.25 ? 2831 HOH B O     1 
HETATM 20383 O  O     . HOH EA 11 .    ? 14.012  75.950  63.055  1.00 30.06 ? 2832 HOH B O     1 
HETATM 20384 O  O     A HOH EA 11 .    ? 0.586   63.557  84.938  0.55 26.42 ? 2833 HOH B O     1 
HETATM 20385 O  O     . HOH EA 11 .    ? 27.291  39.195  104.923 1.00 33.45 ? 2834 HOH B O     1 
HETATM 20386 O  O     . HOH EA 11 .    ? 19.318  58.597  82.462  1.00 27.94 ? 2835 HOH B O     1 
HETATM 20387 O  O     . HOH EA 11 .    ? 2.540   18.879  77.345  1.00 32.25 ? 2836 HOH B O     1 
HETATM 20388 O  O     . HOH EA 11 .    ? 4.853   56.286  75.148  1.00 18.78 ? 2837 HOH B O     1 
HETATM 20389 O  O     . HOH EA 11 .    ? 4.897   -3.726  95.347  1.00 41.86 ? 2838 HOH B O     1 
HETATM 20390 O  O     . HOH EA 11 .    ? 36.301  31.620  103.718 1.00 43.47 ? 2839 HOH B O     1 
HETATM 20391 O  O     . HOH EA 11 .    ? -15.847 52.556  123.788 1.00 43.68 ? 2840 HOH B O     1 
HETATM 20392 O  O     . HOH EA 11 .    ? -1.333  48.990  136.258 1.00 54.45 ? 2841 HOH B O     1 
HETATM 20393 O  O     . HOH EA 11 .    ? 37.436  37.434  89.135  1.00 28.45 ? 2842 HOH B O     1 
HETATM 20394 O  O     . HOH EA 11 .    ? 15.603  49.662  79.023  1.00 32.29 ? 2843 HOH B O     1 
HETATM 20395 O  O     . HOH EA 11 .    ? 27.595  18.928  101.097 1.00 44.75 ? 2844 HOH B O     1 
HETATM 20396 O  O     . HOH EA 11 .    ? 6.046   13.713  62.492  1.00 27.69 ? 2845 HOH B O     1 
HETATM 20397 O  O     . HOH EA 11 .    ? 34.493  16.324  62.124  1.00 44.14 ? 2846 HOH B O     1 
HETATM 20398 O  O     . HOH EA 11 .    ? -19.475 28.852  88.466  1.00 35.23 ? 2847 HOH B O     1 
HETATM 20399 O  O     . HOH EA 11 .    ? 25.796  75.444  76.795  1.00 32.91 ? 2848 HOH B O     1 
HETATM 20400 O  O     . HOH EA 11 .    ? 22.185  14.936  81.082  1.00 26.95 ? 2849 HOH B O     1 
HETATM 20401 O  O     . HOH EA 11 .    ? 24.316  67.684  80.945  1.00 38.26 ? 2850 HOH B O     1 
HETATM 20402 O  O     . HOH EA 11 .    ? 3.326   54.019  57.892  1.00 47.98 ? 2851 HOH B O     1 
HETATM 20403 O  O     . HOH EA 11 .    ? 14.657  9.205   93.624  1.00 24.82 ? 2852 HOH B O     1 
HETATM 20404 O  O     . HOH EA 11 .    ? 2.576   49.001  99.110  1.00 23.14 ? 2853 HOH B O     1 
HETATM 20405 O  O     . HOH EA 11 .    ? -19.730 23.962  112.571 1.00 41.85 ? 2854 HOH B O     1 
HETATM 20406 O  O     . HOH EA 11 .    ? 18.032  74.826  81.983  1.00 37.07 ? 2855 HOH B O     1 
HETATM 20407 O  O     . HOH EA 11 .    ? -6.085  9.146   82.095  1.00 40.84 ? 2856 HOH B O     1 
HETATM 20408 O  O     . HOH EA 11 .    ? 35.812  32.235  61.283  1.00 48.82 ? 2857 HOH B O     1 
HETATM 20409 O  O     . HOH EA 11 .    ? 7.437   66.551  86.768  1.00 37.21 ? 2858 HOH B O     1 
HETATM 20410 O  O     . HOH EA 11 .    ? -34.233 12.850  111.257 1.00 44.34 ? 2859 HOH B O     1 
HETATM 20411 O  O     . HOH EA 11 .    ? 19.355  54.580  104.351 1.00 28.32 ? 2860 HOH B O     1 
HETATM 20412 O  O     . HOH EA 11 .    ? 5.633   53.078  113.562 1.00 43.64 ? 2861 HOH B O     1 
HETATM 20413 O  O     . HOH EA 11 .    ? 17.398  7.951   89.940  1.00 45.75 ? 2862 HOH B O     1 
HETATM 20414 O  O     . HOH EA 11 .    ? 5.803   70.435  61.331  1.00 42.49 ? 2863 HOH B O     1 
HETATM 20415 O  O     . HOH EA 11 .    ? -5.977  35.824  92.629  1.00 31.95 ? 2864 HOH B O     1 
HETATM 20416 O  O     . HOH EA 11 .    ? 25.055  53.521  68.586  1.00 29.03 ? 2865 HOH B O     1 
HETATM 20417 O  O     . HOH EA 11 .    ? 28.367  49.186  98.123  1.00 39.98 ? 2866 HOH B O     1 
HETATM 20418 O  O     . HOH EA 11 .    ? 16.510  14.192  107.060 1.00 28.50 ? 2867 HOH B O     1 
HETATM 20419 O  O     . HOH EA 11 .    ? 35.574  31.421  58.304  1.00 35.19 ? 2868 HOH B O     1 
HETATM 20420 O  O     . HOH EA 11 .    ? 22.926  54.454  53.830  1.00 42.63 ? 2869 HOH B O     1 
HETATM 20421 O  O     . HOH EA 11 .    ? -14.961 19.374  82.693  1.00 31.01 ? 2870 HOH B O     1 
HETATM 20422 O  O     . HOH EA 11 .    ? -4.410  46.620  133.315 1.00 49.20 ? 2871 HOH B O     1 
HETATM 20423 O  O     . HOH EA 11 .    ? 7.978   77.594  85.877  1.00 43.26 ? 2872 HOH B O     1 
HETATM 20424 O  O     . HOH EA 11 .    ? -27.753 14.404  86.321  1.00 41.67 ? 2873 HOH B O     1 
HETATM 20425 O  O     . HOH EA 11 .    ? -7.347  10.520  113.046 1.00 25.32 ? 2874 HOH B O     1 
HETATM 20426 O  O     . HOH EA 11 .    ? 12.281  77.696  64.239  1.00 37.69 ? 2875 HOH B O     1 
HETATM 20427 O  O     . HOH EA 11 .    ? 4.930   35.956  103.989 1.00 48.53 ? 2876 HOH B O     1 
HETATM 20428 O  O     . HOH EA 11 .    ? 9.138   45.758  132.210 1.00 46.62 ? 2877 HOH B O     1 
HETATM 20429 O  O     . HOH EA 11 .    ? 16.343  52.136  79.734  1.00 28.68 ? 2878 HOH B O     1 
HETATM 20430 O  O     . HOH EA 11 .    ? 29.037  65.563  62.323  1.00 32.71 ? 2879 HOH B O     1 
HETATM 20431 O  O     . HOH EA 11 .    ? -4.641  -3.824  91.938  1.00 34.02 ? 2880 HOH B O     1 
HETATM 20432 O  O     . HOH EA 11 .    ? -2.062  60.251  124.126 1.00 38.15 ? 2881 HOH B O     1 
HETATM 20433 O  O     . HOH EA 11 .    ? -32.240 7.176   108.061 1.00 48.38 ? 2882 HOH B O     1 
HETATM 20434 O  O     . HOH EA 11 .    ? 29.657  8.735   86.115  1.00 46.22 ? 2883 HOH B O     1 
HETATM 20435 O  O     . HOH EA 11 .    ? 13.613  18.592  87.521  1.00 33.96 ? 2884 HOH B O     1 
HETATM 20436 O  O     . HOH EA 11 .    ? -22.956 21.813  102.083 1.00 38.92 ? 2885 HOH B O     1 
HETATM 20437 O  O     . HOH EA 11 .    ? 26.577  13.325  90.841  1.00 36.83 ? 2886 HOH B O     1 
HETATM 20438 O  O     . HOH EA 11 .    ? 16.172  10.324  95.652  1.00 27.68 ? 2887 HOH B O     1 
HETATM 20439 O  O     . HOH EA 11 .    ? 17.242  25.270  93.066  1.00 37.52 ? 2888 HOH B O     1 
HETATM 20440 O  O     . HOH EA 11 .    ? 4.604   18.170  127.823 1.00 39.23 ? 2889 HOH B O     1 
HETATM 20441 O  O     . HOH EA 11 .    ? 26.731  41.107  81.278  1.00 35.94 ? 2890 HOH B O     1 
HETATM 20442 O  O     . HOH EA 11 .    ? 20.579  62.836  54.160  1.00 36.50 ? 2891 HOH B O     1 
HETATM 20443 O  O     . HOH EA 11 .    ? -13.526 28.969  97.885  1.00 40.63 ? 2892 HOH B O     1 
HETATM 20444 O  O     . HOH EA 11 .    ? -21.308 -3.706  103.025 1.00 50.23 ? 2893 HOH B O     1 
HETATM 20445 O  O     . HOH EA 11 .    ? -16.748 49.567  116.926 1.00 43.99 ? 2894 HOH B O     1 
HETATM 20446 O  O     . HOH EA 11 .    ? 12.861  61.832  84.701  1.00 37.17 ? 2895 HOH B O     1 
HETATM 20447 O  O     . HOH EA 11 .    ? -9.056  8.094   82.165  1.00 45.36 ? 2896 HOH B O     1 
HETATM 20448 O  O     . HOH EA 11 .    ? 12.748  29.492  50.465  1.00 28.14 ? 2897 HOH B O     1 
HETATM 20449 O  O     . HOH EA 11 .    ? -6.588  39.154  67.532  1.00 34.58 ? 2898 HOH B O     1 
HETATM 20450 O  O     . HOH EA 11 .    ? 31.749  35.254  74.812  1.00 41.21 ? 2899 HOH B O     1 
HETATM 20451 O  O     . HOH EA 11 .    ? 12.414  26.969  88.502  1.00 40.93 ? 2900 HOH B O     1 
HETATM 20452 O  O     . HOH EA 11 .    ? -15.185 -3.759  112.005 1.00 54.06 ? 2901 HOH B O     1 
HETATM 20453 O  O     . HOH EA 11 .    ? 12.509  58.007  94.121  1.00 34.67 ? 2902 HOH B O     1 
HETATM 20454 O  O     . HOH EA 11 .    ? -2.481  42.288  74.295  1.00 33.34 ? 2903 HOH B O     1 
HETATM 20455 O  O     . HOH EA 11 .    ? 15.002  57.146  72.063  1.00 28.26 ? 2904 HOH B O     1 
HETATM 20456 O  O     . HOH EA 11 .    ? -2.694  22.895  79.604  1.00 24.81 ? 2905 HOH B O     1 
HETATM 20457 O  O     . HOH EA 11 .    ? -5.313  37.541  86.040  1.00 33.31 ? 2906 HOH B O     1 
HETATM 20458 O  O     . HOH EA 11 .    ? -1.979  62.476  69.833  1.00 37.52 ? 2907 HOH B O     1 
HETATM 20459 O  O     . HOH EA 11 .    ? -18.111 -4.427  109.666 1.00 45.24 ? 2908 HOH B O     1 
HETATM 20460 O  O     . HOH EA 11 .    ? -2.677  26.682  113.350 1.00 46.00 ? 2909 HOH B O     1 
HETATM 20461 O  O     . HOH EA 11 .    ? 23.433  24.631  47.521  1.00 35.03 ? 2910 HOH B O     1 
HETATM 20462 O  O     . HOH EA 11 .    ? 11.888  28.865  83.457  1.00 29.70 ? 2911 HOH B O     1 
HETATM 20463 O  O     . HOH EA 11 .    ? 30.871  19.805  56.120  1.00 31.27 ? 2912 HOH B O     1 
HETATM 20464 O  O     . HOH EA 11 .    ? -14.117 44.807  113.678 1.00 40.82 ? 2913 HOH B O     1 
HETATM 20465 O  O     . HOH EA 11 .    ? 4.599   25.582  129.127 1.00 39.37 ? 2914 HOH B O     1 
HETATM 20466 O  O     . HOH EA 11 .    ? -0.928  37.837  76.395  1.00 32.37 ? 2915 HOH B O     1 
HETATM 20467 O  O     . HOH EA 11 .    ? 5.231   49.970  54.637  1.00 44.52 ? 2916 HOH B O     1 
HETATM 20468 O  O     . HOH EA 11 .    ? -2.392  -5.519  89.679  1.00 37.68 ? 2917 HOH B O     1 
HETATM 20469 O  O     . HOH EA 11 .    ? -0.197  45.385  77.723  1.00 35.40 ? 2918 HOH B O     1 
HETATM 20470 O  O     . HOH EA 11 .    ? -16.279 8.230   128.058 1.00 49.46 ? 2919 HOH B O     1 
HETATM 20471 O  O     . HOH EA 11 .    ? 31.728  37.400  50.896  1.00 47.58 ? 2920 HOH B O     1 
HETATM 20472 O  O     . HOH EA 11 .    ? 18.406  63.654  55.153  1.00 38.91 ? 2921 HOH B O     1 
HETATM 20473 O  O     . HOH EA 11 .    ? 7.685   34.067  51.341  1.00 34.65 ? 2922 HOH B O     1 
HETATM 20474 O  O     . HOH EA 11 .    ? 22.826  67.808  59.467  1.00 30.10 ? 2923 HOH B O     1 
HETATM 20475 O  O     . HOH EA 11 .    ? 15.187  29.097  49.223  1.00 31.69 ? 2924 HOH B O     1 
HETATM 20476 O  O     . HOH EA 11 .    ? 9.383   0.823   119.687 1.00 43.20 ? 2925 HOH B O     1 
HETATM 20477 O  O     . HOH EA 11 .    ? 11.626  45.653  109.291 1.00 44.10 ? 2926 HOH B O     1 
HETATM 20478 O  O     . HOH EA 11 .    ? -15.066 51.388  127.196 1.00 49.65 ? 2927 HOH B O     1 
HETATM 20479 O  O     . HOH EA 11 .    ? -31.901 21.092  118.009 1.00 51.26 ? 2928 HOH B O     1 
HETATM 20480 O  O     . HOH EA 11 .    ? -5.348  51.113  83.551  1.00 37.89 ? 2929 HOH B O     1 
HETATM 20481 O  O     . HOH EA 11 .    ? -0.629  44.152  56.030  1.00 33.98 ? 2930 HOH B O     1 
HETATM 20482 O  O     . HOH EA 11 .    ? 36.919  21.699  83.954  1.00 38.01 ? 2931 HOH B O     1 
HETATM 20483 O  O     . HOH EA 11 .    ? -0.877  22.857  97.050  1.00 30.62 ? 2932 HOH B O     1 
HETATM 20484 O  O     . HOH EA 11 .    ? -2.521  29.923  97.025  1.00 33.46 ? 2933 HOH B O     1 
HETATM 20485 O  O     . HOH EA 11 .    ? 16.241  8.346   111.231 1.00 44.75 ? 2934 HOH B O     1 
HETATM 20486 O  O     . HOH EA 11 .    ? 28.526  41.897  53.332  1.00 38.80 ? 2935 HOH B O     1 
HETATM 20487 O  O     . HOH EA 11 .    ? -36.535 7.087   96.931  1.00 50.45 ? 2936 HOH B O     1 
HETATM 20488 O  O     . HOH EA 11 .    ? -31.452 18.720  84.821  1.00 54.06 ? 2937 HOH B O     1 
HETATM 20489 O  O     . HOH EA 11 .    ? 2.896   57.352  70.999  1.00 30.09 ? 2938 HOH B O     1 
HETATM 20490 O  O     . HOH EA 11 .    ? 31.149  14.944  64.700  1.00 41.61 ? 2939 HOH B O     1 
HETATM 20491 O  O     . HOH EA 11 .    ? 1.194   56.006  65.873  1.00 40.73 ? 2940 HOH B O     1 
HETATM 20492 O  O     . HOH EA 11 .    ? 17.042  24.812  52.357  1.00 31.49 ? 2941 HOH B O     1 
HETATM 20493 O  O     . HOH EA 11 .    ? -16.221 -0.458  99.176  1.00 39.03 ? 2942 HOH B O     1 
HETATM 20494 O  O     . HOH EA 11 .    ? -32.698 16.606  101.093 1.00 39.42 ? 2943 HOH B O     1 
HETATM 20495 O  O     . HOH EA 11 .    ? 9.402   23.455  122.170 1.00 41.20 ? 2944 HOH B O     1 
HETATM 20496 O  O     . HOH EA 11 .    ? 39.412  40.889  89.314  1.00 40.28 ? 2945 HOH B O     1 
HETATM 20497 O  O     . HOH EA 11 .    ? 33.011  20.323  72.380  1.00 42.88 ? 2946 HOH B O     1 
HETATM 20498 O  O     . HOH EA 11 .    ? 12.676  46.500  111.486 1.00 37.87 ? 2947 HOH B O     1 
HETATM 20499 O  O     . HOH EA 11 .    ? 6.749   36.085  113.889 1.00 42.39 ? 2948 HOH B O     1 
HETATM 20500 O  O     . HOH EA 11 .    ? 4.345   29.650  82.082  1.00 27.18 ? 2949 HOH B O     1 
HETATM 20501 O  O     . HOH EA 11 .    ? -1.679  -9.570  109.421 1.00 36.10 ? 2950 HOH B O     1 
HETATM 20502 O  O     . HOH EA 11 .    ? -7.360  12.358  83.023  1.00 46.94 ? 2951 HOH B O     1 
HETATM 20503 O  O     . HOH EA 11 .    ? 6.389   48.418  114.694 1.00 34.77 ? 2952 HOH B O     1 
HETATM 20504 O  O     . HOH EA 11 .    ? 7.945   -9.202  111.204 1.00 42.53 ? 2953 HOH B O     1 
HETATM 20505 O  O     . HOH EA 11 .    ? 13.020  47.297  79.570  1.00 37.65 ? 2954 HOH B O     1 
HETATM 20506 O  O     . HOH EA 11 .    ? -3.429  14.574  132.045 1.00 38.11 ? 2955 HOH B O     1 
HETATM 20507 O  O     . HOH EA 11 .    ? -6.532  8.209   116.583 1.00 29.41 ? 2956 HOH B O     1 
HETATM 20508 O  O     . HOH EA 11 .    ? 11.529  43.990  51.103  1.00 35.41 ? 2957 HOH B O     1 
HETATM 20509 O  O     . HOH EA 11 .    ? -30.243 20.351  121.600 1.00 51.54 ? 2958 HOH B O     1 
HETATM 20510 O  O     . HOH EA 11 .    ? 14.604  53.472  86.776  1.00 46.39 ? 2959 HOH B O     1 
HETATM 20511 O  O     . HOH EA 11 .    ? 0.066   -1.989  94.888  1.00 34.51 ? 2960 HOH B O     1 
HETATM 20512 O  O     . HOH EA 11 .    ? 6.388   17.473  96.542  1.00 32.28 ? 2961 HOH B O     1 
HETATM 20513 O  O     . HOH EA 11 .    ? -19.613 27.753  91.762  1.00 42.96 ? 2962 HOH B O     1 
HETATM 20514 O  O     . HOH EA 11 .    ? 0.553   4.608   86.115  1.00 32.90 ? 2963 HOH B O     1 
HETATM 20515 O  O     . HOH EA 11 .    ? 16.816  56.229  95.057  1.00 37.82 ? 2964 HOH B O     1 
HETATM 20516 O  O     . HOH EA 11 .    ? 31.110  32.031  83.760  1.00 33.36 ? 2965 HOH B O     1 
HETATM 20517 O  O     . HOH EA 11 .    ? -5.989  39.763  86.239  1.00 32.63 ? 2966 HOH B O     1 
HETATM 20518 O  O     . HOH EA 11 .    ? -0.889  44.170  75.737  1.00 37.59 ? 2967 HOH B O     1 
HETATM 20519 O  O     . HOH EA 11 .    ? -16.306 52.039  115.960 1.00 42.38 ? 2968 HOH B O     1 
HETATM 20520 O  O     . HOH EA 11 .    ? -32.866 18.936  101.290 1.00 46.47 ? 2969 HOH B O     1 
HETATM 20521 O  O     . HOH EA 11 .    ? 28.539  34.019  80.703  1.00 37.72 ? 2970 HOH B O     1 
HETATM 20522 O  O     . HOH EA 11 .    ? 9.564   48.913  108.788 1.00 41.64 ? 2971 HOH B O     1 
HETATM 20523 O  O     . HOH EA 11 .    ? 33.349  15.859  64.493  1.00 42.96 ? 2972 HOH B O     1 
HETATM 20524 O  O     . HOH EA 11 .    ? -7.092  37.233  66.396  1.00 40.50 ? 2973 HOH B O     1 
HETATM 20525 O  O     . HOH EA 11 .    ? -3.962  64.205  70.028  1.00 43.43 ? 2974 HOH B O     1 
HETATM 20526 O  O     . HOH EA 11 .    ? -1.255  37.868  73.697  1.00 25.89 ? 2975 HOH B O     1 
HETATM 20527 O  O     . HOH EA 11 .    ? 2.266   3.964   82.179  1.00 41.08 ? 2976 HOH B O     1 
HETATM 20528 O  O     . HOH EA 11 .    ? 5.122   4.572   78.790  1.00 41.02 ? 2977 HOH B O     1 
HETATM 20529 O  O     . HOH EA 11 .    ? 7.855   19.263  97.543  1.00 42.72 ? 2978 HOH B O     1 
HETATM 20530 O  O     . HOH EA 11 .    ? -12.968 9.662   129.912 1.00 42.52 ? 2979 HOH B O     1 
HETATM 20531 O  O     . HOH EA 11 .    ? 8.541   80.416  85.507  1.00 49.96 ? 2980 HOH B O     1 
HETATM 20532 O  O     . HOH EA 11 .    ? 30.760  42.399  55.453  1.00 41.72 ? 2981 HOH B O     1 
HETATM 20533 O  O     . HOH EA 11 .    ? -31.531 30.000  121.524 1.00 51.24 ? 2982 HOH B O     1 
HETATM 20534 O  O     . HOH EA 11 .    ? -22.088 26.033  91.856  1.00 46.45 ? 2983 HOH B O     1 
HETATM 20535 O  O     . HOH EA 11 .    ? 40.002  38.295  89.034  1.00 39.84 ? 2984 HOH B O     1 
HETATM 20536 O  O     . HOH EA 11 .    ? 21.327  6.045   73.157  1.00 44.36 ? 2985 HOH B O     1 
HETATM 20537 O  O     . HOH EA 11 .    ? -5.017  51.685  102.236 1.00 43.16 ? 2986 HOH B O     1 
HETATM 20538 O  O     . HOH EA 11 .    ? 40.786  30.142  90.447  1.00 33.06 ? 2987 HOH B O     1 
HETATM 20539 O  O     . HOH EA 11 .    ? 16.166  35.497  113.714 1.00 36.93 ? 2988 HOH B O     1 
HETATM 20540 O  O     . HOH EA 11 .    ? 7.421   30.783  90.213  1.00 40.57 ? 2989 HOH B O     1 
HETATM 20541 O  O     . HOH EA 11 .    ? 28.079  71.909  81.152  1.00 46.91 ? 2990 HOH B O     1 
HETATM 20542 O  O     . HOH EA 11 .    ? 23.730  68.776  62.186  1.00 36.70 ? 2991 HOH B O     1 
HETATM 20543 O  O     . HOH EA 11 .    ? 32.191  32.362  75.178  1.00 47.61 ? 2992 HOH B O     1 
HETATM 20544 O  O     . HOH EA 11 .    ? 15.011  51.415  56.292  1.00 39.43 ? 2993 HOH B O     1 
HETATM 20545 O  O     . HOH EA 11 .    ? 4.878   43.581  51.148  1.00 32.07 ? 2994 HOH B O     1 
HETATM 20546 O  O     . HOH EA 11 .    ? 27.501  13.095  66.553  1.00 37.63 ? 2995 HOH B O     1 
HETATM 20547 O  O     . HOH EA 11 .    ? 29.929  73.445  72.513  1.00 35.16 ? 2996 HOH B O     1 
HETATM 20548 O  O     . HOH EA 11 .    ? -6.614  2.797   85.077  1.00 36.77 ? 2997 HOH B O     1 
HETATM 20549 O  O     . HOH EA 11 .    ? 32.972  58.852  67.424  1.00 34.00 ? 2998 HOH B O     1 
HETATM 20550 O  O     . HOH EA 11 .    ? -12.979 5.356   86.003  1.00 44.08 ? 2999 HOH B O     1 
HETATM 20551 O  O     . HOH EA 11 .    ? 27.909  50.909  95.915  1.00 40.14 ? 3000 HOH B O     1 
HETATM 20552 O  O     A HOH EA 11 .    ? 2.552   62.226  83.583  0.55 23.75 ? 3001 HOH B O     1 
HETATM 20553 O  O     . HOH EA 11 .    ? -3.542  48.207  87.942  1.00 46.03 ? 3002 HOH B O     1 
HETATM 20554 O  O     . HOH EA 11 .    ? -10.291 30.226  76.327  1.00 40.01 ? 3003 HOH B O     1 
HETATM 20555 O  O     . HOH EA 11 .    ? -18.325 17.407  78.422  1.00 49.68 ? 3004 HOH B O     1 
HETATM 20556 O  O     . HOH EA 11 .    ? 19.827  45.464  89.942  1.00 20.34 ? 3005 HOH B O     1 
HETATM 20557 O  O     . HOH EA 11 .    ? 22.131  77.776  78.232  1.00 46.30 ? 3006 HOH B O     1 
HETATM 20558 O  O     . HOH EA 11 .    ? 6.406   13.618  69.036  1.00 41.14 ? 3007 HOH B O     1 
HETATM 20559 O  O     . HOH EA 11 .    ? 8.985   17.346  123.291 1.00 44.97 ? 3008 HOH B O     1 
HETATM 20560 O  O     . HOH EA 11 .    ? 30.334  70.890  72.863  1.00 34.86 ? 3009 HOH B O     1 
HETATM 20561 O  O     . HOH EA 11 .    ? 33.572  55.677  67.293  1.00 43.50 ? 3010 HOH B O     1 
HETATM 20562 O  O     . HOH EA 11 .    ? 7.035   28.957  91.749  1.00 43.74 ? 3011 HOH B O     1 
HETATM 20563 O  O     . HOH EA 11 .    ? 20.646  68.728  58.611  1.00 40.45 ? 3012 HOH B O     1 
HETATM 20564 O  O     . HOH EA 11 .    ? -15.252 8.096   125.026 1.00 42.65 ? 3013 HOH B O     1 
HETATM 20565 O  O     . HOH EA 11 .    ? 40.369  45.024  90.665  1.00 38.30 ? 3014 HOH B O     1 
HETATM 20566 O  O     . HOH EA 11 .    ? 21.972  14.550  101.133 1.00 46.54 ? 3015 HOH B O     1 
HETATM 20567 O  O     . HOH EA 11 .    ? 17.094  26.307  109.960 1.00 32.72 ? 3016 HOH B O     1 
HETATM 20568 O  O     . HOH EA 11 .    ? -1.957  26.547  64.742  1.00 36.06 ? 3017 HOH B O     1 
HETATM 20569 O  O     . HOH EA 11 .    ? -2.306  51.942  101.101 1.00 30.78 ? 3018 HOH B O     1 
HETATM 20570 O  O     . HOH EA 11 .    ? 33.587  47.691  64.896  1.00 45.88 ? 3019 HOH B O     1 
HETATM 20571 O  O     . HOH EA 11 .    ? 0.616   24.301  99.179  1.00 39.75 ? 3020 HOH B O     1 
HETATM 20572 O  O     . HOH EA 11 .    ? 8.931   -3.192  105.701 1.00 41.70 ? 3021 HOH B O     1 
HETATM 20573 O  O     . HOH EA 11 .    ? -4.694  50.642  88.614  1.00 51.50 ? 3022 HOH B O     1 
HETATM 20574 O  O     . HOH EA 11 .    ? 25.163  27.372  109.714 1.00 44.20 ? 3023 HOH B O     1 
HETATM 20575 O  O     . HOH EA 11 .    ? 3.910   29.948  94.335  1.00 36.29 ? 3024 HOH B O     1 
HETATM 20576 O  O     . HOH EA 11 .    ? 32.646  20.836  76.155  1.00 37.48 ? 3025 HOH B O     1 
HETATM 20577 O  O     . HOH EA 11 .    ? 7.179   50.026  90.486  1.00 43.42 ? 3026 HOH B O     1 
HETATM 20578 O  O     . HOH EA 11 .    ? 5.337   44.905  53.764  1.00 34.12 ? 3027 HOH B O     1 
HETATM 20579 O  O     . HOH EA 11 .    ? -11.889 30.100  81.608  1.00 41.80 ? 3028 HOH B O     1 
HETATM 20580 O  O     . HOH EA 11 .    ? 13.241  35.421  109.667 1.00 35.50 ? 3029 HOH B O     1 
HETATM 20581 O  O     . HOH EA 11 .    ? 15.288  4.092   72.745  1.00 43.79 ? 3030 HOH B O     1 
HETATM 20582 O  O     . HOH EA 11 .    ? 0.127   19.091  75.822  1.00 41.42 ? 3031 HOH B O     1 
HETATM 20583 O  O     . HOH EA 11 .    ? -32.844 16.702  121.824 1.00 40.36 ? 3032 HOH B O     1 
HETATM 20584 O  O     . HOH EA 11 .    ? 5.793   30.589  98.713  1.00 44.50 ? 3033 HOH B O     1 
HETATM 20585 O  O     . HOH EA 11 .    ? 12.322  -1.579  113.302 1.00 48.80 ? 3034 HOH B O     1 
HETATM 20586 O  O     . HOH EA 11 .    ? 11.065  10.101  123.288 1.00 33.02 ? 3035 HOH B O     1 
HETATM 20587 O  O     . HOH EA 11 .    ? 5.651   32.222  87.562  1.00 31.79 ? 3036 HOH B O     1 
HETATM 20588 O  O     . HOH EA 11 .    ? 18.585  7.286   98.412  1.00 41.95 ? 3037 HOH B O     1 
HETATM 20589 O  O     . HOH EA 11 .    ? 39.089  26.504  92.397  1.00 44.70 ? 3038 HOH B O     1 
HETATM 20590 O  O     . HOH EA 11 .    ? 4.293   55.077  114.699 1.00 47.84 ? 3039 HOH B O     1 
HETATM 20591 O  O     . HOH EA 11 .    ? 9.236   24.682  86.279  1.00 43.81 ? 3040 HOH B O     1 
HETATM 20592 O  O     . HOH EA 11 .    ? 9.479   64.245  87.185  1.00 36.54 ? 3041 HOH B O     1 
HETATM 20593 O  O     . HOH EA 11 .    ? 0.274   18.282  71.915  1.00 35.21 ? 3042 HOH B O     1 
HETATM 20594 O  O     . HOH EA 11 .    ? 6.371   60.728  88.058  1.00 37.63 ? 3043 HOH B O     1 
HETATM 20595 O  O     . HOH EA 11 .    ? 21.707  18.466  111.018 1.00 38.47 ? 3044 HOH B O     1 
HETATM 20596 O  O     . HOH EA 11 .    ? 1.392   14.525  79.809  1.00 31.53 ? 3045 HOH B O     1 
HETATM 20597 O  O     . HOH EA 11 .    ? 12.422  21.337  98.716  1.00 36.42 ? 3046 HOH B O     1 
HETATM 20598 O  O     . HOH EA 11 .    ? -2.717  28.489  69.001  1.00 29.05 ? 3047 HOH B O     1 
HETATM 20599 O  O     . HOH EA 11 .    ? 1.048   64.928  87.093  1.00 42.91 ? 3048 HOH B O     1 
HETATM 20600 O  O     . HOH EA 11 .    ? 23.147  71.472  61.684  1.00 44.81 ? 3049 HOH B O     1 
HETATM 20601 O  O     . HOH EA 11 .    ? -7.217  22.357  78.623  1.00 32.84 ? 3050 HOH B O     1 
HETATM 20602 O  O     . HOH EA 11 .    ? -16.306 6.614   122.541 1.00 43.68 ? 3051 HOH B O     1 
HETATM 20603 O  O     . HOH EA 11 .    ? -7.583  -2.882  117.757 1.00 43.82 ? 3052 HOH B O     1 
HETATM 20604 O  O     . HOH EA 11 .    ? 43.026  34.847  93.412  1.00 43.73 ? 3053 HOH B O     1 
HETATM 20605 O  O     . HOH EA 11 .    ? 22.150  14.520  98.434  1.00 47.83 ? 3054 HOH B O     1 
HETATM 20606 O  O     . HOH EA 11 .    ? 30.995  59.143  60.440  1.00 39.31 ? 3055 HOH B O     1 
HETATM 20607 O  O     . HOH EA 11 .    ? 10.373  53.291  89.224  1.00 43.60 ? 3056 HOH B O     1 
HETATM 20608 O  O     . HOH EA 11 .    ? -2.057  19.875  78.815  1.00 40.04 ? 3057 HOH B O     1 
HETATM 20609 O  O     . HOH EA 11 .    ? 37.368  44.463  90.628  1.00 44.35 ? 3058 HOH B O     1 
HETATM 20610 O  O     . HOH EA 11 .    ? 24.945  70.591  65.291  1.00 39.97 ? 3059 HOH B O     1 
HETATM 20611 O  O     . HOH EA 11 .    ? -17.620 6.872   93.172  1.00 38.39 ? 3060 HOH B O     1 
HETATM 20612 O  O     . HOH EA 11 .    ? 34.699  23.077  94.157  1.00 48.24 ? 3061 HOH B O     1 
HETATM 20613 O  O     . HOH EA 11 .    ? 10.370  74.881  60.697  1.00 44.44 ? 3062 HOH B O     1 
HETATM 20614 O  O     . HOH EA 11 .    ? 5.800   10.833  75.229  1.00 34.31 ? 3063 HOH B O     1 
HETATM 20615 O  O     . HOH EA 11 .    ? 30.530  31.010  79.218  1.00 34.18 ? 3064 HOH B O     1 
HETATM 20616 O  O     . HOH EA 11 .    ? 20.716  23.095  109.993 1.00 34.22 ? 3065 HOH B O     1 
HETATM 20617 O  O     . HOH EA 11 .    ? 5.112   31.720  92.883  1.00 34.37 ? 3066 HOH B O     1 
HETATM 20618 O  O     . HOH EA 11 .    ? -8.626  42.232  72.603  1.00 41.63 ? 3067 HOH B O     1 
HETATM 20619 O  O     . HOH EA 11 .    ? 36.242  22.082  64.879  1.00 47.35 ? 3068 HOH B O     1 
HETATM 20620 O  O     . HOH EA 11 .    ? 15.033  22.163  97.804  1.00 29.89 ? 3069 HOH B O     1 
HETATM 20621 O  O     . HOH EA 11 .    ? 8.507   58.033  95.204  1.00 40.69 ? 3070 HOH B O     1 
HETATM 20622 O  O     . HOH EA 11 .    ? 3.431   13.199  77.715  1.00 39.65 ? 3071 HOH B O     1 
HETATM 20623 O  O     . HOH EA 11 .    ? 33.178  40.564  59.207  1.00 47.14 ? 3072 HOH B O     1 
HETATM 20624 O  O     . HOH EA 11 .    ? 11.891  0.964   113.783 1.00 41.92 ? 3073 HOH B O     1 
HETATM 20625 O  O     B HOH EA 11 .    ? -3.479  60.165  85.397  0.45 27.58 ? 3074 HOH B O     1 
HETATM 20626 O  O     . HOH EA 11 .    ? -2.612  69.517  75.751  1.00 34.98 ? 3075 HOH B O     1 
HETATM 20627 O  O     . HOH EA 11 .    ? 26.340  69.331  61.762  1.00 43.46 ? 3076 HOH B O     1 
HETATM 20628 O  O     . HOH EA 11 .    ? -2.368  41.162  78.147  1.00 34.85 ? 3077 HOH B O     1 
HETATM 20629 O  O     . HOH EA 11 .    ? 1.724   11.364  76.944  1.00 41.50 ? 3078 HOH B O     1 
HETATM 20630 O  O     . HOH EA 11 .    ? 25.705  11.601  68.049  1.00 44.93 ? 3079 HOH B O     1 
HETATM 20631 O  O     . HOH EA 11 .    ? 6.810   2.498   79.839  1.00 39.46 ? 3080 HOH B O     1 
HETATM 20632 O  O     . HOH EA 11 .    ? 21.645  11.540  98.938  1.00 45.01 ? 3081 HOH B O     1 
HETATM 20633 O  O     . HOH EA 11 .    ? 14.068  25.149  100.975 1.00 27.99 ? 3082 HOH B O     1 
HETATM 20634 O  O     . HOH EA 11 .    ? 11.346  53.367  87.155  1.00 43.86 ? 3083 HOH B O     1 
HETATM 20635 O  O     . HOH EA 11 .    ? 12.737  18.365  92.067  1.00 35.67 ? 3084 HOH B O     1 
HETATM 20636 O  O     . HOH EA 11 .    ? -4.051  40.329  60.733  1.00 32.39 ? 3085 HOH B O     1 
HETATM 20637 O  O     . HOH EA 11 .    ? 0.969   55.784  70.260  1.00 36.08 ? 3086 HOH B O     1 
HETATM 20638 O  O     . HOH EA 11 .    ? -7.801  39.315  73.038  1.00 39.80 ? 3087 HOH B O     1 
HETATM 20639 O  O     . HOH EA 11 .    ? -0.930  46.931  98.561  1.00 47.11 ? 3088 HOH B O     1 
HETATM 20640 O  O     . HOH EA 11 .    ? -8.992  27.461  113.251 1.00 51.35 ? 3089 HOH B O     1 
HETATM 20641 O  O     . HOH EA 11 .    ? 24.376  32.682  115.721 1.00 38.09 ? 3090 HOH B O     1 
HETATM 20642 O  O     . HOH EA 11 .    ? -0.336  3.783   81.426  1.00 44.12 ? 3091 HOH B O     1 
HETATM 20643 O  O     . HOH EA 11 .    ? 14.361  51.875  63.189  1.00 33.10 ? 3092 HOH B O     1 
HETATM 20644 O  O     . HOH EA 11 .    ? 12.811  64.132  85.878  1.00 49.66 ? 3093 HOH B O     1 
HETATM 20645 O  O     . HOH EA 11 .    ? 6.287   42.479  47.125  1.00 46.70 ? 3094 HOH B O     1 
HETATM 20646 O  O     . HOH EA 11 .    ? 22.415  56.660  53.849  1.00 46.94 ? 3095 HOH B O     1 
HETATM 20647 O  O     . HOH EA 11 .    ? 20.240  34.155  115.208 1.00 28.08 ? 3096 HOH B O     1 
HETATM 20648 O  O     . HOH EA 11 .    ? 12.190  43.986  53.617  1.00 29.57 ? 3097 HOH B O     1 
HETATM 20649 O  O     . HOH EA 11 .    ? 10.835  0.877   107.066 1.00 42.60 ? 3098 HOH B O     1 
HETATM 20650 O  O     . HOH EA 11 .    ? 5.880   29.815  86.349  1.00 29.59 ? 3099 HOH B O     1 
HETATM 20651 O  O     . HOH EA 11 .    ? 34.567  26.273  56.607  1.00 31.43 ? 3100 HOH B O     1 
HETATM 20652 O  O     . HOH EA 11 .    ? 6.520   15.975  92.164  1.00 31.82 ? 3101 HOH B O     1 
HETATM 20653 O  O     . HOH EA 11 .    ? 1.237   31.622  82.625  1.00 27.85 ? 3102 HOH B O     1 
HETATM 20654 O  O     . HOH EA 11 .    ? -4.698  3.258   83.323  1.00 48.67 ? 3103 HOH B O     1 
HETATM 20655 O  O     . HOH EA 11 .    ? 25.708  68.435  59.160  1.00 47.29 ? 3104 HOH B O     1 
HETATM 20656 O  O     . HOH EA 11 .    ? -19.482 31.851  88.696  1.00 46.30 ? 3105 HOH B O     1 
HETATM 20657 O  O     . HOH EA 11 .    ? 13.684  36.495  74.190  1.00 21.69 ? 3106 HOH B O     1 
HETATM 20658 O  O     . HOH EA 11 .    ? 9.501   3.935   83.823  1.00 32.04 ? 3107 HOH B O     1 
HETATM 20659 O  O     . HOH EA 11 .    ? 11.376  0.786   97.738  1.00 49.24 ? 3108 HOH B O     1 
HETATM 20660 O  O     . HOH EA 11 .    ? -4.405  -1.176  84.586  1.00 52.89 ? 3109 HOH B O     1 
HETATM 20661 O  O     . HOH EA 11 .    ? -0.670  18.629  68.133  1.00 40.11 ? 3110 HOH B O     1 
HETATM 20662 O  O     . HOH EA 11 .    ? 5.300   3.298   85.949  1.00 33.89 ? 3111 HOH B O     1 
HETATM 20663 O  O     . HOH EA 11 .    ? 9.050   47.847  110.845 1.00 44.47 ? 3112 HOH B O     1 
HETATM 20664 O  O     . HOH EA 11 .    ? 7.435   54.068  90.994  1.00 46.67 ? 3113 HOH B O     1 
HETATM 20665 O  O     . HOH EA 11 .    ? 21.969  19.829  107.259 1.00 28.85 ? 3114 HOH B O     1 
HETATM 20666 O  O     . HOH EA 11 .    ? 15.060  44.259  53.076  1.00 37.97 ? 3115 HOH B O     1 
HETATM 20667 O  O     . HOH EA 11 .    ? -0.405  80.458  77.379  1.00 44.71 ? 3116 HOH B O     1 
HETATM 20668 O  O     . HOH EA 11 .    ? 18.308  3.594   73.310  1.00 39.21 ? 3117 HOH B O     1 
HETATM 20669 O  O     . HOH EA 11 .    ? -13.189 55.304  125.093 1.00 41.81 ? 3118 HOH B O     1 
HETATM 20670 O  O     . HOH EA 11 .    ? 27.306  24.605  106.720 1.00 47.36 ? 3119 HOH B O     1 
HETATM 20671 O  O     . HOH EA 11 .    ? 5.464   50.264  113.224 1.00 40.19 ? 3120 HOH B O     1 
HETATM 20672 O  O     . HOH EA 11 .    ? 6.778   61.069  85.372  1.00 27.14 ? 3121 HOH B O     1 
HETATM 20673 O  O     . HOH EA 11 .    ? 29.146  31.289  81.447  1.00 40.62 ? 3122 HOH B O     1 
HETATM 20674 O  O     . HOH EA 11 .    ? 34.631  27.464  61.190  1.00 35.42 ? 3123 HOH B O     1 
HETATM 20675 O  O     . HOH EA 11 .    ? 5.948   5.320   76.021  1.00 44.93 ? 3124 HOH B O     1 
HETATM 20676 O  O     . HOH EA 11 .    ? 18.415  9.367   95.707  1.00 40.28 ? 3125 HOH B O     1 
HETATM 20677 O  O     . HOH EA 11 .    ? 11.901  1.684   116.235 1.00 44.79 ? 3126 HOH B O     1 
HETATM 20678 O  O     . HOH EA 11 .    ? -3.306  12.540  131.022 1.00 41.18 ? 3127 HOH B O     1 
HETATM 20679 O  O     . HOH EA 11 .    ? 8.744   64.951  66.392  1.00 36.61 ? 3128 HOH B O     1 
HETATM 20680 O  O     . HOH EA 11 .    ? 14.182  24.783  98.388  1.00 33.06 ? 3129 HOH B O     1 
HETATM 20681 O  O     . HOH EA 11 .    ? 1.582   22.156  95.448  1.00 37.98 ? 3130 HOH B O     1 
HETATM 20682 O  O     . HOH EA 11 .    ? 30.553  23.826  74.307  1.00 29.41 ? 3131 HOH B O     1 
HETATM 20683 O  O     . HOH EA 11 .    ? -10.775 33.664  84.128  1.00 48.65 ? 3132 HOH B O     1 
HETATM 20684 O  O     . HOH EA 11 .    ? 14.761  4.682   70.119  1.00 48.40 ? 3133 HOH B O     1 
HETATM 20685 O  O     . HOH EA 11 .    ? 0.044   0.572   127.208 1.00 42.80 ? 3134 HOH B O     1 
HETATM 20686 O  O     . HOH EA 11 .    ? 12.622  0.665   109.154 1.00 40.99 ? 3135 HOH B O     1 
HETATM 20687 O  O     . HOH EA 11 .    ? 1.743   2.227   128.769 1.00 43.97 ? 3136 HOH B O     1 
HETATM 20688 O  O     . HOH EA 11 .    ? -27.605 15.888  83.022  1.00 48.21 ? 3137 HOH B O     1 
HETATM 20689 O  O     . HOH EA 11 .    ? 31.727  69.625  80.282  1.00 31.83 ? 3138 HOH B O     1 
HETATM 20690 O  O     . HOH EA 11 .    ? 15.191  55.672  104.547 1.00 36.87 ? 3139 HOH B O     1 
HETATM 20691 O  O     . HOH EA 11 .    ? -8.805  3.859   84.998  1.00 43.95 ? 3140 HOH B O     1 
HETATM 20692 O  O     . HOH EA 11 .    ? 6.960   23.879  124.737 1.00 37.39 ? 3141 HOH B O     1 
HETATM 20693 O  O     . HOH EA 11 .    ? 41.956  36.952  90.269  1.00 40.34 ? 3142 HOH B O     1 
HETATM 20694 O  O     . HOH EA 11 .    ? 18.722  79.005  65.414  1.00 42.31 ? 3143 HOH B O     1 
HETATM 20695 O  O     . HOH EA 11 .    ? -2.135  26.030  101.186 1.00 41.62 ? 3144 HOH B O     1 
HETATM 20696 O  O     . HOH EA 11 .    ? 36.666  42.094  89.247  1.00 39.90 ? 3145 HOH B O     1 
HETATM 20697 O  O     . HOH EA 11 .    ? 5.094   56.041  67.107  1.00 38.88 ? 3146 HOH B O     1 
HETATM 20698 O  O     . HOH EA 11 .    ? 12.779  55.637  105.750 1.00 36.21 ? 3147 HOH B O     1 
HETATM 20699 O  O     . HOH EA 11 .    ? 15.199  22.516  95.227  1.00 45.67 ? 3148 HOH B O     1 
HETATM 20700 O  O     . HOH EA 11 .    ? 3.610   47.949  89.405  1.00 38.66 ? 3149 HOH B O     1 
HETATM 20701 O  O     . HOH EA 11 .    ? 2.084   44.637  97.233  1.00 33.77 ? 3150 HOH B O     1 
HETATM 20702 O  O     . HOH EA 11 .    ? 9.643   17.069  89.830  1.00 34.51 ? 3151 HOH B O     1 
HETATM 20703 O  O     . HOH EA 11 .    ? -25.180 12.934  86.810  1.00 38.00 ? 3152 HOH B O     1 
HETATM 20704 O  O     . HOH EA 11 .    ? -8.966  -0.528  86.542  1.00 47.30 ? 3153 HOH B O     1 
HETATM 20705 O  O     . HOH EA 11 .    ? 32.485  60.096  62.804  1.00 38.67 ? 3154 HOH B O     1 
HETATM 20706 O  O     . HOH EA 11 .    ? -7.108  25.223  75.054  1.00 32.80 ? 3155 HOH B O     1 
HETATM 20707 O  O     . HOH EA 11 .    ? -16.151 7.736   91.045  1.00 35.93 ? 3156 HOH B O     1 
HETATM 20708 O  O     . HOH EA 11 .    ? 7.685   -0.686  86.783  1.00 45.61 ? 3157 HOH B O     1 
HETATM 20709 O  O     . HOH EA 11 .    ? 15.005  6.990   91.924  1.00 41.06 ? 3158 HOH B O     1 
HETATM 20710 O  O     . HOH EA 11 .    ? -8.245  17.086  79.800  1.00 45.05 ? 3159 HOH B O     1 
HETATM 20711 O  O     . HOH EA 11 .    ? 10.259  28.325  85.309  1.00 37.53 ? 3160 HOH B O     1 
HETATM 20712 O  O     . HOH EA 11 .    ? -8.334  33.731  85.290  1.00 32.96 ? 3161 HOH B O     1 
HETATM 20713 O  O     . HOH EA 11 .    ? 26.247  52.492  84.039  1.00 41.79 ? 3162 HOH B O     1 
HETATM 20714 O  O     . HOH EA 11 .    ? 35.407  38.581  64.076  1.00 43.46 ? 3163 HOH B O     1 
HETATM 20715 O  O     . HOH EA 11 .    ? -2.832  37.836  77.975  1.00 35.48 ? 3164 HOH B O     1 
HETATM 20716 O  O     . HOH EA 11 .    ? 22.744  50.397  68.863  1.00 31.15 ? 3165 HOH B O     1 
HETATM 20717 O  O     . HOH EA 11 .    ? -7.421  37.115  83.966  1.00 37.32 ? 3166 HOH B O     1 
HETATM 20718 O  O     . HOH EA 11 .    ? 9.632   10.399  67.984  1.00 43.21 ? 3167 HOH B O     1 
HETATM 20719 O  O     . HOH EA 11 .    ? 20.137  10.904  96.653  1.00 39.91 ? 3168 HOH B O     1 
HETATM 20720 O  O     . HOH EA 11 .    ? 6.466   -4.847  102.169 1.00 45.40 ? 3169 HOH B O     1 
HETATM 20721 O  O     . HOH EA 11 .    ? 4.903   64.343  86.787  1.00 36.37 ? 3170 HOH B O     1 
HETATM 20722 O  O     . HOH EA 11 .    ? -20.903 16.369  80.166  1.00 39.53 ? 3171 HOH B O     1 
HETATM 20723 O  O     . HOH EA 11 .    ? 13.301  36.826  77.087  1.00 23.08 ? 3172 HOH B O     1 
HETATM 20724 O  O     . HOH EA 11 .    ? -5.629  34.473  61.990  1.00 42.87 ? 3173 HOH B O     1 
HETATM 20725 O  O     . HOH EA 11 .    ? 33.538  19.463  54.038  1.00 36.94 ? 3174 HOH B O     1 
HETATM 20726 O  O     . HOH EA 11 .    ? 0.026   28.903  96.746  1.00 25.01 ? 3175 HOH B O     1 
HETATM 20727 O  O     . HOH EA 11 .    ? 24.064  13.822  96.633  1.00 45.78 ? 3176 HOH B O     1 
HETATM 20728 O  O     . HOH EA 11 .    ? 0.336   28.333  99.387  1.00 40.28 ? 3177 HOH B O     1 
HETATM 20729 O  O     . HOH EA 11 .    ? -7.995  35.362  87.693  1.00 39.81 ? 3178 HOH B O     1 
HETATM 20730 O  O     . HOH EA 11 .    ? -10.800 3.701   86.939  1.00 40.25 ? 3179 HOH B O     1 
HETATM 20731 O  O     . HOH EA 11 .    ? -11.311 2.029   88.975  1.00 41.61 ? 3180 HOH B O     1 
HETATM 20732 O  O     . HOH EA 11 .    ? -11.049 47.159  77.399  1.00 41.31 ? 3181 HOH B O     1 
HETATM 20733 O  O     . HOH EA 11 .    ? 2.209   22.040  61.229  1.00 33.56 ? 3182 HOH B O     1 
HETATM 20734 O  O     . HOH EA 11 .    ? -4.335  23.228  72.548  1.00 38.39 ? 3183 HOH B O     1 
HETATM 20735 O  O     . HOH EA 11 .    ? 6.285   12.036  73.079  1.00 40.71 ? 3184 HOH B O     1 
HETATM 20736 O  O     . HOH EA 11 .    ? 21.463  4.454   70.696  1.00 43.42 ? 3185 HOH B O     1 
HETATM 20737 O  O     . HOH EA 11 .    ? 24.417  76.516  78.625  1.00 46.59 ? 3186 HOH B O     1 
HETATM 20738 O  O     . HOH EA 11 .    ? -19.368 19.763  79.005  1.00 51.28 ? 3187 HOH B O     1 
HETATM 20739 O  O     . HOH EA 11 .    ? -6.108  17.970  77.972  1.00 44.13 ? 3188 HOH B O     1 
HETATM 20740 O  O     . HOH EA 11 .    ? -18.270 22.146  80.837  1.00 42.55 ? 3189 HOH B O     1 
HETATM 20741 O  O     . HOH EA 11 .    ? 5.556   70.560  87.283  1.00 42.94 ? 3190 HOH B O     1 
HETATM 20742 O  O     . HOH EA 11 .    ? 13.989  44.696  49.556  1.00 42.09 ? 3191 HOH B O     1 
HETATM 20743 O  O     . HOH EA 11 .    ? 0.610   19.980  64.570  1.00 43.07 ? 3192 HOH B O     1 
HETATM 20744 O  O     . HOH EA 11 .    ? -23.232 14.038  82.450  1.00 36.17 ? 3193 HOH B O     1 
HETATM 20745 O  O     . HOH EA 11 .    ? 6.731   56.120  93.116  1.00 46.00 ? 3194 HOH B O     1 
HETATM 20746 O  O     . HOH EA 11 .    ? 1.900   44.304  78.804  1.00 31.29 ? 3195 HOH B O     1 
HETATM 20747 O  O     . HOH EA 11 .    ? -12.538 -0.569  121.681 1.00 45.52 ? 3196 HOH B O     1 
HETATM 20748 O  O     . HOH EA 11 .    ? -1.259  23.347  63.944  1.00 34.80 ? 3197 HOH B O     1 
HETATM 20749 O  O     . HOH EA 11 .    ? 36.225  28.064  56.047  1.00 42.30 ? 3198 HOH B O     1 
HETATM 20750 O  O     . HOH EA 11 .    ? -7.496  39.332  59.374  1.00 46.50 ? 3199 HOH B O     1 
HETATM 20751 O  O     . HOH EA 11 .    ? 7.806   68.974  87.459  1.00 45.88 ? 3200 HOH B O     1 
HETATM 20752 O  O     . HOH EA 11 .    ? 5.195   -5.937  91.812  1.00 46.40 ? 3201 HOH B O     1 
HETATM 20753 O  O     . HOH EA 11 .    ? 3.273   15.013  75.614  1.00 37.65 ? 3202 HOH B O     1 
HETATM 20754 O  O     . HOH EA 11 .    ? 2.350   32.103  85.078  1.00 25.94 ? 3203 HOH B O     1 
HETATM 20755 O  O     . HOH EA 11 .    ? 34.673  47.718  69.067  1.00 43.69 ? 3204 HOH B O     1 
HETATM 20756 O  O     . HOH EA 11 .    ? 7.135   18.952  89.879  1.00 40.63 ? 3205 HOH B O     1 
HETATM 20757 O  O     . HOH EA 11 .    ? -9.313  34.891  90.500  1.00 46.85 ? 3206 HOH B O     1 
HETATM 20758 O  O     . HOH EA 11 .    ? 7.877   46.104  52.457  1.00 44.14 ? 3207 HOH B O     1 
HETATM 20759 O  O     . HOH EA 11 .    ? -13.947 23.088  81.317  1.00 42.92 ? 3208 HOH B O     1 
HETATM 20760 O  O     . HOH EA 11 .    ? 14.465  44.381  47.354  1.00 49.47 ? 3209 HOH B O     1 
HETATM 20761 O  O     . HOH EA 11 .    ? -4.934  11.214  80.552  1.00 51.78 ? 3210 HOH B O     1 
HETATM 20762 O  O     . HOH EA 11 .    ? -4.883  23.704  75.065  1.00 34.26 ? 3211 HOH B O     1 
HETATM 20763 O  O     . HOH EA 11 .    ? -9.250  -3.266  85.915  1.00 49.35 ? 3212 HOH B O     1 
HETATM 20764 O  O     . HOH EA 11 .    ? 6.185   1.390   82.265  1.00 43.38 ? 3213 HOH B O     1 
HETATM 20765 O  O     . HOH EA 11 .    ? 22.028  31.268  45.276  1.00 38.26 ? 3214 HOH B O     1 
HETATM 20766 O  O     . HOH EA 11 .    ? -2.646  23.693  61.422  1.00 45.02 ? 3215 HOH B O     1 
HETATM 20767 O  O     . HOH EA 11 .    ? 11.203  60.172  92.661  1.00 43.58 ? 3216 HOH B O     1 
HETATM 20768 O  O     . HOH EA 11 .    ? -24.703 12.583  84.205  1.00 41.36 ? 3217 HOH B O     1 
HETATM 20769 O  O     . HOH EA 11 .    ? 19.550  31.885  45.261  1.00 46.64 ? 3218 HOH B O     1 
HETATM 20770 O  O     . HOH EA 11 .    ? -15.698 5.780   88.730  1.00 45.86 ? 3219 HOH B O     1 
HETATM 20771 O  O     . HOH EA 11 .    ? 7.313   2.058   84.324  1.00 38.09 ? 3220 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   ? 0.5424 0.5431 0.6020 0.0730  -0.0056 -0.0685 14   ALA A N   
2     C CA  . ALA A 16   ? 0.5845 0.5847 0.6372 0.0701  -0.0039 -0.0650 14   ALA A CA  
3     C C   . ALA A 16   ? 0.5488 0.5554 0.5946 0.0689  0.0005  -0.0601 14   ALA A C   
4     O O   . ALA A 16   ? 0.5806 0.5963 0.6240 0.0717  0.0026  -0.0625 14   ALA A O   
5     C CB  . ALA A 16   ? 0.6301 0.6333 0.6814 0.0725  -0.0050 -0.0710 14   ALA A CB  
6     N N   . PRO A 17   ? 0.5627 0.5648 0.6057 0.0646  0.0017  -0.0531 15   PRO A N   
7     C CA  . PRO A 17   ? 0.4605 0.4679 0.4977 0.0632  0.0056  -0.0481 15   PRO A CA  
8     C C   . PRO A 17   ? 0.5024 0.5174 0.5334 0.0644  0.0078  -0.0495 15   PRO A C   
9     O O   . PRO A 17   ? 0.4643 0.4777 0.4934 0.0643  0.0067  -0.0515 15   PRO A O   
10    C CB  . PRO A 17   ? 0.5143 0.5143 0.5501 0.0585  0.0057  -0.0415 15   PRO A CB  
11    C CG  . PRO A 17   ? 0.5620 0.5536 0.6041 0.0577  0.0020  -0.0424 15   PRO A CG  
12    C CD  . PRO A 17   ? 0.5104 0.5028 0.5556 0.0611  -0.0004 -0.0495 15   PRO A CD  
13    N N   . ALA A 18   ? 0.4150 0.4385 0.4431 0.0656  0.0109  -0.0484 16   ALA A N   
14    C CA  . ALA A 18   ? 0.3853 0.4170 0.4076 0.0669  0.0132  -0.0490 16   ALA A CA  
15    C C   . ALA A 18   ? 0.3574 0.3858 0.3747 0.0631  0.0143  -0.0437 16   ALA A C   
16    O O   . ALA A 18   ? 0.3570 0.3803 0.3741 0.0597  0.0149  -0.0381 16   ALA A O   
17    C CB  . ALA A 18   ? 0.4078 0.4496 0.4285 0.0685  0.0164  -0.0479 16   ALA A CB  
18    N N   . PRO A 19   ? 0.3489 0.3801 0.3621 0.0638  0.0145  -0.0455 17   PRO A N   
19    C CA  . PRO A 19   ? 0.3162 0.3440 0.3251 0.0604  0.0152  -0.0407 17   PRO A CA  
20    C C   . PRO A 19   ? 0.3180 0.3489 0.3236 0.0582  0.0185  -0.0341 17   PRO A C   
21    O O   . PRO A 19   ? 0.3434 0.3831 0.3472 0.0599  0.0208  -0.0337 17   PRO A O   
22    C CB  . PRO A 19   ? 0.3550 0.3878 0.3603 0.0625  0.0151  -0.0446 17   PRO A CB  
23    C CG  . PRO A 19   ? 0.3817 0.4165 0.3911 0.0664  0.0128  -0.0522 17   PRO A CG  
24    C CD  . PRO A 19   ? 0.3417 0.3791 0.3547 0.0678  0.0136  -0.0524 17   PRO A CD  
25    N N   . PHE A 20   ? 0.3003 0.3241 0.3056 0.0543  0.0184  -0.0291 18   PHE A N   
26    C CA  . PHE A 20   ? 0.3162 0.3412 0.3189 0.0516  0.0209  -0.0227 18   PHE A CA  
27    C C   . PHE A 20   ? 0.3151 0.3435 0.3202 0.0520  0.0225  -0.0207 18   PHE A C   
28    O O   . PHE A 20   ? 0.3543 0.3855 0.3577 0.0502  0.0247  -0.0158 18   PHE A O   
29    C CB  . PHE A 20   ? 0.3185 0.3500 0.3159 0.0519  0.0230  -0.0210 18   PHE A CB  
30    C CG  . PHE A 20   ? 0.2964 0.3250 0.2912 0.0515  0.0216  -0.0225 18   PHE A CG  
31    C CD1 . PHE A 20   ? 0.2979 0.3192 0.2918 0.0481  0.0210  -0.0190 18   PHE A CD1 
32    C CD2 . PHE A 20   ? 0.3041 0.3374 0.2975 0.0545  0.0209  -0.0277 18   PHE A CD2 
33    C CE1 . PHE A 20   ? 0.3372 0.3559 0.3289 0.0476  0.0198  -0.0203 18   PHE A CE1 
34    C CE2 . PHE A 20   ? 0.3348 0.3654 0.3259 0.0541  0.0196  -0.0291 18   PHE A CE2 
35    C CZ  . PHE A 20   ? 0.3276 0.3509 0.3180 0.0506  0.0190  -0.0253 18   PHE A CZ  
36    N N   . ALA A 21   ? 0.3813 0.4095 0.3907 0.0541  0.0211  -0.0244 19   ALA A N   
37    C CA  . ALA A 21   ? 0.3775 0.4089 0.3896 0.0544  0.0225  -0.0227 19   ALA A CA  
38    C C   . ALA A 21   ? 0.3776 0.4028 0.3909 0.0507  0.0226  -0.0172 19   ALA A C   
39    O O   . ALA A 21   ? 0.4446 0.4730 0.4589 0.0501  0.0243  -0.0142 19   ALA A O   
40    C CB  . ALA A 21   ? 0.4222 0.4539 0.4392 0.0576  0.0206  -0.0281 19   ALA A CB  
41    N N   . ASP A 22   ? 0.3325 0.3494 0.3458 0.0481  0.0208  -0.0159 20   ASP A N   
42    C CA  . ASP A 22   ? 0.4147 0.4257 0.4291 0.0447  0.0206  -0.0112 20   ASP A CA  
43    C C   . ASP A 22   ? 0.3081 0.3153 0.3188 0.0418  0.0207  -0.0082 20   ASP A C   
44    O O   . ASP A 22   ? 0.3189 0.3192 0.3305 0.0394  0.0193  -0.0063 20   ASP A O   
45    C CB  . ASP A 22   ? 0.3991 0.4036 0.4182 0.0445  0.0179  -0.0126 20   ASP A CB  
46    C CG  . ASP A 22   ? 0.5708 0.5788 0.5940 0.0470  0.0178  -0.0148 20   ASP A CG  
47    O OD1 . ASP A 22   ? 0.7319 0.7439 0.7554 0.0466  0.0198  -0.0121 20   ASP A OD1 
48    O OD2 . ASP A 22   ? 0.6585 0.6654 0.6851 0.0494  0.0158  -0.0193 20   ASP A OD2 
49    N N   . PHE A 23   ? 0.2850 0.2970 0.2917 0.0423  0.0224  -0.0076 21   PHE A N   
50    C CA  . PHE A 23   ? 0.2623 0.2709 0.2657 0.0401  0.0223  -0.0055 21   PHE A CA  
51    C C   . PHE A 23   ? 0.2650 0.2697 0.2684 0.0366  0.0228  -0.0004 21   PHE A C   
52    O O   . PHE A 23   ? 0.2771 0.2754 0.2807 0.0345  0.0214  0.0005  21   PHE A O   
53    C CB  . PHE A 23   ? 0.2761 0.2912 0.2754 0.0413  0.0240  -0.0056 21   PHE A CB  
54    C CG  . PHE A 23   ? 0.2535 0.2657 0.2495 0.0390  0.0241  -0.0029 21   PHE A CG  
55    C CD1 . PHE A 23   ? 0.2921 0.2986 0.2878 0.0384  0.0221  -0.0049 21   PHE A CD1 
56    C CD2 . PHE A 23   ? 0.3022 0.3172 0.2962 0.0374  0.0261  0.0016  21   PHE A CD2 
57    C CE1 . PHE A 23   ? 0.2772 0.2810 0.2701 0.0363  0.0221  -0.0026 21   PHE A CE1 
58    C CE2 . PHE A 23   ? 0.3084 0.3204 0.2999 0.0354  0.0260  0.0039  21   PHE A CE2 
59    C CZ  . PHE A 23   ? 0.2927 0.2992 0.2835 0.0350  0.0240  0.0016  21   PHE A CZ  
60    N N   . ALA A 24   ? 0.2642 0.2731 0.2678 0.0360  0.0248  0.0028  22   ALA A N   
61    C CA  . ALA A 24   ? 0.2718 0.2774 0.2756 0.0328  0.0253  0.0073  22   ALA A CA  
62    C C   . ALA A 24   ? 0.2770 0.2866 0.2830 0.0326  0.0269  0.0100  22   ALA A C   
63    O O   . ALA A 24   ? 0.2701 0.2821 0.2752 0.0311  0.0284  0.0137  22   ALA A O   
64    C CB  . ALA A 24   ? 0.3090 0.3147 0.3093 0.0314  0.0261  0.0097  22   ALA A CB  
65    N N   . PRO A 25   ? 0.2783 0.2886 0.2876 0.0338  0.0264  0.0084  23   PRO A N   
66    C CA  . PRO A 25   ? 0.2870 0.3015 0.2986 0.0336  0.0279  0.0108  23   PRO A CA  
67    C C   . PRO A 25   ? 0.2844 0.2949 0.2970 0.0303  0.0278  0.0149  23   PRO A C   
68    O O   . PRO A 25   ? 0.2712 0.2754 0.2843 0.0287  0.0260  0.0149  23   PRO A O   
69    C CB  . PRO A 25   ? 0.3587 0.3730 0.3739 0.0356  0.0267  0.0077  23   PRO A CB  
70    C CG  . PRO A 25   ? 0.3259 0.3330 0.3414 0.0352  0.0242  0.0055  23   PRO A CG  
71    C CD  . PRO A 25   ? 0.3417 0.3482 0.3533 0.0351  0.0242  0.0046  23   PRO A CD  
72    N N   . PRO A 26   ? 0.3006 0.3151 0.3137 0.0292  0.0296  0.0184  24   PRO A N   
73    C CA  . PRO A 26   ? 0.2969 0.3079 0.3114 0.0262  0.0293  0.0219  24   PRO A CA  
74    C C   . PRO A 26   ? 0.2931 0.3015 0.3112 0.0257  0.0281  0.0216  24   PRO A C   
75    O O   . PRO A 26   ? 0.2704 0.2808 0.2904 0.0277  0.0279  0.0194  24   PRO A O   
76    C CB  . PRO A 26   ? 0.3110 0.3280 0.3263 0.0257  0.0315  0.0255  24   PRO A CB  
77    C CG  . PRO A 26   ? 0.3343 0.3586 0.3497 0.0286  0.0329  0.0237  24   PRO A CG  
78    C CD  . PRO A 26   ? 0.3016 0.3245 0.3144 0.0308  0.0318  0.0193  24   PRO A CD  
79    N N   . VAL A 27   ? 0.2472 0.2510 0.2660 0.0231  0.0271  0.0236  25   VAL A N   
80    C CA  . VAL A 27   ? 0.2663 0.2678 0.2883 0.0223  0.0259  0.0238  25   VAL A CA  
81    C C   . VAL A 27   ? 0.3052 0.3120 0.3304 0.0231  0.0271  0.0247  25   VAL A C   
82    O O   . VAL A 27   ? 0.3055 0.3124 0.3334 0.0242  0.0263  0.0234  25   VAL A O   
83    C CB  . VAL A 27   ? 0.2825 0.2798 0.3047 0.0193  0.0249  0.0259  25   VAL A CB  
84    C CG1 . VAL A 27   ? 0.2885 0.2844 0.3139 0.0185  0.0237  0.0264  25   VAL A CG1 
85    C CG2 . VAL A 27   ? 0.2832 0.2755 0.3024 0.0187  0.0237  0.0248  25   VAL A CG2 
86    N N   . ARG A 28   ? 0.3016 0.3132 0.3271 0.0227  0.0290  0.0272  26   ARG A N   
87    C CA  . ARG A 28   ? 0.3628 0.3801 0.3915 0.0233  0.0303  0.0286  26   ARG A CA  
88    C C   . ARG A 28   ? 0.3594 0.3831 0.3870 0.0239  0.0326  0.0303  26   ARG A C   
89    O O   . ARG A 28   ? 0.2991 0.3217 0.3238 0.0232  0.0329  0.0312  26   ARG A O   
90    C CB  . ARG A 28   ? 0.3653 0.3811 0.3974 0.0207  0.0298  0.0313  26   ARG A CB  
91    C CG  . ARG A 28   ? 0.4010 0.4161 0.4327 0.0183  0.0303  0.0345  26   ARG A CG  
92    C CD  . ARG A 28   ? 0.4559 0.4689 0.4911 0.0158  0.0294  0.0365  26   ARG A CD  
93    N NE  . ARG A 28   ? 0.4919 0.4987 0.5262 0.0147  0.0273  0.0351  26   ARG A NE  
94    C CZ  . ARG A 28   ? 0.5132 0.5181 0.5488 0.0150  0.0259  0.0336  26   ARG A CZ  
95    N NH1 . ARG A 28   ? 0.4752 0.4835 0.5134 0.0163  0.0263  0.0332  26   ARG A NH1 
96    N NH2 . ARG A 28   ? 0.4310 0.4308 0.4653 0.0139  0.0240  0.0326  26   ARG A NH2 
97    N N   . PRO A 29   ? 0.2828 0.3134 0.3125 0.0253  0.0342  0.0310  27   PRO A N   
98    C CA  . PRO A 29   ? 0.3456 0.3831 0.3745 0.0256  0.0365  0.0335  27   PRO A CA  
99    C C   . PRO A 29   ? 0.2900 0.3259 0.3200 0.0224  0.0367  0.0379  27   PRO A C   
100   O O   . PRO A 29   ? 0.3224 0.3553 0.3556 0.0203  0.0358  0.0395  27   PRO A O   
101   C CB  . PRO A 29   ? 0.3518 0.3969 0.3839 0.0271  0.0379  0.0337  27   PRO A CB  
102   C CG  . PRO A 29   ? 0.3621 0.4044 0.3952 0.0290  0.0364  0.0296  27   PRO A CG  
103   C CD  . PRO A 29   ? 0.3273 0.3604 0.3602 0.0268  0.0341  0.0293  27   PRO A CD  
104   N N   . GLN A 30   ? 0.3124 0.3504 0.3399 0.0222  0.0377  0.0398  28   GLN A N   
105   C CA  . GLN A 30   ? 0.3460 0.3818 0.3746 0.0194  0.0376  0.0437  28   GLN A CA  
106   C C   . GLN A 30   ? 0.3259 0.3677 0.3589 0.0182  0.0391  0.0481  28   GLN A C   
107   O O   . GLN A 30   ? 0.3612 0.4108 0.3939 0.0195  0.0411  0.0497  28   GLN A O   
108   C CB  . GLN A 30   ? 0.3225 0.3582 0.3471 0.0197  0.0380  0.0442  28   GLN A CB  
109   C CG  . GLN A 30   ? 0.2809 0.3109 0.3014 0.0208  0.0364  0.0400  28   GLN A CG  
110   C CD  . GLN A 30   ? 0.2987 0.3204 0.3200 0.0187  0.0343  0.0393  28   GLN A CD  
111   O OE1 . GLN A 30   ? 0.2920 0.3104 0.3133 0.0167  0.0338  0.0412  28   GLN A OE1 
112   N NE2 . GLN A 30   ? 0.3009 0.3195 0.3232 0.0191  0.0331  0.0366  28   GLN A NE2 
113   N N   . SER A 31   ? 0.3107 0.3492 0.3478 0.0158  0.0381  0.0499  29   SER A N   
114   C CA  . SER A 31   ? 0.2779 0.3212 0.3200 0.0143  0.0392  0.0543  29   SER A CA  
115   C C   . SER A 31   ? 0.2979 0.3436 0.3402 0.0130  0.0402  0.0586  29   SER A C   
116   O O   . SER A 31   ? 0.2874 0.3297 0.3262 0.0129  0.0396  0.0582  29   SER A O   
117   C CB  . SER A 31   ? 0.2736 0.3121 0.3201 0.0119  0.0375  0.0547  29   SER A CB  
118   O OG  . SER A 31   ? 0.2771 0.3094 0.3234 0.0098  0.0360  0.0555  29   SER A OG  
119   N N   . THR A 32   ? 0.2641 0.3158 0.3107 0.0119  0.0415  0.0631  30   THR A N   
120   C CA  . THR A 32   ? 0.2546 0.3085 0.3026 0.0102  0.0422  0.0680  30   THR A CA  
121   C C   . THR A 32   ? 0.2783 0.3236 0.3272 0.0079  0.0400  0.0684  30   THR A C   
122   O O   . THR A 32   ? 0.2983 0.3424 0.3452 0.0076  0.0399  0.0698  30   THR A O   
123   C CB  . THR A 32   ? 0.2976 0.3583 0.3516 0.0088  0.0436  0.0731  30   THR A CB  
124   O OG1 . THR A 32   ? 0.3807 0.4503 0.4334 0.0113  0.0458  0.0727  30   THR A OG1 
125   C CG2 . THR A 32   ? 0.3638 0.4264 0.4201 0.0069  0.0440  0.0788  30   THR A CG2 
126   N N   . LEU A 33   ? 0.2729 0.3126 0.3249 0.0064  0.0382  0.0668  31   LEU A N   
127   C CA  . LEU A 33   ? 0.2527 0.2847 0.3058 0.0044  0.0360  0.0665  31   LEU A CA  
128   C C   . LEU A 33   ? 0.2695 0.2963 0.3165 0.0056  0.0351  0.0627  31   LEU A C   
129   O O   . LEU A 33   ? 0.2490 0.2719 0.2954 0.0046  0.0341  0.0634  31   LEU A O   
130   C CB  . LEU A 33   ? 0.2353 0.2635 0.2928 0.0028  0.0342  0.0652  31   LEU A CB  
131   C CG  . LEU A 33   ? 0.2981 0.3299 0.3629 0.0008  0.0345  0.0695  31   LEU A CG  
132   C CD1 . LEU A 33   ? 0.2900 0.3192 0.3584 -0.0002 0.0329  0.0674  31   LEU A CD1 
133   C CD2 . LEU A 33   ? 0.3392 0.3692 0.4076 -0.0014 0.0337  0.0733  31   LEU A CD2 
134   N N   . ARG A 34   ? 0.2422 0.2687 0.2851 0.0078  0.0352  0.0586  32   ARG A N   
135   C CA  . ARG A 34   ? 0.2315 0.2534 0.2690 0.0089  0.0344  0.0551  32   ARG A CA  
136   C C   . ARG A 34   ? 0.2502 0.2754 0.2842 0.0100  0.0356  0.0566  32   ARG A C   
137   O O   . ARG A 34   ? 0.2661 0.2872 0.2975 0.0097  0.0348  0.0558  32   ARG A O   
138   C CB  . ARG A 34   ? 0.2632 0.2845 0.2980 0.0109  0.0341  0.0508  32   ARG A CB  
139   C CG  . ARG A 34   ? 0.2767 0.2934 0.3136 0.0099  0.0324  0.0488  32   ARG A CG  
140   C CD  . ARG A 34   ? 0.2684 0.2780 0.3039 0.0086  0.0304  0.0471  32   ARG A CD  
141   N NE  . ARG A 34   ? 0.2479 0.2547 0.2782 0.0101  0.0300  0.0441  32   ARG A NE  
142   C CZ  . ARG A 34   ? 0.2790 0.2835 0.3076 0.0111  0.0290  0.0408  32   ARG A CZ  
143   N NH1 . ARG A 34   ? 0.2929 0.2974 0.3241 0.0110  0.0284  0.0401  32   ARG A NH1 
144   N NH2 . ARG A 34   ? 0.2943 0.2963 0.3187 0.0123  0.0286  0.0384  32   ARG A NH2 
145   N N   . ARG A 35   ? 0.2450 0.2780 0.2792 0.0112  0.0377  0.0587  33   ARG A N   
146   C CA  . ARG A 35   ? 0.2356 0.2726 0.2663 0.0123  0.0390  0.0603  33   ARG A CA  
147   C C   . ARG A 35   ? 0.2601 0.2957 0.2930 0.0102  0.0386  0.0646  33   ARG A C   
148   O O   . ARG A 35   ? 0.2639 0.2992 0.2935 0.0107  0.0386  0.0649  33   ARG A O   
149   C CB  . ARG A 35   ? 0.2933 0.3401 0.3240 0.0141  0.0414  0.0619  33   ARG A CB  
150   C CG  . ARG A 35   ? 0.3173 0.3659 0.3453 0.0168  0.0417  0.0570  33   ARG A CG  
151   C CD  . ARG A 35   ? 0.4446 0.5035 0.4724 0.0189  0.0441  0.0581  33   ARG A CD  
152   N NE  . ARG A 35   ? 0.5318 0.5918 0.5580 0.0215  0.0440  0.0530  33   ARG A NE  
153   C CZ  . ARG A 35   ? 0.6555 0.7152 0.6771 0.0240  0.0437  0.0487  33   ARG A CZ  
154   N NH1 . ARG A 35   ? 0.6933 0.7524 0.7110 0.0243  0.0436  0.0487  33   ARG A NH1 
155   N NH2 . ARG A 35   ? 0.6469 0.7068 0.6681 0.0262  0.0434  0.0441  33   ARG A NH2 
156   N N   . ALA A 36   ? 0.2324 0.2672 0.2713 0.0078  0.0380  0.0680  34   ALA A N   
157   C CA  . ALA A 36   ? 0.2696 0.3024 0.3115 0.0057  0.0373  0.0720  34   ALA A CA  
158   C C   . ALA A 36   ? 0.2410 0.2654 0.2812 0.0051  0.0351  0.0691  34   ALA A C   
159   O O   . ALA A 36   ? 0.2851 0.3078 0.3251 0.0044  0.0346  0.0711  34   ALA A O   
160   C CB  . ALA A 36   ? 0.2678 0.3012 0.3173 0.0032  0.0369  0.0758  34   ALA A CB  
161   N N   . ILE A 37   ? 0.2489 0.2682 0.2878 0.0053  0.0338  0.0645  35   ILE A N   
162   C CA  . ILE A 37   ? 0.2240 0.2361 0.2605 0.0050  0.0320  0.0614  35   ILE A CA  
163   C C   . ILE A 37   ? 0.2462 0.2589 0.2766 0.0068  0.0326  0.0599  35   ILE A C   
164   O O   . ILE A 37   ? 0.2404 0.2506 0.2700 0.0063  0.0318  0.0607  35   ILE A O   
165   C CB  . ILE A 37   ? 0.2264 0.2342 0.2624 0.0050  0.0307  0.0571  35   ILE A CB  
166   C CG1 . ILE A 37   ? 0.2346 0.2415 0.2768 0.0030  0.0297  0.0583  35   ILE A CG1 
167   C CG2 . ILE A 37   ? 0.1959 0.1975 0.2286 0.0050  0.0290  0.0537  35   ILE A CG2 
168   C CD1 . ILE A 37   ? 0.2365 0.2411 0.2785 0.0032  0.0288  0.0547  35   ILE A CD1 
169   N N   . THR A 38   ? 0.2590 0.2752 0.2856 0.0090  0.0338  0.0576  36   THR A N   
170   C CA  . THR A 38   ? 0.2525 0.2692 0.2735 0.0109  0.0341  0.0555  36   THR A CA  
171   C C   . THR A 38   ? 0.2569 0.2777 0.2774 0.0109  0.0351  0.0595  36   THR A C   
172   O O   . THR A 38   ? 0.2500 0.2688 0.2673 0.0113  0.0345  0.0588  36   THR A O   
173   C CB  . THR A 38   ? 0.2493 0.2698 0.2673 0.0133  0.0351  0.0525  36   THR A CB  
174   O OG1 . THR A 38   ? 0.2431 0.2600 0.2624 0.0131  0.0341  0.0495  36   THR A OG1 
175   C CG2 . THR A 38   ? 0.2438 0.2638 0.2563 0.0152  0.0350  0.0494  36   THR A CG2 
176   N N   . ALA A 39   ? 0.2512 0.2779 0.2752 0.0103  0.0364  0.0640  37   ALA A N   
177   C CA  . ALA A 39   ? 0.2682 0.2998 0.2921 0.0103  0.0375  0.0686  37   ALA A CA  
178   C C   . ALA A 39   ? 0.2870 0.3133 0.3128 0.0085  0.0359  0.0706  37   ALA A C   
179   O O   . ALA A 39   ? 0.2965 0.3252 0.3207 0.0089  0.0362  0.0730  37   ALA A O   
180   C CB  . ALA A 39   ? 0.2247 0.2635 0.2530 0.0096  0.0391  0.0735  37   ALA A CB  
181   N N   . ALA A 40   ? 0.2599 0.2794 0.2892 0.0067  0.0340  0.0694  38   ALA A N   
182   C CA  . ALA A 40   ? 0.2590 0.2733 0.2910 0.0050  0.0323  0.0709  38   ALA A CA  
183   C C   . ALA A 40   ? 0.2528 0.2613 0.2807 0.0056  0.0309  0.0665  38   ALA A C   
184   O O   . ALA A 40   ? 0.2481 0.2523 0.2779 0.0045  0.0294  0.0672  38   ALA A O   
185   C CB  . ALA A 40   ? 0.2254 0.2361 0.2642 0.0027  0.0309  0.0719  38   ALA A CB  
186   N N   . TYR A 41   ? 0.2397 0.2479 0.2623 0.0074  0.0313  0.0621  39   TYR A N   
187   C CA  . TYR A 41   ? 0.2501 0.2526 0.2692 0.0078  0.0299  0.0577  39   TYR A CA  
188   C C   . TYR A 41   ? 0.2603 0.2608 0.2785 0.0076  0.0290  0.0589  39   TYR A C   
189   O O   . TYR A 41   ? 0.2638 0.2588 0.2833 0.0065  0.0273  0.0575  39   TYR A O   
190   C CB  . TYR A 41   ? 0.2420 0.2462 0.2559 0.0100  0.0306  0.0539  39   TYR A CB  
191   C CG  . TYR A 41   ? 0.2403 0.2389 0.2515 0.0103  0.0292  0.0490  39   TYR A CG  
192   C CD1 . TYR A 41   ? 0.2171 0.2103 0.2283 0.0092  0.0276  0.0479  39   TYR A CD1 
193   C CD2 . TYR A 41   ? 0.2672 0.2664 0.2760 0.0117  0.0295  0.0457  39   TYR A CD2 
194   C CE1 . TYR A 41   ? 0.2345 0.2235 0.2433 0.0094  0.0265  0.0438  39   TYR A CE1 
195   C CE2 . TYR A 41   ? 0.2679 0.2624 0.2746 0.0118  0.0282  0.0418  39   TYR A CE2 
196   C CZ  . TYR A 41   ? 0.2309 0.2205 0.2374 0.0106  0.0268  0.0410  39   TYR A CZ  
197   O OH  . TYR A 41   ? 0.2405 0.2261 0.2451 0.0107  0.0256  0.0376  39   TYR A OH  
198   N N   . ARG A 42   ? 0.2843 0.2897 0.3003 0.0087  0.0302  0.0615  40   ARG A N   
199   C CA  . ARG A 42   ? 0.2805 0.2845 0.2955 0.0087  0.0294  0.0627  40   ARG A CA  
200   C C   . ARG A 42   ? 0.2530 0.2616 0.2712 0.0080  0.0301  0.0689  40   ARG A C   
201   O O   . ARG A 42   ? 0.3033 0.3144 0.3194 0.0088  0.0304  0.0708  40   ARG A O   
202   C CB  . ARG A 42   ? 0.3018 0.3069 0.3104 0.0107  0.0298  0.0595  40   ARG A CB  
203   C CG  . ARG A 42   ? 0.2826 0.2823 0.2889 0.0110  0.0287  0.0540  40   ARG A CG  
204   C CD  . ARG A 42   ? 0.3156 0.3161 0.3163 0.0129  0.0289  0.0504  40   ARG A CD  
205   N NE  . ARG A 42   ? 0.2791 0.2756 0.2788 0.0130  0.0281  0.0460  40   ARG A NE  
206   C CZ  . ARG A 42   ? 0.2850 0.2758 0.2846 0.0121  0.0266  0.0435  40   ARG A CZ  
207   N NH1 . ARG A 42   ? 0.2896 0.2778 0.2899 0.0113  0.0256  0.0444  40   ARG A NH1 
208   N NH2 . ARG A 42   ? 0.2566 0.2445 0.2558 0.0120  0.0260  0.0403  40   ARG A NH2 
209   N N   . ARG A 43   ? 0.2558 0.2657 0.2797 0.0065  0.0304  0.0721  41   ARG A N   
210   C CA  . ARG A 43   ? 0.2611 0.2756 0.2889 0.0056  0.0310  0.0786  41   ARG A CA  
211   C C   . ARG A 43   ? 0.3121 0.3231 0.3422 0.0047  0.0294  0.0808  41   ARG A C   
212   O O   . ARG A 43   ? 0.2845 0.2886 0.3165 0.0038  0.0274  0.0782  41   ARG A O   
213   C CB  . ARG A 43   ? 0.2763 0.2914 0.3107 0.0037  0.0310  0.0813  41   ARG A CB  
214   C CG  . ARG A 43   ? 0.2755 0.2948 0.3155 0.0023  0.0314  0.0885  41   ARG A CG  
215   C CD  . ARG A 43   ? 0.3068 0.3279 0.3525 0.0008  0.0318  0.0905  41   ARG A CD  
216   N NE  . ARG A 43   ? 0.3214 0.3483 0.3634 0.0024  0.0340  0.0889  41   ARG A NE  
217   C CZ  . ARG A 43   ? 0.2939 0.3212 0.3384 0.0018  0.0343  0.0878  41   ARG A CZ  
218   N NH1 . ARG A 43   ? 0.3034 0.3259 0.3541 -0.0003 0.0327  0.0880  41   ARG A NH1 
219   N NH2 . ARG A 43   ? 0.2933 0.3263 0.3343 0.0035  0.0363  0.0862  41   ARG A NH2 
220   N N   . PRO A 44   ? 0.3016 0.3175 0.3314 0.0050  0.0301  0.0856  42   PRO A N   
221   C CA  . PRO A 44   ? 0.3268 0.3395 0.3594 0.0043  0.0284  0.0881  42   PRO A CA  
222   C C   . PRO A 44   ? 0.2855 0.2924 0.3260 0.0019  0.0264  0.0894  42   PRO A C   
223   O O   . PRO A 44   ? 0.2951 0.3034 0.3408 0.0005  0.0266  0.0919  42   PRO A O   
224   C CB  . PRO A 44   ? 0.3306 0.3511 0.3631 0.0046  0.0297  0.0945  42   PRO A CB  
225   C CG  . PRO A 44   ? 0.3508 0.3783 0.3771 0.0067  0.0321  0.0928  42   PRO A CG  
226   C CD  . PRO A 44   ? 0.3135 0.3386 0.3401 0.0065  0.0324  0.0886  42   PRO A CD  
227   N N   . GLU A 45   ? 0.3078 0.3084 0.3496 0.0016  0.0242  0.0874  43   GLU A N   
228   C CA  . GLU A 45   ? 0.2945 0.2892 0.3439 -0.0003 0.0220  0.0873  43   GLU A CA  
229   C C   . GLU A 45   ? 0.3110 0.3080 0.3682 -0.0021 0.0216  0.0944  43   GLU A C   
230   O O   . GLU A 45   ? 0.3345 0.3290 0.3987 -0.0038 0.0205  0.0951  43   GLU A O   
231   C CB  . GLU A 45   ? 0.3680 0.3566 0.4169 0.0000  0.0199  0.0840  43   GLU A CB  
232   C CG  . GLU A 45   ? 0.3681 0.3502 0.4219 -0.0012 0.0176  0.0804  43   GLU A CG  
233   C CD  . GLU A 45   ? 0.3139 0.2910 0.3644 -0.0002 0.0163  0.0748  43   GLU A CD  
234   O OE1 . GLU A 45   ? 0.2880 0.2663 0.3318 0.0013  0.0171  0.0732  43   GLU A OE1 
235   O OE2 . GLU A 45   ? 0.2764 0.2486 0.3312 -0.0011 0.0143  0.0719  43   GLU A OE2 
236   N N   . THR A 46   ? 0.3681 0.3702 0.4248 -0.0017 0.0225  0.0998  44   THR A N   
237   C CA  . THR A 46   ? 0.3684 0.3735 0.4327 -0.0034 0.0222  0.1074  44   THR A CA  
238   C C   . THR A 46   ? 0.3242 0.3344 0.3909 -0.0044 0.0239  0.1100  44   THR A C   
239   O O   . THR A 46   ? 0.3658 0.3767 0.4408 -0.0064 0.0232  0.1152  44   THR A O   
240   C CB  . THR A 46   ? 0.3097 0.3205 0.3720 -0.0026 0.0230  0.1129  44   THR A CB  
241   O OG1 . THR A 46   ? 0.3408 0.3583 0.3944 -0.0006 0.0256  0.1117  44   THR A OG1 
242   C CG2 . THR A 46   ? 0.3167 0.3222 0.3786 -0.0020 0.0209  0.1114  44   THR A CG2 
243   N N   . GLU A 47   ? 0.2940 0.3078 0.3542 -0.0029 0.0261  0.1066  45   GLU A N   
244   C CA  . GLU A 47   ? 0.3308 0.3495 0.3933 -0.0037 0.0277  0.1085  45   GLU A CA  
245   C C   . GLU A 47   ? 0.2922 0.3052 0.3586 -0.0049 0.0264  0.1044  45   GLU A C   
246   O O   . GLU A 47   ? 0.3312 0.3463 0.4031 -0.0064 0.0267  0.1071  45   GLU A O   
247   C CB  . GLU A 47   ? 0.3884 0.4141 0.4427 -0.0014 0.0305  0.1067  45   GLU A CB  
248   C CG  . GLU A 47   ? 0.4774 0.5101 0.5274 0.0000  0.0319  0.1105  45   GLU A CG  
249   C CD  . GLU A 47   ? 0.4942 0.5337 0.5363 0.0025  0.0344  0.1077  45   GLU A CD  
250   O OE1 . GLU A 47   ? 0.4898 0.5298 0.5311 0.0028  0.0353  0.1044  45   GLU A OE1 
251   O OE2 . GLU A 47   ? 0.6418 0.6864 0.6788 0.0042  0.0354  0.1088  45   GLU A OE2 
252   N N   . CYS A 48   ? 0.2880 0.2941 0.3517 -0.0043 0.0249  0.0979  46   CYS A N   
253   C CA  . CYS A 48   ? 0.2864 0.2875 0.3531 -0.0052 0.0236  0.0936  46   CYS A CA  
254   C C   . CYS A 48   ? 0.2380 0.2350 0.3146 -0.0075 0.0212  0.0960  46   CYS A C   
255   O O   . CYS A 48   ? 0.2745 0.2705 0.3560 -0.0089 0.0206  0.0954  46   CYS A O   
256   C CB  . CYS A 48   ? 0.2769 0.2725 0.3381 -0.0039 0.0227  0.0864  46   CYS A CB  
257   S SG  . CYS A 48   ? 0.3015 0.3004 0.3520 -0.0013 0.0250  0.0822  46   CYS A SG  
258   N N   . LEU A 49   ? 0.2881 0.2823 0.3679 -0.0080 0.0195  0.0983  47   LEU A N   
259   C CA  . LEU A 49   ? 0.3251 0.3136 0.4141 -0.0098 0.0165  0.0985  47   LEU A CA  
260   C C   . LEU A 49   ? 0.2976 0.2886 0.3960 -0.0121 0.0161  0.1047  47   LEU A C   
261   O O   . LEU A 49   ? 0.3078 0.2949 0.4130 -0.0136 0.0142  0.1030  47   LEU A O   
262   C CB  . LEU A 49   ? 0.3425 0.3270 0.4327 -0.0095 0.0146  0.0988  47   LEU A CB  
263   C CG  . LEU A 49   ? 0.3112 0.2892 0.3984 -0.0085 0.0129  0.0912  47   LEU A CG  
264   C CD1 . LEU A 49   ? 0.3137 0.2870 0.4073 -0.0098 0.0106  0.0877  47   LEU A CD1 
265   C CD2 . LEU A 49   ? 0.2823 0.2619 0.3590 -0.0065 0.0149  0.0864  47   LEU A CD2 
266   N N   . PRO A 50   ? 0.3373 0.3347 0.4368 -0.0125 0.0178  0.1118  48   PRO A N   
267   C CA  . PRO A 50   ? 0.3413 0.3410 0.4509 -0.0149 0.0172  0.1183  48   PRO A CA  
268   C C   . PRO A 50   ? 0.2877 0.2875 0.4006 -0.0161 0.0173  0.1164  48   PRO A C   
269   O O   . PRO A 50   ? 0.3675 0.3638 0.4900 -0.0181 0.0149  0.1172  48   PRO A O   
270   C CB  . PRO A 50   ? 0.3137 0.3222 0.4208 -0.0146 0.0198  0.1256  48   PRO A CB  
271   C CG  . PRO A 50   ? 0.3341 0.3423 0.4335 -0.0125 0.0202  0.1239  48   PRO A CG  
272   C CD  . PRO A 50   ? 0.2910 0.2940 0.3836 -0.0109 0.0199  0.1147  48   PRO A CD  
273   N N   . PRO A 51   ? 0.2754 0.2793 0.3814 -0.0148 0.0198  0.1136  49   PRO A N   
274   C CA  . PRO A 51   ? 0.3115 0.3155 0.4214 -0.0159 0.0197  0.1117  49   PRO A CA  
275   C C   . PRO A 51   ? 0.2775 0.2734 0.3898 -0.0163 0.0168  0.1051  49   PRO A C   
276   O O   . PRO A 51   ? 0.3210 0.3156 0.4401 -0.0179 0.0155  0.1047  49   PRO A O   
277   C CB  . PRO A 51   ? 0.3024 0.3120 0.4034 -0.0140 0.0228  0.1095  49   PRO A CB  
278   C CG  . PRO A 51   ? 0.3273 0.3367 0.4194 -0.0117 0.0237  0.1071  49   PRO A CG  
279   C CD  . PRO A 51   ? 0.3144 0.3230 0.4097 -0.0123 0.0226  0.1118  49   PRO A CD  
280   N N   . LEU A 52   ? 0.2914 0.2824 0.3983 -0.0148 0.0159  0.0998  50   LEU A N   
281   C CA  . LEU A 52   ? 0.2708 0.2549 0.3801 -0.0150 0.0132  0.0936  50   LEU A CA  
282   C C   . LEU A 52   ? 0.2833 0.2631 0.4032 -0.0169 0.0100  0.0957  50   LEU A C   
283   O O   . LEU A 52   ? 0.2812 0.2576 0.4075 -0.0181 0.0078  0.0929  50   LEU A O   
284   C CB  . LEU A 52   ? 0.2715 0.2523 0.3723 -0.0130 0.0131  0.0878  50   LEU A CB  
285   C CG  . LEU A 52   ? 0.2967 0.2810 0.3874 -0.0111 0.0158  0.0851  50   LEU A CG  
286   C CD1 . LEU A 52   ? 0.2755 0.2567 0.3588 -0.0092 0.0156  0.0807  50   LEU A CD1 
287   C CD2 . LEU A 52   ? 0.3159 0.3000 0.4064 -0.0113 0.0158  0.0811  50   LEU A CD2 
288   N N   . VAL A 53   ? 0.3119 0.2919 0.4344 -0.0171 0.0096  0.1005  51   VAL A N   
289   C CA  . VAL A 53   ? 0.3228 0.2990 0.4565 -0.0190 0.0065  0.1036  51   VAL A CA  
290   C C   . VAL A 53   ? 0.3231 0.3015 0.4660 -0.0214 0.0060  0.1074  51   VAL A C   
291   O O   . VAL A 53   ? 0.3009 0.2748 0.4526 -0.0228 0.0030  0.1056  51   VAL A O   
292   C CB  . VAL A 53   ? 0.3085 0.2861 0.4432 -0.0189 0.0066  0.1097  51   VAL A CB  
293   C CG1 . VAL A 53   ? 0.3258 0.3004 0.4734 -0.0211 0.0035  0.1141  51   VAL A CG1 
294   C CG2 . VAL A 53   ? 0.3050 0.2794 0.4323 -0.0168 0.0063  0.1053  51   VAL A CG2 
295   N N   . GLU A 54   ? 0.3044 0.2899 0.4454 -0.0217 0.0089  0.1125  52   GLU A N   
296   C CA  . GLU A 54   ? 0.3459 0.3340 0.4958 -0.0241 0.0086  0.1167  52   GLU A CA  
297   C C   . GLU A 54   ? 0.3054 0.2909 0.4564 -0.0243 0.0075  0.1104  52   GLU A C   
298   O O   . GLU A 54   ? 0.3415 0.3245 0.5025 -0.0263 0.0051  0.1107  52   GLU A O   
299   C CB  . GLU A 54   ? 0.3605 0.3577 0.5075 -0.0242 0.0122  0.1231  52   GLU A CB  
300   C CG  . GLU A 54   ? 0.5020 0.5028 0.6581 -0.0266 0.0121  0.1276  52   GLU A CG  
301   C CD  . GLU A 54   ? 0.5917 0.5890 0.7612 -0.0293 0.0088  0.1322  52   GLU A CD  
302   O OE1 . GLU A 54   ? 0.5365 0.5323 0.7085 -0.0295 0.0078  0.1361  52   GLU A OE1 
303   O OE2 . GLU A 54   ? 0.5764 0.5723 0.7544 -0.0312 0.0071  0.1320  52   GLU A OE2 
304   N N   . ALA A 55   ? 0.2920 0.2780 0.4332 -0.0223 0.0092  0.1045  53   ALA A N   
305   C CA  . ALA A 55   ? 0.2866 0.2708 0.4281 -0.0224 0.0084  0.0988  53   ALA A CA  
306   C C   . ALA A 55   ? 0.3037 0.2806 0.4502 -0.0228 0.0046  0.0932  53   ALA A C   
307   O O   . ALA A 55   ? 0.3228 0.2981 0.4746 -0.0239 0.0028  0.0903  53   ALA A O   
308   C CB  . ALA A 55   ? 0.2845 0.2708 0.4143 -0.0202 0.0109  0.0942  53   ALA A CB  
309   N N   . ALA A 56   ? 0.2877 0.2605 0.4327 -0.0219 0.0033  0.0915  54   ALA A N   
310   C CA  . ALA A 56   ? 0.2792 0.2455 0.4281 -0.0218 -0.0003 0.0857  54   ALA A CA  
311   C C   . ALA A 56   ? 0.3647 0.3278 0.5266 -0.0238 -0.0035 0.0888  54   ALA A C   
312   O O   . ALA A 56   ? 0.3280 0.2858 0.4945 -0.0237 -0.0068 0.0840  54   ALA A O   
313   C CB  . ALA A 56   ? 0.2768 0.2403 0.4180 -0.0197 -0.0002 0.0819  54   ALA A CB  
314   N N   . THR A 57   ? 0.3395 0.3059 0.5077 -0.0256 -0.0029 0.0967  55   THR A N   
315   C CA  . THR A 57   ? 0.3176 0.2809 0.4987 -0.0276 -0.0061 0.1004  55   THR A CA  
316   C C   . THR A 57   ? 0.3551 0.3160 0.5453 -0.0292 -0.0089 0.0973  55   THR A C   
317   O O   . THR A 57   ? 0.3569 0.3212 0.5457 -0.0297 -0.0075 0.0966  55   THR A O   
318   C CB  . THR A 57   ? 0.3289 0.2972 0.5137 -0.0291 -0.0044 0.1105  55   THR A CB  
319   O OG1 . THR A 57   ? 0.3514 0.3214 0.5283 -0.0275 -0.0024 0.1129  55   THR A OG1 
320   C CG2 . THR A 57   ? 0.3837 0.3491 0.5831 -0.0316 -0.0078 0.1153  55   THR A CG2 
321   N N   . GLN A 58   ? 0.3335 0.2886 0.5332 -0.0299 -0.0130 0.0949  56   GLN A N   
322   C CA  . GLN A 58   ? 0.3320 0.2847 0.5418 -0.0314 -0.0162 0.0918  56   GLN A CA  
323   C C   . GLN A 58   ? 0.2898 0.2391 0.5140 -0.0335 -0.0197 0.0964  56   GLN A C   
324   O O   . GLN A 58   ? 0.3427 0.2905 0.5684 -0.0333 -0.0201 0.1003  56   GLN A O   
325   C CB  . GLN A 58   ? 0.3338 0.2826 0.5406 -0.0297 -0.0183 0.0815  56   GLN A CB  
326   C CG  . GLN A 58   ? 0.3069 0.2586 0.4997 -0.0277 -0.0151 0.0771  56   GLN A CG  
327   C CD  . GLN A 58   ? 0.3107 0.2601 0.5019 -0.0266 -0.0171 0.0678  56   GLN A CD  
328   O OE1 . GLN A 58   ? 0.3379 0.2881 0.5335 -0.0276 -0.0183 0.0656  56   GLN A OE1 
329   N NE2 . GLN A 58   ? 0.3358 0.2827 0.5205 -0.0245 -0.0175 0.0623  56   GLN A NE2 
330   N N   . SER A 59   ? 0.3585 0.3067 0.5937 -0.0355 -0.0224 0.0959  57   SER A N   
331   C CA  . SER A 59   ? 0.2966 0.2415 0.5470 -0.0378 -0.0260 0.1004  57   SER A CA  
332   C C   . SER A 59   ? 0.3865 0.3247 0.6408 -0.0365 -0.0296 0.0957  57   SER A C   
333   O O   . SER A 59   ? 0.3896 0.3254 0.6370 -0.0342 -0.0302 0.0874  57   SER A O   
334   C CB  . SER A 59   ? 0.3317 0.2762 0.5929 -0.0399 -0.0285 0.0990  57   SER A CB  
335   O OG  . SER A 59   ? 0.3766 0.3175 0.6372 -0.0385 -0.0311 0.0887  57   SER A OG  
336   N N   . LYS A 60   ? 0.3492 0.2846 0.6152 -0.0381 -0.0322 0.1015  58   LYS A N   
337   C CA  . LYS A 60   ? 0.4017 0.3316 0.6723 -0.0367 -0.0361 0.0967  58   LYS A CA  
338   C C   . LYS A 60   ? 0.3693 0.2943 0.6456 -0.0362 -0.0399 0.0869  58   LYS A C   
339   O O   . LYS A 60   ? 0.4015 0.3226 0.6753 -0.0341 -0.0417 0.0796  58   LYS A O   
340   C CB  . LYS A 60   ? 0.3543 0.2857 0.6344 -0.0375 -0.0383 0.1027  58   LYS A CB  
341   C CG  . LYS A 60   ? 0.4130 0.3390 0.7004 -0.0362 -0.0429 0.0979  58   LYS A CG  
342   C CD  . LYS A 60   ? 0.4799 0.4030 0.7589 -0.0339 -0.0419 0.0959  58   LYS A CD  
343   C CE  . LYS A 60   ? 0.4742 0.3928 0.7613 -0.0327 -0.0464 0.0919  58   LYS A CE  
344   N NZ  . LYS A 60   ? 0.4905 0.4064 0.7697 -0.0304 -0.0455 0.0898  58   LYS A NZ  
345   N N   . GLU A 61   ? 0.3584 0.2851 0.6413 -0.0379 -0.0411 0.0862  59   GLU A N   
346   C CA  . GLU A 61   ? 0.3906 0.3136 0.6789 -0.0375 -0.0448 0.0767  59   GLU A CA  
347   C C   . GLU A 61   ? 0.4013 0.3256 0.6756 -0.0348 -0.0428 0.0683  59   GLU A C   
348   O O   . GLU A 61   ? 0.3929 0.3140 0.6674 -0.0330 -0.0456 0.0594  59   GLU A O   
349   C CB  . GLU A 61   ? 0.3600 0.2860 0.6561 -0.0397 -0.0459 0.0779  59   GLU A CB  
350   N N   . ILE A 62   ? 0.3523 0.2819 0.6141 -0.0344 -0.0380 0.0708  60   ILE A N   
351   C CA  . ILE A 62   ? 0.3471 0.2785 0.5954 -0.0319 -0.0360 0.0633  60   ILE A CA  
352   C C   . ILE A 62   ? 0.3875 0.3165 0.6284 -0.0294 -0.0356 0.0603  60   ILE A C   
353   O O   . ILE A 62   ? 0.3682 0.2960 0.6040 -0.0273 -0.0366 0.0519  60   ILE A O   
354   C CB  . ILE A 62   ? 0.3606 0.2980 0.5984 -0.0320 -0.0311 0.0669  60   ILE A CB  
355   C CG1 . ILE A 62   ? 0.3968 0.3364 0.6396 -0.0336 -0.0319 0.0655  60   ILE A CG1 
356   C CG2 . ILE A 62   ? 0.3814 0.3204 0.6038 -0.0293 -0.0283 0.0618  60   ILE A CG2 
357   C CD1 . ILE A 62   ? 0.3826 0.3281 0.6166 -0.0338 -0.0276 0.0689  60   ILE A CD1 
358   N N   . ARG A 63   ? 0.3609 0.2896 0.6013 -0.0296 -0.0342 0.0672  61   ARG A N   
359   C CA  . ARG A 63   ? 0.3960 0.3227 0.6297 -0.0273 -0.0339 0.0648  61   ARG A CA  
360   C C   . ARG A 63   ? 0.3637 0.2848 0.6058 -0.0263 -0.0387 0.0581  61   ARG A C   
361   O O   . ARG A 63   ? 0.3364 0.2564 0.5720 -0.0239 -0.0389 0.0514  61   ARG A O   
362   C CB  . ARG A 63   ? 0.3576 0.2853 0.5903 -0.0278 -0.0318 0.0739  61   ARG A CB  
363   C CG  . ARG A 63   ? 0.4569 0.3908 0.6792 -0.0281 -0.0268 0.0792  61   ARG A CG  
364   C CD  . ARG A 63   ? 0.5218 0.4576 0.7411 -0.0282 -0.0245 0.0873  61   ARG A CD  
365   N NE  . ARG A 63   ? 0.5078 0.4441 0.7388 -0.0307 -0.0257 0.0961  61   ARG A NE  
366   C CZ  . ARG A 63   ? 0.5705 0.5036 0.8100 -0.0313 -0.0282 0.1001  61   ARG A CZ  
367   N NH1 . ARG A 63   ? 0.5648 0.4938 0.8024 -0.0294 -0.0297 0.0961  61   ARG A NH1 
368   N NH2 . ARG A 63   ? 0.5161 0.4502 0.7662 -0.0339 -0.0291 0.1086  61   ARG A NH2 
369   N N   . ASP A 64   ? 0.4121 0.3300 0.6692 -0.0282 -0.0426 0.0596  62   ASP A N   
370   C CA  . ASP A 64   ? 0.3854 0.2982 0.6516 -0.0272 -0.0475 0.0525  62   ASP A CA  
371   C C   . ASP A 64   ? 0.3931 0.3066 0.6561 -0.0257 -0.0488 0.0420  62   ASP A C   
372   O O   . ASP A 64   ? 0.3894 0.3010 0.6505 -0.0234 -0.0507 0.0342  62   ASP A O   
373   C CB  . ASP A 64   ? 0.3782 0.2873 0.6619 -0.0296 -0.0517 0.0567  62   ASP A CB  
374   C CG  . ASP A 64   ? 0.3345 0.2443 0.6205 -0.0302 -0.0509 0.0658  62   ASP A CG  
375   O OD1 . ASP A 64   ? 0.4896 0.3995 0.7667 -0.0291 -0.0480 0.0687  62   ASP A OD1 
376   O OD2 . ASP A 64   ? 0.4401 0.3511 0.7363 -0.0315 -0.0532 0.0698  62   ASP A OD2 
377   N N   . ALA A 65   ? 0.3477 0.2645 0.6101 -0.0270 -0.0478 0.0419  63   ALA A N   
378   C CA  . ALA A 65   ? 0.3548 0.2732 0.6135 -0.0257 -0.0488 0.0324  63   ALA A CA  
379   C C   . ALA A 65   ? 0.3757 0.2967 0.6186 -0.0231 -0.0456 0.0281  63   ALA A C   
380   O O   . ALA A 65   ? 0.3852 0.3061 0.6255 -0.0211 -0.0473 0.0193  63   ALA A O   
381   C CB  . ALA A 65   ? 0.3872 0.3089 0.6474 -0.0276 -0.0479 0.0341  63   ALA A CB  
382   N N   . ALA A 66   ? 0.3390 0.2627 0.5714 -0.0230 -0.0411 0.0340  64   ALA A N   
383   C CA  . ALA A 66   ? 0.4011 0.3273 0.6190 -0.0207 -0.0380 0.0304  64   ALA A CA  
384   C C   . ALA A 66   ? 0.3862 0.3094 0.6032 -0.0186 -0.0396 0.0264  64   ALA A C   
385   O O   . ALA A 66   ? 0.3652 0.2895 0.5750 -0.0165 -0.0395 0.0193  64   ALA A O   
386   C CB  . ALA A 66   ? 0.3160 0.2455 0.5239 -0.0212 -0.0331 0.0377  64   ALA A CB  
387   N N   . ALA A 67   ? 0.3491 0.2688 0.5734 -0.0192 -0.0410 0.0312  65   ALA A N   
388   C CA  . ALA A 67   ? 0.3965 0.3131 0.6213 -0.0172 -0.0428 0.0274  65   ALA A CA  
389   C C   . ALA A 67   ? 0.3837 0.2985 0.6151 -0.0159 -0.0471 0.0177  65   ALA A C   
390   O O   . ALA A 67   ? 0.3977 0.3126 0.6240 -0.0135 -0.0476 0.0111  65   ALA A O   
391   C CB  . ALA A 67   ? 0.3893 0.3024 0.6227 -0.0182 -0.0441 0.0346  65   ALA A CB  
392   N N   . SER A 68   ? 0.3679 0.2814 0.6106 -0.0174 -0.0503 0.0165  66   SER A N   
393   C CA  . SER A 68   ? 0.3989 0.3110 0.6483 -0.0161 -0.0546 0.0068  66   SER A CA  
394   C C   . SER A 68   ? 0.4429 0.3598 0.6815 -0.0145 -0.0531 -0.0007 66   SER A C   
395   O O   . SER A 68   ? 0.4149 0.3322 0.6522 -0.0122 -0.0550 -0.0090 66   SER A O   
396   C CB  . SER A 68   ? 0.4549 0.3648 0.7191 -0.0183 -0.0584 0.0075  66   SER A CB  
397   O OG  . SER A 68   ? 0.5448 0.4544 0.8146 -0.0170 -0.0624 -0.0024 66   SER A OG  
398   N N   . THR A 69   ? 0.3925 0.3132 0.6231 -0.0155 -0.0497 0.0023  67   THR A N   
399   C CA  . THR A 69   ? 0.3667 0.2921 0.5866 -0.0140 -0.0480 -0.0038 67   THR A CA  
400   C C   . THR A 69   ? 0.3048 0.2316 0.5128 -0.0118 -0.0455 -0.0057 67   THR A C   
401   O O   . THR A 69   ? 0.3566 0.2858 0.5601 -0.0097 -0.0463 -0.0134 67   THR A O   
402   C CB  . THR A 69   ? 0.3732 0.3022 0.5874 -0.0156 -0.0448 0.0007  67   THR A CB  
403   O OG1 . THR A 69   ? 0.3743 0.3025 0.5997 -0.0176 -0.0474 0.0014  67   THR A OG1 
404   C CG2 . THR A 69   ? 0.2962 0.2300 0.4988 -0.0141 -0.0429 -0.0048 67   THR A CG2 
405   N N   . ALA A 70   ? 0.3526 0.2785 0.5556 -0.0121 -0.0425 0.0012  68   ALA A N   
406   C CA  . ALA A 70   ? 0.3687 0.2957 0.5608 -0.0101 -0.0402 -0.0002 68   ALA A CA  
407   C C   . ALA A 70   ? 0.3674 0.2922 0.5641 -0.0081 -0.0435 -0.0065 68   ALA A C   
408   O O   . ALA A 70   ? 0.4041 0.3314 0.5933 -0.0060 -0.0429 -0.0122 68   ALA A O   
409   C CB  . ALA A 70   ? 0.3487 0.2751 0.5362 -0.0108 -0.0369 0.0085  68   ALA A CB  
410   N N   . ARG A 71   ? 0.3692 0.2896 0.5787 -0.0087 -0.0470 -0.0056 69   ARG A N   
411   C CA  . ARG A 71   ? 0.3986 0.3167 0.6138 -0.0066 -0.0505 -0.0122 69   ARG A CA  
412   C C   . ARG A 71   ? 0.3938 0.3149 0.6093 -0.0051 -0.0529 -0.0223 69   ARG A C   
413   O O   . ARG A 71   ? 0.4315 0.3543 0.6429 -0.0026 -0.0534 -0.0288 69   ARG A O   
414   C CB  . ARG A 71   ? 0.3729 0.2854 0.6030 -0.0077 -0.0543 -0.0091 69   ARG A CB  
415   C CG  . ARG A 71   ? 0.3757 0.2857 0.6138 -0.0056 -0.0587 -0.0169 69   ARG A CG  
416   C CD  . ARG A 71   ? 0.4099 0.3140 0.6630 -0.0066 -0.0624 -0.0130 69   ARG A CD  
417   N NE  . ARG A 71   ? 0.4517 0.3538 0.7020 -0.0065 -0.0606 -0.0064 69   ARG A NE  
418   C CZ  . ARG A 71   ? 0.4539 0.3554 0.7012 -0.0041 -0.0610 -0.0099 69   ARG A CZ  
419   N NH1 . ARG A 71   ? 0.4943 0.3973 0.7411 -0.0016 -0.0630 -0.0199 69   ARG A NH1 
420   N NH2 . ARG A 71   ? 0.5140 0.4139 0.7585 -0.0041 -0.0592 -0.0032 69   ARG A NH2 
421   N N   . LYS A 72   ? 0.3529 0.2751 0.5729 -0.0064 -0.0542 -0.0237 70   LYS A N   
422   C CA  . LYS A 72   ? 0.4032 0.3290 0.6234 -0.0049 -0.0564 -0.0332 70   LYS A CA  
423   C C   . LYS A 72   ? 0.4339 0.3655 0.6393 -0.0033 -0.0530 -0.0364 70   LYS A C   
424   O O   . LYS A 72   ? 0.3862 0.3208 0.5894 -0.0011 -0.0544 -0.0445 70   LYS A O   
425   C CB  . LYS A 72   ? 0.3760 0.3023 0.6030 -0.0069 -0.0580 -0.0331 70   LYS A CB  
426   C CG  . LYS A 72   ? 0.4196 0.3503 0.6463 -0.0055 -0.0602 -0.0426 70   LYS A CG  
427   C CD  . LYS A 72   ? 0.4769 0.4075 0.7127 -0.0074 -0.0625 -0.0427 70   LYS A CD  
428   C CE  . LYS A 72   ? 0.5909 0.5257 0.8284 -0.0058 -0.0656 -0.0530 70   LYS A CE  
429   N NZ  . LYS A 72   ? 0.7226 0.6565 0.9714 -0.0075 -0.0688 -0.0540 70   LYS A NZ  
430   N N   . LEU A 73   ? 0.3675 0.3010 0.5629 -0.0045 -0.0486 -0.0301 71   LEU A N   
431   C CA  . LEU A 73   ? 0.3932 0.3318 0.5750 -0.0032 -0.0454 -0.0322 71   LEU A CA  
432   C C   . LEU A 73   ? 0.3859 0.3245 0.5625 -0.0011 -0.0447 -0.0342 71   LEU A C   
433   O O   . LEU A 73   ? 0.4099 0.3528 0.5794 0.0007  -0.0442 -0.0399 71   LEU A O   
434   C CB  . LEU A 73   ? 0.3534 0.2932 0.5267 -0.0048 -0.0410 -0.0247 71   LEU A CB  
435   C CG  . LEU A 73   ? 0.3365 0.2773 0.5132 -0.0068 -0.0411 -0.0224 71   LEU A CG  
436   C CD1 . LEU A 73   ? 0.3470 0.2886 0.5162 -0.0082 -0.0368 -0.0144 71   LEU A CD1 
437   C CD2 . LEU A 73   ? 0.4201 0.3658 0.5942 -0.0059 -0.0423 -0.0296 71   LEU A CD2 
438   N N   . ILE A 74   ? 0.3264 0.2604 0.5063 -0.0014 -0.0446 -0.0293 72   ILE A N   
439   C CA  . ILE A 74   ? 0.3635 0.2974 0.5384 0.0004  -0.0437 -0.0306 72   ILE A CA  
440   C C   . ILE A 74   ? 0.3971 0.3311 0.5786 0.0026  -0.0476 -0.0392 72   ILE A C   
441   O O   . ILE A 74   ? 0.3929 0.3299 0.5683 0.0047  -0.0471 -0.0438 72   ILE A O   
442   C CB  . ILE A 74   ? 0.3858 0.3152 0.5624 -0.0006 -0.0425 -0.0224 72   ILE A CB  
443   C CG1 . ILE A 74   ? 0.4246 0.3556 0.5918 -0.0021 -0.0380 -0.0150 72   ILE A CG1 
444   C CG2 . ILE A 74   ? 0.3898 0.3183 0.5643 0.0014  -0.0426 -0.0243 72   ILE A CG2 
445   C CD1 . ILE A 74   ? 0.3797 0.3071 0.5496 -0.0035 -0.0368 -0.0063 72   ILE A CD1 
446   N N   . GLU A 75   ? 0.4372 0.3681 0.6316 0.0022  -0.0518 -0.0417 73   GLU A N   
447   C CA  . GLU A 75   ? 0.4755 0.4068 0.6768 0.0045  -0.0558 -0.0507 73   GLU A CA  
448   C C   . GLU A 75   ? 0.4519 0.3901 0.6467 0.0061  -0.0558 -0.0588 73   GLU A C   
449   O O   . GLU A 75   ? 0.4384 0.3798 0.6312 0.0086  -0.0567 -0.0656 73   GLU A O   
450   C CB  . GLU A 75   ? 0.4184 0.3450 0.6355 0.0036  -0.0605 -0.0517 73   GLU A CB  
451   C CG  . GLU A 75   ? 0.4432 0.3633 0.6683 0.0031  -0.0617 -0.0460 73   GLU A CG  
452   C CD  . GLU A 75   ? 0.5428 0.4577 0.7832 0.0013  -0.0656 -0.0440 73   GLU A CD  
453   O OE1 . GLU A 75   ? 0.5646 0.4808 0.8096 0.0004  -0.0673 -0.0467 73   GLU A OE1 
454   O OE2 . GLU A 75   ? 0.4579 0.3676 0.7061 0.0009  -0.0671 -0.0395 73   GLU A OE2 
455   N N   . ALA A 76   ? 0.4661 0.4073 0.6574 0.0047  -0.0545 -0.0579 74   ALA A N   
456   C CA  . ALA A 76   ? 0.4497 0.3982 0.6340 0.0061  -0.0542 -0.0646 74   ALA A CA  
457   C C   . ALA A 76   ? 0.4684 0.4210 0.6392 0.0072  -0.0503 -0.0640 74   ALA A C   
458   O O   . ALA A 76   ? 0.5336 0.4918 0.7003 0.0094  -0.0508 -0.0708 74   ALA A O   
459   C CB  . ALA A 76   ? 0.5175 0.4680 0.7006 0.0043  -0.0534 -0.0629 74   ALA A CB  
460   N N   . LEU A 77   ? 0.4567 0.4071 0.6209 0.0059  -0.0466 -0.0558 75   LEU A N   
461   C CA  . LEU A 77   ? 0.4447 0.3985 0.5967 0.0067  -0.0430 -0.0546 75   LEU A CA  
462   C C   . LEU A 77   ? 0.4927 0.4468 0.6456 0.0090  -0.0442 -0.0590 75   LEU A C   
463   O O   . LEU A 77   ? 0.5199 0.4794 0.6656 0.0107  -0.0433 -0.0635 75   LEU A O   
464   C CB  . LEU A 77   ? 0.3964 0.3472 0.5428 0.0049  -0.0393 -0.0452 75   LEU A CB  
465   C CG  . LEU A 77   ? 0.4152 0.3682 0.5551 0.0032  -0.0365 -0.0410 75   LEU A CG  
466   C CD1 . LEU A 77   ? 0.4224 0.3728 0.5565 0.0020  -0.0329 -0.0326 75   LEU A CD1 
467   C CD2 . LEU A 77   ? 0.4201 0.3799 0.5513 0.0043  -0.0354 -0.0456 75   LEU A CD2 
468   N N   . ARG A 78   ? 0.4009 0.3491 0.5625 0.0091  -0.0463 -0.0576 76   ARG A N   
469   C CA  . ARG A 78   ? 0.4632 0.4112 0.6261 0.0114  -0.0476 -0.0615 76   ARG A CA  
470   C C   . ARG A 78   ? 0.4585 0.4100 0.6274 0.0136  -0.0514 -0.0716 76   ARG A C   
471   O O   . ARG A 78   ? 0.5162 0.4699 0.6841 0.0159  -0.0520 -0.0764 76   ARG A O   
472   C CB  . ARG A 78   ? 0.4620 0.4029 0.6327 0.0108  -0.0487 -0.0563 76   ARG A CB  
473   C CG  . ARG A 78   ? 0.4792 0.4179 0.6427 0.0092  -0.0448 -0.0471 76   ARG A CG  
474   C CD  . ARG A 78   ? 0.3976 0.3301 0.5682 0.0089  -0.0460 -0.0423 76   ARG A CD  
475   N NE  . ARG A 78   ? 0.4018 0.3339 0.5637 0.0085  -0.0423 -0.0357 76   ARG A NE  
476   C CZ  . ARG A 78   ? 0.3984 0.3261 0.5636 0.0080  -0.0423 -0.0299 76   ARG A CZ  
477   N NH1 . ARG A 78   ? 0.4122 0.3351 0.5897 0.0078  -0.0457 -0.0291 76   ARG A NH1 
478   N NH2 . ARG A 78   ? 0.4123 0.3406 0.5686 0.0078  -0.0388 -0.0247 76   ARG A NH2 
479   N N   . GLY A 79   ? 0.4971 0.4496 0.6720 0.0132  -0.0538 -0.0752 77   GLY A N   
480   C CA  . GLY A 79   ? 0.5433 0.4990 0.7248 0.0154  -0.0578 -0.0852 77   GLY A CA  
481   C C   . GLY A 79   ? 0.6474 0.6124 0.8200 0.0170  -0.0567 -0.0915 77   GLY A C   
482   O O   . GLY A 79   ? 0.6476 0.6170 0.8232 0.0195  -0.0593 -0.1002 77   GLY A O   
483   N N   . LYS A 80   ? 0.6519 0.6203 0.8138 0.0156  -0.0529 -0.0870 78   LYS A N   
484   C CA  . LYS A 80   ? 0.6668 0.6442 0.8194 0.0168  -0.0515 -0.0916 78   LYS A CA  
485   C C   . LYS A 80   ? 0.6206 0.6010 0.7618 0.0172  -0.0476 -0.0886 78   LYS A C   
486   O O   . LYS A 80   ? 0.6645 0.6527 0.7977 0.0181  -0.0462 -0.0916 78   LYS A O   
487   C CB  . LYS A 80   ? 0.6679 0.6480 0.8173 0.0150  -0.0505 -0.0896 78   LYS A CB  
488   C CG  . LYS A 80   ? 0.6376 0.6135 0.7815 0.0123  -0.0468 -0.0797 78   LYS A CG  
489   C CD  . LYS A 80   ? 0.5974 0.5755 0.7404 0.0108  -0.0466 -0.0784 78   LYS A CD  
490   C CE  . LYS A 80   ? 0.5367 0.5109 0.6752 0.0082  -0.0432 -0.0689 78   LYS A CE  
491   N NZ  . LYS A 80   ? 0.4643 0.4401 0.6036 0.0068  -0.0434 -0.0679 78   LYS A NZ  
492   N N   . HIS A 81   ? 0.5788 0.5535 0.7195 0.0166  -0.0460 -0.0827 79   HIS A N   
493   C CA  . HIS A 81   ? 0.6465 0.6235 0.7770 0.0169  -0.0425 -0.0796 79   HIS A CA  
494   C C   . HIS A 81   ? 0.7329 0.7161 0.8617 0.0197  -0.0434 -0.0870 79   HIS A C   
495   O O   . HIS A 81   ? 0.7622 0.7524 0.8819 0.0202  -0.0412 -0.0883 79   HIS A O   
496   C CB  . HIS A 81   ? 0.6014 0.5708 0.7331 0.0158  -0.0412 -0.0725 79   HIS A CB  
497   N N   . SER A 84   ? 0.7073 0.7126 0.7881 0.0207  -0.0279 -0.0778 82   SER A N   
498   C CA  . SER A 84   ? 0.6599 0.6694 0.7315 0.0192  -0.0249 -0.0737 82   SER A CA  
499   C C   . SER A 84   ? 0.5808 0.6007 0.6472 0.0206  -0.0243 -0.0782 82   SER A C   
500   O O   . SER A 84   ? 0.5090 0.5327 0.5778 0.0227  -0.0257 -0.0838 82   SER A O   
501   C CB  . SER A 84   ? 0.6003 0.6049 0.6667 0.0177  -0.0219 -0.0662 82   SER A CB  
502   N N   . GLY A 85   ? 0.5560 0.5809 0.6155 0.0194  -0.0224 -0.0757 83   GLY A N   
503   C CA  . GLY A 85   ? 0.4254 0.4606 0.4791 0.0203  -0.0214 -0.0784 83   GLY A CA  
504   C C   . GLY A 85   ? 0.4228 0.4587 0.4725 0.0206  -0.0195 -0.0765 83   GLY A C   
505   O O   . GLY A 85   ? 0.4149 0.4576 0.4643 0.0224  -0.0199 -0.0813 83   GLY A O   
506   N N   . VAL A 86   ? 0.4602 0.4895 0.5071 0.0188  -0.0174 -0.0696 84   VAL A N   
507   C CA  . VAL A 86   ? 0.3954 0.4246 0.4390 0.0190  -0.0157 -0.0675 84   VAL A CA  
508   C C   . VAL A 86   ? 0.4064 0.4330 0.4562 0.0210  -0.0177 -0.0717 84   VAL A C   
509   O O   . VAL A 86   ? 0.3699 0.4008 0.4184 0.0222  -0.0173 -0.0739 84   VAL A O   
510   C CB  . VAL A 86   ? 0.4880 0.5102 0.5279 0.0168  -0.0134 -0.0596 84   VAL A CB  
511   C CG1 . VAL A 86   ? 0.4676 0.4935 0.5008 0.0151  -0.0113 -0.0556 84   VAL A CG1 
512   C CG2 . VAL A 86   ? 0.4813 0.4942 0.5264 0.0161  -0.0144 -0.0571 84   VAL A CG2 
513   N N   . GLU A 87   ? 0.4453 0.4652 0.5024 0.0213  -0.0199 -0.0729 85   GLU A N   
514   C CA  . GLU A 87   ? 0.4440 0.4608 0.5080 0.0232  -0.0220 -0.0765 85   GLU A CA  
515   C C   . GLU A 87   ? 0.4657 0.4907 0.5324 0.0257  -0.0240 -0.0850 85   GLU A C   
516   O O   . GLU A 87   ? 0.4442 0.4706 0.5127 0.0275  -0.0246 -0.0881 85   GLU A O   
517   C CB  . GLU A 87   ? 0.5543 0.5621 0.6261 0.0227  -0.0242 -0.0755 85   GLU A CB  
518   N N   . GLY A 88   ? 0.4298 0.4606 0.4966 0.0261  -0.0250 -0.0891 86   GLY A N   
519   C CA  . GLY A 88   ? 0.3837 0.4237 0.4523 0.0287  -0.0268 -0.0974 86   GLY A CA  
520   C C   . GLY A 88   ? 0.3943 0.4435 0.4555 0.0292  -0.0244 -0.0975 86   GLY A C   
521   O O   . GLY A 88   ? 0.3879 0.4436 0.4507 0.0316  -0.0254 -0.1036 86   GLY A O   
522   N N   . LEU A 89   ? 0.3923 0.4424 0.4457 0.0269  -0.0214 -0.0909 87   LEU A N   
523   C CA  . LEU A 89   ? 0.3552 0.4134 0.4018 0.0270  -0.0190 -0.0899 87   LEU A CA  
524   C C   . LEU A 89   ? 0.3233 0.3783 0.3708 0.0277  -0.0185 -0.0890 87   LEU A C   
525   O O   . LEU A 89   ? 0.3273 0.3897 0.3742 0.0294  -0.0185 -0.0930 87   LEU A O   
526   C CB  . LEU A 89   ? 0.3668 0.4254 0.4060 0.0242  -0.0163 -0.0827 87   LEU A CB  
527   C CG  . LEU A 89   ? 0.4500 0.5164 0.4819 0.0236  -0.0137 -0.0800 87   LEU A CG  
528   C CD1 . LEU A 89   ? 0.5013 0.5805 0.5324 0.0255  -0.0143 -0.0862 87   LEU A CD1 
529   C CD2 . LEU A 89   ? 0.4351 0.5001 0.4613 0.0208  -0.0115 -0.0728 87   LEU A CD2 
530   N N   . VAL A 90   ? 0.3353 0.3797 0.3841 0.0264  -0.0181 -0.0838 88   VAL A N   
531   C CA  . VAL A 90   ? 0.3210 0.3615 0.3716 0.0271  -0.0179 -0.0829 88   VAL A CA  
532   C C   . VAL A 90   ? 0.3759 0.4186 0.4335 0.0301  -0.0207 -0.0906 88   VAL A C   
533   O O   . VAL A 90   ? 0.3267 0.3729 0.3841 0.0315  -0.0204 -0.0926 88   VAL A O   
534   C CB  . VAL A 90   ? 0.3023 0.3312 0.3546 0.0255  -0.0176 -0.0767 88   VAL A CB  
535   C CG1 . VAL A 90   ? 0.3350 0.3593 0.3909 0.0266  -0.0183 -0.0768 88   VAL A CG1 
536   C CG2 . VAL A 90   ? 0.3444 0.3717 0.3893 0.0228  -0.0146 -0.0693 88   VAL A CG2 
537   N N   . GLN A 91   ? 0.3786 0.4191 0.4429 0.0311  -0.0235 -0.0950 89   GLN A N   
538   C CA  . GLN A 91   ? 0.4040 0.4459 0.4761 0.0341  -0.0266 -0.1027 89   GLN A CA  
539   C C   . GLN A 91   ? 0.3798 0.4344 0.4498 0.0363  -0.0267 -0.1096 89   GLN A C   
540   O O   . GLN A 91   ? 0.4040 0.4620 0.4768 0.0386  -0.0276 -0.1141 89   GLN A O   
541   C CB  . GLN A 91   ? 0.4660 0.5024 0.5463 0.0345  -0.0298 -0.1056 89   GLN A CB  
542   N N   . GLU A 92   ? 0.3600 0.4223 0.4252 0.0357  -0.0258 -0.1104 90   GLU A N   
543   C CA  . GLU A 92   ? 0.3711 0.4465 0.4345 0.0378  -0.0260 -0.1171 90   GLU A CA  
544   C C   . GLU A 92   ? 0.3572 0.4388 0.4155 0.0381  -0.0237 -0.1157 90   GLU A C   
545   O O   . GLU A 92   ? 0.3520 0.4419 0.4119 0.0408  -0.0245 -0.1221 90   GLU A O   
546   C CB  . GLU A 92   ? 0.3740 0.4566 0.4325 0.0367  -0.0252 -0.1168 90   GLU A CB  
547   C CG  . GLU A 92   ? 0.3720 0.4696 0.4276 0.0388  -0.0251 -0.1229 90   GLU A CG  
548   C CD  . GLU A 92   ? 0.4904 0.5952 0.5415 0.0378  -0.0246 -0.1227 90   GLU A CD  
549   O OE1 . GLU A 92   ? 0.5079 0.6059 0.5583 0.0356  -0.0244 -0.1178 90   GLU A OE1 
550   O OE2 . GLU A 92   ? 0.4436 0.5615 0.4919 0.0394  -0.0245 -0.1273 90   GLU A OE2 
551   N N   . TYR A 93   ? 0.3265 0.4043 0.3789 0.0355  -0.0208 -0.1075 91   TYR A N   
552   C CA  . TYR A 93   ? 0.3126 0.3963 0.3598 0.0354  -0.0184 -0.1054 91   TYR A CA  
553   C C   . TYR A 93   ? 0.2889 0.3645 0.3383 0.0354  -0.0182 -0.1025 91   TYR A C   
554   O O   . TYR A 93   ? 0.3011 0.3798 0.3462 0.0348  -0.0160 -0.0995 91   TYR A O   
555   C CB  . TYR A 93   ? 0.2869 0.3742 0.3256 0.0326  -0.0153 -0.0987 91   TYR A CB  
556   C CG  . TYR A 93   ? 0.3030 0.4013 0.3390 0.0329  -0.0154 -0.1019 91   TYR A CG  
557   C CD1 . TYR A 93   ? 0.2937 0.4054 0.3272 0.0345  -0.0147 -0.1058 91   TYR A CD1 
558   C CD2 . TYR A 93   ? 0.3397 0.4356 0.3757 0.0319  -0.0161 -0.1009 91   TYR A CD2 
559   C CE1 . TYR A 93   ? 0.3263 0.4488 0.3571 0.0349  -0.0148 -0.1087 91   TYR A CE1 
560   C CE2 . TYR A 93   ? 0.3634 0.4698 0.3970 0.0323  -0.0163 -0.1039 91   TYR A CE2 
561   C CZ  . TYR A 93   ? 0.3455 0.4652 0.3763 0.0338  -0.0156 -0.1076 91   TYR A CZ  
562   O OH  . TYR A 93   ? 0.3778 0.5087 0.4059 0.0343  -0.0158 -0.1104 91   TYR A OH  
563   N N   . SER A 94   ? 0.3005 0.3660 0.3566 0.0359  -0.0204 -0.1032 92   SER A N   
564   C CA  . SER A 94   ? 0.2993 0.3570 0.3582 0.0362  -0.0206 -0.1007 92   SER A CA  
565   C C   . SER A 94   ? 0.2432 0.2976 0.2954 0.0334  -0.0175 -0.0923 92   SER A C   
566   O O   . SER A 94   ? 0.2826 0.3376 0.3333 0.0337  -0.0164 -0.0908 92   SER A O   
567   C CB  . SER A 94   ? 0.3595 0.4232 0.4218 0.0391  -0.0217 -0.1070 92   SER A CB  
568   O OG  . SER A 94   ? 0.3689 0.4371 0.4373 0.0418  -0.0246 -0.1155 92   SER A OG  
569   N N   . LEU A 95   ? 0.2326 0.2838 0.2808 0.0309  -0.0161 -0.0870 93   LEU A N   
570   C CA  . LEU A 95   ? 0.2569 0.3050 0.2989 0.0284  -0.0133 -0.0793 93   LEU A CA  
571   C C   . LEU A 95   ? 0.2680 0.3050 0.3126 0.0278  -0.0137 -0.0751 93   LEU A C   
572   O O   . LEU A 95   ? 0.2638 0.2937 0.3138 0.0281  -0.0155 -0.0755 93   LEU A O   
573   C CB  . LEU A 95   ? 0.2415 0.2896 0.2789 0.0260  -0.0120 -0.0753 93   LEU A CB  
574   C CG  . LEU A 95   ? 0.2345 0.2938 0.2686 0.0263  -0.0115 -0.0784 93   LEU A CG  
575   C CD1 . LEU A 95   ? 0.2613 0.3199 0.2907 0.0238  -0.0101 -0.0733 93   LEU A CD1 
576   C CD2 . LEU A 95   ? 0.2518 0.3205 0.2822 0.0269  -0.0100 -0.0793 93   LEU A CD2 
577   N N   . SER A 96   ? 0.2321 0.2679 0.2731 0.0269  -0.0118 -0.0709 94   SER A N   
578   C CA  . SER A 96   ? 0.2339 0.2600 0.2754 0.0257  -0.0115 -0.0654 94   SER A CA  
579   C C   . SER A 96   ? 0.2426 0.2643 0.2805 0.0232  -0.0102 -0.0600 94   SER A C   
580   O O   . SER A 96   ? 0.2338 0.2603 0.2683 0.0223  -0.0093 -0.0599 94   SER A O   
581   C CB  . SER A 96   ? 0.2662 0.2929 0.3041 0.0253  -0.0099 -0.0625 94   SER A CB  
582   O OG  . SER A 96   ? 0.2388 0.2700 0.2699 0.0234  -0.0074 -0.0590 94   SER A OG  
583   N N   . SER A 97   ? 0.2291 0.2421 0.2680 0.0223  -0.0101 -0.0553 95   SER A N   
584   C CA  . SER A 97   ? 0.2662 0.2751 0.3018 0.0200  -0.0088 -0.0501 95   SER A CA  
585   C C   . SER A 97   ? 0.2381 0.2511 0.2664 0.0184  -0.0063 -0.0467 95   SER A C   
586   O O   . SER A 97   ? 0.2333 0.2482 0.2586 0.0171  -0.0054 -0.0452 95   SER A O   
587   C CB  . SER A 97   ? 0.3203 0.3201 0.3578 0.0194  -0.0089 -0.0455 95   SER A CB  
588   O OG  . SER A 97   ? 0.4284 0.4240 0.4730 0.0204  -0.0113 -0.0476 95   SER A OG  
589   N N   . GLN A 98   ? 0.2156 0.2302 0.2414 0.0184  -0.0052 -0.0455 96   GLN A N   
590   C CA  . GLN A 98   ? 0.2047 0.2230 0.2243 0.0168  -0.0030 -0.0422 96   GLN A CA  
591   C C   . GLN A 98   ? 0.1999 0.2275 0.2175 0.0168  -0.0027 -0.0450 96   GLN A C   
592   O O   . GLN A 98   ? 0.2050 0.2351 0.2183 0.0151  -0.0013 -0.0420 96   GLN A O   
593   C CB  . GLN A 98   ? 0.2242 0.2428 0.2423 0.0169  -0.0022 -0.0408 96   GLN A CB  
594   C CG  . GLN A 98   ? 0.2492 0.2594 0.2673 0.0163  -0.0020 -0.0364 96   GLN A CG  
595   C CD  . GLN A 98   ? 0.2338 0.2405 0.2480 0.0142  -0.0005 -0.0313 96   GLN A CD  
596   O OE1 . GLN A 98   ? 0.2552 0.2586 0.2703 0.0137  -0.0008 -0.0304 96   GLN A OE1 
597   N NE2 . GLN A 98   ? 0.2709 0.2783 0.2810 0.0130  0.0010  -0.0282 96   GLN A NE2 
598   N N   . GLU A 99   ? 0.2158 0.2491 0.2365 0.0188  -0.0040 -0.0509 97   GLU A N   
599   C CA  . GLU A 99   ? 0.1887 0.2316 0.2075 0.0190  -0.0038 -0.0538 97   GLU A CA  
600   C C   . GLU A 99   ? 0.1971 0.2393 0.2158 0.0182  -0.0042 -0.0535 97   GLU A C   
601   O O   . GLU A 99   ? 0.2175 0.2653 0.2322 0.0170  -0.0031 -0.0521 97   GLU A O   
602   C CB  . GLU A 99   ? 0.1963 0.2457 0.2188 0.0216  -0.0053 -0.0607 97   GLU A CB  
603   C CG  . GLU A 99   ? 0.2039 0.2564 0.2257 0.0223  -0.0046 -0.0610 97   GLU A CG  
604   C CD  . GLU A 99   ? 0.2336 0.2910 0.2602 0.0252  -0.0064 -0.0681 97   GLU A CD  
605   O OE1 . GLU A 99   ? 0.2310 0.2878 0.2621 0.0268  -0.0084 -0.0728 97   GLU A OE1 
606   O OE2 . GLU A 99   ? 0.2451 0.3067 0.2712 0.0260  -0.0058 -0.0690 97   GLU A OE2 
607   N N   . GLY A 100  ? 0.2135 0.2490 0.2367 0.0188  -0.0058 -0.0547 98   GLY A N   
608   C CA  . GLY A 100  ? 0.2051 0.2394 0.2285 0.0179  -0.0063 -0.0541 98   GLY A CA  
609   C C   . GLY A 100  ? 0.2402 0.2719 0.2586 0.0155  -0.0043 -0.0477 98   GLY A C   
610   O O   . GLY A 100  ? 0.2302 0.2660 0.2459 0.0145  -0.0038 -0.0469 98   GLY A O   
611   N N   . VAL A 101  ? 0.2145 0.2394 0.2318 0.0145  -0.0033 -0.0431 99   VAL A N   
612   C CA  . VAL A 101  ? 0.2322 0.2545 0.2450 0.0123  -0.0015 -0.0373 99   VAL A CA  
613   C C   . VAL A 101  ? 0.2263 0.2564 0.2343 0.0114  -0.0001 -0.0360 99   VAL A C   
614   O O   . VAL A 101  ? 0.2268 0.2587 0.2320 0.0100  0.0007  -0.0334 99   VAL A O   
615   C CB  . VAL A 101  ? 0.2045 0.2193 0.2171 0.0118  -0.0008 -0.0333 99   VAL A CB  
616   C CG1 . VAL A 101  ? 0.2478 0.2608 0.2557 0.0098  0.0010  -0.0279 99   VAL A CG1 
617   C CG2 . VAL A 101  ? 0.2394 0.2468 0.2567 0.0124  -0.0022 -0.0336 99   VAL A CG2 
618   N N   . ALA A 102  ? 0.2023 0.2371 0.2096 0.0121  0.0003  -0.0376 100  ALA A N   
619   C CA  . ALA A 102  ? 0.1915 0.2339 0.1947 0.0110  0.0017  -0.0359 100  ALA A CA  
620   C C   . ALA A 102  ? 0.2071 0.2578 0.2094 0.0111  0.0014  -0.0381 100  ALA A C   
621   O O   . ALA A 102  ? 0.2321 0.2869 0.2308 0.0095  0.0025  -0.0347 100  ALA A O   
622   C CB  . ALA A 102  ? 0.1994 0.2461 0.2028 0.0119  0.0019  -0.0378 100  ALA A CB  
623   N N   . LEU A 103  ? 0.2063 0.2600 0.2120 0.0130  -0.0002 -0.0438 101  LEU A N   
624   C CA  . LEU A 103  ? 0.2094 0.2711 0.2145 0.0134  -0.0007 -0.0466 101  LEU A CA  
625   C C   . LEU A 103  ? 0.2288 0.2873 0.2323 0.0118  -0.0005 -0.0430 101  LEU A C   
626   O O   . LEU A 103  ? 0.2327 0.2978 0.2331 0.0109  0.0001  -0.0415 101  LEU A O   
627   C CB  . LEU A 103  ? 0.2182 0.2818 0.2281 0.0159  -0.0029 -0.0536 101  LEU A CB  
628   C CG  . LEU A 103  ? 0.2114 0.2834 0.2210 0.0166  -0.0037 -0.0574 101  LEU A CG  
629   C CD1 . LEU A 103  ? 0.2284 0.3125 0.2338 0.0165  -0.0025 -0.0574 101  LEU A CD1 
630   C CD2 . LEU A 103  ? 0.2499 0.3223 0.2652 0.0192  -0.0062 -0.0647 101  LEU A CD2 
631   N N   . MET A 104  ? 0.2128 0.2617 0.2187 0.0115  -0.0011 -0.0416 102  MET A N   
632   C CA  . MET A 104  ? 0.2472 0.2932 0.2519 0.0101  -0.0009 -0.0384 102  MET A CA  
633   C C   . MET A 104  ? 0.2270 0.2727 0.2272 0.0080  0.0010  -0.0322 102  MET A C   
634   O O   . MET A 104  ? 0.2527 0.3009 0.2507 0.0069  0.0013  -0.0299 102  MET A O   
635   C CB  . MET A 104  ? 0.2475 0.2838 0.2560 0.0102  -0.0018 -0.0380 102  MET A CB  
636   C CG  . MET A 104  ? 0.2461 0.2823 0.2600 0.0122  -0.0040 -0.0440 102  MET A CG  
637   S SD  . MET A 104  ? 0.3511 0.3974 0.3655 0.0133  -0.0054 -0.0494 102  MET A SD  
638   C CE  . MET A 104  ? 0.3968 0.4396 0.4104 0.0115  -0.0053 -0.0457 102  MET A CE  
639   N N   . CYS A 105  ? 0.2123 0.2549 0.2112 0.0075  0.0020  -0.0295 103  CYS A N   
640   C CA  . CYS A 105  ? 0.2230 0.2657 0.2182 0.0055  0.0035  -0.0240 103  CYS A CA  
641   C C   . CYS A 105  ? 0.2852 0.3384 0.2778 0.0049  0.0041  -0.0237 103  CYS A C   
642   O O   . CYS A 105  ? 0.2776 0.3324 0.2678 0.0033  0.0047  -0.0197 103  CYS A O   
643   C CB  . CYS A 105  ? 0.2721 0.3105 0.2669 0.0052  0.0043  -0.0220 103  CYS A CB  
644   S SG  . CYS A 105  ? 0.2503 0.2770 0.2473 0.0054  0.0040  -0.0207 103  CYS A SG  
645   N N   . LEU A 106  ? 0.2362 0.2969 0.2294 0.0063  0.0037  -0.0278 104  LEU A N   
646   C CA  . LEU A 106  ? 0.2607 0.3325 0.2513 0.0059  0.0043  -0.0277 104  LEU A CA  
647   C C   . LEU A 106  ? 0.2904 0.3664 0.2806 0.0058  0.0036  -0.0284 104  LEU A C   
648   O O   . LEU A 106  ? 0.2979 0.3796 0.2853 0.0044  0.0042  -0.0250 104  LEU A O   
649   C CB  . LEU A 106  ? 0.2368 0.3162 0.2285 0.0077  0.0039  -0.0328 104  LEU A CB  
650   C CG  . LEU A 106  ? 0.2666 0.3593 0.2561 0.0078  0.0043  -0.0338 104  LEU A CG  
651   C CD1 . LEU A 106  ? 0.3193 0.4156 0.3056 0.0054  0.0059  -0.0276 104  LEU A CD1 
652   C CD2 . LEU A 106  ? 0.2827 0.3831 0.2739 0.0101  0.0037  -0.0401 104  LEU A CD2 
653   N N   . ALA A 107  ? 0.2438 0.3172 0.2368 0.0073  0.0021  -0.0329 105  ALA A N   
654   C CA  . ALA A 107  ? 0.2683 0.3455 0.2612 0.0074  0.0013  -0.0339 105  ALA A CA  
655   C C   . ALA A 107  ? 0.3168 0.3892 0.3077 0.0053  0.0020  -0.0279 105  ALA A C   
656   O O   . ALA A 107  ? 0.3244 0.4030 0.3131 0.0044  0.0021  -0.0259 105  ALA A O   
657   C CB  . ALA A 107  ? 0.2832 0.3569 0.2803 0.0092  -0.0006 -0.0395 105  ALA A CB  
658   N N   . GLU A 108  ? 0.2748 0.3366 0.2667 0.0045  0.0024  -0.0250 106  GLU A N   
659   C CA  . GLU A 108  ? 0.2999 0.3569 0.2903 0.0027  0.0030  -0.0194 106  GLU A CA  
660   C C   . GLU A 108  ? 0.3511 0.4137 0.3381 0.0011  0.0042  -0.0148 106  GLU A C   
661   O O   . GLU A 108  ? 0.3586 0.4236 0.3443 -0.0001 0.0042  -0.0116 106  GLU A O   
662   C CB  . GLU A 108  ? 0.2847 0.3307 0.2764 0.0024  0.0034  -0.0173 106  GLU A CB  
663   C CG  . GLU A 108  ? 0.3262 0.3670 0.3165 0.0007  0.0042  -0.0118 106  GLU A CG  
664   C CD  . GLU A 108  ? 0.3874 0.4194 0.3780 0.0003  0.0049  -0.0093 106  GLU A CD  
665   O OE1 . GLU A 108  ? 0.3293 0.3576 0.3218 0.0014  0.0046  -0.0119 106  GLU A OE1 
666   O OE2 . GLU A 108  ? 0.3713 0.4006 0.3604 -0.0010 0.0056  -0.0049 106  GLU A OE2 
667   N N   . ALA A 109  ? 0.3436 0.4088 0.3298 0.0009  0.0050  -0.0142 107  ALA A N   
668   C CA  . ALA A 109  ? 0.3398 0.4105 0.3235 -0.0008 0.0060  -0.0095 107  ALA A CA  
669   C C   . ALA A 109  ? 0.3796 0.4619 0.3617 -0.0008 0.0057  -0.0100 107  ALA A C   
670   O O   . ALA A 109  ? 0.4249 0.5104 0.4054 -0.0024 0.0061  -0.0054 107  ALA A O   
671   C CB  . ALA A 109  ? 0.3845 0.4562 0.3681 -0.0009 0.0068  -0.0094 107  ALA A CB  
672   N N   . LEU A 110  ? 0.3339 0.4230 0.3166 0.0010  0.0051  -0.0157 108  LEU A N   
673   C CA  . LEU A 110  ? 0.3101 0.4112 0.2911 0.0013  0.0048  -0.0168 108  LEU A CA  
674   C C   . LEU A 110  ? 0.3681 0.4686 0.3488 0.0008  0.0041  -0.0154 108  LEU A C   
675   O O   . LEU A 110  ? 0.4189 0.5282 0.3975 0.0001  0.0041  -0.0132 108  LEU A O   
676   C CB  . LEU A 110  ? 0.3158 0.4236 0.2981 0.0038  0.0040  -0.0241 108  LEU A CB  
677   C CG  . LEU A 110  ? 0.3816 0.4937 0.3637 0.0043  0.0048  -0.0254 108  LEU A CG  
678   C CD1 . LEU A 110  ? 0.3425 0.4582 0.3270 0.0070  0.0038  -0.0332 108  LEU A CD1 
679   C CD2 . LEU A 110  ? 0.3641 0.4877 0.3432 0.0029  0.0060  -0.0216 108  LEU A CD2 
680   N N   . LEU A 111  ? 0.3605 0.4513 0.3433 0.0012  0.0033  -0.0165 109  LEU A N   
681   C CA  . LEU A 111  ? 0.3807 0.4704 0.3635 0.0007  0.0026  -0.0150 109  LEU A CA  
682   C C   . LEU A 111  ? 0.4305 0.5162 0.4119 -0.0015 0.0034  -0.0078 109  LEU A C   
683   O O   . LEU A 111  ? 0.4538 0.5397 0.4349 -0.0021 0.0029  -0.0058 109  LEU A O   
684   C CB  . LEU A 111  ? 0.3320 0.4131 0.3179 0.0018  0.0015  -0.0187 109  LEU A CB  
685   C CG  . LEU A 111  ? 0.3795 0.4649 0.3677 0.0041  0.0002  -0.0261 109  LEU A CG  
686   C CD1 . LEU A 111  ? 0.3393 0.4152 0.3315 0.0050  -0.0009 -0.0291 109  LEU A CD1 
687   C CD2 . LEU A 111  ? 0.3464 0.4427 0.3335 0.0047  -0.0007 -0.0285 109  LEU A CD2 
688   N N   . ARG A 112  ? 0.4211 0.5033 0.4019 -0.0027 0.0045  -0.0041 110  ARG A N   
689   C CA  . ARG A 112  ? 0.3673 0.4475 0.3471 -0.0048 0.0050  0.0026  110  ARG A CA  
690   C C   . ARG A 112  ? 0.5281 0.6197 0.5058 -0.0058 0.0052  0.0057  110  ARG A C   
691   O O   . ARG A 112  ? 0.5727 0.6642 0.5500 -0.0075 0.0053  0.0112  110  ARG A O   
692   C CB  . ARG A 112  ? 0.4618 0.5348 0.4422 -0.0056 0.0059  0.0052  110  ARG A CB  
693   C CG  . ARG A 112  ? 0.4339 0.4957 0.4161 -0.0048 0.0058  0.0031  110  ARG A CG  
694   C CD  . ARG A 112  ? 0.4530 0.5090 0.4355 -0.0052 0.0066  0.0046  110  ARG A CD  
695   N NE  . ARG A 112  ? 0.5946 0.6479 0.5768 -0.0071 0.0070  0.0103  110  ARG A NE  
696   C CZ  . ARG A 112  ? 0.6310 0.6756 0.6140 -0.0075 0.0070  0.0126  110  ARG A CZ  
697   N NH1 . ARG A 112  ? 0.6023 0.6402 0.5864 -0.0064 0.0067  0.0102  110  ARG A NH1 
698   N NH2 . ARG A 112  ? 0.6600 0.7029 0.6432 -0.0091 0.0071  0.0174  110  ARG A NH2 
699   N N   . ILE A 113  ? 0.4702 0.5720 0.4469 -0.0048 0.0052  0.0022  111  ILE A N   
700   C CA  . ILE A 113  ? 0.5123 0.6267 0.4869 -0.0054 0.0053  0.0045  111  ILE A CA  
701   C C   . ILE A 113  ? 0.5349 0.6528 0.5091 -0.0048 0.0042  0.0032  111  ILE A C   
702   O O   . ILE A 113  ? 0.5499 0.6695 0.5247 -0.0029 0.0034  -0.0031 111  ILE A O   
703   C CB  . ILE A 113  ? 0.4776 0.6024 0.4512 -0.0043 0.0058  0.0008  111  ILE A CB  
704   C CG1 . ILE A 113  ? 0.3926 0.5147 0.3667 -0.0052 0.0069  0.0028  111  ILE A CG1 
705   C CG2 . ILE A 113  ? 0.5426 0.6816 0.5139 -0.0048 0.0058  0.0028  111  ILE A CG2 
706   C CD1 . ILE A 113  ? 0.4088 0.5413 0.3822 -0.0041 0.0074  -0.0008 111  ILE A CD1 
707   N N   . PRO A 114  ? 0.6334 0.7524 0.6069 -0.0064 0.0040  0.0087  112  PRO A N   
708   C CA  . PRO A 114  ? 0.6337 0.7541 0.6071 -0.0057 0.0028  0.0074  112  PRO A CA  
709   C C   . PRO A 114  ? 0.6179 0.7518 0.5895 -0.0045 0.0022  0.0039  112  PRO A C   
710   O O   . PRO A 114  ? 0.6525 0.7872 0.6249 -0.0029 0.0010  -0.0012 112  PRO A O   
711   C CB  . PRO A 114  ? 0.5497 0.6677 0.5230 -0.0078 0.0028  0.0150  112  PRO A CB  
712   C CG  . PRO A 114  ? 0.6725 0.7848 0.6465 -0.0094 0.0038  0.0194  112  PRO A CG  
713   C CD  . PRO A 114  ? 0.6609 0.7788 0.6341 -0.0087 0.0047  0.0163  112  PRO A CD  
714   N N   . ASP A 115  ? 0.6354 0.7807 0.6049 -0.0051 0.0029  0.0063  113  ASP A N   
715   C CA  . ASP A 115  ? 0.6427 0.8024 0.6103 -0.0039 0.0024  0.0033  113  ASP A CA  
716   C C   . ASP A 115  ? 0.5840 0.7473 0.5520 -0.0015 0.0022  -0.0049 113  ASP A C   
717   O O   . ASP A 115  ? 0.5783 0.7406 0.5467 -0.0014 0.0032  -0.0058 113  ASP A O   
718   C CB  . ASP A 115  ? 0.5914 0.7626 0.5567 -0.0056 0.0032  0.0095  113  ASP A CB  
719   C CG  . ASP A 115  ? 0.6643 0.8518 0.6272 -0.0041 0.0029  0.0060  113  ASP A CG  
720   O OD1 . ASP A 115  ? 0.6958 0.8871 0.6581 -0.0029 0.0017  0.0029  113  ASP A OD1 
721   O OD2 . ASP A 115  ? 0.6719 0.8687 0.6334 -0.0042 0.0040  0.0063  113  ASP A OD2 
722   N N   . THR A 116  ? 0.5712 0.7390 0.5394 0.0005  0.0009  -0.0111 114  THR A N   
723   C CA  . THR A 116  ? 0.5535 0.7237 0.5231 0.0031  0.0003  -0.0196 114  THR A CA  
724   C C   . THR A 116  ? 0.6290 0.8124 0.5965 0.0037  0.0012  -0.0209 114  THR A C   
725   O O   . THR A 116  ? 0.5769 0.7590 0.5457 0.0048  0.0016  -0.0248 114  THR A O   
726   C CB  . THR A 116  ? 0.5715 0.7444 0.5422 0.0050  -0.0017 -0.0259 114  THR A CB  
727   O OG1 . THR A 116  ? 0.6187 0.7796 0.5915 0.0043  -0.0024 -0.0243 114  THR A OG1 
728   C CG2 . THR A 116  ? 0.6146 0.7887 0.5877 0.0077  -0.0026 -0.0350 114  THR A CG2 
729   N N   . ALA A 117  ? 0.5320 0.7287 0.4965 0.0031  0.0015  -0.0176 115  ALA A N   
730   C CA  . ALA A 117  ? 0.5139 0.7248 0.4764 0.0038  0.0024  -0.0189 115  ALA A CA  
731   C C   . ALA A 117  ? 0.4640 0.6717 0.4266 0.0021  0.0042  -0.0142 115  ALA A C   
732   O O   . ALA A 117  ? 0.5121 0.7263 0.4747 0.0033  0.0049  -0.0176 115  ALA A O   
733   C CB  . ALA A 117  ? 0.5651 0.7911 0.5242 0.0032  0.0024  -0.0152 115  ALA A CB  
734   N N   . THR A 118  ? 0.4587 0.6567 0.4219 -0.0005 0.0048  -0.0067 116  THR A N   
735   C CA  . THR A 118  ? 0.5373 0.7310 0.5011 -0.0021 0.0062  -0.0025 116  THR A CA  
736   C C   . THR A 118  ? 0.4689 0.6531 0.4352 -0.0006 0.0062  -0.0083 116  THR A C   
737   O O   . THR A 118  ? 0.5011 0.6888 0.4675 -0.0002 0.0071  -0.0098 116  THR A O   
738   C CB  . THR A 118  ? 0.4369 0.6212 0.4014 -0.0050 0.0065  0.0059  116  THR A CB  
739   O OG1 . THR A 118  ? 0.6328 0.8255 0.5954 -0.0063 0.0063  0.0114  116  THR A OG1 
740   C CG2 . THR A 118  ? 0.4501 0.6316 0.4154 -0.0067 0.0079  0.0105  116  THR A CG2 
741   N N   . ARG A 119  ? 0.4911 0.6633 0.4594 0.0003  0.0051  -0.0115 117  ARG A N   
742   C CA  . ARG A 119  ? 0.5238 0.6864 0.4947 0.0018  0.0049  -0.0168 117  ARG A CA  
743   C C   . ARG A 119  ? 0.4443 0.6161 0.4156 0.0044  0.0046  -0.0243 117  ARG A C   
744   O O   . ARG A 119  ? 0.4840 0.6541 0.4565 0.0050  0.0052  -0.0263 117  ARG A O   
745   C CB  . ARG A 119  ? 0.4673 0.6184 0.4405 0.0024  0.0036  -0.0192 117  ARG A CB  
746   C CG  . ARG A 119  ? 0.4067 0.5465 0.3829 0.0036  0.0033  -0.0234 117  ARG A CG  
747   C CD  . ARG A 119  ? 0.4529 0.5845 0.4316 0.0046  0.0017  -0.0268 117  ARG A CD  
748   N NE  . ARG A 119  ? 0.4785 0.6051 0.4564 0.0028  0.0017  -0.0214 117  ARG A NE  
749   C CZ  . ARG A 119  ? 0.4884 0.6169 0.4665 0.0032  0.0005  -0.0225 117  ARG A CZ  
750   N NH1 . ARG A 119  ? 0.4568 0.5916 0.4359 0.0052  -0.0008 -0.0292 117  ARG A NH1 
751   N NH2 . ARG A 119  ? 0.5955 0.7194 0.5729 0.0015  0.0006  -0.0171 117  ARG A NH2 
752   N N   . ASP A 120  ? 0.5186 0.7005 0.4890 0.0060  0.0036  -0.0288 118  ASP A N   
753   C CA  . ASP A 120  ? 0.4946 0.6856 0.4658 0.0089  0.0030  -0.0369 118  ASP A CA  
754   C C   . ASP A 120  ? 0.4866 0.6894 0.4558 0.0086  0.0046  -0.0353 118  ASP A C   
755   O O   . ASP A 120  ? 0.4824 0.6884 0.4530 0.0106  0.0046  -0.0408 118  ASP A O   
756   C CB  . ASP A 120  ? 0.4356 0.6356 0.4063 0.0107  0.0014  -0.0419 118  ASP A CB  
757   C CG  . ASP A 120  ? 0.5447 0.7336 0.5178 0.0110  -0.0002 -0.0438 118  ASP A CG  
758   O OD1 . ASP A 120  ? 0.5833 0.7578 0.5588 0.0101  -0.0002 -0.0422 118  ASP A OD1 
759   O OD2 . ASP A 120  ? 0.5489 0.7436 0.5216 0.0120  -0.0016 -0.0468 118  ASP A OD2 
760   N N   . ALA A 121  ? 0.4677 0.6771 0.4340 0.0062  0.0058  -0.0276 119  ALA A N   
761   C CA  . ALA A 121  ? 0.5306 0.7510 0.4955 0.0056  0.0074  -0.0251 119  ALA A CA  
762   C C   . ALA A 121  ? 0.5060 0.7166 0.4728 0.0046  0.0084  -0.0232 119  ALA A C   
763   O O   . ALA A 121  ? 0.4869 0.7033 0.4541 0.0057  0.0091  -0.0260 119  ALA A O   
764   C CB  . ALA A 121  ? 0.5631 0.7923 0.5250 0.0030  0.0084  -0.0166 119  ALA A CB  
765   N N   . LEU A 122  ? 0.5016 0.6977 0.4696 0.0027  0.0084  -0.0185 120  LEU A N   
766   C CA  . LEU A 122  ? 0.4935 0.6798 0.4633 0.0019  0.0092  -0.0170 120  LEU A CA  
767   C C   . LEU A 122  ? 0.4968 0.6792 0.4691 0.0047  0.0084  -0.0252 120  LEU A C   
768   O O   . LEU A 122  ? 0.4981 0.6812 0.4712 0.0051  0.0092  -0.0263 120  LEU A O   
769   C CB  . LEU A 122  ? 0.5231 0.6946 0.4938 -0.0001 0.0090  -0.0117 120  LEU A CB  
770   C CG  . LEU A 122  ? 0.5048 0.6678 0.4769 -0.0015 0.0099  -0.0084 120  LEU A CG  
771   C CD1 . LEU A 122  ? 0.6003 0.7726 0.5713 -0.0036 0.0112  -0.0026 120  LEU A CD1 
772   C CD2 . LEU A 122  ? 0.5038 0.6520 0.4770 -0.0030 0.0095  -0.0046 120  LEU A CD2 
773   N N   . ILE A 123  ? 0.4688 0.6471 0.4424 0.0068  0.0069  -0.0311 121  ILE A N   
774   C CA  . ILE A 123  ? 0.4610 0.6357 0.4377 0.0095  0.0059  -0.0390 121  ILE A CA  
775   C C   . ILE A 123  ? 0.4965 0.6853 0.4728 0.0115  0.0062  -0.0440 121  ILE A C   
776   O O   . ILE A 123  ? 0.4596 0.6475 0.4377 0.0125  0.0065  -0.0465 121  ILE A O   
777   C CB  . ILE A 123  ? 0.4078 0.5769 0.3866 0.0111  0.0039  -0.0440 121  ILE A CB  
778   C CG1 . ILE A 123  ? 0.3798 0.5338 0.3594 0.0093  0.0037  -0.0396 121  ILE A CG1 
779   C CG2 . ILE A 123  ? 0.4263 0.5943 0.4086 0.0142  0.0026  -0.0528 121  ILE A CG2 
780   C CD1 . ILE A 123  ? 0.3691 0.5188 0.3505 0.0104  0.0020  -0.0431 121  ILE A CD1 
781   N N   . ARG A 124  ? 0.4331 0.6357 0.4073 0.0123  0.0060  -0.0456 122  ARG A N   
782   C CA  . ARG A 124  ? 0.4401 0.6573 0.4141 0.0147  0.0061  -0.0514 122  ARG A CA  
783   C C   . ARG A 124  ? 0.4888 0.7129 0.4614 0.0134  0.0081  -0.0472 122  ARG A C   
784   O O   . ARG A 124  ? 0.5821 0.8105 0.5562 0.0153  0.0083  -0.0520 122  ARG A O   
785   C CB  . ARG A 124  ? 0.4680 0.6991 0.4394 0.0157  0.0055  -0.0535 122  ARG A CB  
786   N N   . ASP A 125  ? 0.5797 0.8049 0.5499 0.0102  0.0095  -0.0382 123  ASP A N   
787   C CA  . ASP A 125  ? 0.5737 0.8083 0.5425 0.0087  0.0113  -0.0337 123  ASP A CA  
788   C C   . ASP A 125  ? 0.5668 0.7904 0.5373 0.0069  0.0122  -0.0295 123  ASP A C   
789   O O   . ASP A 125  ? 0.6382 0.8686 0.6088 0.0065  0.0134  -0.0282 123  ASP A O   
790   C CB  . ASP A 125  ? 0.6772 0.9216 0.6428 0.0062  0.0123  -0.0260 123  ASP A CB  
791   C CG  . ASP A 125  ? 0.6870 0.9440 0.6504 0.0079  0.0115  -0.0297 123  ASP A CG  
792   O OD1 . ASP A 125  ? 0.6884 0.9531 0.6524 0.0111  0.0108  -0.0382 123  ASP A OD1 
793   O OD2 . ASP A 125  ? 0.6666 0.9259 0.6280 0.0062  0.0114  -0.0244 123  ASP A OD2 
794   N N   . LYS A 126  ? 0.5276 0.7350 0.4996 0.0058  0.0116  -0.0274 124  LYS A N   
795   C CA  . LYS A 126  ? 0.4984 0.6955 0.4717 0.0039  0.0123  -0.0228 124  LYS A CA  
796   C C   . LYS A 126  ? 0.5425 0.7260 0.5187 0.0054  0.0114  -0.0275 124  LYS A C   
797   O O   . LYS A 126  ? 0.5895 0.7708 0.5672 0.0058  0.0118  -0.0284 124  LYS A O   
798   C CB  . LYS A 126  ? 0.6014 0.7921 0.5737 0.0005  0.0127  -0.0141 124  LYS A CB  
799   N N   . ILE A 127  ? 0.5063 0.6806 0.4834 0.0064  0.0100  -0.0301 125  ILE A N   
800   C CA  . ILE A 127  ? 0.4948 0.6556 0.4748 0.0076  0.0091  -0.0335 125  ILE A CA  
801   C C   . ILE A 127  ? 0.4858 0.6508 0.4681 0.0107  0.0083  -0.0416 125  ILE A C   
802   O O   . ILE A 127  ? 0.5592 0.7192 0.5436 0.0113  0.0084  -0.0429 125  ILE A O   
803   C CB  . ILE A 127  ? 0.4064 0.5570 0.3871 0.0076  0.0078  -0.0339 125  ILE A CB  
804   C CG1 . ILE A 127  ? 0.5023 0.6508 0.4807 0.0048  0.0084  -0.0265 125  ILE A CG1 
805   C CG2 . ILE A 127  ? 0.4538 0.5901 0.4375 0.0083  0.0071  -0.0355 125  ILE A CG2 
806   C CD1 . ILE A 127  ? 0.5314 0.6729 0.5097 0.0023  0.0094  -0.0198 125  ILE A CD1 
807   N N   . ALA A 128  ? 0.4169 0.5912 0.3992 0.0129  0.0074  -0.0473 126  ALA A N   
808   C CA  . ALA A 128  ? 0.3947 0.5717 0.3801 0.0163  0.0062  -0.0560 126  ALA A CA  
809   C C   . ALA A 128  ? 0.5260 0.7116 0.5115 0.0170  0.0073  -0.0572 126  ALA A C   
810   O O   . ALA A 128  ? 0.5044 0.6866 0.4932 0.0191  0.0066  -0.0621 126  ALA A O   
811   C CB  . ALA A 128  ? 0.4168 0.6029 0.4021 0.0184  0.0049  -0.0619 126  ALA A CB  
812   N N   . ASP A 129  ? 0.7466 0.9436 0.7290 0.0154  0.0090  -0.0527 127  ASP A N   
813   C CA  . ASP A 129  ? 0.7979 1.0058 0.7804 0.0162  0.0101  -0.0541 127  ASP A CA  
814   C C   . ASP A 129  ? 0.7769 0.9773 0.7604 0.0144  0.0111  -0.0496 127  ASP A C   
815   O O   . ASP A 129  ? 0.8737 1.0809 0.8581 0.0154  0.0118  -0.0516 127  ASP A O   
816   C CB  . ASP A 129  ? 0.7223 0.9467 0.7013 0.0151  0.0115  -0.0508 127  ASP A CB  
817   N N   . GLY A 130  ? 0.6255 0.8127 0.6089 0.0121  0.0112  -0.0440 128  GLY A N   
818   C CA  . GLY A 130  ? 0.7123 0.8925 0.6967 0.0106  0.0120  -0.0401 128  GLY A CA  
819   C C   . GLY A 130  ? 0.7290 0.8940 0.7134 0.0084  0.0118  -0.0349 128  GLY A C   
820   O O   . GLY A 130  ? 0.7221 0.8764 0.7079 0.0094  0.0105  -0.0373 128  GLY A O   
821   N N   . ASN A 131  ? 0.7418 0.9061 0.7250 0.0054  0.0129  -0.0277 129  ASN A N   
822   C CA  . ASN A 131  ? 0.7674 0.9178 0.7511 0.0034  0.0128  -0.0230 129  ASN A CA  
823   C C   . ASN A 131  ? 0.6933 0.8375 0.6757 0.0025  0.0122  -0.0205 129  ASN A C   
824   O O   . ASN A 131  ? 0.7293 0.8787 0.7098 0.0005  0.0128  -0.0158 129  ASN A O   
825   C CB  . ASN A 131  ? 0.7705 0.9229 0.7538 0.0006  0.0140  -0.0164 129  ASN A CB  
826   N N   . TRP A 132  ? 0.5853 0.7185 0.5690 0.0037  0.0111  -0.0234 130  TRP A N   
827   C CA  . TRP A 132  ? 0.5599 0.6857 0.5428 0.0027  0.0106  -0.0207 130  TRP A CA  
828   C C   . TRP A 132  ? 0.4868 0.6048 0.4692 -0.0001 0.0112  -0.0138 130  TRP A C   
829   O O   . TRP A 132  ? 0.5130 0.6286 0.4943 -0.0016 0.0111  -0.0098 130  TRP A O   
830   C CB  . TRP A 132  ? 0.5039 0.6202 0.4888 0.0047  0.0092  -0.0255 130  TRP A CB  
831   C CG  . TRP A 132  ? 0.4190 0.5258 0.4059 0.0053  0.0090  -0.0265 130  TRP A CG  
832   C CD1 . TRP A 132  ? 0.3834 0.4916 0.3725 0.0074  0.0086  -0.0314 130  TRP A CD1 
833   C CD2 . TRP A 132  ? 0.3253 0.4204 0.3125 0.0039  0.0091  -0.0225 130  TRP A CD2 
834   N NE1 . TRP A 132  ? 0.3864 0.4844 0.3769 0.0073  0.0084  -0.0304 130  TRP A NE1 
835   C CE2 . TRP A 132  ? 0.3261 0.4161 0.3153 0.0052  0.0088  -0.0250 130  TRP A CE2 
836   C CE3 . TRP A 132  ? 0.3610 0.4497 0.3470 0.0018  0.0094  -0.0172 130  TRP A CE3 
837   C CZ2 . TRP A 132  ? 0.3313 0.4106 0.3211 0.0045  0.0087  -0.0224 130  TRP A CZ2 
838   C CZ3 . TRP A 132  ? 0.3369 0.4150 0.3235 0.0012  0.0094  -0.0149 130  TRP A CZ3 
839   C CH2 . TRP A 132  ? 0.3304 0.4040 0.3187 0.0025  0.0091  -0.0175 130  TRP A CH2 
840   N N   . LYS A 133  ? 0.5672 0.6810 0.5507 -0.0006 0.0116  -0.0126 131  LYS A N   
841   C CA  . LYS A 133  ? 0.6493 0.7552 0.6328 -0.0030 0.0119  -0.0067 131  LYS A CA  
842   C C   . LYS A 133  ? 0.7632 0.8762 0.7455 -0.0056 0.0126  -0.0007 131  LYS A C   
843   O O   . LYS A 133  ? 0.8302 0.9376 0.8123 -0.0074 0.0125  0.0041  131  LYS A O   
844   C CB  . LYS A 133  ? 0.5354 0.6368 0.5203 -0.0029 0.0121  -0.0070 131  LYS A CB  
845   N N   . SER A 134  ? 0.7761 0.9016 0.7579 -0.0057 0.0133  -0.0007 132  SER A N   
846   C CA  . SER A 134  ? 0.7643 0.8976 0.7454 -0.0083 0.0140  0.0055  132  SER A CA  
847   C C   . SER A 134  ? 0.7772 0.9112 0.7569 -0.0091 0.0137  0.0083  132  SER A C   
848   O O   . SER A 134  ? 0.8153 0.9512 0.7951 -0.0117 0.0139  0.0147  132  SER A O   
849   C CB  . SER A 134  ? 0.7584 0.9066 0.7391 -0.0079 0.0149  0.0042  132  SER A CB  
850   N N   . HIS A 135  ? 0.7685 0.9009 0.7474 -0.0072 0.0130  0.0038  133  HIS A N   
851   C CA  . HIS A 135  ? 0.7636 0.8982 0.7410 -0.0077 0.0126  0.0059  133  HIS A CA  
852   C C   . HIS A 135  ? 0.7398 0.8617 0.7177 -0.0076 0.0117  0.0061  133  HIS A C   
853   O O   . HIS A 135  ? 0.7008 0.8227 0.6779 -0.0087 0.0113  0.0095  133  HIS A O   
854   C CB  . HIS A 135  ? 0.6959 0.8415 0.6720 -0.0056 0.0124  0.0008  133  HIS A CB  
855   C CG  . HIS A 135  ? 0.7753 0.9343 0.7509 -0.0052 0.0133  -0.0004 133  HIS A CG  
856   N ND1 . HIS A 135  ? 0.8044 0.9645 0.7811 -0.0032 0.0134  -0.0058 133  HIS A ND1 
857   C CD2 . HIS A 135  ? 0.7529 0.9251 0.7272 -0.0065 0.0141  0.0033  133  HIS A CD2 
858   C CE1 . HIS A 135  ? 0.7819 0.9555 0.7580 -0.0032 0.0143  -0.0057 133  HIS A CE1 
859   N NE2 . HIS A 135  ? 0.8116 0.9928 0.7861 -0.0053 0.0148  -0.0001 133  HIS A NE2 
860   N N   . LEU A 136  ? 0.7716 0.8833 0.7508 -0.0064 0.0113  0.0027  134  LEU A N   
861   C CA  . LEU A 136  ? 0.7992 0.8994 0.7789 -0.0062 0.0105  0.0028  134  LEU A CA  
862   C C   . LEU A 136  ? 0.8842 0.9731 0.8653 -0.0066 0.0106  0.0040  134  LEU A C   
863   O O   . LEU A 136  ? 0.8923 0.9726 0.8737 -0.0075 0.0103  0.0069  134  LEU A O   
864   C CB  . LEU A 136  ? 0.7006 0.7998 0.6806 -0.0037 0.0097  -0.0035 134  LEU A CB  
865   C CG  . LEU A 136  ? 0.7202 0.8289 0.6990 -0.0030 0.0093  -0.0052 134  LEU A CG  
866   C CD1 . LEU A 136  ? 0.5735 0.6818 0.5535 -0.0003 0.0083  -0.0124 134  LEU A CD1 
867   C CD2 . LEU A 136  ? 0.5499 0.6561 0.5279 -0.0046 0.0090  -0.0007 134  LEU A CD2 
868   N N   . SER A 139  ? 0.5362 0.5935 0.5221 -0.0145 0.0098  0.0246  137  SER A N   
869   C CA  . SER A 139  ? 0.5445 0.5922 0.5317 -0.0150 0.0092  0.0267  137  SER A CA  
870   C C   . SER A 139  ? 0.5108 0.5507 0.4972 -0.0130 0.0091  0.0229  137  SER A C   
871   O O   . SER A 139  ? 0.5288 0.5605 0.5160 -0.0129 0.0088  0.0233  137  SER A O   
872   C CB  . SER A 139  ? 0.5021 0.5512 0.4899 -0.0166 0.0087  0.0313  137  SER A CB  
873   N N   . ARG A 140  ? 0.3658 0.4086 0.3508 -0.0114 0.0093  0.0191  138  ARG A N   
874   C CA  . ARG A 140  ? 0.3302 0.3665 0.3149 -0.0096 0.0092  0.0156  138  ARG A CA  
875   C C   . ARG A 140  ? 0.4001 0.4394 0.3845 -0.0079 0.0094  0.0109  138  ARG A C   
876   O O   . ARG A 140  ? 0.3791 0.4265 0.3629 -0.0076 0.0095  0.0093  138  ARG A O   
877   C CB  . ARG A 140  ? 0.4079 0.4440 0.3922 -0.0095 0.0088  0.0162  138  ARG A CB  
878   C CG  . ARG A 140  ? 0.4851 0.5172 0.4694 -0.0077 0.0086  0.0123  138  ARG A CG  
879   C CD  . ARG A 140  ? 0.5032 0.5386 0.4871 -0.0077 0.0083  0.0125  138  ARG A CD  
880   N NE  . ARG A 140  ? 0.5686 0.5999 0.5531 -0.0062 0.0079  0.0093  138  ARG A NE  
881   C CZ  . ARG A 140  ? 0.6165 0.6511 0.6013 -0.0048 0.0076  0.0051  138  ARG A CZ  
882   N NH1 . ARG A 140  ? 0.5725 0.6144 0.5568 -0.0044 0.0077  0.0029  138  ARG A NH1 
883   N NH2 . ARG A 140  ? 0.5919 0.6224 0.5778 -0.0037 0.0071  0.0028  138  ARG A NH2 
884   N N   . SER A 141  ? 0.3527 0.3858 0.3376 -0.0067 0.0094  0.0086  139  SER A N   
885   C CA  . SER A 141  ? 0.3321 0.3668 0.3173 -0.0049 0.0093  0.0040  139  SER A CA  
886   C C   . SER A 141  ? 0.3076 0.3452 0.2928 -0.0037 0.0089  0.0011  139  SER A C   
887   O O   . SER A 141  ? 0.2997 0.3340 0.2849 -0.0038 0.0086  0.0019  139  SER A O   
888   C CB  . SER A 141  ? 0.2984 0.3249 0.2843 -0.0038 0.0091  0.0025  139  SER A CB  
889   O OG  . SER A 141  ? 0.3099 0.3375 0.2968 -0.0020 0.0089  -0.0018 139  SER A OG  
890   N N   . LEU A 142  ? 0.2802 0.3243 0.2657 -0.0026 0.0088  -0.0026 140  LEU A N   
891   C CA  . LEU A 142  ? 0.2263 0.2726 0.2124 -0.0012 0.0081  -0.0063 140  LEU A CA  
892   C C   . LEU A 142  ? 0.2372 0.2749 0.2249 0.0000  0.0075  -0.0081 140  LEU A C   
893   O O   . LEU A 142  ? 0.2580 0.2953 0.2466 0.0007  0.0069  -0.0100 140  LEU A O   
894   C CB  . LEU A 142  ? 0.2656 0.3199 0.2523 0.0002  0.0079  -0.0106 140  LEU A CB  
895   C CG  . LEU A 142  ? 0.3882 0.4520 0.3741 0.0005  0.0077  -0.0124 140  LEU A CG  
896   C CD1 . LEU A 142  ? 0.4321 0.5025 0.4159 -0.0015 0.0085  -0.0078 140  LEU A CD1 
897   C CD2 . LEU A 142  ? 0.4046 0.4746 0.3917 0.0025  0.0073  -0.0179 140  LEU A CD2 
898   N N   . PHE A 143  ? 0.2399 0.2710 0.2283 0.0002  0.0077  -0.0075 141  PHE A N   
899   C CA  . PHE A 143  ? 0.2512 0.2754 0.2414 0.0015  0.0071  -0.0095 141  PHE A CA  
900   C C   . PHE A 143  ? 0.2745 0.2909 0.2645 0.0008  0.0073  -0.0063 141  PHE A C   
901   O O   . PHE A 143  ? 0.2797 0.2900 0.2710 0.0016  0.0071  -0.0068 141  PHE A O   
902   C CB  . PHE A 143  ? 0.2477 0.2711 0.2391 0.0026  0.0070  -0.0115 141  PHE A CB  
903   C CG  . PHE A 143  ? 0.2263 0.2580 0.2179 0.0033  0.0069  -0.0147 141  PHE A CG  
904   C CD1 . PHE A 143  ? 0.1967 0.2328 0.1898 0.0047  0.0060  -0.0188 141  PHE A CD1 
905   C CD2 . PHE A 143  ? 0.2413 0.2769 0.2319 0.0028  0.0075  -0.0137 141  PHE A CD2 
906   C CE1 . PHE A 143  ? 0.2416 0.2861 0.2350 0.0056  0.0059  -0.0220 141  PHE A CE1 
907   C CE2 . PHE A 143  ? 0.2640 0.3081 0.2549 0.0035  0.0075  -0.0166 141  PHE A CE2 
908   C CZ  . PHE A 143  ? 0.2311 0.2798 0.2233 0.0050  0.0067  -0.0209 141  PHE A CZ  
909   N N   . VAL A 144  ? 0.2597 0.2766 0.2482 -0.0006 0.0077  -0.0030 142  VAL A N   
910   C CA  A VAL A 144  ? 0.2745 0.2846 0.2628 -0.0012 0.0080  -0.0001 142  VAL A CA  
911   C CA  B VAL A 144  ? 0.2747 0.2846 0.2630 -0.0012 0.0080  -0.0001 142  VAL A CA  
912   C C   . VAL A 144  ? 0.2939 0.2995 0.2839 -0.0002 0.0075  -0.0016 142  VAL A C   
913   O O   . VAL A 144  ? 0.3017 0.3010 0.2920 0.0001  0.0077  -0.0005 142  VAL A O   
914   C CB  A VAL A 144  ? 0.2842 0.2962 0.2712 -0.0028 0.0082  0.0033  142  VAL A CB  
915   C CB  B VAL A 144  ? 0.2845 0.2960 0.2715 -0.0028 0.0082  0.0035  142  VAL A CB  
916   C CG1 A VAL A 144  ? 0.2853 0.2908 0.2725 -0.0030 0.0083  0.0055  142  VAL A CG1 
917   C CG1 B VAL A 144  ? 0.3360 0.3507 0.3221 -0.0040 0.0086  0.0056  142  VAL A CG1 
918   C CG2 A VAL A 144  ? 0.3366 0.3514 0.3227 -0.0040 0.0086  0.0058  142  VAL A CG2 
919   C CG2 B VAL A 144  ? 0.3111 0.3279 0.2980 -0.0029 0.0079  0.0027  142  VAL A CG2 
920   N N   . ASN A 145  ? 0.2641 0.2730 0.2552 0.0004  0.0069  -0.0043 143  ASN A N   
921   C CA  . ASN A 145  ? 0.2988 0.3037 0.2921 0.0013  0.0062  -0.0057 143  ASN A CA  
922   C C   . ASN A 145  ? 0.2892 0.2936 0.2852 0.0028  0.0054  -0.0095 143  ASN A C   
923   O O   . ASN A 145  ? 0.2763 0.2794 0.2749 0.0035  0.0045  -0.0115 143  ASN A O   
924   C CB  . ASN A 145  ? 0.2983 0.3065 0.2918 0.0009  0.0058  -0.0060 143  ASN A CB  
925   C CG  . ASN A 145  ? 0.3393 0.3462 0.3310 -0.0005 0.0064  -0.0020 143  ASN A CG  
926   O OD1 . ASN A 145  ? 0.3636 0.3647 0.3555 -0.0007 0.0068  0.0003  143  ASN A OD1 
927   N ND2 . ASN A 145  ? 0.3268 0.3396 0.3172 -0.0013 0.0064  -0.0010 143  ASN A ND2 
928   N N   . ALA A 146  ? 0.2654 0.2707 0.2613 0.0033  0.0055  -0.0105 144  ALA A N   
929   C CA  . ALA A 146  ? 0.2615 0.2666 0.2603 0.0049  0.0046  -0.0142 144  ALA A CA  
930   C C   . ALA A 146  ? 0.2562 0.2542 0.2577 0.0055  0.0041  -0.0137 144  ALA A C   
931   O O   . ALA A 146  ? 0.2819 0.2792 0.2868 0.0067  0.0029  -0.0167 144  ALA A O   
932   C CB  . ALA A 146  ? 0.2397 0.2474 0.2377 0.0053  0.0048  -0.0151 144  ALA A CB  
933   N N   . ALA A 147  ? 0.2676 0.2605 0.2678 0.0048  0.0049  -0.0100 145  ALA A N   
934   C CA  . ALA A 147  ? 0.3019 0.2890 0.3047 0.0053  0.0045  -0.0092 145  ALA A CA  
935   C C   . ALA A 147  ? 0.3189 0.3056 0.3245 0.0054  0.0036  -0.0105 145  ALA A C   
936   O O   . ALA A 147  ? 0.3168 0.3009 0.3264 0.0062  0.0026  -0.0118 145  ALA A O   
937   C CB  . ALA A 147  ? 0.3457 0.3285 0.3462 0.0045  0.0056  -0.0052 145  ALA A CB  
938   N N   . THR A 148  ? 0.2675 0.2573 0.2716 0.0045  0.0039  -0.0102 146  THR A N   
939   C CA  . THR A 148  ? 0.2641 0.2543 0.2709 0.0046  0.0029  -0.0118 146  THR A CA  
940   C C   . THR A 148  ? 0.2730 0.2668 0.2830 0.0058  0.0014  -0.0166 146  THR A C   
941   O O   . THR A 148  ? 0.2891 0.2806 0.3035 0.0065  0.0001  -0.0184 146  THR A O   
942   C CB  . THR A 148  ? 0.3071 0.3005 0.3113 0.0035  0.0035  -0.0103 146  THR A CB  
943   O OG1 . THR A 148  ? 0.3136 0.3034 0.3155 0.0026  0.0047  -0.0061 146  THR A OG1 
944   C CG2 . THR A 148  ? 0.3770 0.3711 0.3839 0.0036  0.0024  -0.0118 146  THR A CG2 
945   N N   . TRP A 149  ? 0.2571 0.2569 0.2652 0.0061  0.0015  -0.0187 147  TRP A N   
946   C CA  . TRP A 149  ? 0.2627 0.2665 0.2737 0.0075  0.0000  -0.0238 147  TRP A CA  
947   C C   . TRP A 149  ? 0.2418 0.2417 0.2566 0.0087  -0.0010 -0.0255 147  TRP A C   
948   O O   . TRP A 149  ? 0.2749 0.2756 0.2942 0.0100  -0.0027 -0.0296 147  TRP A O   
949   C CB  . TRP A 149  ? 0.2726 0.2843 0.2805 0.0076  0.0005  -0.0254 147  TRP A CB  
950   C CG  . TRP A 149  ? 0.2479 0.2644 0.2529 0.0065  0.0010  -0.0241 147  TRP A CG  
951   C CD1 . TRP A 149  ? 0.3085 0.3275 0.3094 0.0051  0.0024  -0.0206 147  TRP A CD1 
952   C CD2 . TRP A 149  ? 0.2739 0.2933 0.2803 0.0066  0.0000  -0.0262 147  TRP A CD2 
953   N NE1 . TRP A 149  ? 0.2798 0.3032 0.2793 0.0044  0.0023  -0.0200 147  TRP A NE1 
954   C CE2 . TRP A 149  ? 0.2789 0.3027 0.2815 0.0054  0.0009  -0.0236 147  TRP A CE2 
955   C CE3 . TRP A 149  ? 0.3162 0.3349 0.3270 0.0077  -0.0018 -0.0301 147  TRP A CE3 
956   C CZ2 . TRP A 149  ? 0.3041 0.3320 0.3068 0.0052  0.0002  -0.0246 147  TRP A CZ2 
957   C CZ3 . TRP A 149  ? 0.3386 0.3613 0.3496 0.0075  -0.0025 -0.0314 147  TRP A CZ3 
958   C CH2 . TRP A 149  ? 0.3806 0.4080 0.3874 0.0063  -0.0015 -0.0287 147  TRP A CH2 
959   N N   . GLY A 150  ? 0.2486 0.2447 0.2621 0.0085  0.0000  -0.0226 148  GLY A N   
960   C CA  . GLY A 150  ? 0.2725 0.2643 0.2897 0.0096  -0.0010 -0.0234 148  GLY A CA  
961   C C   . GLY A 150  ? 0.2738 0.2605 0.2957 0.0097  -0.0021 -0.0230 148  GLY A C   
962   O O   . GLY A 150  ? 0.3354 0.3207 0.3624 0.0109  -0.0038 -0.0257 148  GLY A O   
963   N N   . LEU A 151  ? 0.2969 0.2811 0.3176 0.0085  -0.0013 -0.0196 149  LEU A N   
964   C CA  A LEU A 151  ? 0.3179 0.2979 0.3432 0.0084  -0.0023 -0.0190 149  LEU A CA  
965   C CA  B LEU A 151  ? 0.3179 0.2979 0.3432 0.0084  -0.0023 -0.0190 149  LEU A CA  
966   C C   . LEU A 151  ? 0.3147 0.2975 0.3442 0.0091  -0.0042 -0.0236 149  LEU A C   
967   O O   . LEU A 151  ? 0.3726 0.3526 0.4080 0.0097  -0.0060 -0.0251 149  LEU A O   
968   C CB  A LEU A 151  ? 0.3473 0.3250 0.3702 0.0070  -0.0010 -0.0147 149  LEU A CB  
969   C CB  B LEU A 151  ? 0.3475 0.3252 0.3702 0.0070  -0.0009 -0.0147 149  LEU A CB  
970   C CG  A LEU A 151  ? 0.3716 0.3443 0.3939 0.0066  0.0001  -0.0102 149  LEU A CG  
971   C CG  B LEU A 151  ? 0.3377 0.3103 0.3639 0.0066  -0.0012 -0.0119 149  LEU A CG  
972   C CD1 A LEU A 151  ? 0.3729 0.3445 0.3924 0.0055  0.0015  -0.0067 149  LEU A CD1 
973   C CD1 B LEU A 151  ? 0.3802 0.3491 0.4093 0.0073  -0.0016 -0.0107 149  LEU A CD1 
974   C CD2 A LEU A 151  ? 0.3806 0.3493 0.4089 0.0072  -0.0013 -0.0100 149  LEU A CD2 
975   C CD2 B LEU A 151  ? 0.3759 0.3473 0.3981 0.0054  0.0007  -0.0077 149  LEU A CD2 
976   N N   . VAL A 152  ? 0.2820 0.2707 0.3087 0.0090  -0.0041 -0.0260 150  VAL A N   
977   C CA  . VAL A 152  ? 0.2935 0.2860 0.3237 0.0097  -0.0059 -0.0308 150  VAL A CA  
978   C C   . VAL A 152  ? 0.3489 0.3427 0.3834 0.0115  -0.0077 -0.0357 150  VAL A C   
979   O O   . VAL A 152  ? 0.3476 0.3404 0.3881 0.0124  -0.0098 -0.0391 150  VAL A O   
980   C CB  . VAL A 152  ? 0.3207 0.3203 0.3464 0.0093  -0.0051 -0.0318 150  VAL A CB  
981   C CG1 . VAL A 152  ? 0.4057 0.4106 0.4344 0.0105  -0.0071 -0.0377 150  VAL A CG1 
982   C CG2 . VAL A 152  ? 0.3540 0.3519 0.3768 0.0077  -0.0039 -0.0275 150  VAL A CG2 
983   N N   . VAL A 153  ? 0.2950 0.2911 0.3269 0.0122  -0.0069 -0.0362 151  VAL A N   
984   C CA  . VAL A 153  ? 0.3022 0.3006 0.3377 0.0141  -0.0085 -0.0412 151  VAL A CA  
985   C C   . VAL A 153  ? 0.2900 0.2816 0.3309 0.0147  -0.0098 -0.0404 151  VAL A C   
986   O O   . VAL A 153  ? 0.3508 0.3418 0.3981 0.0161  -0.0121 -0.0445 151  VAL A O   
987   C CB  . VAL A 153  ? 0.2808 0.2848 0.3116 0.0145  -0.0073 -0.0420 151  VAL A CB  
988   C CG1 . VAL A 153  ? 0.3095 0.3155 0.3443 0.0165  -0.0088 -0.0468 151  VAL A CG1 
989   C CG2 . VAL A 153  ? 0.3002 0.3120 0.3268 0.0140  -0.0065 -0.0431 151  VAL A CG2 
990   N N   . THR A 154  ? 0.3171 0.3038 0.3558 0.0138  -0.0084 -0.0352 152  THR A N   
991   C CA  . THR A 154  ? 0.3392 0.3204 0.3822 0.0145  -0.0093 -0.0339 152  THR A CA  
992   C C   . THR A 154  ? 0.3926 0.3674 0.4388 0.0135  -0.0096 -0.0298 152  THR A C   
993   O O   . THR A 154  ? 0.4176 0.3881 0.4686 0.0140  -0.0108 -0.0288 152  THR A O   
994   C CB  . THR A 154  ? 0.3452 0.3262 0.3840 0.0145  -0.0077 -0.0312 152  THR A CB  
995   O OG1 . THR A 154  ? 0.3723 0.3509 0.4062 0.0128  -0.0056 -0.0258 152  THR A OG1 
996   C CG2 . THR A 154  ? 0.3293 0.3170 0.3644 0.0152  -0.0072 -0.0344 152  THR A CG2 
997   N N   . GLY A 155  ? 0.3545 0.3289 0.3984 0.0120  -0.0085 -0.0271 153  GLY A N   
998   C CA  . GLY A 155  ? 0.3597 0.3287 0.4058 0.0110  -0.0083 -0.0226 153  GLY A CA  
999   C C   . GLY A 155  ? 0.4412 0.4072 0.4836 0.0104  -0.0065 -0.0173 153  GLY A C   
1000  O O   . GLY A 155  ? 0.4304 0.3926 0.4742 0.0096  -0.0061 -0.0132 153  GLY A O   
1001  N N   . LYS A 156  ? 0.3695 0.3375 0.4073 0.0108  -0.0054 -0.0173 154  LYS A N   
1002  C CA  . LYS A 156  ? 0.4239 0.3895 0.4583 0.0105  -0.0038 -0.0129 154  LYS A CA  
1003  C C   . LYS A 156  ? 0.3794 0.3475 0.4067 0.0095  -0.0017 -0.0113 154  LYS A C   
1004  O O   . LYS A 156  ? 0.3637 0.3361 0.3884 0.0095  -0.0014 -0.0139 154  LYS A O   
1005  C CB  . LYS A 156  ? 0.4485 0.4140 0.4838 0.0118  -0.0045 -0.0141 154  LYS A CB  
1006  N N   . LEU A 157  ? 0.3842 0.3497 0.4087 0.0088  -0.0002 -0.0069 155  LEU A N   
1007  C CA  . LEU A 157  ? 0.4451 0.4122 0.4636 0.0079  0.0016  -0.0051 155  LEU A CA  
1008  C C   . LEU A 157  ? 0.5108 0.4781 0.5260 0.0083  0.0024  -0.0041 155  LEU A C   
1009  O O   . LEU A 157  ? 0.5010 0.4658 0.5175 0.0089  0.0021  -0.0024 155  LEU A O   
1010  C CB  . LEU A 157  ? 0.4143 0.3789 0.4320 0.0070  0.0026  -0.0013 155  LEU A CB  
1011  C CG  . LEU A 157  ? 0.4991 0.4647 0.5113 0.0062  0.0044  0.0008  155  LEU A CG  
1012  C CD1 . LEU A 157  ? 0.4820 0.4513 0.4921 0.0056  0.0045  -0.0013 155  LEU A CD1 
1013  C CD2 . LEU A 157  ? 0.4661 0.4292 0.4782 0.0057  0.0052  0.0043  155  LEU A CD2 
1014  N N   . THR A 158  ? 0.5259 0.4966 0.5372 0.0080  0.0031  -0.0052 156  THR A N   
1015  C CA  . THR A 158  ? 0.5761 0.5472 0.5838 0.0080  0.0040  -0.0040 156  THR A CA  
1016  C C   . THR A 158  ? 0.5699 0.5417 0.5733 0.0068  0.0054  -0.0019 156  THR A C   
1017  O O   . THR A 158  ? 0.6407 0.6149 0.6433 0.0061  0.0056  -0.0027 156  THR A O   
1018  C CB  . THR A 158  ? 0.6647 0.6395 0.6723 0.0086  0.0035  -0.0071 156  THR A CB  
1019  O OG1 . THR A 158  ? 0.6830 0.6576 0.6952 0.0098  0.0019  -0.0099 156  THR A OG1 
1020  C CG2 . THR A 158  ? 0.6376 0.6120 0.6428 0.0089  0.0040  -0.0058 156  THR A CG2 
1021  N N   . SER A 159  ? 0.4165 0.3864 0.4174 0.0067  0.0063  0.0007  157  SER A N   
1022  C CA  . SER A 159  ? 0.4050 0.3749 0.4026 0.0057  0.0074  0.0026  157  SER A CA  
1023  C C   . SER A 159  ? 0.4127 0.3860 0.4078 0.0051  0.0077  0.0016  157  SER A C   
1024  O O   . SER A 159  ? 0.4393 0.4138 0.4329 0.0041  0.0081  0.0024  157  SER A O   
1025  C CB  . SER A 159  ? 0.5158 0.4830 0.5118 0.0060  0.0081  0.0052  157  SER A CB  
1026  O OG  . SER A 159  ? 0.5879 0.5545 0.5844 0.0069  0.0077  0.0050  157  SER A OG  
1027  N N   . THR A 160  ? 0.4049 0.3800 0.3999 0.0055  0.0073  0.0001  158  THR A N   
1028  C CA  . THR A 160  ? 0.3099 0.2889 0.3031 0.0048  0.0075  -0.0006 158  THR A CA  
1029  C C   . THR A 160  ? 0.3523 0.3351 0.3472 0.0054  0.0068  -0.0038 158  THR A C   
1030  O O   . THR A 160  ? 0.3565 0.3384 0.3542 0.0065  0.0060  -0.0055 158  THR A O   
1031  C CB  . THR A 160  ? 0.3560 0.3343 0.3473 0.0048  0.0079  0.0005  158  THR A CB  
1032  O OG1 . THR A 160  ? 0.3926 0.3698 0.3850 0.0060  0.0073  -0.0005 158  THR A OG1 
1033  C CG2 . THR A 160  ? 0.4640 0.4389 0.4536 0.0044  0.0085  0.0030  158  THR A CG2 
1034  N N   . VAL A 161  ? 0.2529 0.2404 0.2465 0.0047  0.0070  -0.0044 159  VAL A N   
1035  C CA  . VAL A 161  ? 0.2671 0.2599 0.2620 0.0051  0.0065  -0.0075 159  VAL A CA  
1036  C C   . VAL A 161  ? 0.2524 0.2479 0.2470 0.0055  0.0065  -0.0086 159  VAL A C   
1037  O O   . VAL A 161  ? 0.2416 0.2377 0.2341 0.0045  0.0071  -0.0068 159  VAL A O   
1038  C CB  . VAL A 161  ? 0.2832 0.2804 0.2766 0.0039  0.0069  -0.0071 159  VAL A CB  
1039  C CG1 . VAL A 161  ? 0.3209 0.3249 0.3150 0.0043  0.0065  -0.0101 159  VAL A CG1 
1040  C CG2 . VAL A 161  ? 0.3432 0.3380 0.3373 0.0037  0.0068  -0.0064 159  VAL A CG2 
1041  N N   . ASN A 162  ? 0.2244 0.2214 0.2214 0.0069  0.0056  -0.0118 160  ASN A N   
1042  C CA  . ASN A 162  ? 0.2522 0.2527 0.2491 0.0073  0.0056  -0.0131 160  ASN A CA  
1043  C C   . ASN A 162  ? 0.2100 0.2180 0.2061 0.0068  0.0059  -0.0146 160  ASN A C   
1044  O O   . ASN A 162  ? 0.2100 0.2221 0.2081 0.0079  0.0052  -0.0182 160  ASN A O   
1045  C CB  . ASN A 162  ? 0.2371 0.2364 0.2371 0.0092  0.0045  -0.0157 160  ASN A CB  
1046  C CG  . ASN A 162  ? 0.2427 0.2456 0.2426 0.0096  0.0045  -0.0169 160  ASN A CG  
1047  O OD1 . ASN A 162  ? 0.2382 0.2462 0.2362 0.0086  0.0052  -0.0167 160  ASN A OD1 
1048  N ND2 . ASN A 162  ? 0.2935 0.2940 0.2956 0.0110  0.0037  -0.0180 160  ASN A ND2 
1049  N N   . ASP A 163  ? 0.2062 0.2164 0.1998 0.0051  0.0068  -0.0120 161  ASP A N   
1050  C CA  . ASP A 163  ? 0.2291 0.2467 0.2218 0.0043  0.0072  -0.0125 161  ASP A CA  
1051  C C   . ASP A 163  ? 0.2103 0.2345 0.2037 0.0049  0.0071  -0.0148 161  ASP A C   
1052  O O   . ASP A 163  ? 0.2173 0.2486 0.2106 0.0050  0.0072  -0.0166 161  ASP A O   
1053  C CB  . ASP A 163  ? 0.2477 0.2655 0.2381 0.0022  0.0080  -0.0084 161  ASP A CB  
1054  C CG  . ASP A 163  ? 0.2823 0.2970 0.2719 0.0013  0.0083  -0.0057 161  ASP A CG  
1055  O OD1 . ASP A 163  ? 0.2494 0.2589 0.2394 0.0022  0.0080  -0.0060 161  ASP A OD1 
1056  O OD2 . ASP A 163  ? 0.2822 0.2998 0.2707 -0.0003 0.0088  -0.0032 161  ASP A OD2 
1057  N N   . ARG A 164  ? 0.2214 0.2437 0.2153 0.0055  0.0070  -0.0151 162  ARG A N   
1058  C CA  A ARG A 164  ? 0.1959 0.2246 0.1908 0.0062  0.0069  -0.0176 162  ARG A CA  
1059  C CA  B ARG A 164  ? 0.1966 0.2253 0.1915 0.0063  0.0069  -0.0176 162  ARG A CA  
1060  C C   . ARG A 164  ? 0.1861 0.2164 0.1838 0.0085  0.0059  -0.0224 162  ARG A C   
1061  O O   . ARG A 164  ? 0.2074 0.2453 0.2059 0.0093  0.0058  -0.0253 162  ARG A O   
1062  C CB  A ARG A 164  ? 0.2244 0.2509 0.2192 0.0061  0.0070  -0.0164 162  ARG A CB  
1063  C CB  B ARG A 164  ? 0.2246 0.2508 0.2195 0.0062  0.0070  -0.0164 162  ARG A CB  
1064  C CG  A ARG A 164  ? 0.2579 0.2842 0.2507 0.0039  0.0078  -0.0123 162  ARG A CG  
1065  C CG  B ARG A 164  ? 0.2581 0.2838 0.2510 0.0040  0.0077  -0.0123 162  ARG A CG  
1066  C CD  A ARG A 164  ? 0.3222 0.3554 0.3139 0.0024  0.0085  -0.0109 162  ARG A CD  
1067  C CD  B ARG A 164  ? 0.2480 0.2822 0.2402 0.0027  0.0084  -0.0116 162  ARG A CD  
1068  N NE  A ARG A 164  ? 0.2584 0.3004 0.2509 0.0030  0.0087  -0.0135 162  ARG A NE  
1069  N NE  B ARG A 164  ? 0.3504 0.3869 0.3415 0.0016  0.0088  -0.0103 162  ARG A NE  
1070  C CZ  A ARG A 164  ? 0.3874 0.4371 0.3792 0.0022  0.0092  -0.0134 162  ARG A CZ  
1071  C CZ  B ARG A 164  ? 0.3315 0.3764 0.3222 0.0012  0.0092  -0.0108 162  ARG A CZ  
1072  N NH1 A ARG A 164  ? 0.3455 0.3950 0.3358 0.0008  0.0095  -0.0106 162  ARG A NH1 
1073  N NH1 B ARG A 164  ? 0.3882 0.4405 0.3798 0.0019  0.0094  -0.0130 162  ARG A NH1 
1074  N NH2 A ARG A 164  ? 0.2760 0.3343 0.2686 0.0030  0.0093  -0.0161 162  ARG A NH2 
1075  N NH2 B ARG A 164  ? 0.3662 0.4128 0.3558 0.0002  0.0095  -0.0092 162  ARG A NH2 
1076  N N   . SER A 165  ? 0.1851 0.2087 0.1847 0.0096  0.0050  -0.0231 163  SER A N   
1077  C CA  . SER A 165  ? 0.1888 0.2133 0.1919 0.0117  0.0037  -0.0276 163  SER A CA  
1078  C C   . SER A 165  ? 0.1830 0.2124 0.1861 0.0117  0.0036  -0.0296 163  SER A C   
1079  O O   . SER A 165  ? 0.1829 0.2180 0.1880 0.0132  0.0029  -0.0341 163  SER A O   
1080  C CB  . SER A 165  ? 0.2042 0.2201 0.2096 0.0125  0.0028  -0.0270 163  SER A CB  
1081  O OG  . SER A 165  ? 0.2378 0.2538 0.2471 0.0142  0.0013  -0.0310 163  SER A OG  
1082  N N   . LEU A 166  ? 0.1976 0.2252 0.1985 0.0101  0.0043  -0.0266 164  LEU A N   
1083  C CA  . LEU A 166  ? 0.1981 0.2307 0.1988 0.0100  0.0041  -0.0282 164  LEU A CA  
1084  C C   . LEU A 166  ? 0.1759 0.2185 0.1747 0.0096  0.0049  -0.0291 164  LEU A C   
1085  O O   . LEU A 166  ? 0.1904 0.2396 0.1901 0.0105  0.0044  -0.0327 164  LEU A O   
1086  C CB  . LEU A 166  ? 0.1935 0.2219 0.1922 0.0083  0.0047  -0.0244 164  LEU A CB  
1087  C CG  . LEU A 166  ? 0.1964 0.2162 0.1973 0.0089  0.0039  -0.0241 164  LEU A CG  
1088  C CD1 . LEU A 166  ? 0.2363 0.2524 0.2352 0.0073  0.0046  -0.0202 164  LEU A CD1 
1089  C CD2 . LEU A 166  ? 0.2192 0.2399 0.2239 0.0106  0.0024  -0.0287 164  LEU A CD2 
1090  N N   . ALA A 167  ? 0.1887 0.2330 0.1852 0.0081  0.0060  -0.0257 165  ALA A N   
1091  C CA  . ALA A 167  ? 0.2149 0.2693 0.2100 0.0075  0.0068  -0.0259 165  ALA A CA  
1092  C C   . ALA A 167  ? 0.1781 0.2385 0.1754 0.0096  0.0062  -0.0310 165  ALA A C   
1093  O O   . ALA A 167  ? 0.2049 0.2746 0.2020 0.0102  0.0063  -0.0336 165  ALA A O   
1094  C CB  . ALA A 167  ? 0.2165 0.2710 0.2095 0.0054  0.0079  -0.0212 165  ALA A CB  
1095  N N   . ALA A 168  ? 0.1850 0.2405 0.1844 0.0109  0.0055  -0.0325 166  ALA A N   
1096  C CA  . ALA A 168  ? 0.2097 0.2702 0.2119 0.0131  0.0048  -0.0375 166  ALA A CA  
1097  C C   . ALA A 168  ? 0.1850 0.2475 0.1897 0.0151  0.0035  -0.0427 166  ALA A C   
1098  O O   . ALA A 168  ? 0.1934 0.2647 0.1991 0.0165  0.0032  -0.0470 166  ALA A O   
1099  C CB  . ALA A 168  ? 0.1758 0.2294 0.1800 0.0141  0.0041  -0.0377 166  ALA A CB  
1100  N N   . ALA A 169  ? 0.1946 0.2494 0.2006 0.0152  0.0026  -0.0423 167  ALA A N   
1101  C CA  . ALA A 169  ? 0.1789 0.2346 0.1880 0.0169  0.0011  -0.0471 167  ALA A CA  
1102  C C   . ALA A 169  ? 0.1794 0.2441 0.1865 0.0166  0.0015  -0.0484 167  ALA A C   
1103  O O   . ALA A 169  ? 0.1833 0.2540 0.1926 0.0185  0.0004  -0.0539 167  ALA A O   
1104  C CB  . ALA A 169  ? 0.1989 0.2444 0.2097 0.0166  0.0002  -0.0454 167  ALA A CB  
1105  N N   . LEU A 170  ? 0.1989 0.2648 0.2019 0.0143  0.0029  -0.0436 168  LEU A N   
1106  C CA  . LEU A 170  ? 0.1892 0.2639 0.1901 0.0138  0.0033  -0.0441 168  LEU A CA  
1107  C C   . LEU A 170  ? 0.2023 0.2888 0.2024 0.0146  0.0039  -0.0466 168  LEU A C   
1108  O O   . LEU A 170  ? 0.2020 0.2970 0.2027 0.0159  0.0033  -0.0509 168  LEU A O   
1109  C CB  . LEU A 170  ? 0.1966 0.2692 0.1939 0.0110  0.0046  -0.0377 168  LEU A CB  
1110  C CG  . LEU A 170  ? 0.1967 0.2778 0.1916 0.0103  0.0049  -0.0373 168  LEU A CG  
1111  C CD1 . LEU A 170  ? 0.2449 0.3258 0.2421 0.0119  0.0034  -0.0419 168  LEU A CD1 
1112  C CD2 . LEU A 170  ? 0.2570 0.3347 0.2491 0.0076  0.0060  -0.0308 168  LEU A CD2 
1113  N N   . THR A 171  ? 0.1896 0.2774 0.1887 0.0138  0.0049  -0.0442 169  THR A N   
1114  C CA  . THR A 171  ? 0.2043 0.3036 0.2031 0.0146  0.0055  -0.0466 169  THR A CA  
1115  C C   . THR A 171  ? 0.1952 0.2975 0.1978 0.0178  0.0040  -0.0541 169  THR A C   
1116  O O   . THR A 171  ? 0.2124 0.3256 0.2151 0.0192  0.0039  -0.0582 169  THR A O   
1117  C CB  . THR A 171  ? 0.2234 0.3220 0.2214 0.0134  0.0066  -0.0431 169  THR A CB  
1118  O OG1 . THR A 171  ? 0.2522 0.3485 0.2472 0.0104  0.0079  -0.0364 169  THR A OG1 
1119  C CG2 . THR A 171  ? 0.2666 0.3772 0.2648 0.0143  0.0072  -0.0457 169  THR A CG2 
1120  N N   . ARG A 172  ? 0.1867 0.2797 0.1929 0.0191  0.0027  -0.0560 170  ARG A N   
1121  C CA  . ARG A 172  ? 0.1826 0.2774 0.1933 0.0222  0.0009  -0.0630 170  ARG A CA  
1122  C C   . ARG A 172  ? 0.1919 0.2906 0.2041 0.0237  -0.0004 -0.0678 170  ARG A C   
1123  O O   . ARG A 172  ? 0.1923 0.2999 0.2063 0.0259  -0.0011 -0.0738 170  ARG A O   
1124  C CB  . ARG A 172  ? 0.1866 0.2697 0.2010 0.0231  -0.0003 -0.0630 170  ARG A CB  
1125  C CG  . ARG A 172  ? 0.2092 0.2939 0.2288 0.0262  -0.0022 -0.0697 170  ARG A CG  
1126  C CD  . ARG A 172  ? 0.2191 0.2920 0.2428 0.0270  -0.0037 -0.0693 170  ARG A CD  
1127  N NE  . ARG A 172  ? 0.1964 0.2625 0.2176 0.0250  -0.0025 -0.0631 170  ARG A NE  
1128  C CZ  . ARG A 172  ? 0.1818 0.2391 0.2014 0.0231  -0.0021 -0.0582 170  ARG A CZ  
1129  N NH1 . ARG A 172  ? 0.1991 0.2529 0.2194 0.0228  -0.0028 -0.0582 170  ARG A NH1 
1130  N NH2 . ARG A 172  ? 0.1907 0.2430 0.2081 0.0217  -0.0011 -0.0532 170  ARG A NH2 
1131  N N   . LEU A 173  ? 0.1967 0.2891 0.2083 0.0225  -0.0007 -0.0655 171  LEU A N   
1132  C CA  . LEU A 173  ? 0.1926 0.2878 0.2063 0.0239  -0.0023 -0.0703 171  LEU A CA  
1133  C C   . LEU A 173  ? 0.1898 0.2982 0.2000 0.0238  -0.0014 -0.0714 171  LEU A C   
1134  O O   . LEU A 173  ? 0.1978 0.3135 0.2100 0.0259  -0.0027 -0.0777 171  LEU A O   
1135  C CB  . LEU A 173  ? 0.2111 0.2963 0.2253 0.0226  -0.0029 -0.0674 171  LEU A CB  
1136  C CG  . LEU A 173  ? 0.2313 0.3153 0.2407 0.0198  -0.0013 -0.0611 171  LEU A CG  
1137  C CD1 . LEU A 173  ? 0.2525 0.3447 0.2606 0.0200  -0.0017 -0.0635 171  LEU A CD1 
1138  C CD2 . LEU A 173  ? 0.2486 0.3200 0.2590 0.0185  -0.0016 -0.0572 171  LEU A CD2 
1139  N N   . ILE A 174  ? 0.1983 0.3103 0.2036 0.0213  0.0007  -0.0655 172  ILE A N   
1140  C CA  . ILE A 174  ? 0.1970 0.3222 0.1990 0.0210  0.0016  -0.0658 172  ILE A CA  
1141  C C   . ILE A 174  ? 0.2099 0.3464 0.2128 0.0230  0.0018  -0.0706 172  ILE A C   
1142  O O   . ILE A 174  ? 0.2301 0.3775 0.2330 0.0248  0.0013  -0.0755 172  ILE A O   
1143  C CB  . ILE A 174  ? 0.2158 0.3415 0.2131 0.0176  0.0037  -0.0576 172  ILE A CB  
1144  C CG1 . ILE A 174  ? 0.2522 0.3693 0.2487 0.0160  0.0033  -0.0541 172  ILE A CG1 
1145  C CG2 . ILE A 174  ? 0.2419 0.3828 0.2360 0.0173  0.0048  -0.0573 172  ILE A CG2 
1146  C CD1 . ILE A 174  ? 0.2703 0.3849 0.2631 0.0129  0.0050  -0.0460 172  ILE A CD1 
1147  N N   . SER A 175  ? 0.1915 0.3259 0.1952 0.0230  0.0025  -0.0695 173  SER A N   
1148  C CA  . SER A 175  ? 0.1990 0.3445 0.2037 0.0250  0.0027  -0.0739 173  SER A CA  
1149  C C   . SER A 175  ? 0.2314 0.3782 0.2410 0.0287  0.0004  -0.0828 173  SER A C   
1150  O O   . SER A 175  ? 0.2615 0.4202 0.2719 0.0309  0.0002  -0.0882 173  SER A O   
1151  C CB  . SER A 175  ? 0.2553 0.3977 0.2603 0.0242  0.0037  -0.0708 173  SER A CB  
1152  O OG  . SER A 175  ? 0.3147 0.4577 0.3155 0.0210  0.0057  -0.0632 173  SER A OG  
1153  N N   . ARG A 176  ? 0.2108 0.3459 0.2241 0.0294  -0.0015 -0.0845 174  ARG A N   
1154  C CA  . ARG A 176  ? 0.2016 0.3367 0.2206 0.0328  -0.0040 -0.0928 174  ARG A CA  
1155  C C   . ARG A 176  ? 0.2563 0.3973 0.2757 0.0340  -0.0053 -0.0973 174  ARG A C   
1156  O O   . ARG A 176  ? 0.2675 0.4173 0.2897 0.0369  -0.0066 -0.1049 174  ARG A O   
1157  C CB  . ARG A 176  ? 0.2311 0.3512 0.2547 0.0331  -0.0056 -0.0922 174  ARG A CB  
1158  C CG  . ARG A 176  ? 0.2511 0.3698 0.2817 0.0366  -0.0085 -0.1003 174  ARG A CG  
1159  C CD  . ARG A 176  ? 0.2531 0.3573 0.2881 0.0365  -0.0099 -0.0986 174  ARG A CD  
1160  N NE  . ARG A 176  ? 0.2371 0.3323 0.2726 0.0350  -0.0106 -0.0958 174  ARG A NE  
1161  C CZ  . ARG A 176  ? 0.2454 0.3314 0.2783 0.0323  -0.0094 -0.0885 174  ARG A CZ  
1162  N NH1 . ARG A 176  ? 0.2131 0.2964 0.2429 0.0307  -0.0076 -0.0832 174  ARG A NH1 
1163  N NH2 . ARG A 176  ? 0.3184 0.3979 0.3518 0.0311  -0.0101 -0.0867 174  ARG A NH2 
1164  N N   . CYS A 177  ? 0.2460 0.3829 0.2627 0.0317  -0.0049 -0.0929 175  CYS A N   
1165  C CA  . CYS A 177  ? 0.2502 0.3903 0.2679 0.0327  -0.0064 -0.0970 175  CYS A CA  
1166  C C   . CYS A 177  ? 0.2775 0.4280 0.2895 0.0312  -0.0049 -0.0942 175  CYS A C   
1167  O O   . CYS A 177  ? 0.2989 0.4557 0.3114 0.0325  -0.0061 -0.0988 175  CYS A O   
1168  C CB  . CYS A 177  ? 0.2832 0.4094 0.3038 0.0318  -0.0078 -0.0953 175  CYS A CB  
1169  S SG  . CYS A 177  ? 0.2949 0.4084 0.3227 0.0335  -0.0099 -0.0979 175  CYS A SG  
1170  N N   . GLY A 178  ? 0.2835 0.4357 0.2904 0.0284  -0.0024 -0.0868 176  GLY A N   
1171  C CA  . GLY A 178  ? 0.2789 0.4427 0.2807 0.0271  -0.0009 -0.0839 176  GLY A CA  
1172  C C   . GLY A 178  ? 0.2435 0.4047 0.2437 0.0257  -0.0014 -0.0816 176  GLY A C   
1173  O O   . GLY A 178  ? 0.2486 0.3975 0.2505 0.0248  -0.0022 -0.0797 176  GLY A O   
1174  N N   . GLU A 179  ? 0.3049 0.4789 0.3017 0.0256  -0.0008 -0.0817 177  GLU A N   
1175  C CA  . GLU A 179  ? 0.2771 0.4505 0.2718 0.0242  -0.0011 -0.0791 177  GLU A CA  
1176  C C   . GLU A 179  ? 0.2476 0.4131 0.2466 0.0257  -0.0036 -0.0841 177  GLU A C   
1177  O O   . GLU A 179  ? 0.3015 0.4585 0.2999 0.0238  -0.0038 -0.0799 177  GLU A O   
1178  C CB  . GLU A 179  ? 0.2868 0.4771 0.2777 0.0245  -0.0004 -0.0797 177  GLU A CB  
1179  C CG  . GLU A 179  ? 0.3705 0.5612 0.3586 0.0228  -0.0006 -0.0759 177  GLU A CG  
1180  C CD  . GLU A 179  ? 0.5763 0.7699 0.5668 0.0252  -0.0030 -0.0833 177  GLU A CD  
1181  O OE1 . GLU A 179  ? 0.5632 0.7626 0.5567 0.0283  -0.0044 -0.0916 177  GLU A OE1 
1182  O OE2 . GLU A 179  ? 0.6843 0.8745 0.6739 0.0240  -0.0036 -0.0809 177  GLU A OE2 
1183  N N   . PRO A 180  ? 0.2314 0.3991 0.2350 0.0289  -0.0058 -0.0928 178  PRO A N   
1184  C CA  . PRO A 180  ? 0.2636 0.4235 0.2717 0.0300  -0.0083 -0.0972 178  PRO A CA  
1185  C C   . PRO A 180  ? 0.2617 0.4049 0.2721 0.0282  -0.0085 -0.0925 178  PRO A C   
1186  O O   . PRO A 180  ? 0.2785 0.4157 0.2900 0.0275  -0.0096 -0.0917 178  PRO A O   
1187  C CB  . PRO A 180  ? 0.2889 0.4531 0.3024 0.0337  -0.0105 -0.1069 178  PRO A CB  
1188  C CG  . PRO A 180  ? 0.2707 0.4507 0.2807 0.0348  -0.0091 -0.1087 178  PRO A CG  
1189  C CD  . PRO A 180  ? 0.2871 0.4659 0.2921 0.0318  -0.0061 -0.0996 178  PRO A CD  
1190  N N   . VAL A 181  ? 0.2436 0.3794 0.2547 0.0276  -0.0075 -0.0895 179  VAL A N   
1191  C CA  . VAL A 181  ? 0.2256 0.3462 0.2387 0.0260  -0.0077 -0.0851 179  VAL A CA  
1192  C C   . VAL A 181  ? 0.2733 0.3904 0.2815 0.0228  -0.0058 -0.0768 179  VAL A C   
1193  O O   . VAL A 181  ? 0.2590 0.3662 0.2685 0.0216  -0.0063 -0.0740 179  VAL A O   
1194  C CB  . VAL A 181  ? 0.2263 0.3402 0.2418 0.0265  -0.0074 -0.0846 179  VAL A CB  
1195  C CG1 . VAL A 181  ? 0.2407 0.3574 0.2513 0.0246  -0.0048 -0.0787 179  VAL A CG1 
1196  C CG2 . VAL A 181  ? 0.2907 0.3897 0.3097 0.0257  -0.0083 -0.0821 179  VAL A CG2 
1197  N N   . ILE A 182  ? 0.2587 0.3842 0.2616 0.0214  -0.0038 -0.0726 180  ILE A N   
1198  C CA  . ILE A 182  ? 0.2799 0.4027 0.2787 0.0184  -0.0022 -0.0648 180  ILE A CA  
1199  C C   . ILE A 182  ? 0.3099 0.4345 0.3084 0.0182  -0.0033 -0.0656 180  ILE A C   
1200  O O   . ILE A 182  ? 0.2808 0.3971 0.2790 0.0165  -0.0032 -0.0612 180  ILE A O   
1201  C CB  . ILE A 182  ? 0.2624 0.3946 0.2565 0.0169  -0.0001 -0.0603 180  ILE A CB  
1202  C CG1 . ILE A 182  ? 0.2577 0.3878 0.2523 0.0170  0.0009  -0.0594 180  ILE A CG1 
1203  C CG2 . ILE A 182  ? 0.2743 0.4031 0.2647 0.0139  0.0012  -0.0523 180  ILE A CG2 
1204  C CD1 . ILE A 182  ? 0.3261 0.4680 0.3172 0.0162  0.0027  -0.0569 180  ILE A CD1 
1205  N N   . ARG A 183  ? 0.2830 0.4189 0.2816 0.0201  -0.0043 -0.0713 181  ARG A N   
1206  C CA  . ARG A 183  ? 0.3143 0.4530 0.3129 0.0202  -0.0056 -0.0729 181  ARG A CA  
1207  C C   . ARG A 183  ? 0.3463 0.4728 0.3498 0.0206  -0.0075 -0.0749 181  ARG A C   
1208  O O   . ARG A 183  ? 0.3344 0.4562 0.3374 0.0191  -0.0077 -0.0716 181  ARG A O   
1209  C CB  . ARG A 183  ? 0.3553 0.5084 0.3539 0.0227  -0.0067 -0.0800 181  ARG A CB  
1210  C CG  . ARG A 183  ? 0.4447 0.6015 0.4442 0.0236  -0.0086 -0.0837 181  ARG A CG  
1211  C CD  . ARG A 183  ? 0.4834 0.6380 0.4794 0.0209  -0.0077 -0.0766 181  ARG A CD  
1212  N NE  . ARG A 183  ? 0.4971 0.6594 0.4875 0.0190  -0.0054 -0.0701 181  ARG A NE  
1213  C CZ  . ARG A 183  ? 0.5595 0.7182 0.5468 0.0163  -0.0041 -0.0623 181  ARG A CZ  
1214  N NH1 . ARG A 183  ? 0.5040 0.6515 0.4929 0.0152  -0.0048 -0.0598 181  ARG A NH1 
1215  N NH2 . ARG A 183  ? 0.5455 0.7121 0.5283 0.0147  -0.0023 -0.0566 181  ARG A NH2 
1216  N N   . ARG A 184  ? 0.2719 0.3934 0.2805 0.0225  -0.0090 -0.0801 182  ARG A N   
1217  C CA  . ARG A 184  ? 0.3071 0.4174 0.3211 0.0228  -0.0109 -0.0818 182  ARG A CA  
1218  C C   . ARG A 184  ? 0.2764 0.3744 0.2895 0.0203  -0.0096 -0.0742 182  ARG A C   
1219  O O   . ARG A 184  ? 0.3154 0.4062 0.3305 0.0195  -0.0104 -0.0728 182  ARG A O   
1220  C CB  . ARG A 184  ? 0.3322 0.4399 0.3523 0.0254  -0.0128 -0.0885 182  ARG A CB  
1221  C CG  . ARG A 184  ? 0.4131 0.5304 0.4362 0.0282  -0.0151 -0.0975 182  ARG A CG  
1222  C CD  . ARG A 184  ? 0.3848 0.4964 0.4135 0.0288  -0.0178 -0.1011 182  ARG A CD  
1223  N NE  . ARG A 184  ? 0.4498 0.5519 0.4859 0.0301  -0.0198 -0.1044 182  ARG A NE  
1224  C CZ  . ARG A 184  ? 0.4301 0.5196 0.4698 0.0288  -0.0204 -0.1010 182  ARG A CZ  
1225  N NH1 . ARG A 184  ? 0.4457 0.5303 0.4825 0.0262  -0.0192 -0.0947 182  ARG A NH1 
1226  N NH2 . ARG A 184  ? 0.4121 0.4942 0.4588 0.0301  -0.0223 -0.1040 182  ARG A NH2 
1227  N N   . GLY A 185  ? 0.2763 0.3720 0.2865 0.0191  -0.0075 -0.0694 183  GLY A N   
1228  C CA  . GLY A 185  ? 0.2667 0.3518 0.2756 0.0168  -0.0062 -0.0624 183  GLY A CA  
1229  C C   . GLY A 185  ? 0.3218 0.4078 0.3269 0.0147  -0.0053 -0.0572 183  GLY A C   
1230  O O   . GLY A 185  ? 0.3084 0.3858 0.3144 0.0135  -0.0053 -0.0539 183  GLY A O   
1231  N N   . VAL A 186  ? 0.2947 0.3915 0.2957 0.0143  -0.0044 -0.0563 184  VAL A N   
1232  C CA  . VAL A 186  ? 0.3254 0.4238 0.3229 0.0124  -0.0036 -0.0513 184  VAL A CA  
1233  C C   . VAL A 186  ? 0.2919 0.3886 0.2920 0.0129  -0.0054 -0.0540 184  VAL A C   
1234  O O   . VAL A 186  ? 0.3016 0.3922 0.3013 0.0114  -0.0052 -0.0498 184  VAL A O   
1235  C CB  . VAL A 186  ? 0.3384 0.4500 0.3315 0.0120  -0.0026 -0.0500 184  VAL A CB  
1236  C CG1 . VAL A 186  ? 0.3366 0.4514 0.3269 0.0105  -0.0025 -0.0460 184  VAL A CG1 
1237  C CG2 . VAL A 186  ? 0.3235 0.4352 0.3140 0.0108  -0.0006 -0.0453 184  VAL A CG2 
1238  N N   . ASP A 187  ? 0.3276 0.4299 0.3306 0.0151  -0.0073 -0.0613 185  ASP A N   
1239  C CA  . ASP A 187  ? 0.3313 0.4326 0.3372 0.0157  -0.0093 -0.0644 185  ASP A CA  
1240  C C   . ASP A 187  ? 0.3826 0.4705 0.3931 0.0152  -0.0101 -0.0633 185  ASP A C   
1241  O O   . ASP A 187  ? 0.3393 0.4231 0.3508 0.0143  -0.0107 -0.0617 185  ASP A O   
1242  C CB  . ASP A 187  ? 0.3955 0.5056 0.4042 0.0184  -0.0114 -0.0730 185  ASP A CB  
1243  C CG  . ASP A 187  ? 0.4037 0.5286 0.4077 0.0189  -0.0107 -0.0740 185  ASP A CG  
1244  O OD1 . ASP A 187  ? 0.4600 0.5882 0.4591 0.0169  -0.0090 -0.0677 185  ASP A OD1 
1245  O OD2 . ASP A 187  ? 0.4133 0.5469 0.4190 0.0213  -0.0120 -0.0811 185  ASP A OD2 
1246  N N   . MET A 188  ? 0.3256 0.4067 0.3388 0.0157  -0.0100 -0.0640 186  MET A N   
1247  C CA  . MET A 188  ? 0.3191 0.3879 0.3365 0.0152  -0.0106 -0.0624 186  MET A CA  
1248  C C   . MET A 188  ? 0.3714 0.4336 0.3856 0.0127  -0.0087 -0.0545 186  MET A C   
1249  O O   . MET A 188  ? 0.3562 0.4120 0.3724 0.0119  -0.0092 -0.0527 186  MET A O   
1250  C CB  . MET A 188  ? 0.3749 0.4390 0.3955 0.0164  -0.0109 -0.0644 186  MET A CB  
1251  C CG  . MET A 188  ? 0.4314 0.4836 0.4568 0.0159  -0.0116 -0.0628 186  MET A CG  
1252  S SD  . MET A 188  ? 0.5519 0.6022 0.5845 0.0171  -0.0148 -0.0683 186  MET A SD  
1253  C CE  . MET A 188  ? 0.4319 0.4917 0.4673 0.0201  -0.0168 -0.0775 186  MET A CE  
1254  N N   . ALA A 189  ? 0.3214 0.3850 0.3308 0.0116  -0.0066 -0.0500 187  ALA A N   
1255  C CA  . ALA A 189  ? 0.3112 0.3687 0.3178 0.0095  -0.0049 -0.0429 187  ALA A CA  
1256  C C   . ALA A 189  ? 0.3559 0.4163 0.3605 0.0084  -0.0050 -0.0407 187  ALA A C   
1257  O O   . ALA A 189  ? 0.3040 0.3578 0.3088 0.0071  -0.0045 -0.0366 187  ALA A O   
1258  C CB  . ALA A 189  ? 0.3195 0.3786 0.3220 0.0086  -0.0029 -0.0390 187  ALA A CB  
1259  N N   . MET A 190  ? 0.3078 0.3788 0.3107 0.0090  -0.0055 -0.0433 188  MET A N   
1260  C CA  . MET A 190  ? 0.3196 0.3942 0.3208 0.0081  -0.0057 -0.0413 188  MET A CA  
1261  C C   . MET A 190  ? 0.3472 0.4163 0.3528 0.0084  -0.0074 -0.0436 188  MET A C   
1262  O O   . MET A 190  ? 0.3737 0.4390 0.3788 0.0071  -0.0071 -0.0396 188  MET A O   
1263  C CB  . MET A 190  ? 0.3326 0.4204 0.3313 0.0090  -0.0062 -0.0443 188  MET A CB  
1264  C CG  . MET A 190  ? 0.4462 0.5390 0.4422 0.0079  -0.0062 -0.0412 188  MET A CG  
1265  S SD  . MET A 190  ? 0.5297 0.6391 0.5229 0.0091  -0.0069 -0.0450 188  MET A SD  
1266  C CE  . MET A 190  ? 0.4761 0.5912 0.4662 0.0090  -0.0050 -0.0433 188  MET A CE  
1267  N N   . ARG A 191  ? 0.3259 0.3945 0.3361 0.0102  -0.0093 -0.0498 189  ARG A N   
1268  C CA  . ARG A 191  ? 0.3316 0.3947 0.3469 0.0104  -0.0111 -0.0520 189  ARG A CA  
1269  C C   . ARG A 191  ? 0.3649 0.4163 0.3819 0.0091  -0.0102 -0.0473 189  ARG A C   
1270  O O   . ARG A 191  ? 0.3821 0.4293 0.4006 0.0082  -0.0105 -0.0451 189  ARG A O   
1271  C CB  . ARG A 191  ? 0.3219 0.3866 0.3427 0.0126  -0.0134 -0.0597 189  ARG A CB  
1272  N N   . MET A 192  ? 0.3283 0.3747 0.3453 0.0091  -0.0092 -0.0457 190  MET A N   
1273  C CA  . MET A 192  ? 0.2826 0.3186 0.3015 0.0081  -0.0085 -0.0416 190  MET A CA  
1274  C C   . MET A 192  ? 0.3482 0.3818 0.3631 0.0063  -0.0067 -0.0352 190  MET A C   
1275  O O   . MET A 192  ? 0.3140 0.3416 0.3308 0.0054  -0.0067 -0.0326 190  MET A O   
1276  C CB  . MET A 192  ? 0.3170 0.3490 0.3364 0.0086  -0.0078 -0.0414 190  MET A CB  
1277  C CG  . MET A 192  ? 0.3051 0.3374 0.3298 0.0105  -0.0098 -0.0476 190  MET A CG  
1278  S SD  . MET A 192  ? 0.4945 0.5215 0.5200 0.0110  -0.0091 -0.0466 190  MET A SD  
1279  C CE  . MET A 192  ? 0.4733 0.4890 0.5024 0.0099  -0.0090 -0.0423 190  MET A CE  
1280  N N   . MET A 193  ? 0.3202 0.3586 0.3300 0.0056  -0.0052 -0.0324 191  MET A N   
1281  C CA  A MET A 193  ? 0.3490 0.3849 0.3554 0.0040  -0.0037 -0.0263 191  MET A CA  
1282  C CA  B MET A 193  ? 0.3490 0.3847 0.3554 0.0040  -0.0037 -0.0263 191  MET A CA  
1283  C C   . MET A 193  ? 0.3330 0.3727 0.3387 0.0034  -0.0042 -0.0255 191  MET A C   
1284  O O   . MET A 193  ? 0.3611 0.3972 0.3655 0.0021  -0.0034 -0.0208 191  MET A O   
1285  C CB  A MET A 193  ? 0.3409 0.3800 0.3428 0.0033  -0.0021 -0.0234 191  MET A CB  
1286  C CB  B MET A 193  ? 0.3410 0.3797 0.3430 0.0033  -0.0020 -0.0233 191  MET A CB  
1287  C CG  A MET A 193  ? 0.3136 0.3501 0.3159 0.0040  -0.0016 -0.0245 191  MET A CG  
1288  C CG  B MET A 193  ? 0.3010 0.3344 0.3034 0.0036  -0.0012 -0.0228 191  MET A CG  
1289  S SD  A MET A 193  ? 0.3501 0.3916 0.3476 0.0031  0.0001  -0.0212 191  MET A SD  
1290  S SD  B MET A 193  ? 0.3643 0.3997 0.3619 0.0024  0.0007  -0.0182 191  MET A SD  
1291  C CE  A MET A 193  ? 0.4226 0.4559 0.4185 0.0014  0.0015  -0.0146 191  MET A CE  
1292  C CE  B MET A 193  ? 0.3674 0.4151 0.3631 0.0031  0.0003  -0.0215 191  MET A CE  
1293  N N   . GLY A 194  ? 0.3508 0.3977 0.3574 0.0043  -0.0057 -0.0299 192  GLY A N   
1294  C CA  . GLY A 194  ? 0.3251 0.3764 0.3309 0.0038  -0.0064 -0.0292 192  GLY A CA  
1295  C C   . GLY A 194  ? 0.4076 0.4558 0.4183 0.0042  -0.0081 -0.0321 192  GLY A C   
1296  O O   . GLY A 194  ? 0.3990 0.4477 0.4095 0.0035  -0.0085 -0.0301 192  GLY A O   
1297  N N   . GLU A 195  ? 0.3090 0.3539 0.3242 0.0054  -0.0094 -0.0365 193  GLU A N   
1298  C CA  . GLU A 195  ? 0.3561 0.3988 0.3768 0.0058  -0.0114 -0.0398 193  GLU A CA  
1299  C C   . GLU A 195  ? 0.3144 0.3474 0.3402 0.0057  -0.0117 -0.0396 193  GLU A C   
1300  O O   . GLU A 195  ? 0.2958 0.3258 0.3263 0.0055  -0.0131 -0.0407 193  GLU A O   
1301  C CB  . GLU A 195  ? 0.3468 0.3971 0.3697 0.0075  -0.0136 -0.0470 193  GLU A CB  
1302  C CG  . GLU A 195  ? 0.5572 0.6186 0.5753 0.0078  -0.0135 -0.0477 193  GLU A CG  
1303  C CD  . GLU A 195  ? 0.5497 0.6194 0.5696 0.0098  -0.0156 -0.0553 193  GLU A CD  
1304  O OE1 . GLU A 195  ? 0.6055 0.6730 0.6295 0.0111  -0.0166 -0.0597 193  GLU A OE1 
1305  O OE2 . GLU A 195  ? 0.6874 0.7662 0.7051 0.0101  -0.0163 -0.0568 193  GLU A OE2 
1306  N N   . GLN A 196  ? 0.3363 0.3648 0.3615 0.0057  -0.0105 -0.0379 194  GLN A N   
1307  C CA  . GLN A 196  ? 0.3240 0.3442 0.3542 0.0058  -0.0109 -0.0376 194  GLN A CA  
1308  C C   . GLN A 196  ? 0.3607 0.3739 0.3890 0.0044  -0.0089 -0.0313 194  GLN A C   
1309  O O   . GLN A 196  ? 0.4251 0.4328 0.4570 0.0038  -0.0091 -0.0294 194  GLN A O   
1310  C CB  . GLN A 196  ? 0.4016 0.4219 0.4334 0.0071  -0.0115 -0.0413 194  GLN A CB  
1311  C CG  . GLN A 196  ? 0.5593 0.5714 0.5965 0.0072  -0.0121 -0.0408 194  GLN A CG  
1312  C CD  . GLN A 196  ? 0.5341 0.5466 0.5734 0.0087  -0.0129 -0.0446 194  GLN A CD  
1313  O OE1 . GLN A 196  ? 0.5541 0.5734 0.5928 0.0100  -0.0138 -0.0494 194  GLN A OE1 
1314  N NE2 . GLN A 196  ? 0.6318 0.6374 0.6736 0.0087  -0.0126 -0.0425 194  GLN A NE2 
1315  N N   . PHE A 197  ? 0.3329 0.3466 0.3560 0.0040  -0.0069 -0.0280 195  PHE A N   
1316  C CA  . PHE A 197  ? 0.3324 0.3401 0.3535 0.0029  -0.0050 -0.0224 195  PHE A CA  
1317  C C   . PHE A 197  ? 0.3062 0.3145 0.3255 0.0018  -0.0045 -0.0191 195  PHE A C   
1318  O O   . PHE A 197  ? 0.3294 0.3325 0.3486 0.0011  -0.0033 -0.0151 195  PHE A O   
1319  C CB  . PHE A 197  ? 0.3222 0.3305 0.3388 0.0028  -0.0034 -0.0203 195  PHE A CB  
1320  C CG  . PHE A 197  ? 0.4539 0.4614 0.4719 0.0039  -0.0038 -0.0230 195  PHE A CG  
1321  C CD1 . PHE A 197  ? 0.4360 0.4383 0.4591 0.0044  -0.0048 -0.0243 195  PHE A CD1 
1322  C CD2 . PHE A 197  ? 0.4316 0.4439 0.4463 0.0043  -0.0032 -0.0241 195  PHE A CD2 
1323  C CE1 . PHE A 197  ? 0.4989 0.5004 0.5237 0.0055  -0.0053 -0.0268 195  PHE A CE1 
1324  C CE2 . PHE A 197  ? 0.4605 0.4722 0.4767 0.0054  -0.0036 -0.0267 195  PHE A CE2 
1325  C CZ  . PHE A 197  ? 0.4134 0.4196 0.4347 0.0060  -0.0047 -0.0281 195  PHE A CZ  
1326  N N   . VAL A 198  ? 0.3096 0.3245 0.3276 0.0019  -0.0052 -0.0208 196  VAL A N   
1327  C CA  . VAL A 198  ? 0.2883 0.3043 0.3053 0.0010  -0.0051 -0.0182 196  VAL A CA  
1328  C C   . VAL A 198  ? 0.2815 0.3023 0.3016 0.0016  -0.0072 -0.0225 196  VAL A C   
1329  O O   . VAL A 198  ? 0.3126 0.3379 0.3337 0.0026  -0.0085 -0.0273 196  VAL A O   
1330  C CB  . VAL A 198  ? 0.2877 0.3076 0.2992 0.0003  -0.0038 -0.0147 196  VAL A CB  
1331  C CG1 . VAL A 198  ? 0.2802 0.2952 0.2893 -0.0002 -0.0020 -0.0108 196  VAL A CG1 
1332  C CG2 . VAL A 198  ? 0.2788 0.3073 0.2878 0.0009  -0.0044 -0.0176 196  VAL A CG2 
1333  N N   . THR A 199  ? 0.2416 0.2614 0.2632 0.0009  -0.0076 -0.0210 197  THR A N   
1334  C CA  . THR A 199  ? 0.2576 0.2827 0.2814 0.0013  -0.0096 -0.0247 197  THR A CA  
1335  C C   . THR A 199  ? 0.3018 0.3355 0.3208 0.0014  -0.0096 -0.0247 197  THR A C   
1336  O O   . THR A 199  ? 0.3274 0.3679 0.3471 0.0023  -0.0112 -0.0292 197  THR A O   
1337  C CB  . THR A 199  ? 0.3032 0.3249 0.3303 0.0005  -0.0100 -0.0228 197  THR A CB  
1338  O OG1 . THR A 199  ? 0.3041 0.3183 0.3356 0.0003  -0.0099 -0.0221 197  THR A OG1 
1339  C CG2 . THR A 199  ? 0.3148 0.3417 0.3449 0.0010  -0.0124 -0.0271 197  THR A CG2 
1340  N N   . GLY A 200  ? 0.2892 0.3230 0.3036 0.0006  -0.0078 -0.0199 198  GLY A N   
1341  C CA  . GLY A 200  ? 0.2843 0.3262 0.2942 0.0005  -0.0076 -0.0191 198  GLY A CA  
1342  C C   . GLY A 200  ? 0.3342 0.3742 0.3401 -0.0004 -0.0057 -0.0136 198  GLY A C   
1343  O O   . GLY A 200  ? 0.2912 0.3237 0.2976 -0.0010 -0.0045 -0.0104 198  GLY A O   
1344  N N   . GLU A 201  ? 0.3168 0.3641 0.3189 -0.0005 -0.0054 -0.0127 199  GLU A N   
1345  C CA  . GLU A 201  ? 0.3230 0.3691 0.3216 -0.0016 -0.0037 -0.0074 199  GLU A CA  
1346  C C   . GLU A 201  ? 0.2788 0.3226 0.2770 -0.0026 -0.0035 -0.0026 199  GLU A C   
1347  O O   . GLU A 201  ? 0.3316 0.3703 0.3289 -0.0033 -0.0022 0.0015  199  GLU A O   
1348  C CB  . GLU A 201  ? 0.2953 0.3505 0.2904 -0.0015 -0.0036 -0.0075 199  GLU A CB  
1349  C CG  . GLU A 201  ? 0.4172 0.4721 0.4093 -0.0028 -0.0022 -0.0019 199  GLU A CG  
1350  C CD  . GLU A 201  ? 0.6195 0.6844 0.6085 -0.0029 -0.0021 -0.0014 199  GLU A CD  
1351  O OE1 . GLU A 201  ? 0.6119 0.6837 0.6008 -0.0018 -0.0030 -0.0061 199  GLU A OE1 
1352  O OE2 . GLU A 201  ? 0.7186 0.7847 0.7056 -0.0041 -0.0013 0.0036  199  GLU A OE2 
1353  N N   . THR A 202  ? 0.2894 0.3371 0.2886 -0.0025 -0.0047 -0.0033 200  THR A N   
1354  C CA  . THR A 202  ? 0.2732 0.3194 0.2724 -0.0033 -0.0047 0.0008  200  THR A CA  
1355  C C   . THR A 202  ? 0.2579 0.3016 0.2609 -0.0029 -0.0058 -0.0016 200  THR A C   
1356  O O   . THR A 202  ? 0.2731 0.3183 0.2785 -0.0021 -0.0069 -0.0065 200  THR A O   
1357  C CB  . THR A 202  ? 0.2959 0.3508 0.2925 -0.0037 -0.0053 0.0031  200  THR A CB  
1358  O OG1 . THR A 202  ? 0.3346 0.3967 0.3317 -0.0028 -0.0069 -0.0014 200  THR A OG1 
1359  C CG2 . THR A 202  ? 0.3479 0.4066 0.3410 -0.0042 -0.0043 0.0052  200  THR A CG2 
1360  N N   . ILE A 203  ? 0.2363 0.2766 0.2404 -0.0034 -0.0057 0.0019  201  ILE A N   
1361  C CA  . ILE A 203  ? 0.2475 0.2853 0.2554 -0.0032 -0.0066 0.0001  201  ILE A CA  
1362  C C   . ILE A 203  ? 0.2497 0.2953 0.2582 -0.0027 -0.0085 -0.0033 201  ILE A C   
1363  O O   . ILE A 203  ? 0.2632 0.3083 0.2753 -0.0022 -0.0098 -0.0073 201  ILE A O   
1364  C CB  . ILE A 203  ? 0.2557 0.2887 0.2645 -0.0038 -0.0059 0.0046  201  ILE A CB  
1365  C CG1 . ILE A 203  ? 0.2216 0.2515 0.2348 -0.0037 -0.0067 0.0029  201  ILE A CG1 
1366  C CG2 . ILE A 203  ? 0.2926 0.3306 0.2990 -0.0043 -0.0063 0.0082  201  ILE A CG2 
1367  C CD1 . ILE A 203  ? 0.2258 0.2505 0.2421 -0.0033 -0.0065 0.0000  201  ILE A CD1 
1368  N N   . ARG A 204  ? 0.2873 0.3407 0.2925 -0.0029 -0.0090 -0.0020 202  ARG A N   
1369  C CA  . ARG A 204  ? 0.2795 0.3415 0.2849 -0.0022 -0.0108 -0.0055 202  ARG A CA  
1370  C C   . ARG A 204  ? 0.2857 0.3505 0.2922 -0.0012 -0.0117 -0.0118 202  ARG A C   
1371  O O   . ARG A 204  ? 0.2736 0.3409 0.2831 -0.0005 -0.0134 -0.0164 202  ARG A O   
1372  C CB  . ARG A 204  ? 0.3481 0.4185 0.3494 -0.0026 -0.0109 -0.0023 202  ARG A CB  
1373  C CG  . ARG A 204  ? 0.4680 0.5386 0.4696 -0.0032 -0.0114 0.0019  202  ARG A CG  
1374  C CD  . ARG A 204  ? 0.4600 0.5359 0.4578 -0.0040 -0.0109 0.0071  202  ARG A CD  
1375  N NE  . ARG A 204  ? 0.4437 0.5186 0.4425 -0.0045 -0.0114 0.0115  202  ARG A NE  
1376  C CZ  . ARG A 204  ? 0.4898 0.5562 0.4902 -0.0050 -0.0105 0.0149  202  ARG A CZ  
1377  N NH1 . ARG A 204  ? 0.3404 0.3990 0.3416 -0.0051 -0.0090 0.0148  202  ARG A NH1 
1378  N NH2 . ARG A 204  ? 0.3939 0.4603 0.3955 -0.0053 -0.0111 0.0183  202  ARG A NH2 
1379  N N   . GLU A 205  ? 0.2939 0.3585 0.2983 -0.0010 -0.0106 -0.0121 203  GLU A N   
1380  C CA  . GLU A 205  ? 0.2889 0.3557 0.2948 0.0002  -0.0114 -0.0182 203  GLU A CA  
1381  C C   . GLU A 205  ? 0.2923 0.3511 0.3035 0.0005  -0.0120 -0.0211 203  GLU A C   
1382  O O   . GLU A 205  ? 0.2926 0.3535 0.3071 0.0014  -0.0137 -0.0267 203  GLU A O   
1383  C CB  . GLU A 205  ? 0.3145 0.3819 0.3173 0.0002  -0.0099 -0.0174 203  GLU A CB  
1384  C CG  . GLU A 205  ? 0.3990 0.4703 0.4027 0.0016  -0.0108 -0.0235 203  GLU A CG  
1385  C CD  . GLU A 205  ? 0.5302 0.6032 0.5306 0.0015  -0.0092 -0.0222 203  GLU A CD  
1386  O OE1 . GLU A 205  ? 0.4144 0.4795 0.4154 0.0011  -0.0080 -0.0204 203  GLU A OE1 
1387  O OE2 . GLU A 205  ? 0.5738 0.6564 0.5711 0.0019  -0.0093 -0.0229 203  GLU A OE2 
1388  N N   . ALA A 206  ? 0.2610 0.3108 0.2733 -0.0003 -0.0106 -0.0173 204  ALA A N   
1389  C CA  . ALA A 206  ? 0.2910 0.3335 0.3084 -0.0002 -0.0110 -0.0192 204  ALA A CA  
1390  C C   . ALA A 206  ? 0.2522 0.2957 0.2737 -0.0002 -0.0129 -0.0215 204  ALA A C   
1391  O O   . ALA A 206  ? 0.2901 0.3321 0.3164 0.0004  -0.0144 -0.0259 204  ALA A O   
1392  C CB  . ALA A 206  ? 0.2677 0.3016 0.2850 -0.0011 -0.0091 -0.0143 204  ALA A CB  
1393  N N   . LEU A 207  ? 0.2566 0.3028 0.2766 -0.0007 -0.0130 -0.0186 205  LEU A N   
1394  C CA  . LEU A 207  ? 0.2463 0.2941 0.2702 -0.0007 -0.0148 -0.0205 205  LEU A CA  
1395  C C   . LEU A 207  ? 0.3149 0.3704 0.3400 0.0004  -0.0171 -0.0268 205  LEU A C   
1396  O O   . LEU A 207  ? 0.3434 0.3983 0.3737 0.0007  -0.0190 -0.0307 205  LEU A O   
1397  C CB  . LEU A 207  ? 0.2723 0.3221 0.2940 -0.0014 -0.0145 -0.0159 205  LEU A CB  
1398  C CG  . LEU A 207  ? 0.2721 0.3142 0.2941 -0.0023 -0.0126 -0.0106 205  LEU A CG  
1399  C CD1 . LEU A 207  ? 0.2607 0.3055 0.2798 -0.0028 -0.0122 -0.0059 205  LEU A CD1 
1400  C CD2 . LEU A 207  ? 0.2317 0.2680 0.2595 -0.0025 -0.0132 -0.0116 205  LEU A CD2 
1401  N N   . LYS A 208  ? 0.2942 0.3574 0.3148 0.0010  -0.0171 -0.0278 206  LYS A N   
1402  C CA  . LYS A 208  ? 0.3191 0.3906 0.3406 0.0023  -0.0192 -0.0343 206  LYS A CA  
1403  C C   . LYS A 208  ? 0.3140 0.3817 0.3404 0.0032  -0.0203 -0.0398 206  LYS A C   
1404  O O   . LYS A 208  ? 0.3694 0.4397 0.4001 0.0040  -0.0227 -0.0454 206  LYS A O   
1405  C CB  . LYS A 208  ? 0.3150 0.3956 0.3306 0.0028  -0.0186 -0.0339 206  LYS A CB  
1406  N N   . ARG A 209  ? 0.3026 0.3639 0.3289 0.0030  -0.0187 -0.0383 207  ARG A N   
1407  C CA  . ARG A 209  ? 0.3372 0.3948 0.3681 0.0039  -0.0197 -0.0430 207  ARG A CA  
1408  C C   . ARG A 209  ? 0.3675 0.4166 0.4050 0.0033  -0.0205 -0.0430 207  ARG A C   
1409  O O   . ARG A 209  ? 0.3755 0.4211 0.4180 0.0039  -0.0217 -0.0468 207  ARG A O   
1410  C CB  . ARG A 209  ? 0.3441 0.3986 0.3720 0.0039  -0.0177 -0.0412 207  ARG A CB  
1411  C CG  . ARG A 209  ? 0.3999 0.4636 0.4225 0.0047  -0.0173 -0.0423 207  ARG A CG  
1412  C CD  . ARG A 209  ? 0.3781 0.4388 0.3970 0.0043  -0.0150 -0.0388 207  ARG A CD  
1413  N NE  . ARG A 209  ? 0.4936 0.5633 0.5080 0.0050  -0.0146 -0.0401 207  ARG A NE  
1414  C CZ  . ARG A 209  ? 0.5326 0.6017 0.5438 0.0049  -0.0129 -0.0380 207  ARG A CZ  
1415  N NH1 . ARG A 209  ? 0.4464 0.5065 0.4582 0.0042  -0.0114 -0.0347 207  ARG A NH1 
1416  N NH2 . ARG A 209  ? 0.5654 0.6438 0.5728 0.0055  -0.0126 -0.0392 207  ARG A NH2 
1417  N N   . SER A 210  ? 0.3279 0.3739 0.3660 0.0021  -0.0200 -0.0387 208  SER A N   
1418  C CA  . SER A 210  ? 0.3091 0.3476 0.3535 0.0013  -0.0205 -0.0380 208  SER A CA  
1419  C C   . SER A 210  ? 0.3482 0.3895 0.3984 0.0016  -0.0234 -0.0427 208  SER A C   
1420  O O   . SER A 210  ? 0.3106 0.3463 0.3674 0.0011  -0.0244 -0.0434 208  SER A O   
1421  C CB  . SER A 210  ? 0.3068 0.3407 0.3493 0.0000  -0.0184 -0.0313 208  SER A CB  
1422  O OG  . SER A 210  ? 0.3068 0.3377 0.3447 -0.0003 -0.0160 -0.0273 208  SER A OG  
1423  N N   . LYS A 211  ? 0.3459 0.3959 0.3939 0.0024  -0.0249 -0.0459 209  LYS A N   
1424  C CA  . LYS A 211  ? 0.3795 0.4328 0.4328 0.0026  -0.0277 -0.0501 209  LYS A CA  
1425  C C   . LYS A 211  ? 0.3362 0.3873 0.3968 0.0034  -0.0302 -0.0564 209  LYS A C   
1426  O O   . LYS A 211  ? 0.3431 0.3914 0.4107 0.0030  -0.0321 -0.0581 209  LYS A O   
1427  C CB  . LYS A 211  ? 0.4320 0.4961 0.4808 0.0035  -0.0287 -0.0524 209  LYS A CB  
1428  C CG  . LYS A 211  ? 0.4626 0.5296 0.5035 0.0029  -0.0262 -0.0465 209  LYS A CG  
1429  C CD  . LYS A 211  ? 0.5307 0.6068 0.5685 0.0032  -0.0272 -0.0465 209  LYS A CD  
1430  C CE  . LYS A 211  ? 0.6199 0.6925 0.6596 0.0019  -0.0271 -0.0422 209  LYS A CE  
1431  N NZ  . LYS A 211  ? 0.6337 0.6979 0.6719 0.0007  -0.0243 -0.0355 209  LYS A NZ  
1432  N N   . GLU A 212  ? 0.3569 0.4092 0.4166 0.0047  -0.0303 -0.0599 210  GLU A N   
1433  C CA  . GLU A 212  ? 0.4132 0.4641 0.4802 0.0057  -0.0329 -0.0664 210  GLU A CA  
1434  C C   . GLU A 212  ? 0.3747 0.4155 0.4492 0.0045  -0.0332 -0.0643 210  GLU A C   
1435  O O   . GLU A 212  ? 0.3906 0.4301 0.4729 0.0045  -0.0360 -0.0681 210  GLU A O   
1436  C CB  . GLU A 212  ? 0.4390 0.4921 0.5034 0.0072  -0.0325 -0.0694 210  GLU A CB  
1437  C CG  . GLU A 212  ? 0.5161 0.5674 0.5882 0.0085  -0.0352 -0.0762 210  GLU A CG  
1438  C CD  . GLU A 212  ? 0.6467 0.7007 0.7159 0.0100  -0.0347 -0.0791 210  GLU A CD  
1439  O OE1 . GLU A 212  ? 0.7089 0.7676 0.7701 0.0101  -0.0324 -0.0763 210  GLU A OE1 
1440  O OE2 . GLU A 212  ? 0.7684 0.8197 0.8438 0.0111  -0.0367 -0.0840 210  GLU A OE2 
1441  N N   . LEU A 213  ? 0.3614 0.3953 0.4337 0.0034  -0.0305 -0.0581 211  LEU A N   
1442  C CA  . LEU A 213  ? 0.3822 0.4071 0.4613 0.0023  -0.0306 -0.0556 211  LEU A CA  
1443  C C   . LEU A 213  ? 0.3318 0.3546 0.4132 0.0007  -0.0303 -0.0515 211  LEU A C   
1444  O O   . LEU A 213  ? 0.3312 0.3488 0.4201 -0.0002 -0.0315 -0.0510 211  LEU A O   
1445  C CB  . LEU A 213  ? 0.3165 0.3355 0.3927 0.0019  -0.0279 -0.0509 211  LEU A CB  
1446  C CG  . LEU A 213  ? 0.3254 0.3449 0.4019 0.0034  -0.0286 -0.0551 211  LEU A CG  
1447  C CD1 . LEU A 213  ? 0.3846 0.3979 0.4589 0.0029  -0.0261 -0.0503 211  LEU A CD1 
1448  C CD2 . LEU A 213  ? 0.3561 0.3745 0.4419 0.0042  -0.0321 -0.0613 211  LEU A CD2 
1449  N N   . GLU A 214  ? 0.3122 0.3391 0.3875 0.0003  -0.0289 -0.0485 212  GLU A N   
1450  C CA  . GLU A 214  ? 0.2920 0.3178 0.3700 -0.0009 -0.0291 -0.0455 212  GLU A CA  
1451  C C   . GLU A 214  ? 0.3424 0.3709 0.4277 -0.0007 -0.0327 -0.0512 212  GLU A C   
1452  O O   . GLU A 214  ? 0.3682 0.3931 0.4598 -0.0018 -0.0335 -0.0498 212  GLU A O   
1453  C CB  . GLU A 214  ? 0.2874 0.3176 0.3579 -0.0011 -0.0273 -0.0418 212  GLU A CB  
1454  C CG  . GLU A 214  ? 0.3128 0.3389 0.3778 -0.0017 -0.0239 -0.0354 212  GLU A CG  
1455  C CD  . GLU A 214  ? 0.3425 0.3722 0.4015 -0.0020 -0.0225 -0.0314 212  GLU A CD  
1456  O OE1 . GLU A 214  ? 0.3284 0.3653 0.3855 -0.0015 -0.0239 -0.0340 212  GLU A OE1 
1457  O OE2 . GLU A 214  ? 0.3412 0.3667 0.3974 -0.0028 -0.0200 -0.0259 212  GLU A OE2 
1458  N N   . GLU A 215  ? 0.3316 0.3669 0.4164 0.0008  -0.0348 -0.0577 213  GLU A N   
1459  C CA  . GLU A 215  ? 0.3842 0.4225 0.4763 0.0013  -0.0385 -0.0639 213  GLU A CA  
1460  C C   . GLU A 215  ? 0.4482 0.4797 0.5501 0.0010  -0.0405 -0.0662 213  GLU A C   
1461  O O   . GLU A 215  ? 0.4739 0.5050 0.5836 0.0006  -0.0433 -0.0693 213  GLU A O   
1462  C CB  . GLU A 215  ? 0.4153 0.4629 0.5041 0.0033  -0.0403 -0.0707 213  GLU A CB  
1463  N N   . LYS A 216  ? 0.4226 0.4486 0.5244 0.0011  -0.0391 -0.0645 214  LYS A N   
1464  C CA  . LYS A 216  ? 0.4337 0.4528 0.5449 0.0007  -0.0409 -0.0657 214  LYS A CA  
1465  C C   . LYS A 216  ? 0.4625 0.4741 0.5774 -0.0015 -0.0393 -0.0587 214  LYS A C   
1466  O O   . LYS A 216  ? 0.5072 0.5132 0.6307 -0.0021 -0.0408 -0.0587 214  LYS A O   
1467  C CB  . LYS A 216  ? 0.4039 0.4209 0.5137 0.0018  -0.0403 -0.0673 214  LYS A CB  
1468  N N   . GLY A 217  ? 0.3879 0.3998 0.4970 -0.0025 -0.0365 -0.0527 215  GLY A N   
1469  C CA  . GLY A 217  ? 0.3572 0.3632 0.4692 -0.0043 -0.0348 -0.0461 215  GLY A CA  
1470  C C   . GLY A 217  ? 0.3501 0.3522 0.4558 -0.0047 -0.0311 -0.0397 215  GLY A C   
1471  O O   . GLY A 217  ? 0.3492 0.3469 0.4569 -0.0061 -0.0295 -0.0342 215  GLY A O   
1472  N N   . PHE A 218  ? 0.2945 0.2984 0.3928 -0.0035 -0.0296 -0.0404 216  PHE A N   
1473  C CA  . PHE A 218  ? 0.2960 0.2969 0.3879 -0.0038 -0.0261 -0.0345 216  PHE A CA  
1474  C C   . PHE A 218  ? 0.2659 0.2697 0.3512 -0.0043 -0.0240 -0.0306 216  PHE A C   
1475  O O   . PHE A 218  ? 0.2858 0.2951 0.3699 -0.0040 -0.0251 -0.0328 216  PHE A O   
1476  C CB  . PHE A 218  ? 0.2618 0.2638 0.3485 -0.0025 -0.0254 -0.0365 216  PHE A CB  
1477  C CG  . PHE A 218  ? 0.2833 0.2813 0.3758 -0.0020 -0.0269 -0.0391 216  PHE A CG  
1478  C CD1 . PHE A 218  ? 0.3309 0.3309 0.4293 -0.0011 -0.0302 -0.0459 216  PHE A CD1 
1479  C CD2 . PHE A 218  ? 0.3001 0.2924 0.3922 -0.0024 -0.0250 -0.0349 216  PHE A CD2 
1480  C CE1 . PHE A 218  ? 0.3221 0.3183 0.4264 -0.0006 -0.0318 -0.0483 216  PHE A CE1 
1481  C CE2 . PHE A 218  ? 0.3377 0.3263 0.4353 -0.0020 -0.0264 -0.0369 216  PHE A CE2 
1482  C CZ  . PHE A 218  ? 0.3133 0.3036 0.4171 -0.0010 -0.0299 -0.0436 216  PHE A CZ  
1483  N N   . SER A 219  ? 0.2692 0.2696 0.3505 -0.0048 -0.0210 -0.0248 217  SER A N   
1484  C CA  . SER A 219  ? 0.2373 0.2399 0.3117 -0.0050 -0.0188 -0.0211 217  SER A CA  
1485  C C   . SER A 219  ? 0.2223 0.2237 0.2897 -0.0044 -0.0164 -0.0188 217  SER A C   
1486  O O   . SER A 219  ? 0.2394 0.2384 0.3074 -0.0040 -0.0164 -0.0201 217  SER A O   
1487  C CB  . SER A 219  ? 0.2951 0.2950 0.3719 -0.0062 -0.0176 -0.0162 217  SER A CB  
1488  O OG  . SER A 219  ? 0.2873 0.2816 0.3661 -0.0067 -0.0161 -0.0126 217  SER A OG  
1489  N N   . TYR A 220  ? 0.2349 0.2379 0.2961 -0.0045 -0.0145 -0.0153 218  TYR A N   
1490  C CA  . TYR A 220  ? 0.2245 0.2269 0.2790 -0.0040 -0.0124 -0.0134 218  TYR A CA  
1491  C C   . TYR A 220  ? 0.2293 0.2291 0.2806 -0.0045 -0.0099 -0.0078 218  TYR A C   
1492  O O   . TYR A 220  ? 0.2247 0.2254 0.2767 -0.0050 -0.0098 -0.0058 218  TYR A O   
1493  C CB  . TYR A 220  ? 0.2240 0.2328 0.2732 -0.0032 -0.0130 -0.0159 218  TYR A CB  
1494  C CG  . TYR A 220  ? 0.2248 0.2361 0.2754 -0.0023 -0.0148 -0.0213 218  TYR A CG  
1495  C CD1 . TYR A 220  ? 0.2717 0.2860 0.3273 -0.0020 -0.0175 -0.0262 218  TYR A CD1 
1496  C CD2 . TYR A 220  ? 0.2601 0.2709 0.3074 -0.0017 -0.0138 -0.0218 218  TYR A CD2 
1497  C CE1 . TYR A 220  ? 0.2511 0.2679 0.3084 -0.0009 -0.0192 -0.0317 218  TYR A CE1 
1498  C CE2 . TYR A 220  ? 0.2501 0.2634 0.2989 -0.0007 -0.0155 -0.0271 218  TYR A CE2 
1499  C CZ  . TYR A 220  ? 0.2788 0.2951 0.3326 -0.0002 -0.0182 -0.0321 218  TYR A CZ  
1500  O OH  . TYR A 220  ? 0.2803 0.2994 0.3359 0.0010  -0.0199 -0.0377 218  TYR A OH  
1501  N N   . SER A 221  ? 0.2330 0.2296 0.2808 -0.0043 -0.0081 -0.0055 219  SER A N   
1502  C CA  . SER A 221  ? 0.2242 0.2192 0.2676 -0.0044 -0.0057 -0.0010 219  SER A CA  
1503  C C   . SER A 221  ? 0.2632 0.2593 0.3009 -0.0038 -0.0049 -0.0011 219  SER A C   
1504  O O   . SER A 221  ? 0.2891 0.2833 0.3267 -0.0035 -0.0047 -0.0024 219  SER A O   
1505  C CB  . SER A 221  ? 0.2464 0.2362 0.2921 -0.0048 -0.0042 0.0023  219  SER A CB  
1506  O OG  . SER A 221  ? 0.2901 0.2787 0.3316 -0.0046 -0.0021 0.0061  219  SER A OG  
1507  N N   . TYR A 222  ? 0.1976 0.1967 0.2308 -0.0038 -0.0044 0.0003  220  TYR A N   
1508  C CA  . TYR A 222  ? 0.2319 0.2329 0.2600 -0.0034 -0.0038 0.0002  220  TYR A CA  
1509  C C   . TYR A 222  ? 0.2320 0.2289 0.2570 -0.0034 -0.0017 0.0038  220  TYR A C   
1510  O O   . TYR A 222  ? 0.2537 0.2488 0.2784 -0.0036 -0.0007 0.0070  220  TYR A O   
1511  C CB  . TYR A 222  ? 0.2213 0.2282 0.2464 -0.0034 -0.0045 0.0001  220  TYR A CB  
1512  C CG  . TYR A 222  ? 0.2155 0.2270 0.2432 -0.0032 -0.0067 -0.0041 220  TYR A CG  
1513  C CD1 . TYR A 222  ? 0.2073 0.2219 0.2348 -0.0026 -0.0077 -0.0082 220  TYR A CD1 
1514  C CD2 . TYR A 222  ? 0.2212 0.2343 0.2522 -0.0035 -0.0079 -0.0044 220  TYR A CD2 
1515  C CE1 . TYR A 222  ? 0.2289 0.2479 0.2592 -0.0022 -0.0099 -0.0127 220  TYR A CE1 
1516  C CE2 . TYR A 222  ? 0.2281 0.2455 0.2618 -0.0032 -0.0100 -0.0087 220  TYR A CE2 
1517  C CZ  . TYR A 222  ? 0.2149 0.2353 0.2483 -0.0025 -0.0111 -0.0129 220  TYR A CZ  
1518  O OH  . TYR A 222  ? 0.2644 0.2894 0.3007 -0.0020 -0.0134 -0.0177 220  TYR A OH  
1519  N N   . ASP A 223  ? 0.2602 0.2561 0.2833 -0.0031 -0.0011 0.0030  221  ASP A N   
1520  C CA  . ASP A 223  ? 0.3051 0.2974 0.3252 -0.0030 0.0006  0.0057  221  ASP A CA  
1521  C C   . ASP A 223  ? 0.3339 0.3294 0.3494 -0.0030 0.0009  0.0062  221  ASP A C   
1522  O O   . ASP A 223  ? 0.2855 0.2836 0.2998 -0.0028 0.0004  0.0038  221  ASP A O   
1523  C CB  . ASP A 223  ? 0.3760 0.3648 0.3979 -0.0027 0.0009  0.0046  221  ASP A CB  
1524  C CG  . ASP A 223  ? 0.3838 0.3698 0.4023 -0.0025 0.0025  0.0066  221  ASP A CG  
1525  O OD1 . ASP A 223  ? 0.3950 0.3804 0.4109 -0.0026 0.0035  0.0094  221  ASP A OD1 
1526  O OD2 . ASP A 223  ? 0.4299 0.4144 0.4488 -0.0021 0.0025  0.0053  221  ASP A OD2 
1527  N N   . MET A 224  ? 0.3070 0.3024 0.3202 -0.0032 0.0016  0.0093  222  MET A N   
1528  C CA  . MET A 224  ? 0.3344 0.3330 0.3439 -0.0035 0.0017  0.0105  222  MET A CA  
1529  C C   . MET A 224  ? 0.3410 0.3369 0.3480 -0.0033 0.0029  0.0113  222  MET A C   
1530  O O   . MET A 224  ? 0.4839 0.4818 0.4882 -0.0037 0.0031  0.0128  222  MET A O   
1531  C CB  . MET A 224  ? 0.3674 0.3669 0.3761 -0.0038 0.0017  0.0136  222  MET A CB  
1532  C CG  . MET A 224  ? 0.3625 0.3651 0.3736 -0.0039 0.0005  0.0129  222  MET A CG  
1533  S SD  . MET A 224  ? 0.4115 0.4209 0.4226 -0.0038 -0.0012 0.0089  222  MET A SD  
1534  C CE  . MET A 224  ? 0.3729 0.3870 0.3795 -0.0042 -0.0011 0.0109  222  MET A CE  
1535  N N   . LEU A 225  ? 0.4314 0.4231 0.4397 -0.0030 0.0035  0.0105  223  LEU A N   
1536  C CA  . LEU A 225  ? 0.3877 0.3774 0.3943 -0.0027 0.0043  0.0104  223  LEU A CA  
1537  C C   . LEU A 225  ? 0.4499 0.4372 0.4541 -0.0028 0.0054  0.0134  223  LEU A C   
1538  O O   . LEU A 225  ? 0.4660 0.4521 0.4684 -0.0027 0.0060  0.0135  223  LEU A O   
1539  C CB  . LEU A 225  ? 0.3607 0.3546 0.3657 -0.0027 0.0037  0.0080  223  LEU A CB  
1540  C CG  . LEU A 225  ? 0.3520 0.3473 0.3597 -0.0022 0.0025  0.0041  223  LEU A CG  
1541  C CD1 . LEU A 225  ? 0.3661 0.3665 0.3721 -0.0020 0.0019  0.0015  223  LEU A CD1 
1542  C CD2 . LEU A 225  ? 0.3539 0.3441 0.3640 -0.0018 0.0030  0.0037  223  LEU A CD2 
1543  N N   . GLY A 226  ? 0.4598 0.4463 0.4642 -0.0030 0.0056  0.0158  224  GLY A N   
1544  C CA  . GLY A 226  ? 0.3800 0.3638 0.3829 -0.0029 0.0065  0.0182  224  GLY A CA  
1545  C C   . GLY A 226  ? 0.3490 0.3285 0.3529 -0.0022 0.0075  0.0185  224  GLY A C   
1546  O O   . GLY A 226  ? 0.3514 0.3298 0.3576 -0.0019 0.0077  0.0181  224  GLY A O   
1547  N N   . GLU A 227  ? 0.3422 0.3194 0.3442 -0.0019 0.0082  0.0194  225  GLU A N   
1548  C CA  . GLU A 227  ? 0.3222 0.2959 0.3246 -0.0011 0.0093  0.0200  225  GLU A CA  
1549  C C   . GLU A 227  ? 0.3312 0.3033 0.3316 -0.0009 0.0097  0.0208  225  GLU A C   
1550  O O   . GLU A 227  ? 0.3194 0.2928 0.3183 -0.0015 0.0092  0.0208  225  GLU A O   
1551  C CB  . GLU A 227  ? 0.3563 0.3289 0.3597 -0.0009 0.0097  0.0186  225  GLU A CB  
1552  C CG  . GLU A 227  ? 0.3735 0.3463 0.3752 -0.0009 0.0095  0.0173  225  GLU A CG  
1553  C CD  . GLU A 227  ? 0.5121 0.4839 0.5155 -0.0006 0.0095  0.0160  225  GLU A CD  
1554  O OE1 . GLU A 227  ? 0.4030 0.3765 0.4082 -0.0009 0.0087  0.0144  225  GLU A OE1 
1555  O OE2 . GLU A 227  ? 0.4296 0.3991 0.4327 0.0000  0.0103  0.0166  225  GLU A OE2 
1556  N N   . ALA A 228  ? 0.3122 0.2818 0.3127 0.0000  0.0105  0.0214  226  ALA A N   
1557  C CA  . ALA A 228  ? 0.3316 0.2994 0.3305 0.0004  0.0109  0.0216  226  ALA A CA  
1558  C C   . ALA A 228  ? 0.3369 0.3052 0.3354 -0.0001 0.0100  0.0226  226  ALA A C   
1559  O O   . ALA A 228  ? 0.3312 0.2998 0.3284 -0.0006 0.0097  0.0225  226  ALA A O   
1560  C CB  . ALA A 228  ? 0.4050 0.3722 0.4024 0.0005  0.0112  0.0205  226  ALA A CB  
1561  N N   . ALA A 229  ? 0.2748 0.2436 0.2749 -0.0001 0.0096  0.0238  227  ALA A N   
1562  C CA  . ALA A 229  ? 0.2679 0.2368 0.2682 -0.0006 0.0086  0.0252  227  ALA A CA  
1563  C C   . ALA A 229  ? 0.2779 0.2441 0.2778 0.0000  0.0087  0.0250  227  ALA A C   
1564  O O   . ALA A 229  ? 0.2669 0.2313 0.2669 0.0012  0.0095  0.0242  227  ALA A O   
1565  C CB  . ALA A 229  ? 0.2606 0.2299 0.2631 -0.0004 0.0081  0.0265  227  ALA A CB  
1566  N N   . THR A 230  ? 0.2624 0.2288 0.2619 -0.0008 0.0079  0.0257  228  THR A N   
1567  C CA  . THR A 230  ? 0.2901 0.2541 0.2897 -0.0004 0.0077  0.0254  228  THR A CA  
1568  C C   . THR A 230  ? 0.2637 0.2264 0.2658 -0.0003 0.0066  0.0268  228  THR A C   
1569  O O   . THR A 230  ? 0.2727 0.2330 0.2757 0.0006  0.0063  0.0260  228  THR A O   
1570  C CB  . THR A 230  ? 0.3541 0.3192 0.3522 -0.0014 0.0075  0.0253  228  THR A CB  
1571  O OG1 . THR A 230  ? 0.3980 0.3643 0.3942 -0.0013 0.0084  0.0239  228  THR A OG1 
1572  C CG2 . THR A 230  ? 0.4122 0.3748 0.4104 -0.0009 0.0073  0.0246  228  THR A CG2 
1573  N N   . THR A 231  ? 0.2833 0.2477 0.2867 -0.0012 0.0057  0.0288  229  THR A N   
1574  C CA  . THR A 231  ? 0.2185 0.1818 0.2249 -0.0013 0.0043  0.0306  229  THR A CA  
1575  C C   . THR A 231  ? 0.2370 0.2016 0.2449 -0.0011 0.0041  0.0317  229  THR A C   
1576  O O   . THR A 231  ? 0.2639 0.2307 0.2705 -0.0012 0.0048  0.0314  229  THR A O   
1577  C CB  . THR A 231  ? 0.2933 0.2582 0.3003 -0.0030 0.0032  0.0329  229  THR A CB  
1578  O OG1 . THR A 231  ? 0.2835 0.2525 0.2894 -0.0042 0.0031  0.0344  229  THR A OG1 
1579  C CG2 . THR A 231  ? 0.2820 0.2466 0.2872 -0.0035 0.0035  0.0318  229  THR A CG2 
1580  N N   . ALA A 232  ? 0.2669 0.2299 0.2779 -0.0007 0.0029  0.0329  230  ALA A N   
1581  C CA  . ALA A 232  ? 0.2667 0.2310 0.2796 -0.0006 0.0023  0.0344  230  ALA A CA  
1582  C C   . ALA A 232  ? 0.3077 0.2760 0.3196 -0.0022 0.0018  0.0366  230  ALA A C   
1583  O O   . ALA A 232  ? 0.2961 0.2668 0.3077 -0.0022 0.0021  0.0367  230  ALA A O   
1584  C CB  . ALA A 232  ? 0.2756 0.2376 0.2925 0.0000  0.0008  0.0356  230  ALA A CB  
1585  N N   . ALA A 233  ? 0.3076 0.2772 0.3191 -0.0036 0.0011  0.0383  231  ALA A N   
1586  C CA  . ALA A 233  ? 0.3330 0.3074 0.3434 -0.0051 0.0007  0.0404  231  ALA A CA  
1587  C C   . ALA A 233  ? 0.3176 0.2948 0.3248 -0.0052 0.0020  0.0382  231  ALA A C   
1588  O O   . ALA A 233  ? 0.3371 0.3181 0.3438 -0.0056 0.0018  0.0387  231  ALA A O   
1589  C CB  . ALA A 233  ? 0.3597 0.3355 0.3705 -0.0067 -0.0002 0.0428  231  ALA A CB  
1590  N N   . ASP A 234  ? 0.3005 0.2760 0.3058 -0.0047 0.0031  0.0356  232  ASP A N   
1591  C CA  . ASP A 234  ? 0.3050 0.2824 0.3080 -0.0045 0.0042  0.0333  232  ASP A CA  
1592  C C   . ASP A 234  ? 0.2984 0.2758 0.3024 -0.0037 0.0045  0.0324  232  ASP A C   
1593  O O   . ASP A 234  ? 0.2880 0.2686 0.2914 -0.0040 0.0045  0.0318  232  ASP A O   
1594  C CB  . ASP A 234  ? 0.3788 0.3536 0.3804 -0.0038 0.0053  0.0309  232  ASP A CB  
1595  C CG  . ASP A 234  ? 0.5100 0.4859 0.5101 -0.0047 0.0052  0.0310  232  ASP A CG  
1596  O OD1 . ASP A 234  ? 0.4919 0.4712 0.4919 -0.0060 0.0044  0.0329  232  ASP A OD1 
1597  O OD2 . ASP A 234  ? 0.6041 0.5777 0.6032 -0.0042 0.0059  0.0293  232  ASP A OD2 
1598  N N   . ALA A 235  ? 0.2619 0.2358 0.2675 -0.0025 0.0048  0.0321  233  ALA A N   
1599  C CA  . ALA A 235  ? 0.2511 0.2251 0.2580 -0.0017 0.0052  0.0315  233  ALA A CA  
1600  C C   . ALA A 235  ? 0.2865 0.2636 0.2948 -0.0023 0.0040  0.0333  233  ALA A C   
1601  O O   . ALA A 235  ? 0.2767 0.2558 0.2852 -0.0023 0.0042  0.0326  233  ALA A O   
1602  C CB  . ALA A 235  ? 0.2548 0.2254 0.2633 -0.0003 0.0056  0.0310  233  ALA A CB  
1603  N N   . GLU A 236  ? 0.2642 0.2417 0.2737 -0.0028 0.0028  0.0358  234  GLU A N   
1604  C CA  . GLU A 236  ? 0.2786 0.2594 0.2892 -0.0034 0.0016  0.0380  234  GLU A CA  
1605  C C   . GLU A 236  ? 0.2492 0.2350 0.2576 -0.0045 0.0014  0.0378  234  GLU A C   
1606  O O   . GLU A 236  ? 0.2885 0.2775 0.2973 -0.0047 0.0009  0.0379  234  GLU A O   
1607  C CB  . GLU A 236  ? 0.2988 0.2790 0.3116 -0.0039 0.0002  0.0411  234  GLU A CB  
1608  C CG  . GLU A 236  ? 0.4281 0.4040 0.4439 -0.0026 -0.0002 0.0412  234  GLU A CG  
1609  C CD  . GLU A 236  ? 0.5678 0.5417 0.5857 -0.0031 -0.0015 0.0435  234  GLU A CD  
1610  O OE1 . GLU A 236  ? 0.6336 0.6102 0.6509 -0.0046 -0.0022 0.0458  234  GLU A OE1 
1611  O OE2 . GLU A 236  ? 0.6680 0.6380 0.6885 -0.0019 -0.0018 0.0429  234  GLU A OE2 
1612  N N   . ARG A 237  ? 0.2633 0.2502 0.2695 -0.0052 0.0018  0.0372  235  ARG A N   
1613  C CA  . ARG A 237  ? 0.2840 0.2761 0.2882 -0.0060 0.0017  0.0364  235  ARG A CA  
1614  C C   . ARG A 237  ? 0.3193 0.3118 0.3231 -0.0054 0.0024  0.0332  235  ARG A C   
1615  O O   . ARG A 237  ? 0.2947 0.2914 0.2983 -0.0056 0.0018  0.0325  235  ARG A O   
1616  C CB  . ARG A 237  ? 0.3132 0.3062 0.3154 -0.0067 0.0021  0.0361  235  ARG A CB  
1617  C CG  . ARG A 237  ? 0.4321 0.4303 0.4320 -0.0071 0.0022  0.0342  235  ARG A CG  
1618  C CD  . ARG A 237  ? 0.5291 0.5296 0.5273 -0.0080 0.0024  0.0348  235  ARG A CD  
1619  N NE  . ARG A 237  ? 0.6253 0.6210 0.6232 -0.0075 0.0033  0.0333  235  ARG A NE  
1620  C CZ  . ARG A 237  ? 0.5532 0.5480 0.5499 -0.0069 0.0041  0.0301  235  ARG A CZ  
1621  N NH1 . ARG A 237  ? 0.6398 0.6379 0.6357 -0.0067 0.0041  0.0277  235  ARG A NH1 
1622  N NH2 . ARG A 237  ? 0.6019 0.5923 0.5984 -0.0065 0.0049  0.0292  235  ARG A NH2 
1623  N N   . TYR A 238  ? 0.2553 0.2435 0.2593 -0.0045 0.0035  0.0312  236  TYR A N   
1624  C CA  . TYR A 238  ? 0.2482 0.2364 0.2527 -0.0040 0.0040  0.0286  236  TYR A CA  
1625  C C   . TYR A 238  ? 0.2441 0.2331 0.2508 -0.0037 0.0035  0.0291  236  TYR A C   
1626  O O   . TYR A 238  ? 0.2981 0.2895 0.3054 -0.0038 0.0031  0.0276  236  TYR A O   
1627  C CB  . TYR A 238  ? 0.2595 0.2433 0.2640 -0.0033 0.0053  0.0271  236  TYR A CB  
1628  C CG  . TYR A 238  ? 0.2626 0.2459 0.2649 -0.0035 0.0057  0.0259  236  TYR A CG  
1629  C CD1 . TYR A 238  ? 0.3064 0.2935 0.3075 -0.0040 0.0053  0.0245  236  TYR A CD1 
1630  C CD2 . TYR A 238  ? 0.2921 0.2718 0.2938 -0.0030 0.0065  0.0259  236  TYR A CD2 
1631  C CE1 . TYR A 238  ? 0.3718 0.3588 0.3712 -0.0041 0.0058  0.0233  236  TYR A CE1 
1632  C CE2 . TYR A 238  ? 0.3330 0.3125 0.3330 -0.0031 0.0069  0.0248  236  TYR A CE2 
1633  C CZ  . TYR A 238  ? 0.3818 0.3648 0.3806 -0.0037 0.0066  0.0236  236  TYR A CZ  
1634  O OH  . TYR A 238  ? 0.4126 0.3955 0.4099 -0.0038 0.0069  0.0224  236  TYR A OH  
1635  N N   . TYR A 239  ? 0.2523 0.2392 0.2605 -0.0033 0.0033  0.0312  237  TYR A N   
1636  C CA  . TYR A 239  ? 0.2179 0.2058 0.2285 -0.0030 0.0027  0.0319  237  TYR A CA  
1637  C C   . TYR A 239  ? 0.2646 0.2579 0.2750 -0.0038 0.0014  0.0327  237  TYR A C   
1638  O O   . TYR A 239  ? 0.2400 0.2355 0.2514 -0.0038 0.0010  0.0314  237  TYR A O   
1639  C CB  . TYR A 239  ? 0.2641 0.2492 0.2765 -0.0023 0.0025  0.0339  237  TYR A CB  
1640  C CG  . TYR A 239  ? 0.2773 0.2638 0.2923 -0.0019 0.0019  0.0346  237  TYR A CG  
1641  C CD1 . TYR A 239  ? 0.2839 0.2739 0.2995 -0.0025 0.0004  0.0367  237  TYR A CD1 
1642  C CD2 . TYR A 239  ? 0.2674 0.2522 0.2842 -0.0010 0.0028  0.0334  237  TYR A CD2 
1643  C CE1 . TYR A 239  ? 0.3096 0.3010 0.3276 -0.0021 -0.0002 0.0373  237  TYR A CE1 
1644  C CE2 . TYR A 239  ? 0.3033 0.2896 0.3226 -0.0007 0.0022  0.0340  237  TYR A CE2 
1645  C CZ  . TYR A 239  ? 0.3302 0.3196 0.3501 -0.0012 0.0007  0.0358  237  TYR A CZ  
1646  O OH  . TYR A 239  ? 0.3684 0.3595 0.3910 -0.0008 0.0000  0.0364  237  TYR A OH  
1647  N N   . ARG A 240  ? 0.2413 0.2370 0.2504 -0.0045 0.0006  0.0348  238  ARG A N   
1648  C CA  A ARG A 240  ? 0.2523 0.2539 0.2611 -0.0052 -0.0007 0.0358  238  ARG A CA  
1649  C CA  B ARG A 240  ? 0.2526 0.2541 0.2613 -0.0052 -0.0007 0.0358  238  ARG A CA  
1650  C C   . ARG A 240  ? 0.2482 0.2537 0.2553 -0.0055 -0.0007 0.0327  238  ARG A C   
1651  O O   . ARG A 240  ? 0.2586 0.2687 0.2659 -0.0056 -0.0016 0.0322  238  ARG A O   
1652  C CB  A ARG A 240  ? 0.2985 0.3023 0.3067 -0.0061 -0.0016 0.0394  238  ARG A CB  
1653  C CB  B ARG A 240  ? 0.2983 0.3021 0.3064 -0.0061 -0.0016 0.0394  238  ARG A CB  
1654  C CG  A ARG A 240  ? 0.3057 0.3102 0.3115 -0.0067 -0.0011 0.0393  238  ARG A CG  
1655  C CG  B ARG A 240  ? 0.3056 0.3098 0.3115 -0.0067 -0.0011 0.0394  238  ARG A CG  
1656  C CD  A ARG A 240  ? 0.2905 0.2983 0.2962 -0.0078 -0.0022 0.0434  238  ARG A CD  
1657  C CD  B ARG A 240  ? 0.2924 0.2985 0.2988 -0.0077 -0.0021 0.0437  238  ARG A CD  
1658  N NE  A ARG A 240  ? 0.2344 0.2422 0.2384 -0.0085 -0.0016 0.0436  238  ARG A NE  
1659  N NE  B ARG A 240  ? 0.3096 0.3117 0.3190 -0.0072 -0.0028 0.0460  238  ARG A NE  
1660  C CZ  A ARG A 240  ? 0.2688 0.2716 0.2738 -0.0085 -0.0013 0.0446  238  ARG A CZ  
1661  C CZ  B ARG A 240  ? 0.2589 0.2560 0.2699 -0.0070 -0.0027 0.0471  238  ARG A CZ  
1662  N NH1 A ARG A 240  ? 0.2627 0.2605 0.2705 -0.0079 -0.0016 0.0457  238  ARG A NH1 
1663  N NH1 B ARG A 240  ? 0.2932 0.2891 0.3029 -0.0076 -0.0022 0.0470  238  ARG A NH1 
1664  N NH2 A ARG A 240  ? 0.3048 0.3079 0.3082 -0.0091 -0.0008 0.0443  238  ARG A NH2 
1665  N NH2 B ARG A 240  ? 0.2374 0.2307 0.2515 -0.0062 -0.0032 0.0481  238  ARG A NH2 
1666  N N   . ASP A 241  ? 0.2476 0.2512 0.2532 -0.0054 0.0003  0.0305  239  ASP A N   
1667  C CA  A ASP A 241  ? 0.2729 0.2795 0.2777 -0.0054 0.0003  0.0271  239  ASP A CA  
1668  C CA  B ASP A 241  ? 0.2732 0.2798 0.2780 -0.0054 0.0003  0.0271  239  ASP A CA  
1669  C C   . ASP A 241  ? 0.2632 0.2687 0.2704 -0.0049 0.0002  0.0248  239  ASP A C   
1670  O O   . ASP A 241  ? 0.2779 0.2876 0.2856 -0.0049 -0.0008 0.0228  239  ASP A O   
1671  C CB  A ASP A 241  ? 0.3449 0.3492 0.3481 -0.0053 0.0013  0.0254  239  ASP A CB  
1672  C CB  B ASP A 241  ? 0.3448 0.3491 0.3480 -0.0053 0.0013  0.0254  239  ASP A CB  
1673  C CG  A ASP A 241  ? 0.3492 0.3558 0.3502 -0.0060 0.0013  0.0271  239  ASP A CG  
1674  C CG  B ASP A 241  ? 0.3796 0.3879 0.3819 -0.0053 0.0010  0.0221  239  ASP A CG  
1675  O OD1 A ASP A 241  ? 0.3896 0.4003 0.3901 -0.0066 0.0004  0.0297  239  ASP A OD1 
1676  O OD1 B ASP A 241  ? 0.3870 0.4016 0.3881 -0.0057 0.0000  0.0220  239  ASP A OD1 
1677  O OD2 A ASP A 241  ? 0.4468 0.4512 0.4466 -0.0060 0.0021  0.0262  239  ASP A OD2 
1678  O OD2 B ASP A 241  ? 0.4388 0.4442 0.4417 -0.0049 0.0015  0.0195  239  ASP A OD2 
1679  N N   . TYR A 242  ? 0.2460 0.2463 0.2551 -0.0043 0.0011  0.0251  240  TYR A N   
1680  C CA  . TYR A 242  ? 0.2302 0.2296 0.2421 -0.0040 0.0010  0.0236  240  TYR A CA  
1681  C C   . TYR A 242  ? 0.2274 0.2303 0.2408 -0.0041 -0.0002 0.0246  240  TYR A C   
1682  O O   . TYR A 242  ? 0.2197 0.2249 0.2349 -0.0041 -0.0010 0.0227  240  TYR A O   
1683  C CB  . TYR A 242  ? 0.1989 0.1930 0.2124 -0.0034 0.0023  0.0243  240  TYR A CB  
1684  C CG  . TYR A 242  ? 0.2133 0.2039 0.2260 -0.0031 0.0035  0.0230  240  TYR A CG  
1685  C CD1 . TYR A 242  ? 0.2806 0.2721 0.2933 -0.0033 0.0033  0.0204  240  TYR A CD1 
1686  C CD2 . TYR A 242  ? 0.2529 0.2395 0.2652 -0.0026 0.0047  0.0243  240  TYR A CD2 
1687  C CE1 . TYR A 242  ? 0.2914 0.2797 0.3036 -0.0031 0.0043  0.0195  240  TYR A CE1 
1688  C CE2 . TYR A 242  ? 0.2476 0.2314 0.2590 -0.0023 0.0057  0.0233  240  TYR A CE2 
1689  C CZ  . TYR A 242  ? 0.2474 0.2320 0.2588 -0.0026 0.0055  0.0211  240  TYR A CZ  
1690  O OH  . TYR A 242  ? 0.2411 0.2229 0.2519 -0.0023 0.0065  0.0204  240  TYR A OH  
1691  N N   . GLU A 243  ? 0.2119 0.2148 0.2251 -0.0041 -0.0005 0.0277  241  GLU A N   
1692  C CA  . GLU A 243  ? 0.2034 0.2095 0.2182 -0.0041 -0.0018 0.0291  241  GLU A CA  
1693  C C   . GLU A 243  ? 0.2365 0.2492 0.2501 -0.0046 -0.0031 0.0280  241  GLU A C   
1694  O O   . GLU A 243  ? 0.2253 0.2409 0.2407 -0.0046 -0.0041 0.0266  241  GLU A O   
1695  C CB  . GLU A 243  ? 0.2507 0.2556 0.2656 -0.0040 -0.0020 0.0328  241  GLU A CB  
1696  C CG  . GLU A 243  ? 0.2762 0.2844 0.2928 -0.0040 -0.0034 0.0349  241  GLU A CG  
1697  C CD  . GLU A 243  ? 0.2759 0.2831 0.2928 -0.0041 -0.0039 0.0387  241  GLU A CD  
1698  O OE1 . GLU A 243  ? 0.3909 0.3973 0.4061 -0.0045 -0.0037 0.0400  241  GLU A OE1 
1699  O OE2 . GLU A 243  ? 0.3027 0.3100 0.3220 -0.0036 -0.0047 0.0405  241  GLU A OE2 
1700  N N   . SER A 244  ? 0.2273 0.2428 0.2379 -0.0051 -0.0032 0.0283  242  SER A N   
1701  C CA  . SER A 244  ? 0.2145 0.2372 0.2236 -0.0055 -0.0045 0.0270  242  SER A CA  
1702  C C   . SER A 244  ? 0.2218 0.2456 0.2319 -0.0051 -0.0047 0.0223  242  SER A C   
1703  O O   . SER A 244  ? 0.2621 0.2913 0.2728 -0.0051 -0.0060 0.0205  242  SER A O   
1704  C CB  . SER A 244  ? 0.2608 0.2867 0.2668 -0.0060 -0.0043 0.0284  242  SER A CB  
1705  O OG  . SER A 244  ? 0.3126 0.3354 0.3175 -0.0059 -0.0032 0.0263  242  SER A OG  
1706  N N   . ALA A 245  ? 0.2050 0.2239 0.2158 -0.0049 -0.0036 0.0203  243  ALA A N   
1707  C CA  . ALA A 245  ? 0.2405 0.2596 0.2531 -0.0046 -0.0040 0.0161  243  ALA A CA  
1708  C C   . ALA A 245  ? 0.2099 0.2283 0.2263 -0.0045 -0.0047 0.0154  243  ALA A C   
1709  O O   . ALA A 245  ? 0.2245 0.2463 0.2427 -0.0044 -0.0060 0.0123  243  ALA A O   
1710  C CB  . ALA A 245  ? 0.2454 0.2591 0.2581 -0.0044 -0.0026 0.0148  243  ALA A CB  
1711  N N   . ILE A 246  ? 0.1990 0.2133 0.2170 -0.0044 -0.0039 0.0181  244  ILE A N   
1712  C CA  . ILE A 246  ? 0.1884 0.2024 0.2101 -0.0043 -0.0045 0.0177  244  ILE A CA  
1713  C C   . ILE A 246  ? 0.2218 0.2421 0.2437 -0.0044 -0.0063 0.0174  244  ILE A C   
1714  O O   . ILE A 246  ? 0.2339 0.2563 0.2587 -0.0044 -0.0075 0.0149  244  ILE A O   
1715  C CB  . ILE A 246  ? 0.1898 0.1993 0.2129 -0.0041 -0.0033 0.0207  244  ILE A CB  
1716  C CG1 . ILE A 246  ? 0.1893 0.1933 0.2128 -0.0039 -0.0016 0.0203  244  ILE A CG1 
1717  C CG2 . ILE A 246  ? 0.2204 0.2309 0.2472 -0.0040 -0.0040 0.0208  244  ILE A CG2 
1718  C CD1 . ILE A 246  ? 0.2181 0.2180 0.2420 -0.0034 -0.0003 0.0230  244  ILE A CD1 
1719  N N   . HIS A 247  ? 0.2018 0.2255 0.2209 -0.0046 -0.0067 0.0200  245  HIS A N   
1720  C CA  . HIS A 247  ? 0.1919 0.2224 0.2109 -0.0046 -0.0085 0.0199  245  HIS A CA  
1721  C C   . HIS A 247  ? 0.2104 0.2460 0.2289 -0.0046 -0.0097 0.0155  245  HIS A C   
1722  O O   . HIS A 247  ? 0.2367 0.2761 0.2573 -0.0044 -0.0112 0.0133  245  HIS A O   
1723  C CB  . HIS A 247  ? 0.2228 0.2564 0.2389 -0.0049 -0.0087 0.0239  245  HIS A CB  
1724  C CG  . HIS A 247  ? 0.2336 0.2636 0.2510 -0.0048 -0.0084 0.0279  245  HIS A CG  
1725  N ND1 . HIS A 247  ? 0.2163 0.2466 0.2366 -0.0045 -0.0092 0.0287  245  HIS A ND1 
1726  C CD2 . HIS A 247  ? 0.2605 0.2865 0.2770 -0.0048 -0.0074 0.0312  245  HIS A CD2 
1727  C CE1 . HIS A 247  ? 0.2619 0.2887 0.2831 -0.0043 -0.0087 0.0322  245  HIS A CE1 
1728  N NE2 . HIS A 247  ? 0.2600 0.2840 0.2791 -0.0044 -0.0077 0.0337  245  HIS A NE2 
1729  N N   . ALA A 248  ? 0.1895 0.2258 0.2055 -0.0046 -0.0091 0.0140  246  ALA A N   
1730  C CA  . ALA A 248  ? 0.2330 0.2746 0.2487 -0.0043 -0.0103 0.0094  246  ALA A CA  
1731  C C   . ALA A 248  ? 0.2499 0.2888 0.2700 -0.0040 -0.0109 0.0054  246  ALA A C   
1732  O O   . ALA A 248  ? 0.2275 0.2711 0.2493 -0.0038 -0.0127 0.0018  246  ALA A O   
1733  C CB  . ALA A 248  ? 0.2562 0.2984 0.2686 -0.0042 -0.0094 0.0086  246  ALA A CB  
1734  N N   . ILE A 249  ? 0.2170 0.2485 0.2392 -0.0042 -0.0096 0.0059  247  ILE A N   
1735  C CA  . ILE A 249  ? 0.2236 0.2520 0.2505 -0.0041 -0.0101 0.0029  247  ILE A CA  
1736  C C   . ILE A 249  ? 0.2158 0.2455 0.2463 -0.0043 -0.0113 0.0031  247  ILE A C   
1737  O O   . ILE A 249  ? 0.2330 0.2644 0.2673 -0.0043 -0.0129 -0.0005 247  ILE A O   
1738  C CB  . ILE A 249  ? 0.2056 0.2264 0.2336 -0.0043 -0.0083 0.0043  247  ILE A CB  
1739  C CG1 . ILE A 249  ? 0.2145 0.2344 0.2394 -0.0040 -0.0074 0.0034  247  ILE A CG1 
1740  C CG2 . ILE A 249  ? 0.2352 0.2528 0.2689 -0.0044 -0.0088 0.0022  247  ILE A CG2 
1741  C CD1 . ILE A 249  ? 0.2237 0.2368 0.2483 -0.0041 -0.0054 0.0059  247  ILE A CD1 
1742  N N   . GLY A 250  ? 0.2126 0.2413 0.2425 -0.0044 -0.0106 0.0072  248  GLY A N   
1743  C CA  . GLY A 250  ? 0.2421 0.2720 0.2755 -0.0046 -0.0116 0.0077  248  GLY A CA  
1744  C C   . GLY A 250  ? 0.2392 0.2768 0.2723 -0.0044 -0.0138 0.0056  248  GLY A C   
1745  O O   . GLY A 250  ? 0.2421 0.2815 0.2790 -0.0045 -0.0153 0.0035  248  GLY A O   
1746  N N   . LYS A 251  ? 0.2212 0.2637 0.2497 -0.0042 -0.0141 0.0062  249  LYS A N   
1747  C CA  . LYS A 251  ? 0.2026 0.2535 0.2302 -0.0039 -0.0162 0.0041  249  LYS A CA  
1748  C C   . LYS A 251  ? 0.2269 0.2801 0.2570 -0.0036 -0.0177 -0.0019 249  LYS A C   
1749  O O   . LYS A 251  ? 0.2610 0.3191 0.2934 -0.0034 -0.0197 -0.0047 249  LYS A O   
1750  C CB  . LYS A 251  ? 0.2222 0.2783 0.2445 -0.0039 -0.0160 0.0061  249  LYS A CB  
1751  C CG  . LYS A 251  ? 0.2635 0.3194 0.2838 -0.0042 -0.0154 0.0119  249  LYS A CG  
1752  C CD  . LYS A 251  ? 0.2963 0.3574 0.3118 -0.0043 -0.0152 0.0137  249  LYS A CD  
1753  C CE  . LYS A 251  ? 0.2568 0.3165 0.2707 -0.0047 -0.0145 0.0198  249  LYS A CE  
1754  N NZ  . LYS A 251  ? 0.2417 0.3057 0.2514 -0.0050 -0.0141 0.0216  249  LYS A NZ  
1755  N N   . ALA A 252  ? 0.2242 0.2741 0.2540 -0.0035 -0.0168 -0.0041 250  ALA A N   
1756  C CA  . ALA A 252  ? 0.2192 0.2707 0.2518 -0.0031 -0.0183 -0.0100 250  ALA A CA  
1757  C C   . ALA A 252  ? 0.2459 0.2928 0.2850 -0.0034 -0.0190 -0.0117 250  ALA A C   
1758  O O   . ALA A 252  ? 0.2535 0.3034 0.2963 -0.0031 -0.0212 -0.0164 250  ALA A O   
1759  C CB  . ALA A 252  ? 0.2862 0.3351 0.3169 -0.0028 -0.0171 -0.0113 250  ALA A CB  
1760  N N   . SER A 253  ? 0.2404 0.2803 0.2811 -0.0040 -0.0173 -0.0079 251  SER A N   
1761  C CA  . SER A 253  ? 0.2226 0.2585 0.2697 -0.0045 -0.0179 -0.0088 251  SER A CA  
1762  C C   . SER A 253  ? 0.2568 0.2976 0.3069 -0.0046 -0.0200 -0.0103 251  SER A C   
1763  O O   . SER A 253  ? 0.2691 0.3100 0.3248 -0.0047 -0.0218 -0.0139 251  SER A O   
1764  C CB  . SER A 253  ? 0.2182 0.2475 0.2660 -0.0050 -0.0156 -0.0040 251  SER A CB  
1765  O OG  . SER A 253  ? 0.2497 0.2761 0.3038 -0.0056 -0.0161 -0.0044 251  SER A OG  
1766  N N   . ALA A 254  ? 0.2166 0.2615 0.2635 -0.0044 -0.0200 -0.0075 252  ALA A N   
1767  C CA  . ALA A 254  ? 0.2351 0.2859 0.2838 -0.0043 -0.0222 -0.0088 252  ALA A CA  
1768  C C   . ALA A 254  ? 0.2830 0.3307 0.3385 -0.0049 -0.0230 -0.0094 252  ALA A C   
1769  O O   . ALA A 254  ? 0.2726 0.3238 0.3321 -0.0049 -0.0253 -0.0134 252  ALA A O   
1770  C CB  . ALA A 254  ? 0.2935 0.3517 0.3410 -0.0036 -0.0244 -0.0140 252  ALA A CB  
1771  N N   . GLY A 255  ? 0.2414 0.2828 0.2985 -0.0054 -0.0209 -0.0055 253  GLY A N   
1772  C CA  . GLY A 255  ? 0.2743 0.3132 0.3377 -0.0061 -0.0213 -0.0052 253  GLY A CA  
1773  C C   . GLY A 255  ? 0.2921 0.3272 0.3614 -0.0067 -0.0219 -0.0081 253  GLY A C   
1774  O O   . GLY A 255  ? 0.2905 0.3244 0.3659 -0.0074 -0.0226 -0.0081 253  GLY A O   
1775  N N   . ARG A 256  ? 0.2725 0.3056 0.3404 -0.0065 -0.0217 -0.0103 254  ARG A N   
1776  C CA  . ARG A 256  ? 0.2742 0.3034 0.3482 -0.0070 -0.0223 -0.0128 254  ARG A CA  
1777  C C   . ARG A 256  ? 0.2869 0.3097 0.3637 -0.0078 -0.0202 -0.0086 254  ARG A C   
1778  O O   . ARG A 256  ? 0.2694 0.2891 0.3525 -0.0086 -0.0208 -0.0096 254  ARG A O   
1779  C CB  . ARG A 256  ? 0.2508 0.2797 0.3228 -0.0064 -0.0227 -0.0162 254  ARG A CB  
1780  C CG  . ARG A 256  ? 0.3040 0.3391 0.3768 -0.0057 -0.0256 -0.0222 254  ARG A CG  
1781  C CD  . ARG A 256  ? 0.2804 0.3156 0.3511 -0.0049 -0.0258 -0.0256 254  ARG A CD  
1782  N NE  . ARG A 256  ? 0.2721 0.3093 0.3347 -0.0043 -0.0239 -0.0232 254  ARG A NE  
1783  C CZ  . ARG A 256  ? 0.3153 0.3528 0.3747 -0.0036 -0.0235 -0.0250 254  ARG A CZ  
1784  N NH1 . ARG A 256  ? 0.2865 0.3216 0.3499 -0.0034 -0.0245 -0.0289 254  ARG A NH1 
1785  N NH2 . ARG A 256  ? 0.2643 0.3047 0.3166 -0.0032 -0.0220 -0.0228 254  ARG A NH2 
1786  N N   . GLY A 257  ? 0.2643 0.2853 0.3368 -0.0077 -0.0177 -0.0039 255  GLY A N   
1787  C CA  . GLY A 257  ? 0.2342 0.2502 0.3090 -0.0083 -0.0155 0.0000  255  GLY A CA  
1788  C C   . GLY A 257  ? 0.2218 0.2331 0.2947 -0.0082 -0.0138 0.0009  255  GLY A C   
1789  O O   . GLY A 257  ? 0.2378 0.2493 0.3079 -0.0077 -0.0143 -0.0017 255  GLY A O   
1790  N N   . ILE A 258  ? 0.2035 0.2108 0.2782 -0.0086 -0.0119 0.0045  256  ILE A N   
1791  C CA  . ILE A 258  ? 0.2267 0.2300 0.2986 -0.0084 -0.0099 0.0061  256  ILE A CA  
1792  C C   . ILE A 258  ? 0.2092 0.2098 0.2853 -0.0088 -0.0108 0.0040  256  ILE A C   
1793  O O   . ILE A 258  ? 0.2187 0.2164 0.2921 -0.0085 -0.0097 0.0044  256  ILE A O   
1794  C CB  . ILE A 258  ? 0.2199 0.2208 0.2915 -0.0084 -0.0073 0.0108  256  ILE A CB  
1795  C CG1 . ILE A 258  ? 0.2134 0.2135 0.2924 -0.0095 -0.0076 0.0121  256  ILE A CG1 
1796  C CG2 . ILE A 258  ? 0.2202 0.2233 0.2874 -0.0077 -0.0065 0.0128  256  ILE A CG2 
1797  C CD1 . ILE A 258  ? 0.2358 0.2344 0.3146 -0.0094 -0.0049 0.0167  256  ILE A CD1 
1798  N N   . TYR A 259  ? 0.2281 0.2293 0.3111 -0.0096 -0.0130 0.0016  257  TYR A N   
1799  C CA  . TYR A 259  ? 0.1989 0.1973 0.2872 -0.0101 -0.0142 -0.0004 257  TYR A CA  
1800  C C   . TYR A 259  ? 0.2389 0.2396 0.3270 -0.0095 -0.0168 -0.0061 257  TYR A C   
1801  O O   . TYR A 259  ? 0.2769 0.2755 0.3639 -0.0090 -0.0168 -0.0077 257  TYR A O   
1802  C CB  . TYR A 259  ? 0.2601 0.2574 0.3572 -0.0114 -0.0153 0.0007  257  TYR A CB  
1803  C CG  . TYR A 259  ? 0.2648 0.2609 0.3622 -0.0120 -0.0127 0.0062  257  TYR A CG  
1804  C CD1 . TYR A 259  ? 0.2819 0.2749 0.3764 -0.0118 -0.0101 0.0098  257  TYR A CD1 
1805  C CD2 . TYR A 259  ? 0.2666 0.2653 0.3668 -0.0125 -0.0129 0.0076  257  TYR A CD2 
1806  C CE1 . TYR A 259  ? 0.2557 0.2484 0.3502 -0.0120 -0.0078 0.0145  257  TYR A CE1 
1807  C CE2 . TYR A 259  ? 0.2572 0.2554 0.3576 -0.0128 -0.0104 0.0124  257  TYR A CE2 
1808  C CZ  . TYR A 259  ? 0.2450 0.2404 0.3424 -0.0125 -0.0079 0.0158  257  TYR A CZ  
1809  O OH  . TYR A 259  ? 0.2622 0.2579 0.3597 -0.0126 -0.0055 0.0201  257  TYR A OH  
1810  N N   . GLU A 260  ? 0.2331 0.2384 0.3222 -0.0093 -0.0189 -0.0092 258  GLU A N   
1811  C CA  . GLU A 260  ? 0.2776 0.2862 0.3662 -0.0085 -0.0213 -0.0150 258  GLU A CA  
1812  C C   . GLU A 260  ? 0.2687 0.2800 0.3485 -0.0073 -0.0201 -0.0153 258  GLU A C   
1813  O O   . GLU A 260  ? 0.3401 0.3527 0.4183 -0.0065 -0.0210 -0.0190 258  GLU A O   
1814  C CB  . GLU A 260  ? 0.3272 0.3406 0.4197 -0.0086 -0.0240 -0.0185 258  GLU A CB  
1815  C CG  . GLU A 260  ? 0.3877 0.4055 0.4797 -0.0075 -0.0266 -0.0249 258  GLU A CG  
1816  C CD  . GLU A 260  ? 0.4884 0.5123 0.5823 -0.0073 -0.0292 -0.0285 258  GLU A CD  
1817  O OE1 . GLU A 260  ? 0.5233 0.5472 0.6215 -0.0082 -0.0297 -0.0267 258  GLU A OE1 
1818  O OE2 . GLU A 260  ? 0.4753 0.5046 0.5663 -0.0062 -0.0308 -0.0330 258  GLU A OE2 
1819  N N   . GLY A 261  ? 0.2318 0.2441 0.3061 -0.0072 -0.0181 -0.0113 259  GLY A N   
1820  C CA  . GLY A 261  ? 0.1978 0.2133 0.2644 -0.0063 -0.0173 -0.0113 259  GLY A CA  
1821  C C   . GLY A 261  ? 0.2380 0.2496 0.3002 -0.0061 -0.0148 -0.0085 259  GLY A C   
1822  O O   . GLY A 261  ? 0.2327 0.2391 0.2969 -0.0066 -0.0134 -0.0059 259  GLY A O   
1823  N N   . PRO A 262  ? 0.2164 0.2307 0.2722 -0.0054 -0.0143 -0.0088 260  PRO A N   
1824  C CA  . PRO A 262  ? 0.2131 0.2241 0.2646 -0.0051 -0.0122 -0.0067 260  PRO A CA  
1825  C C   . PRO A 262  ? 0.2053 0.2133 0.2542 -0.0054 -0.0098 -0.0014 260  PRO A C   
1826  O O   . PRO A 262  ? 0.2570 0.2665 0.3061 -0.0056 -0.0097 0.0007  260  PRO A O   
1827  C CB  . PRO A 262  ? 0.2527 0.2688 0.2989 -0.0044 -0.0127 -0.0088 260  PRO A CB  
1828  C CG  . PRO A 262  ? 0.2288 0.2507 0.2747 -0.0043 -0.0141 -0.0095 260  PRO A CG  
1829  C CD  . PRO A 262  ? 0.2750 0.2962 0.3277 -0.0048 -0.0158 -0.0114 260  PRO A CD  
1830  N N   . GLY A 263  ? 0.2218 0.2258 0.2685 -0.0052 -0.0080 0.0005  261  GLY A N   
1831  C CA  . GLY A 263  ? 0.2316 0.2330 0.2753 -0.0052 -0.0058 0.0049  261  GLY A CA  
1832  C C   . GLY A 263  ? 0.2264 0.2266 0.2648 -0.0048 -0.0045 0.0058  261  GLY A C   
1833  O O   . GLY A 263  ? 0.2056 0.2078 0.2421 -0.0045 -0.0052 0.0032  261  GLY A O   
1834  N N   . ILE A 264  ? 0.2183 0.2156 0.2544 -0.0046 -0.0025 0.0094  262  ILE A N   
1835  C CA  . ILE A 264  ? 0.2160 0.2119 0.2474 -0.0043 -0.0013 0.0105  262  ILE A CA  
1836  C C   . ILE A 264  ? 0.2336 0.2246 0.2656 -0.0041 0.0005  0.0124  262  ILE A C   
1837  O O   . ILE A 264  ? 0.2188 0.2080 0.2539 -0.0043 0.0011  0.0141  262  ILE A O   
1838  C CB  . ILE A 264  ? 0.1996 0.1974 0.2271 -0.0041 -0.0009 0.0128  262  ILE A CB  
1839  C CG1 . ILE A 264  ? 0.2154 0.2128 0.2384 -0.0039 -0.0002 0.0132  262  ILE A CG1 
1840  C CG2 . ILE A 264  ? 0.2231 0.2186 0.2516 -0.0039 0.0003  0.0160  262  ILE A CG2 
1841  C CD1 . ILE A 264  ? 0.2413 0.2410 0.2612 -0.0039 -0.0001 0.0156  262  ILE A CD1 
1842  N N   . SER A 265  ? 0.1994 0.1886 0.2285 -0.0039 0.0013  0.0123  263  SER A N   
1843  C CA  . SER A 265  ? 0.2137 0.1989 0.2423 -0.0036 0.0030  0.0143  263  SER A CA  
1844  C C   . SER A 265  ? 0.2610 0.2456 0.2849 -0.0032 0.0041  0.0159  263  SER A C   
1845  O O   . SER A 265  ? 0.2882 0.2749 0.3092 -0.0032 0.0035  0.0150  263  SER A O   
1846  C CB  . SER A 265  ? 0.2376 0.2208 0.2676 -0.0036 0.0028  0.0126  263  SER A CB  
1847  O OG  . SER A 265  ? 0.2884 0.2713 0.3238 -0.0040 0.0018  0.0115  263  SER A OG  
1848  N N   . ILE A 266  ? 0.2246 0.2068 0.2480 -0.0028 0.0055  0.0184  264  ILE A N   
1849  C CA  . ILE A 266  ? 0.2084 0.1896 0.2280 -0.0023 0.0064  0.0198  264  ILE A CA  
1850  C C   . ILE A 266  ? 0.2181 0.1962 0.2369 -0.0018 0.0079  0.0207  264  ILE A C   
1851  O O   . ILE A 266  ? 0.2278 0.2046 0.2491 -0.0018 0.0084  0.0210  264  ILE A O   
1852  C CB  . ILE A 266  ? 0.2322 0.2142 0.2518 -0.0020 0.0065  0.0218  264  ILE A CB  
1853  C CG1 . ILE A 266  ? 0.2575 0.2381 0.2798 -0.0016 0.0076  0.0232  264  ILE A CG1 
1854  C CG2 . ILE A 266  ? 0.2519 0.2375 0.2724 -0.0025 0.0050  0.0212  264  ILE A CG2 
1855  C CD1 . ILE A 266  ? 0.2696 0.2504 0.2918 -0.0010 0.0079  0.0249  264  ILE A CD1 
1856  N N   . LYS A 267  ? 0.2100 0.1870 0.2254 -0.0014 0.0084  0.0211  265  LYS A N   
1857  C CA  . LYS A 267  ? 0.2211 0.1955 0.2353 -0.0008 0.0097  0.0219  265  LYS A CA  
1858  C C   . LYS A 267  ? 0.2131 0.1868 0.2259 -0.0001 0.0103  0.0234  265  LYS A C   
1859  O O   . LYS A 267  ? 0.2194 0.1938 0.2306 -0.0002 0.0097  0.0237  265  LYS A O   
1860  C CB  . LYS A 267  ? 0.2453 0.2189 0.2570 -0.0008 0.0096  0.0207  265  LYS A CB  
1861  C CG  . LYS A 267  ? 0.2933 0.2667 0.3069 -0.0011 0.0092  0.0193  265  LYS A CG  
1862  C CD  . LYS A 267  ? 0.3270 0.2998 0.3383 -0.0010 0.0092  0.0180  265  LYS A CD  
1863  C CE  . LYS A 267  ? 0.4140 0.3860 0.4277 -0.0011 0.0088  0.0167  265  LYS A CE  
1864  N NZ  . LYS A 267  ? 0.3996 0.3735 0.4166 -0.0016 0.0074  0.0150  265  LYS A NZ  
1865  N N   . LEU A 268  ? 0.2253 0.1981 0.2391 0.0007  0.0115  0.0245  266  LEU A N   
1866  C CA  . LEU A 268  ? 0.2066 0.1788 0.2196 0.0016  0.0119  0.0254  266  LEU A CA  
1867  C C   . LEU A 268  ? 0.2027 0.1734 0.2127 0.0019  0.0119  0.0251  266  LEU A C   
1868  O O   . LEU A 268  ? 0.2376 0.2080 0.2473 0.0023  0.0115  0.0255  266  LEU A O   
1869  C CB  . LEU A 268  ? 0.2083 0.1806 0.2228 0.0025  0.0133  0.0263  266  LEU A CB  
1870  C CG  . LEU A 268  ? 0.2271 0.2011 0.2451 0.0022  0.0133  0.0270  266  LEU A CG  
1871  C CD1 . LEU A 268  ? 0.2286 0.2034 0.2480 0.0031  0.0148  0.0281  266  LEU A CD1 
1872  C CD2 . LEU A 268  ? 0.2694 0.2447 0.2887 0.0020  0.0123  0.0272  266  LEU A CD2 
1873  N N   . SER A 269  ? 0.2148 0.1846 0.2233 0.0017  0.0122  0.0243  267  SER A N   
1874  C CA  . SER A 269  ? 0.2308 0.1993 0.2366 0.0020  0.0121  0.0239  267  SER A CA  
1875  C C   . SER A 269  ? 0.2580 0.2274 0.2630 0.0011  0.0109  0.0240  267  SER A C   
1876  O O   . SER A 269  ? 0.2420 0.2104 0.2456 0.0012  0.0107  0.0241  267  SER A O   
1877  C CB  . SER A 269  ? 0.2326 0.2002 0.2370 0.0020  0.0126  0.0231  267  SER A CB  
1878  O OG  . SER A 269  ? 0.2645 0.2330 0.2690 0.0010  0.0119  0.0222  267  SER A OG  
1879  N N   . ALA A 270  ? 0.2351 0.2066 0.2411 0.0003  0.0101  0.0239  268  ALA A N   
1880  C CA  . ALA A 270  ? 0.2252 0.1985 0.2304 -0.0006 0.0090  0.0243  268  ALA A CA  
1881  C C   . ALA A 270  ? 0.2352 0.2085 0.2415 -0.0003 0.0084  0.0260  268  ALA A C   
1882  O O   . ALA A 270  ? 0.2309 0.2053 0.2365 -0.0010 0.0075  0.0270  268  ALA A O   
1883  C CB  . ALA A 270  ? 0.2245 0.2008 0.2304 -0.0014 0.0082  0.0234  268  ALA A CB  
1884  N N   . LEU A 271  ? 0.2248 0.1972 0.2329 0.0005  0.0089  0.0264  269  LEU A N   
1885  C CA  . LEU A 271  ? 0.2395 0.2124 0.2493 0.0008  0.0082  0.0277  269  LEU A CA  
1886  C C   . LEU A 271  ? 0.2151 0.1855 0.2252 0.0019  0.0084  0.0281  269  LEU A C   
1887  O O   . LEU A 271  ? 0.2487 0.2191 0.2607 0.0022  0.0076  0.0292  269  LEU A O   
1888  C CB  . LEU A 271  ? 0.2356 0.2098 0.2477 0.0010  0.0084  0.0278  269  LEU A CB  
1889  C CG  . LEU A 271  ? 0.2521 0.2291 0.2646 -0.0001 0.0076  0.0273  269  LEU A CG  
1890  C CD1 . LEU A 271  ? 0.2882 0.2662 0.3035 0.0002  0.0078  0.0273  269  LEU A CD1 
1891  C CD2 . LEU A 271  ? 0.2431 0.2222 0.2551 -0.0008 0.0062  0.0285  269  LEU A CD2 
1892  N N   . HIS A 272  ? 0.2398 0.2083 0.2484 0.0024  0.0092  0.0271  270  HIS A N   
1893  C CA  . HIS A 272  ? 0.2334 0.1999 0.2425 0.0035  0.0091  0.0269  270  HIS A CA  
1894  C C   . HIS A 272  ? 0.2393 0.2043 0.2461 0.0035  0.0095  0.0259  270  HIS A C   
1895  O O   . HIS A 272  ? 0.2451 0.2104 0.2505 0.0035  0.0105  0.0251  270  HIS A O   
1896  C CB  . HIS A 272  ? 0.2406 0.2069 0.2512 0.0051  0.0100  0.0264  270  HIS A CB  
1897  C CG  . HIS A 272  ? 0.2587 0.2234 0.2706 0.0064  0.0095  0.0260  270  HIS A CG  
1898  N ND1 . HIS A 272  ? 0.3048 0.2678 0.3157 0.0072  0.0096  0.0247  270  HIS A ND1 
1899  C CD2 . HIS A 272  ? 0.2927 0.2573 0.3074 0.0071  0.0086  0.0265  270  HIS A CD2 
1900  C CE1 . HIS A 272  ? 0.2911 0.2529 0.3042 0.0083  0.0088  0.0243  270  HIS A CE1 
1901  N NE2 . HIS A 272  ? 0.3126 0.2752 0.3280 0.0084  0.0082  0.0254  270  HIS A NE2 
1902  N N   . PRO A 273  ? 0.2424 0.2058 0.2491 0.0036  0.0087  0.0260  271  PRO A N   
1903  C CA  . PRO A 273  ? 0.2219 0.1841 0.2266 0.0036  0.0090  0.0249  271  PRO A CA  
1904  C C   . PRO A 273  ? 0.2848 0.2460 0.2889 0.0052  0.0101  0.0233  271  PRO A C   
1905  O O   . PRO A 273  ? 0.2849 0.2455 0.2871 0.0053  0.0105  0.0223  271  PRO A O   
1906  C CB  . PRO A 273  ? 0.2592 0.2202 0.2650 0.0030  0.0075  0.0258  271  PRO A CB  
1907  C CG  . PRO A 273  ? 0.2724 0.2329 0.2812 0.0037  0.0067  0.0267  271  PRO A CG  
1908  C CD  . PRO A 273  ? 0.2750 0.2377 0.2841 0.0035  0.0073  0.0273  271  PRO A CD  
1909  N N   . ARG A 274  ? 0.2420 0.2034 0.2476 0.0066  0.0105  0.0229  272  ARG A N   
1910  C CA  . ARG A 274  ? 0.2286 0.1901 0.2335 0.0082  0.0116  0.0214  272  ARG A CA  
1911  C C   . ARG A 274  ? 0.2261 0.1897 0.2314 0.0087  0.0130  0.0218  272  ARG A C   
1912  O O   . ARG A 274  ? 0.2634 0.2281 0.2700 0.0102  0.0136  0.0213  272  ARG A O   
1913  C CB  . ARG A 274  ? 0.2238 0.1842 0.2304 0.0098  0.0109  0.0202  272  ARG A CB  
1914  C CG  . ARG A 274  ? 0.2382 0.1963 0.2453 0.0092  0.0093  0.0199  272  ARG A CG  
1915  C CD  . ARG A 274  ? 0.2544 0.2121 0.2587 0.0089  0.0097  0.0190  272  ARG A CD  
1916  N NE  . ARG A 274  ? 0.2859 0.2446 0.2886 0.0105  0.0110  0.0173  272  ARG A NE  
1917  C CZ  . ARG A 274  ? 0.2590 0.2174 0.2622 0.0123  0.0107  0.0152  272  ARG A CZ  
1918  N NH1 . ARG A 274  ? 0.2669 0.2235 0.2728 0.0127  0.0091  0.0144  272  ARG A NH1 
1919  N NH2 . ARG A 274  ? 0.2925 0.2528 0.2939 0.0137  0.0120  0.0139  272  ARG A NH2 
1920  N N   . TYR A 275  ? 0.2114 0.1759 0.2160 0.0075  0.0135  0.0227  273  TYR A N   
1921  C CA  . TYR A 275  ? 0.2013 0.1676 0.2069 0.0077  0.0146  0.0234  273  TYR A CA  
1922  C C   . TYR A 275  ? 0.2325 0.1995 0.2366 0.0086  0.0159  0.0230  273  TYR A C   
1923  O O   . TYR A 275  ? 0.2446 0.2113 0.2473 0.0079  0.0162  0.0231  273  TYR A O   
1924  C CB  . TYR A 275  ? 0.2245 0.1913 0.2305 0.0060  0.0142  0.0242  273  TYR A CB  
1925  C CG  . TYR A 275  ? 0.2160 0.1845 0.2237 0.0059  0.0151  0.0250  273  TYR A CG  
1926  C CD1 . TYR A 275  ? 0.2186 0.1886 0.2283 0.0068  0.0158  0.0256  273  TYR A CD1 
1927  C CD2 . TYR A 275  ? 0.2210 0.1896 0.2286 0.0049  0.0153  0.0252  273  TYR A CD2 
1928  C CE1 . TYR A 275  ? 0.2411 0.2128 0.2526 0.0065  0.0166  0.0266  273  TYR A CE1 
1929  C CE2 . TYR A 275  ? 0.2215 0.1914 0.2312 0.0047  0.0159  0.0261  273  TYR A CE2 
1930  C CZ  . TYR A 275  ? 0.2226 0.1942 0.2343 0.0054  0.0166  0.0270  273  TYR A CZ  
1931  O OH  . TYR A 275  ? 0.2550 0.2282 0.2693 0.0051  0.0173  0.0282  273  TYR A OH  
1932  N N   . SER A 276  ? 0.2191 0.1874 0.2234 0.0103  0.0167  0.0224  274  SER A N   
1933  C CA  . SER A 276  ? 0.2142 0.1841 0.2170 0.0113  0.0180  0.0222  274  SER A CA  
1934  C C   . SER A 276  ? 0.2369 0.2097 0.2409 0.0131  0.0190  0.0220  274  SER A C   
1935  O O   . SER A 276  ? 0.2354 0.2081 0.2410 0.0139  0.0184  0.0212  274  SER A O   
1936  C CB  . SER A 276  ? 0.2729 0.2413 0.2732 0.0119  0.0175  0.0207  274  SER A CB  
1937  O OG  . SER A 276  ? 0.3153 0.2832 0.3162 0.0132  0.0168  0.0189  274  SER A OG  
1938  N N   . ARG A 277  ? 0.2429 0.2184 0.2460 0.0138  0.0204  0.0227  275  ARG A N   
1939  C CA  . ARG A 277  ? 0.2076 0.1869 0.2115 0.0157  0.0216  0.0225  275  ARG A CA  
1940  C C   . ARG A 277  ? 0.2334 0.2126 0.2366 0.0176  0.0210  0.0196  275  ARG A C   
1941  O O   . ARG A 277  ? 0.2382 0.2194 0.2431 0.0191  0.0212  0.0187  275  ARG A O   
1942  C CB  . ARG A 277  ? 0.2433 0.2260 0.2459 0.0160  0.0232  0.0240  275  ARG A CB  
1943  C CG  . ARG A 277  ? 0.2410 0.2289 0.2439 0.0182  0.0246  0.0236  275  ARG A CG  
1944  C CD  . ARG A 277  ? 0.2454 0.2352 0.2515 0.0183  0.0250  0.0243  275  ARG A CD  
1945  N NE  . ARG A 277  ? 0.2297 0.2250 0.2360 0.0205  0.0264  0.0239  275  ARG A NE  
1946  C CZ  . ARG A 277  ? 0.2460 0.2426 0.2521 0.0227  0.0261  0.0209  275  ARG A CZ  
1947  N NH1 . ARG A 277  ? 0.2442 0.2366 0.2501 0.0230  0.0244  0.0183  275  ARG A NH1 
1948  N NH2 . ARG A 277  ? 0.2416 0.2442 0.2481 0.0247  0.0276  0.0204  275  ARG A NH2 
1949  N N   . ALA A 278  ? 0.2524 0.2294 0.2535 0.0177  0.0202  0.0181  276  ALA A N   
1950  C CA  . ALA A 278  ? 0.2626 0.2392 0.2636 0.0196  0.0193  0.0151  276  ALA A CA  
1951  C C   . ALA A 278  ? 0.2474 0.2218 0.2513 0.0196  0.0179  0.0143  276  ALA A C   
1952  O O   . ALA A 278  ? 0.2684 0.2434 0.2737 0.0215  0.0173  0.0120  276  ALA A O   
1953  C CB  . ALA A 278  ? 0.2616 0.2359 0.2603 0.0193  0.0184  0.0138  276  ALA A CB  
1954  N N   . GLN A 279  ? 0.2303 0.2023 0.2354 0.0176  0.0172  0.0162  277  GLN A N   
1955  C CA  . GLN A 279  ? 0.2160 0.1860 0.2239 0.0173  0.0157  0.0161  277  GLN A CA  
1956  C C   . GLN A 279  ? 0.2857 0.2576 0.2958 0.0170  0.0164  0.0177  277  GLN A C   
1957  O O   . GLN A 279  ? 0.2452 0.2156 0.2571 0.0159  0.0153  0.0188  277  GLN A O   
1958  C CB  . GLN A 279  ? 0.2427 0.2092 0.2503 0.0152  0.0143  0.0171  277  GLN A CB  
1959  C CG  . GLN A 279  ? 0.2674 0.2319 0.2732 0.0153  0.0135  0.0156  277  GLN A CG  
1960  C CD  . GLN A 279  ? 0.3374 0.3010 0.3452 0.0170  0.0123  0.0132  277  GLN A CD  
1961  O OE1 . GLN A 279  ? 0.3943 0.3567 0.4051 0.0172  0.0111  0.0133  277  GLN A OE1 
1962  N NE2 . GLN A 279  ? 0.2665 0.2307 0.2727 0.0184  0.0125  0.0109  277  GLN A NE2 
1963  N N   . ALA A 280  ? 0.2476 0.2234 0.2577 0.0181  0.0181  0.0180  278  ALA A N   
1964  C CA  . ALA A 280  ? 0.2475 0.2254 0.2598 0.0175  0.0188  0.0199  278  ALA A CA  
1965  C C   . ALA A 280  ? 0.2251 0.2025 0.2406 0.0182  0.0176  0.0193  278  ALA A C   
1966  O O   . ALA A 280  ? 0.2540 0.2313 0.2713 0.0170  0.0173  0.0210  278  ALA A O   
1967  C CB  . ALA A 280  ? 0.2614 0.2440 0.2734 0.0187  0.0208  0.0204  278  ALA A CB  
1968  N N   . ALA A 281  ? 0.2293 0.2065 0.2458 0.0202  0.0169  0.0170  279  ALA A N   
1969  C CA  . ALA A 281  ? 0.2600 0.2366 0.2800 0.0210  0.0156  0.0165  279  ALA A CA  
1970  C C   . ALA A 281  ? 0.2632 0.2359 0.2841 0.0190  0.0138  0.0179  279  ALA A C   
1971  O O   . ALA A 281  ? 0.2581 0.2309 0.2815 0.0185  0.0131  0.0192  279  ALA A O   
1972  C CB  . ALA A 281  ? 0.2865 0.2633 0.3078 0.0236  0.0149  0.0132  279  ALA A CB  
1973  N N   . ARG A 282  ? 0.2159 0.1856 0.2348 0.0179  0.0129  0.0179  280  ARG A N   
1974  C CA  . ARG A 282  ? 0.2552 0.2222 0.2748 0.0159  0.0113  0.0196  280  ARG A CA  
1975  C C   . ARG A 282  ? 0.2428 0.2110 0.2616 0.0140  0.0119  0.0219  280  ARG A C   
1976  O O   . ARG A 282  ? 0.2532 0.2209 0.2735 0.0128  0.0108  0.0235  280  ARG A O   
1977  C CB  . ARG A 282  ? 0.2664 0.2305 0.2841 0.0151  0.0104  0.0192  280  ARG A CB  
1978  C CG  . ARG A 282  ? 0.3263 0.2887 0.3457 0.0167  0.0091  0.0169  280  ARG A CG  
1979  C CD  . ARG A 282  ? 0.2929 0.2523 0.3113 0.0153  0.0079  0.0172  280  ARG A CD  
1980  N NE  . ARG A 282  ? 0.2993 0.2575 0.3188 0.0133  0.0066  0.0199  280  ARG A NE  
1981  C CZ  . ARG A 282  ? 0.2710 0.2278 0.2892 0.0114  0.0059  0.0212  280  ARG A CZ  
1982  N NH1 . ARG A 282  ? 0.2574 0.2134 0.2734 0.0113  0.0062  0.0200  280  ARG A NH1 
1983  N NH2 . ARG A 282  ? 0.2711 0.2278 0.2903 0.0097  0.0048  0.0238  280  ARG A NH2 
1984  N N   . VAL A 283  ? 0.2318 0.2016 0.2484 0.0136  0.0136  0.0221  281  VAL A N   
1985  C CA  . VAL A 283  ? 0.2227 0.1936 0.2391 0.0119  0.0141  0.0239  281  VAL A CA  
1986  C C   . VAL A 283  ? 0.2541 0.2271 0.2736 0.0122  0.0141  0.0248  281  VAL A C   
1987  O O   . VAL A 283  ? 0.2471 0.2200 0.2676 0.0108  0.0132  0.0260  281  VAL A O   
1988  C CB  . VAL A 283  ? 0.2113 0.1836 0.2257 0.0117  0.0157  0.0240  281  VAL A CB  
1989  C CG1 . VAL A 283  ? 0.2703 0.2439 0.2857 0.0102  0.0161  0.0256  281  VAL A CG1 
1990  C CG2 . VAL A 283  ? 0.2450 0.2151 0.2565 0.0112  0.0154  0.0233  281  VAL A CG2 
1991  N N   . MET A 284  ? 0.2312 0.2064 0.2522 0.0140  0.0150  0.0240  282  MET A N   
1992  C CA  . MET A 284  ? 0.2307 0.2083 0.2548 0.0142  0.0151  0.0249  282  MET A CA  
1993  C C   . MET A 284  ? 0.2411 0.2172 0.2676 0.0145  0.0132  0.0249  282  MET A C   
1994  O O   . MET A 284  ? 0.2752 0.2523 0.3038 0.0138  0.0126  0.0262  282  MET A O   
1995  C CB  . MET A 284  ? 0.2427 0.2237 0.2679 0.0162  0.0167  0.0241  282  MET A CB  
1996  C CG  . MET A 284  ? 0.2649 0.2481 0.2881 0.0160  0.0186  0.0246  282  MET A CG  
1997  S SD  . MET A 284  ? 0.2820 0.2656 0.3056 0.0134  0.0190  0.0271  282  MET A SD  
1998  C CE  . MET A 284  ? 0.2804 0.2672 0.3083 0.0135  0.0191  0.0282  282  MET A CE  
1999  N N   . GLY A 285  ? 0.2394 0.2131 0.2658 0.0154  0.0121  0.0237  283  GLY A N   
2000  C CA  . GLY A 285  ? 0.2403 0.2124 0.2695 0.0156  0.0101  0.0241  283  GLY A CA  
2001  C C   . GLY A 285  ? 0.2575 0.2278 0.2861 0.0135  0.0086  0.0261  283  GLY A C   
2002  O O   . GLY A 285  ? 0.2746 0.2449 0.3057 0.0131  0.0072  0.0274  283  GLY A O   
2003  N N   . GLU A 286  ? 0.2383 0.2076 0.2637 0.0120  0.0090  0.0263  284  GLU A N   
2004  C CA  . GLU A 286  ? 0.2471 0.2151 0.2717 0.0102  0.0075  0.0279  284  GLU A CA  
2005  C C   . GLU A 286  ? 0.2671 0.2367 0.2896 0.0083  0.0081  0.0288  284  GLU A C   
2006  O O   . GLU A 286  ? 0.2797 0.2500 0.3023 0.0070  0.0069  0.0303  284  GLU A O   
2007  C CB  . GLU A 286  ? 0.2675 0.2329 0.2908 0.0101  0.0068  0.0272  284  GLU A CB  
2008  C CG  . GLU A 286  ? 0.2935 0.2569 0.3193 0.0119  0.0059  0.0260  284  GLU A CG  
2009  C CD  . GLU A 286  ? 0.3261 0.2872 0.3505 0.0119  0.0055  0.0248  284  GLU A CD  
2010  O OE1 . GLU A 286  ? 0.3437 0.3042 0.3657 0.0102  0.0054  0.0258  284  GLU A OE1 
2011  O OE2 . GLU A 286  ? 0.3360 0.2960 0.3617 0.0137  0.0053  0.0226  284  GLU A OE2 
2012  N N   . LEU A 287  ? 0.2306 0.2007 0.2511 0.0083  0.0097  0.0278  285  LEU A N   
2013  C CA  A LEU A 287  ? 0.2334 0.2048 0.2526 0.0067  0.0100  0.0283  285  LEU A CA  
2014  C CA  B LEU A 287  ? 0.2340 0.2054 0.2532 0.0067  0.0100  0.0283  285  LEU A CA  
2015  C C   . LEU A 287  ? 0.2639 0.2377 0.2854 0.0065  0.0102  0.0290  285  LEU A C   
2016  O O   . LEU A 287  ? 0.2497 0.2248 0.2714 0.0052  0.0093  0.0297  285  LEU A O   
2017  C CB  A LEU A 287  ? 0.2293 0.2002 0.2461 0.0067  0.0114  0.0273  285  LEU A CB  
2018  C CB  B LEU A 287  ? 0.2297 0.2006 0.2466 0.0068  0.0114  0.0273  285  LEU A CB  
2019  C CG  A LEU A 287  ? 0.2585 0.2295 0.2734 0.0052  0.0114  0.0273  285  LEU A CG  
2020  C CG  B LEU A 287  ? 0.2549 0.2270 0.2713 0.0056  0.0120  0.0275  285  LEU A CG  
2021  C CD1 A LEU A 287  ? 0.2355 0.2056 0.2484 0.0055  0.0126  0.0265  285  LEU A CD1 
2022  C CD1 B LEU A 287  ? 0.2884 0.2610 0.3042 0.0040  0.0107  0.0278  285  LEU A CD1 
2023  C CD2 A LEU A 287  ? 0.3021 0.2751 0.3186 0.0042  0.0113  0.0278  285  LEU A CD2 
2024  C CD2 B LEU A 287  ? 0.2397 0.2111 0.2542 0.0058  0.0132  0.0268  285  LEU A CD2 
2025  N N   . LEU A 288  ? 0.2323 0.2072 0.2555 0.0078  0.0113  0.0287  286  LEU A N   
2026  C CA  . LEU A 288  ? 0.2544 0.2318 0.2802 0.0076  0.0115  0.0294  286  LEU A CA  
2027  C C   . LEU A 288  ? 0.2566 0.2349 0.2843 0.0070  0.0098  0.0303  286  LEU A C   
2028  O O   . LEU A 288  ? 0.2480 0.2280 0.2766 0.0058  0.0095  0.0308  286  LEU A O   
2029  C CB  . LEU A 288  ? 0.2792 0.2582 0.3069 0.0094  0.0128  0.0290  286  LEU A CB  
2030  C CG  . LEU A 288  ? 0.3298 0.3117 0.3609 0.0093  0.0130  0.0298  286  LEU A CG  
2031  C CD1 . LEU A 288  ? 0.2817 0.2648 0.3131 0.0078  0.0136  0.0304  286  LEU A CD1 
2032  C CD2 . LEU A 288  ? 0.4647 0.4486 0.4976 0.0113  0.0142  0.0293  286  LEU A CD2 
2033  N N   . PRO A 289  ? 0.2364 0.2137 0.2650 0.0078  0.0086  0.0307  287  PRO A N   
2034  C CA  . PRO A 289  ? 0.2171 0.1957 0.2476 0.0071  0.0070  0.0321  287  PRO A CA  
2035  C C   . PRO A 289  ? 0.2344 0.2138 0.2629 0.0053  0.0060  0.0327  287  PRO A C   
2036  O O   . PRO A 289  ? 0.2374 0.2191 0.2671 0.0045  0.0050  0.0336  287  PRO A O   
2037  C CB  . PRO A 289  ? 0.2597 0.2365 0.2915 0.0082  0.0058  0.0326  287  PRO A CB  
2038  C CG  . PRO A 289  ? 0.3200 0.2955 0.3519 0.0100  0.0070  0.0309  287  PRO A CG  
2039  C CD  . PRO A 289  ? 0.2731 0.2485 0.3020 0.0093  0.0086  0.0300  287  PRO A CD  
2040  N N   . ARG A 290  ? 0.2316 0.2093 0.2571 0.0046  0.0062  0.0323  288  ARG A N   
2041  C CA  . ARG A 290  ? 0.2372 0.2163 0.2608 0.0030  0.0055  0.0325  288  ARG A CA  
2042  C C   . ARG A 290  ? 0.2259 0.2069 0.2497 0.0022  0.0060  0.0315  288  ARG A C   
2043  O O   . ARG A 290  ? 0.2177 0.2012 0.2417 0.0013  0.0049  0.0317  288  ARG A O   
2044  C CB  . ARG A 290  ? 0.2487 0.2259 0.2694 0.0026  0.0057  0.0321  288  ARG A CB  
2045  C CG  . ARG A 290  ? 0.2642 0.2393 0.2852 0.0031  0.0049  0.0331  288  ARG A CG  
2046  C CD  . ARG A 290  ? 0.3067 0.2799 0.3251 0.0027  0.0051  0.0326  288  ARG A CD  
2047  N NE  . ARG A 290  ? 0.3701 0.3412 0.3899 0.0033  0.0041  0.0335  288  ARG A NE  
2048  C CZ  . ARG A 290  ? 0.3857 0.3543 0.4045 0.0037  0.0044  0.0327  288  ARG A CZ  
2049  N NH1 . ARG A 290  ? 0.3185 0.2865 0.3346 0.0036  0.0057  0.0311  288  ARG A NH1 
2050  N NH2 . ARG A 290  ? 0.4609 0.4275 0.4817 0.0042  0.0032  0.0334  288  ARG A NH2 
2051  N N   . VAL A 291  ? 0.2219 0.2020 0.2459 0.0027  0.0075  0.0305  289  VAL A N   
2052  C CA  . VAL A 291  ? 0.2175 0.1991 0.2427 0.0019  0.0078  0.0298  289  VAL A CA  
2053  C C   . VAL A 291  ? 0.2202 0.2043 0.2486 0.0019  0.0071  0.0304  289  VAL A C   
2054  O O   . VAL A 291  ? 0.2142 0.2004 0.2437 0.0009  0.0063  0.0299  289  VAL A O   
2055  C CB  . VAL A 291  ? 0.2292 0.2097 0.2546 0.0024  0.0095  0.0293  289  VAL A CB  
2056  C CG1 . VAL A 291  ? 0.2209 0.2026 0.2481 0.0014  0.0095  0.0287  289  VAL A CG1 
2057  C CG2 . VAL A 291  ? 0.2575 0.2357 0.2797 0.0025  0.0101  0.0287  289  VAL A CG2 
2058  N N   . LYS A 292  ? 0.2101 0.1942 0.2403 0.0031  0.0074  0.0312  290  LYS A N   
2059  C CA  . LYS A 292  ? 0.2057 0.1922 0.2392 0.0032  0.0067  0.0319  290  LYS A CA  
2060  C C   . LYS A 292  ? 0.2291 0.2176 0.2624 0.0023  0.0048  0.0324  290  LYS A C   
2061  O O   . LYS A 292  ? 0.1945 0.1856 0.2297 0.0016  0.0040  0.0322  290  LYS A O   
2062  C CB  . LYS A 292  ? 0.2139 0.2002 0.2493 0.0048  0.0072  0.0325  290  LYS A CB  
2063  C CG  . LYS A 292  ? 0.2391 0.2281 0.2781 0.0050  0.0064  0.0332  290  LYS A CG  
2064  C CD  . LYS A 292  ? 0.2364 0.2255 0.2777 0.0068  0.0067  0.0336  290  LYS A CD  
2065  C CE  . LYS A 292  ? 0.2568 0.2488 0.3017 0.0068  0.0058  0.0344  290  LYS A CE  
2066  N NZ  . LYS A 292  ? 0.2793 0.2719 0.3270 0.0087  0.0063  0.0344  290  LYS A NZ  
2067  N N   . ALA A 293  ? 0.2108 0.1983 0.2420 0.0023  0.0039  0.0332  291  ALA A N   
2068  C CA  . ALA A 293  ? 0.2130 0.2031 0.2438 0.0015  0.0021  0.0341  291  ALA A CA  
2069  C C   . ALA A 293  ? 0.1845 0.1769 0.2140 0.0002  0.0017  0.0327  291  ALA A C   
2070  O O   . ALA A 293  ? 0.2264 0.2221 0.2567 -0.0004 0.0004  0.0327  291  ALA A O   
2071  C CB  . ALA A 293  ? 0.2062 0.1951 0.2354 0.0015  0.0013  0.0357  291  ALA A CB  
2072  N N   . LEU A 294  ? 0.1944 0.1851 0.2217 -0.0002 0.0026  0.0313  292  LEU A N   
2073  C CA  . LEU A 294  ? 0.2051 0.1978 0.2317 -0.0012 0.0021  0.0295  292  LEU A CA  
2074  C C   . LEU A 294  ? 0.1892 0.1832 0.2191 -0.0014 0.0021  0.0284  292  LEU A C   
2075  O O   . LEU A 294  ? 0.1991 0.1961 0.2299 -0.0021 0.0008  0.0272  292  LEU A O   
2076  C CB  . LEU A 294  ? 0.2169 0.2073 0.2411 -0.0014 0.0031  0.0283  292  LEU A CB  
2077  C CG  . LEU A 294  ? 0.2079 0.1974 0.2289 -0.0014 0.0030  0.0292  292  LEU A CG  
2078  C CD1 . LEU A 294  ? 0.2258 0.2129 0.2448 -0.0015 0.0042  0.0279  292  LEU A CD1 
2079  C CD2 . LEU A 294  ? 0.2284 0.2218 0.2479 -0.0022 0.0015  0.0296  292  LEU A CD2 
2080  N N   . ALA A 295  ? 0.1929 0.1849 0.2250 -0.0008 0.0034  0.0288  293  ALA A N   
2081  C CA  . ALA A 295  ? 0.2141 0.2073 0.2499 -0.0011 0.0034  0.0281  293  ALA A CA  
2082  C C   . ALA A 295  ? 0.2263 0.2227 0.2646 -0.0011 0.0021  0.0286  293  ALA A C   
2083  O O   . ALA A 295  ? 0.1978 0.1965 0.2387 -0.0019 0.0011  0.0275  293  ALA A O   
2084  C CB  . ALA A 295  ? 0.2146 0.2059 0.2521 -0.0004 0.0053  0.0289  293  ALA A CB  
2085  N N   . LEU A 296  ? 0.1841 0.1808 0.2220 -0.0004 0.0017  0.0303  294  LEU A N   
2086  C CA  . LEU A 296  ? 0.1985 0.1984 0.2385 -0.0003 0.0003  0.0311  294  LEU A CA  
2087  C C   . LEU A 296  ? 0.2046 0.2080 0.2435 -0.0013 -0.0015 0.0301  294  LEU A C   
2088  O O   . LEU A 296  ? 0.2073 0.2139 0.2487 -0.0016 -0.0028 0.0295  294  LEU A O   
2089  C CB  . LEU A 296  ? 0.2036 0.2029 0.2434 0.0007  0.0000  0.0332  294  LEU A CB  
2090  C CG  . LEU A 296  ? 0.2459 0.2432 0.2879 0.0020  0.0014  0.0339  294  LEU A CG  
2091  C CD1 . LEU A 296  ? 0.2574 0.2533 0.2989 0.0031  0.0010  0.0355  294  LEU A CD1 
2092  C CD2 . LEU A 296  ? 0.2433 0.2430 0.2895 0.0021  0.0014  0.0339  294  LEU A CD2 
2093  N N   . LEU A 297  ? 0.1887 0.1919 0.2240 -0.0017 -0.0018 0.0297  295  LEU A N   
2094  C CA  . LEU A 297  ? 0.2211 0.2283 0.2549 -0.0024 -0.0034 0.0285  295  LEU A CA  
2095  C C   . LEU A 297  ? 0.2076 0.2158 0.2431 -0.0031 -0.0037 0.0255  295  LEU A C   
2096  O O   . LEU A 297  ? 0.2206 0.2327 0.2574 -0.0034 -0.0052 0.0240  295  LEU A O   
2097  C CB  . LEU A 297  ? 0.2820 0.2893 0.3117 -0.0027 -0.0034 0.0291  295  LEU A CB  
2098  C CG  . LEU A 297  ? 0.2913 0.3039 0.3190 -0.0032 -0.0051 0.0286  295  LEU A CG  
2099  C CD1 . LEU A 297  ? 0.3040 0.3203 0.3328 -0.0031 -0.0066 0.0307  295  LEU A CD1 
2100  C CD2 . LEU A 297  ? 0.3104 0.3227 0.3342 -0.0035 -0.0047 0.0293  295  LEU A CD2 
2101  N N   . ALA A 298  ? 0.2043 0.2089 0.2401 -0.0031 -0.0023 0.0245  296  ALA A N   
2102  C CA  . ALA A 298  ? 0.2201 0.2250 0.2586 -0.0037 -0.0026 0.0218  296  ALA A CA  
2103  C C   . ALA A 298  ? 0.2132 0.2196 0.2565 -0.0039 -0.0033 0.0218  296  ALA A C   
2104  O O   . ALA A 298  ? 0.2093 0.2181 0.2550 -0.0045 -0.0048 0.0194  296  ALA A O   
2105  C CB  . ALA A 298  ? 0.2315 0.2321 0.2699 -0.0037 -0.0010 0.0216  296  ALA A CB  
2106  N N   . LYS A 299  ? 0.1912 0.1963 0.2361 -0.0033 -0.0023 0.0241  297  LYS A N   
2107  C CA  . LYS A 299  ? 0.1878 0.1949 0.2373 -0.0035 -0.0028 0.0243  297  LYS A CA  
2108  C C   . LYS A 299  ? 0.2350 0.2467 0.2850 -0.0037 -0.0051 0.0235  297  LYS A C   
2109  O O   . LYS A 299  ? 0.2345 0.2485 0.2882 -0.0043 -0.0063 0.0219  297  LYS A O   
2110  C CB  . LYS A 299  ? 0.1799 0.1855 0.2305 -0.0026 -0.0014 0.0269  297  LYS A CB  
2111  C CG  . LYS A 299  ? 0.2103 0.2187 0.2649 -0.0025 -0.0022 0.0275  297  LYS A CG  
2112  C CD  . LYS A 299  ? 0.2338 0.2411 0.2900 -0.0015 -0.0007 0.0297  297  LYS A CD  
2113  C CE  . LYS A 299  ? 0.2454 0.2560 0.3049 -0.0011 -0.0018 0.0305  297  LYS A CE  
2114  N NZ  . LYS A 299  ? 0.3358 0.3458 0.3975 0.0000  -0.0003 0.0322  297  LYS A NZ  
2115  N N   . ASN A 300  ? 0.2063 0.2196 0.2527 -0.0033 -0.0057 0.0247  298  ASN A N   
2116  C CA  . ASN A 300  ? 0.2132 0.2315 0.2600 -0.0034 -0.0078 0.0244  298  ASN A CA  
2117  C C   . ASN A 300  ? 0.2029 0.2245 0.2496 -0.0041 -0.0094 0.0210  298  ASN A C   
2118  O O   . ASN A 300  ? 0.2355 0.2611 0.2848 -0.0043 -0.0111 0.0196  298  ASN A O   
2119  C CB  . ASN A 300  ? 0.2600 0.2796 0.3033 -0.0029 -0.0082 0.0269  298  ASN A CB  
2120  C CG  . ASN A 300  ? 0.3194 0.3443 0.3636 -0.0029 -0.0103 0.0274  298  ASN A CG  
2121  O OD1 . ASN A 300  ? 0.4044 0.4299 0.4518 -0.0025 -0.0106 0.0288  298  ASN A OD1 
2122  N ND2 . ASN A 300  ? 0.2772 0.3065 0.3189 -0.0032 -0.0117 0.0263  298  ASN A ND2 
2123  N N   . TYR A 301  ? 0.1923 0.2125 0.2363 -0.0043 -0.0089 0.0194  299  TYR A N   
2124  C CA  . TYR A 301  ? 0.2040 0.2272 0.2484 -0.0047 -0.0104 0.0156  299  TYR A CA  
2125  C C   . TYR A 301  ? 0.2176 0.2385 0.2668 -0.0052 -0.0105 0.0132  299  TYR A C   
2126  O O   . TYR A 301  ? 0.2337 0.2572 0.2845 -0.0055 -0.0121 0.0096  299  TYR A O   
2127  C CB  . TYR A 301  ? 0.2073 0.2303 0.2472 -0.0046 -0.0099 0.0148  299  TYR A CB  
2128  C CG  . TYR A 301  ? 0.2064 0.2331 0.2417 -0.0044 -0.0104 0.0165  299  TYR A CG  
2129  C CD1 . TYR A 301  ? 0.2290 0.2624 0.2636 -0.0044 -0.0124 0.0152  299  TYR A CD1 
2130  C CD2 . TYR A 301  ? 0.2086 0.2326 0.2408 -0.0042 -0.0090 0.0195  299  TYR A CD2 
2131  C CE1 . TYR A 301  ? 0.2190 0.2565 0.2496 -0.0043 -0.0128 0.0173  299  TYR A CE1 
2132  C CE2 . TYR A 301  ? 0.2209 0.2484 0.2494 -0.0042 -0.0095 0.0215  299  TYR A CE2 
2133  C CZ  . TYR A 301  ? 0.2774 0.3117 0.3051 -0.0043 -0.0114 0.0207  299  TYR A CZ  
2134  O OH  . TYR A 301  ? 0.2341 0.2725 0.2584 -0.0044 -0.0119 0.0232  299  TYR A OH  
2135  N N   . ASP A 302  ? 0.1987 0.2154 0.2505 -0.0053 -0.0088 0.0151  300  ASP A N   
2136  C CA  . ASP A 302  ? 0.2073 0.2215 0.2640 -0.0059 -0.0086 0.0139  300  ASP A CA  
2137  C C   . ASP A 302  ? 0.2111 0.2236 0.2670 -0.0062 -0.0087 0.0112  300  ASP A C   
2138  O O   . ASP A 302  ? 0.2151 0.2285 0.2746 -0.0066 -0.0103 0.0081  300  ASP A O   
2139  C CB  . ASP A 302  ? 0.2215 0.2388 0.2835 -0.0065 -0.0106 0.0122  300  ASP A CB  
2140  C CG  . ASP A 302  ? 0.2684 0.2829 0.3363 -0.0072 -0.0099 0.0127  300  ASP A CG  
2141  O OD1 . ASP A 302  ? 0.2522 0.2633 0.3198 -0.0070 -0.0077 0.0155  300  ASP A OD1 
2142  O OD2 . ASP A 302  ? 0.2922 0.3082 0.3652 -0.0079 -0.0117 0.0103  300  ASP A OD2 
2143  N N   . ILE A 303  ? 0.2031 0.2128 0.2547 -0.0058 -0.0071 0.0125  301  ILE A N   
2144  C CA  . ILE A 303  ? 0.2069 0.2143 0.2576 -0.0059 -0.0069 0.0105  301  ILE A CA  
2145  C C   . ILE A 303  ? 0.2154 0.2178 0.2663 -0.0058 -0.0047 0.0130  301  ILE A C   
2146  O O   . ILE A 303  ? 0.2045 0.2056 0.2547 -0.0055 -0.0032 0.0160  301  ILE A O   
2147  C CB  . ILE A 303  ? 0.1977 0.2071 0.2429 -0.0054 -0.0072 0.0094  301  ILE A CB  
2148  C CG1 . ILE A 303  ? 0.1951 0.2028 0.2357 -0.0049 -0.0054 0.0129  301  ILE A CG1 
2149  C CG2 . ILE A 303  ? 0.1975 0.2130 0.2421 -0.0053 -0.0093 0.0073  301  ILE A CG2 
2150  C CD1 . ILE A 303  ? 0.2270 0.2364 0.2626 -0.0047 -0.0054 0.0123  301  ILE A CD1 
2151  N N   . GLY A 304  ? 0.2197 0.2198 0.2717 -0.0061 -0.0046 0.0115  302  GLY A N   
2152  C CA  . GLY A 304  ? 0.1985 0.1943 0.2501 -0.0060 -0.0025 0.0138  302  GLY A CA  
2153  C C   . GLY A 304  ? 0.2123 0.2069 0.2578 -0.0052 -0.0011 0.0152  302  GLY A C   
2154  O O   . GLY A 304  ? 0.2157 0.2121 0.2575 -0.0050 -0.0018 0.0138  302  GLY A O   
2155  N N   . LEU A 305  ? 0.1892 0.1811 0.2337 -0.0049 0.0009  0.0180  303  LEU A N   
2156  C CA  . LEU A 305  ? 0.1800 0.1701 0.2196 -0.0042 0.0023  0.0193  303  LEU A CA  
2157  C C   . LEU A 305  ? 0.2209 0.2078 0.2613 -0.0041 0.0039  0.0205  303  LEU A C   
2158  O O   . LEU A 305  ? 0.2133 0.1996 0.2557 -0.0039 0.0051  0.0226  303  LEU A O   
2159  C CB  . LEU A 305  ? 0.2151 0.2059 0.2525 -0.0036 0.0029  0.0214  303  LEU A CB  
2160  C CG  . LEU A 305  ? 0.2461 0.2352 0.2788 -0.0029 0.0040  0.0225  303  LEU A CG  
2161  C CD1 . LEU A 305  ? 0.2388 0.2295 0.2696 -0.0026 0.0035  0.0237  303  LEU A CD1 
2162  C CD2 . LEU A 305  ? 0.3044 0.2905 0.3370 -0.0023 0.0059  0.0241  303  LEU A CD2 
2163  N N   . ASN A 306  ? 0.2161 0.2013 0.2549 -0.0041 0.0040  0.0193  304  ASN A N   
2164  C CA  . ASN A 306  ? 0.2283 0.2107 0.2680 -0.0041 0.0052  0.0204  304  ASN A CA  
2165  C C   . ASN A 306  ? 0.2266 0.2072 0.2614 -0.0032 0.0067  0.0216  304  ASN A C   
2166  O O   . ASN A 306  ? 0.2303 0.2111 0.2614 -0.0030 0.0063  0.0205  304  ASN A O   
2167  C CB  . ASN A 306  ? 0.2027 0.1842 0.2446 -0.0045 0.0040  0.0182  304  ASN A CB  
2168  C CG  . ASN A 306  ? 0.2211 0.1997 0.2633 -0.0044 0.0052  0.0195  304  ASN A CG  
2169  O OD1 . ASN A 306  ? 0.2921 0.2694 0.3307 -0.0040 0.0057  0.0190  304  ASN A OD1 
2170  N ND2 . ASN A 306  ? 0.2150 0.1930 0.2616 -0.0049 0.0056  0.0215  304  ASN A ND2 
2171  N N   . ILE A 307  ? 0.1986 0.1779 0.2337 -0.0028 0.0084  0.0238  305  ILE A N   
2172  C CA  . ILE A 307  ? 0.1963 0.1739 0.2273 -0.0020 0.0097  0.0247  305  ILE A CA  
2173  C C   . ILE A 307  ? 0.2003 0.1760 0.2313 -0.0021 0.0100  0.0244  305  ILE A C   
2174  O O   . ILE A 307  ? 0.2089 0.1841 0.2429 -0.0023 0.0106  0.0259  305  ILE A O   
2175  C CB  . ILE A 307  ? 0.2192 0.1970 0.2500 -0.0011 0.0113  0.0269  305  ILE A CB  
2176  C CG1 . ILE A 307  ? 0.2510 0.2306 0.2820 -0.0009 0.0109  0.0271  305  ILE A CG1 
2177  C CG2 . ILE A 307  ? 0.2454 0.2216 0.2721 -0.0002 0.0125  0.0273  305  ILE A CG2 
2178  C CD1 . ILE A 307  ? 0.2900 0.2704 0.3219 0.0000  0.0123  0.0289  305  ILE A CD1 
2179  N N   . ASP A 308  ? 0.2011 0.1759 0.2290 -0.0020 0.0095  0.0228  306  ASP A N   
2180  C CA  . ASP A 308  ? 0.1969 0.1700 0.2248 -0.0020 0.0096  0.0223  306  ASP A CA  
2181  C C   . ASP A 308  ? 0.2211 0.1929 0.2473 -0.0013 0.0114  0.0245  306  ASP A C   
2182  O O   . ASP A 308  ? 0.2253 0.1974 0.2490 -0.0005 0.0124  0.0255  306  ASP A O   
2183  C CB  . ASP A 308  ? 0.2463 0.2193 0.2709 -0.0019 0.0088  0.0201  306  ASP A CB  
2184  C CG  . ASP A 308  ? 0.2750 0.2498 0.3015 -0.0025 0.0070  0.0175  306  ASP A CG  
2185  O OD1 . ASP A 308  ? 0.2667 0.2422 0.2974 -0.0030 0.0061  0.0171  306  ASP A OD1 
2186  O OD2 . ASP A 308  ? 0.3224 0.2981 0.3463 -0.0024 0.0064  0.0156  306  ASP A OD2 
2187  N N   . ALA A 309  ? 0.2111 0.1816 0.2390 -0.0014 0.0116  0.0252  307  ALA A N   
2188  C CA  . ALA A 309  ? 0.2157 0.1856 0.2419 -0.0006 0.0132  0.0272  307  ALA A CA  
2189  C C   . ALA A 309  ? 0.2242 0.1927 0.2465 -0.0001 0.0132  0.0261  307  ALA A C   
2190  O O   . ALA A 309  ? 0.2313 0.1989 0.2540 -0.0005 0.0121  0.0243  307  ALA A O   
2191  C CB  . ALA A 309  ? 0.2015 0.1714 0.2319 -0.0011 0.0135  0.0294  307  ALA A CB  
2192  N N   . GLU A 310  ? 0.2183 0.1868 0.2372 0.0009  0.0145  0.0270  308  GLU A N   
2193  C CA  . GLU A 310  ? 0.2283 0.1956 0.2435 0.0014  0.0145  0.0259  308  GLU A CA  
2194  C C   . GLU A 310  ? 0.2216 0.1887 0.2358 0.0021  0.0157  0.0275  308  GLU A C   
2195  O O   . GLU A 310  ? 0.2260 0.1932 0.2430 0.0018  0.0159  0.0291  308  GLU A O   
2196  C CB  . GLU A 310  ? 0.2378 0.2053 0.2497 0.0017  0.0145  0.0249  308  GLU A CB  
2197  C CG  . GLU A 310  ? 0.2479 0.2162 0.2608 0.0009  0.0133  0.0236  308  GLU A CG  
2198  C CD  . GLU A 310  ? 0.2563 0.2249 0.2664 0.0011  0.0130  0.0231  308  GLU A CD  
2199  O OE1 . GLU A 310  ? 0.2852 0.2532 0.2928 0.0011  0.0127  0.0221  308  GLU A OE1 
2200  O OE2 . GLU A 310  ? 0.2547 0.2241 0.2655 0.0013  0.0131  0.0238  308  GLU A OE2 
2201  N N   . GLU A 311  ? 0.2280 0.1950 0.2384 0.0031  0.0164  0.0272  309  GLU A N   
2202  C CA  . GLU A 311  ? 0.2342 0.2014 0.2432 0.0039  0.0173  0.0284  309  GLU A CA  
2203  C C   . GLU A 311  ? 0.2020 0.1714 0.2125 0.0044  0.0186  0.0308  309  GLU A C   
2204  O O   . GLU A 311  ? 0.2280 0.1987 0.2395 0.0045  0.0190  0.0312  309  GLU A O   
2205  C CB  . GLU A 311  ? 0.2403 0.2070 0.2452 0.0048  0.0175  0.0271  309  GLU A CB  
2206  C CG  . GLU A 311  ? 0.2578 0.2228 0.2611 0.0043  0.0164  0.0251  309  GLU A CG  
2207  C CD  . GLU A 311  ? 0.3051 0.2700 0.3079 0.0038  0.0156  0.0237  309  GLU A CD  
2208  O OE1 . GLU A 311  ? 0.2565 0.2221 0.2608 0.0036  0.0157  0.0242  309  GLU A OE1 
2209  O OE2 . GLU A 311  ? 0.3899 0.3541 0.3909 0.0035  0.0149  0.0223  309  GLU A OE2 
2210  N N   . ALA A 312  ? 0.2101 0.1805 0.2207 0.0048  0.0193  0.0327  310  ALA A N   
2211  C CA  . ALA A 312  ? 0.2070 0.1803 0.2193 0.0052  0.0207  0.0354  310  ALA A CA  
2212  C C   . ALA A 312  ? 0.2020 0.1776 0.2118 0.0066  0.0218  0.0349  310  ALA A C   
2213  O O   . ALA A 312  ? 0.2256 0.2039 0.2372 0.0068  0.0227  0.0365  310  ALA A O   
2214  C CB  . ALA A 312  ? 0.2211 0.1954 0.2334 0.0055  0.0212  0.0377  310  ALA A CB  
2215  N N   . ASP A 313  ? 0.2413 0.2159 0.2474 0.0075  0.0216  0.0326  311  ASP A N   
2216  C CA  . ASP A 313  ? 0.2429 0.2195 0.2472 0.0090  0.0224  0.0317  311  ASP A CA  
2217  C C   . ASP A 313  ? 0.2247 0.2007 0.2303 0.0087  0.0219  0.0306  311  ASP A C   
2218  O O   . ASP A 313  ? 0.2290 0.2064 0.2338 0.0100  0.0223  0.0296  311  ASP A O   
2219  C CB  . ASP A 313  ? 0.2184 0.1945 0.2188 0.0102  0.0223  0.0297  311  ASP A CB  
2220  C CG  . ASP A 313  ? 0.2817 0.2541 0.2809 0.0095  0.0209  0.0275  311  ASP A CG  
2221  O OD1 . ASP A 313  ? 0.2687 0.2393 0.2696 0.0082  0.0200  0.0273  311  ASP A OD1 
2222  O OD2 . ASP A 313  ? 0.3403 0.3120 0.3368 0.0103  0.0206  0.0259  311  ASP A OD2 
2223  N N   . ARG A 314  ? 0.2244 0.1987 0.2324 0.0072  0.0209  0.0307  312  ARG A N   
2224  C CA  . ARG A 314  ? 0.2164 0.1906 0.2260 0.0069  0.0204  0.0301  312  ARG A CA  
2225  C C   . ARG A 314  ? 0.2052 0.1812 0.2187 0.0062  0.0207  0.0319  312  ARG A C   
2226  O O   . ARG A 314  ? 0.2159 0.1925 0.2311 0.0060  0.0204  0.0316  312  ARG A O   
2227  C CB  . ARG A 314  ? 0.2101 0.1815 0.2192 0.0058  0.0188  0.0284  312  ARG A CB  
2228  C CG  . ARG A 314  ? 0.2367 0.2067 0.2425 0.0065  0.0184  0.0267  312  ARG A CG  
2229  C CD  . ARG A 314  ? 0.2601 0.2281 0.2650 0.0054  0.0171  0.0256  312  ARG A CD  
2230  N NE  . ARG A 314  ? 0.2752 0.2421 0.2782 0.0058  0.0165  0.0243  312  ARG A NE  
2231  C CZ  . ARG A 314  ? 0.2558 0.2216 0.2576 0.0050  0.0155  0.0234  312  ARG A CZ  
2232  N NH1 . ARG A 314  ? 0.2535 0.2191 0.2555 0.0040  0.0150  0.0232  312  ARG A NH1 
2233  N NH2 . ARG A 314  ? 0.2828 0.2477 0.2835 0.0052  0.0149  0.0228  312  ARG A NH2 
2234  N N   . LEU A 315  ? 0.2014 0.1786 0.2169 0.0057  0.0213  0.0340  313  LEU A N   
2235  C CA  . LEU A 315  ? 0.2112 0.1900 0.2310 0.0047  0.0215  0.0360  313  LEU A CA  
2236  C C   . LEU A 315  ? 0.2201 0.2021 0.2409 0.0056  0.0226  0.0367  313  LEU A C   
2237  O O   . LEU A 315  ? 0.2132 0.1956 0.2365 0.0051  0.0221  0.0365  313  LEU A O   
2238  C CB  . LEU A 315  ? 0.2110 0.1906 0.2329 0.0041  0.0220  0.0386  313  LEU A CB  
2239  C CG  . LEU A 315  ? 0.2071 0.1870 0.2346 0.0026  0.0214  0.0405  313  LEU A CG  
2240  C CD1 . LEU A 315  ? 0.2325 0.2128 0.2620 0.0020  0.0216  0.0433  313  LEU A CD1 
2241  C CD2 . LEU A 315  ? 0.2411 0.2242 0.2714 0.0025  0.0222  0.0420  313  LEU A CD2 
2242  N N   . GLU A 316  ? 0.2305 0.2155 0.2495 0.0071  0.0241  0.0375  314  GLU A N   
2243  C CA  . GLU A 316  ? 0.2156 0.2044 0.2359 0.0081  0.0252  0.0382  314  GLU A CA  
2244  C C   . GLU A 316  ? 0.2251 0.2129 0.2445 0.0089  0.0246  0.0357  314  GLU A C   
2245  O O   . GLU A 316  ? 0.2323 0.2220 0.2543 0.0090  0.0247  0.0360  314  GLU A O   
2246  C CB  . GLU A 316  ? 0.2366 0.2297 0.2552 0.0096  0.0270  0.0395  314  GLU A CB  
2247  C CG  . GLU A 316  ? 0.2446 0.2394 0.2653 0.0085  0.0276  0.0430  314  GLU A CG  
2248  C CD  . GLU A 316  ? 0.2057 0.2056 0.2247 0.0099  0.0294  0.0448  314  GLU A CD  
2249  O OE1 . GLU A 316  ? 0.2667 0.2708 0.2851 0.0115  0.0306  0.0442  314  GLU A OE1 
2250  O OE2 . GLU A 316  ? 0.2493 0.2494 0.2678 0.0095  0.0296  0.0467  314  GLU A OE2 
2251  N N   . LEU A 317  ? 0.2273 0.2121 0.2435 0.0094  0.0237  0.0333  315  LEU A N   
2252  C CA  . LEU A 317  ? 0.2413 0.2247 0.2572 0.0100  0.0227  0.0313  315  LEU A CA  
2253  C C   . LEU A 317  ? 0.2270 0.2092 0.2458 0.0084  0.0216  0.0317  315  LEU A C   
2254  O O   . LEU A 317  ? 0.2200 0.2032 0.2405 0.0089  0.0213  0.0313  315  LEU A O   
2255  C CB  . LEU A 317  ? 0.2510 0.2313 0.2636 0.0103  0.0218  0.0292  315  LEU A CB  
2256  C CG  . LEU A 317  ? 0.2590 0.2374 0.2716 0.0106  0.0205  0.0275  315  LEU A CG  
2257  C CD1 . LEU A 317  ? 0.2840 0.2648 0.2977 0.0125  0.0211  0.0268  315  LEU A CD1 
2258  C CD2 . LEU A 317  ? 0.3231 0.2985 0.3329 0.0106  0.0196  0.0260  315  LEU A CD2 
2259  N N   . SER A 318  ? 0.2200 0.2004 0.2395 0.0068  0.0208  0.0321  316  SER A N   
2260  C CA  . SER A 318  ? 0.2116 0.1913 0.2337 0.0054  0.0195  0.0320  316  SER A CA  
2261  C C   . SER A 318  ? 0.2278 0.2104 0.2539 0.0052  0.0201  0.0337  316  SER A C   
2262  O O   . SER A 318  ? 0.2231 0.2060 0.2514 0.0046  0.0192  0.0334  316  SER A O   
2263  C CB  . SER A 318  ? 0.2053 0.1829 0.2278 0.0039  0.0185  0.0318  316  SER A CB  
2264  O OG  . SER A 318  ? 0.2048 0.1834 0.2298 0.0032  0.0191  0.0336  316  SER A OG  
2265  N N   . LEU A 319  ? 0.2129 0.1981 0.2402 0.0056  0.0216  0.0356  317  LEU A N   
2266  C CA  . LEU A 319  ? 0.2389 0.2275 0.2702 0.0053  0.0223  0.0374  317  LEU A CA  
2267  C C   . LEU A 319  ? 0.2209 0.2115 0.2523 0.0067  0.0227  0.0366  317  LEU A C   
2268  O O   . LEU A 319  ? 0.2165 0.2089 0.2514 0.0063  0.0225  0.0372  317  LEU A O   
2269  C CB  . LEU A 319  ? 0.2178 0.2095 0.2502 0.0055  0.0240  0.0400  317  LEU A CB  
2270  C CG  . LEU A 319  ? 0.2395 0.2296 0.2732 0.0040  0.0236  0.0415  317  LEU A CG  
2271  C CD1 . LEU A 319  ? 0.2421 0.2360 0.2769 0.0042  0.0253  0.0447  317  LEU A CD1 
2272  C CD2 . LEU A 319  ? 0.2441 0.2328 0.2823 0.0021  0.0221  0.0418  317  LEU A CD2 
2273  N N   . ASP A 320  ? 0.2214 0.2116 0.2495 0.0084  0.0230  0.0349  318  ASP A N   
2274  C CA  . ASP A 320  ? 0.2209 0.2126 0.2496 0.0099  0.0230  0.0338  318  ASP A CA  
2275  C C   . ASP A 320  ? 0.2348 0.2242 0.2647 0.0091  0.0212  0.0329  318  ASP A C   
2276  O O   . ASP A 320  ? 0.2650 0.2561 0.2973 0.0096  0.0210  0.0330  318  ASP A O   
2277  C CB  . ASP A 320  ? 0.2320 0.2235 0.2574 0.0119  0.0234  0.0319  318  ASP A CB  
2278  C CG  . ASP A 320  ? 0.3159 0.3117 0.3407 0.0133  0.0253  0.0327  318  ASP A CG  
2279  O OD1 . ASP A 320  ? 0.3194 0.3194 0.3467 0.0138  0.0265  0.0339  318  ASP A OD1 
2280  O OD2 . ASP A 320  ? 0.3228 0.3180 0.3444 0.0138  0.0258  0.0323  318  ASP A OD2 
2281  N N   . LEU A 321  ? 0.2232 0.2091 0.2514 0.0079  0.0198  0.0322  319  LEU A N   
2282  C CA  A LEU A 321  ? 0.2445 0.2290 0.2737 0.0070  0.0181  0.0316  319  LEU A CA  
2283  C CA  B LEU A 321  ? 0.2445 0.2290 0.2737 0.0070  0.0181  0.0316  319  LEU A CA  
2284  C C   . LEU A 321  ? 0.2438 0.2299 0.2767 0.0056  0.0177  0.0327  319  LEU A C   
2285  O O   . LEU A 321  ? 0.2447 0.2319 0.2798 0.0055  0.0169  0.0327  319  LEU A O   
2286  C CB  A LEU A 321  ? 0.2519 0.2332 0.2782 0.0061  0.0169  0.0306  319  LEU A CB  
2287  C CB  B LEU A 321  ? 0.2520 0.2333 0.2783 0.0062  0.0168  0.0305  319  LEU A CB  
2288  C CG  A LEU A 321  ? 0.2590 0.2386 0.2821 0.0074  0.0170  0.0294  319  LEU A CG  
2289  C CG  B LEU A 321  ? 0.2588 0.2382 0.2822 0.0073  0.0165  0.0294  319  LEU A CG  
2290  C CD1 A LEU A 321  ? 0.2377 0.2147 0.2579 0.0065  0.0163  0.0287  319  LEU A CD1 
2291  C CD1 B LEU A 321  ? 0.2347 0.2134 0.2554 0.0080  0.0176  0.0289  319  LEU A CD1 
2292  C CD2 A LEU A 321  ? 0.2997 0.2789 0.3233 0.0083  0.0160  0.0288  319  LEU A CD2 
2293  C CD2 B LEU A 321  ? 0.2394 0.2168 0.2615 0.0063  0.0148  0.0288  319  LEU A CD2 
2294  N N   . LEU A 322  ? 0.2252 0.2116 0.2593 0.0045  0.0182  0.0337  320  LEU A N   
2295  C CA  . LEU A 322  ? 0.2103 0.1981 0.2487 0.0031  0.0177  0.0347  320  LEU A CA  
2296  C C   . LEU A 322  ? 0.2276 0.2190 0.2693 0.0037  0.0186  0.0360  320  LEU A C   
2297  O O   . LEU A 322  ? 0.2204 0.2129 0.2652 0.0030  0.0176  0.0360  320  LEU A O   
2298  C CB  . LEU A 322  ? 0.1900 0.1774 0.2297 0.0020  0.0181  0.0359  320  LEU A CB  
2299  C CG  . LEU A 322  ? 0.2175 0.2059 0.2624 0.0004  0.0172  0.0368  320  LEU A CG  
2300  C CD1 . LEU A 322  ? 0.2048 0.1917 0.2502 -0.0006 0.0151  0.0347  320  LEU A CD1 
2301  C CD2 . LEU A 322  ? 0.2266 0.2148 0.2737 -0.0006 0.0177  0.0385  320  LEU A CD2 
2302  N N   . GLU A 323  ? 0.2213 0.2148 0.2622 0.0052  0.0203  0.0368  321  GLU A N   
2303  C CA  . GLU A 323  ? 0.2352 0.2328 0.2791 0.0060  0.0214  0.0379  321  GLU A CA  
2304  C C   . GLU A 323  ? 0.2242 0.2220 0.2686 0.0069  0.0204  0.0366  321  GLU A C   
2305  O O   . GLU A 323  ? 0.2381 0.2380 0.2862 0.0064  0.0200  0.0372  321  GLU A O   
2306  C CB  . GLU A 323  ? 0.2471 0.2476 0.2895 0.0076  0.0235  0.0386  321  GLU A CB  
2307  C CG  . GLU A 323  ? 0.3645 0.3697 0.4093 0.0091  0.0246  0.0390  321  GLU A CG  
2308  C CD  . GLU A 323  ? 0.3720 0.3820 0.4197 0.0087  0.0264  0.0419  321  GLU A CD  
2309  O OE1 . GLU A 323  ? 0.4108 0.4203 0.4583 0.0075  0.0269  0.0436  321  GLU A OE1 
2310  O OE2 . GLU A 323  ? 0.3892 0.4037 0.4397 0.0095  0.0273  0.0426  321  GLU A OE2 
2311  N N   . VAL A 324  ? 0.2225 0.2180 0.2636 0.0081  0.0198  0.0348  322  VAL A N   
2312  C CA  . VAL A 324  ? 0.2287 0.2241 0.2706 0.0090  0.0187  0.0339  322  VAL A CA  
2313  C C   . VAL A 324  ? 0.2274 0.2219 0.2712 0.0074  0.0169  0.0340  322  VAL A C   
2314  O O   . VAL A 324  ? 0.2426 0.2391 0.2893 0.0075  0.0163  0.0343  322  VAL A O   
2315  C CB  . VAL A 324  ? 0.2754 0.2681 0.3140 0.0103  0.0182  0.0322  322  VAL A CB  
2316  C CG1 . VAL A 324  ? 0.3024 0.2949 0.3426 0.0111  0.0167  0.0316  322  VAL A CG1 
2317  C CG2 . VAL A 324  ? 0.3019 0.2962 0.3391 0.0122  0.0198  0.0316  322  VAL A CG2 
2318  N N   . LEU A 325  ? 0.2126 0.2047 0.2547 0.0058  0.0159  0.0337  323  LEU A N   
2319  C CA  . LEU A 325  ? 0.1980 0.1898 0.2415 0.0044  0.0141  0.0334  323  LEU A CA  
2320  C C   . LEU A 325  ? 0.2161 0.2107 0.2643 0.0035  0.0141  0.0343  323  LEU A C   
2321  O O   . LEU A 325  ? 0.2059 0.2019 0.2564 0.0032  0.0128  0.0343  323  LEU A O   
2322  C CB  . LEU A 325  ? 0.2001 0.1893 0.2410 0.0032  0.0132  0.0325  323  LEU A CB  
2323  C CG  . LEU A 325  ? 0.2607 0.2474 0.2974 0.0038  0.0128  0.0316  323  LEU A CG  
2324  C CD1 . LEU A 325  ? 0.2407 0.2253 0.2750 0.0027  0.0126  0.0309  323  LEU A CD1 
2325  C CD2 . LEU A 325  ? 0.2598 0.2466 0.2964 0.0039  0.0112  0.0314  323  LEU A CD2 
2326  N N   . CYS A 326  ? 0.2041 0.1997 0.2540 0.0029  0.0154  0.0355  324  CYS A N   
2327  C CA  . CYS A 326  ? 0.1729 0.1711 0.2279 0.0018  0.0152  0.0366  324  CYS A CA  
2328  C C   . CYS A 326  ? 0.2155 0.2172 0.2733 0.0028  0.0160  0.0375  324  CYS A C   
2329  O O   . CYS A 326  ? 0.2206 0.2245 0.2827 0.0019  0.0153  0.0381  324  CYS A O   
2330  C CB  . CYS A 326  ? 0.2060 0.2043 0.2626 0.0008  0.0163  0.0381  324  CYS A CB  
2331  S SG  . CYS A 326  ? 0.2600 0.2545 0.3151 -0.0007 0.0149  0.0367  324  CYS A SG  
2332  N N   . LEU A 327  ? 0.2134 0.2159 0.2692 0.0047  0.0173  0.0375  325  LEU A N   
2333  C CA  . LEU A 327  ? 0.2279 0.2341 0.2864 0.0061  0.0180  0.0379  325  LEU A CA  
2334  C C   . LEU A 327  ? 0.2164 0.2217 0.2746 0.0070  0.0163  0.0367  325  LEU A C   
2335  O O   . LEU A 327  ? 0.2267 0.2349 0.2875 0.0081  0.0165  0.0369  325  LEU A O   
2336  C CB  . LEU A 327  ? 0.2521 0.2603 0.3091 0.0080  0.0201  0.0382  325  LEU A CB  
2337  C CG  . LEU A 327  ? 0.2898 0.2999 0.3475 0.0072  0.0219  0.0401  325  LEU A CG  
2338  C CD1 . LEU A 327  ? 0.3506 0.3635 0.4063 0.0093  0.0240  0.0401  325  LEU A CD1 
2339  C CD2 . LEU A 327  ? 0.3073 0.3209 0.3705 0.0057  0.0221  0.0422  325  LEU A CD2 
2340  N N   . ASP A 328  ? 0.2165 0.2185 0.2719 0.0064  0.0147  0.0356  326  ASP A N   
2341  C CA  . ASP A 328  ? 0.2092 0.2105 0.2643 0.0072  0.0131  0.0349  326  ASP A CA  
2342  C C   . ASP A 328  ? 0.1964 0.1996 0.2549 0.0061  0.0115  0.0353  326  ASP A C   
2343  O O   . ASP A 328  ? 0.2211 0.2235 0.2794 0.0044  0.0103  0.0350  326  ASP A O   
2344  C CB  . ASP A 328  ? 0.2188 0.2163 0.2696 0.0069  0.0120  0.0341  326  ASP A CB  
2345  C CG  . ASP A 328  ? 0.2692 0.2658 0.3195 0.0079  0.0105  0.0339  326  ASP A CG  
2346  O OD1 . ASP A 328  ? 0.2756 0.2741 0.3287 0.0079  0.0093  0.0344  326  ASP A OD1 
2347  O OD2 . ASP A 328  ? 0.2901 0.2841 0.3376 0.0086  0.0103  0.0334  326  ASP A OD2 
2348  N N   . GLY A 329  ? 0.2168 0.2226 0.2784 0.0072  0.0114  0.0357  327  GLY A N   
2349  C CA  . GLY A 329  ? 0.2261 0.2343 0.2912 0.0062  0.0099  0.0361  327  GLY A CA  
2350  C C   . GLY A 329  ? 0.2323 0.2390 0.2957 0.0054  0.0076  0.0356  327  GLY A C   
2351  O O   . GLY A 329  ? 0.2347 0.2432 0.3002 0.0041  0.0062  0.0355  327  GLY A O   
2352  N N   . ASP A 330  ? 0.2156 0.2195 0.2752 0.0060  0.0070  0.0352  328  ASP A N   
2353  C CA  . ASP A 330  ? 0.2339 0.2373 0.2918 0.0051  0.0048  0.0351  328  ASP A CA  
2354  C C   . ASP A 330  ? 0.2071 0.2104 0.2638 0.0032  0.0043  0.0342  328  ASP A C   
2355  O O   . ASP A 330  ? 0.2351 0.2395 0.2912 0.0024  0.0025  0.0339  328  ASP A O   
2356  C CB  . ASP A 330  ? 0.2223 0.2228 0.2766 0.0059  0.0044  0.0353  328  ASP A CB  
2357  C CG  . ASP A 330  ? 0.3134 0.3140 0.3694 0.0077  0.0041  0.0360  328  ASP A CG  
2358  O OD1 . ASP A 330  ? 0.3249 0.3281 0.3845 0.0083  0.0036  0.0364  328  ASP A OD1 
2359  O OD2 . ASP A 330  ? 0.2916 0.2895 0.3456 0.0087  0.0042  0.0359  328  ASP A OD2 
2360  N N   . LEU A 331  ? 0.1881 0.1902 0.2445 0.0027  0.0058  0.0338  329  LEU A N   
2361  C CA  . LEU A 331  ? 0.2145 0.2162 0.2705 0.0011  0.0053  0.0327  329  LEU A CA  
2362  C C   . LEU A 331  ? 0.2158 0.2197 0.2765 0.0000  0.0051  0.0326  329  LEU A C   
2363  O O   . LEU A 331  ? 0.2243 0.2277 0.2857 -0.0013 0.0046  0.0316  329  LEU A O   
2364  C CB  . LEU A 331  ? 0.2167 0.2153 0.2696 0.0010  0.0067  0.0324  329  LEU A CB  
2365  C CG  . LEU A 331  ? 0.2236 0.2199 0.2717 0.0016  0.0064  0.0321  329  LEU A CG  
2366  C CD1 . LEU A 331  ? 0.2299 0.2234 0.2753 0.0018  0.0080  0.0319  329  LEU A CD1 
2367  C CD2 . LEU A 331  ? 0.2357 0.2325 0.2821 0.0006  0.0045  0.0311  329  LEU A CD2 
2368  N N   . SER A 332  ? 0.2115 0.2179 0.2760 0.0005  0.0055  0.0337  330  SER A N   
2369  C CA  . SER A 332  ? 0.2439 0.2527 0.3135 -0.0006 0.0054  0.0339  330  SER A CA  
2370  C C   . SER A 332  ? 0.2445 0.2547 0.3158 -0.0019 0.0030  0.0324  330  SER A C   
2371  O O   . SER A 332  ? 0.2504 0.2611 0.3194 -0.0016 0.0014  0.0316  330  SER A O   
2372  C CB  . SER A 332  ? 0.2595 0.2712 0.3328 0.0004  0.0063  0.0353  330  SER A CB  
2373  O OG  . SER A 332  ? 0.2875 0.3007 0.3611 0.0011  0.0049  0.0352  330  SER A OG  
2374  N N   . GLY A 333  ? 0.2089 0.2198 0.2843 -0.0033 0.0026  0.0320  331  GLY A N   
2375  C CA  . GLY A 333  ? 0.2137 0.2263 0.2914 -0.0045 0.0002  0.0300  331  GLY A CA  
2376  C C   . GLY A 333  ? 0.2163 0.2268 0.2918 -0.0053 -0.0007 0.0279  331  GLY A C   
2377  O O   . GLY A 333  ? 0.2944 0.3063 0.3721 -0.0062 -0.0028 0.0257  331  GLY A O   
2378  N N   . TRP A 334  ? 0.2088 0.2162 0.2801 -0.0048 0.0007  0.0282  332  TRP A N   
2379  C CA  . TRP A 334  ? 0.2244 0.2298 0.2930 -0.0054 -0.0001 0.0262  332  TRP A CA  
2380  C C   . TRP A 334  ? 0.2030 0.2057 0.2727 -0.0058 0.0015  0.0270  332  TRP A C   
2381  O O   . TRP A 334  ? 0.2168 0.2183 0.2850 -0.0050 0.0036  0.0291  332  TRP A O   
2382  C CB  . TRP A 334  ? 0.2212 0.2257 0.2836 -0.0044 0.0000  0.0260  332  TRP A CB  
2383  C CG  . TRP A 334  ? 0.1828 0.1853 0.2417 -0.0046 -0.0002 0.0245  332  TRP A CG  
2384  C CD1 . TRP A 334  ? 0.1978 0.2013 0.2565 -0.0053 -0.0020 0.0218  332  TRP A CD1 
2385  C CD2 . TRP A 334  ? 0.1851 0.1846 0.2397 -0.0040 0.0014  0.0253  332  TRP A CD2 
2386  N NE1 . TRP A 334  ? 0.2016 0.2030 0.2564 -0.0051 -0.0015 0.0210  332  TRP A NE1 
2387  C CE2 . TRP A 334  ? 0.1884 0.1871 0.2406 -0.0044 0.0006  0.0232  332  TRP A CE2 
2388  C CE3 . TRP A 334  ? 0.2010 0.1986 0.2538 -0.0030 0.0034  0.0274  332  TRP A CE3 
2389  C CZ2 . TRP A 334  ? 0.2014 0.1974 0.2495 -0.0040 0.0017  0.0234  332  TRP A CZ2 
2390  C CZ3 . TRP A 334  ? 0.2076 0.2025 0.2564 -0.0026 0.0045  0.0274  332  TRP A CZ3 
2391  C CH2 . TRP A 334  ? 0.2162 0.2102 0.2626 -0.0032 0.0036  0.0255  332  TRP A CH2 
2392  N N   . ASN A 335  ? 0.1978 0.1998 0.2702 -0.0069 0.0003  0.0253  333  ASN A N   
2393  C CA  . ASN A 335  ? 0.1804 0.1798 0.2545 -0.0075 0.0013  0.0261  333  ASN A CA  
2394  C C   . ASN A 335  ? 0.1909 0.1877 0.2609 -0.0073 0.0011  0.0243  333  ASN A C   
2395  O O   . ASN A 335  ? 0.2098 0.2045 0.2819 -0.0080 0.0012  0.0243  333  ASN A O   
2396  C CB  . ASN A 335  ? 0.2198 0.2198 0.3012 -0.0090 0.0000  0.0257  333  ASN A CB  
2397  C CG  . ASN A 335  ? 0.2438 0.2459 0.3298 -0.0093 0.0011  0.0286  333  ASN A CG  
2398  O OD1 . ASN A 335  ? 0.2316 0.2342 0.3155 -0.0084 0.0033  0.0311  333  ASN A OD1 
2399  N ND2 . ASN A 335  ? 0.2933 0.2970 0.3860 -0.0106 -0.0005 0.0280  333  ASN A ND2 
2400  N N   . GLY A 336  ? 0.1999 0.1970 0.2645 -0.0065 0.0007  0.0230  334  GLY A N   
2401  C CA  . GLY A 336  ? 0.1723 0.1676 0.2332 -0.0064 0.0003  0.0211  334  GLY A CA  
2402  C C   . GLY A 336  ? 0.1833 0.1758 0.2401 -0.0057 0.0023  0.0227  334  GLY A C   
2403  O O   . GLY A 336  ? 0.1990 0.1900 0.2532 -0.0057 0.0020  0.0212  334  GLY A O   
2404  N N   . MET A 337  ? 0.2053 0.1973 0.2615 -0.0051 0.0042  0.0254  335  MET A N   
2405  C CA  A MET A 337  ? 0.2091 0.1987 0.2615 -0.0044 0.0060  0.0266  335  MET A CA  
2406  C CA  B MET A 337  ? 0.2092 0.1988 0.2616 -0.0044 0.0060  0.0266  335  MET A CA  
2407  C C   . MET A 337  ? 0.1860 0.1736 0.2404 -0.0050 0.0064  0.0267  335  MET A C   
2408  O O   . MET A 337  ? 0.2230 0.2111 0.2825 -0.0058 0.0065  0.0280  335  MET A O   
2409  C CB  A MET A 337  ? 0.2258 0.2159 0.2776 -0.0034 0.0079  0.0290  335  MET A CB  
2410  C CB  B MET A 337  ? 0.2257 0.2158 0.2775 -0.0034 0.0079  0.0290  335  MET A CB  
2411  C CG  A MET A 337  ? 0.2524 0.2404 0.3000 -0.0024 0.0096  0.0299  335  MET A CG  
2412  C CG  B MET A 337  ? 0.2599 0.2479 0.3082 -0.0025 0.0097  0.0301  335  MET A CG  
2413  S SD  A MET A 337  ? 0.3343 0.3212 0.3762 -0.0017 0.0089  0.0285  335  MET A SD  
2414  S SD  B MET A 337  ? 0.2594 0.2476 0.3038 -0.0009 0.0107  0.0308  335  MET A SD  
2415  C CE  A MET A 337  ? 0.2903 0.2792 0.3325 -0.0008 0.0088  0.0295  335  MET A CE  
2416  C CE  B MET A 337  ? 0.2418 0.2298 0.2833 -0.0012 0.0087  0.0289  335  MET A CE  
2417  N N   . GLY A 338  ? 0.1899 0.1754 0.2407 -0.0047 0.0065  0.0257  336  GLY A N   
2418  C CA  . GLY A 338  ? 0.2027 0.1862 0.2553 -0.0052 0.0066  0.0258  336  GLY A CA  
2419  C C   . GLY A 338  ? 0.2080 0.1895 0.2564 -0.0044 0.0084  0.0271  336  GLY A C   
2420  O O   . GLY A 338  ? 0.2116 0.1931 0.2554 -0.0035 0.0091  0.0271  336  GLY A O   
2421  N N   . PHE A 339  ? 0.1866 0.1667 0.2371 -0.0047 0.0090  0.0284  337  PHE A N   
2422  C CA  . PHE A 339  ? 0.2042 0.1831 0.2511 -0.0039 0.0108  0.0299  337  PHE A CA  
2423  C C   . PHE A 339  ? 0.2069 0.1838 0.2558 -0.0044 0.0104  0.0302  337  PHE A C   
2424  O O   . PHE A 339  ? 0.2132 0.1902 0.2676 -0.0054 0.0098  0.0312  337  PHE A O   
2425  C CB  . PHE A 339  ? 0.2037 0.1844 0.2511 -0.0033 0.0127  0.0328  337  PHE A CB  
2426  C CG  . PHE A 339  ? 0.2260 0.2062 0.2692 -0.0021 0.0145  0.0340  337  PHE A CG  
2427  C CD1 . PHE A 339  ? 0.2236 0.2037 0.2620 -0.0009 0.0151  0.0331  337  PHE A CD1 
2428  C CD2 . PHE A 339  ? 0.2248 0.2050 0.2692 -0.0022 0.0155  0.0362  337  PHE A CD2 
2429  C CE1 . PHE A 339  ? 0.2286 0.2085 0.2635 0.0003  0.0165  0.0339  337  PHE A CE1 
2430  C CE2 . PHE A 339  ? 0.2449 0.2252 0.2853 -0.0010 0.0171  0.0371  337  PHE A CE2 
2431  C CZ  . PHE A 339  ? 0.2570 0.2371 0.2926 0.0003  0.0176  0.0357  337  PHE A CZ  
2432  N N   . VAL A 340  ? 0.2111 0.1862 0.2559 -0.0038 0.0107  0.0293  338  VAL A N   
2433  C CA  . VAL A 340  ? 0.2013 0.1745 0.2477 -0.0041 0.0103  0.0295  338  VAL A CA  
2434  C C   . VAL A 340  ? 0.2134 0.1867 0.2594 -0.0037 0.0122  0.0329  338  VAL A C   
2435  O O   . VAL A 340  ? 0.2175 0.1918 0.2594 -0.0027 0.0138  0.0339  338  VAL A O   
2436  C CB  . VAL A 340  ? 0.2011 0.1727 0.2433 -0.0036 0.0097  0.0268  338  VAL A CB  
2437  C CG1 . VAL A 340  ? 0.2060 0.1756 0.2499 -0.0038 0.0092  0.0269  338  VAL A CG1 
2438  C CG2 . VAL A 340  ? 0.2282 0.2007 0.2704 -0.0039 0.0079  0.0235  338  VAL A CG2 
2439  N N   . VAL A 341  ? 0.1981 0.1707 0.2487 -0.0045 0.0118  0.0347  339  VAL A N   
2440  C CA  A VAL A 341  ? 0.1944 0.1674 0.2446 -0.0042 0.0134  0.0380  339  VAL A CA  
2441  C CA  B VAL A 341  ? 0.1946 0.1677 0.2448 -0.0042 0.0134  0.0380  339  VAL A CA  
2442  C C   . VAL A 341  ? 0.2069 0.1774 0.2585 -0.0044 0.0123  0.0377  339  VAL A C   
2443  O O   . VAL A 341  ? 0.2303 0.1992 0.2865 -0.0053 0.0104  0.0362  339  VAL A O   
2444  C CB  A VAL A 341  ? 0.2167 0.1923 0.2719 -0.0049 0.0142  0.0418  339  VAL A CB  
2445  C CB  B VAL A 341  ? 0.2167 0.1923 0.2719 -0.0049 0.0142  0.0418  339  VAL A CB  
2446  C CG1 A VAL A 341  ? 0.2246 0.2021 0.2775 -0.0041 0.0163  0.0452  339  VAL A CG1 
2447  C CG1 B VAL A 341  ? 0.2305 0.2090 0.2840 -0.0043 0.0155  0.0421  339  VAL A CG1 
2448  C CG2 A VAL A 341  ? 0.2268 0.2047 0.2826 -0.0049 0.0146  0.0415  339  VAL A CG2 
2449  C CG2 B VAL A 341  ? 0.2336 0.2082 0.2961 -0.0065 0.0123  0.0418  339  VAL A CG2 
2450  N N   . GLN A 342  ? 0.2107 0.1809 0.2583 -0.0035 0.0135  0.0388  340  GLN A N   
2451  C CA  . GLN A 342  ? 0.2191 0.1868 0.2669 -0.0034 0.0125  0.0382  340  GLN A CA  
2452  C C   . GLN A 342  ? 0.2113 0.1795 0.2633 -0.0039 0.0129  0.0425  340  GLN A C   
2453  O O   . GLN A 342  ? 0.2289 0.1994 0.2785 -0.0033 0.0148  0.0455  340  GLN A O   
2454  C CB  . GLN A 342  ? 0.2007 0.1679 0.2417 -0.0022 0.0134  0.0366  340  GLN A CB  
2455  C CG  . GLN A 342  ? 0.2184 0.1854 0.2556 -0.0018 0.0129  0.0330  340  GLN A CG  
2456  C CD  . GLN A 342  ? 0.2177 0.1853 0.2486 -0.0006 0.0143  0.0327  340  GLN A CD  
2457  O OE1 . GLN A 342  ? 0.2237 0.1931 0.2532 0.0000  0.0159  0.0348  340  GLN A OE1 
2458  N NE2 . GLN A 342  ? 0.2226 0.1889 0.2499 -0.0002 0.0137  0.0299  340  GLN A NE2 
2459  N N   . ALA A 343  ? 0.1863 0.1526 0.2447 -0.0050 0.0111  0.0426  341  ALA A N   
2460  C CA  . ALA A 343  ? 0.2306 0.1971 0.2941 -0.0057 0.0110  0.0470  341  ALA A CA  
2461  C C   . ALA A 343  ? 0.2503 0.2163 0.3107 -0.0049 0.0117  0.0486  341  ALA A C   
2462  O O   . ALA A 343  ? 0.2278 0.1951 0.2910 -0.0052 0.0122  0.0531  341  ALA A O   
2463  C CB  . ALA A 343  ? 0.2447 0.2089 0.3164 -0.0071 0.0084  0.0463  341  ALA A CB  
2464  N N   . TYR A 344  ? 0.2180 0.1826 0.2729 -0.0037 0.0116  0.0453  342  TYR A N   
2465  C CA  . TYR A 344  ? 0.2215 0.1860 0.2732 -0.0028 0.0123  0.0470  342  TYR A CA  
2466  C C   . TYR A 344  ? 0.2228 0.1910 0.2694 -0.0019 0.0148  0.0495  342  TYR A C   
2467  O O   . TYR A 344  ? 0.2346 0.2036 0.2785 -0.0011 0.0156  0.0513  342  TYR A O   
2468  C CB  . TYR A 344  ? 0.2239 0.1860 0.2718 -0.0020 0.0114  0.0428  342  TYR A CB  
2469  C CG  . TYR A 344  ? 0.2110 0.1735 0.2519 -0.0010 0.0122  0.0393  342  TYR A CG  
2470  C CD1 . TYR A 344  ? 0.1977 0.1624 0.2357 -0.0008 0.0136  0.0393  342  TYR A CD1 
2471  C CD2 . TYR A 344  ? 0.2058 0.1665 0.2436 -0.0004 0.0114  0.0361  342  TYR A CD2 
2472  C CE1 . TYR A 344  ? 0.2085 0.1733 0.2409 0.0000  0.0141  0.0364  342  TYR A CE1 
2473  C CE2 . TYR A 344  ? 0.2207 0.1819 0.2529 0.0003  0.0120  0.0333  342  TYR A CE2 
2474  C CZ  . TYR A 344  ? 0.2269 0.1899 0.2565 0.0004  0.0133  0.0335  342  TYR A CZ  
2475  O OH  . TYR A 344  ? 0.2314 0.1945 0.2559 0.0010  0.0136  0.0310  342  TYR A OH  
2476  N N   . GLY A 345  ? 0.2167 0.1872 0.2620 -0.0019 0.0160  0.0495  343  GLY A N   
2477  C CA  . GLY A 345  ? 0.2300 0.2042 0.2707 -0.0008 0.0183  0.0512  343  GLY A CA  
2478  C C   . GLY A 345  ? 0.2250 0.2031 0.2695 -0.0013 0.0195  0.0563  343  GLY A C   
2479  O O   . GLY A 345  ? 0.2312 0.2094 0.2816 -0.0027 0.0188  0.0579  343  GLY A O   
2480  N N   . LYS A 346  ? 0.2240 0.2055 0.2649 -0.0002 0.0212  0.0587  344  LYS A N   
2481  C CA  . LYS A 346  ? 0.2350 0.2214 0.2788 -0.0006 0.0225  0.0639  344  LYS A CA  
2482  C C   . LYS A 346  ? 0.2558 0.2457 0.3008 -0.0008 0.0238  0.0646  344  LYS A C   
2483  O O   . LYS A 346  ? 0.2343 0.2278 0.2836 -0.0016 0.0245  0.0690  344  LYS A O   
2484  C CB  . LYS A 346  ? 0.2266 0.2166 0.2654 0.0009  0.0241  0.0658  344  LYS A CB  
2485  C CG  . LYS A 346  ? 0.2427 0.2297 0.2809 0.0011  0.0229  0.0659  344  LYS A CG  
2486  C CD  . LYS A 346  ? 0.2644 0.2554 0.2974 0.0027  0.0244  0.0673  344  LYS A CD  
2487  C CE  . LYS A 346  ? 0.2474 0.2359 0.2808 0.0026  0.0231  0.0683  344  LYS A CE  
2488  N NZ  . LYS A 346  ? 0.2707 0.2629 0.2983 0.0044  0.0243  0.0689  344  LYS A NZ  
2489  N N   . ARG A 347  ? 0.2342 0.2232 0.2757 0.0000  0.0240  0.0605  345  ARG A N   
2490  C CA  . ARG A 347  ? 0.2231 0.2154 0.2657 0.0000  0.0250  0.0608  345  ARG A CA  
2491  C C   . ARG A 347  ? 0.2315 0.2215 0.2800 -0.0017 0.0236  0.0604  345  ARG A C   
2492  O O   . ARG A 347  ? 0.2378 0.2308 0.2884 -0.0019 0.0243  0.0612  345  ARG A O   
2493  C CB  . ARG A 347  ? 0.2227 0.2153 0.2593 0.0018  0.0258  0.0568  345  ARG A CB  
2494  C CG  . ARG A 347  ? 0.2186 0.2147 0.2499 0.0037  0.0274  0.0574  345  ARG A CG  
2495  C CD  . ARG A 347  ? 0.2109 0.2059 0.2368 0.0053  0.0276  0.0530  345  ARG A CD  
2496  N NE  . ARG A 347  ? 0.2357 0.2254 0.2594 0.0051  0.0260  0.0499  345  ARG A NE  
2497  C CZ  . ARG A 347  ? 0.2266 0.2139 0.2466 0.0059  0.0255  0.0460  345  ARG A CZ  
2498  N NH1 . ARG A 347  ? 0.2221 0.2116 0.2402 0.0072  0.0263  0.0445  345  ARG A NH1 
2499  N NH2 . ARG A 347  ? 0.2268 0.2099 0.2454 0.0055  0.0241  0.0437  345  ARG A NH2 
2500  N N   . CYS A 348  ? 0.2301 0.2154 0.2816 -0.0028 0.0214  0.0590  346  CYS A N   
2501  C CA  . CYS A 348  ? 0.2318 0.2147 0.2882 -0.0042 0.0196  0.0572  346  CYS A CA  
2502  C C   . CYS A 348  ? 0.2322 0.2183 0.2948 -0.0054 0.0200  0.0605  346  CYS A C   
2503  O O   . CYS A 348  ? 0.2267 0.2134 0.2900 -0.0056 0.0199  0.0588  346  CYS A O   
2504  C CB  . CYS A 348  ? 0.2416 0.2199 0.3015 -0.0052 0.0173  0.0559  346  CYS A CB  
2505  S SG  . CYS A 348  ? 0.2887 0.2641 0.3527 -0.0063 0.0148  0.0517  346  CYS A SG  
2506  N N   . PRO A 349  ? 0.2315 0.2198 0.2988 -0.0064 0.0204  0.0654  347  PRO A N   
2507  C CA  . PRO A 349  ? 0.2382 0.2297 0.3118 -0.0078 0.0207  0.0687  347  PRO A CA  
2508  C C   . PRO A 349  ? 0.2064 0.2031 0.2768 -0.0067 0.0230  0.0691  347  PRO A C   
2509  O O   . PRO A 349  ? 0.2303 0.2285 0.3044 -0.0075 0.0229  0.0692  347  PRO A O   
2510  C CB  . PRO A 349  ? 0.2378 0.2311 0.3163 -0.0089 0.0208  0.0744  347  PRO A CB  
2511  C CG  . PRO A 349  ? 0.2510 0.2441 0.3238 -0.0075 0.0216  0.0746  347  PRO A CG  
2512  C CD  . PRO A 349  ? 0.2470 0.2354 0.3143 -0.0064 0.0206  0.0687  347  PRO A CD  
2513  N N   . PHE A 350  ? 0.2284 0.2277 0.2922 -0.0048 0.0249  0.0689  348  PHE A N   
2514  C CA  . PHE A 350  ? 0.2277 0.2321 0.2883 -0.0034 0.0269  0.0687  348  PHE A CA  
2515  C C   . PHE A 350  ? 0.2231 0.2250 0.2809 -0.0026 0.0263  0.0637  348  PHE A C   
2516  O O   . PHE A 350  ? 0.2217 0.2267 0.2803 -0.0023 0.0271  0.0635  348  PHE A O   
2517  C CB  . PHE A 350  ? 0.2345 0.2426 0.2893 -0.0015 0.0289  0.0697  348  PHE A CB  
2518  C CG  . PHE A 350  ? 0.2613 0.2717 0.3184 -0.0022 0.0294  0.0748  348  PHE A CG  
2519  C CD1 . PHE A 350  ? 0.3046 0.3210 0.3662 -0.0031 0.0307  0.0800  348  PHE A CD1 
2520  C CD2 . PHE A 350  ? 0.2457 0.2526 0.3011 -0.0022 0.0284  0.0746  348  PHE A CD2 
2521  C CE1 . PHE A 350  ? 0.3236 0.3426 0.3878 -0.0039 0.0311  0.0852  348  PHE A CE1 
2522  C CE2 . PHE A 350  ? 0.2830 0.2921 0.3410 -0.0029 0.0286  0.0796  348  PHE A CE2 
2523  C CZ  . PHE A 350  ? 0.3451 0.3601 0.4075 -0.0038 0.0299  0.0851  348  PHE A CZ  
2524  N N   . VAL A 351  ? 0.2074 0.2041 0.2621 -0.0024 0.0248  0.0599  349  VAL A N   
2525  C CA  . VAL A 351  ? 0.2045 0.1986 0.2573 -0.0020 0.0238  0.0555  349  VAL A CA  
2526  C C   . VAL A 351  ? 0.2005 0.1941 0.2594 -0.0037 0.0224  0.0556  349  VAL A C   
2527  O O   . VAL A 351  ? 0.2266 0.2214 0.2856 -0.0033 0.0225  0.0541  349  VAL A O   
2528  C CB  . VAL A 351  ? 0.2188 0.2078 0.2676 -0.0017 0.0224  0.0520  349  VAL A CB  
2529  C CG1 . VAL A 351  ? 0.2062 0.1932 0.2535 -0.0015 0.0212  0.0481  349  VAL A CG1 
2530  C CG2 . VAL A 351  ? 0.2299 0.2197 0.2726 0.0001  0.0237  0.0517  349  VAL A CG2 
2531  N N   . LEU A 352  ? 0.2376 0.2295 0.3022 -0.0054 0.0210  0.0573  350  LEU A N   
2532  C CA  . LEU A 352  ? 0.1971 0.1886 0.2682 -0.0070 0.0195  0.0573  350  LEU A CA  
2533  C C   . LEU A 352  ? 0.2183 0.2150 0.2927 -0.0073 0.0210  0.0605  350  LEU A C   
2534  O O   . LEU A 352  ? 0.2219 0.2194 0.2987 -0.0077 0.0204  0.0591  350  LEU A O   
2535  C CB  . LEU A 352  ? 0.2156 0.2043 0.2928 -0.0088 0.0176  0.0586  350  LEU A CB  
2536  C CG  . LEU A 352  ? 0.2202 0.2038 0.2954 -0.0086 0.0156  0.0546  350  LEU A CG  
2537  C CD1 . LEU A 352  ? 0.2623 0.2432 0.3439 -0.0100 0.0138  0.0560  350  LEU A CD1 
2538  C CD2 . LEU A 352  ? 0.2545 0.2365 0.3288 -0.0085 0.0141  0.0500  350  LEU A CD2 
2539  N N   . ASP A 353  ? 0.2535 0.2544 0.3283 -0.0071 0.0230  0.0648  351  ASP A N   
2540  C CA  . ASP A 353  ? 0.2641 0.2709 0.3414 -0.0071 0.0247  0.0677  351  ASP A CA  
2541  C C   . ASP A 353  ? 0.2135 0.2220 0.2864 -0.0054 0.0256  0.0644  351  ASP A C   
2542  O O   . ASP A 353  ? 0.2382 0.2492 0.3142 -0.0057 0.0257  0.0646  351  ASP A O   
2543  C CB  . ASP A 353  ? 0.2404 0.2524 0.3172 -0.0067 0.0270  0.0724  351  ASP A CB  
2544  C CG  . ASP A 353  ? 0.2623 0.2739 0.3451 -0.0086 0.0262  0.0768  351  ASP A CG  
2545  O OD1 . ASP A 353  ? 0.2773 0.2856 0.3665 -0.0106 0.0240  0.0768  351  ASP A OD1 
2546  O OD2 . ASP A 353  ? 0.3311 0.3457 0.4123 -0.0082 0.0276  0.0803  351  ASP A OD2 
2547  N N   . PHE A 354  ? 0.2123 0.2192 0.2780 -0.0035 0.0261  0.0616  352  PHE A N   
2548  C CA  . PHE A 354  ? 0.2199 0.2278 0.2817 -0.0017 0.0267  0.0585  352  PHE A CA  
2549  C C   . PHE A 354  ? 0.2247 0.2293 0.2883 -0.0025 0.0246  0.0554  352  PHE A C   
2550  O O   . PHE A 354  ? 0.2155 0.2224 0.2802 -0.0020 0.0249  0.0547  352  PHE A O   
2551  C CB  . PHE A 354  ? 0.2298 0.2362 0.2844 0.0002  0.0273  0.0560  352  PHE A CB  
2552  C CG  . PHE A 354  ? 0.2131 0.2188 0.2642 0.0018  0.0271  0.0523  352  PHE A CG  
2553  C CD1 . PHE A 354  ? 0.2240 0.2344 0.2739 0.0035  0.0287  0.0524  352  PHE A CD1 
2554  C CD2 . PHE A 354  ? 0.2414 0.2421 0.2906 0.0015  0.0252  0.0490  352  PHE A CD2 
2555  C CE1 . PHE A 354  ? 0.2505 0.2600 0.2979 0.0050  0.0283  0.0491  352  PHE A CE1 
2556  C CE2 . PHE A 354  ? 0.2817 0.2818 0.3282 0.0028  0.0249  0.0461  352  PHE A CE2 
2557  C CZ  . PHE A 354  ? 0.2538 0.2580 0.2996 0.0046  0.0264  0.0462  352  PHE A CZ  
2558  N N   . ILE A 355  ? 0.2130 0.2126 0.2771 -0.0036 0.0226  0.0536  353  ILE A N   
2559  C CA  . ILE A 355  ? 0.2004 0.1975 0.2657 -0.0042 0.0205  0.0504  353  ILE A CA  
2560  C C   . ILE A 355  ? 0.2371 0.2362 0.3093 -0.0057 0.0198  0.0519  353  ILE A C   
2561  O O   . ILE A 355  ? 0.2123 0.2122 0.2855 -0.0056 0.0191  0.0502  353  ILE A O   
2562  C CB  . ILE A 355  ? 0.2034 0.1955 0.2676 -0.0048 0.0186  0.0480  353  ILE A CB  
2563  C CG1 . ILE A 355  ? 0.2288 0.2189 0.2858 -0.0033 0.0191  0.0459  353  ILE A CG1 
2564  C CG2 . ILE A 355  ? 0.2279 0.2182 0.2943 -0.0057 0.0163  0.0450  353  ILE A CG2 
2565  C CD1 . ILE A 355  ? 0.2357 0.2217 0.2917 -0.0038 0.0175  0.0439  353  ILE A CD1 
2566  N N   . ILE A 356  ? 0.2182 0.2181 0.2959 -0.0073 0.0197  0.0551  354  ILE A N   
2567  C CA  . ILE A 356  ? 0.1816 0.1837 0.2668 -0.0089 0.0190  0.0568  354  ILE A CA  
2568  C C   . ILE A 356  ? 0.1785 0.1858 0.2639 -0.0080 0.0208  0.0583  354  ILE A C   
2569  O O   . ILE A 356  ? 0.2185 0.2271 0.3071 -0.0085 0.0200  0.0575  354  ILE A O   
2570  C CB  . ILE A 356  ? 0.2067 0.2088 0.2980 -0.0107 0.0186  0.0607  354  ILE A CB  
2571  C CG1 . ILE A 356  ? 0.2208 0.2174 0.3131 -0.0115 0.0162  0.0584  354  ILE A CG1 
2572  C CG2 . ILE A 356  ? 0.2424 0.2477 0.3419 -0.0124 0.0183  0.0633  354  ILE A CG2 
2573  C CD1 . ILE A 356  ? 0.2397 0.2355 0.3366 -0.0128 0.0160  0.0621  354  ILE A CD1 
2574  N N   . ASP A 357  ? 0.1992 0.2099 0.2808 -0.0066 0.0233  0.0602  355  ASP A N   
2575  C CA  . ASP A 357  ? 0.2310 0.2472 0.3128 -0.0054 0.0251  0.0612  355  ASP A CA  
2576  C C   . ASP A 357  ? 0.2469 0.2619 0.3250 -0.0039 0.0244  0.0572  355  ASP A C   
2577  O O   . ASP A 357  ? 0.2152 0.2330 0.2960 -0.0038 0.0245  0.0570  355  ASP A O   
2578  C CB  . ASP A 357  ? 0.2033 0.2239 0.2817 -0.0039 0.0277  0.0636  355  ASP A CB  
2579  C CG  . ASP A 357  ? 0.2442 0.2707 0.3220 -0.0023 0.0296  0.0638  355  ASP A CG  
2580  O OD1 . ASP A 357  ? 0.3083 0.3396 0.3915 -0.0032 0.0304  0.0668  355  ASP A OD1 
2581  O OD2 . ASP A 357  ? 0.2575 0.2837 0.3298 0.0000  0.0301  0.0608  355  ASP A OD2 
2582  N N   . LEU A 358  ? 0.2051 0.2158 0.2775 -0.0029 0.0237  0.0540  356  LEU A N   
2583  C CA  . LEU A 358  ? 0.2043 0.2136 0.2736 -0.0017 0.0229  0.0506  356  LEU A CA  
2584  C C   . LEU A 358  ? 0.2142 0.2222 0.2876 -0.0031 0.0207  0.0492  356  LEU A C   
2585  O O   . LEU A 358  ? 0.2248 0.2343 0.2986 -0.0025 0.0203  0.0480  356  LEU A O   
2586  C CB  . LEU A 358  ? 0.1889 0.1939 0.2518 -0.0007 0.0224  0.0479  356  LEU A CB  
2587  C CG  . LEU A 358  ? 0.1960 0.1989 0.2560 0.0003  0.0212  0.0446  356  LEU A CG  
2588  C CD1 . LEU A 358  ? 0.2474 0.2538 0.3068 0.0021  0.0224  0.0445  356  LEU A CD1 
2589  C CD2 . LEU A 358  ? 0.2183 0.2172 0.2727 0.0009  0.0207  0.0426  356  LEU A CD2 
2590  N N   . ALA A 359  ? 0.2306 0.2360 0.3072 -0.0050 0.0191  0.0493  357  ALA A N   
2591  C CA  . ALA A 359  ? 0.2371 0.2418 0.3182 -0.0064 0.0168  0.0479  357  ALA A CA  
2592  C C   . ALA A 359  ? 0.2252 0.2344 0.3121 -0.0070 0.0173  0.0501  357  ALA A C   
2593  O O   . ALA A 359  ? 0.2356 0.2457 0.3242 -0.0071 0.0162  0.0486  357  ALA A O   
2594  C CB  . ALA A 359  ? 0.2427 0.2441 0.3270 -0.0081 0.0150  0.0475  357  ALA A CB  
2595  N N   . ARG A 360  ? 0.2156 0.2281 0.3056 -0.0075 0.0191  0.0539  358  ARG A N   
2596  C CA  . ARG A 360  ? 0.2298 0.2472 0.3253 -0.0080 0.0198  0.0563  358  ARG A CA  
2597  C C   . ARG A 360  ? 0.2710 0.2917 0.3636 -0.0059 0.0211  0.0552  358  ARG A C   
2598  O O   . ARG A 360  ? 0.2768 0.2995 0.3727 -0.0061 0.0203  0.0547  358  ARG A O   
2599  C CB  . ARG A 360  ? 0.2615 0.2825 0.3606 -0.0089 0.0217  0.0610  358  ARG A CB  
2600  C CG  . ARG A 360  ? 0.3509 0.3691 0.4549 -0.0112 0.0202  0.0627  358  ARG A CG  
2601  C CD  . ARG A 360  ? 0.3387 0.3615 0.4475 -0.0122 0.0220  0.0682  358  ARG A CD  
2602  N NE  . ARG A 360  ? 0.3747 0.3943 0.4871 -0.0140 0.0208  0.0701  358  ARG A NE  
2603  C CZ  . ARG A 360  ? 0.4485 0.4660 0.5684 -0.0163 0.0184  0.0704  358  ARG A CZ  
2604  N NH1 . ARG A 360  ? 0.4463 0.4648 0.5709 -0.0171 0.0170  0.0691  358  ARG A NH1 
2605  N NH2 . ARG A 360  ? 0.4724 0.4866 0.5955 -0.0176 0.0172  0.0719  358  ARG A NH2 
2606  N N   . ARG A 361  ? 0.2415 0.2625 0.3280 -0.0039 0.0228  0.0547  359  ARG A N   
2607  C CA  . ARG A 361  ? 0.2415 0.2655 0.3256 -0.0017 0.0239  0.0535  359  ARG A CA  
2608  C C   . ARG A 361  ? 0.2545 0.2756 0.3372 -0.0012 0.0218  0.0501  359  ARG A C   
2609  O O   . ARG A 361  ? 0.2699 0.2938 0.3544 -0.0004 0.0217  0.0497  359  ARG A O   
2610  C CB  . ARG A 361  ? 0.2707 0.2950 0.3487 0.0005  0.0257  0.0530  359  ARG A CB  
2611  C CG  . ARG A 361  ? 0.2882 0.3171 0.3670 0.0006  0.0281  0.0564  359  ARG A CG  
2612  C CD  . ARG A 361  ? 0.3241 0.3539 0.3968 0.0031  0.0297  0.0552  359  ARG A CD  
2613  N NE  . ARG A 361  ? 0.3137 0.3383 0.3818 0.0030  0.0290  0.0539  359  ARG A NE  
2614  C CZ  . ARG A 361  ? 0.3057 0.3267 0.3685 0.0046  0.0284  0.0506  359  ARG A CZ  
2615  N NH1 . ARG A 361  ? 0.2853 0.3067 0.3470 0.0062  0.0281  0.0482  359  ARG A NH1 
2616  N NH2 . ARG A 361  ? 0.2742 0.2913 0.3332 0.0044  0.0280  0.0499  359  ARG A NH2 
2617  N N   . SER A 362  ? 0.2360 0.2520 0.3154 -0.0016 0.0202  0.0479  360  SER A N   
2618  C CA  . SER A 362  ? 0.2357 0.2493 0.3130 -0.0011 0.0183  0.0450  360  SER A CA  
2619  C C   . SER A 362  ? 0.2416 0.2553 0.3238 -0.0028 0.0161  0.0444  360  SER A C   
2620  O O   . SER A 362  ? 0.2661 0.2795 0.3477 -0.0024 0.0146  0.0426  360  SER A O   
2621  C CB  . SER A 362  ? 0.2379 0.2467 0.3097 -0.0008 0.0175  0.0429  360  SER A CB  
2622  O OG  . SER A 362  ? 0.2208 0.2271 0.2941 -0.0026 0.0164  0.0429  360  SER A OG  
2623  N N   . GLY A 363  ? 0.2471 0.2612 0.3342 -0.0048 0.0158  0.0460  361  GLY A N   
2624  C CA  . GLY A 363  ? 0.2208 0.2346 0.3126 -0.0064 0.0134  0.0449  361  GLY A CA  
2625  C C   . GLY A 363  ? 0.2847 0.2944 0.3739 -0.0069 0.0112  0.0418  361  GLY A C   
2626  O O   . GLY A 363  ? 0.2699 0.2797 0.3621 -0.0079 0.0089  0.0401  361  GLY A O   
2627  N N   . ARG A 364  ? 0.2423 0.2489 0.3259 -0.0062 0.0117  0.0410  362  ARG A N   
2628  C CA  . ARG A 364  ? 0.2442 0.2473 0.3249 -0.0065 0.0098  0.0381  362  ARG A CA  
2629  C C   . ARG A 364  ? 0.2456 0.2465 0.3289 -0.0079 0.0093  0.0384  362  ARG A C   
2630  O O   . ARG A 364  ? 0.2506 0.2510 0.3334 -0.0078 0.0110  0.0406  362  ARG A O   
2631  C CB  . ARG A 364  ? 0.2867 0.2877 0.3602 -0.0049 0.0105  0.0370  362  ARG A CB  
2632  C CG  . ARG A 364  ? 0.3596 0.3623 0.4306 -0.0032 0.0114  0.0373  362  ARG A CG  
2633  C CD  . ARG A 364  ? 0.2611 0.2634 0.3297 -0.0029 0.0096  0.0352  362  ARG A CD  
2634  N NE  . ARG A 364  ? 0.2205 0.2248 0.2887 -0.0014 0.0101  0.0358  362  ARG A NE  
2635  C CZ  . ARG A 364  ? 0.2364 0.2395 0.3003 0.0001  0.0106  0.0354  362  ARG A CZ  
2636  N NH1 . ARG A 364  ? 0.2259 0.2260 0.2852 0.0003  0.0105  0.0345  362  ARG A NH1 
2637  N NH2 . ARG A 364  ? 0.2089 0.2140 0.2736 0.0014  0.0109  0.0360  362  ARG A NH2 
2638  N N   . ARG A 365  ? 0.2260 0.2256 0.3118 -0.0090 0.0069  0.0360  363  ARG A N   
2639  C CA  . ARG A 365  ? 0.2107 0.2080 0.2996 -0.0102 0.0060  0.0359  363  ARG A CA  
2640  C C   . ARG A 365  ? 0.2375 0.2316 0.3202 -0.0094 0.0061  0.0341  363  ARG A C   
2641  O O   . ARG A 365  ? 0.2450 0.2379 0.3260 -0.0094 0.0043  0.0309  363  ARG A O   
2642  C CB  . ARG A 365  ? 0.2059 0.2033 0.3006 -0.0116 0.0032  0.0336  363  ARG A CB  
2643  C CG  . ARG A 365  ? 0.2264 0.2213 0.3257 -0.0129 0.0020  0.0334  363  ARG A CG  
2644  C CD  . ARG A 365  ? 0.2858 0.2818 0.3934 -0.0145 -0.0004 0.0324  363  ARG A CD  
2645  N NE  . ARG A 365  ? 0.2567 0.2500 0.3696 -0.0157 -0.0015 0.0328  363  ARG A NE  
2646  C CZ  . ARG A 365  ? 0.2429 0.2340 0.3574 -0.0160 -0.0041 0.0289  363  ARG A CZ  
2647  N NH1 . ARG A 365  ? 0.2565 0.2484 0.3680 -0.0153 -0.0057 0.0245  363  ARG A NH1 
2648  N NH2 . ARG A 365  ? 0.2448 0.2332 0.3641 -0.0169 -0.0050 0.0296  363  ARG A NH2 
2649  N N   . ILE A 366  ? 0.2218 0.2150 0.3012 -0.0086 0.0083  0.0363  364  ILE A N   
2650  C CA  . ILE A 366  ? 0.1998 0.1904 0.2731 -0.0077 0.0085  0.0348  364  ILE A CA  
2651  C C   . ILE A 366  ? 0.2166 0.2045 0.2918 -0.0086 0.0068  0.0329  364  ILE A C   
2652  O O   . ILE A 366  ? 0.2231 0.2104 0.3037 -0.0098 0.0064  0.0343  364  ILE A O   
2653  C CB  . ILE A 366  ? 0.2009 0.1914 0.2707 -0.0067 0.0111  0.0374  364  ILE A CB  
2654  C CG1 . ILE A 366  ? 0.2359 0.2292 0.3039 -0.0055 0.0126  0.0385  364  ILE A CG1 
2655  C CG2 . ILE A 366  ? 0.2209 0.2086 0.2848 -0.0058 0.0113  0.0358  364  ILE A CG2 
2656  C CD1 . ILE A 366  ? 0.2515 0.2459 0.3168 -0.0043 0.0151  0.0408  364  ILE A CD1 
2657  N N   . MET A 367  ? 0.2021 0.1887 0.2733 -0.0081 0.0056  0.0297  365  MET A N   
2658  C CA  . MET A 367  ? 0.2144 0.1986 0.2869 -0.0087 0.0039  0.0274  365  MET A CA  
2659  C C   . MET A 367  ? 0.2205 0.2024 0.2898 -0.0081 0.0054  0.0288  365  MET A C   
2660  O O   . MET A 367  ? 0.2528 0.2344 0.3159 -0.0070 0.0067  0.0287  365  MET A O   
2661  C CB  . MET A 367  ? 0.2211 0.2058 0.2905 -0.0083 0.0022  0.0234  365  MET A CB  
2662  C CG  . MET A 367  ? 0.2122 0.1999 0.2836 -0.0085 0.0009  0.0222  365  MET A CG  
2663  S SD  . MET A 367  ? 0.2422 0.2318 0.3100 -0.0081 -0.0012 0.0178  365  MET A SD  
2664  C CE  . MET A 367  ? 0.2720 0.2613 0.3459 -0.0090 -0.0040 0.0141  365  MET A CE  
2665  N N   . VAL A 368  ? 0.1872 0.1677 0.2609 -0.0089 0.0053  0.0304  366  VAL A N   
2666  C CA  . VAL A 368  ? 0.1997 0.1784 0.2707 -0.0084 0.0068  0.0323  366  VAL A CA  
2667  C C   . VAL A 368  ? 0.2221 0.1981 0.2940 -0.0086 0.0051  0.0298  366  VAL A C   
2668  O O   . VAL A 368  ? 0.2192 0.1942 0.2975 -0.0097 0.0033  0.0294  366  VAL A O   
2669  C CB  . VAL A 368  ? 0.2048 0.1845 0.2797 -0.0090 0.0082  0.0368  366  VAL A CB  
2670  C CG1 . VAL A 368  ? 0.2485 0.2268 0.3203 -0.0084 0.0097  0.0388  366  VAL A CG1 
2671  C CG2 . VAL A 368  ? 0.2390 0.2221 0.3133 -0.0087 0.0099  0.0390  366  VAL A CG2 
2672  N N   . ARG A 369  ? 0.1947 0.1696 0.2605 -0.0076 0.0054  0.0279  367  ARG A N   
2673  C CA  . ARG A 369  ? 0.2083 0.1809 0.2746 -0.0076 0.0039  0.0255  367  ARG A CA  
2674  C C   . ARG A 369  ? 0.2450 0.2158 0.3111 -0.0074 0.0052  0.0284  367  ARG A C   
2675  O O   . ARG A 369  ? 0.2254 0.1963 0.2860 -0.0065 0.0071  0.0298  367  ARG A O   
2676  C CB  . ARG A 369  ? 0.2115 0.1843 0.2718 -0.0066 0.0035  0.0220  367  ARG A CB  
2677  C CG  . ARG A 369  ? 0.2323 0.2032 0.2934 -0.0065 0.0021  0.0193  367  ARG A CG  
2678  C CD  . ARG A 369  ? 0.2476 0.2188 0.3019 -0.0055 0.0024  0.0171  367  ARG A CD  
2679  N NE  . ARG A 369  ? 0.2277 0.2016 0.2799 -0.0054 0.0016  0.0146  367  ARG A NE  
2680  C CZ  . ARG A 369  ? 0.2526 0.2278 0.2988 -0.0047 0.0023  0.0140  367  ARG A CZ  
2681  N NH1 . ARG A 369  ? 0.2619 0.2357 0.3035 -0.0041 0.0039  0.0154  367  ARG A NH1 
2682  N NH2 . ARG A 369  ? 0.2582 0.2363 0.3031 -0.0047 0.0014  0.0122  367  ARG A NH2 
2683  N N   . LEU A 370  ? 0.2213 0.1905 0.2936 -0.0082 0.0040  0.0293  368  LEU A N   
2684  C CA  . LEU A 370  ? 0.1919 0.1595 0.2646 -0.0081 0.0048  0.0322  368  LEU A CA  
2685  C C   . LEU A 370  ? 0.2201 0.1853 0.2909 -0.0075 0.0036  0.0290  368  LEU A C   
2686  O O   . LEU A 370  ? 0.2220 0.1861 0.2968 -0.0078 0.0012  0.0258  368  LEU A O   
2687  C CB  . LEU A 370  ? 0.2184 0.1856 0.2995 -0.0095 0.0040  0.0354  368  LEU A CB  
2688  C CG  . LEU A 370  ? 0.2125 0.1786 0.2944 -0.0095 0.0050  0.0393  368  LEU A CG  
2689  C CD1 . LEU A 370  ? 0.2455 0.2143 0.3220 -0.0088 0.0080  0.0429  368  LEU A CD1 
2690  C CD2 . LEU A 370  ? 0.2343 0.1998 0.3257 -0.0111 0.0036  0.0423  368  LEU A CD2 
2691  N N   . VAL A 371  ? 0.1990 0.1638 0.2638 -0.0065 0.0051  0.0298  369  VAL A N   
2692  C CA  . VAL A 371  ? 0.1939 0.1568 0.2566 -0.0057 0.0043  0.0272  369  VAL A CA  
2693  C C   . VAL A 371  ? 0.2018 0.1635 0.2645 -0.0055 0.0053  0.0306  369  VAL A C   
2694  O O   . VAL A 371  ? 0.2275 0.1904 0.2903 -0.0057 0.0069  0.0348  369  VAL A O   
2695  C CB  . VAL A 371  ? 0.2221 0.1860 0.2773 -0.0047 0.0050  0.0244  369  VAL A CB  
2696  C CG1 . VAL A 371  ? 0.2211 0.1869 0.2759 -0.0050 0.0042  0.0218  369  VAL A CG1 
2697  C CG2 . VAL A 371  ? 0.2214 0.1860 0.2708 -0.0040 0.0075  0.0272  369  VAL A CG2 
2698  N N   . LYS A 372  ? 0.2271 0.1868 0.2893 -0.0050 0.0043  0.0289  370  LYS A N   
2699  C CA  . LYS A 372  ? 0.2256 0.1846 0.2867 -0.0046 0.0054  0.0322  370  LYS A CA  
2700  C C   . LYS A 372  ? 0.2182 0.1784 0.2710 -0.0034 0.0075  0.0323  370  LYS A C   
2701  O O   . LYS A 372  ? 0.2752 0.2369 0.3258 -0.0032 0.0094  0.0358  370  LYS A O   
2702  C CB  . LYS A 372  ? 0.2466 0.2029 0.3117 -0.0045 0.0034  0.0309  370  LYS A CB  
2703  C CG  . LYS A 372  ? 0.2483 0.2034 0.3227 -0.0057 0.0014  0.0320  370  LYS A CG  
2704  C CD  . LYS A 372  ? 0.2620 0.2142 0.3420 -0.0056 -0.0009 0.0308  370  LYS A CD  
2705  C CE  . LYS A 372  ? 0.2734 0.2244 0.3633 -0.0070 -0.0031 0.0315  370  LYS A CE  
2706  N NZ  . LYS A 372  ? 0.2511 0.1990 0.3476 -0.0068 -0.0060 0.0293  370  LYS A NZ  
2707  N N   . GLY A 373  ? 0.2315 0.1915 0.2798 -0.0027 0.0072  0.0285  371  GLY A N   
2708  C CA  . GLY A 373  ? 0.2201 0.1811 0.2610 -0.0018 0.0089  0.0284  371  GLY A CA  
2709  C C   . GLY A 373  ? 0.2070 0.1671 0.2443 -0.0011 0.0083  0.0253  371  GLY A C   
2710  O O   . GLY A 373  ? 0.2228 0.1814 0.2624 -0.0009 0.0072  0.0247  371  GLY A O   
2711  N N   . ALA A 374  ? 0.2209 0.1820 0.2528 -0.0006 0.0090  0.0236  372  ALA A N   
2712  C CA  . ALA A 374  ? 0.2361 0.1971 0.2651 -0.0001 0.0083  0.0204  372  ALA A CA  
2713  C C   . ALA A 374  ? 0.2663 0.2270 0.2902 0.0007  0.0095  0.0211  372  ALA A C   
2714  O O   . ALA A 374  ? 0.2774 0.2381 0.2990 0.0011  0.0090  0.0188  372  ALA A O   
2715  C CB  . ALA A 374  ? 0.2568 0.2196 0.2837 -0.0003 0.0079  0.0178  372  ALA A CB  
2716  N N   . TYR A 375  ? 0.2371 0.1979 0.2594 0.0011  0.0110  0.0241  373  TYR A N   
2717  C CA  . TYR A 375  ? 0.2160 0.1770 0.2332 0.0019  0.0121  0.0245  373  TYR A CA  
2718  C C   . TYR A 375  ? 0.2057 0.1662 0.2234 0.0025  0.0126  0.0268  373  TYR A C   
2719  O O   . TYR A 375  ? 0.2264 0.1877 0.2405 0.0032  0.0138  0.0280  373  TYR A O   
2720  C CB  . TYR A 375  ? 0.2416 0.2040 0.2558 0.0022  0.0135  0.0254  373  TYR A CB  
2721  C CG  . TYR A 375  ? 0.2053 0.1683 0.2191 0.0017  0.0130  0.0237  373  TYR A CG  
2722  C CD1 . TYR A 375  ? 0.2273 0.1909 0.2447 0.0010  0.0126  0.0240  373  TYR A CD1 
2723  C CD2 . TYR A 375  ? 0.2671 0.2304 0.2773 0.0018  0.0129  0.0218  373  TYR A CD2 
2724  C CE1 . TYR A 375  ? 0.2372 0.2019 0.2544 0.0006  0.0121  0.0226  373  TYR A CE1 
2725  C CE2 . TYR A 375  ? 0.2977 0.2620 0.3077 0.0013  0.0124  0.0207  373  TYR A CE2 
2726  C CZ  . TYR A 375  ? 0.3137 0.2787 0.3270 0.0008  0.0120  0.0210  373  TYR A CZ  
2727  O OH  . TYR A 375  ? 0.3312 0.2976 0.3443 0.0003  0.0114  0.0200  373  TYR A OH  
2728  N N   . TRP A 376  ? 0.2188 0.1781 0.2409 0.0021  0.0115  0.0274  374  TRP A N   
2729  C CA  . TRP A 376  ? 0.2432 0.2025 0.2666 0.0025  0.0119  0.0306  374  TRP A CA  
2730  C C   . TRP A 376  ? 0.2688 0.2283 0.2878 0.0035  0.0125  0.0304  374  TRP A C   
2731  O O   . TRP A 376  ? 0.2290 0.1899 0.2455 0.0041  0.0138  0.0328  374  TRP A O   
2732  C CB  . TRP A 376  ? 0.2379 0.1956 0.2677 0.0019  0.0103  0.0312  374  TRP A CB  
2733  C CG  . TRP A 376  ? 0.2388 0.1966 0.2703 0.0021  0.0106  0.0352  374  TRP A CG  
2734  C CD1 . TRP A 376  ? 0.2432 0.2027 0.2765 0.0018  0.0117  0.0394  374  TRP A CD1 
2735  C CD2 . TRP A 376  ? 0.2641 0.2210 0.2953 0.0028  0.0100  0.0355  374  TRP A CD2 
2736  N NE1 . TRP A 376  ? 0.2425 0.2022 0.2768 0.0022  0.0117  0.0426  374  TRP A NE1 
2737  C CE2 . TRP A 376  ? 0.2537 0.2117 0.2868 0.0028  0.0106  0.0402  374  TRP A CE2 
2738  C CE3 . TRP A 376  ? 0.2784 0.2340 0.3083 0.0034  0.0090  0.0323  374  TRP A CE3 
2739  C CZ2 . TRP A 376  ? 0.2769 0.2345 0.3104 0.0034  0.0101  0.0419  374  TRP A CZ2 
2740  C CZ3 . TRP A 376  ? 0.3045 0.2595 0.3349 0.0041  0.0085  0.0338  374  TRP A CZ3 
2741  C CH2 . TRP A 376  ? 0.3047 0.2606 0.3369 0.0041  0.0090  0.0386  374  TRP A CH2 
2742  N N   . ASP A 377  ? 0.2512 0.2094 0.2690 0.0037  0.0114  0.0274  375  ASP A N   
2743  C CA  A ASP A 377  ? 0.2541 0.2125 0.2682 0.0046  0.0118  0.0274  375  ASP A CA  
2744  C CA  B ASP A 377  ? 0.2545 0.2129 0.2685 0.0046  0.0117  0.0270  375  ASP A CA  
2745  C C   . ASP A 377  ? 0.2468 0.2067 0.2557 0.0052  0.0132  0.0272  375  ASP A C   
2746  O O   . ASP A 377  ? 0.2560 0.2167 0.2621 0.0060  0.0140  0.0284  375  ASP A O   
2747  C CB  A ASP A 377  ? 0.2936 0.2510 0.3078 0.0048  0.0105  0.0242  375  ASP A CB  
2748  C CB  B ASP A 377  ? 0.2913 0.2489 0.3045 0.0047  0.0106  0.0233  375  ASP A CB  
2749  C CG  A ASP A 377  ? 0.3206 0.2784 0.3337 0.0044  0.0100  0.0208  375  ASP A CG  
2750  C CG  B ASP A 377  ? 0.3624 0.3187 0.3806 0.0046  0.0089  0.0223  375  ASP A CG  
2751  O OD1 A ASP A 377  ? 0.3508 0.3095 0.3606 0.0042  0.0110  0.0206  375  ASP A OD1 
2752  O OD1 B ASP A 377  ? 0.4474 0.4028 0.4690 0.0046  0.0085  0.0249  375  ASP A OD1 
2753  O OD2 A ASP A 377  ? 0.3426 0.2999 0.3582 0.0042  0.0087  0.0184  375  ASP A OD2 
2754  O OD2 B ASP A 377  ? 0.4312 0.3875 0.4500 0.0044  0.0079  0.0190  375  ASP A OD2 
2755  N N   . ALA A 378  ? 0.2419 0.2022 0.2495 0.0047  0.0135  0.0258  376  ALA A N   
2756  C CA  . ALA A 378  ? 0.2334 0.1948 0.2368 0.0053  0.0146  0.0255  376  ALA A CA  
2757  C C   . ALA A 378  ? 0.2200 0.1830 0.2231 0.0058  0.0159  0.0283  376  ALA A C   
2758  O O   . ALA A 378  ? 0.2471 0.2113 0.2468 0.0068  0.0167  0.0284  376  ALA A O   
2759  C CB  . ALA A 378  ? 0.2472 0.2086 0.2500 0.0046  0.0144  0.0237  376  ALA A CB  
2760  N N   . GLU A 379  ? 0.2158 0.1793 0.2227 0.0053  0.0160  0.0305  377  GLU A N   
2761  C CA  . GLU A 379  ? 0.1971 0.1630 0.2038 0.0059  0.0174  0.0334  377  GLU A CA  
2762  C C   . GLU A 379  ? 0.2247 0.1918 0.2302 0.0067  0.0178  0.0354  377  GLU A C   
2763  O O   . GLU A 379  ? 0.2464 0.2161 0.2494 0.0077  0.0190  0.0366  377  GLU A O   
2764  C CB  . GLU A 379  ? 0.2218 0.1882 0.2332 0.0049  0.0174  0.0356  377  GLU A CB  
2765  C CG  . GLU A 379  ? 0.2284 0.1942 0.2411 0.0042  0.0171  0.0339  377  GLU A CG  
2766  C CD  . GLU A 379  ? 0.2455 0.2129 0.2550 0.0048  0.0182  0.0331  377  GLU A CD  
2767  O OE1 . GLU A 379  ? 0.2500 0.2191 0.2565 0.0060  0.0193  0.0337  377  GLU A OE1 
2768  O OE2 . GLU A 379  ? 0.2443 0.2112 0.2547 0.0043  0.0177  0.0318  377  GLU A OE2 
2769  N N   . ILE A 380  ? 0.2129 0.1784 0.2205 0.0064  0.0167  0.0356  378  ILE A N   
2770  C CA  . ILE A 380  ? 0.2356 0.2022 0.2421 0.0072  0.0169  0.0376  378  ILE A CA  
2771  C C   . ILE A 380  ? 0.2556 0.2230 0.2568 0.0084  0.0173  0.0356  378  ILE A C   
2772  O O   . ILE A 380  ? 0.2356 0.2058 0.2342 0.0094  0.0183  0.0370  378  ILE A O   
2773  C CB  . ILE A 380  ? 0.2256 0.1899 0.2358 0.0067  0.0153  0.0379  378  ILE A CB  
2774  C CG1 . ILE A 380  ? 0.2274 0.1907 0.2437 0.0056  0.0146  0.0399  378  ILE A CG1 
2775  C CG2 . ILE A 380  ? 0.2461 0.2117 0.2553 0.0076  0.0154  0.0403  378  ILE A CG2 
2776  C CD1 . ILE A 380  ? 0.2454 0.2116 0.2638 0.0054  0.0158  0.0445  378  ILE A CD1 
2777  N N   . LYS A 381  ? 0.2142 0.1795 0.2139 0.0081  0.0165  0.0321  379  LYS A N   
2778  C CA  . LYS A 381  ? 0.2307 0.1964 0.2259 0.0090  0.0167  0.0300  379  LYS A CA  
2779  C C   . LYS A 381  ? 0.2528 0.2206 0.2452 0.0098  0.0179  0.0299  379  LYS A C   
2780  O O   . LYS A 381  ? 0.2345 0.2043 0.2240 0.0110  0.0183  0.0298  379  LYS A O   
2781  C CB  . LYS A 381  ? 0.2266 0.1900 0.2213 0.0084  0.0157  0.0268  379  LYS A CB  
2782  C CG  . LYS A 381  ? 0.2440 0.2078 0.2348 0.0090  0.0157  0.0247  379  LYS A CG  
2783  C CD  . LYS A 381  ? 0.2423 0.2045 0.2328 0.0083  0.0147  0.0220  379  LYS A CD  
2784  C CE  . LYS A 381  ? 0.2417 0.2042 0.2291 0.0088  0.0146  0.0203  379  LYS A CE  
2785  N NZ  . LYS A 381  ? 0.2478 0.2095 0.2351 0.0080  0.0137  0.0181  379  LYS A NZ  
2786  N N   . ARG A 382  ? 0.2219 0.1897 0.2156 0.0093  0.0183  0.0298  380  ARG A N   
2787  C CA  . ARG A 382  ? 0.2389 0.2086 0.2304 0.0102  0.0192  0.0291  380  ARG A CA  
2788  C C   . ARG A 382  ? 0.2414 0.2148 0.2320 0.0114  0.0204  0.0315  380  ARG A C   
2789  O O   . ARG A 382  ? 0.2580 0.2335 0.2457 0.0127  0.0209  0.0304  380  ARG A O   
2790  C CB  . ARG A 382  ? 0.2790 0.2481 0.2725 0.0094  0.0193  0.0289  380  ARG A CB  
2791  C CG  . ARG A 382  ? 0.3390 0.3094 0.3308 0.0103  0.0199  0.0277  380  ARG A CG  
2792  C CD  . ARG A 382  ? 0.5332 0.5016 0.5229 0.0103  0.0191  0.0248  380  ARG A CD  
2793  N NE  . ARG A 382  ? 0.5856 0.5553 0.5724 0.0117  0.0192  0.0237  380  ARG A NE  
2794  C CZ  . ARG A 382  ? 0.5483 0.5166 0.5334 0.0118  0.0184  0.0214  380  ARG A CZ  
2795  N NH1 . ARG A 382  ? 0.6551 0.6209 0.6408 0.0106  0.0174  0.0203  380  ARG A NH1 
2796  N NH2 . ARG A 382  ? 0.4466 0.4163 0.4294 0.0132  0.0185  0.0202  380  ARG A NH2 
2797  N N   . ALA A 383  ? 0.2316 0.2062 0.2251 0.0109  0.0208  0.0347  381  ALA A N   
2798  C CA  . ALA A 383  ? 0.2069 0.1860 0.1997 0.0119  0.0220  0.0375  381  ALA A CA  
2799  C C   . ALA A 383  ? 0.2395 0.2201 0.2293 0.0131  0.0219  0.0376  381  ALA A C   
2800  O O   . ALA A 383  ? 0.2462 0.2311 0.2335 0.0145  0.0229  0.0380  381  ALA A O   
2801  C CB  . ALA A 383  ? 0.2412 0.2212 0.2385 0.0109  0.0223  0.0415  381  ALA A CB  
2802  N N   . GLN A 384  ? 0.2377 0.2154 0.2279 0.0125  0.0207  0.0370  382  GLN A N   
2803  C CA  . GLN A 384  ? 0.2416 0.2207 0.2290 0.0136  0.0205  0.0369  382  GLN A CA  
2804  C C   . GLN A 384  ? 0.2466 0.2262 0.2301 0.0147  0.0204  0.0332  382  GLN A C   
2805  O O   . GLN A 384  ? 0.2820 0.2652 0.2626 0.0162  0.0209  0.0331  382  GLN A O   
2806  C CB  . GLN A 384  ? 0.2393 0.2151 0.2285 0.0128  0.0191  0.0368  382  GLN A CB  
2807  C CG  . GLN A 384  ? 0.2287 0.2046 0.2224 0.0120  0.0188  0.0407  382  GLN A CG  
2808  C CD  . GLN A 384  ? 0.2352 0.2079 0.2308 0.0116  0.0173  0.0404  382  GLN A CD  
2809  O OE1 . GLN A 384  ? 0.2678 0.2382 0.2620 0.0115  0.0165  0.0370  382  GLN A OE1 
2810  N NE2 . GLN A 384  ? 0.2603 0.2333 0.2595 0.0112  0.0168  0.0440  382  GLN A NE2 
2811  N N   . LEU A 385  ? 0.2406 0.2169 0.2240 0.0141  0.0198  0.0301  383  LEU A N   
2812  C CA  . LEU A 385  ? 0.2525 0.2287 0.2330 0.0149  0.0195  0.0268  383  LEU A CA  
2813  C C   . LEU A 385  ? 0.2587 0.2386 0.2377 0.0164  0.0206  0.0265  383  LEU A C   
2814  O O   . LEU A 385  ? 0.2719 0.2538 0.2482 0.0178  0.0205  0.0245  383  LEU A O   
2815  C CB  . LEU A 385  ? 0.2456 0.2181 0.2270 0.0138  0.0187  0.0244  383  LEU A CB  
2816  C CG  . LEU A 385  ? 0.2811 0.2506 0.2632 0.0127  0.0175  0.0234  383  LEU A CG  
2817  C CD1 . LEU A 385  ? 0.2829 0.2499 0.2660 0.0115  0.0170  0.0217  383  LEU A CD1 
2818  C CD2 . LEU A 385  ? 0.3002 0.2702 0.2797 0.0135  0.0170  0.0218  383  LEU A CD2 
2819  N N   . ASP A 386  ? 0.2556 0.2368 0.2365 0.0161  0.0215  0.0282  384  ASP A N   
2820  C CA  . ASP A 386  ? 0.2548 0.2396 0.2346 0.0175  0.0225  0.0276  384  ASP A CA  
2821  C C   . ASP A 386  ? 0.2582 0.2486 0.2367 0.0188  0.0237  0.0300  384  ASP A C   
2822  O O   . ASP A 386  ? 0.2669 0.2615 0.2444 0.0203  0.0246  0.0295  384  ASP A O   
2823  C CB  . ASP A 386  ? 0.2594 0.2433 0.2419 0.0167  0.0230  0.0282  384  ASP A CB  
2824  C CG  . ASP A 386  ? 0.3531 0.3327 0.3363 0.0158  0.0219  0.0254  384  ASP A CG  
2825  O OD1 . ASP A 386  ? 0.3695 0.3471 0.3510 0.0160  0.0209  0.0230  384  ASP A OD1 
2826  O OD2 . ASP A 386  ? 0.3405 0.3189 0.3260 0.0149  0.0220  0.0259  384  ASP A OD2 
2827  N N   . GLY A 387  ? 0.2628 0.2539 0.2416 0.0184  0.0236  0.0328  385  GLY A N   
2828  C CA  . GLY A 387  ? 0.2602 0.2572 0.2378 0.0197  0.0246  0.0357  385  GLY A CA  
2829  C C   . GLY A 387  ? 0.2886 0.2897 0.2681 0.0197  0.0261  0.0387  385  GLY A C   
2830  O O   . GLY A 387  ? 0.2947 0.3021 0.2723 0.0213  0.0272  0.0395  385  GLY A O   
2831  N N   . LEU A 388  ? 0.2611 0.2593 0.2444 0.0179  0.0261  0.0405  386  LEU A N   
2832  C CA  . LEU A 388  ? 0.2801 0.2819 0.2656 0.0178  0.0274  0.0431  386  LEU A CA  
2833  C C   . LEU A 388  ? 0.2683 0.2732 0.2561 0.0171  0.0280  0.0486  386  LEU A C   
2834  O O   . LEU A 388  ? 0.2829 0.2864 0.2711 0.0166  0.0272  0.0503  386  LEU A O   
2835  C CB  . LEU A 388  ? 0.2698 0.2674 0.2584 0.0164  0.0271  0.0420  386  LEU A CB  
2836  C CG  . LEU A 388  ? 0.2955 0.2904 0.2819 0.0171  0.0265  0.0371  386  LEU A CG  
2837  C CD1 . LEU A 388  ? 0.2938 0.2849 0.2831 0.0157  0.0260  0.0362  386  LEU A CD1 
2838  C CD2 . LEU A 388  ? 0.2807 0.2807 0.2644 0.0193  0.0274  0.0352  386  LEU A CD2 
2839  N N   . ALA A 389  ? 0.3095 0.3193 0.2991 0.0172  0.0294  0.0515  387  ALA A N   
2840  C CA  . ALA A 389  ? 0.3244 0.3388 0.3161 0.0167  0.0302  0.0572  387  ALA A CA  
2841  C C   . ALA A 389  ? 0.2727 0.2820 0.2692 0.0145  0.0289  0.0602  387  ALA A C   
2842  O O   . ALA A 389  ? 0.3277 0.3384 0.3256 0.0142  0.0286  0.0641  387  ALA A O   
2843  C CB  . ALA A 389  ? 0.3007 0.3212 0.2938 0.0170  0.0320  0.0597  387  ALA A CB  
2844  N N   . ASP A 390  ? 0.2535 0.2571 0.2530 0.0131  0.0280  0.0583  388  ASP A N   
2845  C CA  . ASP A 390  ? 0.2872 0.2864 0.2920 0.0111  0.0267  0.0606  388  ASP A CA  
2846  C C   . ASP A 390  ? 0.2910 0.2841 0.2969 0.0102  0.0255  0.0564  388  ASP A C   
2847  O O   . ASP A 390  ? 0.2517 0.2441 0.2544 0.0110  0.0258  0.0525  388  ASP A O   
2848  C CB  . ASP A 390  ? 0.2803 0.2829 0.2900 0.0099  0.0275  0.0659  388  ASP A CB  
2849  C CG  . ASP A 390  ? 0.2981 0.2978 0.3134 0.0083  0.0260  0.0696  388  ASP A CG  
2850  O OD1 . ASP A 390  ? 0.3053 0.2988 0.3224 0.0075  0.0243  0.0672  388  ASP A OD1 
2851  O OD2 . ASP A 390  ? 0.3415 0.3455 0.3598 0.0078  0.0266  0.0752  388  ASP A OD2 
2852  N N   . PHE A 391  ? 0.2602 0.2491 0.2710 0.0085  0.0242  0.0574  389  PHE A N   
2853  C CA  . PHE A 391  ? 0.2650 0.2489 0.2769 0.0076  0.0230  0.0536  389  PHE A CA  
2854  C C   . PHE A 391  ? 0.2451 0.2298 0.2603 0.0067  0.0236  0.0543  389  PHE A C   
2855  O O   . PHE A 391  ? 0.2476 0.2359 0.2659 0.0063  0.0244  0.0584  389  PHE A O   
2856  C CB  . PHE A 391  ? 0.2393 0.2185 0.2548 0.0065  0.0211  0.0534  389  PHE A CB  
2857  C CG  . PHE A 391  ? 0.2115 0.1899 0.2242 0.0074  0.0205  0.0527  389  PHE A CG  
2858  C CD1 . PHE A 391  ? 0.2669 0.2436 0.2751 0.0082  0.0202  0.0484  389  PHE A CD1 
2859  C CD2 . PHE A 391  ? 0.2331 0.2131 0.2477 0.0074  0.0203  0.0567  389  PHE A CD2 
2860  C CE1 . PHE A 391  ? 0.2738 0.2499 0.2794 0.0090  0.0196  0.0477  389  PHE A CE1 
2861  C CE2 . PHE A 391  ? 0.2508 0.2303 0.2626 0.0083  0.0197  0.0560  389  PHE A CE2 
2862  C CZ  . PHE A 391  ? 0.2689 0.2465 0.2763 0.0091  0.0194  0.0514  389  PHE A CZ  
2863  N N   . PRO A 392  ? 0.2236 0.2057 0.2382 0.0065  0.0231  0.0506  390  PRO A N   
2864  C CA  . PRO A 392  ? 0.2377 0.2202 0.2557 0.0055  0.0233  0.0510  390  PRO A CA  
2865  C C   . PRO A 392  ? 0.2473 0.2262 0.2710 0.0038  0.0217  0.0514  390  PRO A C   
2866  O O   . PRO A 392  ? 0.2465 0.2253 0.2734 0.0029  0.0215  0.0513  390  PRO A O   
2867  C CB  . PRO A 392  ? 0.2136 0.1949 0.2279 0.0063  0.0234  0.0468  390  PRO A CB  
2868  C CG  . PRO A 392  ? 0.2370 0.2147 0.2484 0.0065  0.0222  0.0438  390  PRO A CG  
2869  C CD  . PRO A 392  ? 0.2151 0.1943 0.2256 0.0071  0.0225  0.0461  390  PRO A CD  
2870  N N   . VAL A 393  ? 0.2415 0.2176 0.2665 0.0034  0.0203  0.0514  391  VAL A N   
2871  C CA  . VAL A 393  ? 0.2192 0.1918 0.2499 0.0020  0.0185  0.0513  391  VAL A CA  
2872  C C   . VAL A 393  ? 0.2351 0.2078 0.2693 0.0016  0.0179  0.0550  391  VAL A C   
2873  O O   . VAL A 393  ? 0.2417 0.2165 0.2728 0.0026  0.0187  0.0568  391  VAL A O   
2874  C CB  . VAL A 393  ? 0.2091 0.1777 0.2384 0.0020  0.0169  0.0465  391  VAL A CB  
2875  C CG1 . VAL A 393  ? 0.2311 0.1996 0.2581 0.0020  0.0172  0.0433  391  VAL A CG1 
2876  C CG2 . VAL A 393  ? 0.2239 0.1918 0.2486 0.0031  0.0169  0.0452  391  VAL A CG2 
2877  N N   . PHE A 394  ? 0.2098 0.1802 0.2507 0.0003  0.0163  0.0561  392  PHE A N   
2878  C CA  . PHE A 394  ? 0.2250 0.1947 0.2702 -0.0002 0.0152  0.0595  392  PHE A CA  
2879  C C   . PHE A 394  ? 0.2454 0.2121 0.2881 0.0007  0.0141  0.0567  392  PHE A C   
2880  O O   . PHE A 394  ? 0.2516 0.2164 0.2907 0.0012  0.0137  0.0519  392  PHE A O   
2881  C CB  . PHE A 394  ? 0.2435 0.2111 0.2973 -0.0018 0.0135  0.0610  392  PHE A CB  
2882  C CG  . PHE A 394  ? 0.2428 0.2136 0.2994 -0.0028 0.0146  0.0640  392  PHE A CG  
2883  C CD1 . PHE A 394  ? 0.2785 0.2540 0.3354 -0.0028 0.0163  0.0695  392  PHE A CD1 
2884  C CD2 . PHE A 394  ? 0.2515 0.2213 0.3102 -0.0036 0.0142  0.0614  392  PHE A CD2 
2885  C CE1 . PHE A 394  ? 0.2496 0.2287 0.3090 -0.0036 0.0175  0.0724  392  PHE A CE1 
2886  C CE2 . PHE A 394  ? 0.2260 0.1991 0.2872 -0.0044 0.0153  0.0643  392  PHE A CE2 
2887  C CZ  . PHE A 394  ? 0.2690 0.2467 0.3307 -0.0044 0.0170  0.0697  392  PHE A CZ  
2888  N N   . THR A 395  ? 0.2493 0.2161 0.2940 0.0008  0.0135  0.0599  393  THR A N   
2889  C CA  . THR A 395  ? 0.2759 0.2403 0.3189 0.0017  0.0124  0.0578  393  THR A CA  
2890  C C   . THR A 395  ? 0.2788 0.2395 0.3291 0.0010  0.0098  0.0581  393  THR A C   
2891  O O   . THR A 395  ? 0.2643 0.2225 0.3139 0.0017  0.0086  0.0554  393  THR A O   
2892  C CB  . THR A 395  ? 0.2481 0.2156 0.2867 0.0029  0.0136  0.0606  393  THR A CB  
2893  O OG1 . THR A 395  ? 0.2694 0.2395 0.3124 0.0022  0.0138  0.0668  393  THR A OG1 
2894  C CG2 . THR A 395  ? 0.2947 0.2656 0.3258 0.0040  0.0158  0.0591  393  THR A CG2 
2895  N N   . ARG A 396  ? 0.2638 0.2241 0.3215 -0.0004 0.0090  0.0611  394  ARG A N   
2896  C CA  . ARG A 396  ? 0.2651 0.2214 0.3308 -0.0012 0.0062  0.0606  394  ARG A CA  
2897  C C   . ARG A 396  ? 0.2686 0.2229 0.3378 -0.0021 0.0051  0.0570  394  ARG A C   
2898  O O   . ARG A 396  ? 0.2666 0.2230 0.3364 -0.0029 0.0062  0.0584  394  ARG A O   
2899  C CB  . ARG A 396  ? 0.3110 0.2680 0.3837 -0.0022 0.0055  0.0671  394  ARG A CB  
2900  C CG  . ARG A 396  ? 0.2937 0.2527 0.3637 -0.0012 0.0062  0.0710  394  ARG A CG  
2901  C CD  . ARG A 396  ? 0.3261 0.2854 0.4043 -0.0024 0.0050  0.0775  394  ARG A CD  
2902  N NE  . ARG A 396  ? 0.3674 0.3304 0.4423 -0.0016 0.0061  0.0823  394  ARG A NE  
2903  C CZ  . ARG A 396  ? 0.4486 0.4102 0.5273 -0.0014 0.0045  0.0852  394  ARG A CZ  
2904  N NH1 . ARG A 396  ? 0.4674 0.4239 0.5542 -0.0019 0.0015  0.0840  394  ARG A NH1 
2905  N NH2 . ARG A 396  ? 0.3940 0.3595 0.4685 -0.0004 0.0057  0.0891  394  ARG A NH2 
2906  N N   . LYS A 397  ? 0.2790 0.2299 0.3506 -0.0018 0.0030  0.0521  395  LYS A N   
2907  C CA  . LYS A 397  ? 0.2654 0.2149 0.3399 -0.0025 0.0018  0.0480  395  LYS A CA  
2908  C C   . LYS A 397  ? 0.2743 0.2235 0.3572 -0.0041 0.0008  0.0513  395  LYS A C   
2909  O O   . LYS A 397  ? 0.2674 0.2175 0.3512 -0.0049 0.0011  0.0500  395  LYS A O   
2910  C CB  . LYS A 397  ? 0.3273 0.2738 0.4037 -0.0018 -0.0005 0.0424  395  LYS A CB  
2911  C CG  . LYS A 397  ? 0.3328 0.2790 0.4094 -0.0020 -0.0014 0.0370  395  LYS A CG  
2912  C CD  . LYS A 397  ? 0.3447 0.2888 0.4310 -0.0031 -0.0040 0.0365  395  LYS A CD  
2913  C CE  . LYS A 397  ? 0.3359 0.2804 0.4221 -0.0031 -0.0049 0.0307  395  LYS A CE  
2914  N NZ  . LYS A 397  ? 0.3364 0.2788 0.4325 -0.0040 -0.0077 0.0297  395  LYS A NZ  
2915  N N   . ILE A 398  ? 0.2647 0.2130 0.3541 -0.0047 -0.0003 0.0559  396  ILE A N   
2916  C CA  . ILE A 398  ? 0.2732 0.2211 0.3717 -0.0065 -0.0015 0.0594  396  ILE A CA  
2917  C C   . ILE A 398  ? 0.2393 0.1914 0.3354 -0.0073 0.0011  0.0635  396  ILE A C   
2918  O O   . ILE A 398  ? 0.2806 0.2331 0.3825 -0.0087 0.0005  0.0648  396  ILE A O   
2919  C CB  . ILE A 398  ? 0.3355 0.2815 0.4416 -0.0069 -0.0034 0.0639  396  ILE A CB  
2920  C CG1 . ILE A 398  ? 0.3622 0.3065 0.4794 -0.0088 -0.0056 0.0662  396  ILE A CG1 
2921  C CG2 . ILE A 398  ? 0.2765 0.2261 0.3787 -0.0067 -0.0011 0.0702  396  ILE A CG2 
2922  C CD1 . ILE A 398  ? 0.4154 0.3559 0.5419 -0.0090 -0.0087 0.0677  396  ILE A CD1 
2923  N N   . HIS A 399  ? 0.2547 0.2103 0.3425 -0.0063 0.0038  0.0653  397  HIS A N   
2924  C CA  . HIS A 399  ? 0.3004 0.2605 0.3854 -0.0068 0.0064  0.0685  397  HIS A CA  
2925  C C   . HIS A 399  ? 0.2419 0.2021 0.3246 -0.0069 0.0068  0.0640  397  HIS A C   
2926  O O   . HIS A 399  ? 0.2563 0.2185 0.3421 -0.0080 0.0073  0.0659  397  HIS A O   
2927  C CB  . HIS A 399  ? 0.2730 0.2370 0.3496 -0.0054 0.0090  0.0706  397  HIS A CB  
2928  C CG  . HIS A 399  ? 0.2694 0.2347 0.3481 -0.0054 0.0089  0.0761  397  HIS A CG  
2929  N ND1 . HIS A 399  ? 0.2712 0.2398 0.3430 -0.0040 0.0108  0.0778  397  HIS A ND1 
2930  C CD2 . HIS A 399  ? 0.3439 0.3078 0.4311 -0.0065 0.0071  0.0804  397  HIS A CD2 
2931  C CE1 . HIS A 399  ? 0.2872 0.2567 0.3628 -0.0043 0.0102  0.0831  397  HIS A CE1 
2932  N NE2 . HIS A 399  ? 0.3092 0.2757 0.3942 -0.0059 0.0080  0.0850  397  HIS A NE2 
2933  N N   . THR A 400  ? 0.2278 0.1861 0.3053 -0.0058 0.0065  0.0581  398  THR A N   
2934  C CA  . THR A 400  ? 0.2032 0.1614 0.2791 -0.0059 0.0064  0.0537  398  THR A CA  
2935  C C   . THR A 400  ? 0.2277 0.1840 0.3123 -0.0073 0.0040  0.0527  398  THR A C   
2936  O O   . THR A 400  ? 0.2357 0.1933 0.3214 -0.0080 0.0044  0.0521  398  THR A O   
2937  C CB  . THR A 400  ? 0.2530 0.2097 0.3227 -0.0046 0.0061  0.0480  398  THR A CB  
2938  O OG1 . THR A 400  ? 0.2537 0.2125 0.3155 -0.0034 0.0084  0.0490  398  THR A OG1 
2939  C CG2 . THR A 400  ? 0.2364 0.1930 0.3049 -0.0047 0.0057  0.0434  398  THR A CG2 
2940  N N   . ASP A 401  ? 0.2413 0.1944 0.3327 -0.0077 0.0015  0.0524  399  ASP A N   
2941  C CA  . ASP A 401  ? 0.2338 0.1849 0.3342 -0.0090 -0.0010 0.0511  399  ASP A CA  
2942  C C   . ASP A 401  ? 0.2278 0.1810 0.3338 -0.0106 -0.0004 0.0567  399  ASP A C   
2943  O O   . ASP A 401  ? 0.2600 0.2136 0.3697 -0.0116 -0.0011 0.0555  399  ASP A O   
2944  C CB  . ASP A 401  ? 0.2402 0.1873 0.3474 -0.0089 -0.0041 0.0497  399  ASP A CB  
2945  C CG  . ASP A 401  ? 0.2773 0.2227 0.3802 -0.0074 -0.0051 0.0431  399  ASP A CG  
2946  O OD1 . ASP A 401  ? 0.2873 0.2341 0.3842 -0.0068 -0.0042 0.0390  399  ASP A OD1 
2947  O OD2 . ASP A 401  ? 0.3235 0.2664 0.4291 -0.0067 -0.0067 0.0423  399  ASP A OD2 
2948  N N   . VAL A 402  ? 0.2395 0.1945 0.3463 -0.0110 0.0009  0.0630  400  VAL A N   
2949  C CA  . VAL A 402  ? 0.2446 0.2027 0.3565 -0.0126 0.0017  0.0689  400  VAL A CA  
2950  C C   . VAL A 402  ? 0.2206 0.1827 0.3267 -0.0124 0.0043  0.0686  400  VAL A C   
2951  O O   . VAL A 402  ? 0.2498 0.2134 0.3606 -0.0137 0.0042  0.0699  400  VAL A O   
2952  C CB  . VAL A 402  ? 0.2778 0.2380 0.3910 -0.0128 0.0027  0.0760  400  VAL A CB  
2953  C CG1 . VAL A 402  ? 0.2404 0.2049 0.3579 -0.0144 0.0041  0.0824  400  VAL A CG1 
2954  C CG2 . VAL A 402  ? 0.2923 0.2481 0.4130 -0.0132 -0.0002 0.0768  400  VAL A CG2 
2955  N N   . SER A 403  ? 0.2658 0.2297 0.3620 -0.0107 0.0065  0.0668  401  SER A N   
2956  C CA  . SER A 403  ? 0.2338 0.2011 0.3245 -0.0103 0.0088  0.0659  401  SER A CA  
2957  C C   . SER A 403  ? 0.2687 0.2345 0.3617 -0.0108 0.0073  0.0613  401  SER A C   
2958  O O   . SER A 403  ? 0.2422 0.2106 0.3369 -0.0116 0.0081  0.0624  401  SER A O   
2959  C CB  . SER A 403  ? 0.2490 0.2174 0.3295 -0.0083 0.0107  0.0635  401  SER A CB  
2960  O OG  . SER A 403  ? 0.2464 0.2177 0.3221 -0.0078 0.0125  0.0621  401  SER A OG  
2961  N N   . TYR A 404  ? 0.2316 0.1936 0.3249 -0.0104 0.0052  0.0560  402  TYR A N   
2962  C CA  . TYR A 404  ? 0.2452 0.2061 0.3403 -0.0108 0.0036  0.0513  402  TYR A CA  
2963  C C   . TYR A 404  ? 0.2412 0.2021 0.3461 -0.0127 0.0020  0.0534  402  TYR A C   
2964  O O   . TYR A 404  ? 0.2324 0.1952 0.3382 -0.0132 0.0023  0.0526  402  TYR A O   
2965  C CB  . TYR A 404  ? 0.2269 0.1844 0.3213 -0.0100 0.0015  0.0456  402  TYR A CB  
2966  C CG  . TYR A 404  ? 0.2243 0.1817 0.3181 -0.0099 0.0002  0.0401  402  TYR A CG  
2967  C CD1 . TYR A 404  ? 0.2336 0.1902 0.3356 -0.0111 -0.0022 0.0386  402  TYR A CD1 
2968  C CD2 . TYR A 404  ? 0.2252 0.1836 0.3108 -0.0087 0.0013  0.0365  402  TYR A CD2 
2969  C CE1 . TYR A 404  ? 0.2547 0.2118 0.3560 -0.0109 -0.0034 0.0335  402  TYR A CE1 
2970  C CE2 . TYR A 404  ? 0.2122 0.1711 0.2973 -0.0086 0.0001  0.0318  402  TYR A CE2 
2971  C CZ  . TYR A 404  ? 0.2249 0.1833 0.3176 -0.0096 -0.0022 0.0302  402  TYR A CZ  
2972  O OH  . TYR A 404  ? 0.2575 0.2171 0.3496 -0.0095 -0.0035 0.0255  402  TYR A OH  
2973  N N   . ILE A 405  ? 0.2455 0.2044 0.3582 -0.0136 0.0003  0.0562  403  ILE A N   
2974  C CA  . ILE A 405  ? 0.2616 0.2201 0.3846 -0.0156 -0.0016 0.0581  403  ILE A CA  
2975  C C   . ILE A 405  ? 0.2499 0.2129 0.3737 -0.0166 0.0008  0.0638  403  ILE A C   
2976  O O   . ILE A 405  ? 0.2496 0.2138 0.3782 -0.0178 0.0002  0.0638  403  ILE A O   
2977  C CB  . ILE A 405  ? 0.2664 0.2214 0.3981 -0.0163 -0.0042 0.0600  403  ILE A CB  
2978  C CG1 . ILE A 405  ? 0.2773 0.2283 0.4087 -0.0152 -0.0067 0.0533  403  ILE A CG1 
2979  C CG2 . ILE A 405  ? 0.2665 0.2211 0.4096 -0.0185 -0.0062 0.0627  403  ILE A CG2 
2980  C CD1 . ILE A 405  ? 0.3440 0.2915 0.4803 -0.0150 -0.0087 0.0544  403  ILE A CD1 
2981  N N   . ALA A 406  ? 0.2560 0.2221 0.3748 -0.0160 0.0035  0.0684  404  ALA A N   
2982  C CA  . ALA A 406  ? 0.2468 0.2181 0.3656 -0.0167 0.0059  0.0736  404  ALA A CA  
2983  C C   . ALA A 406  ? 0.2616 0.2353 0.3753 -0.0160 0.0074  0.0704  404  ALA A C   
2984  O O   . ALA A 406  ? 0.2757 0.2526 0.3931 -0.0171 0.0080  0.0727  404  ALA A O   
2985  C CB  . ALA A 406  ? 0.2837 0.2583 0.3971 -0.0157 0.0086  0.0782  404  ALA A CB  
2986  N N   . CYS A 407  ? 0.2519 0.2244 0.3574 -0.0143 0.0078  0.0653  405  CYS A N   
2987  C CA  . CYS A 407  ? 0.2391 0.2136 0.3398 -0.0136 0.0090  0.0622  405  CYS A CA  
2988  C C   . CYS A 407  ? 0.2722 0.2451 0.3784 -0.0147 0.0066  0.0587  405  CYS A C   
2989  O O   . CYS A 407  ? 0.2365 0.2120 0.3425 -0.0148 0.0073  0.0582  405  CYS A O   
2990  C CB  . CYS A 407  ? 0.2195 0.1931 0.3105 -0.0116 0.0100  0.0583  405  CYS A CB  
2991  S SG  . CYS A 407  ? 0.2941 0.2712 0.3781 -0.0102 0.0132  0.0623  405  CYS A SG  
2992  N N   . ALA A 408  ? 0.2475 0.2164 0.3590 -0.0153 0.0036  0.0561  406  ALA A N   
2993  C CA  . ALA A 408  ? 0.2167 0.1844 0.3343 -0.0163 0.0011  0.0527  406  ALA A CA  
2994  C C   . ALA A 408  ? 0.2185 0.1883 0.3447 -0.0182 0.0009  0.0571  406  ALA A C   
2995  O O   . ALA A 408  ? 0.2603 0.2314 0.3892 -0.0189 0.0001  0.0555  406  ALA A O   
2996  C CB  . ALA A 408  ? 0.2688 0.2321 0.3907 -0.0163 -0.0021 0.0487  406  ALA A CB  
2997  N N   . ALA A 409  ? 0.2479 0.2183 0.3785 -0.0192 0.0014  0.0631  407  ALA A N   
2998  C CA  . ALA A 409  ? 0.2664 0.2396 0.4052 -0.0211 0.0015  0.0681  407  ALA A CA  
2999  C C   . ALA A 409  ? 0.2583 0.2367 0.3927 -0.0208 0.0043  0.0696  407  ALA A C   
3000  O O   . ALA A 409  ? 0.2521 0.2324 0.3919 -0.0221 0.0038  0.0703  407  ALA A O   
3001  C CB  . ALA A 409  ? 0.2578 0.2315 0.4012 -0.0221 0.0019  0.0748  407  ALA A CB  
3002  N N   . LYS A 410  ? 0.2319 0.2126 0.3566 -0.0190 0.0072  0.0699  408  LYS A N   
3003  C CA  . LYS A 410  ? 0.2149 0.2004 0.3351 -0.0183 0.0097  0.0707  408  LYS A CA  
3004  C C   . LYS A 410  ? 0.2273 0.2120 0.3463 -0.0180 0.0086  0.0652  408  LYS A C   
3005  O O   . LYS A 410  ? 0.2434 0.2314 0.3649 -0.0186 0.0091  0.0661  408  LYS A O   
3006  C CB  . LYS A 410  ? 0.2444 0.2320 0.3548 -0.0163 0.0126  0.0711  408  LYS A CB  
3007  C CG  . LYS A 410  ? 0.2655 0.2581 0.3710 -0.0152 0.0152  0.0717  408  LYS A CG  
3008  C CD  . LYS A 410  ? 0.2740 0.2680 0.3702 -0.0130 0.0175  0.0712  408  LYS A CD  
3009  C CE  . LYS A 410  ? 0.2858 0.2821 0.3820 -0.0130 0.0189  0.0764  408  LYS A CE  
3010  N NZ  . LYS A 410  ? 0.2957 0.2983 0.3961 -0.0139 0.0207  0.0820  408  LYS A NZ  
3011  N N   . LEU A 411  ? 0.2191 0.2000 0.3342 -0.0170 0.0071  0.0597  409  LEU A N   
3012  C CA  . LEU A 411  ? 0.2149 0.1955 0.3284 -0.0166 0.0059  0.0546  409  LEU A CA  
3013  C C   . LEU A 411  ? 0.2077 0.1879 0.3306 -0.0184 0.0033  0.0539  409  LEU A C   
3014  O O   . LEU A 411  ? 0.2184 0.2009 0.3420 -0.0186 0.0032  0.0525  409  LEU A O   
3015  C CB  . LEU A 411  ? 0.2235 0.2006 0.3313 -0.0153 0.0047  0.0493  409  LEU A CB  
3016  C CG  . LEU A 411  ? 0.2061 0.1841 0.3038 -0.0134 0.0071  0.0486  409  LEU A CG  
3017  C CD1 . LEU A 411  ? 0.2480 0.2225 0.3413 -0.0124 0.0060  0.0446  409  LEU A CD1 
3018  C CD2 . LEU A 411  ? 0.2356 0.2163 0.3291 -0.0126 0.0082  0.0471  409  LEU A CD2 
3019  N N   . LEU A 412  ? 0.2063 0.1836 0.3369 -0.0197 0.0011  0.0547  410  LEU A N   
3020  C CA  . LEU A 412  ? 0.2048 0.1815 0.3451 -0.0215 -0.0018 0.0536  410  LEU A CA  
3021  C C   . LEU A 412  ? 0.2365 0.2172 0.3825 -0.0230 -0.0007 0.0586  410  LEU A C   
3022  O O   . LEU A 412  ? 0.2993 0.2805 0.4521 -0.0243 -0.0027 0.0573  410  LEU A O   
3023  C CB  . LEU A 412  ? 0.2493 0.2218 0.3971 -0.0224 -0.0047 0.0531  410  LEU A CB  
3024  C CG  . LEU A 412  ? 0.2364 0.2052 0.3805 -0.0210 -0.0067 0.0466  410  LEU A CG  
3025  C CD1 . LEU A 412  ? 0.2928 0.2575 0.4439 -0.0216 -0.0092 0.0465  410  LEU A CD1 
3026  C CD2 . LEU A 412  ? 0.2988 0.2682 0.4438 -0.0209 -0.0087 0.0407  410  LEU A CD2 
3027  N N   . ALA A 413  ? 0.2389 0.2229 0.3823 -0.0229 0.0023  0.0641  411  ALA A N   
3028  C CA  . ALA A 413  ? 0.2445 0.2335 0.3925 -0.0241 0.0038  0.0688  411  ALA A CA  
3029  C C   . ALA A 413  ? 0.2705 0.2630 0.4129 -0.0230 0.0054  0.0667  411  ALA A C   
3030  O O   . ALA A 413  ? 0.2822 0.2791 0.4284 -0.0238 0.0065  0.0699  411  ALA A O   
3031  C CB  . ALA A 413  ? 0.3091 0.3013 0.4567 -0.0244 0.0064  0.0756  411  ALA A CB  
3032  N N   . ALA A 414  ? 0.2588 0.2497 0.3929 -0.0211 0.0055  0.0617  412  ALA A N   
3033  C CA  . ALA A 414  ? 0.2947 0.2888 0.4231 -0.0198 0.0071  0.0600  412  ALA A CA  
3034  C C   . ALA A 414  ? 0.2778 0.2697 0.4043 -0.0192 0.0049  0.0539  412  ALA A C   
3035  O O   . ALA A 414  ? 0.2352 0.2283 0.3547 -0.0176 0.0060  0.0515  412  ALA A O   
3036  C CB  . ALA A 414  ? 0.3053 0.3009 0.4243 -0.0177 0.0102  0.0610  412  ALA A CB  
3037  N N   . THR A 415  ? 0.2541 0.2434 0.3871 -0.0205 0.0017  0.0512  413  THR A N   
3038  C CA  . THR A 415  ? 0.2734 0.2614 0.4046 -0.0198 -0.0005 0.0452  413  THR A CA  
3039  C C   . THR A 415  ? 0.2616 0.2532 0.3931 -0.0198 -0.0004 0.0444  413  THR A C   
3040  O O   . THR A 415  ? 0.2783 0.2699 0.4063 -0.0190 -0.0016 0.0400  413  THR A O   
3041  C CB  . THR A 415  ? 0.2834 0.2681 0.4219 -0.0210 -0.0041 0.0421  413  THR A CB  
3042  O OG1 . THR A 415  ? 0.2930 0.2788 0.4417 -0.0231 -0.0054 0.0447  413  THR A OG1 
3043  C CG2 . THR A 415  ? 0.3021 0.2829 0.4402 -0.0208 -0.0044 0.0425  413  THR A CG2 
3044  N N   . ASP A 416  ? 0.2608 0.2559 0.3966 -0.0208 0.0011  0.0488  414  ASP A N   
3045  C CA  . ASP A 416  ? 0.2861 0.2850 0.4216 -0.0205 0.0014  0.0482  414  ASP A CA  
3046  C C   . ASP A 416  ? 0.2752 0.2755 0.4009 -0.0183 0.0037  0.0473  414  ASP A C   
3047  O O   . ASP A 416  ? 0.3498 0.3519 0.4735 -0.0176 0.0034  0.0451  414  ASP A O   
3048  C CB  . ASP A 416  ? 0.3030 0.3058 0.4456 -0.0220 0.0025  0.0532  414  ASP A CB  
3049  C CG  . ASP A 416  ? 0.3961 0.4012 0.5360 -0.0215 0.0059  0.0583  414  ASP A CG  
3050  O OD1 . ASP A 416  ? 0.3883 0.3907 0.5259 -0.0213 0.0063  0.0594  414  ASP A OD1 
3051  O OD2 . ASP A 416  ? 0.5392 0.5490 0.6792 -0.0213 0.0080  0.0612  414  ASP A OD2 
3052  N N   . VAL A 417  ? 0.2421 0.2415 0.3619 -0.0171 0.0060  0.0490  415  VAL A N   
3053  C CA  . VAL A 417  ? 0.3169 0.3177 0.4282 -0.0151 0.0081  0.0485  415  VAL A CA  
3054  C C   . VAL A 417  ? 0.2735 0.2708 0.3773 -0.0137 0.0080  0.0455  415  VAL A C   
3055  O O   . VAL A 417  ? 0.2535 0.2514 0.3507 -0.0121 0.0090  0.0441  415  VAL A O   
3056  C CB  . VAL A 417  ? 0.3269 0.3313 0.4372 -0.0145 0.0113  0.0531  415  VAL A CB  
3057  C CG1 . VAL A 417  ? 0.4112 0.4200 0.5286 -0.0158 0.0116  0.0562  415  VAL A CG1 
3058  C CG2 . VAL A 417  ? 0.3199 0.3226 0.4301 -0.0149 0.0122  0.0558  415  VAL A CG2 
3059  N N   . VAL A 418  ? 0.2344 0.2281 0.3390 -0.0142 0.0067  0.0445  416  VAL A N   
3060  C CA  . VAL A 418  ? 0.2030 0.1937 0.3011 -0.0131 0.0062  0.0411  416  VAL A CA  
3061  C C   . VAL A 418  ? 0.1985 0.1865 0.3004 -0.0140 0.0032  0.0375  416  VAL A C   
3062  O O   . VAL A 418  ? 0.2240 0.2118 0.3337 -0.0155 0.0015  0.0381  416  VAL A O   
3063  C CB  . VAL A 418  ? 0.1887 0.1778 0.2824 -0.0123 0.0081  0.0432  416  VAL A CB  
3064  C CG1 . VAL A 418  ? 0.2661 0.2582 0.3553 -0.0110 0.0111  0.0458  416  VAL A CG1 
3065  C CG2 . VAL A 418  ? 0.2330 0.2209 0.3328 -0.0137 0.0077  0.0461  416  VAL A CG2 
3066  N N   . PHE A 419  ? 0.2010 0.1873 0.2975 -0.0129 0.0023  0.0338  417  PHE A N   
3067  C CA  . PHE A 419  ? 0.2178 0.2020 0.3167 -0.0133 -0.0005 0.0297  417  PHE A CA  
3068  C C   . PHE A 419  ? 0.1933 0.1743 0.2894 -0.0129 -0.0002 0.0294  417  PHE A C   
3069  O O   . PHE A 419  ? 0.2265 0.2069 0.3153 -0.0116 0.0007  0.0280  417  PHE A O   
3070  C CB  . PHE A 419  ? 0.2037 0.1893 0.2985 -0.0125 -0.0017 0.0255  417  PHE A CB  
3071  C CG  . PHE A 419  ? 0.2319 0.2164 0.3282 -0.0126 -0.0045 0.0208  417  PHE A CG  
3072  C CD1 . PHE A 419  ? 0.2535 0.2375 0.3581 -0.0138 -0.0070 0.0193  417  PHE A CD1 
3073  C CD2 . PHE A 419  ? 0.2222 0.2064 0.3119 -0.0114 -0.0047 0.0177  417  PHE A CD2 
3074  C CE1 . PHE A 419  ? 0.2143 0.1976 0.3205 -0.0137 -0.0097 0.0143  417  PHE A CE1 
3075  C CE2 . PHE A 419  ? 0.1979 0.1819 0.2891 -0.0113 -0.0072 0.0132  417  PHE A CE2 
3076  C CZ  . PHE A 419  ? 0.2191 0.2027 0.3184 -0.0123 -0.0097 0.0112  417  PHE A CZ  
3077  N N   . PRO A 420  ? 0.2060 0.1849 0.3080 -0.0139 -0.0010 0.0309  418  PRO A N   
3078  C CA  . PRO A 420  ? 0.2172 0.1932 0.3169 -0.0133 -0.0008 0.0309  418  PRO A CA  
3079  C C   . PRO A 420  ? 0.2236 0.1980 0.3219 -0.0127 -0.0030 0.0255  418  PRO A C   
3080  O O   . PRO A 420  ? 0.2281 0.2028 0.3312 -0.0132 -0.0056 0.0221  418  PRO A O   
3081  C CB  . PRO A 420  ? 0.2054 0.1801 0.3132 -0.0147 -0.0014 0.0344  418  PRO A CB  
3082  C CG  . PRO A 420  ? 0.2290 0.2066 0.3415 -0.0159 -0.0007 0.0376  418  PRO A CG  
3083  C CD  . PRO A 420  ? 0.2282 0.2076 0.3395 -0.0156 -0.0019 0.0336  418  PRO A CD  
3084  N N   . GLN A 421  ? 0.1989 0.1720 0.2908 -0.0115 -0.0021 0.0246  419  GLN A N   
3085  C CA  . GLN A 421  ? 0.2231 0.1953 0.3125 -0.0107 -0.0038 0.0197  419  GLN A CA  
3086  C C   . GLN A 421  ? 0.2191 0.1883 0.3079 -0.0103 -0.0035 0.0205  419  GLN A C   
3087  O O   . GLN A 421  ? 0.2312 0.2002 0.3142 -0.0096 -0.0013 0.0227  419  GLN A O   
3088  C CB  . GLN A 421  ? 0.1909 0.1652 0.2722 -0.0096 -0.0028 0.0178  419  GLN A CB  
3089  C CG  . GLN A 421  ? 0.2059 0.1833 0.2875 -0.0099 -0.0029 0.0176  419  GLN A CG  
3090  C CD  . GLN A 421  ? 0.2300 0.2092 0.3037 -0.0088 -0.0015 0.0173  419  GLN A CD  
3091  O OE1 . GLN A 421  ? 0.2418 0.2204 0.3109 -0.0082 0.0008  0.0201  419  GLN A OE1 
3092  N NE2 . GLN A 421  ? 0.2369 0.2185 0.3090 -0.0085 -0.0030 0.0139  419  GLN A NE2 
3093  N N   . PHE A 422  ? 0.1973 0.1645 0.2925 -0.0108 -0.0058 0.0187  420  PHE A N   
3094  C CA  . PHE A 422  ? 0.2246 0.1889 0.3210 -0.0106 -0.0058 0.0201  420  PHE A CA  
3095  C C   . PHE A 422  ? 0.2039 0.1675 0.2960 -0.0093 -0.0068 0.0154  420  PHE A C   
3096  O O   . PHE A 422  ? 0.2269 0.1899 0.3233 -0.0092 -0.0094 0.0110  420  PHE A O   
3097  C CB  . PHE A 422  ? 0.2220 0.1841 0.3285 -0.0119 -0.0079 0.0214  420  PHE A CB  
3098  C CG  . PHE A 422  ? 0.2483 0.2117 0.3590 -0.0133 -0.0067 0.0266  420  PHE A CG  
3099  C CD1 . PHE A 422  ? 0.2466 0.2108 0.3539 -0.0133 -0.0039 0.0319  420  PHE A CD1 
3100  C CD2 . PHE A 422  ? 0.2293 0.1935 0.3473 -0.0145 -0.0086 0.0258  420  PHE A CD2 
3101  C CE1 . PHE A 422  ? 0.2288 0.1948 0.3398 -0.0144 -0.0027 0.0366  420  PHE A CE1 
3102  C CE2 . PHE A 422  ? 0.2427 0.2085 0.3647 -0.0158 -0.0075 0.0306  420  PHE A CE2 
3103  C CZ  . PHE A 422  ? 0.2430 0.2099 0.3614 -0.0158 -0.0045 0.0361  420  PHE A CZ  
3104  N N   . ALA A 423  ? 0.2143 0.1783 0.2983 -0.0083 -0.0046 0.0162  421  ALA A N   
3105  C CA  . ALA A 423  ? 0.2223 0.1863 0.3015 -0.0071 -0.0050 0.0123  421  ALA A CA  
3106  C C   . ALA A 423  ? 0.2596 0.2206 0.3412 -0.0068 -0.0055 0.0131  421  ALA A C   
3107  O O   . ALA A 423  ? 0.2992 0.2590 0.3788 -0.0068 -0.0037 0.0173  421  ALA A O   
3108  C CB  . ALA A 423  ? 0.2238 0.1895 0.2939 -0.0063 -0.0026 0.0132  421  ALA A CB  
3109  N N   . THR A 424  ? 0.2130 0.1730 0.2990 -0.0065 -0.0081 0.0090  422  THR A N   
3110  C CA  . THR A 424  ? 0.2327 0.1897 0.3212 -0.0061 -0.0088 0.0094  422  THR A CA  
3111  C C   . THR A 424  ? 0.2562 0.2131 0.3482 -0.0053 -0.0117 0.0033  422  THR A C   
3112  O O   . THR A 424  ? 0.2624 0.2206 0.3586 -0.0055 -0.0137 -0.0002 422  THR A O   
3113  C CB  . THR A 424  ? 0.2627 0.2172 0.3585 -0.0072 -0.0091 0.0141  422  THR A CB  
3114  O OG1 . THR A 424  ? 0.2699 0.2217 0.3674 -0.0067 -0.0096 0.0150  422  THR A OG1 
3115  C CG2 . THR A 424  ? 0.2924 0.2463 0.3976 -0.0083 -0.0118 0.0126  422  THR A CG2 
3116  N N   . HIS A 425  ? 0.2502 0.2058 0.3404 -0.0042 -0.0118 0.0020  423  HIS A N   
3117  C CA  . HIS A 425  ? 0.2366 0.1918 0.3310 -0.0033 -0.0146 -0.0035 423  HIS A CA  
3118  C C   . HIS A 425  ? 0.2562 0.2074 0.3592 -0.0035 -0.0165 -0.0022 423  HIS A C   
3119  O O   . HIS A 425  ? 0.2949 0.2453 0.4024 -0.0026 -0.0191 -0.0067 423  HIS A O   
3120  C CB  . HIS A 425  ? 0.2771 0.2343 0.3643 -0.0018 -0.0138 -0.0065 423  HIS A CB  
3121  C CG  . HIS A 425  ? 0.2610 0.2223 0.3405 -0.0016 -0.0123 -0.0079 423  HIS A CG  
3122  N ND1 . HIS A 425  ? 0.3130 0.2756 0.3841 -0.0011 -0.0099 -0.0065 423  HIS A ND1 
3123  C CD2 . HIS A 425  ? 0.2902 0.2548 0.3696 -0.0019 -0.0130 -0.0103 423  HIS A CD2 
3124  C CE1 . HIS A 425  ? 0.3018 0.2681 0.3681 -0.0011 -0.0092 -0.0078 423  HIS A CE1 
3125  N NE2 . HIS A 425  ? 0.2984 0.2660 0.3693 -0.0015 -0.0110 -0.0101 423  HIS A NE2 
3126  N N   . ASN A 426  ? 0.2555 0.2045 0.3610 -0.0047 -0.0154 0.0040  424  ASN A N   
3127  C CA  . ASN A 426  ? 0.2623 0.2075 0.3757 -0.0051 -0.0170 0.0066  424  ASN A CA  
3128  C C   . ASN A 426  ? 0.3379 0.2817 0.4620 -0.0062 -0.0198 0.0058  424  ASN A C   
3129  O O   . ASN A 426  ? 0.2917 0.2362 0.4178 -0.0077 -0.0191 0.0094  424  ASN A O   
3130  C CB  . ASN A 426  ? 0.2870 0.2314 0.3975 -0.0057 -0.0143 0.0139  424  ASN A CB  
3131  C CG  . ASN A 426  ? 0.2761 0.2171 0.3938 -0.0061 -0.0157 0.0174  424  ASN A CG  
3132  O OD1 . ASN A 426  ? 0.3291 0.2679 0.4567 -0.0068 -0.0185 0.0169  424  ASN A OD1 
3133  N ND2 . ASN A 426  ? 0.2892 0.2298 0.4022 -0.0056 -0.0138 0.0211  424  ASN A ND2 
3134  N N   . ALA A 427  ? 0.2538 0.1957 0.3852 -0.0056 -0.0232 0.0012  425  ALA A N   
3135  C CA  . ALA A 427  ? 0.2622 0.2027 0.4044 -0.0066 -0.0264 -0.0003 425  ALA A CA  
3136  C C   . ALA A 427  ? 0.2628 0.2005 0.4123 -0.0085 -0.0264 0.0069  425  ALA A C   
3137  O O   . ALA A 427  ? 0.2753 0.2128 0.4321 -0.0099 -0.0279 0.0076  425  ALA A O   
3138  C CB  . ALA A 427  ? 0.3007 0.2396 0.4499 -0.0053 -0.0302 -0.0068 425  ALA A CB  
3139  N N   . GLN A 428  ? 0.2988 0.2349 0.4468 -0.0086 -0.0248 0.0123  426  GLN A N   
3140  C CA  . GLN A 428  ? 0.3115 0.2458 0.4660 -0.0104 -0.0246 0.0198  426  GLN A CA  
3141  C C   . GLN A 428  ? 0.2959 0.2333 0.4458 -0.0117 -0.0216 0.0243  426  GLN A C   
3142  O O   . GLN A 428  ? 0.2931 0.2305 0.4502 -0.0134 -0.0223 0.0276  426  GLN A O   
3143  C CB  . GLN A 428  ? 0.3027 0.2351 0.4561 -0.0099 -0.0237 0.0244  426  GLN A CB  
3144  C CG  . GLN A 428  ? 0.3227 0.2531 0.4851 -0.0117 -0.0244 0.0319  426  GLN A CG  
3145  C CD  . GLN A 428  ? 0.3765 0.3099 0.5359 -0.0133 -0.0213 0.0387  426  GLN A CD  
3146  O OE1 . GLN A 428  ? 0.3856 0.3220 0.5345 -0.0127 -0.0179 0.0397  426  GLN A OE1 
3147  N NE2 . GLN A 428  ? 0.3160 0.2487 0.4851 -0.0153 -0.0225 0.0435  426  GLN A NE2 
3148  N N   . THR A 429  ? 0.2962 0.2365 0.4347 -0.0108 -0.0183 0.0245  427  THR A N   
3149  C CA  . THR A 429  ? 0.2727 0.2162 0.4062 -0.0116 -0.0155 0.0278  427  THR A CA  
3150  C C   . THR A 429  ? 0.3061 0.2509 0.4437 -0.0124 -0.0170 0.0245  427  THR A C   
3151  O O   . THR A 429  ? 0.2826 0.2286 0.4240 -0.0139 -0.0165 0.0283  427  THR A O   
3152  C CB  . THR A 429  ? 0.3056 0.2516 0.4268 -0.0102 -0.0125 0.0267  427  THR A CB  
3153  O OG1 . THR A 429  ? 0.2975 0.2423 0.4151 -0.0093 -0.0115 0.0286  427  THR A OG1 
3154  C CG2 . THR A 429  ? 0.2849 0.2339 0.4014 -0.0109 -0.0095 0.0310  427  THR A CG2 
3155  N N   . LEU A 430  ? 0.2502 0.1953 0.3871 -0.0113 -0.0190 0.0173  428  LEU A N   
3156  C CA  . LEU A 430  ? 0.2684 0.2152 0.4088 -0.0119 -0.0207 0.0135  428  LEU A CA  
3157  C C   . LEU A 430  ? 0.3197 0.2643 0.4725 -0.0136 -0.0233 0.0153  428  LEU A C   
3158  O O   . LEU A 430  ? 0.2832 0.2295 0.4389 -0.0150 -0.0231 0.0172  428  LEU A O   
3159  C CB  . LEU A 430  ? 0.2520 0.1996 0.3905 -0.0102 -0.0227 0.0053  428  LEU A CB  
3160  C CG  . LEU A 430  ? 0.3276 0.2783 0.4664 -0.0101 -0.0242 -0.0001 428  LEU A CG  
3161  C CD1 . LEU A 430  ? 0.3550 0.3074 0.4896 -0.0081 -0.0253 -0.0071 428  LEU A CD1 
3162  C CD2 . LEU A 430  ? 0.3340 0.2834 0.4846 -0.0114 -0.0275 -0.0014 428  LEU A CD2 
3163  N N   . ALA A 431  ? 0.2852 0.2262 0.4460 -0.0135 -0.0260 0.0146  429  ALA A N   
3164  C CA  . ALA A 431  ? 0.3024 0.2410 0.4762 -0.0152 -0.0291 0.0160  429  ALA A CA  
3165  C C   . ALA A 431  ? 0.2719 0.2109 0.4484 -0.0173 -0.0271 0.0246  429  ALA A C   
3166  O O   . ALA A 431  ? 0.2863 0.2257 0.4706 -0.0190 -0.0284 0.0261  429  ALA A O   
3167  C CB  . ALA A 431  ? 0.2892 0.2235 0.4708 -0.0146 -0.0322 0.0144  429  ALA A CB  
3168  N N   . ALA A 432  ? 0.2719 0.2115 0.4424 -0.0171 -0.0240 0.0303  430  ALA A N   
3169  C CA  . ALA A 432  ? 0.2947 0.2358 0.4670 -0.0189 -0.0219 0.0386  430  ALA A CA  
3170  C C   . ALA A 432  ? 0.2669 0.2118 0.4361 -0.0196 -0.0201 0.0392  430  ALA A C   
3171  O O   . ALA A 432  ? 0.2919 0.2379 0.4680 -0.0215 -0.0202 0.0436  430  ALA A O   
3172  C CB  . ALA A 432  ? 0.2878 0.2297 0.4521 -0.0181 -0.0187 0.0435  430  ALA A CB  
3173  N N   . ILE A 433  ? 0.2944 0.2417 0.4538 -0.0182 -0.0185 0.0348  431  ILE A N   
3174  C CA  . ILE A 433  ? 0.2866 0.2377 0.4426 -0.0187 -0.0167 0.0353  431  ILE A CA  
3175  C C   . ILE A 433  ? 0.2743 0.2254 0.4380 -0.0196 -0.0198 0.0310  431  ILE A C   
3176  O O   . ILE A 433  ? 0.2829 0.2362 0.4498 -0.0209 -0.0194 0.0334  431  ILE A O   
3177  C CB  . ILE A 433  ? 0.2870 0.2404 0.4303 -0.0169 -0.0141 0.0325  431  ILE A CB  
3178  C CG1 . ILE A 433  ? 0.3274 0.2812 0.4639 -0.0163 -0.0110 0.0373  431  ILE A CG1 
3179  C CG2 . ILE A 433  ? 0.3050 0.2620 0.4452 -0.0172 -0.0129 0.0319  431  ILE A CG2 
3180  C CD1 . ILE A 433  ? 0.3124 0.2677 0.4374 -0.0145 -0.0088 0.0345  431  ILE A CD1 
3181  N N   . TYR A 434  ? 0.2650 0.2139 0.4317 -0.0187 -0.0230 0.0244  432  TYR A N   
3182  C CA  . TYR A 434  ? 0.2943 0.2432 0.4690 -0.0194 -0.0263 0.0198  432  TYR A CA  
3183  C C   . TYR A 434  ? 0.3244 0.2719 0.5113 -0.0217 -0.0280 0.0245  432  TYR A C   
3184  O O   . TYR A 434  ? 0.3137 0.2632 0.5050 -0.0230 -0.0287 0.0244  432  TYR A O   
3185  C CB  . TYR A 434  ? 0.2946 0.2414 0.4716 -0.0179 -0.0296 0.0123  432  TYR A CB  
3186  C CG  . TYR A 434  ? 0.2947 0.2411 0.4818 -0.0185 -0.0338 0.0072  432  TYR A CG  
3187  C CD1 . TYR A 434  ? 0.3418 0.2917 0.5270 -0.0184 -0.0342 0.0032  432  TYR A CD1 
3188  C CD2 . TYR A 434  ? 0.3314 0.2737 0.5303 -0.0190 -0.0375 0.0062  432  TYR A CD2 
3189  C CE1 . TYR A 434  ? 0.3131 0.2630 0.5075 -0.0188 -0.0381 -0.0019 432  TYR A CE1 
3190  C CE2 . TYR A 434  ? 0.3316 0.2735 0.5402 -0.0195 -0.0415 0.0010  432  TYR A CE2 
3191  C CZ  . TYR A 434  ? 0.4019 0.3477 0.6082 -0.0194 -0.0418 -0.0031 432  TYR A CZ  
3192  O OH  . TYR A 434  ? 0.4635 0.4091 0.6796 -0.0198 -0.0460 -0.0085 432  TYR A OH  
3193  N N   . HIS A 435  ? 0.2867 0.2311 0.4795 -0.0225 -0.0286 0.0289  433  HIS A N   
3194  C CA  . HIS A 435  ? 0.3102 0.2534 0.5151 -0.0249 -0.0302 0.0342  433  HIS A CA  
3195  C C   . HIS A 435  ? 0.2976 0.2445 0.4999 -0.0263 -0.0265 0.0421  433  HIS A C   
3196  O O   . HIS A 435  ? 0.3139 0.2619 0.5242 -0.0283 -0.0273 0.0452  433  HIS A O   
3197  C CB  . HIS A 435  ? 0.3221 0.2608 0.5350 -0.0252 -0.0324 0.0364  433  HIS A CB  
3198  C CG  . HIS A 435  ? 0.3738 0.3091 0.5930 -0.0242 -0.0368 0.0286  433  HIS A CG  
3199  N ND1 . HIS A 435  ? 0.4064 0.3398 0.6380 -0.0254 -0.0409 0.0258  433  HIS A ND1 
3200  C CD2 . HIS A 435  ? 0.3090 0.2427 0.5235 -0.0219 -0.0377 0.0226  433  HIS A CD2 
3201  C CE1 . HIS A 435  ? 0.3664 0.2974 0.6009 -0.0238 -0.0442 0.0182  433  HIS A CE1 
3202  N NE2 . HIS A 435  ? 0.3313 0.2625 0.5554 -0.0216 -0.0423 0.0161  433  HIS A NE2 
3203  N N   . MET A 436  ? 0.3164 0.2653 0.5077 -0.0252 -0.0226 0.0451  434  MET A N   
3204  C CA  . MET A 436  ? 0.2850 0.2381 0.4728 -0.0261 -0.0191 0.0516  434  MET A CA  
3205  C C   . MET A 436  ? 0.3081 0.2646 0.4950 -0.0265 -0.0187 0.0494  434  MET A C   
3206  O O   . MET A 436  ? 0.3623 0.3217 0.5531 -0.0282 -0.0175 0.0544  434  MET A O   
3207  C CB  . MET A 436  ? 0.2952 0.2501 0.4707 -0.0244 -0.0153 0.0535  434  MET A CB  
3208  C CG  . MET A 436  ? 0.3096 0.2693 0.4812 -0.0250 -0.0116 0.0598  434  MET A CG  
3209  S SD  . MET A 436  ? 0.3342 0.2959 0.4910 -0.0227 -0.0075 0.0603  434  MET A SD  
3210  C CE  . MET A 436  ? 0.3465 0.3054 0.5056 -0.0226 -0.0079 0.0645  434  MET A CE  
3211  N N   . ALA A 437  ? 0.2756 0.2322 0.4576 -0.0251 -0.0197 0.0421  435  ALA A N   
3212  C CA  . ALA A 437  ? 0.2850 0.2449 0.4651 -0.0253 -0.0193 0.0398  435  ALA A CA  
3213  C C   . ALA A 437  ? 0.3619 0.3216 0.5543 -0.0272 -0.0225 0.0390  435  ALA A C   
3214  O O   . ALA A 437  ? 0.3433 0.3063 0.5364 -0.0280 -0.0219 0.0397  435  ALA A O   
3215  C CB  . ALA A 437  ? 0.2956 0.2560 0.4671 -0.0232 -0.0195 0.0324  435  ALA A CB  
3216  N N   . GLY A 438  ? 0.3815 0.3372 0.5836 -0.0279 -0.0261 0.0375  436  GLY A N   
3217  C CA  . GLY A 438  ? 0.4095 0.3644 0.6245 -0.0299 -0.0295 0.0372  436  GLY A CA  
3218  C C   . GLY A 438  ? 0.3807 0.3360 0.5970 -0.0291 -0.0324 0.0288  436  GLY A C   
3219  O O   . GLY A 438  ? 0.3673 0.3238 0.5745 -0.0271 -0.0320 0.0231  436  GLY A O   
3220  N N   . LYS A 439  ? 0.4812 0.4362 0.7094 -0.0310 -0.0356 0.0282  437  LYS A N   
3221  C CA  . LYS A 439  ? 0.4987 0.4537 0.7309 -0.0304 -0.0394 0.0198  437  LYS A CA  
3222  C C   . LYS A 439  ? 0.4632 0.4231 0.6890 -0.0299 -0.0382 0.0172  437  LYS A C   
3223  O O   . LYS A 439  ? 0.5982 0.5592 0.8218 -0.0285 -0.0402 0.0096  437  LYS A O   
3224  C CB  . LYS A 439  ? 0.5871 0.5394 0.8354 -0.0325 -0.0437 0.0199  437  LYS A CB  
3225  N N   . ASP A 440  ? 0.4578 0.4209 0.6807 -0.0309 -0.0349 0.0232  438  ASP A N   
3226  C CA  . ASP A 440  ? 0.4770 0.4447 0.6942 -0.0304 -0.0337 0.0211  438  ASP A CA  
3227  C C   . ASP A 440  ? 0.4731 0.4424 0.6760 -0.0279 -0.0312 0.0183  438  ASP A C   
3228  O O   . ASP A 440  ? 0.4977 0.4668 0.6931 -0.0273 -0.0277 0.0226  438  ASP A O   
3229  C CB  . ASP A 440  ? 0.5555 0.5264 0.7742 -0.0322 -0.0310 0.0284  438  ASP A CB  
3230  C CG  . ASP A 440  ? 0.6235 0.5940 0.8566 -0.0348 -0.0338 0.0307  438  ASP A CG  
3231  O OD1 . ASP A 440  ? 0.6200 0.5875 0.8620 -0.0353 -0.0381 0.0261  438  ASP A OD1 
3232  O OD2 . ASP A 440  ? 0.6551 0.6284 0.8908 -0.0364 -0.0318 0.0369  438  ASP A OD2 
3233  N N   . PHE A 441  ? 0.4058 0.3767 0.6051 -0.0265 -0.0329 0.0112  439  PHE A N   
3234  C CA  . PHE A 441  ? 0.3953 0.3681 0.5816 -0.0243 -0.0307 0.0086  439  PHE A CA  
3235  C C   . PHE A 441  ? 0.4216 0.3988 0.6046 -0.0236 -0.0315 0.0041  439  PHE A C   
3236  O O   . PHE A 441  ? 0.3580 0.3361 0.5483 -0.0241 -0.0349 0.0000  439  PHE A O   
3237  C CB  . PHE A 441  ? 0.3322 0.3024 0.5154 -0.0226 -0.0319 0.0040  439  PHE A CB  
3238  C CG  . PHE A 441  ? 0.3510 0.3232 0.5210 -0.0205 -0.0293 0.0023  439  PHE A CG  
3239  C CD1 . PHE A 441  ? 0.3361 0.3076 0.4985 -0.0201 -0.0256 0.0075  439  PHE A CD1 
3240  C CD2 . PHE A 441  ? 0.3485 0.3236 0.5139 -0.0191 -0.0307 -0.0042 439  PHE A CD2 
3241  C CE1 . PHE A 441  ? 0.2522 0.2254 0.4032 -0.0184 -0.0234 0.0061  439  PHE A CE1 
3242  C CE2 . PHE A 441  ? 0.3227 0.2999 0.4765 -0.0174 -0.0284 -0.0051 439  PHE A CE2 
3243  C CZ  . PHE A 441  ? 0.2777 0.2536 0.4246 -0.0171 -0.0248 0.0000  439  PHE A CZ  
3244  N N   . HIS A 442  ? 0.3576 0.3375 0.5296 -0.0223 -0.0285 0.0050  440  HIS A N   
3245  C CA  . HIS A 442  ? 0.3533 0.3375 0.5200 -0.0212 -0.0290 0.0006  440  HIS A CA  
3246  C C   . HIS A 442  ? 0.3796 0.3646 0.5339 -0.0193 -0.0264 0.0003  440  HIS A C   
3247  O O   . HIS A 442  ? 0.3089 0.2922 0.4585 -0.0191 -0.0233 0.0050  440  HIS A O   
3248  C CB  . HIS A 442  ? 0.3453 0.3328 0.5138 -0.0222 -0.0282 0.0036  440  HIS A CB  
3249  C CG  . HIS A 442  ? 0.3273 0.3153 0.4902 -0.0223 -0.0240 0.0102  440  HIS A CG  
3250  N ND1 . HIS A 442  ? 0.3363 0.3228 0.5044 -0.0239 -0.0225 0.0163  440  HIS A ND1 
3251  C CD2 . HIS A 442  ? 0.3422 0.3325 0.4953 -0.0210 -0.0212 0.0116  440  HIS A CD2 
3252  C CE1 . HIS A 442  ? 0.3297 0.3179 0.4910 -0.0233 -0.0188 0.0207  440  HIS A CE1 
3253  N NE2 . HIS A 442  ? 0.3608 0.3509 0.5131 -0.0216 -0.0180 0.0179  440  HIS A NE2 
3254  N N   . VAL A 443  ? 0.3541 0.3422 0.5034 -0.0179 -0.0276 -0.0051 441  VAL A N   
3255  C CA  . VAL A 443  ? 0.3662 0.3556 0.5040 -0.0162 -0.0252 -0.0051 441  VAL A CA  
3256  C C   . VAL A 443  ? 0.3361 0.3268 0.4690 -0.0164 -0.0219 0.0004  441  VAL A C   
3257  O O   . VAL A 443  ? 0.3238 0.3172 0.4593 -0.0171 -0.0221 0.0014  441  VAL A O   
3258  C CB  . VAL A 443  ? 0.3923 0.3858 0.5261 -0.0148 -0.0272 -0.0114 441  VAL A CB  
3259  C CG1 . VAL A 443  ? 0.3496 0.3453 0.4721 -0.0135 -0.0245 -0.0101 441  VAL A CG1 
3260  C CG2 . VAL A 443  ? 0.4390 0.4312 0.5755 -0.0141 -0.0298 -0.0169 441  VAL A CG2 
3261  N N   . GLY A 444  ? 0.2725 0.2615 0.3986 -0.0158 -0.0189 0.0038  442  GLY A N   
3262  C CA  . GLY A 444  ? 0.2441 0.2339 0.3662 -0.0158 -0.0156 0.0091  442  GLY A CA  
3263  C C   . GLY A 444  ? 0.2505 0.2376 0.3762 -0.0169 -0.0138 0.0145  442  GLY A C   
3264  O O   . GLY A 444  ? 0.2659 0.2535 0.3871 -0.0165 -0.0108 0.0187  442  GLY A O   
3265  N N   . LYS A 445  ? 0.2508 0.2354 0.3846 -0.0180 -0.0156 0.0145  443  LYS A N   
3266  C CA  . LYS A 445  ? 0.2416 0.2242 0.3790 -0.0191 -0.0138 0.0202  443  LYS A CA  
3267  C C   . LYS A 445  ? 0.2320 0.2122 0.3627 -0.0180 -0.0117 0.0219  443  LYS A C   
3268  O O   . LYS A 445  ? 0.2526 0.2334 0.3794 -0.0178 -0.0087 0.0265  443  LYS A O   
3269  C CB  . LYS A 445  ? 0.2862 0.2665 0.4348 -0.0207 -0.0166 0.0202  443  LYS A CB  
3270  C CG  . LYS A 445  ? 0.3051 0.2843 0.4582 -0.0220 -0.0148 0.0269  443  LYS A CG  
3271  C CD  . LYS A 445  ? 0.3616 0.3389 0.5269 -0.0240 -0.0176 0.0275  443  LYS A CD  
3272  C CE  . LYS A 445  ? 0.4556 0.4328 0.6252 -0.0254 -0.0157 0.0350  443  LYS A CE  
3273  N NZ  . LYS A 445  ? 0.5381 0.5136 0.7208 -0.0276 -0.0186 0.0364  443  LYS A NZ  
3274  N N   . TYR A 446  ? 0.2318 0.2098 0.3613 -0.0172 -0.0132 0.0180  444  TYR A N   
3275  C CA  . TYR A 446  ? 0.2380 0.2140 0.3605 -0.0160 -0.0115 0.0185  444  TYR A CA  
3276  C C   . TYR A 446  ? 0.2320 0.2074 0.3524 -0.0149 -0.0137 0.0123  444  TYR A C   
3277  O O   . TYR A 446  ? 0.2288 0.2052 0.3538 -0.0151 -0.0166 0.0079  444  TYR A O   
3278  C CB  . TYR A 446  ? 0.2070 0.1800 0.3335 -0.0168 -0.0108 0.0228  444  TYR A CB  
3279  C CG  . TYR A 446  ? 0.2717 0.2417 0.4071 -0.0176 -0.0140 0.0207  444  TYR A CG  
3280  C CD1 . TYR A 446  ? 0.2846 0.2521 0.4186 -0.0166 -0.0153 0.0173  444  TYR A CD1 
3281  C CD2 . TYR A 446  ? 0.3406 0.3103 0.4864 -0.0194 -0.0159 0.0222  444  TYR A CD2 
3282  C CE1 . TYR A 446  ? 0.3841 0.3488 0.5268 -0.0171 -0.0184 0.0151  444  TYR A CE1 
3283  C CE2 . TYR A 446  ? 0.3209 0.2876 0.4756 -0.0201 -0.0191 0.0203  444  TYR A CE2 
3284  C CZ  . TYR A 446  ? 0.3498 0.3140 0.5030 -0.0189 -0.0204 0.0165  444  TYR A CZ  
3285  O OH  . TYR A 446  ? 0.5460 0.5070 0.7086 -0.0195 -0.0238 0.0143  444  TYR A OH  
3286  N N   . GLU A 447  ? 0.2134 0.1875 0.3270 -0.0137 -0.0125 0.0118  445  GLU A N   
3287  C CA  . GLU A 447  ? 0.2395 0.2134 0.3516 -0.0126 -0.0144 0.0062  445  GLU A CA  
3288  C C   . GLU A 447  ? 0.2328 0.2036 0.3421 -0.0119 -0.0134 0.0073  445  GLU A C   
3289  O O   . GLU A 447  ? 0.2393 0.2088 0.3462 -0.0121 -0.0109 0.0122  445  GLU A O   
3290  C CB  . GLU A 447  ? 0.2011 0.1785 0.3055 -0.0114 -0.0141 0.0029  445  GLU A CB  
3291  C CG  . GLU A 447  ? 0.2233 0.2012 0.3186 -0.0106 -0.0109 0.0060  445  GLU A CG  
3292  C CD  . GLU A 447  ? 0.2416 0.2231 0.3300 -0.0097 -0.0106 0.0037  445  GLU A CD  
3293  O OE1 . GLU A 447  ? 0.2538 0.2382 0.3441 -0.0098 -0.0126 0.0004  445  GLU A OE1 
3294  O OE2 . GLU A 447  ? 0.2305 0.2120 0.3115 -0.0089 -0.0085 0.0054  445  GLU A OE2 
3295  N N   . PHE A 448  ? 0.2364 0.2065 0.3461 -0.0111 -0.0154 0.0026  446  PHE A N   
3296  C CA  . PHE A 448  ? 0.2342 0.2023 0.3397 -0.0101 -0.0144 0.0027  446  PHE A CA  
3297  C C   . PHE A 448  ? 0.1997 0.1705 0.2956 -0.0087 -0.0132 0.0003  446  PHE A C   
3298  O O   . PHE A 448  ? 0.2389 0.2132 0.3323 -0.0085 -0.0135 -0.0020 446  PHE A O   
3299  C CB  . PHE A 448  ? 0.2436 0.2093 0.3557 -0.0098 -0.0173 -0.0010 446  PHE A CB  
3300  C CG  . PHE A 448  ? 0.2377 0.2002 0.3596 -0.0112 -0.0186 0.0020  446  PHE A CG  
3301  C CD1 . PHE A 448  ? 0.2614 0.2211 0.3838 -0.0117 -0.0169 0.0074  446  PHE A CD1 
3302  C CD2 . PHE A 448  ? 0.2504 0.2129 0.3811 -0.0121 -0.0215 -0.0004 446  PHE A CD2 
3303  C CE1 . PHE A 448  ? 0.3019 0.2590 0.4336 -0.0131 -0.0181 0.0108  446  PHE A CE1 
3304  C CE2 . PHE A 448  ? 0.2888 0.2484 0.4293 -0.0136 -0.0229 0.0027  446  PHE A CE2 
3305  C CZ  . PHE A 448  ? 0.2896 0.2465 0.4306 -0.0141 -0.0211 0.0086  446  PHE A CZ  
3306  N N   . GLN A 449  ? 0.2207 0.1901 0.3114 -0.0079 -0.0117 0.0011  447  GLN A N   
3307  C CA  . GLN A 449  ? 0.2175 0.1894 0.2998 -0.0067 -0.0107 -0.0011 447  GLN A CA  
3308  C C   . GLN A 449  ? 0.2627 0.2330 0.3435 -0.0057 -0.0110 -0.0030 447  GLN A C   
3309  O O   . GLN A 449  ? 0.2434 0.2102 0.3277 -0.0059 -0.0110 -0.0010 447  GLN A O   
3310  C CB  . GLN A 449  ? 0.2191 0.1917 0.2942 -0.0066 -0.0076 0.0031  447  GLN A CB  
3311  C CG  . GLN A 449  ? 0.2161 0.1906 0.2920 -0.0074 -0.0072 0.0049  447  GLN A CG  
3312  C CD  . GLN A 449  ? 0.2260 0.2020 0.2946 -0.0070 -0.0047 0.0075  447  GLN A CD  
3313  O OE1 . GLN A 449  ? 0.2715 0.2465 0.3347 -0.0063 -0.0031 0.0086  447  GLN A OE1 
3314  N NE2 . GLN A 449  ? 0.2288 0.2072 0.2974 -0.0073 -0.0045 0.0083  447  GLN A NE2 
3315  N N   . CYS A 450  ? 0.2337 0.2069 0.3093 -0.0047 -0.0112 -0.0068 448  CYS A N   
3316  C CA  . CYS A 450  ? 0.2403 0.2127 0.3141 -0.0036 -0.0115 -0.0090 448  CYS A CA  
3317  C C   . CYS A 450  ? 0.2615 0.2375 0.3269 -0.0028 -0.0102 -0.0102 448  CYS A C   
3318  O O   . CYS A 450  ? 0.2536 0.2328 0.3155 -0.0030 -0.0096 -0.0099 448  CYS A O   
3319  C CB  . CYS A 450  ? 0.2554 0.2281 0.3358 -0.0031 -0.0147 -0.0144 448  CYS A CB  
3320  S SG  . CYS A 450  ? 0.2838 0.2627 0.3631 -0.0023 -0.0167 -0.0209 448  CYS A SG  
3321  N N   . LEU A 451  ? 0.2346 0.2102 0.2971 -0.0019 -0.0098 -0.0113 449  LEU A N   
3322  C CA  . LEU A 451  ? 0.2459 0.2249 0.3010 -0.0012 -0.0087 -0.0124 449  LEU A CA  
3323  C C   . LEU A 451  ? 0.2429 0.2266 0.2986 -0.0003 -0.0107 -0.0182 449  LEU A C   
3324  O O   . LEU A 451  ? 0.2721 0.2552 0.3330 0.0003  -0.0128 -0.0220 449  LEU A O   
3325  C CB  . LEU A 451  ? 0.2608 0.2374 0.3125 -0.0008 -0.0071 -0.0105 449  LEU A CB  
3326  C CG  . LEU A 451  ? 0.3575 0.3373 0.4020 -0.0002 -0.0060 -0.0112 449  LEU A CG  
3327  C CD1 . LEU A 451  ? 0.3208 0.3024 0.3600 -0.0008 -0.0042 -0.0081 449  LEU A CD1 
3328  C CD2 . LEU A 451  ? 0.3553 0.3322 0.3982 0.0003  -0.0050 -0.0098 449  LEU A CD2 
3329  N N   . HIS A 452  ? 0.2421 0.2307 0.2926 -0.0002 -0.0102 -0.0190 450  HIS A N   
3330  C CA  . HIS A 452  ? 0.2618 0.2562 0.3114 0.0008  -0.0118 -0.0243 450  HIS A CA  
3331  C C   . HIS A 452  ? 0.2559 0.2502 0.3053 0.0019  -0.0121 -0.0270 450  HIS A C   
3332  O O   . HIS A 452  ? 0.3035 0.2954 0.3495 0.0019  -0.0104 -0.0242 450  HIS A O   
3333  C CB  . HIS A 452  ? 0.2579 0.2575 0.3006 0.0007  -0.0106 -0.0231 450  HIS A CB  
3334  C CG  . HIS A 452  ? 0.2477 0.2541 0.2883 0.0017  -0.0117 -0.0278 450  HIS A CG  
3335  N ND1 . HIS A 452  ? 0.2882 0.2998 0.3311 0.0021  -0.0138 -0.0320 450  HIS A ND1 
3336  C CD2 . HIS A 452  ? 0.2865 0.2960 0.3230 0.0025  -0.0111 -0.0291 450  HIS A CD2 
3337  C CE1 . HIS A 452  ? 0.3081 0.3260 0.3481 0.0032  -0.0143 -0.0357 450  HIS A CE1 
3338  N NE2 . HIS A 452  ? 0.3058 0.3226 0.3420 0.0034  -0.0126 -0.0339 450  HIS A NE2 
3339  N N   . GLY A 453  ? 0.3469 0.3443 0.4000 0.0029  -0.0145 -0.0328 451  GLY A N   
3340  C CA  . GLY A 453  ? 0.3701 0.3686 0.4231 0.0042  -0.0150 -0.0362 451  GLY A CA  
3341  C C   . GLY A 453  ? 0.4694 0.4613 0.5261 0.0043  -0.0150 -0.0345 451  GLY A C   
3342  O O   . GLY A 453  ? 0.4927 0.4847 0.5480 0.0052  -0.0147 -0.0356 451  GLY A O   
3343  N N   . MET A 454  ? 0.3465 0.3331 0.4082 0.0033  -0.0153 -0.0316 452  MET A N   
3344  C CA  . MET A 454  ? 0.3158 0.2962 0.3815 0.0032  -0.0153 -0.0292 452  MET A CA  
3345  C C   . MET A 454  ? 0.3799 0.3568 0.4543 0.0025  -0.0173 -0.0292 452  MET A C   
3346  O O   . MET A 454  ? 0.3434 0.3175 0.4246 0.0030  -0.0193 -0.0314 452  MET A O   
3347  C CB  . MET A 454  ? 0.3699 0.3473 0.4304 0.0023  -0.0123 -0.0229 452  MET A CB  
3348  C CG  . MET A 454  ? 0.3661 0.3376 0.4306 0.0020  -0.0121 -0.0194 452  MET A CG  
3349  S SD  . MET A 454  ? 0.5074 0.4777 0.5748 0.0035  -0.0136 -0.0229 452  MET A SD  
3350  C CE  . MET A 454  ? 0.4794 0.4532 0.5369 0.0041  -0.0112 -0.0226 452  MET A CE  
3351  N N   . GLY A 455  ? 0.3215 0.2986 0.3964 0.0013  -0.0169 -0.0269 453  GLY A N   
3352  C CA  . GLY A 455  ? 0.2986 0.2724 0.3818 0.0004  -0.0187 -0.0263 453  GLY A CA  
3353  C C   . GLY A 455  ? 0.3561 0.3327 0.4451 0.0008  -0.0218 -0.0320 453  GLY A C   
3354  O O   . GLY A 455  ? 0.3225 0.2961 0.4197 0.0000  -0.0236 -0.0318 453  GLY A O   
3355  N N   . GLU A 456  ? 0.3344 0.3169 0.4198 0.0019  -0.0224 -0.0369 454  GLU A N   
3356  C CA  . GLU A 456  ? 0.3369 0.3227 0.4277 0.0023  -0.0255 -0.0426 454  GLU A CA  
3357  C C   . GLU A 456  ? 0.3652 0.3483 0.4655 0.0031  -0.0287 -0.0471 454  GLU A C   
3358  O O   . GLU A 456  ? 0.3587 0.3414 0.4664 0.0027  -0.0313 -0.0495 454  GLU A O   
3359  C CB  . GLU A 456  ? 0.3993 0.3930 0.4841 0.0035  -0.0256 -0.0471 454  GLU A CB  
3360  C CG  . GLU A 456  ? 0.4959 0.4929 0.5732 0.0027  -0.0232 -0.0434 454  GLU A CG  
3361  C CD  . GLU A 456  ? 0.4136 0.4113 0.4824 0.0029  -0.0203 -0.0402 454  GLU A CD  
3362  O OE1 . GLU A 456  ? 0.4307 0.4247 0.4999 0.0032  -0.0197 -0.0392 454  GLU A OE1 
3363  O OE2 . GLU A 456  ? 0.4265 0.4285 0.4888 0.0027  -0.0189 -0.0387 454  GLU A OE2 
3364  N N   . PRO A 457  ? 0.4161 0.3974 0.5171 0.0042  -0.0290 -0.0485 455  PRO A N   
3365  C CA  . PRO A 457  ? 0.4162 0.3943 0.5274 0.0049  -0.0324 -0.0525 455  PRO A CA  
3366  C C   . PRO A 457  ? 0.3671 0.3389 0.4864 0.0032  -0.0333 -0.0482 455  PRO A C   
3367  O O   . PRO A 457  ? 0.3833 0.3540 0.5119 0.0031  -0.0366 -0.0517 455  PRO A O   
3368  C CB  . PRO A 457  ? 0.3513 0.3279 0.4606 0.0062  -0.0318 -0.0528 455  PRO A CB  
3369  C CG  . PRO A 457  ? 0.4052 0.3872 0.5038 0.0068  -0.0291 -0.0527 455  PRO A CG  
3370  C CD  . PRO A 457  ? 0.3872 0.3698 0.4806 0.0051  -0.0267 -0.0474 455  PRO A CD  
3371  N N   . LEU A 458  ? 0.3746 0.3427 0.4910 0.0018  -0.0305 -0.0407 456  LEU A N   
3372  C CA  . LEU A 458  ? 0.2939 0.2569 0.4178 0.0000  -0.0311 -0.0360 456  LEU A CA  
3373  C C   . LEU A 458  ? 0.3034 0.2684 0.4298 -0.0012 -0.0319 -0.0363 456  LEU A C   
3374  O O   . LEU A 458  ? 0.3046 0.2674 0.4407 -0.0019 -0.0347 -0.0374 456  LEU A O   
3375  C CB  . LEU A 458  ? 0.3253 0.2851 0.4445 -0.0011 -0.0277 -0.0280 456  LEU A CB  
3376  C CG  . LEU A 458  ? 0.2999 0.2557 0.4256 -0.0030 -0.0277 -0.0221 456  LEU A CG  
3377  C CD1 . LEU A 458  ? 0.2970 0.2487 0.4347 -0.0032 -0.0312 -0.0236 456  LEU A CD1 
3378  C CD2 . LEU A 458  ? 0.3427 0.2964 0.4628 -0.0037 -0.0242 -0.0148 456  LEU A CD2 
3379  N N   . TYR A 459  ? 0.3048 0.2740 0.4230 -0.0014 -0.0297 -0.0352 457  TYR A N   
3380  C CA  . TYR A 459  ? 0.3189 0.2896 0.4394 -0.0026 -0.0301 -0.0344 457  TYR A CA  
3381  C C   . TYR A 459  ? 0.3196 0.2944 0.4443 -0.0018 -0.0334 -0.0417 457  TYR A C   
3382  O O   . TYR A 459  ? 0.3276 0.3030 0.4567 -0.0029 -0.0346 -0.0416 457  TYR A O   
3383  C CB  . TYR A 459  ? 0.2921 0.2652 0.4032 -0.0032 -0.0266 -0.0299 457  TYR A CB  
3384  C CG  . TYR A 459  ? 0.2814 0.2501 0.3918 -0.0045 -0.0241 -0.0224 457  TYR A CG  
3385  C CD1 . TYR A 459  ? 0.3144 0.2806 0.4311 -0.0061 -0.0243 -0.0185 457  TYR A CD1 
3386  C CD2 . TYR A 459  ? 0.2714 0.2386 0.3754 -0.0040 -0.0216 -0.0193 457  TYR A CD2 
3387  C CE1 . TYR A 459  ? 0.2626 0.2256 0.3788 -0.0071 -0.0220 -0.0117 457  TYR A CE1 
3388  C CE2 . TYR A 459  ? 0.2359 0.1997 0.3394 -0.0050 -0.0194 -0.0127 457  TYR A CE2 
3389  C CZ  . TYR A 459  ? 0.2552 0.2171 0.3647 -0.0065 -0.0196 -0.0089 457  TYR A CZ  
3390  O OH  . TYR A 459  ? 0.2909 0.2503 0.4000 -0.0074 -0.0173 -0.0024 457  TYR A OH  
3391  N N   . GLU A 460  ? 0.3315 0.3094 0.4553 0.0001  -0.0350 -0.0481 458  GLU A N   
3392  C CA  . GLU A 460  ? 0.3359 0.3172 0.4658 0.0010  -0.0387 -0.0555 458  GLU A CA  
3393  C C   . GLU A 460  ? 0.3868 0.3629 0.5294 0.0004  -0.0421 -0.0569 458  GLU A C   
3394  O O   . GLU A 460  ? 0.4069 0.3850 0.5562 0.0008  -0.0454 -0.0625 458  GLU A O   
3395  C CB  . GLU A 460  ? 0.4247 0.4114 0.5503 0.0033  -0.0395 -0.0623 458  GLU A CB  
3396  C CG  . GLU A 460  ? 0.5096 0.5034 0.6246 0.0037  -0.0373 -0.0623 458  GLU A CG  
3397  C CD  . GLU A 460  ? 0.6778 0.6777 0.7880 0.0059  -0.0376 -0.0681 458  GLU A CD  
3398  O OE1 . GLU A 460  ? 0.6730 0.6707 0.7851 0.0070  -0.0381 -0.0699 458  GLU A OE1 
3399  O OE2 . GLU A 460  ? 0.6452 0.6525 0.7499 0.0065  -0.0374 -0.0706 458  GLU A OE2 
3400  N N   . GLU A 461  ? 0.3500 0.3198 0.4964 -0.0005 -0.0414 -0.0518 459  GLU A N   
3401  C CA  . GLU A 461  ? 0.3895 0.3538 0.5483 -0.0016 -0.0443 -0.0511 459  GLU A CA  
3402  C C   . GLU A 461  ? 0.3784 0.3405 0.5401 -0.0040 -0.0432 -0.0444 459  GLU A C   
3403  O O   . GLU A 461  ? 0.3649 0.3225 0.5370 -0.0054 -0.0452 -0.0424 459  GLU A O   
3404  C CB  . GLU A 461  ? 0.3380 0.2970 0.5002 -0.0012 -0.0444 -0.0488 459  GLU A CB  
3405  C CG  . GLU A 461  ? 0.3888 0.3500 0.5486 0.0013  -0.0454 -0.0550 459  GLU A CG  
3406  C CD  . GLU A 461  ? 0.4523 0.4161 0.6195 0.0028  -0.0498 -0.0643 459  GLU A CD  
3407  O OE1 . GLU A 461  ? 0.4573 0.4190 0.6345 0.0018  -0.0528 -0.0656 459  GLU A OE1 
3408  O OE2 . GLU A 461  ? 0.4991 0.4674 0.6621 0.0050  -0.0503 -0.0705 459  GLU A OE2 
3409  N N   . VAL A 462  ? 0.3646 0.3299 0.5176 -0.0047 -0.0401 -0.0411 460  VAL A N   
3410  C CA  . VAL A 462  ? 0.3279 0.2917 0.4820 -0.0069 -0.0384 -0.0344 460  VAL A CA  
3411  C C   . VAL A 462  ? 0.3660 0.3346 0.5191 -0.0072 -0.0389 -0.0367 460  VAL A C   
3412  O O   . VAL A 462  ? 0.3586 0.3262 0.5193 -0.0087 -0.0406 -0.0357 460  VAL A O   
3413  C CB  . VAL A 462  ? 0.3529 0.3157 0.4981 -0.0073 -0.0340 -0.0272 460  VAL A CB  
3414  C CG1 . VAL A 462  ? 0.3093 0.2718 0.4551 -0.0093 -0.0321 -0.0209 460  VAL A CG1 
3415  C CG2 . VAL A 462  ? 0.3307 0.2888 0.4778 -0.0071 -0.0335 -0.0243 460  VAL A CG2 
3416  N N   . VAL A 463  ? 0.3211 0.2951 0.4648 -0.0059 -0.0377 -0.0396 461  VAL A N   
3417  C CA  . VAL A 463  ? 0.3390 0.3180 0.4804 -0.0062 -0.0379 -0.0413 461  VAL A CA  
3418  C C   . VAL A 463  ? 0.4159 0.3971 0.5655 -0.0056 -0.0423 -0.0487 461  VAL A C   
3419  O O   . VAL A 463  ? 0.4192 0.4005 0.5722 -0.0042 -0.0448 -0.0546 461  VAL A O   
3420  C CB  . VAL A 463  ? 0.3583 0.3425 0.4875 -0.0049 -0.0355 -0.0420 461  VAL A CB  
3421  C CG1 . VAL A 463  ? 0.3604 0.3502 0.4873 -0.0051 -0.0358 -0.0436 461  VAL A CG1 
3422  C CG2 . VAL A 463  ? 0.3188 0.3005 0.4407 -0.0055 -0.0314 -0.0350 461  VAL A CG2 
3423  N N   . GLY A 464  ? 0.4059 0.3889 0.5591 -0.0067 -0.0434 -0.0488 462  GLY A N   
3424  C CA  . GLY A 464  ? 0.4595 0.4459 0.6195 -0.0061 -0.0475 -0.0562 462  GLY A CA  
3425  C C   . GLY A 464  ? 0.4811 0.4627 0.6545 -0.0076 -0.0506 -0.0562 462  GLY A C   
3426  O O   . GLY A 464  ? 0.3854 0.3610 0.5643 -0.0085 -0.0504 -0.0520 462  GLY A O   
3427  N N   . ARG A 465  ? 0.4454 0.4302 0.6249 -0.0077 -0.0537 -0.0608 463  ARG A N   
3428  C CA  . ARG A 465  ? 0.4557 0.4363 0.6488 -0.0093 -0.0571 -0.0611 463  ARG A CA  
3429  C C   . ARG A 465  ? 0.5020 0.4784 0.7038 -0.0085 -0.0602 -0.0650 463  ARG A C   
3430  O O   . ARG A 465  ? 0.5724 0.5431 0.7850 -0.0101 -0.0619 -0.0623 463  ARG A O   
3431  C CB  . ARG A 465  ? 0.4297 0.4152 0.6270 -0.0093 -0.0601 -0.0663 463  ARG A CB  
3432  N N   . GLY A 466  ? 0.4301 0.4091 0.6277 -0.0060 -0.0609 -0.0712 464  GLY A N   
3433  C CA  . GLY A 466  ? 0.4373 0.4124 0.6429 -0.0050 -0.0639 -0.0753 464  GLY A CA  
3434  C C   . GLY A 466  ? 0.4790 0.4480 0.6836 -0.0055 -0.0615 -0.0689 464  GLY A C   
3435  O O   . GLY A 466  ? 0.4834 0.4485 0.6952 -0.0047 -0.0640 -0.0715 464  GLY A O   
3436  N N   . LYS A 467  ? 0.4540 0.4223 0.6500 -0.0067 -0.0570 -0.0608 465  LYS A N   
3437  C CA  . LYS A 467  ? 0.3787 0.3419 0.5728 -0.0071 -0.0545 -0.0544 465  LYS A CA  
3438  C C   . LYS A 467  ? 0.3964 0.3559 0.5940 -0.0098 -0.0527 -0.0456 465  LYS A C   
3439  O O   . LYS A 467  ? 0.4180 0.3752 0.6269 -0.0113 -0.0555 -0.0453 465  LYS A O   
3440  C CB  . LYS A 467  ? 0.3716 0.3379 0.5519 -0.0056 -0.0507 -0.0537 465  LYS A CB  
3441  C CG  . LYS A 467  ? 0.4403 0.4109 0.6174 -0.0029 -0.0524 -0.0623 465  LYS A CG  
3442  C CD  . LYS A 467  ? 0.4249 0.3914 0.6097 -0.0018 -0.0551 -0.0655 465  LYS A CD  
3443  C CE  . LYS A 467  ? 0.5081 0.4797 0.6901 0.0010  -0.0569 -0.0745 465  LYS A CE  
3444  N NZ  . LYS A 467  ? 0.4618 0.4295 0.6499 0.0024  -0.0590 -0.0773 465  LYS A NZ  
3445  N N   . LEU A 468  ? 0.3989 0.3581 0.5876 -0.0105 -0.0483 -0.0384 466  LEU A N   
3446  C CA  . LEU A 468  ? 0.3485 0.3052 0.5396 -0.0129 -0.0462 -0.0299 466  LEU A CA  
3447  C C   . LEU A 468  ? 0.3671 0.3282 0.5537 -0.0138 -0.0445 -0.0283 466  LEU A C   
3448  O O   . LEU A 468  ? 0.3863 0.3462 0.5753 -0.0157 -0.0430 -0.0218 466  LEU A O   
3449  C CB  . LEU A 468  ? 0.3862 0.3404 0.5708 -0.0130 -0.0425 -0.0231 466  LEU A CB  
3450  C CG  . LEU A 468  ? 0.3626 0.3127 0.5501 -0.0121 -0.0436 -0.0237 466  LEU A CG  
3451  C CD1 . LEU A 468  ? 0.4047 0.3527 0.5861 -0.0125 -0.0398 -0.0162 466  LEU A CD1 
3452  C CD2 . LEU A 468  ? 0.3820 0.3279 0.5844 -0.0131 -0.0478 -0.0246 466  LEU A CD2 
3453  N N   . ASP A 469  ? 0.3823 0.3485 0.5625 -0.0123 -0.0449 -0.0340 467  ASP A N   
3454  C CA  . ASP A 469  ? 0.3351 0.3058 0.5113 -0.0129 -0.0437 -0.0333 467  ASP A CA  
3455  C C   . ASP A 469  ? 0.3104 0.2809 0.4791 -0.0138 -0.0392 -0.0253 467  ASP A C   
3456  O O   . ASP A 469  ? 0.2984 0.2696 0.4690 -0.0154 -0.0383 -0.0212 467  ASP A O   
3457  C CB  . ASP A 469  ? 0.3482 0.3189 0.5357 -0.0144 -0.0470 -0.0347 467  ASP A CB  
3458  C CG  . ASP A 469  ? 0.4534 0.4299 0.6371 -0.0142 -0.0471 -0.0374 467  ASP A CG  
3459  O OD1 . ASP A 469  ? 0.4226 0.4035 0.5964 -0.0126 -0.0459 -0.0403 467  ASP A OD1 
3460  O OD2 . ASP A 469  ? 0.5817 0.5585 0.7724 -0.0158 -0.0485 -0.0362 467  ASP A OD2 
3461  N N   . ARG A 470  ? 0.3073 0.2771 0.4674 -0.0128 -0.0364 -0.0233 468  ARG A N   
3462  C CA  . ARG A 470  ? 0.3193 0.2895 0.4708 -0.0132 -0.0322 -0.0169 468  ARG A CA  
3463  C C   . ARG A 470  ? 0.3027 0.2766 0.4426 -0.0114 -0.0304 -0.0194 468  ARG A C   
3464  O O   . ARG A 470  ? 0.3140 0.2883 0.4518 -0.0099 -0.0314 -0.0240 468  ARG A O   
3465  C CB  . ARG A 470  ? 0.2722 0.2379 0.4246 -0.0138 -0.0303 -0.0108 468  ARG A CB  
3466  C CG  . ARG A 470  ? 0.2757 0.2380 0.4395 -0.0158 -0.0317 -0.0071 468  ARG A CG  
3467  C CD  . ARG A 470  ? 0.3079 0.2723 0.4738 -0.0174 -0.0307 -0.0031 468  ARG A CD  
3468  N NE  . ARG A 470  ? 0.3118 0.2734 0.4895 -0.0195 -0.0324 0.0003  468  ARG A NE  
3469  C CZ  . ARG A 470  ? 0.3146 0.2762 0.5023 -0.0204 -0.0360 -0.0029 468  ARG A CZ  
3470  N NH1 . ARG A 470  ? 0.3268 0.2912 0.5141 -0.0194 -0.0383 -0.0100 468  ARG A NH1 
3471  N NH2 . ARG A 470  ? 0.3573 0.3163 0.5559 -0.0224 -0.0373 0.0012  468  ARG A NH2 
3472  N N   . PRO A 471  ? 0.3002 0.2769 0.4329 -0.0115 -0.0278 -0.0166 469  PRO A N   
3473  C CA  . PRO A 471  ? 0.2378 0.2183 0.3601 -0.0101 -0.0263 -0.0185 469  PRO A CA  
3474  C C   . PRO A 471  ? 0.2609 0.2392 0.3763 -0.0094 -0.0235 -0.0154 469  PRO A C   
3475  O O   . PRO A 471  ? 0.2575 0.2321 0.3742 -0.0102 -0.0218 -0.0103 469  PRO A O   
3476  C CB  . PRO A 471  ? 0.2516 0.2353 0.3703 -0.0106 -0.0247 -0.0158 469  PRO A CB  
3477  C CG  . PRO A 471  ? 0.2820 0.2625 0.4060 -0.0123 -0.0236 -0.0099 469  PRO A CG  
3478  C CD  . PRO A 471  ? 0.2900 0.2671 0.4246 -0.0131 -0.0264 -0.0116 469  PRO A CD  
3479  N N   . CYS A 472  ? 0.2593 0.2404 0.3672 -0.0080 -0.0229 -0.0184 470  CYS A N   
3480  C CA  . CYS A 472  ? 0.2551 0.2347 0.3558 -0.0072 -0.0204 -0.0161 470  CYS A CA  
3481  C C   . CYS A 472  ? 0.2501 0.2340 0.3414 -0.0065 -0.0187 -0.0162 470  CYS A C   
3482  O O   . CYS A 472  ? 0.2762 0.2647 0.3659 -0.0057 -0.0202 -0.0207 470  CYS A O   
3483  C CB  . CYS A 472  ? 0.2582 0.2363 0.3606 -0.0062 -0.0219 -0.0199 470  CYS A CB  
3484  S SG  . CYS A 472  ? 0.2798 0.2559 0.3741 -0.0054 -0.0189 -0.0168 470  CYS A SG  
3485  N N   . ARG A 473  ? 0.2261 0.2087 0.3115 -0.0066 -0.0156 -0.0112 471  ARG A N   
3486  C CA  . ARG A 473  ? 0.2209 0.2068 0.2976 -0.0060 -0.0139 -0.0107 471  ARG A CA  
3487  C C   . ARG A 473  ? 0.2507 0.2360 0.3222 -0.0050 -0.0128 -0.0113 471  ARG A C   
3488  O O   . ARG A 473  ? 0.2544 0.2358 0.3257 -0.0051 -0.0115 -0.0084 471  ARG A O   
3489  C CB  . ARG A 473  ? 0.2082 0.1935 0.2819 -0.0066 -0.0114 -0.0053 471  ARG A CB  
3490  C CG  . ARG A 473  ? 0.2227 0.2116 0.2887 -0.0060 -0.0102 -0.0049 471  ARG A CG  
3491  C CD  . ARG A 473  ? 0.2304 0.2187 0.2943 -0.0065 -0.0081 -0.0001 471  ARG A CD  
3492  N NE  . ARG A 473  ? 0.2405 0.2291 0.3105 -0.0074 -0.0091 0.0005  471  ARG A NE  
3493  C CZ  . ARG A 473  ? 0.2670 0.2593 0.3382 -0.0075 -0.0105 -0.0013 471  ARG A CZ  
3494  N NH1 . ARG A 473  ? 0.2477 0.2439 0.3139 -0.0068 -0.0109 -0.0032 471  ARG A NH1 
3495  N NH2 . ARG A 473  ? 0.2538 0.2460 0.3315 -0.0084 -0.0116 -0.0010 471  ARG A NH2 
3496  N N   . ILE A 474  ? 0.2444 0.2339 0.3114 -0.0041 -0.0134 -0.0148 472  ILE A N   
3497  C CA  . ILE A 474  ? 0.2313 0.2212 0.2935 -0.0031 -0.0126 -0.0159 472  ILE A CA  
3498  C C   . ILE A 474  ? 0.2454 0.2356 0.3000 -0.0032 -0.0099 -0.0118 472  ILE A C   
3499  O O   . ILE A 474  ? 0.2546 0.2486 0.3057 -0.0033 -0.0096 -0.0113 472  ILE A O   
3500  C CB  . ILE A 474  ? 0.2341 0.2292 0.2956 -0.0021 -0.0146 -0.0217 472  ILE A CB  
3501  C CG1 . ILE A 474  ? 0.2939 0.2884 0.3637 -0.0019 -0.0176 -0.0263 472  ILE A CG1 
3502  C CG2 . ILE A 474  ? 0.2596 0.2556 0.3160 -0.0012 -0.0136 -0.0226 472  ILE A CG2 
3503  C CD1 . ILE A 474  ? 0.3043 0.3048 0.3741 -0.0007 -0.0199 -0.0328 472  ILE A CD1 
3504  N N   . TYR A 475  ? 0.2384 0.2249 0.2909 -0.0032 -0.0081 -0.0088 473  TYR A N   
3505  C CA  . TYR A 475  ? 0.2600 0.2465 0.3056 -0.0031 -0.0058 -0.0056 473  TYR A CA  
3506  C C   . TYR A 475  ? 0.2731 0.2634 0.3142 -0.0023 -0.0061 -0.0084 473  TYR A C   
3507  O O   . TYR A 475  ? 0.2446 0.2343 0.2862 -0.0017 -0.0065 -0.0107 473  TYR A O   
3508  C CB  . TYR A 475  ? 0.2685 0.2502 0.3140 -0.0032 -0.0041 -0.0020 473  TYR A CB  
3509  C CG  . TYR A 475  ? 0.2858 0.2666 0.3255 -0.0031 -0.0017 0.0016  473  TYR A CG  
3510  C CD1 . TYR A 475  ? 0.2833 0.2639 0.3218 -0.0035 -0.0005 0.0048  473  TYR A CD1 
3511  C CD2 . TYR A 475  ? 0.4417 0.4217 0.4775 -0.0025 -0.0008 0.0016  473  TYR A CD2 
3512  C CE1 . TYR A 475  ? 0.2820 0.2616 0.3157 -0.0033 0.0015  0.0078  473  TYR A CE1 
3513  C CE2 . TYR A 475  ? 0.5073 0.4863 0.5383 -0.0025 0.0011  0.0046  473  TYR A CE2 
3514  C CZ  . TYR A 475  ? 0.4274 0.4061 0.4574 -0.0028 0.0022  0.0076  473  TYR A CZ  
3515  O OH  . TYR A 475  ? 0.5013 0.4790 0.5270 -0.0025 0.0038  0.0101  473  TYR A OH  
3516  N N   . ALA A 476  ? 0.2535 0.2482 0.2905 -0.0023 -0.0058 -0.0082 474  ALA A N   
3517  C CA  . ALA A 476  ? 0.2551 0.2550 0.2886 -0.0017 -0.0065 -0.0112 474  ALA A CA  
3518  C C   . ALA A 476  ? 0.2297 0.2304 0.2570 -0.0017 -0.0046 -0.0081 474  ALA A C   
3519  O O   . ALA A 476  ? 0.2520 0.2541 0.2767 -0.0022 -0.0040 -0.0054 474  ALA A O   
3520  C CB  . ALA A 476  ? 0.2743 0.2798 0.3086 -0.0016 -0.0082 -0.0137 474  ALA A CB  
3521  N N   . PRO A 477  ? 0.2409 0.2403 0.2659 -0.0013 -0.0038 -0.0083 475  PRO A N   
3522  C CA  . PRO A 477  ? 0.2422 0.2425 0.2617 -0.0015 -0.0023 -0.0055 475  PRO A CA  
3523  C C   . PRO A 477  ? 0.2373 0.2446 0.2538 -0.0015 -0.0029 -0.0066 475  PRO A C   
3524  O O   . PRO A 477  ? 0.2598 0.2718 0.2775 -0.0010 -0.0044 -0.0106 475  PRO A O   
3525  C CB  . PRO A 477  ? 0.2340 0.2323 0.2529 -0.0010 -0.0017 -0.0065 475  PRO A CB  
3526  C CG  . PRO A 477  ? 0.3210 0.3154 0.3453 -0.0007 -0.0027 -0.0083 475  PRO A CG  
3527  C CD  . PRO A 477  ? 0.2636 0.2610 0.2915 -0.0007 -0.0045 -0.0111 475  PRO A CD  
3528  N N   . VAL A 478  ? 0.2399 0.2480 0.2527 -0.0020 -0.0018 -0.0029 476  VAL A N   
3529  C CA  . VAL A 478  ? 0.2642 0.2791 0.2740 -0.0022 -0.0023 -0.0028 476  VAL A CA  
3530  C C   . VAL A 478  ? 0.3012 0.3159 0.3070 -0.0026 -0.0009 0.0005  476  VAL A C   
3531  O O   . VAL A 478  ? 0.3136 0.3236 0.3188 -0.0031 0.0003  0.0040  476  VAL A O   
3532  C CB  . VAL A 478  ? 0.2521 0.2688 0.2627 -0.0027 -0.0029 -0.0011 476  VAL A CB  
3533  C CG1 . VAL A 478  ? 0.2806 0.3047 0.2880 -0.0029 -0.0034 -0.0004 476  VAL A CG1 
3534  C CG2 . VAL A 478  ? 0.2627 0.2794 0.2777 -0.0023 -0.0044 -0.0044 476  VAL A CG2 
3535  N N   . GLY A 479  ? 0.2687 0.2887 0.2720 -0.0025 -0.0010 -0.0007 477  GLY A N   
3536  C CA  . GLY A 479  ? 0.3038 0.3239 0.3038 -0.0031 0.0002  0.0025  477  GLY A CA  
3537  C C   . GLY A 479  ? 0.3126 0.3385 0.3105 -0.0028 0.0001  0.0006  477  GLY A C   
3538  O O   . GLY A 479  ? 0.2906 0.3197 0.2896 -0.0020 -0.0008 -0.0038 477  GLY A O   
3539  N N   . THR A 480  ? 0.3237 0.3509 0.3188 -0.0036 0.0010  0.0039  478  THR A N   
3540  C CA  . THR A 480  ? 0.3515 0.3842 0.3444 -0.0035 0.0012  0.0030  478  THR A CA  
3541  C C   . THR A 480  ? 0.3850 0.4137 0.3786 -0.0029 0.0017  0.0007  478  THR A C   
3542  O O   . THR A 480  ? 0.3865 0.4080 0.3819 -0.0026 0.0021  0.0007  478  THR A O   
3543  C CB  . THR A 480  ? 0.3849 0.4197 0.3754 -0.0047 0.0019  0.0077  478  THR A CB  
3544  O OG1 . THR A 480  ? 0.4669 0.4938 0.4578 -0.0052 0.0028  0.0106  478  THR A OG1 
3545  C CG2 . THR A 480  ? 0.3731 0.4121 0.3632 -0.0054 0.0012  0.0103  478  THR A CG2 
3546  N N   . HIS A 481  ? 0.3868 0.4208 0.3789 -0.0026 0.0019  -0.0010 479  HIS A N   
3547  C CA  . HIS A 481  ? 0.4312 0.4622 0.4238 -0.0020 0.0023  -0.0029 479  HIS A CA  
3548  C C   . HIS A 481  ? 0.4536 0.4773 0.4457 -0.0026 0.0035  0.0006  479  HIS A C   
3549  O O   . HIS A 481  ? 0.4410 0.4587 0.4346 -0.0020 0.0037  -0.0004 479  HIS A O   
3550  C CB  . HIS A 481  ? 0.3778 0.4165 0.3685 -0.0018 0.0024  -0.0045 479  HIS A CB  
3551  C CG  . HIS A 481  ? 0.4515 0.4978 0.4427 -0.0007 0.0013  -0.0090 479  HIS A CG  
3552  N ND1 . HIS A 481  ? 0.4544 0.5088 0.4443 -0.0002 0.0012  -0.0113 479  HIS A ND1 
3553  C CD2 . HIS A 481  ? 0.4443 0.4917 0.4376 0.0000  0.0000  -0.0118 479  HIS A CD2 
3554  C CE1 . HIS A 481  ? 0.4609 0.5213 0.4518 0.0009  0.0000  -0.0157 479  HIS A CE1 
3555  N NE2 . HIS A 481  ? 0.4511 0.5071 0.4441 0.0010  -0.0009 -0.0161 479  HIS A NE2 
3556  N N   . GLU A 482  ? 0.4522 0.4766 0.4425 -0.0038 0.0041  0.0049  480  GLU A N   
3557  C CA  . GLU A 482  ? 0.5172 0.5350 0.5072 -0.0043 0.0049  0.0080  480  GLU A CA  
3558  C C   . GLU A 482  ? 0.5321 0.5427 0.5240 -0.0039 0.0050  0.0082  480  GLU A C   
3559  O O   . GLU A 482  ? 0.4839 0.4889 0.4763 -0.0035 0.0056  0.0082  480  GLU A O   
3560  C CB  . GLU A 482  ? 0.5242 0.5440 0.5128 -0.0057 0.0051  0.0125  480  GLU A CB  
3561  N N   . THR A 483  ? 0.4298 0.4408 0.4227 -0.0040 0.0045  0.0086  481  THR A N   
3562  C CA  . THR A 483  ? 0.4931 0.4980 0.4878 -0.0037 0.0046  0.0092  481  THR A CA  
3563  C C   . THR A 483  ? 0.4507 0.4525 0.4477 -0.0028 0.0045  0.0061  481  THR A C   
3564  O O   . THR A 483  ? 0.4606 0.4567 0.4586 -0.0025 0.0051  0.0069  481  THR A O   
3565  C CB  . THR A 483  ? 0.4836 0.4904 0.4792 -0.0040 0.0039  0.0101  481  THR A CB  
3566  O OG1 . THR A 483  ? 0.5342 0.5442 0.5281 -0.0049 0.0039  0.0134  481  THR A OG1 
3567  C CG2 . THR A 483  ? 0.5520 0.5530 0.5497 -0.0038 0.0042  0.0112  481  THR A CG2 
3568  N N   . LEU A 484  ? 0.4192 0.4249 0.4172 -0.0022 0.0036  0.0024  482  LEU A N   
3569  C CA  . LEU A 484  ? 0.4020 0.4046 0.4030 -0.0013 0.0031  -0.0005 482  LEU A CA  
3570  C C   . LEU A 484  ? 0.4077 0.4069 0.4084 -0.0009 0.0038  -0.0008 482  LEU A C   
3571  O O   . LEU A 484  ? 0.4860 0.4802 0.4888 -0.0005 0.0039  -0.0009 482  LEU A O   
3572  C CB  . LEU A 484  ? 0.3932 0.4009 0.3959 -0.0007 0.0017  -0.0047 482  LEU A CB  
3573  C CG  . LEU A 484  ? 0.4368 0.4503 0.4382 -0.0001 0.0014  -0.0076 482  LEU A CG  
3574  C CD1 . LEU A 484  ? 0.4483 0.4591 0.4521 0.0009  0.0010  -0.0107 482  LEU A CD1 
3575  C CD2 . LEU A 484  ? 0.4598 0.4807 0.4614 0.0001  0.0001  -0.0104 482  LEU A CD2 
3576  N N   . LEU A 485  ? 0.4522 0.4544 0.4504 -0.0010 0.0042  -0.0006 483  LEU A N   
3577  C CA  . LEU A 485  ? 0.4238 0.4234 0.4216 -0.0006 0.0047  -0.0011 483  LEU A CA  
3578  C C   . LEU A 485  ? 0.4754 0.4690 0.4726 -0.0008 0.0058  0.0020  483  LEU A C   
3579  O O   . LEU A 485  ? 0.4628 0.4531 0.4605 -0.0003 0.0061  0.0016  483  LEU A O   
3580  C CB  . LEU A 485  ? 0.3865 0.3914 0.3819 -0.0008 0.0050  -0.0015 483  LEU A CB  
3581  C CG  . LEU A 485  ? 0.4640 0.4756 0.4599 -0.0001 0.0040  -0.0054 483  LEU A CG  
3582  C CD1 . LEU A 485  ? 0.4893 0.5072 0.4825 -0.0006 0.0045  -0.0048 483  LEU A CD1 
3583  C CD2 . LEU A 485  ? 0.3945 0.4043 0.3933 0.0012  0.0033  -0.0092 483  LEU A CD2 
3584  N N   . ALA A 486  ? 0.4614 0.4537 0.4576 -0.0015 0.0062  0.0050  484  ALA A N   
3585  C CA  . ALA A 486  ? 0.3865 0.3740 0.3818 -0.0017 0.0072  0.0077  484  ALA A CA  
3586  C C   . ALA A 486  ? 0.4769 0.4595 0.4740 -0.0009 0.0075  0.0074  484  ALA A C   
3587  O O   . ALA A 486  ? 0.4754 0.4552 0.4717 -0.0006 0.0081  0.0082  484  ALA A O   
3588  C CB  . ALA A 486  ? 0.4524 0.4396 0.4472 -0.0024 0.0074  0.0105  484  ALA A CB  
3589  N N   . TYR A 487  ? 0.4666 0.4485 0.4664 -0.0007 0.0070  0.0065  485  TYR A N   
3590  C CA  . TYR A 487  ? 0.4565 0.4343 0.4585 -0.0001 0.0072  0.0068  485  TYR A CA  
3591  C C   . TYR A 487  ? 0.4676 0.4460 0.4730 0.0003  0.0060  0.0040  485  TYR A C   
3592  O O   . TYR A 487  ? 0.4625 0.4383 0.4710 0.0005  0.0058  0.0043  485  TYR A O   
3593  C CB  . TYR A 487  ? 0.4813 0.4567 0.4840 -0.0003 0.0078  0.0092  485  TYR A CB  
3594  C CG  . TYR A 487  ? 0.4631 0.4377 0.4630 -0.0005 0.0087  0.0116  485  TYR A CG  
3595  C CD1 . TYR A 487  ? 0.5496 0.5216 0.5481 -0.0001 0.0095  0.0127  485  TYR A CD1 
3596  C CD2 . TYR A 487  ? 0.4130 0.3896 0.4121 -0.0011 0.0085  0.0126  485  TYR A CD2 
3597  C CE1 . TYR A 487  ? 0.5827 0.5539 0.5792 -0.0002 0.0100  0.0144  485  TYR A CE1 
3598  C CE2 . TYR A 487  ? 0.5406 0.5161 0.5378 -0.0013 0.0090  0.0147  485  TYR A CE2 
3599  C CZ  . TYR A 487  ? 0.5904 0.5631 0.5864 -0.0008 0.0097  0.0154  485  TYR A CZ  
3600  O OH  . TYR A 487  ? 0.5899 0.5615 0.5847 -0.0009 0.0100  0.0170  485  TYR A OH  
3601  N N   . LEU A 488  ? 0.4500 0.4321 0.4553 0.0005  0.0052  0.0012  486  LEU A N   
3602  C CA  . LEU A 488  ? 0.4463 0.4291 0.4553 0.0011  0.0039  -0.0021 486  LEU A CA  
3603  C C   . LEU A 488  ? 0.4441 0.4230 0.4554 0.0018  0.0038  -0.0023 486  LEU A C   
3604  O O   . LEU A 488  ? 0.3944 0.3719 0.4101 0.0022  0.0027  -0.0037 486  LEU A O   
3605  C CB  . LEU A 488  ? 0.4101 0.3986 0.4183 0.0014  0.0030  -0.0054 486  LEU A CB  
3606  C CG  . LEU A 488  ? 0.4770 0.4670 0.4894 0.0022  0.0013  -0.0096 486  LEU A CG  
3607  C CD1 . LEU A 488  ? 0.4212 0.4103 0.4366 0.0019  0.0005  -0.0097 486  LEU A CD1 
3608  C CD2 . LEU A 488  ? 0.3940 0.3906 0.4050 0.0027  0.0006  -0.0131 486  LEU A CD2 
3609  N N   . VAL A 489  ? 0.3983 0.3756 0.4072 0.0020  0.0047  -0.0007 487  VAL A N   
3610  C CA  . VAL A 489  ? 0.3765 0.3504 0.3873 0.0026  0.0046  -0.0005 487  VAL A CA  
3611  C C   . VAL A 489  ? 0.3966 0.3668 0.4104 0.0025  0.0047  0.0018  487  VAL A C   
3612  O O   . VAL A 489  ? 0.3695 0.3378 0.3875 0.0029  0.0038  0.0012  487  VAL A O   
3613  C CB  . VAL A 489  ? 0.4160 0.3891 0.4232 0.0028  0.0057  0.0010  487  VAL A CB  
3614  C CG1 . VAL A 489  ? 0.4276 0.3970 0.4366 0.0034  0.0058  0.0023  487  VAL A CG1 
3615  C CG2 . VAL A 489  ? 0.4325 0.4094 0.4381 0.0031  0.0053  -0.0015 487  VAL A CG2 
3616  N N   . ARG A 490  ? 0.3977 0.3669 0.4096 0.0019  0.0059  0.0047  488  ARG A N   
3617  C CA  . ARG A 490  ? 0.3621 0.3286 0.3767 0.0018  0.0062  0.0071  488  ARG A CA  
3618  C C   . ARG A 490  ? 0.4553 0.4221 0.4748 0.0015  0.0048  0.0055  488  ARG A C   
3619  O O   . ARG A 490  ? 0.4111 0.3756 0.4347 0.0015  0.0043  0.0065  488  ARG A O   
3620  C CB  . ARG A 490  ? 0.4460 0.4123 0.4580 0.0013  0.0075  0.0098  488  ARG A CB  
3621  C CG  . ARG A 490  ? 0.3903 0.3546 0.4048 0.0012  0.0080  0.0124  488  ARG A CG  
3622  C CD  . ARG A 490  ? 0.4123 0.3769 0.4247 0.0010  0.0092  0.0145  488  ARG A CD  
3623  N NE  . ARG A 490  ? 0.4445 0.4112 0.4572 0.0004  0.0086  0.0134  488  ARG A NE  
3624  C CZ  . ARG A 490  ? 0.4737 0.4418 0.4833 0.0002  0.0090  0.0137  488  ARG A CZ  
3625  N NH1 . ARG A 490  ? 0.3806 0.3480 0.3868 0.0005  0.0100  0.0148  488  ARG A NH1 
3626  N NH2 . ARG A 490  ? 0.5027 0.4729 0.5130 -0.0003 0.0084  0.0129  488  ARG A NH2 
3627  N N   . ARG A 491  ? 0.4212 0.3911 0.4405 0.0013  0.0040  0.0030  489  ARG A N   
3628  C CA  . ARG A 491  ? 0.4334 0.4040 0.4574 0.0011  0.0025  0.0011  489  ARG A CA  
3629  C C   . ARG A 491  ? 0.5580 0.5280 0.5863 0.0017  0.0008  -0.0019 489  ARG A C   
3630  O O   . ARG A 491  ? 0.4637 0.4323 0.4975 0.0016  -0.0005 -0.0025 489  ARG A O   
3631  C CB  . ARG A 491  ? 0.5070 0.4818 0.5292 0.0008  0.0021  -0.0007 489  ARG A CB  
3632  C CG  . ARG A 491  ? 0.6226 0.6003 0.6479 0.0011  0.0001  -0.0051 489  ARG A CG  
3633  C CD  . ARG A 491  ? 0.6545 0.6339 0.6819 0.0006  -0.0007 -0.0057 489  ARG A CD  
3634  N NE  . ARG A 491  ? 0.7004 0.6819 0.7237 0.0000  0.0004  -0.0035 489  ARG A NE  
3635  C CZ  . ARG A 491  ? 0.7067 0.6865 0.7302 -0.0006 0.0013  -0.0004 489  ARG A CZ  
3636  N NH1 . ARG A 491  ? 0.6648 0.6411 0.6921 -0.0008 0.0013  0.0012  489  ARG A NH1 
3637  N NH2 . ARG A 491  ? 0.6807 0.6625 0.7008 -0.0010 0.0020  0.0012  489  ARG A NH2 
3638  N N   . LEU A 492  ? 0.4772 0.4483 0.5037 0.0025  0.0007  -0.0038 490  LEU A N   
3639  C CA  . LEU A 492  ? 0.4721 0.4426 0.5029 0.0033  -0.0010 -0.0068 490  LEU A CA  
3640  C C   . LEU A 492  ? 0.5551 0.5210 0.5893 0.0034  -0.0010 -0.0041 490  LEU A C   
3641  O O   . LEU A 492  ? 0.5308 0.4949 0.5710 0.0037  -0.0027 -0.0053 490  LEU A O   
3642  C CB  . LEU A 492  ? 0.4137 0.3872 0.4415 0.0041  -0.0010 -0.0094 490  LEU A CB  
3643  C CG  . LEU A 492  ? 0.4665 0.4455 0.4913 0.0041  -0.0011 -0.0122 490  LEU A CG  
3644  C CD1 . LEU A 492  ? 0.4750 0.4571 0.4962 0.0047  -0.0006 -0.0135 490  LEU A CD1 
3645  C CD2 . LEU A 492  ? 0.5324 0.5139 0.5617 0.0046  -0.0032 -0.0165 490  LEU A CD2 
3646  N N   . LEU A 493  ? 0.4127 0.3768 0.4434 0.0032  0.0007  -0.0003 491  LEU A N   
3647  C CA  . LEU A 493  ? 0.4370 0.3976 0.4704 0.0033  0.0008  0.0027  491  LEU A CA  
3648  C C   . LEU A 493  ? 0.5131 0.4717 0.5516 0.0026  0.0003  0.0048  491  LEU A C   
3649  O O   . LEU A 493  ? 0.5450 0.5011 0.5881 0.0027  -0.0004 0.0065  491  LEU A O   
3650  C CB  . LEU A 493  ? 0.4488 0.4086 0.4770 0.0033  0.0029  0.0062  491  LEU A CB  
3651  C CG  . LEU A 493  ? 0.5496 0.5109 0.5731 0.0039  0.0034  0.0048  491  LEU A CG  
3652  C CD1 . LEU A 493  ? 0.5313 0.4912 0.5515 0.0041  0.0049  0.0082  491  LEU A CD1 
3653  C CD2 . LEU A 493  ? 0.5769 0.5385 0.6034 0.0048  0.0018  0.0016  491  LEU A CD2 
3654  N N   . GLU A 494  ? 0.5647 0.5247 0.6029 0.0019  0.0006  0.0049  492  GLU A N   
3655  C CA  . GLU A 494  ? 0.5785 0.5371 0.6216 0.0011  0.0002  0.0070  492  GLU A CA  
3656  C C   . GLU A 494  ? 0.5837 0.5407 0.6344 0.0011  -0.0023 0.0050  492  GLU A C   
3657  O O   . GLU A 494  ? 0.5403 0.4949 0.5961 0.0007  -0.0027 0.0078  492  GLU A O   
3658  C CB  . GLU A 494  ? 0.5117 0.4725 0.5535 0.0004  0.0005  0.0064  492  GLU A CB  
3659  N N   . ASN A 495  ? 0.5693 0.5279 0.6212 0.0018  -0.0039 0.0000  493  ASN A N   
3660  C CA  . ASN A 495  ? 0.6257 0.5830 0.6852 0.0021  -0.0066 -0.0029 493  ASN A CA  
3661  C C   . ASN A 495  ? 0.6098 0.5667 0.6700 0.0034  -0.0076 -0.0055 493  ASN A C   
3662  O O   . ASN A 495  ? 0.4935 0.4499 0.5597 0.0040  -0.0100 -0.0091 493  ASN A O   
3663  C CB  . ASN A 495  ? 0.5336 0.4938 0.5952 0.0021  -0.0081 -0.0073 493  ASN A CB  
3664  C CG  . ASN A 495  ? 0.4924 0.4531 0.5540 0.0008  -0.0073 -0.0048 493  ASN A CG  
3665  O OD1 . ASN A 495  ? 0.4384 0.3966 0.5053 0.0000  -0.0078 -0.0021 493  ASN A OD1 
3666  N ND2 . ASN A 495  ? 0.4022 0.3663 0.4580 0.0007  -0.0062 -0.0055 493  ASN A ND2 
3667  N N   . GLY A 496  ? 0.5975 0.5546 0.6521 0.0039  -0.0059 -0.0039 494  GLY A N   
3668  C CA  . GLY A 496  ? 0.6083 0.5657 0.6629 0.0051  -0.0068 -0.0066 494  GLY A CA  
3669  C C   . GLY A 496  ? 0.6684 0.6228 0.7230 0.0055  -0.0062 -0.0032 494  GLY A C   
3670  O O   . GLY A 496  ? 0.6339 0.5884 0.6890 0.0066  -0.0071 -0.0054 494  GLY A O   
3671  N N   . ALA A 497  ? 0.5726 0.5250 0.6267 0.0046  -0.0049 0.0021  495  ALA A N   
3672  C CA  . ALA A 497  ? 0.5512 0.5014 0.6056 0.0050  -0.0044 0.0057  495  ALA A CA  
3673  C C   . ALA A 497  ? 0.4773 0.4245 0.5403 0.0051  -0.0068 0.0061  495  ALA A C   
3674  O O   . ALA A 497  ? 0.4998 0.4462 0.5689 0.0047  -0.0085 0.0046  495  ALA A O   
3675  C CB  . ALA A 497  ? 0.4811 0.4310 0.5318 0.0042  -0.0022 0.0111  495  ALA A CB  
3676  N N   . ASN A 498  ? 0.5103 0.4558 0.5742 0.0058  -0.0070 0.0083  496  ASN A N   
3677  C CA  . ASN A 498  ? 0.4820 0.4246 0.5545 0.0060  -0.0095 0.0088  496  ASN A CA  
3678  C C   . ASN A 498  ? 0.5268 0.4674 0.6055 0.0047  -0.0101 0.0126  496  ASN A C   
3679  O O   . ASN A 498  ? 0.4986 0.4369 0.5859 0.0046  -0.0127 0.0117  496  ASN A O   
3680  C CB  . ASN A 498  ? 0.5477 0.4891 0.6195 0.0069  -0.0094 0.0115  496  ASN A CB  
3681  N N   . SER A 499  ? 0.4749 0.4166 0.5498 0.0036  -0.0079 0.0168  497  SER A N   
3682  C CA  . SER A 499  ? 0.4762 0.4168 0.5565 0.0022  -0.0081 0.0207  497  SER A CA  
3683  C C   . SER A 499  ? 0.4212 0.3626 0.5032 0.0015  -0.0087 0.0177  497  SER A C   
3684  O O   . SER A 499  ? 0.4053 0.3458 0.4930 0.0003  -0.0093 0.0202  497  SER A O   
3685  C CB  . SER A 499  ? 0.5361 0.4781 0.6116 0.0016  -0.0054 0.0267  497  SER A CB  
3686  O OG  . SER A 499  ? 0.5299 0.4744 0.5963 0.0020  -0.0031 0.0253  497  SER A OG  
3687  N N   . SER A 500  ? 0.4211 0.3647 0.4986 0.0021  -0.0085 0.0125  498  SER A N   
3688  C CA  . SER A 500  ? 0.3805 0.3256 0.4589 0.0015  -0.0089 0.0096  498  SER A CA  
3689  C C   . SER A 500  ? 0.4217 0.3652 0.5093 0.0015  -0.0122 0.0061  498  SER A C   
3690  O O   . SER A 500  ? 0.4089 0.3513 0.5000 0.0026  -0.0142 0.0029  498  SER A O   
3691  C CB  . SER A 500  ? 0.4301 0.3785 0.5010 0.0022  -0.0079 0.0054  498  SER A CB  
3692  O OG  . SER A 500  ? 0.5091 0.4589 0.5722 0.0020  -0.0051 0.0085  498  SER A OG  
3693  N N   . PHE A 501  ? 0.3580 0.3016 0.4497 0.0003  -0.0128 0.0066  499  PHE A N   
3694  C CA  . PHE A 501  ? 0.3690 0.3112 0.4699 0.0002  -0.0161 0.0030  499  PHE A CA  
3695  C C   . PHE A 501  ? 0.4515 0.3958 0.5516 0.0017  -0.0177 -0.0045 499  PHE A C   
3696  O O   . PHE A 501  ? 0.4422 0.3849 0.5491 0.0026  -0.0205 -0.0081 499  PHE A O   
3697  C CB  . PHE A 501  ? 0.3170 0.2598 0.4213 -0.0013 -0.0163 0.0041  499  PHE A CB  
3698  C CG  . PHE A 501  ? 0.3509 0.2926 0.4646 -0.0014 -0.0198 -0.0002 499  PHE A CG  
3699  C CD1 . PHE A 501  ? 0.3387 0.2768 0.4624 -0.0021 -0.0220 0.0021  499  PHE A CD1 
3700  C CD2 . PHE A 501  ? 0.3882 0.3329 0.5009 -0.0006 -0.0210 -0.0067 499  PHE A CD2 
3701  C CE1 . PHE A 501  ? 0.3726 0.3095 0.5058 -0.0022 -0.0256 -0.0021 499  PHE A CE1 
3702  C CE2 . PHE A 501  ? 0.3537 0.2976 0.4752 -0.0006 -0.0244 -0.0112 499  PHE A CE2 
3703  C CZ  . PHE A 501  ? 0.3985 0.3383 0.5304 -0.0013 -0.0268 -0.0091 499  PHE A CZ  
3704  N N   . VAL A 502  ? 0.4162 0.3643 0.5083 0.0020  -0.0161 -0.0069 500  VAL A N   
3705  C CA  . VAL A 502  ? 0.4576 0.4088 0.5487 0.0034  -0.0175 -0.0139 500  VAL A CA  
3706  C C   . VAL A 502  ? 0.5045 0.4553 0.5952 0.0049  -0.0181 -0.0161 500  VAL A C   
3707  O O   . VAL A 502  ? 0.5290 0.4808 0.6237 0.0062  -0.0205 -0.0218 500  VAL A O   
3708  C CB  . VAL A 502  ? 0.4671 0.4228 0.5496 0.0033  -0.0154 -0.0150 500  VAL A CB  
3709  N N   . HIS A 503  ? 0.4271 0.3767 0.5132 0.0049  -0.0160 -0.0118 501  HIS A N   
3710  C CA  . HIS A 503  ? 0.4797 0.4285 0.5661 0.0063  -0.0167 -0.0133 501  HIS A CA  
3711  C C   . HIS A 503  ? 0.4978 0.4426 0.5944 0.0067  -0.0197 -0.0135 501  HIS A C   
3712  O O   . HIS A 503  ? 0.4685 0.4133 0.5687 0.0082  -0.0217 -0.0180 501  HIS A O   
3713  C CB  . HIS A 503  ? 0.4789 0.4272 0.5585 0.0062  -0.0140 -0.0084 501  HIS A CB  
3714  C CG  . HIS A 503  ? 0.5595 0.5072 0.6389 0.0076  -0.0145 -0.0096 501  HIS A CG  
3715  N ND1 . HIS A 503  ? 0.5791 0.5231 0.6640 0.0078  -0.0157 -0.0068 501  HIS A ND1 
3716  C CD2 . HIS A 503  ? 0.5533 0.5039 0.6279 0.0088  -0.0141 -0.0132 501  HIS A CD2 
3717  C CE1 . HIS A 503  ? 0.5272 0.4716 0.6106 0.0092  -0.0160 -0.0087 501  HIS A CE1 
3718  N NE2 . HIS A 503  ? 0.5812 0.5297 0.6584 0.0098  -0.0150 -0.0127 501  HIS A NE2 
3719  N N   . ARG A 504  ? 0.4165 0.3580 0.5184 0.0053  -0.0200 -0.0086 502  ARG A N   
3720  C CA  . ARG A 504  ? 0.4142 0.3516 0.5262 0.0053  -0.0228 -0.0077 502  ARG A CA  
3721  C C   . ARG A 504  ? 0.4791 0.4161 0.5996 0.0058  -0.0263 -0.0137 502  ARG A C   
3722  O O   . ARG A 504  ? 0.4140 0.3487 0.5421 0.0069  -0.0292 -0.0163 502  ARG A O   
3723  C CB  . ARG A 504  ? 0.4476 0.3823 0.5626 0.0036  -0.0219 0.0000  502  ARG A CB  
3724  C CG  . ARG A 504  ? 0.4449 0.3796 0.5531 0.0035  -0.0191 0.0057  502  ARG A CG  
3725  C CD  . ARG A 504  ? 0.4885 0.4228 0.5964 0.0017  -0.0173 0.0128  502  ARG A CD  
3726  N NE  . ARG A 504  ? 0.4808 0.4121 0.5994 0.0006  -0.0196 0.0155  502  ARG A NE  
3727  C CZ  . ARG A 504  ? 0.5691 0.4975 0.6944 0.0006  -0.0213 0.0188  502  ARG A CZ  
3728  N NH1 . ARG A 504  ? 0.5609 0.4889 0.6833 0.0019  -0.0209 0.0195  502  ARG A NH1 
3729  N NH2 . ARG A 504  ? 0.5590 0.4848 0.6944 -0.0006 -0.0234 0.0217  502  ARG A NH2 
3730  N N   . ILE A 505  ? 0.4905 0.4300 0.6104 0.0052  -0.0263 -0.0162 503  ILE A N   
3731  C CA  . ILE A 505  ? 0.4704 0.4101 0.5983 0.0058  -0.0298 -0.0224 503  ILE A CA  
3732  C C   . ILE A 505  ? 0.5194 0.4617 0.6465 0.0081  -0.0312 -0.0297 503  ILE A C   
3733  O O   . ILE A 505  ? 0.5099 0.4512 0.6456 0.0092  -0.0347 -0.0348 503  ILE A O   
3734  C CB  . ILE A 505  ? 0.4899 0.4325 0.6164 0.0047  -0.0294 -0.0239 503  ILE A CB  
3735  C CG1 . ILE A 505  ? 0.5428 0.4859 0.6777 0.0055  -0.0332 -0.0308 503  ILE A CG1 
3736  C CG2 . ILE A 505  ? 0.5288 0.4765 0.6440 0.0051  -0.0266 -0.0254 503  ILE A CG2 
3737  C CD1 . ILE A 505  ? 0.4153 0.3560 0.5586 0.0038  -0.0349 -0.0288 503  ILE A CD1 
3738  N N   . ASN A 506  ? 0.4687 0.4146 0.5860 0.0089  -0.0287 -0.0303 504  ASN A N   
3739  C CA  . ASN A 506  ? 0.5256 0.4746 0.6415 0.0111  -0.0296 -0.0367 504  ASN A CA  
3740  C C   . ASN A 506  ? 0.5896 0.5354 0.7088 0.0122  -0.0306 -0.0358 504  ASN A C   
3741  O O   . ASN A 506  ? 0.6546 0.6027 0.7746 0.0142  -0.0319 -0.0413 504  ASN A O   
3742  C CB  . ASN A 506  ? 0.5303 0.4848 0.6347 0.0113  -0.0266 -0.0375 504  ASN A CB  
3743  C CG  . ASN A 506  ? 0.5864 0.5455 0.6881 0.0109  -0.0264 -0.0406 504  ASN A CG  
3744  O OD1 . ASN A 506  ? 0.6931 0.6526 0.8013 0.0112  -0.0290 -0.0448 504  ASN A OD1 
3745  N ND2 . ASN A 506  ? 0.7018 0.6644 0.7939 0.0103  -0.0234 -0.0385 504  ASN A ND2 
3746  N N   . ASP A 507  ? 0.4818 0.4229 0.6031 0.0111  -0.0300 -0.0289 505  ASP A N   
3747  C CA  . ASP A 507  ? 0.5147 0.4529 0.6390 0.0121  -0.0308 -0.0272 505  ASP A CA  
3748  C C   . ASP A 507  ? 0.6213 0.5555 0.7585 0.0126  -0.0350 -0.0295 505  ASP A C   
3749  O O   . ASP A 507  ? 0.5233 0.4538 0.6671 0.0110  -0.0360 -0.0253 505  ASP A O   
3750  C CB  . ASP A 507  ? 0.4900 0.4256 0.6104 0.0107  -0.0283 -0.0187 505  ASP A CB  
3751  C CG  . ASP A 507  ? 0.5825 0.5160 0.7042 0.0118  -0.0287 -0.0168 505  ASP A CG  
3752  O OD1 . ASP A 507  ? 0.6129 0.5452 0.7414 0.0134  -0.0317 -0.0211 505  ASP A OD1 
3753  O OD2 . ASP A 507  ? 0.5377 0.4708 0.6536 0.0111  -0.0263 -0.0111 505  ASP A OD2 
3754  N N   . PRO A 508  ? 0.6221 0.5570 0.7636 0.0148  -0.0375 -0.0359 506  PRO A N   
3755  C CA  . PRO A 508  ? 0.5894 0.5202 0.7441 0.0155  -0.0419 -0.0384 506  PRO A CA  
3756  C C   . PRO A 508  ? 0.5161 0.4411 0.6771 0.0147  -0.0427 -0.0314 506  PRO A C   
3757  O O   . PRO A 508  ? 0.6534 0.5742 0.8260 0.0144  -0.0462 -0.0314 506  PRO A O   
3758  C CB  . PRO A 508  ? 0.5974 0.5312 0.7535 0.0183  -0.0438 -0.0468 506  PRO A CB  
3759  C CG  . PRO A 508  ? 0.6822 0.6226 0.8261 0.0188  -0.0406 -0.0494 506  PRO A CG  
3760  C CD  . PRO A 508  ? 0.6137 0.5535 0.7488 0.0168  -0.0367 -0.0413 506  PRO A CD  
3761  N N   . LYS A 509  ? 0.5282 0.4529 0.6822 0.0142  -0.0399 -0.0254 507  LYS A N   
3762  C CA  . LYS A 509  ? 0.5640 0.4841 0.7230 0.0134  -0.0404 -0.0180 507  LYS A CA  
3763  C C   . LYS A 509  ? 0.5910 0.5092 0.7509 0.0107  -0.0391 -0.0105 507  LYS A C   
3764  O O   . LYS A 509  ? 0.6582 0.5732 0.8220 0.0098  -0.0393 -0.0035 507  LYS A O   
3765  C CB  . LYS A 509  ? 0.6108 0.5320 0.7618 0.0141  -0.0380 -0.0149 507  LYS A CB  
3766  N N   . VAL A 510  ? 0.5445 0.4651 0.7010 0.0095  -0.0378 -0.0115 508  VAL A N   
3767  C CA  . VAL A 510  ? 0.4984 0.4177 0.6563 0.0071  -0.0367 -0.0051 508  VAL A CA  
3768  C C   . VAL A 510  ? 0.4774 0.3945 0.6464 0.0064  -0.0402 -0.0082 508  VAL A C   
3769  O O   . VAL A 510  ? 0.4918 0.4115 0.6606 0.0072  -0.0412 -0.0152 508  VAL A O   
3770  C CB  . VAL A 510  ? 0.5068 0.4301 0.6530 0.0061  -0.0326 -0.0036 508  VAL A CB  
3771  C CG1 . VAL A 510  ? 0.4693 0.3917 0.6173 0.0037  -0.0315 0.0031  508  VAL A CG1 
3772  C CG2 . VAL A 510  ? 0.5015 0.4269 0.6372 0.0069  -0.0295 -0.0013 508  VAL A CG2 
3773  N N   . SER A 511  ? 0.4268 0.3397 0.6059 0.0051  -0.0422 -0.0028 509  SER A N   
3774  C CA  . SER A 511  ? 0.5131 0.4235 0.7042 0.0043  -0.0459 -0.0053 509  SER A CA  
3775  C C   . SER A 511  ? 0.4665 0.3788 0.6556 0.0023  -0.0443 -0.0034 509  SER A C   
3776  O O   . SER A 511  ? 0.4395 0.3543 0.6195 0.0011  -0.0404 0.0016  509  SER A O   
3777  C CB  . SER A 511  ? 0.5220 0.4272 0.7254 0.0034  -0.0487 0.0003  509  SER A CB  
3778  O OG  . SER A 511  ? 0.5108 0.4158 0.7125 0.0012  -0.0462 0.0101  509  SER A OG  
3779  N N   . ILE A 512  ? 0.4830 0.3942 0.6811 0.0019  -0.0475 -0.0077 510  ILE A N   
3780  C CA  . ILE A 512  ? 0.5090 0.4219 0.7068 -0.0001 -0.0465 -0.0062 510  ILE A CA  
3781  C C   . ILE A 512  ? 0.5390 0.4497 0.7406 -0.0026 -0.0454 0.0039  510  ILE A C   
3782  O O   . ILE A 512  ? 0.4684 0.3816 0.6642 -0.0042 -0.0424 0.0080  510  ILE A O   
3783  C CB  . ILE A 512  ? 0.4369 0.3492 0.6442 0.0002  -0.0505 -0.0135 510  ILE A CB  
3784  C CG1 . ILE A 512  ? 0.4709 0.3868 0.6730 0.0029  -0.0511 -0.0234 510  ILE A CG1 
3785  C CG2 . ILE A 512  ? 0.4468 0.3607 0.6547 -0.0019 -0.0497 -0.0116 510  ILE A CG2 
3786  C CD1 . ILE A 512  ? 0.4963 0.4132 0.7055 0.0034  -0.0546 -0.0314 510  ILE A CD1 
3787  N N   . ASP A 513  ? 0.4858 0.3922 0.6971 -0.0030 -0.0478 0.0081  511  ASP A N   
3788  C CA  . ASP A 513  ? 0.4253 0.3304 0.6398 -0.0053 -0.0465 0.0183  511  ASP A CA  
3789  C C   . ASP A 513  ? 0.4665 0.3750 0.6678 -0.0055 -0.0416 0.0239  511  ASP A C   
3790  O O   . ASP A 513  ? 0.4373 0.3475 0.6367 -0.0074 -0.0392 0.0308  511  ASP A O   
3791  C CB  . ASP A 513  ? 0.5486 0.4489 0.7750 -0.0054 -0.0499 0.0219  511  ASP A CB  
3792  C CG  . ASP A 513  ? 0.6239 0.5203 0.8655 -0.0059 -0.0550 0.0180  511  ASP A CG  
3793  O OD1 . ASP A 513  ? 0.6267 0.5239 0.8718 -0.0075 -0.0555 0.0175  511  ASP A OD1 
3794  O OD2 . ASP A 513  ? 0.7034 0.5961 0.9538 -0.0046 -0.0587 0.0155  511  ASP A OD2 
3795  N N   . GLU A 514  ? 0.4531 0.3630 0.6456 -0.0035 -0.0401 0.0210  512  GLU A N   
3796  C CA  . GLU A 514  ? 0.4297 0.3430 0.6094 -0.0034 -0.0356 0.0253  512  GLU A CA  
3797  C C   . GLU A 514  ? 0.3940 0.3113 0.5650 -0.0040 -0.0327 0.0235  512  GLU A C   
3798  O O   . GLU A 514  ? 0.4538 0.3735 0.6183 -0.0051 -0.0294 0.0292  512  GLU A O   
3799  C CB  . GLU A 514  ? 0.4991 0.4130 0.6720 -0.0011 -0.0349 0.0220  512  GLU A CB  
3800  C CG  . GLU A 514  ? 0.5808 0.4916 0.7594 -0.0006 -0.0365 0.0262  512  GLU A CG  
3801  C CD  . GLU A 514  ? 0.6751 0.5860 0.8496 0.0019  -0.0370 0.0210  512  GLU A CD  
3802  O OE1 . GLU A 514  ? 0.6685 0.5804 0.8413 0.0033  -0.0379 0.0127  512  GLU A OE1 
3803  O OE2 . GLU A 514  ? 0.7838 0.6941 0.9567 0.0024  -0.0364 0.0253  512  GLU A OE2 
3804  N N   . LEU A 515  ? 0.4457 0.3639 0.6166 -0.0032 -0.0340 0.0157  513  LEU A N   
3805  C CA  . LEU A 515  ? 0.4547 0.3769 0.6173 -0.0036 -0.0315 0.0137  513  LEU A CA  
3806  C C   . LEU A 515  ? 0.3821 0.3045 0.5494 -0.0059 -0.0313 0.0178  513  LEU A C   
3807  O O   . LEU A 515  ? 0.3866 0.3122 0.5465 -0.0065 -0.0285 0.0189  513  LEU A O   
3808  C CB  . LEU A 515  ? 0.4200 0.3438 0.5813 -0.0020 -0.0331 0.0042  513  LEU A CB  
3809  C CG  . LEU A 515  ? 0.4246 0.3499 0.5787 0.0003  -0.0325 -0.0004 513  LEU A CG  
3810  C CD1 . LEU A 515  ? 0.4368 0.3641 0.5917 0.0018  -0.0346 -0.0097 513  LEU A CD1 
3811  C CD2 . LEU A 515  ? 0.4035 0.3319 0.5445 0.0003  -0.0281 0.0026  513  LEU A CD2 
3812  N N   . ILE A 516  ? 0.3792 0.2983 0.5590 -0.0071 -0.0344 0.0199  514  ILE A N   
3813  C CA  . ILE A 516  ? 0.3533 0.2727 0.5385 -0.0094 -0.0344 0.0241  514  ILE A CA  
3814  C C   . ILE A 516  ? 0.3651 0.2842 0.5521 -0.0111 -0.0327 0.0341  514  ILE A C   
3815  O O   . ILE A 516  ? 0.3743 0.2937 0.5673 -0.0132 -0.0329 0.0387  514  ILE A O   
3816  C CB  . ILE A 516  ? 0.3950 0.3116 0.5935 -0.0100 -0.0390 0.0200  514  ILE A CB  
3817  C CG1 . ILE A 516  ? 0.4522 0.3640 0.6622 -0.0101 -0.0423 0.0224  514  ILE A CG1 
3818  C CG2 . ILE A 516  ? 0.3974 0.3153 0.5934 -0.0081 -0.0406 0.0098  514  ILE A CG2 
3819  C CD1 . ILE A 516  ? 0.4271 0.3356 0.6517 -0.0110 -0.0470 0.0197  514  ILE A CD1 
3820  N N   . ALA A 517  ? 0.3528 0.2719 0.5348 -0.0102 -0.0311 0.0376  515  ALA A N   
3821  C CA  . ALA A 517  ? 0.3852 0.3054 0.5670 -0.0116 -0.0290 0.0471  515  ALA A CA  
3822  C C   . ALA A 517  ? 0.3855 0.3101 0.5606 -0.0128 -0.0254 0.0505  515  ALA A C   
3823  O O   . ALA A 517  ? 0.3533 0.2805 0.5187 -0.0118 -0.0232 0.0465  515  ALA A O   
3824  C CB  . ALA A 517  ? 0.4048 0.3253 0.5796 -0.0101 -0.0274 0.0492  515  ALA A CB  
3825  N N   . ASP A 518  ? 0.3662 0.2916 0.5471 -0.0148 -0.0250 0.0580  516  ASP A N   
3826  C CA  . ASP A 518  ? 0.3576 0.2874 0.5339 -0.0161 -0.0219 0.0619  516  ASP A CA  
3827  C C   . ASP A 518  ? 0.3531 0.2867 0.5188 -0.0154 -0.0179 0.0667  516  ASP A C   
3828  O O   . ASP A 518  ? 0.3499 0.2842 0.5181 -0.0160 -0.0174 0.0738  516  ASP A O   
3829  C CB  . ASP A 518  ? 0.4075 0.3371 0.5954 -0.0186 -0.0233 0.0680  516  ASP A CB  
3830  C CG  . ASP A 518  ? 0.3797 0.3140 0.5638 -0.0199 -0.0203 0.0714  516  ASP A CG  
3831  O OD1 . ASP A 518  ? 0.3598 0.2973 0.5327 -0.0188 -0.0173 0.0690  516  ASP A OD1 
3832  O OD2 . ASP A 518  ? 0.4252 0.3601 0.6184 -0.0221 -0.0212 0.0766  516  ASP A OD2 
3833  N N   . PRO A 519  ? 0.3398 0.2761 0.4939 -0.0141 -0.0151 0.0632  517  PRO A N   
3834  C CA  . PRO A 519  ? 0.3454 0.2853 0.4896 -0.0133 -0.0115 0.0672  517  PRO A CA  
3835  C C   . PRO A 519  ? 0.3173 0.2612 0.4629 -0.0149 -0.0094 0.0755  517  PRO A C   
3836  O O   . PRO A 519  ? 0.3321 0.2787 0.4734 -0.0144 -0.0074 0.0805  517  PRO A O   
3837  C CB  . PRO A 519  ? 0.3271 0.2690 0.4606 -0.0120 -0.0094 0.0614  517  PRO A CB  
3838  C CG  . PRO A 519  ? 0.3555 0.2964 0.4934 -0.0128 -0.0111 0.0569  517  PRO A CG  
3839  C CD  . PRO A 519  ? 0.3495 0.2862 0.4994 -0.0135 -0.0151 0.0559  517  PRO A CD  
3840  N N   . VAL A 520  ? 0.3336 0.2786 0.4851 -0.0166 -0.0098 0.0770  518  VAL A N   
3841  C CA  . VAL A 520  ? 0.3077 0.2573 0.4608 -0.0181 -0.0076 0.0848  518  VAL A CA  
3842  C C   . VAL A 520  ? 0.3560 0.3050 0.5169 -0.0192 -0.0089 0.0921  518  VAL A C   
3843  O O   . VAL A 520  ? 0.3538 0.3072 0.5114 -0.0193 -0.0065 0.0986  518  VAL A O   
3844  C CB  . VAL A 520  ? 0.3215 0.2721 0.4805 -0.0199 -0.0082 0.0845  518  VAL A CB  
3845  C CG1 . VAL A 520  ? 0.3390 0.2951 0.4994 -0.0214 -0.0058 0.0927  518  VAL A CG1 
3846  C CG2 . VAL A 520  ? 0.3564 0.3075 0.5077 -0.0187 -0.0071 0.0774  518  VAL A CG2 
3847  N N   . GLU A 521  ? 0.3761 0.3200 0.5476 -0.0199 -0.0127 0.0910  519  GLU A N   
3848  C CA  . GLU A 521  ? 0.3706 0.3136 0.5507 -0.0210 -0.0144 0.0981  519  GLU A CA  
3849  C C   . GLU A 521  ? 0.4462 0.3885 0.6207 -0.0192 -0.0139 0.0988  519  GLU A C   
3850  O O   . GLU A 521  ? 0.4048 0.3490 0.5820 -0.0198 -0.0136 0.1064  519  GLU A O   
3851  C CB  . GLU A 521  ? 0.3860 0.3233 0.5800 -0.0223 -0.0190 0.0965  519  GLU A CB  
3852  C CG  . GLU A 521  ? 0.4545 0.3928 0.6559 -0.0245 -0.0197 0.0975  519  GLU A CG  
3853  C CD  . GLU A 521  ? 0.5611 0.5054 0.7630 -0.0263 -0.0169 0.1068  519  GLU A CD  
3854  O OE1 . GLU A 521  ? 0.5640 0.5101 0.7676 -0.0267 -0.0164 0.1142  519  GLU A OE1 
3855  O OE2 . GLU A 521  ? 0.5765 0.5242 0.7769 -0.0272 -0.0152 0.1067  519  GLU A OE2 
3856  N N   . VAL A 522  ? 0.3810 0.3212 0.5480 -0.0171 -0.0139 0.0913  520  VAL A N   
3857  C CA  . VAL A 522  ? 0.3084 0.2484 0.4695 -0.0153 -0.0134 0.0917  520  VAL A CA  
3858  C C   . VAL A 522  ? 0.4406 0.3869 0.5919 -0.0148 -0.0093 0.0966  520  VAL A C   
3859  O O   . VAL A 522  ? 0.4039 0.3520 0.5547 -0.0146 -0.0087 0.1023  520  VAL A O   
3860  C CB  . VAL A 522  ? 0.3740 0.3107 0.5295 -0.0132 -0.0142 0.0825  520  VAL A CB  
3861  C CG1 . VAL A 522  ? 0.4084 0.3456 0.5569 -0.0113 -0.0132 0.0829  520  VAL A CG1 
3862  C CG2 . VAL A 522  ? 0.4467 0.3778 0.6126 -0.0134 -0.0185 0.0776  520  VAL A CG2 
3863  N N   . VAL A 523  ? 0.3378 0.2876 0.4811 -0.0145 -0.0064 0.0944  521  VAL A N   
3864  C CA  . VAL A 523  ? 0.3443 0.3003 0.4786 -0.0139 -0.0027 0.0986  521  VAL A CA  
3865  C C   . VAL A 523  ? 0.3811 0.3414 0.5214 -0.0157 -0.0020 0.1080  521  VAL A C   
3866  O O   . VAL A 523  ? 0.3747 0.3393 0.5112 -0.0152 -0.0002 0.1133  521  VAL A O   
3867  C CB  . VAL A 523  ? 0.2710 0.2297 0.3970 -0.0133 -0.0001 0.0941  521  VAL A CB  
3868  C CG1 . VAL A 523  ? 0.3479 0.3136 0.4664 -0.0129 0.0036  0.0988  521  VAL A CG1 
3869  C CG2 . VAL A 523  ? 0.3339 0.2894 0.4527 -0.0114 -0.0004 0.0859  521  VAL A CG2 
3870  N N   . ARG A 524  ? 0.3586 0.3182 0.5084 -0.0178 -0.0033 0.1103  522  ARG A N   
3871  C CA  . ARG A 524  ? 0.3820 0.3462 0.5383 -0.0198 -0.0027 0.1196  522  ARG A CA  
3872  C C   . ARG A 524  ? 0.4391 0.4029 0.5998 -0.0200 -0.0040 0.1259  522  ARG A C   
3873  O O   . ARG A 524  ? 0.4758 0.4456 0.6366 -0.0207 -0.0023 0.1339  522  ARG A O   
3874  C CB  . ARG A 524  ? 0.4505 0.4126 0.6182 -0.0222 -0.0049 0.1205  522  ARG A CB  
3875  C CG  . ARG A 524  ? 0.4620 0.4286 0.6379 -0.0245 -0.0046 0.1307  522  ARG A CG  
3876  C CD  . ARG A 524  ? 0.4985 0.4616 0.6881 -0.0270 -0.0077 0.1317  522  ARG A CD  
3877  N NE  . ARG A 524  ? 0.5082 0.4696 0.6965 -0.0270 -0.0078 0.1245  522  ARG A NE  
3878  C CZ  . ARG A 524  ? 0.4571 0.4236 0.6411 -0.0274 -0.0050 0.1249  522  ARG A CZ  
3879  N NH1 . ARG A 524  ? 0.4457 0.4198 0.6258 -0.0276 -0.0017 0.1316  522  ARG A NH1 
3880  N NH2 . ARG A 524  ? 0.4586 0.4230 0.6424 -0.0274 -0.0057 0.1183  522  ARG A NH2 
3881  N N   . ALA A 525  ? 0.4234 0.3809 0.5878 -0.0192 -0.0071 0.1223  523  ALA A N   
3882  C CA  . ALA A 525  ? 0.5119 0.4681 0.6823 -0.0195 -0.0091 0.1280  523  ALA A CA  
3883  C C   . ALA A 525  ? 0.4860 0.4441 0.6466 -0.0172 -0.0075 0.1279  523  ALA A C   
3884  O O   . ALA A 525  ? 0.5409 0.4990 0.7056 -0.0173 -0.0088 0.1333  523  ALA A O   
3885  C CB  . ALA A 525  ? 0.4102 0.3583 0.5916 -0.0199 -0.0137 0.1243  523  ALA A CB  
3886  N N   . MET A 526  ? 0.4220 0.3820 0.5705 -0.0153 -0.0049 0.1222  524  MET A N   
3887  C CA  . MET A 526  ? 0.4754 0.4371 0.6150 -0.0132 -0.0036 0.1217  524  MET A CA  
3888  C C   . MET A 526  ? 0.4671 0.4366 0.6041 -0.0134 -0.0012 0.1306  524  MET A C   
3889  O O   . MET A 526  ? 0.4438 0.4183 0.5824 -0.0149 0.0005  0.1355  524  MET A O   
3890  C CB  . MET A 526  ? 0.5191 0.4811 0.6469 -0.0113 -0.0015 0.1137  524  MET A CB  
3891  C CG  . MET A 526  ? 0.4825 0.4376 0.6113 -0.0104 -0.0039 0.1051  524  MET A CG  
3892  S SD  . MET A 526  ? 0.7814 0.7372 0.8971 -0.0084 -0.0015 0.0965  524  MET A SD  
3893  C CE  . MET A 526  ? 0.6381 0.5864 0.7584 -0.0081 -0.0049 0.0878  524  MET A CE  
3894  N N   . PRO A 527  ? 0.5740 0.5449 0.7071 -0.0121 -0.0011 0.1329  525  PRO A N   
3895  C CA  . PRO A 527  ? 0.5900 0.5689 0.7209 -0.0122 0.0010  0.1416  525  PRO A CA  
3896  C C   . PRO A 527  ? 0.5546 0.5410 0.6757 -0.0116 0.0051  0.1413  525  PRO A C   
3897  O O   . PRO A 527  ? 0.5433 0.5365 0.6662 -0.0127 0.0068  0.1481  525  PRO A O   
3898  C CB  . PRO A 527  ? 0.5184 0.4967 0.6456 -0.0104 0.0002  0.1418  525  PRO A CB  
3899  C CG  . PRO A 527  ? 0.5861 0.5579 0.7092 -0.0089 -0.0009 0.1319  525  PRO A CG  
3900  C CD  . PRO A 527  ? 0.5607 0.5266 0.6915 -0.0103 -0.0029 0.1278  525  PRO A CD  
3901  N N   . VAL A 528  ? 0.5268 0.5124 0.6380 -0.0097 0.0065  0.1336  526  VAL A N   
3902  C CA  . VAL A 528  ? 0.4009 0.3926 0.5032 -0.0088 0.0100  0.1319  526  VAL A CA  
3903  C C   . VAL A 528  ? 0.4027 0.3899 0.5048 -0.0091 0.0098  0.1246  526  VAL A C   
3904  O O   . VAL A 528  ? 0.4911 0.4730 0.5893 -0.0079 0.0089  0.1172  526  VAL A O   
3905  C CB  . VAL A 528  ? 0.4763 0.4715 0.5673 -0.0063 0.0119  0.1293  526  VAL A CB  
3906  C CG1 . VAL A 528  ? 0.4445 0.4452 0.5269 -0.0053 0.0152  0.1265  526  VAL A CG1 
3907  C CG2 . VAL A 528  ? 0.4726 0.4731 0.5637 -0.0060 0.0121  0.1368  526  VAL A CG2 
3908  N N   . VAL A 529  ? 0.3914 0.3809 0.4974 -0.0107 0.0107  0.1267  527  VAL A N   
3909  C CA  . VAL A 529  ? 0.3559 0.3417 0.4620 -0.0110 0.0104  0.1202  527  VAL A CA  
3910  C C   . VAL A 529  ? 0.3789 0.3665 0.4733 -0.0089 0.0128  0.1141  527  VAL A C   
3911  O O   . VAL A 529  ? 0.3897 0.3842 0.4777 -0.0079 0.0156  0.1163  527  VAL A O   
3912  C CB  . VAL A 529  ? 0.3576 0.3462 0.4703 -0.0131 0.0109  0.1242  527  VAL A CB  
3913  C CG1 . VAL A 529  ? 0.3325 0.3181 0.4441 -0.0132 0.0109  0.1174  527  VAL A CG1 
3914  C CG2 . VAL A 529  ? 0.4152 0.4008 0.5406 -0.0153 0.0080  0.1296  527  VAL A CG2 
3915  N N   . GLY A 530  ? 0.3297 0.3114 0.4217 -0.0081 0.0116  0.1064  528  GLY A N   
3916  C CA  . GLY A 530  ? 0.3380 0.3207 0.4200 -0.0064 0.0135  0.1006  528  GLY A CA  
3917  C C   . GLY A 530  ? 0.2842 0.2685 0.3579 -0.0043 0.0145  0.0991  528  GLY A C   
3918  O O   . GLY A 530  ? 0.3347 0.3213 0.4002 -0.0029 0.0164  0.0955  528  GLY A O   
3919  N N   . ALA A 531  ? 0.3409 0.3239 0.4167 -0.0041 0.0131  0.1018  529  ALA A N   
3920  C CA  . ALA A 531  ? 0.3050 0.2894 0.3730 -0.0021 0.0138  0.1003  529  ALA A CA  
3921  C C   . ALA A 531  ? 0.3020 0.2820 0.3644 -0.0009 0.0134  0.0920  529  ALA A C   
3922  O O   . ALA A 531  ? 0.3279 0.3021 0.3941 -0.0015 0.0115  0.0879  529  ALA A O   
3923  C CB  . ALA A 531  ? 0.3326 0.3157 0.4049 -0.0022 0.0119  0.1043  529  ALA A CB  
3924  N N   . LYS A 532  ? 0.2946 0.2776 0.3480 0.0009  0.0152  0.0897  530  LYS A N   
3925  C CA  . LYS A 532  ? 0.3175 0.2970 0.3652 0.0021  0.0149  0.0826  530  LYS A CA  
3926  C C   . LYS A 532  ? 0.3138 0.2879 0.3646 0.0022  0.0124  0.0806  530  LYS A C   
3927  O O   . LYS A 532  ? 0.3118 0.2859 0.3667 0.0020  0.0112  0.0848  530  LYS A O   
3928  C CB  . LYS A 532  ? 0.3488 0.3329 0.3875 0.0040  0.0169  0.0816  530  LYS A CB  
3929  C CG  . LYS A 532  ? 0.4071 0.3881 0.4399 0.0052  0.0167  0.0748  530  LYS A CG  
3930  C CD  . LYS A 532  ? 0.3524 0.3379 0.3772 0.0070  0.0184  0.0740  530  LYS A CD  
3931  C CE  . LYS A 532  ? 0.3818 0.3702 0.4065 0.0077  0.0181  0.0783  530  LYS A CE  
3932  N NZ  . LYS A 532  ? 0.3514 0.3348 0.3781 0.0078  0.0159  0.0766  530  LYS A NZ  
3933  N N   . HIS A 533  ? 0.2869 0.2567 0.3360 0.0025  0.0115  0.0742  531  HIS A N   
3934  C CA  . HIS A 533  ? 0.2850 0.2503 0.3359 0.0029  0.0093  0.0715  531  HIS A CA  
3935  C C   . HIS A 533  ? 0.3312 0.2987 0.3777 0.0043  0.0097  0.0731  531  HIS A C   
3936  O O   . HIS A 533  ? 0.3369 0.3080 0.3761 0.0055  0.0115  0.0722  531  HIS A O   
3937  C CB  . HIS A 533  ? 0.3025 0.2645 0.3504 0.0033  0.0089  0.0644  531  HIS A CB  
3938  C CG  . HIS A 533  ? 0.3532 0.3107 0.4049 0.0035  0.0064  0.0612  531  HIS A CG  
3939  N ND1 . HIS A 533  ? 0.3308 0.2877 0.3808 0.0046  0.0056  0.0609  531  HIS A ND1 
3940  C CD2 . HIS A 533  ? 0.4147 0.3684 0.4721 0.0028  0.0044  0.0580  531  HIS A CD2 
3941  C CE1 . HIS A 533  ? 0.4304 0.3833 0.4849 0.0047  0.0034  0.0576  531  HIS A CE1 
3942  N NE2 . HIS A 533  ? 0.4630 0.4139 0.5219 0.0036  0.0025  0.0557  531  HIS A NE2 
3943  N N   . ASP A 534  ? 0.3172 0.2827 0.3688 0.0043  0.0077  0.0754  532  ASP A N   
3944  C CA  . ASP A 534  ? 0.3516 0.3191 0.3998 0.0056  0.0077  0.0773  532  ASP A CA  
3945  C C   . ASP A 534  ? 0.3690 0.3359 0.4098 0.0071  0.0081  0.0715  532  ASP A C   
3946  O O   . ASP A 534  ? 0.4158 0.3861 0.4512 0.0083  0.0091  0.0725  532  ASP A O   
3947  C CB  . ASP A 534  ? 0.3566 0.3211 0.4124 0.0054  0.0051  0.0800  532  ASP A CB  
3948  C CG  . ASP A 534  ? 0.5737 0.5397 0.6367 0.0040  0.0046  0.0872  532  ASP A CG  
3949  O OD1 . ASP A 534  ? 0.6402 0.6115 0.7009 0.0036  0.0067  0.0913  532  ASP A OD1 
3950  O OD2 . ASP A 534  ? 0.7165 0.6788 0.7879 0.0033  0.0021  0.0889  532  ASP A OD2 
3951  N N   . ARG A 535  ? 0.3042 0.2672 0.3450 0.0070  0.0073  0.0657  533  ARG A N   
3952  C CA  . ARG A 535  ? 0.3093 0.2713 0.3444 0.0081  0.0074  0.0604  533  ARG A CA  
3953  C C   . ARG A 535  ? 0.3454 0.3091 0.3736 0.0084  0.0093  0.0570  533  ARG A C   
3954  O O   . ARG A 535  ? 0.3604 0.3231 0.3845 0.0091  0.0093  0.0524  533  ARG A O   
3955  C CB  . ARG A 535  ? 0.3870 0.3443 0.4263 0.0080  0.0052  0.0561  533  ARG A CB  
3956  N N   . ILE A 536  ? 0.2993 0.2657 0.3267 0.0079  0.0110  0.0592  534  ILE A N   
3957  C CA  . ILE A 536  ? 0.3192 0.2874 0.3406 0.0082  0.0127  0.0561  534  ILE A CA  
3958  C C   . ILE A 536  ? 0.3355 0.3091 0.3526 0.0091  0.0145  0.0593  534  ILE A C   
3959  O O   . ILE A 536  ? 0.3363 0.3128 0.3559 0.0087  0.0152  0.0642  534  ILE A O   
3960  C CB  . ILE A 536  ? 0.2971 0.2639 0.3210 0.0071  0.0130  0.0549  534  ILE A CB  
3961  C CG1 . ILE A 536  ? 0.3912 0.3535 0.4189 0.0064  0.0111  0.0510  534  ILE A CG1 
3962  C CG2 . ILE A 536  ? 0.3232 0.2922 0.3413 0.0075  0.0148  0.0524  534  ILE A CG2 
3963  C CD1 . ILE A 536  ? 0.3603 0.3214 0.3908 0.0053  0.0110  0.0498  534  ILE A CD1 
3964  N N   . ALA A 537  ? 0.2793 0.2544 0.2901 0.0104  0.0152  0.0566  535  ALA A N   
3965  C CA  . ALA A 537  ? 0.2935 0.2742 0.2999 0.0116  0.0168  0.0589  535  ALA A CA  
3966  C C   . ALA A 537  ? 0.2754 0.2586 0.2795 0.0116  0.0186  0.0581  535  ALA A C   
3967  O O   . ALA A 537  ? 0.2849 0.2656 0.2876 0.0114  0.0186  0.0539  535  ALA A O   
3968  C CB  . ALA A 537  ? 0.3079 0.2895 0.3088 0.0130  0.0167  0.0560  535  ALA A CB  
3969  N N   . LEU A 538  ? 0.2639 0.2524 0.2680 0.0119  0.0199  0.0622  536  LEU A N   
3970  C CA  . LEU A 538  ? 0.2666 0.2585 0.2675 0.0125  0.0217  0.0610  536  LEU A CA  
3971  C C   . LEU A 538  ? 0.3027 0.2955 0.2974 0.0141  0.0220  0.0565  536  LEU A C   
3972  O O   . LEU A 538  ? 0.2857 0.2788 0.2780 0.0149  0.0213  0.0559  536  LEU A O   
3973  C CB  . LEU A 538  ? 0.2675 0.2663 0.2688 0.0128  0.0232  0.0662  536  LEU A CB  
3974  C CG  . LEU A 538  ? 0.2942 0.2931 0.3020 0.0111  0.0232  0.0712  536  LEU A CG  
3975  C CD1 . LEU A 538  ? 0.3786 0.3852 0.3864 0.0116  0.0247  0.0768  536  LEU A CD1 
3976  C CD2 . LEU A 538  ? 0.2931 0.2900 0.3027 0.0102  0.0236  0.0689  536  LEU A CD2 
3977  N N   . PRO A 539  ? 0.2624 0.2554 0.2546 0.0145  0.0228  0.0531  537  PRO A N   
3978  C CA  . PRO A 539  ? 0.2556 0.2489 0.2427 0.0159  0.0228  0.0486  537  PRO A CA  
3979  C C   . PRO A 539  ? 0.2500 0.2489 0.2333 0.0177  0.0233  0.0497  537  PRO A C   
3980  O O   . PRO A 539  ? 0.2660 0.2640 0.2463 0.0185  0.0225  0.0469  537  PRO A O   
3981  C CB  . PRO A 539  ? 0.2590 0.2527 0.2452 0.0160  0.0237  0.0461  537  PRO A CB  
3982  C CG  . PRO A 539  ? 0.2609 0.2514 0.2520 0.0142  0.0235  0.0477  537  PRO A CG  
3983  C CD  . PRO A 539  ? 0.2568 0.2491 0.2515 0.0135  0.0235  0.0529  537  PRO A CD  
3984  N N   . ALA A 540  ? 0.2663 0.2713 0.2498 0.0182  0.0246  0.0538  538  ALA A N   
3985  C CA  . ALA A 540  ? 0.2773 0.2886 0.2571 0.0200  0.0251  0.0551  538  ALA A CA  
3986  C C   . ALA A 540  ? 0.3398 0.3498 0.3198 0.0199  0.0238  0.0568  538  ALA A C   
3987  O O   . ALA A 540  ? 0.3336 0.3477 0.3098 0.0215  0.0238  0.0564  538  ALA A O   
3988  C CB  . ALA A 540  ? 0.3149 0.3335 0.2954 0.0203  0.0268  0.0599  538  ALA A CB  
3989  N N   . GLU A 541  ? 0.2870 0.2918 0.2715 0.0182  0.0226  0.0586  539  GLU A N   
3990  C CA  . GLU A 541  ? 0.3209 0.3247 0.3067 0.0182  0.0213  0.0609  539  GLU A CA  
3991  C C   . GLU A 541  ? 0.2980 0.2955 0.2837 0.0178  0.0197  0.0566  539  GLU A C   
3992  O O   . GLU A 541  ? 0.3004 0.2956 0.2884 0.0175  0.0183  0.0581  539  GLU A O   
3993  C CB  . GLU A 541  ? 0.3593 0.3627 0.3511 0.0167  0.0210  0.0667  539  GLU A CB  
3994  C CG  . GLU A 541  ? 0.4129 0.4232 0.4051 0.0169  0.0227  0.0716  539  GLU A CG  
3995  C CD  . GLU A 541  ? 0.5436 0.5538 0.5422 0.0153  0.0222  0.0780  539  GLU A CD  
3996  O OE1 . GLU A 541  ? 0.6824 0.6899 0.6840 0.0149  0.0206  0.0800  539  GLU A OE1 
3997  O OE2 . GLU A 541  ? 0.6355 0.6486 0.6366 0.0145  0.0234  0.0810  539  GLU A OE2 
3998  N N   . LEU A 542  ? 0.2810 0.2761 0.2641 0.0180  0.0197  0.0514  540  LEU A N   
3999  C CA  . LEU A 542  ? 0.3142 0.3039 0.2973 0.0176  0.0183  0.0473  540  LEU A CA  
4000  C C   . LEU A 542  ? 0.3180 0.3085 0.2991 0.0186  0.0173  0.0471  540  LEU A C   
4001  O O   . LEU A 542  ? 0.3408 0.3273 0.3236 0.0180  0.0159  0.0457  540  LEU A O   
4002  C CB  . LEU A 542  ? 0.3200 0.3083 0.3001 0.0179  0.0186  0.0423  540  LEU A CB  
4003  C CG  . LEU A 542  ? 0.4039 0.3884 0.3863 0.0165  0.0188  0.0406  540  LEU A CG  
4004  C CD1 . LEU A 542  ? 0.2908 0.2734 0.2703 0.0168  0.0185  0.0356  540  LEU A CD1 
4005  C CD2 . LEU A 542  ? 0.3387 0.3188 0.3257 0.0150  0.0177  0.0415  540  LEU A CD2 
4006  N N   . PHE A 543  ? 0.2786 0.2747 0.2562 0.0201  0.0179  0.0483  541  PHE A N   
4007  C CA  . PHE A 543  ? 0.2966 0.2941 0.2721 0.0212  0.0169  0.0478  541  PHE A CA  
4008  C C   . PHE A 543  ? 0.3200 0.3208 0.2973 0.0214  0.0166  0.0535  541  PHE A C   
4009  O O   . PHE A 543  ? 0.3294 0.3325 0.3047 0.0225  0.0159  0.0539  541  PHE A O   
4010  C CB  . PHE A 543  ? 0.3253 0.3268 0.2954 0.0229  0.0173  0.0444  541  PHE A CB  
4011  C CG  . PHE A 543  ? 0.3094 0.3078 0.2783 0.0226  0.0175  0.0394  541  PHE A CG  
4012  C CD1 . PHE A 543  ? 0.3462 0.3388 0.3165 0.0215  0.0164  0.0364  541  PHE A CD1 
4013  C CD2 . PHE A 543  ? 0.2885 0.2901 0.2552 0.0234  0.0187  0.0379  541  PHE A CD2 
4014  C CE1 . PHE A 543  ? 0.3310 0.3209 0.3007 0.0211  0.0165  0.0324  541  PHE A CE1 
4015  C CE2 . PHE A 543  ? 0.2807 0.2791 0.2470 0.0231  0.0186  0.0336  541  PHE A CE2 
4016  C CZ  . PHE A 543  ? 0.3202 0.3128 0.2879 0.0218  0.0175  0.0311  541  PHE A CZ  
4017  N N   . GLY A 544  ? 0.2788 0.2799 0.2601 0.0204  0.0171  0.0580  542  GLY A N   
4018  C CA  . GLY A 544  ? 0.3130 0.3166 0.2971 0.0204  0.0166  0.0639  542  GLY A CA  
4019  C C   . GLY A 544  ? 0.3013 0.3128 0.2811 0.0221  0.0174  0.0662  542  GLY A C   
4020  O O   . GLY A 544  ? 0.3146 0.3313 0.2908 0.0231  0.0189  0.0654  542  GLY A O   
4021  N N   . ASP A 545  ? 0.3468 0.3596 0.3270 0.0227  0.0162  0.0688  543  ASP A N   
4022  C CA  . ASP A 545  ? 0.3850 0.4060 0.3616 0.0243  0.0167  0.0718  543  ASP A CA  
4023  C C   . ASP A 545  ? 0.3666 0.3904 0.3368 0.0261  0.0168  0.0664  543  ASP A C   
4024  O O   . ASP A 545  ? 0.4209 0.4523 0.3872 0.0278  0.0174  0.0679  543  ASP A O   
4025  C CB  . ASP A 545  ? 0.4159 0.4372 0.3955 0.0243  0.0152  0.0767  543  ASP A CB  
4026  C CG  . ASP A 545  ? 0.5949 0.6145 0.5813 0.0226  0.0149  0.0828  543  ASP A CG  
4027  O OD1 . ASP A 545  ? 0.6235 0.6449 0.6112 0.0218  0.0163  0.0849  543  ASP A OD1 
4028  O OD2 . ASP A 545  ? 0.8245 0.8409 0.8154 0.0221  0.0131  0.0856  543  ASP A OD2 
4029  N N   . ALA A 546  ? 0.3323 0.3505 0.3014 0.0259  0.0161  0.0603  544  ALA A N   
4030  C CA  . ALA A 546  ? 0.3333 0.3536 0.2972 0.0275  0.0159  0.0551  544  ALA A CA  
4031  C C   . ALA A 546  ? 0.3919 0.4179 0.3520 0.0287  0.0175  0.0534  544  ALA A C   
4032  O O   . ALA A 546  ? 0.3833 0.4157 0.3392 0.0306  0.0177  0.0524  544  ALA A O   
4033  C CB  . ALA A 546  ? 0.3325 0.3456 0.2969 0.0267  0.0149  0.0495  544  ALA A CB  
4034  N N   . ARG A 547  ? 0.3220 0.3460 0.2837 0.0278  0.0187  0.0528  545  ARG A N   
4035  C CA  . ARG A 547  ? 0.3168 0.3460 0.2754 0.0290  0.0201  0.0509  545  ARG A CA  
4036  C C   . ARG A 547  ? 0.2582 0.2846 0.2200 0.0276  0.0213  0.0519  545  ARG A C   
4037  O O   . ARG A 547  ? 0.3189 0.3387 0.2847 0.0257  0.0207  0.0527  545  ARG A O   
4038  C CB  . ARG A 547  ? 0.3871 0.4156 0.3421 0.0303  0.0196  0.0440  545  ARG A CB  
4039  C CG  . ARG A 547  ? 0.3605 0.3807 0.3175 0.0288  0.0188  0.0400  545  ARG A CG  
4040  C CD  . ARG A 547  ? 0.4054 0.4249 0.3595 0.0299  0.0179  0.0339  545  ARG A CD  
4041  N NE  . ARG A 547  ? 0.3675 0.3793 0.3237 0.0283  0.0167  0.0312  545  ARG A NE  
4042  C CZ  . ARG A 547  ? 0.3233 0.3305 0.2809 0.0273  0.0169  0.0284  545  ARG A CZ  
4043  N NH1 . ARG A 547  ? 0.3243 0.3335 0.2815 0.0278  0.0180  0.0274  545  ARG A NH1 
4044  N NH2 . ARG A 547  ? 0.3352 0.3362 0.2947 0.0259  0.0159  0.0266  545  ARG A NH2 
4045  N N   . THR A 548  ? 0.2696 0.3016 0.2295 0.0286  0.0228  0.0517  546  THR A N   
4046  C CA  . THR A 548  ? 0.2578 0.2884 0.2205 0.0275  0.0240  0.0524  546  THR A CA  
4047  C C   . THR A 548  ? 0.2724 0.2981 0.2344 0.0275  0.0237  0.0463  546  THR A C   
4048  O O   . THR A 548  ? 0.2801 0.3080 0.2385 0.0292  0.0236  0.0418  546  THR A O   
4049  C CB  . THR A 548  ? 0.3127 0.3523 0.2738 0.0288  0.0259  0.0552  546  THR A CB  
4050  O OG1 . THR A 548  ? 0.3685 0.4134 0.3303 0.0288  0.0261  0.0615  546  THR A OG1 
4051  C CG2 . THR A 548  ? 0.3105 0.3488 0.2747 0.0276  0.0271  0.0562  546  THR A CG2 
4052  N N   . ASN A 549  ? 0.2602 0.2791 0.2257 0.0255  0.0235  0.0460  547  ASN A N   
4053  C CA  . ASN A 549  ? 0.2406 0.2549 0.2059 0.0253  0.0232  0.0409  547  ASN A CA  
4054  C C   . ASN A 549  ? 0.2733 0.2925 0.2371 0.0266  0.0246  0.0393  547  ASN A C   
4055  O O   . ASN A 549  ? 0.2882 0.3125 0.2527 0.0269  0.0260  0.0430  547  ASN A O   
4056  C CB  . ASN A 549  ? 0.2528 0.2601 0.2224 0.0230  0.0227  0.0415  547  ASN A CB  
4057  C CG  . ASN A 549  ? 0.2420 0.2439 0.2114 0.0225  0.0220  0.0365  547  ASN A CG  
4058  O OD1 . ASN A 549  ? 0.2652 0.2677 0.2319 0.0237  0.0216  0.0324  547  ASN A OD1 
4059  N ND2 . ASN A 549  ? 0.2538 0.2508 0.2267 0.0207  0.0218  0.0369  547  ASN A ND2 
4060  N N   . SER A 550  ? 0.2509 0.2687 0.2128 0.0276  0.0241  0.0339  548  SER A N   
4061  C CA  . SER A 550  ? 0.2442 0.2654 0.2056 0.0287  0.0251  0.0319  548  SER A CA  
4062  C C   . SER A 550  ? 0.2818 0.2997 0.2469 0.0270  0.0259  0.0338  548  SER A C   
4063  O O   . SER A 550  ? 0.2826 0.2941 0.2503 0.0250  0.0251  0.0347  548  SER A O   
4064  C CB  . SER A 550  ? 0.2512 0.2703 0.2109 0.0299  0.0241  0.0257  548  SER A CB  
4065  O OG  . SER A 550  ? 0.2696 0.2806 0.2314 0.0280  0.0229  0.0239  548  SER A OG  
4066  N N   . ALA A 551  ? 0.2656 0.2883 0.2308 0.0279  0.0273  0.0342  549  ALA A N   
4067  C CA  . ALA A 551  ? 0.2849 0.3053 0.2536 0.0265  0.0280  0.0358  549  ALA A CA  
4068  C C   . ALA A 551  ? 0.2747 0.2929 0.2434 0.0272  0.0278  0.0310  549  ALA A C   
4069  O O   . ALA A 551  ? 0.2790 0.3009 0.2453 0.0293  0.0278  0.0274  549  ALA A O   
4070  C CB  . ALA A 551  ? 0.2838 0.3113 0.2534 0.0269  0.0299  0.0403  549  ALA A CB  
4071  N N   . GLY A 552  ? 0.2684 0.2807 0.2401 0.0254  0.0273  0.0308  550  GLY A N   
4072  C CA  . GLY A 552  ? 0.2801 0.2901 0.2526 0.0257  0.0271  0.0271  550  GLY A CA  
4073  C C   . GLY A 552  ? 0.2535 0.2667 0.2280 0.0258  0.0285  0.0289  550  GLY A C   
4074  O O   . GLY A 552  ? 0.2936 0.3126 0.2684 0.0261  0.0299  0.0325  550  GLY A O   
4075  N N   . LEU A 553  ? 0.2745 0.2843 0.2508 0.0255  0.0281  0.0265  551  LEU A N   
4076  C CA  . LEU A 553  ? 0.2735 0.2858 0.2522 0.0256  0.0292  0.0277  551  LEU A CA  
4077  C C   . LEU A 553  ? 0.2729 0.2787 0.2547 0.0235  0.0284  0.0276  551  LEU A C   
4078  O O   . LEU A 553  ? 0.3143 0.3147 0.2958 0.0229  0.0269  0.0249  551  LEU A O   
4079  C CB  . LEU A 553  ? 0.3054 0.3220 0.2830 0.0281  0.0296  0.0239  551  LEU A CB  
4080  C CG  . LEU A 553  ? 0.2923 0.3171 0.2668 0.0305  0.0306  0.0236  551  LEU A CG  
4081  C CD1 . LEU A 553  ? 0.3448 0.3728 0.3186 0.0332  0.0305  0.0187  551  LEU A CD1 
4082  C CD2 . LEU A 553  ? 0.3056 0.3367 0.2808 0.0302  0.0326  0.0288  551  LEU A CD2 
4083  N N   . ASP A 554  ? 0.2471 0.2537 0.2318 0.0223  0.0293  0.0307  552  ASP A N   
4084  C CA  . ASP A 554  ? 0.2783 0.2793 0.2660 0.0204  0.0285  0.0309  552  ASP A CA  
4085  C C   . ASP A 554  ? 0.2744 0.2758 0.2633 0.0213  0.0285  0.0283  552  ASP A C   
4086  O O   . ASP A 554  ? 0.2578 0.2634 0.2483 0.0218  0.0297  0.0297  552  ASP A O   
4087  C CB  . ASP A 554  ? 0.2595 0.2610 0.2505 0.0186  0.0291  0.0353  552  ASP A CB  
4088  C CG  . ASP A 554  ? 0.2912 0.2874 0.2852 0.0166  0.0281  0.0353  552  ASP A CG  
4089  O OD1 . ASP A 554  ? 0.3103 0.3025 0.3037 0.0165  0.0270  0.0321  552  ASP A OD1 
4090  O OD2 . ASP A 554  ? 0.3039 0.2998 0.3010 0.0150  0.0283  0.0384  552  ASP A OD2 
4091  N N   . LEU A 555  ? 0.2644 0.2614 0.2528 0.0214  0.0271  0.0248  553  LEU A N   
4092  C CA  . LEU A 555  ? 0.2619 0.2588 0.2517 0.0224  0.0268  0.0224  553  LEU A CA  
4093  C C   . LEU A 555  ? 0.2723 0.2665 0.2655 0.0206  0.0266  0.0239  553  LEU A C   
4094  O O   . LEU A 555  ? 0.2910 0.2841 0.2857 0.0211  0.0260  0.0221  553  LEU A O   
4095  C CB  . LEU A 555  ? 0.2508 0.2443 0.2395 0.0232  0.0252  0.0184  553  LEU A CB  
4096  C CG  . LEU A 555  ? 0.3029 0.2993 0.2886 0.0251  0.0252  0.0161  553  LEU A CG  
4097  C CD1 . LEU A 555  ? 0.3122 0.3049 0.2976 0.0257  0.0233  0.0122  553  LEU A CD1 
4098  C CD2 . LEU A 555  ? 0.3305 0.3340 0.3157 0.0275  0.0266  0.0157  553  LEU A CD2 
4099  N N   . SER A 556  ? 0.2574 0.2503 0.2519 0.0187  0.0268  0.0271  554  SER A N   
4100  C CA  . SER A 556  ? 0.2616 0.2532 0.2594 0.0171  0.0267  0.0288  554  SER A CA  
4101  C C   . SER A 556  ? 0.2777 0.2744 0.2776 0.0172  0.0283  0.0319  554  SER A C   
4102  O O   . SER A 556  ? 0.2702 0.2665 0.2733 0.0160  0.0284  0.0334  554  SER A O   
4103  C CB  . SER A 556  ? 0.2867 0.2736 0.2855 0.0149  0.0256  0.0298  554  SER A CB  
4104  O OG  . SER A 556  ? 0.2958 0.2840 0.2952 0.0140  0.0262  0.0327  554  SER A OG  
4105  N N   . ASN A 557  ? 0.2662 0.2680 0.2645 0.0185  0.0296  0.0330  555  ASN A N   
4106  C CA  . ASN A 557  ? 0.2495 0.2569 0.2497 0.0185  0.0313  0.0365  555  ASN A CA  
4107  C C   . ASN A 557  ? 0.2652 0.2777 0.2654 0.0206  0.0324  0.0350  555  ASN A C   
4108  O O   . ASN A 557  ? 0.2490 0.2643 0.2464 0.0228  0.0326  0.0323  555  ASN A O   
4109  C CB  . ASN A 557  ? 0.2534 0.2640 0.2518 0.0187  0.0320  0.0390  555  ASN A CB  
4110  C CG  . ASN A 557  ? 0.2598 0.2767 0.2604 0.0185  0.0337  0.0435  555  ASN A CG  
4111  O OD1 . ASN A 557  ? 0.2940 0.3164 0.2951 0.0198  0.0350  0.0435  555  ASN A OD1 
4112  N ND2 . ASN A 557  ? 0.2836 0.3000 0.2858 0.0168  0.0337  0.0474  555  ASN A ND2 
4113  N N   . GLU A 558  ? 0.2753 0.2894 0.2790 0.0200  0.0329  0.0364  556  GLU A N   
4114  C CA  . GLU A 558  ? 0.2825 0.3015 0.2868 0.0220  0.0338  0.0347  556  GLU A CA  
4115  C C   . GLU A 558  ? 0.2664 0.2937 0.2689 0.0240  0.0357  0.0357  556  GLU A C   
4116  O O   . GLU A 558  ? 0.2929 0.3241 0.2942 0.0265  0.0362  0.0326  556  GLU A O   
4117  C CB  . GLU A 558  ? 0.3097 0.3292 0.3183 0.0209  0.0341  0.0365  556  GLU A CB  
4118  C CG  . GLU A 558  ? 0.3003 0.3130 0.3108 0.0195  0.0323  0.0349  556  GLU A CG  
4119  C CD  . GLU A 558  ? 0.2904 0.3002 0.2995 0.0211  0.0311  0.0305  556  GLU A CD  
4120  O OE1 . GLU A 558  ? 0.2900 0.3032 0.2974 0.0235  0.0315  0.0279  556  GLU A OE1 
4121  O OE2 . GLU A 558  ? 0.2879 0.2922 0.2979 0.0198  0.0295  0.0295  556  GLU A OE2 
4122  N N   . GLU A 559  ? 0.2472 0.2776 0.2498 0.0230  0.0367  0.0399  557  GLU A N   
4123  C CA  . GLU A 559  ? 0.2815 0.3204 0.2819 0.0249  0.0385  0.0411  557  GLU A CA  
4124  C C   . GLU A 559  ? 0.2610 0.3000 0.2568 0.0270  0.0379  0.0372  557  GLU A C   
4125  O O   . GLU A 559  ? 0.2742 0.3195 0.2680 0.0297  0.0387  0.0348  557  GLU A O   
4126  C CB  . GLU A 559  ? 0.3298 0.3716 0.3314 0.0232  0.0394  0.0469  557  GLU A CB  
4127  C CG  . GLU A 559  ? 0.3220 0.3649 0.3288 0.0211  0.0400  0.0513  557  GLU A CG  
4128  C CD  . GLU A 559  ? 0.4382 0.4826 0.4468 0.0192  0.0405  0.0571  557  GLU A CD  
4129  O OE1 . GLU A 559  ? 0.5357 0.5813 0.5412 0.0197  0.0405  0.0578  557  GLU A OE1 
4130  O OE2 . GLU A 559  ? 0.4417 0.4860 0.4551 0.0171  0.0406  0.0609  557  GLU A OE2 
4131  N N   . THR A 560  ? 0.2766 0.3089 0.2709 0.0259  0.0363  0.0364  558  THR A N   
4132  C CA  . THR A 560  ? 0.2834 0.3151 0.2737 0.0276  0.0355  0.0326  558  THR A CA  
4133  C C   . THR A 560  ? 0.2596 0.2902 0.2497 0.0296  0.0346  0.0272  558  THR A C   
4134  O O   . THR A 560  ? 0.3066 0.3415 0.2942 0.0322  0.0348  0.0239  558  THR A O   
4135  C CB  . THR A 560  ? 0.2932 0.3175 0.2826 0.0258  0.0339  0.0327  558  THR A CB  
4136  O OG1 . THR A 560  ? 0.2889 0.3140 0.2793 0.0240  0.0344  0.0377  558  THR A OG1 
4137  C CG2 . THR A 560  ? 0.3316 0.3556 0.3171 0.0275  0.0330  0.0290  558  THR A CG2 
4138  N N   . LEU A 561  ? 0.2452 0.2704 0.2381 0.0285  0.0336  0.0261  559  LEU A N   
4139  C CA  . LEU A 561  ? 0.2316 0.2553 0.2248 0.0303  0.0326  0.0213  559  LEU A CA  
4140  C C   . LEU A 561  ? 0.2616 0.2932 0.2553 0.0330  0.0340  0.0199  559  LEU A C   
4141  O O   . LEU A 561  ? 0.2778 0.3110 0.2707 0.0355  0.0333  0.0153  559  LEU A O   
4142  C CB  . LEU A 561  ? 0.2395 0.2565 0.2358 0.0285  0.0313  0.0212  559  LEU A CB  
4143  C CG  . LEU A 561  ? 0.2437 0.2532 0.2394 0.0263  0.0297  0.0215  559  LEU A CG  
4144  C CD1 . LEU A 561  ? 0.2813 0.2855 0.2801 0.0245  0.0286  0.0220  559  LEU A CD1 
4145  C CD2 . LEU A 561  ? 0.2497 0.2566 0.2429 0.0276  0.0283  0.0175  559  LEU A CD2 
4146  N N   . ALA A 562  ? 0.2467 0.2837 0.2421 0.0325  0.0358  0.0237  560  ALA A N   
4147  C CA  . ALA A 562  ? 0.2651 0.3104 0.2612 0.0350  0.0373  0.0224  560  ALA A CA  
4148  C C   . ALA A 562  ? 0.2922 0.3452 0.2847 0.0375  0.0383  0.0211  560  ALA A C   
4149  O O   . ALA A 562  ? 0.2965 0.3543 0.2883 0.0405  0.0384  0.0169  560  ALA A O   
4150  C CB  . ALA A 562  ? 0.3055 0.3549 0.3048 0.0336  0.0390  0.0271  560  ALA A CB  
4151  N N   . SER A 563  ? 0.2967 0.3512 0.2869 0.0364  0.0389  0.0246  561  SER A N   
4152  C CA  A SER A 563  ? 0.3032 0.3650 0.2896 0.0387  0.0397  0.0236  561  SER A CA  
4153  C CA  B SER A 563  ? 0.3031 0.3649 0.2894 0.0387  0.0397  0.0235  561  SER A CA  
4154  C C   . SER A 563  ? 0.2769 0.3352 0.2608 0.0405  0.0378  0.0177  561  SER A C   
4155  O O   . SER A 563  ? 0.3156 0.3801 0.2974 0.0435  0.0380  0.0138  561  SER A O   
4156  C CB  A SER A 563  ? 0.3322 0.3954 0.3171 0.0368  0.0405  0.0291  561  SER A CB  
4157  C CB  B SER A 563  ? 0.3336 0.3976 0.3185 0.0370  0.0407  0.0291  561  SER A CB  
4158  O OG  A SER A 563  ? 0.3404 0.4102 0.3212 0.0390  0.0410  0.0280  561  SER A OG  
4159  O OG  B SER A 563  ? 0.3530 0.4081 0.3375 0.0348  0.0390  0.0297  561  SER A OG  
4160  N N   . LEU A 564  ? 0.3001 0.3486 0.2843 0.0386  0.0359  0.0168  562  LEU A N   
4161  C CA  A LEU A 564  ? 0.2954 0.3400 0.2780 0.0400  0.0339  0.0115  562  LEU A CA  
4162  C CA  B LEU A 564  ? 0.2956 0.3401 0.2782 0.0400  0.0339  0.0115  562  LEU A CA  
4163  C C   . LEU A 564  ? 0.2970 0.3422 0.2814 0.0424  0.0331  0.0062  562  LEU A C   
4164  O O   . LEU A 564  ? 0.3109 0.3584 0.2939 0.0450  0.0322  0.0013  562  LEU A O   
4165  C CB  A LEU A 564  ? 0.2947 0.3291 0.2777 0.0373  0.0321  0.0121  562  LEU A CB  
4166  C CB  B LEU A 564  ? 0.2949 0.3292 0.2781 0.0373  0.0321  0.0121  562  LEU A CB  
4167  C CG  A LEU A 564  ? 0.3052 0.3355 0.2864 0.0380  0.0301  0.0080  562  LEU A CG  
4168  C CG  B LEU A 564  ? 0.3269 0.3593 0.3071 0.0364  0.0315  0.0131  562  LEU A CG  
4169  C CD1 A LEU A 564  ? 0.3425 0.3787 0.3197 0.0394  0.0307  0.0079  562  LEU A CD1 
4170  C CD1 B LEU A 564  ? 0.2777 0.3004 0.2590 0.0339  0.0297  0.0130  562  LEU A CD1 
4171  C CD2 A LEU A 564  ? 0.2900 0.3113 0.2719 0.0350  0.0287  0.0095  562  LEU A CD2 
4172  C CD2 B LEU A 564  ? 0.3413 0.3776 0.3185 0.0392  0.0309  0.0086  562  LEU A CD2 
4173  N N   . THR A 565  ? 0.2749 0.3181 0.2629 0.0417  0.0332  0.0069  563  THR A N   
4174  C CA  . THR A 565  ? 0.2956 0.3396 0.2861 0.0441  0.0323  0.0021  563  THR A CA  
4175  C C   . THR A 565  ? 0.2724 0.3266 0.2613 0.0477  0.0335  -0.0010 563  THR A C   
4176  O O   . THR A 565  ? 0.2996 0.3544 0.2886 0.0504  0.0321  -0.0067 563  THR A O   
4177  C CB  . THR A 565  ? 0.2944 0.3368 0.2888 0.0429  0.0328  0.0042  563  THR A CB  
4178  O OG1 . THR A 565  ? 0.2817 0.3147 0.2777 0.0399  0.0313  0.0060  563  THR A OG1 
4179  C CG2 . THR A 565  ? 0.3243 0.3689 0.3215 0.0457  0.0321  -0.0006 563  THR A CG2 
4180  N N   . GLU A 566  ? 0.2911 0.3537 0.2786 0.0479  0.0360  0.0028  564  GLU A N   
4181  C CA  . GLU A 566  ? 0.2934 0.3670 0.2792 0.0514  0.0373  0.0002  564  GLU A CA  
4182  C C   . GLU A 566  ? 0.2939 0.3701 0.2757 0.0532  0.0366  -0.0029 564  GLU A C   
4183  O O   . GLU A 566  ? 0.3334 0.4147 0.3144 0.0566  0.0361  -0.0085 564  GLU A O   
4184  C CB  . GLU A 566  ? 0.3520 0.4343 0.3376 0.0508  0.0402  0.0059  564  GLU A CB  
4185  C CG  . GLU A 566  ? 0.4111 0.4915 0.4011 0.0492  0.0409  0.0086  564  GLU A CG  
4186  C CD  . GLU A 566  ? 0.5587 0.6395 0.5516 0.0517  0.0400  0.0032  564  GLU A CD  
4187  O OE1 . GLU A 566  ? 0.5915 0.6797 0.5834 0.0553  0.0403  -0.0014 564  GLU A OE1 
4188  O OE2 . GLU A 566  ? 0.5271 0.6008 0.5236 0.0502  0.0389  0.0034  564  GLU A OE2 
4189  N N   . ALA A 567  ? 0.2929 0.3654 0.2721 0.0509  0.0364  0.0004  565  ALA A N   
4190  C CA  . ALA A 567  ? 0.3010 0.3757 0.2765 0.0525  0.0355  -0.0024 565  ALA A CA  
4191  C C   . ALA A 567  ? 0.2501 0.3183 0.2266 0.0538  0.0327  -0.0090 565  ALA A C   
4192  O O   . ALA A 567  ? 0.3269 0.3995 0.3016 0.0567  0.0319  -0.0141 565  ALA A O   
4193  C CB  . ALA A 567  ? 0.3076 0.3790 0.2808 0.0497  0.0357  0.0027  565  ALA A CB  
4194  N N   . LEU A 568  ? 0.2779 0.3359 0.2575 0.0516  0.0311  -0.0090 566  LEU A N   
4195  C CA  . LEU A 568  ? 0.2532 0.3048 0.2347 0.0525  0.0284  -0.0147 566  LEU A CA  
4196  C C   . LEU A 568  ? 0.2784 0.3345 0.2622 0.0561  0.0278  -0.0205 566  LEU A C   
4197  O O   . LEU A 568  ? 0.2936 0.3502 0.2774 0.0585  0.0260  -0.0263 566  LEU A O   
4198  C CB  . LEU A 568  ? 0.2737 0.3143 0.2581 0.0493  0.0269  -0.0127 566  LEU A CB  
4199  C CG  . LEU A 568  ? 0.2862 0.3216 0.2687 0.0460  0.0270  -0.0080 566  LEU A CG  
4200  C CD1 . LEU A 568  ? 0.2763 0.3025 0.2619 0.0431  0.0259  -0.0060 566  LEU A CD1 
4201  C CD2 . LEU A 568  ? 0.3362 0.3702 0.3160 0.0464  0.0256  -0.0105 566  LEU A CD2 
4202  N N   . ARG A 569  ? 0.2662 0.3258 0.2524 0.0566  0.0292  -0.0192 567  ARG A N   
4203  C CA  . ARG A 569  ? 0.2848 0.3496 0.2734 0.0602  0.0288  -0.0247 567  ARG A CA  
4204  C C   . ARG A 569  ? 0.3274 0.4030 0.3127 0.0638  0.0297  -0.0283 567  ARG A C   
4205  O O   . ARG A 569  ? 0.3452 0.4226 0.3316 0.0670  0.0279  -0.0351 567  ARG A O   
4206  C CB  . ARG A 569  ? 0.3267 0.3948 0.3181 0.0600  0.0306  -0.0220 567  ARG A CB  
4207  C CG  . ARG A 569  ? 0.3907 0.4488 0.3862 0.0575  0.0293  -0.0203 567  ARG A CG  
4208  C CD  . ARG A 569  ? 0.4424 0.5044 0.4405 0.0573  0.0311  -0.0173 567  ARG A CD  
4209  N NE  . ARG A 569  ? 0.4216 0.4747 0.4231 0.0544  0.0301  -0.0146 567  ARG A NE  
4210  C CZ  . ARG A 569  ? 0.5339 0.5883 0.5378 0.0533  0.0314  -0.0111 567  ARG A CZ  
4211  N NH1 . ARG A 569  ? 0.5751 0.6390 0.5785 0.0545  0.0339  -0.0095 567  ARG A NH1 
4212  N NH2 . ARG A 569  ? 0.5955 0.6417 0.6023 0.0508  0.0302  -0.0091 567  ARG A NH2 
4213  N N   . GLU A 570  ? 0.3066 0.3895 0.2878 0.0632  0.0321  -0.0238 568  GLU A N   
4214  C CA  . GLU A 570  ? 0.3026 0.3966 0.2801 0.0665  0.0330  -0.0266 568  GLU A CA  
4215  C C   . GLU A 570  ? 0.4121 0.5032 0.3878 0.0676  0.0306  -0.0314 568  GLU A C   
4216  O O   . GLU A 570  ? 0.3648 0.4626 0.3394 0.0712  0.0299  -0.0375 568  GLU A O   
4217  C CB  . GLU A 570  ? 0.3316 0.4335 0.3055 0.0652  0.0360  -0.0198 568  GLU A CB  
4218  C CG  . GLU A 570  ? 0.4872 0.5949 0.4632 0.0649  0.0385  -0.0159 568  GLU A CG  
4219  C CD  . GLU A 570  ? 0.5570 0.6702 0.5306 0.0628  0.0411  -0.0079 568  GLU A CD  
4220  O OE1 . GLU A 570  ? 0.6893 0.8007 0.6599 0.0612  0.0409  -0.0050 568  GLU A OE1 
4221  O OE2 . GLU A 570  ? 0.6988 0.8183 0.6740 0.0626  0.0433  -0.0045 568  GLU A OE2 
4222  N N   . SER A 571  ? 0.3228 0.4039 0.2981 0.0644  0.0292  -0.0291 569  SER A N   
4223  C CA  . SER A 571  ? 0.3234 0.4013 0.2974 0.0652  0.0268  -0.0334 569  SER A CA  
4224  C C   . SER A 571  ? 0.3491 0.4233 0.3271 0.0675  0.0240  -0.0411 569  SER A C   
4225  O O   . SER A 571  ? 0.3279 0.4040 0.3050 0.0698  0.0222  -0.0467 569  SER A O   
4226  C CB  . SER A 571  ? 0.2909 0.3588 0.2643 0.0612  0.0259  -0.0292 569  SER A CB  
4227  O OG  . SER A 571  ? 0.3274 0.3847 0.3052 0.0594  0.0240  -0.0300 569  SER A OG  
4228  N N   . ALA A 572  ? 0.3471 0.4160 0.3298 0.0670  0.0234  -0.0414 570  ALA A N   
4229  C CA  . ALA A 572  ? 0.3315 0.3966 0.3190 0.0691  0.0205  -0.0483 570  ALA A CA  
4230  C C   . ALA A 572  ? 0.3929 0.4682 0.3810 0.0739  0.0207  -0.0545 570  ALA A C   
4231  O O   . ALA A 572  ? 0.4418 0.5152 0.4336 0.0763  0.0180  -0.0613 570  ALA A O   
4232  C CB  . ALA A 572  ? 0.4069 0.4631 0.3994 0.0670  0.0196  -0.0464 570  ALA A CB  
4233  N N   . ALA A 573  ? 0.4065 0.4927 0.3914 0.0752  0.0237  -0.0522 571  ALA A N   
4234  C CA  . ALA A 573  ? 0.3926 0.4903 0.3773 0.0798  0.0243  -0.0578 571  ALA A CA  
4235  C C   . ALA A 573  ? 0.4860 0.5917 0.4663 0.0823  0.0240  -0.0616 571  ALA A C   
4236  O O   . ALA A 573  ? 0.4734 0.5895 0.4532 0.0865  0.0243  -0.0670 571  ALA A O   
4237  C CB  . ALA A 573  ? 0.4208 0.5276 0.4044 0.0800  0.0278  -0.0532 571  ALA A CB  
4238  N N   . MET A 574  ? 0.3836 0.4850 0.3607 0.0801  0.0234  -0.0590 572  MET A N   
4239  C CA  . MET A 574  ? 0.4794 0.5886 0.4519 0.0822  0.0233  -0.0617 572  MET A CA  
4240  C C   . MET A 574  ? 0.4514 0.5571 0.4264 0.0846  0.0196  -0.0704 572  MET A C   
4241  O O   . MET A 574  ? 0.3921 0.4863 0.3716 0.0829  0.0170  -0.0719 572  MET A O   
4242  C CB  . MET A 574  ? 0.4111 0.5178 0.3791 0.0787  0.0244  -0.0548 572  MET A CB  
4243  C CG  . MET A 574  ? 0.4171 0.5281 0.3828 0.0765  0.0280  -0.0463 572  MET A CG  
4244  S SD  . MET A 574  ? 0.4700 0.5773 0.4315 0.0725  0.0289  -0.0383 572  MET A SD  
4245  C CE  . MET A 574  ? 0.6030 0.7205 0.5593 0.0757  0.0284  -0.0424 572  MET A CE  
4246  N N   . LYS A 575  ? 0.4176 0.5338 0.3899 0.0884  0.0193  -0.0759 573  LYS A N   
4247  C CA  . LYS A 575  ? 0.4774 0.5919 0.4521 0.0912  0.0157  -0.0849 573  LYS A CA  
4248  C C   . LYS A 575  ? 0.3765 0.4874 0.3480 0.0894  0.0144  -0.0838 573  LYS A C   
4249  O O   . LYS A 575  ? 0.4008 0.5202 0.3684 0.0918  0.0143  -0.0870 573  LYS A O   
4250  C CB  . LYS A 575  ? 0.4831 0.6113 0.4571 0.0966  0.0158  -0.0923 573  LYS A CB  
4251  C CG  . LYS A 575  ? 0.5714 0.7021 0.5500 0.0989  0.0162  -0.0953 573  LYS A CG  
4252  C CD  . LYS A 575  ? 0.6186 0.7362 0.6049 0.0981  0.0127  -0.0990 573  LYS A CD  
4253  C CE  . LYS A 575  ? 0.6960 0.8165 0.6873 0.1010  0.0127  -0.1029 573  LYS A CE  
4254  N NZ  . LYS A 575  ? 0.6961 0.8035 0.6951 0.0999  0.0094  -0.1053 573  LYS A NZ  
4255  N N   . TRP A 576  ? 0.3402 0.4385 0.3135 0.0851  0.0135  -0.0793 574  TRP A N   
4256  C CA  . TRP A 576  ? 0.3342 0.4276 0.3051 0.0829  0.0123  -0.0777 574  TRP A CA  
4257  C C   . TRP A 576  ? 0.3179 0.4112 0.2906 0.0857  0.0087  -0.0865 574  TRP A C   
4258  O O   . TRP A 576  ? 0.3432 0.4320 0.3219 0.0871  0.0060  -0.0925 574  TRP A O   
4259  C CB  . TRP A 576  ? 0.3097 0.3895 0.2832 0.0782  0.0116  -0.0723 574  TRP A CB  
4260  C CG  . TRP A 576  ? 0.3360 0.4148 0.3079 0.0752  0.0148  -0.0637 574  TRP A CG  
4261  C CD1 . TRP A 576  ? 0.3348 0.4087 0.3103 0.0737  0.0155  -0.0611 574  TRP A CD1 
4262  C CD2 . TRP A 576  ? 0.2724 0.3549 0.2389 0.0732  0.0174  -0.0567 574  TRP A CD2 
4263  N NE1 . TRP A 576  ? 0.2940 0.3685 0.2668 0.0710  0.0184  -0.0531 574  TRP A NE1 
4264  C CE2 . TRP A 576  ? 0.2996 0.3792 0.2671 0.0706  0.0196  -0.0503 574  TRP A CE2 
4265  C CE3 . TRP A 576  ? 0.2995 0.3876 0.2608 0.0734  0.0181  -0.0553 574  TRP A CE3 
4266  C CZ2 . TRP A 576  ? 0.3426 0.4243 0.3065 0.0682  0.0222  -0.0425 574  TRP A CZ2 
4267  C CZ3 . TRP A 576  ? 0.3366 0.4268 0.2943 0.0710  0.0207  -0.0473 574  TRP A CZ3 
4268  C CH2 . TRP A 576  ? 0.3282 0.4152 0.2874 0.0684  0.0227  -0.0411 574  TRP A CH2 
4269  N N   . THR A 577  ? 0.3256 0.4244 0.2937 0.0864  0.0085  -0.0872 575  THR A N   
4270  C CA  . THR A 577  ? 0.3014 0.4000 0.2712 0.0887  0.0050  -0.0953 575  THR A CA  
4271  C C   . THR A 577  ? 0.3416 0.4371 0.3080 0.0863  0.0044  -0.0923 575  THR A C   
4272  O O   . THR A 577  ? 0.3593 0.4564 0.3208 0.0840  0.0070  -0.0849 575  THR A O   
4273  C CB  . THR A 577  ? 0.3403 0.4528 0.3079 0.0940  0.0049  -0.1026 575  THR A CB  
4274  O OG1 . THR A 577  ? 0.3762 0.4995 0.3364 0.0944  0.0078  -0.0982 575  THR A OG1 
4275  C CG2 . THR A 577  ? 0.3905 0.5075 0.3615 0.0968  0.0057  -0.1058 575  THR A CG2 
4276  N N   . ALA A 578  ? 0.3224 0.4134 0.2918 0.0869  0.0008  -0.0983 576  ALA A N   
4277  C CA  . ALA A 578  ? 0.2903 0.3795 0.2568 0.0854  -0.0003 -0.0972 576  ALA A CA  
4278  C C   . ALA A 578  ? 0.3693 0.4640 0.3367 0.0893  -0.0034 -0.1067 576  ALA A C   
4279  O O   . ALA A 578  ? 0.3631 0.4542 0.3368 0.0910  -0.0063 -0.1136 576  ALA A O   
4280  C CB  . ALA A 578  ? 0.3134 0.3885 0.2836 0.0809  -0.0019 -0.0936 576  ALA A CB  
4281  N N   . LEU A 579  ? 0.3383 0.4420 0.3000 0.0907  -0.0028 -0.1070 577  LEU A N   
4282  C CA  . LEU A 579  ? 0.3533 0.4645 0.3148 0.0948  -0.0054 -0.1160 577  LEU A CA  
4283  C C   . LEU A 579  ? 0.2944 0.4041 0.2531 0.0932  -0.0067 -0.1150 577  LEU A C   
4284  O O   . LEU A 579  ? 0.3221 0.4291 0.2771 0.0899  -0.0047 -0.1069 577  LEU A O   
4285  C CB  . LEU A 579  ? 0.3399 0.4673 0.2962 0.0991  -0.0032 -0.1183 577  LEU A CB  
4286  C CG  . LEU A 579  ? 0.4189 0.5507 0.3763 0.1006  -0.0009 -0.1178 577  LEU A CG  
4287  C CD1 . LEU A 579  ? 0.4457 0.5948 0.3976 0.1050  0.0011  -0.1204 577  LEU A CD1 
4288  C CD2 . LEU A 579  ? 0.4563 0.5809 0.4219 0.1019  -0.0039 -0.1248 577  LEU A CD2 
4289  N N   . PRO A 580  ? 0.3190 0.4304 0.2797 0.0956  -0.0103 -0.1232 578  PRO A N   
4290  C CA  . PRO A 580  ? 0.3150 0.4281 0.2721 0.0949  -0.0114 -0.1228 578  PRO A CA  
4291  C C   . PRO A 580  ? 0.3718 0.4989 0.3205 0.0969  -0.0084 -0.1198 578  PRO A C   
4292  O O   . PRO A 580  ? 0.3974 0.5365 0.3440 0.1014  -0.0085 -0.1258 578  PRO A O   
4293  C CB  . PRO A 580  ? 0.3214 0.4346 0.2833 0.0978  -0.0159 -0.1335 578  PRO A CB  
4294  C CG  . PRO A 580  ? 0.3706 0.4786 0.3399 0.0990  -0.0176 -0.1385 578  PRO A CG  
4295  C CD  . PRO A 580  ? 0.3584 0.4709 0.3250 0.0993  -0.0136 -0.1336 578  PRO A CD  
4296  N N   . GLN A 581  ? 0.3056 0.4317 0.2496 0.0938  -0.0057 -0.1105 579  GLN A N   
4297  C CA  . GLN A 581  ? 0.3565 0.4952 0.2929 0.0951  -0.0026 -0.1059 579  GLN A CA  
4298  C C   . GLN A 581  ? 0.3636 0.5051 0.2965 0.0951  -0.0042 -0.1065 579  GLN A C   
4299  O O   . GLN A 581  ? 0.3551 0.4910 0.2863 0.0917  -0.0035 -0.0997 579  GLN A O   
4300  C CB  . GLN A 581  ? 0.3301 0.4659 0.2642 0.0916  0.0012  -0.0952 579  GLN A CB  
4301  C CG  . GLN A 581  ? 0.3184 0.4521 0.2557 0.0915  0.0029  -0.0941 579  GLN A CG  
4302  C CD  . GLN A 581  ? 0.3718 0.5197 0.3066 0.0959  0.0045  -0.0977 579  GLN A CD  
4303  O OE1 . GLN A 581  ? 0.3824 0.5426 0.3124 0.0989  0.0047  -0.1000 579  GLN A OE1 
4304  N NE2 . GLN A 581  ? 0.3908 0.5375 0.3289 0.0964  0.0056  -0.0982 579  GLN A NE2 
4305  N N   . LEU A 582  ? 0.3783 0.5287 0.3103 0.0992  -0.0064 -0.1149 580  LEU A N   
4306  C CA  . LEU A 582  ? 0.3868 0.5413 0.3154 0.0997  -0.0081 -0.1161 580  LEU A CA  
4307  C C   . LEU A 582  ? 0.3845 0.5518 0.3051 0.1006  -0.0049 -0.1099 580  LEU A C   
4308  O O   . LEU A 582  ? 0.3948 0.5692 0.3126 0.1014  -0.0017 -0.1059 580  LEU A O   
4309  C CB  . LEU A 582  ? 0.3519 0.5112 0.2830 0.1037  -0.0120 -0.1279 580  LEU A CB  
4310  C CG  . LEU A 582  ? 0.4933 0.6398 0.4316 0.1021  -0.0162 -0.1331 580  LEU A CG  
4311  C CD1 . LEU A 582  ? 0.4382 0.5726 0.3836 0.1000  -0.0166 -0.1330 580  LEU A CD1 
4312  C CD2 . LEU A 582  ? 0.4785 0.6316 0.4187 0.1063  -0.0200 -0.1445 580  LEU A CD2 
4313  N N   . ALA A 583  ? 0.3703 0.5407 0.2873 0.1004  -0.0059 -0.1089 581  ALA A N   
4314  C CA  . ALA A 583  ? 0.3739 0.5566 0.2835 0.1013  -0.0033 -0.1029 581  ALA A CA  
4315  C C   . ALA A 583  ? 0.4485 0.6475 0.3545 0.1062  -0.0023 -0.1074 581  ALA A C   
4316  O O   . ALA A 583  ? 0.5166 0.7259 0.4175 0.1067  0.0010  -0.1010 581  ALA A O   
4317  C CB  . ALA A 583  ? 0.3938 0.5780 0.3006 0.1011  -0.0053 -0.1029 581  ALA A CB  
4318  N N   . THR A 584  ? 0.3696 0.5714 0.2787 0.1098  -0.0050 -0.1183 582  THR A N   
4319  C CA  . THR A 584  ? 0.4526 0.6704 0.3588 0.1149  -0.0046 -0.1245 582  THR A CA  
4320  C C   . THR A 584  ? 0.4543 0.6736 0.3627 0.1159  -0.0024 -0.1246 582  THR A C   
4321  O O   . THR A 584  ? 0.4969 0.7298 0.4033 0.1197  -0.0015 -0.1280 582  THR A O   
4322  C CB  . THR A 584  ? 0.5128 0.7328 0.4219 0.1185  -0.0091 -0.1370 582  THR A CB  
4323  O OG1 . THR A 584  ? 0.5047 0.7095 0.4221 0.1168  -0.0118 -0.1416 582  THR A OG1 
4324  C CG2 . THR A 584  ? 0.4791 0.7013 0.3854 0.1182  -0.0112 -0.1371 582  THR A CG2 
4325  N N   . GLY A 585  ? 0.4281 0.6336 0.3412 0.1123  -0.0016 -0.1204 583  GLY A N   
4326  C CA  . GLY A 585  ? 0.3911 0.5966 0.3069 0.1130  0.0003  -0.1206 583  GLY A CA  
4327  C C   . GLY A 585  ? 0.4700 0.6603 0.3941 0.1114  -0.0022 -0.1250 583  GLY A C   
4328  O O   . GLY A 585  ? 0.4451 0.6252 0.3730 0.1098  -0.0055 -0.1281 583  GLY A O   
4329  N N   . PRO A 586  ? 0.4709 0.6597 0.3983 0.1118  -0.0008 -0.1252 584  PRO A N   
4330  C CA  . PRO A 586  ? 0.3543 0.5294 0.2899 0.1105  -0.0033 -0.1294 584  PRO A CA  
4331  C C   . PRO A 586  ? 0.4755 0.6515 0.4154 0.1141  -0.0078 -0.1416 584  PRO A C   
4332  O O   . PRO A 586  ? 0.4749 0.6644 0.4121 0.1188  -0.0084 -0.1483 584  PRO A O   
4333  C CB  . PRO A 586  ? 0.4974 0.6748 0.4345 0.1113  -0.0007 -0.1277 584  PRO A CB  
4334  C CG  . PRO A 586  ? 0.4688 0.6595 0.3985 0.1119  0.0035  -0.1207 584  PRO A CG  
4335  C CD  . PRO A 586  ? 0.4987 0.6995 0.4227 0.1138  0.0028  -0.1224 584  PRO A CD  
4336  N N   . ALA A 587  ? 0.4290 0.5908 0.3758 0.1120  -0.0111 -0.1444 585  ALA A N   
4337  C CA  . ALA A 587  ? 0.4350 0.5956 0.3874 0.1149  -0.0158 -0.1557 585  ALA A CA  
4338  C C   . ALA A 587  ? 0.4516 0.6044 0.4123 0.1155  -0.0175 -0.1605 585  ALA A C   
4339  O O   . ALA A 587  ? 0.4826 0.6269 0.4457 0.1124  -0.0157 -0.1542 585  ALA A O   
4340  C CB  . ALA A 587  ? 0.4523 0.6033 0.4069 0.1121  -0.0189 -0.1559 585  ALA A CB  
4341  N N   . ALA A 588  ? 0.4205 0.5768 0.3860 0.1197  -0.0212 -0.1717 586  ALA A N   
4342  C CA  . ALA A 588  ? 0.4462 0.5949 0.4207 0.1205  -0.0235 -0.1772 586  ALA A CA  
4343  C C   . ALA A 588  ? 0.4453 0.5770 0.4273 0.1166  -0.0269 -0.1766 586  ALA A C   
4344  O O   . ALA A 588  ? 0.4817 0.6094 0.4630 0.1145  -0.0285 -0.1755 586  ALA A O   
4345  C CB  . ALA A 588  ? 0.4676 0.6246 0.4467 0.1244  -0.0269 -0.1862 586  ALA A CB  
4346  N N   . GLY A 589  ? 0.4179 0.5399 0.4074 0.1156  -0.0280 -0.1771 587  GLY A N   
4347  C CA  . GLY A 589  ? 0.3996 0.5061 0.3971 0.1119  -0.0313 -0.1765 587  GLY A CA  
4348  C C   . GLY A 589  ? 0.4804 0.5786 0.4859 0.1116  -0.0323 -0.1772 587  GLY A C   
4349  O O   . GLY A 589  ? 0.4927 0.5975 0.4980 0.1146  -0.0307 -0.1794 587  GLY A O   
4350  N N   . GLU A 590  ? 0.4720 0.5561 0.4847 0.1079  -0.0349 -0.1753 588  GLU A N   
4351  C CA  . GLU A 590  ? 0.5122 0.5870 0.5331 0.1070  -0.0361 -0.1750 588  GLU A CA  
4352  C C   . GLU A 590  ? 0.4439 0.5166 0.4605 0.1039  -0.0314 -0.1647 588  GLU A C   
4353  O O   . GLU A 590  ? 0.4582 0.5265 0.4703 0.0997  -0.0292 -0.1560 588  GLU A O   
4354  C CB  . GLU A 590  ? 0.5230 0.5838 0.5528 0.1037  -0.0403 -0.1753 588  GLU A CB  
4355  N N   . THR A 591  ? 0.3989 0.4749 0.4170 0.1062  -0.0301 -0.1659 589  THR A N   
4356  C CA  . THR A 591  ? 0.4076 0.4833 0.4218 0.1040  -0.0257 -0.1571 589  THR A CA  
4357  C C   . THR A 591  ? 0.3910 0.4547 0.4133 0.1016  -0.0270 -0.1547 589  THR A C   
4358  O O   . THR A 591  ? 0.4466 0.5078 0.4770 0.1041  -0.0304 -0.1618 589  THR A O   
4359  C CB  . THR A 591  ? 0.3924 0.4821 0.4016 0.1082  -0.0226 -0.1593 589  THR A CB  
4360  O OG1 . THR A 591  ? 0.4040 0.5055 0.4056 0.1105  -0.0215 -0.1614 589  THR A OG1 
4361  C CG2 . THR A 591  ? 0.4117 0.5013 0.4168 0.1056  -0.0180 -0.1498 589  THR A CG2 
4362  N N   . ARG A 592  ? 0.3684 0.4250 0.3887 0.0970  -0.0245 -0.1449 590  ARG A N   
4363  C CA  . ARG A 592  ? 0.3680 0.4141 0.3950 0.0946  -0.0253 -0.1415 590  ARG A CA  
4364  C C   . ARG A 592  ? 0.3602 0.4064 0.3818 0.0918  -0.0207 -0.1319 590  ARG A C   
4365  O O   . ARG A 592  ? 0.3702 0.4223 0.3835 0.0908  -0.0172 -0.1270 590  ARG A O   
4366  C CB  . ARG A 592  ? 0.4115 0.4449 0.4448 0.0908  -0.0287 -0.1400 590  ARG A CB  
4367  C CG  . ARG A 592  ? 0.4354 0.4653 0.4629 0.0863  -0.0267 -0.1319 590  ARG A CG  
4368  C CD  . ARG A 592  ? 0.5061 0.5230 0.5399 0.0819  -0.0291 -0.1280 590  ARG A CD  
4369  N NE  . ARG A 592  ? 0.5200 0.5343 0.5485 0.0780  -0.0275 -0.1214 590  ARG A NE  
4370  C CZ  . ARG A 592  ? 0.4879 0.5005 0.5115 0.0747  -0.0240 -0.1127 590  ARG A CZ  
4371  N NH1 . ARG A 592  ? 0.4380 0.4506 0.4610 0.0745  -0.0216 -0.1090 590  ARG A NH1 
4372  N NH2 . ARG A 592  ? 0.4943 0.5050 0.5135 0.0716  -0.0229 -0.1077 590  ARG A NH2 
4373  N N   . THR A 593  ? 0.3628 0.4026 0.3896 0.0905  -0.0207 -0.1293 591  THR A N   
4374  C CA  . THR A 593  ? 0.3615 0.4008 0.3841 0.0878  -0.0167 -0.1205 591  THR A CA  
4375  C C   . THR A 593  ? 0.3933 0.4234 0.4144 0.0824  -0.0161 -0.1124 591  THR A C   
4376  O O   . THR A 593  ? 0.3827 0.4047 0.4080 0.0804  -0.0192 -0.1131 591  THR A O   
4377  C CB  . THR A 593  ? 0.4193 0.4557 0.4477 0.0886  -0.0170 -0.1207 591  THR A CB  
4378  O OG1 . THR A 593  ? 0.4225 0.4478 0.4599 0.0872  -0.0211 -0.1224 591  THR A OG1 
4379  C CG2 . THR A 593  ? 0.4345 0.4813 0.4634 0.0940  -0.0168 -0.1282 591  THR A CG2 
4380  N N   . VAL A 594  ? 0.2950 0.3267 0.3101 0.0800  -0.0121 -0.1046 592  VAL A N   
4381  C CA  . VAL A 594  ? 0.3209 0.3445 0.3346 0.0750  -0.0111 -0.0964 592  VAL A CA  
4382  C C   . VAL A 594  ? 0.3262 0.3452 0.3426 0.0733  -0.0098 -0.0916 592  VAL A C   
4383  O O   . VAL A 594  ? 0.3395 0.3648 0.3533 0.0747  -0.0071 -0.0902 592  VAL A O   
4384  C CB  . VAL A 594  ? 0.3024 0.3312 0.3074 0.0736  -0.0078 -0.0911 592  VAL A CB  
4385  C CG1 . VAL A 594  ? 0.3333 0.3539 0.3371 0.0686  -0.0066 -0.0829 592  VAL A CG1 
4386  C CG2 . VAL A 594  ? 0.3275 0.3608 0.3299 0.0753  -0.0092 -0.0958 592  VAL A CG2 
4387  N N   . LEU A 595  ? 0.3336 0.3423 0.3553 0.0702  -0.0118 -0.0889 593  LEU A N   
4388  C CA  . LEU A 595  ? 0.3101 0.3140 0.3353 0.0687  -0.0112 -0.0849 593  LEU A CA  
4389  C C   . LEU A 595  ? 0.3127 0.3119 0.3344 0.0640  -0.0090 -0.0761 593  LEU A C   
4390  O O   . LEU A 595  ? 0.3348 0.3305 0.3544 0.0614  -0.0093 -0.0735 593  LEU A O   
4391  C CB  . LEU A 595  ? 0.3258 0.3219 0.3604 0.0688  -0.0153 -0.0883 593  LEU A CB  
4392  C CG  . LEU A 595  ? 0.3959 0.3955 0.4355 0.0733  -0.0183 -0.0977 593  LEU A CG  
4393  C CD1 . LEU A 595  ? 0.4020 0.3929 0.4517 0.0730  -0.0225 -0.1001 593  LEU A CD1 
4394  C CD2 . LEU A 595  ? 0.3361 0.3452 0.3732 0.0772  -0.0161 -0.1006 593  LEU A CD2 
4395  N N   . ASN A 596  ? 0.3093 0.3087 0.3305 0.0632  -0.0067 -0.0717 594  ASN A N   
4396  C CA  . ASN A 596  ? 0.2982 0.2929 0.3170 0.0590  -0.0048 -0.0638 594  ASN A CA  
4397  C C   . ASN A 596  ? 0.3003 0.2852 0.3247 0.0561  -0.0077 -0.0621 594  ASN A C   
4398  O O   . ASN A 596  ? 0.2922 0.2731 0.3233 0.0567  -0.0100 -0.0641 594  ASN A O   
4399  C CB  . ASN A 596  ? 0.2841 0.2814 0.3025 0.0592  -0.0024 -0.0606 594  ASN A CB  
4400  C CG  . ASN A 596  ? 0.2902 0.2838 0.3059 0.0552  -0.0002 -0.0527 594  ASN A CG  
4401  O OD1 . ASN A 596  ? 0.2997 0.2869 0.3160 0.0520  -0.0012 -0.0496 594  ASN A OD1 
4402  N ND2 . ASN A 596  ? 0.3240 0.3221 0.3370 0.0553  0.0027  -0.0496 594  ASN A ND2 
4403  N N   . PRO A 597  ? 0.2995 0.2803 0.3217 0.0528  -0.0077 -0.0584 595  PRO A N   
4404  C CA  . PRO A 597  ? 0.2565 0.2286 0.2841 0.0500  -0.0104 -0.0565 595  PRO A CA  
4405  C C   . PRO A 597  ? 0.2860 0.2537 0.3167 0.0480  -0.0101 -0.0520 595  PRO A C   
4406  O O   . PRO A 597  ? 0.2862 0.2475 0.3230 0.0466  -0.0128 -0.0514 595  PRO A O   
4407  C CB  . PRO A 597  ? 0.3110 0.2816 0.3342 0.0471  -0.0096 -0.0529 595  PRO A CB  
4408  C CG  . PRO A 597  ? 0.3429 0.3202 0.3586 0.0476  -0.0060 -0.0508 595  PRO A CG  
4409  C CD  . PRO A 597  ? 0.2601 0.2444 0.2752 0.0517  -0.0054 -0.0558 595  PRO A CD  
4410  N N   . GLY A 598  ? 0.2606 0.2319 0.2877 0.0480  -0.0071 -0.0487 596  GLY A N   
4411  C CA  . GLY A 598  ? 0.2728 0.2406 0.3027 0.0464  -0.0068 -0.0446 596  GLY A CA  
4412  C C   . GLY A 598  ? 0.3012 0.2698 0.3364 0.0491  -0.0080 -0.0480 596  GLY A C   
4413  O O   . GLY A 598  ? 0.3177 0.2832 0.3560 0.0479  -0.0082 -0.0449 596  GLY A O   
4414  N N   . ASP A 599  ? 0.3035 0.2766 0.3398 0.0529  -0.0089 -0.0545 597  ASP A N   
4415  C CA  . ASP A 599  ? 0.2794 0.2542 0.3206 0.0561  -0.0101 -0.0587 597  ASP A CA  
4416  C C   . ASP A 599  ? 0.3147 0.2946 0.3566 0.0601  -0.0113 -0.0664 597  ASP A C   
4417  O O   . ASP A 599  ? 0.2962 0.2842 0.3327 0.0623  -0.0089 -0.0682 597  ASP A O   
4418  C CB  . ASP A 599  ? 0.2732 0.2530 0.3116 0.0567  -0.0069 -0.0560 597  ASP A CB  
4419  C CG  . ASP A 599  ? 0.3397 0.3209 0.3837 0.0598  -0.0081 -0.0598 597  ASP A CG  
4420  O OD1 . ASP A 599  ? 0.3545 0.3345 0.4042 0.0623  -0.0112 -0.0657 597  ASP A OD1 
4421  O OD2 . ASP A 599  ? 0.4019 0.3855 0.4450 0.0598  -0.0060 -0.0568 597  ASP A OD2 
4422  N N   . HIS A 600  ? 0.2971 0.2725 0.3455 0.0610  -0.0153 -0.0710 598  HIS A N   
4423  C CA  . HIS A 600  ? 0.3707 0.3504 0.4201 0.0647  -0.0170 -0.0788 598  HIS A CA  
4424  C C   . HIS A 600  ? 0.3526 0.3397 0.4029 0.0692  -0.0164 -0.0843 598  HIS A C   
4425  O O   . HIS A 600  ? 0.3822 0.3753 0.4314 0.0727  -0.0170 -0.0908 598  HIS A O   
4426  C CB  . HIS A 600  ? 0.3766 0.3490 0.4341 0.0643  -0.0217 -0.0822 598  HIS A CB  
4427  C CG  . HIS A 600  ? 0.3649 0.3321 0.4210 0.0606  -0.0223 -0.0785 598  HIS A CG  
4428  N ND1 . HIS A 600  ? 0.3700 0.3304 0.4331 0.0594  -0.0263 -0.0801 598  HIS A ND1 
4429  C CD2 . HIS A 600  ? 0.3341 0.3023 0.3829 0.0578  -0.0196 -0.0734 598  HIS A CD2 
4430  C CE1 . HIS A 600  ? 0.4038 0.3615 0.4637 0.0560  -0.0258 -0.0761 598  HIS A CE1 
4431  N NE2 . HIS A 600  ? 0.3829 0.3452 0.4341 0.0551  -0.0218 -0.0721 598  HIS A NE2 
4432  N N   . ARG A 601  ? 0.3256 0.3129 0.3775 0.0694  -0.0152 -0.0818 599  ARG A N   
4433  C CA  . ARG A 601  ? 0.3442 0.3396 0.3962 0.0736  -0.0140 -0.0863 599  ARG A CA  
4434  C C   . ARG A 601  ? 0.3761 0.3814 0.4191 0.0745  -0.0098 -0.0851 599  ARG A C   
4435  O O   . ARG A 601  ? 0.3820 0.3959 0.4241 0.0785  -0.0089 -0.0898 599  ARG A O   
4436  C CB  . ARG A 601  ? 0.3574 0.3503 0.4136 0.0732  -0.0138 -0.0833 599  ARG A CB  
4437  C CG  . ARG A 601  ? 0.3678 0.3510 0.4330 0.0721  -0.0179 -0.0834 599  ARG A CG  
4438  C CD  . ARG A 601  ? 0.3808 0.3613 0.4489 0.0708  -0.0172 -0.0788 599  ARG A CD  
4439  N NE  . ARG A 601  ? 0.3589 0.3391 0.4206 0.0671  -0.0138 -0.0708 599  ARG A NE  
4440  C CZ  . ARG A 601  ? 0.3977 0.3765 0.4601 0.0655  -0.0126 -0.0658 599  ARG A CZ  
4441  N NH1 . ARG A 601  ? 0.4344 0.4117 0.5034 0.0673  -0.0143 -0.0675 599  ARG A NH1 
4442  N NH2 . ARG A 601  ? 0.3741 0.3529 0.4306 0.0621  -0.0096 -0.0590 599  ARG A NH2 
4443  N N   . ASP A 602  ? 0.3344 0.3388 0.3712 0.0711  -0.0074 -0.0787 600  ASP A N   
4444  C CA  . ASP A 602  ? 0.3731 0.3861 0.4018 0.0714  -0.0035 -0.0764 600  ASP A CA  
4445  C C   . ASP A 602  ? 0.3990 0.4162 0.4242 0.0729  -0.0041 -0.0805 600  ASP A C   
4446  O O   . ASP A 602  ? 0.3554 0.3678 0.3790 0.0703  -0.0049 -0.0784 600  ASP A O   
4447  C CB  . ASP A 602  ? 0.3424 0.3520 0.3669 0.0670  -0.0009 -0.0677 600  ASP A CB  
4448  C CG  . ASP A 602  ? 0.4162 0.4342 0.4331 0.0670  0.0029  -0.0646 600  ASP A CG  
4449  O OD1 . ASP A 602  ? 0.3809 0.4080 0.3958 0.0705  0.0041  -0.0684 600  ASP A OD1 
4450  O OD2 . ASP A 602  ? 0.3510 0.3664 0.3639 0.0635  0.0046  -0.0584 600  ASP A OD2 
4451  N N   . VAL A 603  ? 0.3432 0.3696 0.3672 0.0772  -0.0038 -0.0865 601  VAL A N   
4452  C CA  . VAL A 603  ? 0.3383 0.3701 0.3587 0.0790  -0.0043 -0.0908 601  VAL A CA  
4453  C C   . VAL A 603  ? 0.3685 0.4071 0.3803 0.0778  -0.0003 -0.0855 601  VAL A C   
4454  O O   . VAL A 603  ? 0.3652 0.4112 0.3740 0.0789  0.0027  -0.0834 601  VAL A O   
4455  C CB  . VAL A 603  ? 0.3568 0.3963 0.3798 0.0844  -0.0058 -0.0999 601  VAL A CB  
4456  C CG1 . VAL A 603  ? 0.3742 0.4194 0.3935 0.0863  -0.0066 -0.1047 601  VAL A CG1 
4457  C CG2 . VAL A 603  ? 0.4455 0.4777 0.4779 0.0855  -0.0098 -0.1049 601  VAL A CG2 
4458  N N   . VAL A 604  ? 0.3162 0.3522 0.3244 0.0755  -0.0004 -0.0830 602  VAL A N   
4459  C CA  . VAL A 604  ? 0.2882 0.3295 0.2888 0.0740  0.0030  -0.0773 602  VAL A CA  
4460  C C   . VAL A 604  ? 0.3173 0.3697 0.3132 0.0774  0.0038  -0.0816 602  VAL A C   
4461  O O   . VAL A 604  ? 0.3290 0.3898 0.3195 0.0779  0.0070  -0.0783 602  VAL A O   
4462  C CB  . VAL A 604  ? 0.3059 0.3389 0.3050 0.0695  0.0028  -0.0718 602  VAL A CB  
4463  C CG1 . VAL A 604  ? 0.3100 0.3480 0.3019 0.0680  0.0062  -0.0659 602  VAL A CG1 
4464  C CG2 . VAL A 604  ? 0.3045 0.3274 0.3082 0.0663  0.0020  -0.0678 602  VAL A CG2 
4465  N N   . GLY A 605  ? 0.3316 0.3845 0.3297 0.0798  0.0008  -0.0888 603  GLY A N   
4466  C CA  . GLY A 605  ? 0.3156 0.3795 0.3094 0.0834  0.0012  -0.0934 603  GLY A CA  
4467  C C   . GLY A 605  ? 0.3496 0.4120 0.3473 0.0857  -0.0028 -0.1019 603  GLY A C   
4468  O O   . GLY A 605  ? 0.3469 0.4009 0.3517 0.0854  -0.0060 -0.1051 603  GLY A O   
4469  N N   . SER A 606  ? 0.3240 0.3949 0.3173 0.0881  -0.0029 -0.1055 604  SER A N   
4470  C CA  . SER A 606  ? 0.3309 0.4022 0.3274 0.0908  -0.0067 -0.1142 604  SER A CA  
4471  C C   . SER A 606  ? 0.3451 0.4178 0.3367 0.0897  -0.0069 -0.1132 604  SER A C   
4472  O O   . SER A 606  ? 0.3676 0.4474 0.3520 0.0892  -0.0038 -0.1085 604  SER A O   
4473  C CB  . SER A 606  ? 0.3801 0.4630 0.3769 0.0964  -0.0070 -0.1224 604  SER A CB  
4474  O OG  . SER A 606  ? 0.5486 0.6294 0.5514 0.0978  -0.0076 -0.1248 604  SER A OG  
4475  N N   . VAL A 607  ? 0.3199 0.3857 0.3156 0.0891  -0.0106 -0.1173 605  VAL A N   
4476  C CA  . VAL A 607  ? 0.3252 0.3921 0.3170 0.0882  -0.0113 -0.1170 605  VAL A CA  
4477  C C   . VAL A 607  ? 0.3215 0.3930 0.3159 0.0922  -0.0149 -0.1272 605  VAL A C   
4478  O O   . VAL A 607  ? 0.3560 0.4223 0.3582 0.0934  -0.0184 -0.1333 605  VAL A O   
4479  C CB  . VAL A 607  ? 0.3377 0.3922 0.3317 0.0832  -0.0125 -0.1117 605  VAL A CB  
4480  C CG1 . VAL A 607  ? 0.3314 0.3753 0.3348 0.0824  -0.0161 -0.1150 605  VAL A CG1 
4481  C CG2 . VAL A 607  ? 0.3256 0.3816 0.3161 0.0827  -0.0135 -0.1124 605  VAL A CG2 
4482  N N   . THR A 608  ? 0.3362 0.4176 0.3244 0.0942  -0.0141 -0.1291 606  THR A N   
4483  C CA  . THR A 608  ? 0.3627 0.4487 0.3526 0.0976  -0.0175 -0.1383 606  THR A CA  
4484  C C   . THR A 608  ? 0.3599 0.4402 0.3488 0.0946  -0.0191 -0.1362 606  THR A C   
4485  O O   . THR A 608  ? 0.3523 0.4352 0.3344 0.0927  -0.0165 -0.1297 606  THR A O   
4486  C CB  . THR A 608  ? 0.3600 0.4621 0.3436 0.1022  -0.0158 -0.1421 606  THR A CB  
4487  O OG1 . THR A 608  ? 0.3858 0.4933 0.3705 0.1048  -0.0141 -0.1438 606  THR A OG1 
4488  C CG2 . THR A 608  ? 0.3602 0.4673 0.3454 0.1058  -0.0195 -0.1522 606  THR A CG2 
4489  N N   . GLU A 609  ? 0.4033 0.4755 0.3994 0.0942  -0.0234 -0.1413 607  GLU A N   
4490  C CA  . GLU A 609  ? 0.4079 0.4731 0.4044 0.0908  -0.0250 -0.1388 607  GLU A CA  
4491  C C   . GLU A 609  ? 0.3828 0.4555 0.3769 0.0936  -0.0272 -0.1454 607  GLU A C   
4492  O O   . GLU A 609  ? 0.3809 0.4618 0.3760 0.0982  -0.0288 -0.1538 607  GLU A O   
4493  C CB  . GLU A 609  ? 0.4280 0.4797 0.4340 0.0881  -0.0284 -0.1393 607  GLU A CB  
4494  C CG  . GLU A 609  ? 0.4982 0.5424 0.5052 0.0847  -0.0259 -0.1313 607  GLU A CG  
4495  C CD  . GLU A 609  ? 0.6229 0.6538 0.6380 0.0811  -0.0287 -0.1294 607  GLU A CD  
4496  O OE1 . GLU A 609  ? 0.6365 0.6638 0.6593 0.0824  -0.0329 -0.1362 607  GLU A OE1 
4497  O OE2 . GLU A 609  ? 0.4872 0.5117 0.5011 0.0769  -0.0266 -0.1211 607  GLU A OE2 
4498  N N   . THR A 610  ? 0.3443 0.4147 0.3353 0.0908  -0.0271 -0.1413 608  THR A N   
4499  C CA  . THR A 610  ? 0.3676 0.4459 0.3548 0.0930  -0.0284 -0.1458 608  THR A CA  
4500  C C   . THR A 610  ? 0.4003 0.4735 0.3954 0.0937  -0.0337 -0.1540 608  THR A C   
4501  O O   . THR A 610  ? 0.4112 0.4726 0.4126 0.0903  -0.0357 -0.1521 608  THR A O   
4502  C CB  . THR A 610  ? 0.3467 0.4244 0.3276 0.0897  -0.0262 -0.1377 608  THR A CB  
4503  O OG1 . THR A 610  ? 0.3367 0.4161 0.3122 0.0881  -0.0216 -0.1291 608  THR A OG1 
4504  C CG2 . THR A 610  ? 0.4190 0.5071 0.3943 0.0922  -0.0268 -0.1413 608  THR A CG2 
4505  N N   . SER A 611  ? 0.4098 0.4922 0.4045 0.0981  -0.0359 -0.1630 609  SER A N   
4506  C CA  . SER A 611  ? 0.4461 0.5247 0.4476 0.0988  -0.0410 -0.1708 609  SER A CA  
4507  C C   . SER A 611  ? 0.4333 0.5094 0.4321 0.0958  -0.0415 -0.1670 609  SER A C   
4508  O O   . SER A 611  ? 0.4043 0.4856 0.3946 0.0948  -0.0382 -0.1608 609  SER A O   
4509  C CB  . SER A 611  ? 0.4313 0.5215 0.4328 0.1047  -0.0433 -0.1818 609  SER A CB  
4510  O OG  . SER A 611  ? 0.4323 0.5340 0.4246 0.1063  -0.0415 -0.1812 609  SER A OG  
4511  N N   . GLU A 612  ? 0.4662 0.5342 0.4726 0.0943  -0.0458 -0.1708 610  GLU A N   
4512  C CA  . GLU A 612  ? 0.4802 0.5462 0.4848 0.0917  -0.0466 -0.1681 610  GLU A CA  
4513  C C   . GLU A 612  ? 0.4234 0.5023 0.4207 0.0951  -0.0464 -0.1720 610  GLU A C   
4514  O O   . GLU A 612  ? 0.4116 0.4927 0.4026 0.0933  -0.0446 -0.1665 610  GLU A O   
4515  C CB  . GLU A 612  ? 0.5559 0.6119 0.5708 0.0898  -0.0516 -0.1723 610  GLU A CB  
4516  C CG  . GLU A 612  ? 0.6760 0.7188 0.6974 0.0854  -0.0516 -0.1662 610  GLU A CG  
4517  C CD  . GLU A 612  ? 0.7626 0.7957 0.7933 0.0826  -0.0560 -0.1680 610  GLU A CD  
4518  O OE1 . GLU A 612  ? 0.7910 0.8271 0.8224 0.0836  -0.0588 -0.1731 610  GLU A OE1 
4519  O OE2 . GLU A 612  ? 0.7334 0.7561 0.7707 0.0793  -0.0567 -0.1642 610  GLU A OE2 
4520  N N   . GLU A 613  ? 0.4097 0.4977 0.4075 0.1002  -0.0482 -0.1814 611  GLU A N   
4521  C CA  . GLU A 613  ? 0.4357 0.5376 0.4261 0.1038  -0.0479 -0.1852 611  GLU A CA  
4522  C C   . GLU A 613  ? 0.3903 0.5000 0.3700 0.1035  -0.0425 -0.1767 611  GLU A C   
4523  O O   . GLU A 613  ? 0.3810 0.4966 0.3540 0.1033  -0.0414 -0.1737 611  GLU A O   
4524  C CB  . GLU A 613  ? 0.4815 0.5924 0.4744 0.1096  -0.0504 -0.1968 611  GLU A CB  
4525  N N   . ASP A 614  ? 0.4319 0.5415 0.4102 0.1034  -0.0392 -0.1724 612  ASP A N   
4526  C CA  . ASP A 614  ? 0.3615 0.4788 0.3305 0.1031  -0.0341 -0.1643 612  ASP A CA  
4527  C C   . ASP A 614  ? 0.3896 0.4991 0.3557 0.0980  -0.0319 -0.1536 612  ASP A C   
4528  O O   . ASP A 614  ? 0.3671 0.4835 0.3254 0.0977  -0.0289 -0.1477 612  ASP A O   
4529  C CB  . ASP A 614  ? 0.3646 0.4840 0.3334 0.1044  -0.0314 -0.1628 612  ASP A CB  
4530  C CG  . ASP A 614  ? 0.4255 0.5578 0.3934 0.1103  -0.0321 -0.1720 612  ASP A CG  
4531  O OD1 . ASP A 614  ? 0.4643 0.6063 0.4291 0.1133  -0.0338 -0.1776 612  ASP A OD1 
4532  O OD2 . ASP A 614  ? 0.4637 0.5969 0.4340 0.1119  -0.0312 -0.1736 612  ASP A OD2 
4533  N N   . ALA A 615  ? 0.3401 0.4358 0.3127 0.0940  -0.0333 -0.1510 613  ALA A N   
4534  C CA  . ALA A 615  ? 0.3825 0.4713 0.3527 0.0893  -0.0316 -0.1418 613  ALA A CA  
4535  C C   . ALA A 615  ? 0.4012 0.4945 0.3678 0.0895  -0.0328 -0.1426 613  ALA A C   
4536  O O   . ALA A 615  ? 0.3738 0.4698 0.3339 0.0879  -0.0301 -0.1354 613  ALA A O   
4537  C CB  . ALA A 615  ? 0.3584 0.4325 0.3367 0.0853  -0.0332 -0.1397 613  ALA A CB  
4538  N N   . ARG A 616  ? 0.4120 0.5063 0.3830 0.0914  -0.0371 -0.1513 614  ARG A N   
4539  C CA  . ARG A 616  ? 0.4324 0.5318 0.3999 0.0919  -0.0386 -0.1528 614  ARG A CA  
4540  C C   . ARG A 616  ? 0.3738 0.4883 0.3322 0.0955  -0.0363 -0.1527 614  ARG A C   
4541  O O   . ARG A 616  ? 0.3705 0.4891 0.3231 0.0947  -0.0351 -0.1482 614  ARG A O   
4542  C CB  . ARG A 616  ? 0.4478 0.5453 0.4226 0.0934  -0.0439 -0.1628 614  ARG A CB  
4543  C CG  . ARG A 616  ? 0.5322 0.6150 0.5164 0.0895  -0.0464 -0.1621 614  ARG A CG  
4544  C CD  . ARG A 616  ? 0.5631 0.6439 0.5548 0.0905  -0.0518 -0.1711 614  ARG A CD  
4545  N NE  . ARG A 616  ? 0.6220 0.7112 0.6153 0.0957  -0.0541 -0.1814 614  ARG A NE  
4546  C CZ  . ARG A 616  ? 0.6520 0.7369 0.6532 0.0971  -0.0567 -0.1876 614  ARG A CZ  
4547  N NH1 . ARG A 616  ? 0.5514 0.6238 0.5600 0.0936  -0.0573 -0.1842 614  ARG A NH1 
4548  N NH2 . ARG A 616  ? 0.6316 0.7254 0.6338 0.1022  -0.0588 -0.1974 614  ARG A NH2 
4549  N N   . ARG A 617  ? 0.3421 0.4652 0.2990 0.0995  -0.0356 -0.1574 615  ARG A N   
4550  C CA  . ARG A 617  ? 0.3609 0.4991 0.3090 0.1028  -0.0330 -0.1565 615  ARG A CA  
4551  C C   . ARG A 617  ? 0.3628 0.5012 0.3046 0.1000  -0.0282 -0.1447 615  ARG A C   
4552  O O   . ARG A 617  ? 0.3573 0.5047 0.2919 0.1007  -0.0265 -0.1408 615  ARG A O   
4553  C CB  . ARG A 617  ? 0.3888 0.5361 0.3371 0.1074  -0.0329 -0.1634 615  ARG A CB  
4554  C CG  . ARG A 617  ? 0.4933 0.6574 0.4326 0.1111  -0.0302 -0.1626 615  ARG A CG  
4555  C CD  . ARG A 617  ? 0.5660 0.7409 0.5066 0.1164  -0.0318 -0.1728 615  ARG A CD  
4556  N NE  . ARG A 617  ? 0.5641 0.7359 0.5085 0.1170  -0.0306 -0.1737 615  ARG A NE  
4557  C CZ  . ARG A 617  ? 0.6742 0.8535 0.6139 0.1181  -0.0266 -0.1692 615  ARG A CZ  
4558  N NH1 . ARG A 617  ? 0.5857 0.7762 0.5170 0.1185  -0.0233 -0.1629 615  ARG A NH1 
4559  N NH2 . ARG A 617  ? 0.5645 0.7404 0.5086 0.1186  -0.0259 -0.1707 615  ARG A NH2 
4560  N N   . ALA A 618  ? 0.3615 0.4898 0.3060 0.0967  -0.0262 -0.1387 616  ALA A N   
4561  C CA  . ALA A 618  ? 0.3317 0.4597 0.2710 0.0940  -0.0219 -0.1278 616  ALA A CA  
4562  C C   . ALA A 618  ? 0.3248 0.4496 0.2615 0.0910  -0.0218 -0.1219 616  ALA A C   
4563  O O   . ALA A 618  ? 0.3224 0.4534 0.2527 0.0907  -0.0190 -0.1151 616  ALA A O   
4564  C CB  . ALA A 618  ? 0.3024 0.4198 0.2461 0.0911  -0.0203 -0.1234 616  ALA A CB  
4565  N N   . VAL A 619  ? 0.3223 0.4377 0.2643 0.0888  -0.0249 -0.1243 617  VAL A N   
4566  C CA  . VAL A 619  ? 0.3186 0.4313 0.2584 0.0862  -0.0251 -0.1194 617  VAL A CA  
4567  C C   . VAL A 619  ? 0.3457 0.4712 0.2793 0.0893  -0.0255 -0.1214 617  VAL A C   
4568  O O   . VAL A 619  ? 0.3398 0.4686 0.2681 0.0881  -0.0236 -0.1145 617  VAL A O   
4569  C CB  . VAL A 619  ? 0.3624 0.4635 0.3095 0.0835  -0.0285 -0.1222 617  VAL A CB  
4570  C CG1 . VAL A 619  ? 0.3817 0.4808 0.3266 0.0809  -0.0287 -0.1173 617  VAL A CG1 
4571  C CG2 . VAL A 619  ? 0.3704 0.4594 0.3233 0.0803  -0.0279 -0.1193 617  VAL A CG2 
4572  N N   . ARG A 620  ? 0.3502 0.4834 0.2845 0.0933  -0.0282 -0.1309 618  ARG A N   
4573  C CA  . ARG A 620  ? 0.3576 0.5040 0.2859 0.0965  -0.0288 -0.1332 618  ARG A CA  
4574  C C   . ARG A 620  ? 0.3536 0.5111 0.2740 0.0980  -0.0247 -0.1269 618  ARG A C   
4575  O O   . ARG A 620  ? 0.3995 0.5643 0.3141 0.0982  -0.0237 -0.1226 618  ARG A O   
4576  C CB  . ARG A 620  ? 0.3679 0.5211 0.2988 0.1008  -0.0325 -0.1452 618  ARG A CB  
4577  N N   . LEU A 621  ? 0.3168 0.4756 0.2373 0.0987  -0.0223 -0.1259 619  LEU A N   
4578  C CA  . LEU A 621  ? 0.3713 0.5403 0.2850 0.0998  -0.0182 -0.1192 619  LEU A CA  
4579  C C   . LEU A 621  ? 0.3526 0.5156 0.2639 0.0956  -0.0155 -0.1077 619  LEU A C   
4580  O O   . LEU A 621  ? 0.3785 0.5504 0.2838 0.0960  -0.0133 -0.1016 619  LEU A O   
4581  C CB  . LEU A 621  ? 0.3271 0.4978 0.2423 0.1012  -0.0164 -0.1206 619  LEU A CB  
4582  C CG  . LEU A 621  ? 0.3610 0.5400 0.2778 0.1061  -0.0185 -0.1316 619  LEU A CG  
4583  C CD1 . LEU A 621  ? 0.3746 0.5513 0.2944 0.1065  -0.0168 -0.1322 619  LEU A CD1 
4584  C CD2 . LEU A 621  ? 0.3714 0.5682 0.2808 0.1102  -0.0178 -0.1332 619  LEU A CD2 
4585  N N   . ALA A 622  ? 0.3352 0.4836 0.2517 0.0915  -0.0157 -0.1045 620  ALA A N   
4586  C CA  . ALA A 622  ? 0.3400 0.4821 0.2549 0.0875  -0.0135 -0.0944 620  ALA A CA  
4587  C C   . ALA A 622  ? 0.3391 0.4842 0.2510 0.0872  -0.0147 -0.0927 620  ALA A C   
4588  O O   . ALA A 622  ? 0.3426 0.4909 0.2502 0.0861  -0.0125 -0.0847 620  ALA A O   
4589  C CB  . ALA A 622  ? 0.2965 0.4229 0.2177 0.0835  -0.0138 -0.0925 620  ALA A CB  
4590  N N   . ALA A 623  ? 0.3082 0.4523 0.2226 0.0883  -0.0184 -0.1001 621  ALA A N   
4591  C CA  . ALA A 623  ? 0.3438 0.4913 0.2556 0.0882  -0.0199 -0.0993 621  ALA A CA  
4592  C C   . ALA A 623  ? 0.3473 0.5105 0.2517 0.0916  -0.0187 -0.0978 621  ALA A C   
4593  O O   . ALA A 623  ? 0.3582 0.5244 0.2586 0.0906  -0.0177 -0.0913 621  ALA A O   
4594  C CB  . ALA A 623  ? 0.3738 0.5182 0.2902 0.0890  -0.0243 -0.1083 621  ALA A CB  
4595  N N   . ASP A 624  ? 0.3755 0.5490 0.2780 0.0955  -0.0187 -0.1036 622  ASP A N   
4596  C CA  . ASP A 624  ? 0.4501 0.6399 0.3455 0.0989  -0.0174 -0.1024 622  ASP A CA  
4597  C C   . ASP A 624  ? 0.4291 0.6214 0.3203 0.0972  -0.0132 -0.0911 622  ASP A C   
4598  O O   . ASP A 624  ? 0.4746 0.6764 0.3604 0.0980  -0.0122 -0.0860 622  ASP A O   
4599  C CB  . ASP A 624  ? 0.4822 0.6824 0.3769 0.1034  -0.0179 -0.1109 622  ASP A CB  
4600  C CG  . ASP A 624  ? 0.6189 0.8197 0.5170 0.1059  -0.0224 -0.1225 622  ASP A CG  
4601  O OD1 . ASP A 624  ? 0.6153 0.8117 0.5148 0.1046  -0.0250 -0.1236 622  ASP A OD1 
4602  O OD2 . ASP A 624  ? 0.7174 0.9233 0.6171 0.1092  -0.0234 -0.1307 622  ASP A OD2 
4603  N N   . ALA A 625  ? 0.4436 0.6276 0.3378 0.0948  -0.0109 -0.0870 623  ALA A N   
4604  C CA  . ALA A 625  ? 0.4582 0.6435 0.3496 0.0930  -0.0071 -0.0766 623  ALA A CA  
4605  C C   . ALA A 625  ? 0.4468 0.6224 0.3392 0.0888  -0.0065 -0.0683 623  ALA A C   
4606  O O   . ALA A 625  ? 0.4807 0.6570 0.3711 0.0871  -0.0036 -0.0593 623  ALA A O   
4607  C CB  . ALA A 625  ? 0.5009 0.6815 0.3953 0.0923  -0.0050 -0.0763 623  ALA A CB  
4608  N N   . ALA A 626  ? 0.4157 0.5820 0.3114 0.0870  -0.0092 -0.0710 624  ALA A N   
4609  C CA  . ALA A 626  ? 0.3758 0.5321 0.2731 0.0830  -0.0086 -0.0636 624  ALA A CA  
4610  C C   . ALA A 626  ? 0.4199 0.5836 0.3123 0.0830  -0.0072 -0.0556 624  ALA A C   
4611  O O   . ALA A 626  ? 0.4070 0.5658 0.2998 0.0802  -0.0050 -0.0471 624  ALA A O   
4612  C CB  . ALA A 626  ? 0.3918 0.5383 0.2935 0.0814  -0.0119 -0.0685 624  ALA A CB  
4613  N N   . PRO A 627  ? 0.4034 0.5787 0.2914 0.0858  -0.0084 -0.0575 625  PRO A N   
4614  C CA  . PRO A 627  ? 0.4387 0.6211 0.3223 0.0857  -0.0070 -0.0489 625  PRO A CA  
4615  C C   . PRO A 627  ? 0.3946 0.5823 0.2759 0.0855  -0.0034 -0.0412 625  PRO A C   
4616  O O   . PRO A 627  ? 0.4171 0.6027 0.2982 0.0832  -0.0018 -0.0321 625  PRO A O   
4617  C CB  . PRO A 627  ? 0.4791 0.6749 0.3582 0.0895  -0.0091 -0.0540 625  PRO A CB  
4618  C CG  . PRO A 627  ? 0.4242 0.6153 0.3069 0.0905  -0.0123 -0.0646 625  PRO A CG  
4619  C CD  . PRO A 627  ? 0.4512 0.6335 0.3383 0.0893  -0.0114 -0.0674 625  PRO A CD  
4620  N N   . ASP A 628  ? 0.4090 0.6038 0.2891 0.0878  -0.0021 -0.0446 626  ASP A N   
4621  C CA  . ASP A 628  ? 0.3950 0.5964 0.2729 0.0878  0.0013  -0.0372 626  ASP A CA  
4622  C C   . ASP A 628  ? 0.4192 0.6078 0.3013 0.0837  0.0032  -0.0307 626  ASP A C   
4623  O O   . ASP A 628  ? 0.4141 0.6046 0.2953 0.0822  0.0056  -0.0216 626  ASP A O   
4624  C CB  . ASP A 628  ? 0.3984 0.6097 0.2746 0.0912  0.0022  -0.0430 626  ASP A CB  
4625  C CG  . ASP A 628  ? 0.5008 0.7272 0.3721 0.0956  0.0006  -0.0487 626  ASP A CG  
4626  O OD1 . ASP A 628  ? 0.6007 0.8326 0.4689 0.0959  -0.0003 -0.0455 626  ASP A OD1 
4627  O OD2 . ASP A 628  ? 0.5992 0.8324 0.4700 0.0987  0.0002  -0.0564 626  ASP A OD2 
4628  N N   . TRP A 629  ? 0.3567 0.5325 0.2438 0.0819  0.0022  -0.0353 627  TRP A N   
4629  C CA  . TRP A 629  ? 0.3311 0.4951 0.2221 0.0782  0.0039  -0.0296 627  TRP A CA  
4630  C C   . TRP A 629  ? 0.3377 0.4938 0.2300 0.0751  0.0034  -0.0234 627  TRP A C   
4631  O O   . TRP A 629  ? 0.3590 0.5110 0.2526 0.0726  0.0054  -0.0155 627  TRP A O   
4632  C CB  . TRP A 629  ? 0.3375 0.4910 0.2333 0.0773  0.0029  -0.0362 627  TRP A CB  
4633  C CG  . TRP A 629  ? 0.3161 0.4579 0.2159 0.0736  0.0045  -0.0309 627  TRP A CG  
4634  C CD1 . TRP A 629  ? 0.2929 0.4212 0.1971 0.0706  0.0033  -0.0315 627  TRP A CD1 
4635  C CD2 . TRP A 629  ? 0.3329 0.4758 0.2325 0.0724  0.0076  -0.0239 627  TRP A CD2 
4636  N NE1 . TRP A 629  ? 0.2997 0.4210 0.2064 0.0678  0.0054  -0.0257 627  TRP A NE1 
4637  C CE2 . TRP A 629  ? 0.2761 0.4059 0.1803 0.0688  0.0080  -0.0210 627  TRP A CE2 
4638  C CE3 . TRP A 629  ? 0.3068 0.4611 0.2033 0.0741  0.0100  -0.0198 627  TRP A CE3 
4639  C CZ2 . TRP A 629  ? 0.3149 0.4421 0.2205 0.0669  0.0105  -0.0145 627  TRP A CZ2 
4640  C CZ3 . TRP A 629  ? 0.3511 0.5026 0.2492 0.0719  0.0126  -0.0130 627  TRP A CZ3 
4641  C CH2 . TRP A 629  ? 0.3475 0.4854 0.2502 0.0684  0.0128  -0.0106 627  TRP A CH2 
4642  N N   . ALA A 630  ? 0.3211 0.4751 0.2135 0.0753  0.0007  -0.0271 628  ALA A N   
4643  C CA  . ALA A 630  ? 0.3635 0.5111 0.2571 0.0728  0.0001  -0.0215 628  ALA A CA  
4644  C C   . ALA A 630  ? 0.3911 0.5473 0.2814 0.0731  0.0017  -0.0128 628  ALA A C   
4645  O O   . ALA A 630  ? 0.3875 0.5378 0.2795 0.0705  0.0022  -0.0058 628  ALA A O   
4646  C CB  . ALA A 630  ? 0.3612 0.5070 0.2553 0.0733  -0.0031 -0.0273 628  ALA A CB  
4647  N N   . ALA A 631  ? 0.3474 0.5176 0.2330 0.0762  0.0024  -0.0129 629  ALA A N   
4648  C CA  . ALA A 631  ? 0.4101 0.5899 0.2924 0.0766  0.0037  -0.0044 629  ALA A CA  
4649  C C   . ALA A 631  ? 0.3783 0.5574 0.2618 0.0749  0.0068  0.0036  629  ALA A C   
4650  O O   . ALA A 631  ? 0.4125 0.5968 0.2948 0.0744  0.0079  0.0121  629  ALA A O   
4651  C CB  . ALA A 631  ? 0.4008 0.5968 0.2774 0.0807  0.0034  -0.0075 629  ALA A CB  
4652  N N   . VAL A 632  ? 0.3242 0.4974 0.2105 0.0739  0.0081  0.0013  630  VAL A N   
4653  C CA  . VAL A 632  ? 0.3538 0.5247 0.2421 0.0718  0.0108  0.0088  630  VAL A CA  
4654  C C   . VAL A 632  ? 0.3507 0.5094 0.2430 0.0682  0.0104  0.0143  630  VAL A C   
4655  O O   . VAL A 632  ? 0.3466 0.4942 0.2420 0.0667  0.0089  0.0100  630  VAL A O   
4656  C CB  . VAL A 632  ? 0.3741 0.5413 0.2645 0.0718  0.0121  0.0043  630  VAL A CB  
4657  C CG1 . VAL A 632  ? 0.3337 0.4974 0.2268 0.0693  0.0147  0.0120  630  VAL A CG1 
4658  C CG2 . VAL A 632  ? 0.3402 0.5205 0.2267 0.0757  0.0124  -0.0014 630  VAL A CG2 
4659  N N   . PRO A 633  ? 0.3389 0.4998 0.2316 0.0669  0.0116  0.0237  631  PRO A N   
4660  C CA  . PRO A 633  ? 0.3107 0.4607 0.2073 0.0639  0.0109  0.0285  631  PRO A CA  
4661  C C   . PRO A 633  ? 0.3298 0.4667 0.2312 0.0612  0.0114  0.0268  631  PRO A C   
4662  O O   . PRO A 633  ? 0.3341 0.4710 0.2362 0.0611  0.0131  0.0259  631  PRO A O   
4663  C CB  . PRO A 633  ? 0.3705 0.5265 0.2671 0.0632  0.0123  0.0389  631  PRO A CB  
4664  C CG  . PRO A 633  ? 0.3669 0.5386 0.2583 0.0663  0.0132  0.0392  631  PRO A CG  
4665  C CD  . PRO A 633  ? 0.3536 0.5276 0.2432 0.0682  0.0135  0.0303  631  PRO A CD  
4666  N N   . PRO A 634  ? 0.2869 0.4126 0.1916 0.0590  0.0099  0.0264  632  PRO A N   
4667  C CA  . PRO A 634  ? 0.2944 0.4080 0.2036 0.0565  0.0103  0.0246  632  PRO A CA  
4668  C C   . PRO A 634  ? 0.2957 0.4078 0.2073 0.0548  0.0127  0.0306  632  PRO A C   
4669  O O   . PRO A 634  ? 0.2957 0.4030 0.2090 0.0540  0.0136  0.0278  632  PRO A O   
4670  C CB  . PRO A 634  ? 0.3504 0.4548 0.2625 0.0545  0.0085  0.0255  632  PRO A CB  
4671  C CG  . PRO A 634  ? 0.3719 0.4829 0.2807 0.0565  0.0067  0.0242  632  PRO A CG  
4672  C CD  . PRO A 634  ? 0.3249 0.4494 0.2295 0.0589  0.0078  0.0273  632  PRO A CD  
4673  N N   . SER A 635  ? 0.3427 0.4589 0.2546 0.0543  0.0135  0.0388  633  SER A N   
4674  C CA  . SER A 635  ? 0.3615 0.4765 0.2763 0.0525  0.0156  0.0448  633  SER A CA  
4675  C C   . SER A 635  ? 0.3347 0.4570 0.2474 0.0541  0.0176  0.0429  633  SER A C   
4676  O O   . SER A 635  ? 0.3301 0.4482 0.2456 0.0526  0.0190  0.0438  633  SER A O   
4677  C CB  . SER A 635  ? 0.4233 0.5428 0.3390 0.0519  0.0160  0.0541  633  SER A CB  
4678  O OG  . SER A 635  ? 0.5836 0.7169 0.4948 0.0544  0.0166  0.0561  633  SER A OG  
4679  N N   . GLU A 636  ? 0.3010 0.4347 0.2088 0.0571  0.0175  0.0400  634  GLU A N   
4680  C CA  . GLU A 636  ? 0.3421 0.4837 0.2478 0.0589  0.0193  0.0376  634  GLU A CA  
4681  C C   . GLU A 636  ? 0.3277 0.4628 0.2342 0.0593  0.0187  0.0286  634  GLU A C   
4682  O O   . GLU A 636  ? 0.3335 0.4689 0.2411 0.0594  0.0203  0.0274  634  GLU A O   
4683  C CB  . GLU A 636  ? 0.3272 0.4839 0.2275 0.0622  0.0194  0.0373  634  GLU A CB  
4684  C CG  . GLU A 636  ? 0.4684 0.6346 0.3663 0.0646  0.0212  0.0342  634  GLU A CG  
4685  C CD  . GLU A 636  ? 0.5874 0.7525 0.4883 0.0627  0.0237  0.0397  634  GLU A CD  
4686  O OE1 . GLU A 636  ? 0.4863 0.6521 0.3891 0.0609  0.0246  0.0487  634  GLU A OE1 
4687  O OE2 . GLU A 636  ? 0.4740 0.6374 0.3760 0.0631  0.0246  0.0352  634  GLU A OE2 
4688  N N   . ARG A 637  ? 0.3001 0.4293 0.2067 0.0595  0.0164  0.0225  635  ARG A N   
4689  C CA  . ARG A 637  ? 0.2705 0.3920 0.1791 0.0593  0.0156  0.0149  635  ARG A CA  
4690  C C   . ARG A 637  ? 0.3007 0.4114 0.2140 0.0562  0.0167  0.0177  635  ARG A C   
4691  O O   . ARG A 637  ? 0.2893 0.3976 0.2041 0.0561  0.0175  0.0146  635  ARG A O   
4692  C CB  . ARG A 637  ? 0.2804 0.3969 0.1889 0.0596  0.0129  0.0089  635  ARG A CB  
4693  C CG  . ARG A 637  ? 0.3082 0.4354 0.2123 0.0626  0.0116  0.0061  635  ARG A CG  
4694  C CD  . ARG A 637  ? 0.3203 0.4433 0.2246 0.0633  0.0088  -0.0016 635  ARG A CD  
4695  N NE  . ARG A 637  ? 0.3015 0.4145 0.2087 0.0607  0.0075  0.0002  635  ARG A NE  
4696  C CZ  . ARG A 637  ? 0.3634 0.4777 0.2694 0.0609  0.0059  0.0012  635  ARG A CZ  
4697  N NH1 . ARG A 637  ? 0.3545 0.4799 0.2563 0.0635  0.0054  0.0012  635  ARG A NH1 
4698  N NH2 . ARG A 637  ? 0.3340 0.4386 0.2431 0.0585  0.0048  0.0022  635  ARG A NH2 
4699  N N   . ALA A 638  ? 0.3199 0.4242 0.2357 0.0537  0.0165  0.0234  636  ALA A N   
4700  C CA  . ALA A 638  ? 0.2933 0.3881 0.2136 0.0507  0.0174  0.0263  636  ALA A CA  
4701  C C   . ALA A 638  ? 0.3182 0.4175 0.2390 0.0506  0.0198  0.0304  636  ALA A C   
4702  O O   . ALA A 638  ? 0.2699 0.3632 0.1937 0.0492  0.0207  0.0297  636  ALA A O   
4703  C CB  . ALA A 638  ? 0.2784 0.3670 0.2013 0.0485  0.0167  0.0317  636  ALA A CB  
4704  N N   . ALA A 639  ? 0.3063 0.4167 0.2245 0.0521  0.0210  0.0350  637  ALA A N   
4705  C CA  . ALA A 639  ? 0.2985 0.4146 0.2173 0.0521  0.0234  0.0390  637  ALA A CA  
4706  C C   . ALA A 639  ? 0.2897 0.4085 0.2073 0.0539  0.0241  0.0325  637  ALA A C   
4707  O O   . ALA A 639  ? 0.3093 0.4270 0.2291 0.0531  0.0257  0.0339  637  ALA A O   
4708  C CB  . ALA A 639  ? 0.2839 0.4124 0.2000 0.0534  0.0244  0.0454  637  ALA A CB  
4709  N N   . CYS A 640  ? 0.2713 0.3933 0.1859 0.0564  0.0227  0.0251  638  CYS A N   
4710  C CA  . CYS A 640  ? 0.2991 0.4218 0.2135 0.0581  0.0229  0.0180  638  CYS A CA  
4711  C C   . CYS A 640  ? 0.3028 0.4127 0.2217 0.0557  0.0226  0.0158  638  CYS A C   
4712  O O   . CYS A 640  ? 0.3113 0.4208 0.2318 0.0558  0.0238  0.0145  638  CYS A O   
4713  C CB  . CYS A 640  ? 0.2931 0.4198 0.2046 0.0610  0.0210  0.0100  638  CYS A CB  
4714  S SG  . CYS A 640  ? 0.3317 0.4753 0.2374 0.0645  0.0214  0.0108  638  CYS A SG  
4715  N N   . LEU A 641  ? 0.2814 0.3812 0.2023 0.0537  0.0209  0.0153  639  LEU A N   
4716  C CA  . LEU A 641  ? 0.2673 0.3555 0.1923 0.0513  0.0205  0.0135  639  LEU A CA  
4717  C C   . LEU A 641  ? 0.2745 0.3601 0.2024 0.0492  0.0225  0.0197  639  LEU A C   
4718  O O   . LEU A 641  ? 0.2870 0.3684 0.2174 0.0484  0.0231  0.0179  639  LEU A O   
4719  C CB  . LEU A 641  ? 0.2688 0.3479 0.1954 0.0495  0.0185  0.0126  639  LEU A CB  
4720  C CG  . LEU A 641  ? 0.2999 0.3764 0.2260 0.0507  0.0162  0.0048  639  LEU A CG  
4721  C CD1 . LEU A 641  ? 0.3186 0.4051 0.2405 0.0538  0.0154  0.0017  639  LEU A CD1 
4722  C CD2 . LEU A 641  ? 0.2850 0.3522 0.2133 0.0484  0.0146  0.0049  639  LEU A CD2 
4723  N N   . ASP A 642  ? 0.2934 0.3817 0.2215 0.0481  0.0233  0.0270  640  ASP A N   
4724  C CA  . ASP A 642  ? 0.2753 0.3614 0.2067 0.0460  0.0250  0.0329  640  ASP A CA  
4725  C C   . ASP A 642  ? 0.2639 0.3576 0.1947 0.0474  0.0270  0.0330  640  ASP A C   
4726  O O   . ASP A 642  ? 0.2683 0.3579 0.2022 0.0459  0.0280  0.0340  640  ASP A O   
4727  C CB  . ASP A 642  ? 0.2906 0.3784 0.2229 0.0447  0.0253  0.0408  640  ASP A CB  
4728  C CG  . ASP A 642  ? 0.3015 0.3793 0.2363 0.0425  0.0236  0.0416  640  ASP A CG  
4729  O OD1 . ASP A 642  ? 0.3403 0.4090 0.2772 0.0413  0.0227  0.0375  640  ASP A OD1 
4730  O OD2 . ASP A 642  ? 0.3153 0.3948 0.2502 0.0421  0.0231  0.0464  640  ASP A OD2 
4731  N N   . ARG A 643  ? 0.2889 0.3941 0.2157 0.0503  0.0276  0.0317  641  ARG A N   
4732  C CA  . ARG A 643  ? 0.2904 0.4037 0.2165 0.0519  0.0295  0.0310  641  ARG A CA  
4733  C C   . ARG A 643  ? 0.2657 0.3737 0.1932 0.0525  0.0290  0.0237  641  ARG A C   
4734  O O   . ARG A 643  ? 0.3139 0.4221 0.2434 0.0522  0.0304  0.0241  641  ARG A O   
4735  C CB  . ARG A 643  ? 0.3068 0.4341 0.2280 0.0552  0.0300  0.0304  641  ARG A CB  
4736  C CG  . ARG A 643  ? 0.3174 0.4527 0.2378 0.0546  0.0314  0.0393  641  ARG A CG  
4737  C CD  . ARG A 643  ? 0.3196 0.4702 0.2351 0.0580  0.0323  0.0389  641  ARG A CD  
4738  N NE  . ARG A 643  ? 0.3348 0.4879 0.2466 0.0603  0.0303  0.0330  641  ARG A NE  
4739  C CZ  . ARG A 643  ? 0.3391 0.4950 0.2487 0.0604  0.0292  0.0359  641  ARG A CZ  
4740  N NH1 . ARG A 643  ? 0.3771 0.5333 0.2882 0.0584  0.0299  0.0448  641  ARG A NH1 
4741  N NH2 . ARG A 643  ? 0.3768 0.5353 0.2830 0.0627  0.0274  0.0298  641  ARG A NH2 
4742  N N   . ALA A 644  ? 0.2712 0.3742 0.1979 0.0533  0.0268  0.0170  642  ALA A N   
4743  C CA  . ALA A 644  ? 0.2828 0.3802 0.2116 0.0538  0.0260  0.0103  642  ALA A CA  
4744  C C   . ALA A 644  ? 0.2880 0.3747 0.2212 0.0506  0.0263  0.0126  642  ALA A C   
4745  O O   . ALA A 644  ? 0.2766 0.3609 0.2119 0.0507  0.0267  0.0100  642  ALA A O   
4746  C CB  . ALA A 644  ? 0.2988 0.3926 0.2267 0.0548  0.0234  0.0034  642  ALA A CB  
4747  N N   . ALA A 645  ? 0.2761 0.3563 0.2109 0.0479  0.0259  0.0174  643  ALA A N   
4748  C CA  . ALA A 645  ? 0.2401 0.3107 0.1790 0.0450  0.0261  0.0197  643  ALA A CA  
4749  C C   . ALA A 645  ? 0.2702 0.3443 0.2108 0.0444  0.0283  0.0242  643  ALA A C   
4750  O O   . ALA A 645  ? 0.2816 0.3507 0.2252 0.0433  0.0287  0.0232  643  ALA A O   
4751  C CB  . ALA A 645  ? 0.2774 0.3415 0.2177 0.0425  0.0252  0.0236  643  ALA A CB  
4752  N N   . GLU A 646  ? 0.2906 0.3737 0.2297 0.0451  0.0298  0.0293  644  GLU A N   
4753  C CA  . GLU A 646  ? 0.3204 0.4083 0.2613 0.0446  0.0320  0.0337  644  GLU A CA  
4754  C C   . GLU A 646  ? 0.2906 0.3827 0.2310 0.0468  0.0328  0.0286  644  GLU A C   
4755  O O   . GLU A 646  ? 0.3114 0.4014 0.2546 0.0458  0.0338  0.0295  644  GLU A O   
4756  C CB  . GLU A 646  ? 0.3230 0.4211 0.2621 0.0452  0.0334  0.0401  644  GLU A CB  
4757  C CG  . GLU A 646  ? 0.4146 0.5089 0.3550 0.0430  0.0327  0.0461  644  GLU A CG  
4758  C CD  . GLU A 646  ? 0.5636 0.6494 0.5092 0.0398  0.0329  0.0503  644  GLU A CD  
4759  O OE1 . GLU A 646  ? 0.6181 0.7049 0.5660 0.0392  0.0343  0.0515  644  GLU A OE1 
4760  O OE2 . GLU A 646  ? 0.5242 0.6026 0.4718 0.0379  0.0315  0.0522  644  GLU A OE2 
4761  N N   . LEU A 647  ? 0.3021 0.4002 0.2390 0.0498  0.0321  0.0230  645  LEU A N   
4762  C CA  . LEU A 647  ? 0.2975 0.3999 0.2342 0.0523  0.0326  0.0176  645  LEU A CA  
4763  C C   . LEU A 647  ? 0.3231 0.4148 0.2633 0.0511  0.0314  0.0132  645  LEU A C   
4764  O O   . LEU A 647  ? 0.3260 0.4183 0.2683 0.0515  0.0323  0.0120  645  LEU A O   
4765  C CB  . LEU A 647  ? 0.2908 0.4014 0.2234 0.0558  0.0317  0.0118  645  LEU A CB  
4766  C CG  . LEU A 647  ? 0.3197 0.4434 0.2484 0.0576  0.0332  0.0156  645  LEU A CG  
4767  C CD1 . LEU A 647  ? 0.3140 0.4447 0.2388 0.0611  0.0318  0.0091  645  LEU A CD1 
4768  C CD2 . LEU A 647  ? 0.3671 0.4999 0.2963 0.0583  0.0358  0.0192  645  LEU A CD2 
4769  N N   . MET A 648  ? 0.2688 0.3510 0.2098 0.0497  0.0294  0.0110  646  MET A N   
4770  C CA  . MET A 648  ? 0.2907 0.3630 0.2350 0.0484  0.0282  0.0074  646  MET A CA  
4771  C C   . MET A 648  ? 0.2910 0.3581 0.2389 0.0456  0.0293  0.0123  646  MET A C   
4772  O O   . MET A 648  ? 0.3014 0.3649 0.2520 0.0454  0.0294  0.0102  646  MET A O   
4773  C CB  . MET A 648  ? 0.2427 0.3068 0.1873 0.0474  0.0258  0.0044  646  MET A CB  
4774  C CG  . MET A 648  ? 0.3021 0.3697 0.2443 0.0502  0.0242  -0.0021 646  MET A CG  
4775  S SD  . MET A 648  ? 0.3281 0.3846 0.2723 0.0487  0.0213  -0.0062 646  MET A SD  
4776  C CE  . MET A 648  ? 0.3461 0.4089 0.2877 0.0523  0.0195  -0.0136 646  MET A CE  
4777  N N   . GLN A 649  ? 0.2709 0.3373 0.2191 0.0436  0.0301  0.0188  647  GLN A N   
4778  C CA  . GLN A 649  ? 0.2623 0.3243 0.2142 0.0409  0.0311  0.0235  647  GLN A CA  
4779  C C   . GLN A 649  ? 0.2777 0.3463 0.2306 0.0420  0.0331  0.0246  647  GLN A C   
4780  O O   . GLN A 649  ? 0.2994 0.3637 0.2554 0.0409  0.0333  0.0243  647  GLN A O   
4781  C CB  . GLN A 649  ? 0.2930 0.3543 0.2454 0.0389  0.0315  0.0302  647  GLN A CB  
4782  C CG  . GLN A 649  ? 0.2753 0.3312 0.2321 0.0361  0.0321  0.0346  647  GLN A CG  
4783  C CD  . GLN A 649  ? 0.2942 0.3389 0.2532 0.0341  0.0304  0.0321  647  GLN A CD  
4784  O OE1 . GLN A 649  ? 0.2916 0.3316 0.2506 0.0329  0.0292  0.0329  647  GLN A OE1 
4785  N NE2 . GLN A 649  ? 0.3088 0.3499 0.2698 0.0338  0.0303  0.0292  647  GLN A NE2 
4786  N N   . ALA A 650  ? 0.2897 0.3693 0.2399 0.0441  0.0344  0.0259  648  ALA A N   
4787  C CA  . ALA A 650  ? 0.2973 0.3845 0.2484 0.0452  0.0365  0.0271  648  ALA A CA  
4788  C C   . ALA A 650  ? 0.3562 0.4429 0.3079 0.0472  0.0360  0.0202  648  ALA A C   
4789  O O   . ALA A 650  ? 0.3782 0.4659 0.3324 0.0471  0.0371  0.0206  648  ALA A O   
4790  C CB  . ALA A 650  ? 0.3428 0.4429 0.2905 0.0472  0.0380  0.0299  648  ALA A CB  
4791  N N   . ARG A 651  ? 0.3011 0.3860 0.2509 0.0490  0.0341  0.0138  649  ARG A N   
4792  C CA  . ARG A 651  ? 0.2984 0.3829 0.2491 0.0512  0.0333  0.0068  649  ARG A CA  
4793  C C   . ARG A 651  ? 0.2903 0.3627 0.2446 0.0492  0.0316  0.0045  649  ARG A C   
4794  O O   . ARG A 651  ? 0.2955 0.3661 0.2513 0.0508  0.0305  -0.0012 649  ARG A O   
4795  C CB  . ARG A 651  ? 0.3323 0.4217 0.2797 0.0543  0.0319  0.0008  649  ARG A CB  
4796  C CG  . ARG A 651  ? 0.3999 0.4927 0.3481 0.0575  0.0313  -0.0065 649  ARG A CG  
4797  C CD  . ARG A 651  ? 0.3721 0.4774 0.3165 0.0612  0.0317  -0.0096 649  ARG A CD  
4798  N NE  . ARG A 651  ? 0.4194 0.5272 0.3648 0.0645  0.0306  -0.0176 649  ARG A NE  
4799  C CZ  . ARG A 651  ? 0.4429 0.5564 0.3900 0.0662  0.0320  -0.0190 649  ARG A CZ  
4800  N NH1 . ARG A 651  ? 0.4343 0.5508 0.3821 0.0648  0.0344  -0.0129 649  ARG A NH1 
4801  N NH2 . ARG A 651  ? 0.4677 0.5837 0.4159 0.0695  0.0306  -0.0268 649  ARG A NH2 
4802  N N   . MET A 652  ? 0.2857 0.3500 0.2416 0.0459  0.0313  0.0087  650  MET A N   
4803  C CA  . MET A 652  ? 0.2656 0.3189 0.2244 0.0441  0.0296  0.0066  650  MET A CA  
4804  C C   . MET A 652  ? 0.2829 0.3344 0.2448 0.0446  0.0295  0.0037  650  MET A C   
4805  O O   . MET A 652  ? 0.2971 0.3432 0.2605 0.0450  0.0276  -0.0011 650  MET A O   
4806  C CB  . MET A 652  ? 0.2954 0.3419 0.2558 0.0406  0.0296  0.0120  650  MET A CB  
4807  C CG  . MET A 652  ? 0.2913 0.3275 0.2547 0.0385  0.0281  0.0103  650  MET A CG  
4808  S SD  . MET A 652  ? 0.3334 0.3623 0.2986 0.0348  0.0280  0.0159  650  MET A SD  
4809  C CE  . MET A 652  ? 0.3106 0.3386 0.2728 0.0348  0.0268  0.0154  650  MET A CE  
4810  N N   . PRO A 653  ? 0.2971 0.3529 0.2605 0.0447  0.0314  0.0065  651  PRO A N   
4811  C CA  . PRO A 653  ? 0.2909 0.3445 0.2576 0.0452  0.0311  0.0036  651  PRO A CA  
4812  C C   . PRO A 653  ? 0.3158 0.3722 0.2823 0.0485  0.0299  -0.0034 651  PRO A C   
4813  O O   . PRO A 653  ? 0.2939 0.3441 0.2632 0.0485  0.0283  -0.0072 651  PRO A O   
4814  C CB  . PRO A 653  ? 0.2658 0.3257 0.2336 0.0450  0.0336  0.0080  651  PRO A CB  
4815  C CG  . PRO A 653  ? 0.3210 0.3819 0.2876 0.0429  0.0346  0.0144  651  PRO A CG  
4816  C CD  . PRO A 653  ? 0.3008 0.3631 0.2636 0.0440  0.0337  0.0127  651  PRO A CD  
4817  N N   . THR A 654  ? 0.2812 0.3470 0.2446 0.0513  0.0306  -0.0054 652  THR A N   
4818  C CA  . THR A 654  ? 0.3070 0.3760 0.2703 0.0547  0.0293  -0.0127 652  THR A CA  
4819  C C   . THR A 654  ? 0.3274 0.3888 0.2909 0.0544  0.0265  -0.0168 652  THR A C   
4820  O O   . THR A 654  ? 0.3179 0.3755 0.2841 0.0556  0.0245  -0.0222 652  THR A O   
4821  C CB  . THR A 654  ? 0.2918 0.3734 0.2513 0.0578  0.0306  -0.0137 652  THR A CB  
4822  O OG1 . THR A 654  ? 0.3031 0.3922 0.2628 0.0580  0.0333  -0.0095 652  THR A OG1 
4823  C CG2 . THR A 654  ? 0.3053 0.3906 0.2650 0.0616  0.0291  -0.0219 652  THR A CG2 
4824  N N   . LEU A 655  ? 0.2704 0.3295 0.2314 0.0527  0.0261  -0.0141 653  LEU A N   
4825  C CA  . LEU A 655  ? 0.2652 0.3169 0.2266 0.0520  0.0235  -0.0174 653  LEU A CA  
4826  C C   . LEU A 655  ? 0.3103 0.3514 0.2759 0.0497  0.0221  -0.0176 653  LEU A C   
4827  O O   . LEU A 655  ? 0.3048 0.3410 0.2725 0.0501  0.0198  -0.0223 653  LEU A O   
4828  C CB  . LEU A 655  ? 0.2743 0.3253 0.2326 0.0504  0.0236  -0.0137 653  LEU A CB  
4829  C CG  . LEU A 655  ? 0.3213 0.3829 0.2754 0.0526  0.0248  -0.0132 653  LEU A CG  
4830  C CD1 . LEU A 655  ? 0.3198 0.3801 0.2713 0.0508  0.0248  -0.0091 653  LEU A CD1 
4831  C CD2 . LEU A 655  ? 0.3592 0.4253 0.3123 0.0561  0.0232  -0.0206 653  LEU A CD2 
4832  N N   . LEU A 656  ? 0.2835 0.3213 0.2506 0.0472  0.0235  -0.0125 654  LEU A N   
4833  C CA  . LEU A 656  ? 0.3093 0.3380 0.2803 0.0450  0.0222  -0.0124 654  LEU A CA  
4834  C C   . LEU A 656  ? 0.3351 0.3633 0.3093 0.0471  0.0210  -0.0177 654  LEU A C   
4835  O O   . LEU A 656  ? 0.3163 0.3377 0.2933 0.0465  0.0187  -0.0204 654  LEU A O   
4836  C CB  . LEU A 656  ? 0.3440 0.3711 0.3163 0.0426  0.0240  -0.0068 654  LEU A CB  
4837  C CG  . LEU A 656  ? 0.3628 0.3895 0.3331 0.0403  0.0252  -0.0011 654  LEU A CG  
4838  C CD1 . LEU A 656  ? 0.3229 0.3474 0.2955 0.0381  0.0264  0.0035  654  LEU A CD1 
4839  C CD2 . LEU A 656  ? 0.3488 0.3692 0.3185 0.0387  0.0235  -0.0015 654  LEU A CD2 
4840  N N   . GLY A 657  ? 0.3191 0.3548 0.2933 0.0495  0.0223  -0.0188 655  GLY A N   
4841  C CA  . GLY A 657  ? 0.3282 0.3639 0.3059 0.0517  0.0211  -0.0238 655  GLY A CA  
4842  C C   . GLY A 657  ? 0.3182 0.3527 0.2968 0.0537  0.0185  -0.0303 655  GLY A C   
4843  O O   . GLY A 657  ? 0.2938 0.3227 0.2765 0.0540  0.0164  -0.0337 655  GLY A O   
4844  N N   . LEU A 658  ? 0.2821 0.3216 0.2570 0.0551  0.0185  -0.0319 656  LEU A N   
4845  C CA  . LEU A 658  ? 0.2771 0.3157 0.2529 0.0571  0.0158  -0.0383 656  LEU A CA  
4846  C C   . LEU A 658  ? 0.2814 0.3096 0.2595 0.0543  0.0135  -0.0380 656  LEU A C   
4847  O O   . LEU A 658  ? 0.3085 0.3320 0.2906 0.0549  0.0109  -0.0425 656  LEU A O   
4848  C CB  . LEU A 658  ? 0.2741 0.3212 0.2452 0.0592  0.0164  -0.0398 656  LEU A CB  
4849  C CG  . LEU A 658  ? 0.2912 0.3387 0.2630 0.0616  0.0136  -0.0469 656  LEU A CG  
4850  C CD1 . LEU A 658  ? 0.3170 0.3649 0.2933 0.0644  0.0120  -0.0533 656  LEU A CD1 
4851  C CD2 . LEU A 658  ? 0.2935 0.3510 0.2600 0.0639  0.0146  -0.0480 656  LEU A CD2 
4852  N N   . ILE A 659  ? 0.2762 0.3009 0.2521 0.0512  0.0144  -0.0326 657  ILE A N   
4853  C CA  . ILE A 659  ? 0.2515 0.2671 0.2293 0.0485  0.0125  -0.0319 657  ILE A CA  
4854  C C   . ILE A 659  ? 0.2996 0.3083 0.2825 0.0471  0.0114  -0.0316 657  ILE A C   
4855  O O   . ILE A 659  ? 0.2696 0.2722 0.2559 0.0464  0.0089  -0.0340 657  ILE A O   
4856  C CB  . ILE A 659  ? 0.2684 0.2824 0.2430 0.0457  0.0138  -0.0262 657  ILE A CB  
4857  C CG1 . ILE A 659  ? 0.2801 0.3004 0.2503 0.0471  0.0143  -0.0268 657  ILE A CG1 
4858  C CG2 . ILE A 659  ? 0.2710 0.2761 0.2478 0.0427  0.0121  -0.0250 657  ILE A CG2 
4859  C CD1 . ILE A 659  ? 0.3168 0.3370 0.2839 0.0449  0.0159  -0.0210 657  ILE A CD1 
4860  N N   . ILE A 660  ? 0.2846 0.2943 0.2681 0.0466  0.0132  -0.0286 658  ILE A N   
4861  C CA  . ILE A 660  ? 0.2702 0.2739 0.2583 0.0454  0.0122  -0.0280 658  ILE A CA  
4862  C C   . ILE A 660  ? 0.3022 0.3050 0.2947 0.0477  0.0098  -0.0340 658  ILE A C   
4863  O O   . ILE A 660  ? 0.3200 0.3158 0.3166 0.0465  0.0075  -0.0348 658  ILE A O   
4864  C CB  . ILE A 660  ? 0.2580 0.2644 0.2460 0.0450  0.0146  -0.0242 658  ILE A CB  
4865  C CG1 . ILE A 660  ? 0.2847 0.2893 0.2702 0.0418  0.0163  -0.0181 658  ILE A CG1 
4866  C CG2 . ILE A 660  ? 0.2937 0.2961 0.2867 0.0449  0.0135  -0.0250 658  ILE A CG2 
4867  C CD1 . ILE A 660  ? 0.3482 0.3564 0.3334 0.0415  0.0187  -0.0143 658  ILE A CD1 
4868  N N   . ARG A 661  ? 0.2850 0.2949 0.2767 0.0513  0.0101  -0.0382 659  ARG A N   
4869  C CA  . ARG A 661  ? 0.3093 0.3189 0.3059 0.0539  0.0078  -0.0443 659  ARG A CA  
4870  C C   . ARG A 661  ? 0.3244 0.3319 0.3222 0.0549  0.0049  -0.0493 659  ARG A C   
4871  O O   . ARG A 661  ? 0.2987 0.3013 0.3020 0.0553  0.0021  -0.0528 659  ARG A O   
4872  C CB  . ARG A 661  ? 0.3132 0.3318 0.3089 0.0575  0.0093  -0.0471 659  ARG A CB  
4873  C CG  . ARG A 661  ? 0.3295 0.3486 0.3265 0.0568  0.0111  -0.0434 659  ARG A CG  
4874  C CD  . ARG A 661  ? 0.3327 0.3616 0.3289 0.0602  0.0129  -0.0457 659  ARG A CD  
4875  N NE  . ARG A 661  ? 0.3476 0.3788 0.3472 0.0639  0.0108  -0.0532 659  ARG A NE  
4876  C CZ  . ARG A 661  ? 0.3043 0.3440 0.3017 0.0674  0.0109  -0.0580 659  ARG A CZ  
4877  N NH1 . ARG A 661  ? 0.3417 0.3885 0.3332 0.0676  0.0132  -0.0559 659  ARG A NH1 
4878  N NH2 . ARG A 661  ? 0.3364 0.3778 0.3379 0.0709  0.0087  -0.0652 659  ARG A NH2 
4879  N N   . GLU A 662  ? 0.2982 0.3094 0.2915 0.0552  0.0054  -0.0495 660  GLU A N   
4880  C CA  . GLU A 662  ? 0.3048 0.3147 0.2995 0.0562  0.0026  -0.0547 660  GLU A CA  
4881  C C   . GLU A 662  ? 0.2907 0.2916 0.2876 0.0528  0.0008  -0.0524 660  GLU A C   
4882  O O   . GLU A 662  ? 0.3338 0.3304 0.3352 0.0530  -0.0022 -0.0563 660  GLU A O   
4883  C CB  . GLU A 662  ? 0.3363 0.3541 0.3254 0.0581  0.0037  -0.0562 660  GLU A CB  
4884  C CG  . GLU A 662  ? 0.3158 0.3325 0.3062 0.0591  0.0007  -0.0615 660  GLU A CG  
4885  C CD  . GLU A 662  ? 0.3754 0.4006 0.3604 0.0612  0.0016  -0.0634 660  GLU A CD  
4886  O OE1 . GLU A 662  ? 0.3464 0.3755 0.3261 0.0602  0.0044  -0.0583 660  GLU A OE1 
4887  O OE2 . GLU A 662  ? 0.3549 0.3830 0.3410 0.0639  -0.0006 -0.0699 660  GLU A OE2 
4888  N N   . ALA A 663  ? 0.3149 0.3131 0.3089 0.0496  0.0026  -0.0461 661  ALA A N   
4889  C CA  . ALA A 663  ? 0.3140 0.3052 0.3090 0.0464  0.0012  -0.0438 661  ALA A CA  
4890  C C   . ALA A 663  ? 0.3239 0.3082 0.3224 0.0435  0.0010  -0.0397 661  ALA A C   
4891  O O   . ALA A 663  ? 0.4096 0.3884 0.4092 0.0407  -0.0001 -0.0374 661  ALA A O   
4892  C CB  . ALA A 663  ? 0.2942 0.2877 0.2836 0.0450  0.0031  -0.0401 661  ALA A CB  
4893  N N   . GLY A 664  ? 0.3284 0.3134 0.3285 0.0440  0.0020  -0.0387 662  GLY A N   
4894  C CA  . GLY A 664  ? 0.3272 0.3060 0.3306 0.0414  0.0016  -0.0350 662  GLY A CA  
4895  C C   . GLY A 664  ? 0.3360 0.3134 0.3361 0.0383  0.0037  -0.0288 662  GLY A C   
4896  O O   . GLY A 664  ? 0.4193 0.3913 0.4217 0.0357  0.0030  -0.0257 662  GLY A O   
4897  N N   . LYS A 665  ? 0.3227 0.3050 0.3177 0.0387  0.0062  -0.0269 663  LYS A N   
4898  C CA  . LYS A 665  ? 0.3066 0.2877 0.2987 0.0359  0.0080  -0.0214 663  LYS A CA  
4899  C C   . LYS A 665  ? 0.2533 0.2359 0.2453 0.0355  0.0100  -0.0181 663  LYS A C   
4900  O O   . LYS A 665  ? 0.2661 0.2532 0.2584 0.0377  0.0109  -0.0196 663  LYS A O   
4901  C CB  . LYS A 665  ? 0.2960 0.2813 0.2831 0.0363  0.0094  -0.0207 663  LYS A CB  
4902  C CG  . LYS A 665  ? 0.3483 0.3324 0.3353 0.0366  0.0074  -0.0238 663  LYS A CG  
4903  C CD  . LYS A 665  ? 0.4657 0.4504 0.4488 0.0351  0.0084  -0.0208 663  LYS A CD  
4904  C CE  . LYS A 665  ? 0.4205 0.4030 0.4042 0.0348  0.0063  -0.0234 663  LYS A CE  
4905  N NZ  . LYS A 665  ? 0.4529 0.4358 0.4330 0.0333  0.0072  -0.0204 663  LYS A NZ  
4906  N N   . SER A 666  ? 0.2977 0.2768 0.2894 0.0326  0.0107  -0.0136 664  SER A N   
4907  C CA  . SER A 666  ? 0.2933 0.2740 0.2847 0.0319  0.0127  -0.0101 664  SER A CA  
4908  C C   . SER A 666  ? 0.3185 0.3049 0.3058 0.0326  0.0150  -0.0083 664  SER A C   
4909  O O   . SER A 666  ? 0.3044 0.2927 0.2888 0.0330  0.0151  -0.0089 664  SER A O   
4910  C CB  . SER A 666  ? 0.3212 0.2969 0.3134 0.0287  0.0126  -0.0062 664  SER A CB  
4911  O OG  . SER A 666  ? 0.3494 0.3249 0.3385 0.0272  0.0132  -0.0041 664  SER A OG  
4912  N N   . ALA A 667  ? 0.2889 0.2782 0.2763 0.0327  0.0168  -0.0059 665  ALA A N   
4913  C CA  . ALA A 667  ? 0.3035 0.2984 0.2878 0.0331  0.0190  -0.0034 665  ALA A CA  
4914  C C   . ALA A 667  ? 0.3168 0.3095 0.2989 0.0308  0.0194  -0.0001 665  ALA A C   
4915  O O   . ALA A 667  ? 0.2743 0.2706 0.2534 0.0315  0.0201  0.0004  665  ALA A O   
4916  C CB  . ALA A 667  ? 0.3085 0.3061 0.2941 0.0330  0.0207  -0.0008 665  ALA A CB  
4917  N N   . LEU A 668  ? 0.2994 0.2866 0.2829 0.0283  0.0188  0.0020  666  LEU A N   
4918  C CA  . LEU A 668  ? 0.2966 0.2815 0.2786 0.0262  0.0189  0.0047  666  LEU A CA  
4919  C C   . LEU A 668  ? 0.3123 0.2971 0.2922 0.0268  0.0178  0.0026  666  LEU A C   
4920  O O   . LEU A 668  ? 0.2929 0.2797 0.2703 0.0267  0.0186  0.0041  666  LEU A O   
4921  C CB  . LEU A 668  ? 0.3796 0.3588 0.3638 0.0237  0.0180  0.0062  666  LEU A CB  
4922  C CG  . LEU A 668  ? 0.5808 0.5582 0.5644 0.0214  0.0185  0.0096  666  LEU A CG  
4923  C CD1 . LEU A 668  ? 0.4883 0.4699 0.4711 0.0217  0.0203  0.0123  666  LEU A CD1 
4924  C CD2 . LEU A 668  ? 0.5025 0.4762 0.4888 0.0196  0.0179  0.0107  666  LEU A CD2 
4925  N N   . ASN A 669  ? 0.2834 0.2657 0.2646 0.0274  0.0160  -0.0010 667  ASN A N   
4926  C CA  . ASN A 669  ? 0.3010 0.2831 0.2807 0.0279  0.0148  -0.0033 667  ASN A CA  
4927  C C   . ASN A 669  ? 0.2721 0.2604 0.2492 0.0306  0.0155  -0.0052 667  ASN A C   
4928  O O   . ASN A 669  ? 0.2943 0.2840 0.2690 0.0308  0.0153  -0.0055 667  ASN A O   
4929  C CB  . ASN A 669  ? 0.3083 0.2863 0.2909 0.0278  0.0125  -0.0065 667  ASN A CB  
4930  C CG  . ASN A 669  ? 0.3432 0.3156 0.3280 0.0250  0.0118  -0.0042 667  ASN A CG  
4931  O OD1 . ASN A 669  ? 0.3967 0.3680 0.3802 0.0232  0.0126  -0.0011 667  ASN A OD1 
4932  N ND2 . ASN A 669  ? 0.3791 0.3483 0.3674 0.0248  0.0101  -0.0058 667  ASN A ND2 
4933  N N   . ALA A 670  ? 0.2637 0.2562 0.2411 0.0326  0.0163  -0.0066 668  ALA A N   
4934  C CA  . ALA A 670  ? 0.2782 0.2779 0.2530 0.0353  0.0171  -0.0084 668  ALA A CA  
4935  C C   . ALA A 670  ? 0.2845 0.2880 0.2562 0.0347  0.0190  -0.0040 668  ALA A C   
4936  O O   . ALA A 670  ? 0.2678 0.2756 0.2365 0.0360  0.0192  -0.0045 668  ALA A O   
4937  C CB  . ALA A 670  ? 0.2940 0.2979 0.2701 0.0377  0.0176  -0.0108 668  ALA A CB  
4938  N N   . ILE A 671  ? 0.2625 0.2645 0.2351 0.0328  0.0203  0.0003  669  ILE A N   
4939  C CA  . ILE A 671  ? 0.2472 0.2521 0.2179 0.0320  0.0219  0.0047  669  ILE A CA  
4940  C C   . ILE A 671  ? 0.2859 0.2883 0.2549 0.0309  0.0209  0.0053  669  ILE A C   
4941  O O   . ILE A 671  ? 0.2804 0.2870 0.2468 0.0317  0.0215  0.0065  669  ILE A O   
4942  C CB  . ILE A 671  ? 0.2638 0.2665 0.2367 0.0299  0.0229  0.0089  669  ILE A CB  
4943  C CG1 . ILE A 671  ? 0.2866 0.2933 0.2609 0.0311  0.0242  0.0089  669  ILE A CG1 
4944  C CG2 . ILE A 671  ? 0.3036 0.3078 0.2754 0.0287  0.0240  0.0134  669  ILE A CG2 
4945  C CD1 . ILE A 671  ? 0.3183 0.3219 0.2955 0.0290  0.0248  0.0121  669  ILE A CD1 
4946  N N   . ALA A 672  ? 0.2880 0.2838 0.2586 0.0291  0.0195  0.0045  670  ALA A N   
4947  C CA  . ALA A 672  ? 0.2723 0.2656 0.2416 0.0280  0.0186  0.0050  670  ALA A CA  
4948  C C   . ALA A 672  ? 0.2878 0.2839 0.2549 0.0299  0.0176  0.0015  670  ALA A C   
4949  O O   . ALA A 672  ? 0.2867 0.2843 0.2517 0.0299  0.0176  0.0025  670  ALA A O   
4950  C CB  . ALA A 672  ? 0.3149 0.3014 0.2865 0.0258  0.0173  0.0047  670  ALA A CB  
4951  N N   . GLU A 673  ? 0.2622 0.2595 0.2301 0.0318  0.0168  -0.0026 671  GLU A N   
4952  C CA  A GLU A 673  ? 0.2503 0.2509 0.2164 0.0339  0.0157  -0.0066 671  GLU A CA  
4953  C CA  B GLU A 673  ? 0.2506 0.2511 0.2167 0.0338  0.0157  -0.0065 671  GLU A CA  
4954  C C   . GLU A 673  ? 0.2684 0.2767 0.2311 0.0358  0.0171  -0.0053 671  GLU A C   
4955  O O   . GLU A 673  ? 0.2607 0.2714 0.2210 0.0364  0.0166  -0.0058 671  GLU A O   
4956  C CB  A GLU A 673  ? 0.2736 0.2739 0.2419 0.0356  0.0145  -0.0114 671  GLU A CB  
4957  C CB  B GLU A 673  ? 0.2746 0.2747 0.2429 0.0355  0.0143  -0.0115 671  GLU A CB  
4958  C CG  A GLU A 673  ? 0.3361 0.3403 0.3031 0.0381  0.0132  -0.0162 671  GLU A CG  
4959  C CG  B GLU A 673  ? 0.3365 0.3418 0.3029 0.0383  0.0134  -0.0158 671  GLU A CG  
4960  C CD  A GLU A 673  ? 0.3044 0.3036 0.2731 0.0372  0.0108  -0.0189 671  GLU A CD  
4961  C CD  B GLU A 673  ? 0.3186 0.3204 0.2877 0.0389  0.0108  -0.0210 671  GLU A CD  
4962  O OE1 A GLU A 673  ? 0.3378 0.3305 0.3088 0.0346  0.0101  -0.0172 671  GLU A OE1 
4963  O OE1 B GLU A 673  ? 0.3002 0.2973 0.2731 0.0380  0.0100  -0.0218 671  GLU A OE1 
4964  O OE2 A GLU A 673  ? 0.3039 0.3059 0.2716 0.0390  0.0095  -0.0228 671  GLU A OE2 
4965  O OE2 B GLU A 673  ? 0.2987 0.3026 0.2665 0.0402  0.0096  -0.0241 671  GLU A OE2 
4966  N N   . VAL A 674  ? 0.2491 0.2619 0.2116 0.0366  0.0189  -0.0035 672  VAL A N   
4967  C CA  . VAL A 674  ? 0.2471 0.2682 0.2065 0.0383  0.0204  -0.0017 672  VAL A CA  
4968  C C   . VAL A 674  ? 0.2793 0.2998 0.2373 0.0365  0.0211  0.0034  672  VAL A C   
4969  O O   . VAL A 674  ? 0.2554 0.2807 0.2106 0.0376  0.0212  0.0042  672  VAL A O   
4970  C CB  . VAL A 674  ? 0.2726 0.2990 0.2324 0.0395  0.0223  -0.0005 672  VAL A CB  
4971  C CG1 . VAL A 674  ? 0.2494 0.2850 0.2059 0.0411  0.0239  0.0020  672  VAL A CG1 
4972  C CG2 . VAL A 674  ? 0.2583 0.2855 0.2197 0.0416  0.0214  -0.0060 672  VAL A CG2 
4973  N N   . ARG A 675  ? 0.2707 0.2854 0.2310 0.0339  0.0213  0.0068  673  ARG A N   
4974  C CA  . ARG A 675  ? 0.2215 0.2349 0.1814 0.0322  0.0216  0.0111  673  ARG A CA  
4975  C C   . ARG A 675  ? 0.2316 0.2434 0.1898 0.0323  0.0201  0.0092  673  ARG A C   
4976  O O   . ARG A 675  ? 0.2581 0.2729 0.2145 0.0325  0.0203  0.0117  673  ARG A O   
4977  C CB  . ARG A 675  ? 0.2227 0.2296 0.1856 0.0295  0.0217  0.0137  673  ARG A CB  
4978  C CG  . ARG A 675  ? 0.2652 0.2740 0.2299 0.0290  0.0233  0.0169  673  ARG A CG  
4979  C CD  . ARG A 675  ? 0.2789 0.2816 0.2464 0.0264  0.0231  0.0195  673  ARG A CD  
4980  N NE  . ARG A 675  ? 0.2690 0.2713 0.2364 0.0253  0.0231  0.0229  673  ARG A NE  
4981  C CZ  . ARG A 675  ? 0.2918 0.2888 0.2614 0.0232  0.0225  0.0245  673  ARG A CZ  
4982  N NH1 . ARG A 675  ? 0.2695 0.2616 0.2411 0.0219  0.0220  0.0231  673  ARG A NH1 
4983  N NH2 . ARG A 675  ? 0.2504 0.2474 0.2201 0.0226  0.0224  0.0275  673  ARG A NH2 
4984  N N   . GLU A 676  ? 0.2481 0.2554 0.2072 0.0321  0.0184  0.0051  674  GLU A N   
4985  C CA  . GLU A 676  ? 0.2650 0.2708 0.2230 0.0321  0.0168  0.0031  674  GLU A CA  
4986  C C   . GLU A 676  ? 0.2396 0.2524 0.1943 0.0346  0.0167  0.0013  674  GLU A C   
4987  O O   . GLU A 676  ? 0.2468 0.2609 0.1997 0.0347  0.0162  0.0022  674  GLU A O   
4988  C CB  . GLU A 676  ? 0.2399 0.2403 0.2001 0.0314  0.0150  -0.0009 674  GLU A CB  
4989  C CG  . GLU A 676  ? 0.3088 0.3064 0.2685 0.0306  0.0135  -0.0021 674  GLU A CG  
4990  C CD  . GLU A 676  ? 0.5205 0.5122 0.4823 0.0279  0.0132  0.0003  674  GLU A CD  
4991  O OE1 . GLU A 676  ? 0.6300 0.6201 0.5931 0.0267  0.0144  0.0033  674  GLU A OE1 
4992  O OE2 . GLU A 676  ? 0.4420 0.4308 0.4043 0.0270  0.0119  -0.0010 674  GLU A OE2 
4993  N N   . ALA A 677  ? 0.2542 0.2720 0.2083 0.0369  0.0171  -0.0014 675  ALA A N   
4994  C CA  . ALA A 677  ? 0.2307 0.2562 0.1816 0.0396  0.0170  -0.0034 675  ALA A CA  
4995  C C   . ALA A 677  ? 0.2576 0.2886 0.2061 0.0397  0.0186  0.0019  675  ALA A C   
4996  O O   . ALA A 677  ? 0.2581 0.2929 0.2040 0.0406  0.0181  0.0021  675  ALA A O   
4997  C CB  . ALA A 677  ? 0.2335 0.2636 0.1843 0.0421  0.0172  -0.0074 675  ALA A CB  
4998  N N   . ILE A 678  ? 0.2459 0.2774 0.1955 0.0386  0.0203  0.0064  676  ILE A N   
4999  C CA  . ILE A 678  ? 0.2530 0.2892 0.2012 0.0384  0.0218  0.0121  676  ILE A CA  
5000  C C   . ILE A 678  ? 0.2391 0.2712 0.1876 0.0367  0.0208  0.0147  676  ILE A C   
5001  O O   . ILE A 678  ? 0.2520 0.2888 0.1984 0.0374  0.0210  0.0173  676  ILE A O   
5002  C CB  . ILE A 678  ? 0.2478 0.2840 0.1984 0.0372  0.0236  0.0163  676  ILE A CB  
5003  C CG1 . ILE A 678  ? 0.2642 0.3063 0.2143 0.0393  0.0247  0.0140  676  ILE A CG1 
5004  C CG2 . ILE A 678  ? 0.2580 0.2972 0.2086 0.0362  0.0247  0.0229  676  ILE A CG2 
5005  C CD1 . ILE A 678  ? 0.2412 0.2816 0.1944 0.0379  0.0261  0.0167  676  ILE A CD1 
5006  N N   . ASP A 679  ? 0.2398 0.2634 0.1908 0.0346  0.0199  0.0140  677  ASP A N   
5007  C CA  . ASP A 679  ? 0.2439 0.2634 0.1955 0.0330  0.0190  0.0161  677  ASP A CA  
5008  C C   . ASP A 679  ? 0.2592 0.2804 0.2084 0.0342  0.0174  0.0131  677  ASP A C   
5009  O O   . ASP A 679  ? 0.2546 0.2771 0.2028 0.0341  0.0171  0.0157  677  ASP A O   
5010  C CB  . ASP A 679  ? 0.2486 0.2597 0.2035 0.0306  0.0183  0.0156  677  ASP A CB  
5011  C CG  . ASP A 679  ? 0.2929 0.3023 0.2504 0.0291  0.0197  0.0191  677  ASP A CG  
5012  O OD1 . ASP A 679  ? 0.3170 0.3303 0.2744 0.0293  0.0209  0.0234  677  ASP A OD1 
5013  O OD2 . ASP A 679  ? 0.3600 0.3640 0.3198 0.0277  0.0194  0.0179  677  ASP A OD2 
5014  N N   . PHE A 680  ? 0.2495 0.2706 0.1981 0.0354  0.0163  0.0076  678  PHE A N   
5015  C CA  . PHE A 680  ? 0.2523 0.2758 0.1986 0.0369  0.0148  0.0043  678  PHE A CA  
5016  C C   . PHE A 680  ? 0.2755 0.3078 0.2185 0.0389  0.0155  0.0063  678  PHE A C   
5017  O O   . PHE A 680  ? 0.2514 0.2852 0.1928 0.0391  0.0147  0.0075  678  PHE A O   
5018  C CB  . PHE A 680  ? 0.2467 0.2699 0.1933 0.0382  0.0135  -0.0020 678  PHE A CB  
5019  C CG  . PHE A 680  ? 0.2427 0.2580 0.1923 0.0364  0.0120  -0.0046 678  PHE A CG  
5020  C CD1 . PHE A 680  ? 0.2650 0.2764 0.2152 0.0349  0.0109  -0.0039 678  PHE A CD1 
5021  C CD2 . PHE A 680  ? 0.2414 0.2534 0.1934 0.0362  0.0116  -0.0077 678  PHE A CD2 
5022  C CE1 . PHE A 680  ? 0.2776 0.2825 0.2305 0.0332  0.0095  -0.0061 678  PHE A CE1 
5023  C CE2 . PHE A 680  ? 0.2662 0.2714 0.2212 0.0345  0.0101  -0.0096 678  PHE A CE2 
5024  C CZ  . PHE A 680  ? 0.2852 0.2870 0.2406 0.0329  0.0092  -0.0087 678  PHE A CZ  
5025  N N   . LEU A 681  ? 0.2544 0.2930 0.1961 0.0405  0.0169  0.0068  679  LEU A N   
5026  C CA  . LEU A 681  ? 0.2350 0.2831 0.1733 0.0425  0.0177  0.0090  679  LEU A CA  
5027  C C   . LEU A 681  ? 0.2727 0.3210 0.2111 0.0412  0.0183  0.0156  679  LEU A C   
5028  O O   . LEU A 681  ? 0.2623 0.3147 0.1985 0.0421  0.0177  0.0168  679  LEU A O   
5029  C CB  . LEU A 681  ? 0.2663 0.3210 0.2039 0.0441  0.0195  0.0091  679  LEU A CB  
5030  C CG  . LEU A 681  ? 0.2720 0.3283 0.2092 0.0462  0.0187  0.0020  679  LEU A CG  
5031  C CD1 . LEU A 681  ? 0.2557 0.3157 0.1937 0.0471  0.0204  0.0022  679  LEU A CD1 
5032  C CD2 . LEU A 681  ? 0.2803 0.3445 0.2139 0.0491  0.0177  -0.0016 679  LEU A CD2 
5033  N N   . ARG A 682  ? 0.2505 0.2943 0.1920 0.0389  0.0193  0.0198  680  ARG A N   
5034  C CA  . ARG A 682  ? 0.2438 0.2877 0.1863 0.0377  0.0197  0.0262  680  ARG A CA  
5035  C C   . ARG A 682  ? 0.2739 0.3121 0.2173 0.0365  0.0180  0.0260  680  ARG A C   
5036  O O   . ARG A 682  ? 0.2669 0.3075 0.2098 0.0365  0.0177  0.0298  680  ARG A O   
5037  C CB  . ARG A 682  ? 0.2388 0.2794 0.1847 0.0357  0.0211  0.0304  680  ARG A CB  
5038  C CG  . ARG A 682  ? 0.2721 0.3201 0.2173 0.0368  0.0230  0.0324  680  ARG A CG  
5039  C CD  . ARG A 682  ? 0.2717 0.3160 0.2207 0.0348  0.0241  0.0360  680  ARG A CD  
5040  N NE  . ARG A 682  ? 0.2717 0.3234 0.2202 0.0359  0.0260  0.0380  680  ARG A NE  
5041  C CZ  . ARG A 682  ? 0.3293 0.3793 0.2808 0.0346  0.0272  0.0399  680  ARG A CZ  
5042  N NH1 . ARG A 682  ? 0.2789 0.3202 0.2339 0.0324  0.0266  0.0399  680  ARG A NH1 
5043  N NH2 . ARG A 682  ? 0.3172 0.3749 0.2680 0.0358  0.0290  0.0417  680  ARG A NH2 
5044  N N   . TYR A 683  ? 0.2540 0.2851 0.1989 0.0354  0.0169  0.0218  681  TYR A N   
5045  C CA  . TYR A 683  ? 0.2253 0.2514 0.1711 0.0344  0.0153  0.0213  681  TYR A CA  
5046  C C   . TYR A 683  ? 0.2614 0.2922 0.2040 0.0362  0.0141  0.0192  681  TYR A C   
5047  O O   . TYR A 683  ? 0.2480 0.2794 0.1905 0.0360  0.0134  0.0219  681  TYR A O   
5048  C CB  . TYR A 683  ? 0.2421 0.2605 0.1902 0.0329  0.0145  0.0173  681  TYR A CB  
5049  C CG  . TYR A 683  ? 0.2415 0.2553 0.1906 0.0318  0.0129  0.0164  681  TYR A CG  
5050  C CD1 . TYR A 683  ? 0.2524 0.2622 0.2040 0.0301  0.0129  0.0200  681  TYR A CD1 
5051  C CD2 . TYR A 683  ? 0.2337 0.2474 0.1815 0.0326  0.0114  0.0118  681  TYR A CD2 
5052  C CE1 . TYR A 683  ? 0.2289 0.2351 0.1816 0.0292  0.0115  0.0189  681  TYR A CE1 
5053  C CE2 . TYR A 683  ? 0.2558 0.2659 0.2047 0.0316  0.0100  0.0111  681  TYR A CE2 
5054  C CZ  . TYR A 683  ? 0.2439 0.2504 0.1951 0.0300  0.0101  0.0146  681  TYR A CZ  
5055  O OH  . TYR A 683  ? 0.2887 0.2921 0.2410 0.0291  0.0088  0.0137  681  TYR A OH  
5056  N N   . TYR A 684  ? 0.2359 0.2703 0.1763 0.0381  0.0136  0.0142  682  TYR A N   
5057  C CA  . TYR A 684  ? 0.2271 0.2663 0.1646 0.0399  0.0123  0.0118  682  TYR A CA  
5058  C C   . TYR A 684  ? 0.2821 0.3299 0.2169 0.0414  0.0131  0.0162  682  TYR A C   
5059  O O   . TYR A 684  ? 0.2479 0.2986 0.1809 0.0422  0.0120  0.0167  682  TYR A O   
5060  C CB  . TYR A 684  ? 0.2533 0.2945 0.1895 0.0417  0.0114  0.0052  682  TYR A CB  
5061  C CG  . TYR A 684  ? 0.2411 0.2741 0.1802 0.0401  0.0102  0.0010  682  TYR A CG  
5062  C CD1 . TYR A 684  ? 0.2451 0.2719 0.1863 0.0382  0.0091  0.0014  682  TYR A CD1 
5063  C CD2 . TYR A 684  ? 0.2471 0.2791 0.1872 0.0407  0.0101  -0.0033 682  TYR A CD2 
5064  C CE1 . TYR A 684  ? 0.2537 0.2737 0.1977 0.0367  0.0080  -0.0019 682  TYR A CE1 
5065  C CE2 . TYR A 684  ? 0.2197 0.2445 0.1628 0.0392  0.0089  -0.0066 682  TYR A CE2 
5066  C CZ  . TYR A 684  ? 0.2538 0.2727 0.1988 0.0371  0.0079  -0.0057 682  TYR A CZ  
5067  O OH  . TYR A 684  ? 0.2668 0.2792 0.2148 0.0356  0.0068  -0.0085 682  TYR A OH  
5068  N N   . ALA A 685  ? 0.2405 0.2926 0.1750 0.0417  0.0150  0.0197  683  ALA A N   
5069  C CA  . ALA A 685  ? 0.2546 0.3148 0.1871 0.0428  0.0158  0.0251  683  ALA A CA  
5070  C C   . ALA A 685  ? 0.2726 0.3293 0.2072 0.0411  0.0153  0.0305  683  ALA A C   
5071  O O   . ALA A 685  ? 0.2549 0.3164 0.1877 0.0421  0.0147  0.0329  683  ALA A O   
5072  C CB  . ALA A 685  ? 0.2637 0.3286 0.1964 0.0430  0.0180  0.0284  683  ALA A CB  
5073  N N   . GLU A 686  ? 0.2476 0.2962 0.1863 0.0387  0.0155  0.0324  684  GLU A N   
5074  C CA  . GLU A 686  ? 0.2552 0.3002 0.1965 0.0372  0.0149  0.0372  684  GLU A CA  
5075  C C   . GLU A 686  ? 0.2935 0.3357 0.2344 0.0373  0.0129  0.0344  684  GLU A C   
5076  O O   . GLU A 686  ? 0.2836 0.3277 0.2246 0.0376  0.0121  0.0378  684  GLU A O   
5077  C CB  . GLU A 686  ? 0.2626 0.2997 0.2085 0.0347  0.0154  0.0391  684  GLU A CB  
5078  C CG  . GLU A 686  ? 0.3410 0.3733 0.2905 0.0332  0.0144  0.0429  684  GLU A CG  
5079  C CD  . GLU A 686  ? 0.3913 0.4289 0.3414 0.0336  0.0146  0.0497  684  GLU A CD  
5080  O OE1 . GLU A 686  ? 0.3619 0.4072 0.3100 0.0347  0.0158  0.0526  684  GLU A OE1 
5081  O OE2 . GLU A 686  ? 0.3967 0.4310 0.3497 0.0327  0.0134  0.0524  684  GLU A OE2 
5082  N N   . GLN A 687  ? 0.2537 0.2918 0.1942 0.0372  0.0120  0.0282  685  GLN A N   
5083  C CA  . GLN A 687  ? 0.2418 0.2775 0.1821 0.0373  0.0101  0.0254  685  GLN A CA  
5084  C C   . GLN A 687  ? 0.2639 0.3078 0.2005 0.0396  0.0093  0.0252  685  GLN A C   
5085  O O   . GLN A 687  ? 0.2708 0.3147 0.2074 0.0398  0.0080  0.0261  685  GLN A O   
5086  C CB  . GLN A 687  ? 0.2290 0.2597 0.1699 0.0368  0.0093  0.0191  685  GLN A CB  
5087  C CG  . GLN A 687  ? 0.2471 0.2696 0.1918 0.0344  0.0097  0.0193  685  GLN A CG  
5088  C CD  . GLN A 687  ? 0.2866 0.3048 0.2341 0.0329  0.0090  0.0224  685  GLN A CD  
5089  O OE1 . GLN A 687  ? 0.2994 0.3171 0.2468 0.0331  0.0076  0.0211  685  GLN A OE1 
5090  N NE2 . GLN A 687  ? 0.3508 0.3662 0.3010 0.0316  0.0100  0.0264  685  GLN A NE2 
5091  N N   . THR A 688  ? 0.2424 0.2935 0.1758 0.0415  0.0101  0.0239  686  THR A N   
5092  C CA  . THR A 688  ? 0.2374 0.2975 0.1669 0.0439  0.0095  0.0240  686  THR A CA  
5093  C C   . THR A 688  ? 0.2518 0.3157 0.1815 0.0438  0.0098  0.0313  686  THR A C   
5094  O O   . THR A 688  ? 0.2839 0.3507 0.2124 0.0447  0.0085  0.0322  686  THR A O   
5095  C CB  . THR A 688  ? 0.2629 0.3306 0.1891 0.0461  0.0105  0.0214  686  THR A CB  
5096  O OG1 . THR A 688  ? 0.2699 0.3344 0.1963 0.0464  0.0096  0.0141  686  THR A OG1 
5097  C CG2 . THR A 688  ? 0.2496 0.3281 0.1717 0.0486  0.0101  0.0224  686  THR A CG2 
5098  N N   . ARG A 689  ? 0.2793 0.3432 0.2108 0.0428  0.0115  0.0367  687  ARG A N   
5099  C CA  . ARG A 689  ? 0.2661 0.3335 0.1987 0.0426  0.0118  0.0442  687  ARG A CA  
5100  C C   . ARG A 689  ? 0.2799 0.3408 0.2158 0.0412  0.0101  0.0460  687  ARG A C   
5101  O O   . ARG A 689  ? 0.3056 0.3698 0.2418 0.0416  0.0095  0.0510  687  ARG A O   
5102  C CB  . ARG A 689  ? 0.2822 0.3497 0.2173 0.0413  0.0137  0.0494  687  ARG A CB  
5103  C CG  . ARG A 689  ? 0.3111 0.3877 0.2430 0.0430  0.0154  0.0494  687  ARG A CG  
5104  C CD  . ARG A 689  ? 0.3071 0.3844 0.2420 0.0416  0.0172  0.0557  687  ARG A CD  
5105  N NE  . ARG A 689  ? 0.3253 0.3931 0.2641 0.0395  0.0176  0.0541  687  ARG A NE  
5106  C CZ  . ARG A 689  ? 0.3679 0.4353 0.3064 0.0395  0.0189  0.0510  687  ARG A CZ  
5107  N NH1 . ARG A 689  ? 0.3628 0.4385 0.2975 0.0416  0.0199  0.0489  687  ARG A NH1 
5108  N NH2 . ARG A 689  ? 0.3278 0.3865 0.2699 0.0375  0.0191  0.0499  687  ARG A NH2 
5109  N N   . ARG A 690  ? 0.2735 0.3254 0.2119 0.0397  0.0094  0.0420  688  ARG A N   
5110  C CA  . ARG A 690  ? 0.2767 0.3226 0.2182 0.0385  0.0079  0.0428  688  ARG A CA  
5111  C C   . ARG A 690  ? 0.3110 0.3588 0.2501 0.0398  0.0061  0.0393  688  ARG A C   
5112  O O   . ARG A 690  ? 0.2926 0.3377 0.2339 0.0394  0.0047  0.0410  688  ARG A O   
5113  C CB  . ARG A 690  ? 0.2517 0.2880 0.1967 0.0364  0.0079  0.0400  688  ARG A CB  
5114  C CG  . ARG A 690  ? 0.3091 0.3422 0.2575 0.0348  0.0094  0.0435  688  ARG A CG  
5115  C CD  . ARG A 690  ? 0.3801 0.4117 0.3325 0.0339  0.0090  0.0498  688  ARG A CD  
5116  N NE  . ARG A 690  ? 0.3566 0.3822 0.3121 0.0331  0.0073  0.0486  688  ARG A NE  
5117  C CZ  . ARG A 690  ? 0.3756 0.4027 0.3314 0.0338  0.0058  0.0505  688  ARG A CZ  
5118  N NH1 . ARG A 690  ? 0.3814 0.4160 0.3348 0.0353  0.0057  0.0541  688  ARG A NH1 
5119  N NH2 . ARG A 690  ? 0.3422 0.3638 0.3009 0.0331  0.0044  0.0487  688  ARG A NH2 
5120  N N   . THR A 691  ? 0.2657 0.3178 0.2009 0.0414  0.0058  0.0342  689  THR A N   
5121  C CA  . THR A 691  ? 0.2509 0.3028 0.1849 0.0422  0.0039  0.0299  689  THR A CA  
5122  C C   . THR A 691  ? 0.3358 0.3970 0.2653 0.0448  0.0031  0.0282  689  THR A C   
5123  O O   . THR A 691  ? 0.3424 0.4057 0.2712 0.0455  0.0015  0.0285  689  THR A O   
5124  C CB  . THR A 691  ? 0.2596 0.3052 0.1947 0.0412  0.0034  0.0233  689  THR A CB  
5125  O OG1 . THR A 691  ? 0.3057 0.3538 0.2389 0.0420  0.0045  0.0202  689  THR A OG1 
5126  C CG2 . THR A 691  ? 0.3079 0.3444 0.2475 0.0387  0.0037  0.0244  689  THR A CG2 
5127  N N   . LEU A 692  ? 0.2928 0.3598 0.2192 0.0462  0.0041  0.0260  690  LEU A N   
5128  C CA  . LEU A 692  ? 0.2856 0.3601 0.2078 0.0487  0.0030  0.0217  690  LEU A CA  
5129  C C   . LEU A 692  ? 0.3313 0.4154 0.2505 0.0505  0.0028  0.0264  690  LEU A C   
5130  O O   . LEU A 692  ? 0.3429 0.4316 0.2617 0.0507  0.0043  0.0322  690  LEU A O   
5131  C CB  . LEU A 692  ? 0.3100 0.3877 0.2301 0.0499  0.0039  0.0169  690  LEU A CB  
5132  C CG  . LEU A 692  ? 0.3182 0.3872 0.2411 0.0485  0.0035  0.0112  690  LEU A CG  
5133  C CD1 . LEU A 692  ? 0.3145 0.3874 0.2354 0.0502  0.0039  0.0059  690  LEU A CD1 
5134  C CD2 . LEU A 692  ? 0.3561 0.4204 0.2804 0.0479  0.0013  0.0073  690  LEU A CD2 
5135  N N   . GLY A 693  ? 0.2849 0.3723 0.2023 0.0519  0.0008  0.0239  691  GLY A N   
5136  C CA  . GLY A 693  ? 0.3235 0.4201 0.2379 0.0537  0.0003  0.0278  691  GLY A CA  
5137  C C   . GLY A 693  ? 0.3704 0.4743 0.2807 0.0563  -0.0012 0.0217  691  GLY A C   
5138  O O   . GLY A 693  ? 0.3698 0.4714 0.2800 0.0566  -0.0018 0.0145  691  GLY A O   
5139  N N   . PRO A 694  ? 0.3617 0.4746 0.2690 0.0581  -0.0021 0.0245  692  PRO A N   
5140  C CA  . PRO A 694  ? 0.3838 0.5053 0.2868 0.0609  -0.0035 0.0187  692  PRO A CA  
5141  C C   . PRO A 694  ? 0.3713 0.4874 0.2756 0.0607  -0.0059 0.0115  692  PRO A C   
5142  O O   . PRO A 694  ? 0.4248 0.5451 0.3269 0.0625  -0.0069 0.0045  692  PRO A O   
5143  C CB  . PRO A 694  ? 0.4507 0.5820 0.3508 0.0625  -0.0040 0.0247  692  PRO A CB  
5144  C CG  . PRO A 694  ? 0.4274 0.5574 0.3297 0.0609  -0.0021 0.0337  692  PRO A CG  
5145  C CD  . PRO A 694  ? 0.3573 0.4740 0.2649 0.0579  -0.0016 0.0334  692  PRO A CD  
5146  N N   . GLY A 695  ? 0.3264 0.4336 0.2347 0.0586  -0.0068 0.0127  693  GLY A N   
5147  C CA  . GLY A 695  ? 0.3993 0.5017 0.3092 0.0582  -0.0090 0.0063  693  GLY A CA  
5148  C C   . GLY A 695  ? 0.3792 0.4733 0.2919 0.0567  -0.0088 0.0006  693  GLY A C   
5149  O O   . GLY A 695  ? 0.3948 0.4850 0.3093 0.0562  -0.0106 -0.0047 693  GLY A O   
5150  N N   . HIS A 696  ? 0.3556 0.4471 0.2690 0.0558  -0.0066 0.0018  694  HIS A N   
5151  C CA  . HIS A 696  ? 0.3370 0.4210 0.2532 0.0544  -0.0064 -0.0032 694  HIS A CA  
5152  C C   . HIS A 696  ? 0.3985 0.4887 0.3120 0.0566  -0.0064 -0.0085 694  HIS A C   
5153  O O   . HIS A 696  ? 0.3651 0.4566 0.2779 0.0569  -0.0045 -0.0076 694  HIS A O   
5154  C CB  . HIS A 696  ? 0.3545 0.4310 0.2737 0.0520  -0.0043 0.0013  694  HIS A CB  
5155  C CG  . HIS A 696  ? 0.3103 0.3827 0.2318 0.0503  -0.0043 0.0072  694  HIS A CG  
5156  N ND1 . HIS A 696  ? 0.3487 0.4232 0.2701 0.0501  -0.0028 0.0144  694  HIS A ND1 
5157  C CD2 . HIS A 696  ? 0.3248 0.3916 0.2492 0.0489  -0.0057 0.0069  694  HIS A CD2 
5158  C CE1 . HIS A 696  ? 0.3429 0.4127 0.2672 0.0487  -0.0034 0.0180  694  HIS A CE1 
5159  N NE2 . HIS A 696  ? 0.3449 0.4102 0.2709 0.0481  -0.0050 0.0135  694  HIS A NE2 
5160  N N   . GLY A 697  ? 0.3589 0.4535 0.2709 0.0584  -0.0086 -0.0142 695  GLY A N   
5161  C CA  . GLY A 697  ? 0.3572 0.4590 0.2665 0.0611  -0.0090 -0.0198 695  GLY A CA  
5162  C C   . GLY A 697  ? 0.3341 0.4296 0.2465 0.0602  -0.0089 -0.0251 695  GLY A C   
5163  O O   . GLY A 697  ? 0.3399 0.4260 0.2564 0.0579  -0.0097 -0.0269 695  GLY A O   
5164  N N   . PRO A 698  ? 0.3400 0.4408 0.2505 0.0621  -0.0080 -0.0276 696  PRO A N   
5165  C CA  . PRO A 698  ? 0.3164 0.4115 0.2301 0.0616  -0.0081 -0.0329 696  PRO A CA  
5166  C C   . PRO A 698  ? 0.3024 0.3947 0.2187 0.0619  -0.0112 -0.0407 696  PRO A C   
5167  O O   . PRO A 698  ? 0.3485 0.4463 0.2631 0.0635  -0.0132 -0.0436 696  PRO A O   
5168  C CB  . PRO A 698  ? 0.3927 0.4966 0.3033 0.0643  -0.0068 -0.0343 696  PRO A CB  
5169  C CG  . PRO A 698  ? 0.4654 0.5774 0.3718 0.0651  -0.0050 -0.0272 696  PRO A CG  
5170  C CD  . PRO A 698  ? 0.4548 0.5672 0.3605 0.0648  -0.0066 -0.0252 696  PRO A CD  
5171  N N   . LEU A 699  ? 0.2964 0.3802 0.2172 0.0602  -0.0116 -0.0439 697  LEU A N   
5172  C CA  . LEU A 699  ? 0.3157 0.3969 0.2398 0.0605  -0.0146 -0.0516 697  LEU A CA  
5173  C C   . LEU A 699  ? 0.3010 0.3909 0.2231 0.0641  -0.0158 -0.0582 697  LEU A C   
5174  O O   . LEU A 699  ? 0.3098 0.4028 0.2323 0.0656  -0.0185 -0.0639 697  LEU A O   
5175  C CB  . LEU A 699  ? 0.2904 0.3610 0.2200 0.0579  -0.0146 -0.0529 697  LEU A CB  
5176  C CG  . LEU A 699  ? 0.3201 0.3819 0.2523 0.0543  -0.0137 -0.0475 697  LEU A CG  
5177  C CD1 . LEU A 699  ? 0.3165 0.3695 0.2537 0.0522  -0.0138 -0.0492 697  LEU A CD1 
5178  C CD2 . LEU A 699  ? 0.3418 0.4026 0.2749 0.0535  -0.0157 -0.0480 697  LEU A CD2 
5179  N N   . GLY A 700  ? 0.2797 0.3738 0.1999 0.0656  -0.0139 -0.0578 698  GLY A N   
5180  C CA  . GLY A 700  ? 0.2885 0.3899 0.2078 0.0690  -0.0150 -0.0649 698  GLY A CA  
5181  C C   . GLY A 700  ? 0.2916 0.3881 0.2141 0.0686  -0.0141 -0.0669 698  GLY A C   
5182  O O   . GLY A 700  ? 0.3082 0.3980 0.2323 0.0661  -0.0120 -0.0616 698  GLY A O   
5183  N N   . PRO A 701  ? 0.2992 0.3989 0.2233 0.0711  -0.0159 -0.0748 699  PRO A N   
5184  C CA  . PRO A 701  ? 0.2856 0.3810 0.2130 0.0710  -0.0152 -0.0769 699  PRO A CA  
5185  C C   . PRO A 701  ? 0.2912 0.3733 0.2244 0.0672  -0.0155 -0.0751 699  PRO A C   
5186  O O   . PRO A 701  ? 0.3092 0.3856 0.2462 0.0657  -0.0180 -0.0777 699  PRO A O   
5187  C CB  . PRO A 701  ? 0.3146 0.4150 0.2436 0.0744  -0.0180 -0.0867 699  PRO A CB  
5188  C CG  . PRO A 701  ? 0.3553 0.4670 0.2793 0.0772  -0.0189 -0.0884 699  PRO A CG  
5189  C CD  . PRO A 701  ? 0.3141 0.4221 0.2369 0.0745  -0.0186 -0.0822 699  PRO A CD  
5190  N N   . ILE A 702  ? 0.3228 0.4004 0.2567 0.0655  -0.0130 -0.0704 700  ILE A N   
5191  C CA  A ILE A 702  ? 0.2808 0.3466 0.2198 0.0619  -0.0130 -0.0681 700  ILE A CA  
5192  C CA  B ILE A 702  ? 0.2812 0.3470 0.2201 0.0618  -0.0129 -0.0680 700  ILE A CA  
5193  C C   . ILE A 702  ? 0.2885 0.3512 0.2312 0.0624  -0.0131 -0.0717 700  ILE A C   
5194  O O   . ILE A 702  ? 0.2915 0.3594 0.2319 0.0642  -0.0112 -0.0712 700  ILE A O   
5195  C CB  A ILE A 702  ? 0.2826 0.3448 0.2197 0.0591  -0.0101 -0.0593 700  ILE A CB  
5196  C CB  B ILE A 702  ? 0.2826 0.3450 0.2196 0.0592  -0.0100 -0.0591 700  ILE A CB  
5197  C CG1 A ILE A 702  ? 0.3024 0.3652 0.2376 0.0581  -0.0107 -0.0563 700  ILE A CG1 
5198  C CG1 B ILE A 702  ? 0.2935 0.3590 0.2271 0.0588  -0.0099 -0.0554 700  ILE A CG1 
5199  C CG2 A ILE A 702  ? 0.2961 0.3476 0.2381 0.0558  -0.0096 -0.0571 700  ILE A CG2 
5200  C CG2 B ILE A 702  ? 0.2944 0.3454 0.2364 0.0556  -0.0099 -0.0570 700  ILE A CG2 
5201  C CD1 A ILE A 702  ? 0.3031 0.3626 0.2370 0.0555  -0.0083 -0.0481 700  ILE A CD1 
5202  C CD1 B ILE A 702  ? 0.3183 0.3778 0.2551 0.0568  -0.0123 -0.0570 700  ILE A CD1 
5203  N N   . VAL A 703  ? 0.2779 0.3324 0.2267 0.0608  -0.0154 -0.0751 701  VAL A N   
5204  C CA  . VAL A 703  ? 0.2497 0.2999 0.2031 0.0609  -0.0159 -0.0782 701  VAL A CA  
5205  C C   . VAL A 703  ? 0.2773 0.3192 0.2325 0.0574  -0.0138 -0.0717 701  VAL A C   
5206  O O   . VAL A 703  ? 0.2720 0.3069 0.2295 0.0543  -0.0143 -0.0687 701  VAL A O   
5207  C CB  . VAL A 703  ? 0.2929 0.3389 0.2526 0.0611  -0.0198 -0.0853 701  VAL A CB  
5208  C CG1 . VAL A 703  ? 0.3055 0.3458 0.2706 0.0608  -0.0204 -0.0875 701  VAL A CG1 
5209  C CG2 . VAL A 703  ? 0.3246 0.3796 0.2826 0.0650  -0.0219 -0.0925 701  VAL A CG2 
5210  N N   . CYS A 704  ? 0.2699 0.3131 0.2240 0.0580  -0.0114 -0.0694 702  CYS A N   
5211  C CA  . CYS A 704  ? 0.2634 0.2994 0.2190 0.0549  -0.0094 -0.0635 702  CYS A CA  
5212  C C   . CYS A 704  ? 0.2606 0.2916 0.2217 0.0549  -0.0105 -0.0669 702  CYS A C   
5213  O O   . CYS A 704  ? 0.2786 0.3142 0.2395 0.0576  -0.0103 -0.0702 702  CYS A O   
5214  C CB  . CYS A 704  ? 0.2571 0.2980 0.2078 0.0553  -0.0059 -0.0577 702  CYS A CB  
5215  S SG  . CYS A 704  ? 0.2814 0.3281 0.2262 0.0552  -0.0047 -0.0529 702  CYS A SG  
5216  N N   . ILE A 705  ? 0.2489 0.2709 0.2150 0.0519  -0.0119 -0.0660 703  ILE A N   
5217  C CA  . ILE A 705  ? 0.2521 0.2683 0.2242 0.0514  -0.0133 -0.0686 703  ILE A CA  
5218  C C   . ILE A 705  ? 0.2459 0.2560 0.2188 0.0483  -0.0111 -0.0621 703  ILE A C   
5219  O O   . ILE A 705  ? 0.2873 0.2930 0.2601 0.0454  -0.0106 -0.0577 703  ILE A O   
5220  C CB  . ILE A 705  ? 0.2947 0.3058 0.2726 0.0505  -0.0169 -0.0729 703  ILE A CB  
5221  C CG1 . ILE A 705  ? 0.3393 0.3570 0.3166 0.0538  -0.0192 -0.0800 703  ILE A CG1 
5222  C CG2 . ILE A 705  ? 0.3114 0.3158 0.2961 0.0495  -0.0184 -0.0745 703  ILE A CG2 
5223  C CD1 . ILE A 705  ? 0.3536 0.3673 0.3360 0.0528  -0.0228 -0.0838 703  ILE A CD1 
5224  N N   . SER A 706  ? 0.2891 0.2994 0.2628 0.0491  -0.0098 -0.0618 704  SER A N   
5225  C CA  . SER A 706  ? 0.2979 0.3040 0.2713 0.0467  -0.0074 -0.0556 704  SER A CA  
5226  C C   . SER A 706  ? 0.3178 0.3177 0.2971 0.0457  -0.0085 -0.0566 704  SER A C   
5227  O O   . SER A 706  ? 0.2951 0.2953 0.2782 0.0477  -0.0106 -0.0622 704  SER A O   
5228  C CB  . SER A 706  ? 0.3299 0.3424 0.2982 0.0482  -0.0043 -0.0526 704  SER A CB  
5229  O OG  . SER A 706  ? 0.3195 0.3379 0.2878 0.0516  -0.0046 -0.0575 704  SER A OG  
5230  N N   . PRO A 707  ? 0.3048 0.2991 0.2853 0.0427  -0.0073 -0.0514 705  PRO A N   
5231  C CA  . PRO A 707  ? 0.3120 0.3000 0.2983 0.0414  -0.0085 -0.0516 705  PRO A CA  
5232  C C   . PRO A 707  ? 0.2851 0.2750 0.2712 0.0428  -0.0068 -0.0510 705  PRO A C   
5233  O O   . PRO A 707  ? 0.3008 0.2964 0.2821 0.0442  -0.0043 -0.0495 705  PRO A O   
5234  C CB  . PRO A 707  ? 0.2741 0.2564 0.2608 0.0375  -0.0077 -0.0458 705  PRO A CB  
5235  C CG  . PRO A 707  ? 0.2783 0.2646 0.2589 0.0374  -0.0049 -0.0417 705  PRO A CG  
5236  C CD  . PRO A 707  ? 0.3137 0.3068 0.2908 0.0402  -0.0052 -0.0452 705  PRO A CD  
5237  N N   . TRP A 708  ? 0.3106 0.2957 0.3021 0.0422  -0.0081 -0.0520 706  TRP A N   
5238  C CA  . TRP A 708  ? 0.2767 0.2632 0.2687 0.0435  -0.0067 -0.0517 706  TRP A CA  
5239  C C   . TRP A 708  ? 0.2746 0.2585 0.2649 0.0410  -0.0042 -0.0450 706  TRP A C   
5240  O O   . TRP A 708  ? 0.3278 0.3141 0.3171 0.0419  -0.0024 -0.0438 706  TRP A O   
5241  C CB  . TRP A 708  ? 0.2892 0.2718 0.2881 0.0443  -0.0094 -0.0557 706  TRP A CB  
5242  C CG  . TRP A 708  ? 0.3360 0.3108 0.3401 0.0412  -0.0116 -0.0540 706  TRP A CG  
5243  C CD1 . TRP A 708  ? 0.4532 0.4253 0.4613 0.0408  -0.0146 -0.0572 706  TRP A CD1 
5244  C CD2 . TRP A 708  ? 0.3257 0.2950 0.3318 0.0380  -0.0109 -0.0487 706  TRP A CD2 
5245  N NE1 . TRP A 708  ? 0.4185 0.3838 0.4309 0.0375  -0.0158 -0.0538 706  TRP A NE1 
5246  C CE2 . TRP A 708  ? 0.3539 0.3176 0.3650 0.0358  -0.0135 -0.0486 706  TRP A CE2 
5247  C CE3 . TRP A 708  ? 0.2673 0.2361 0.2716 0.0369  -0.0084 -0.0439 706  TRP A CE3 
5248  C CZ2 . TRP A 708  ? 0.4186 0.3768 0.4326 0.0325  -0.0136 -0.0438 706  TRP A CZ2 
5249  C CZ3 . TRP A 708  ? 0.3078 0.2709 0.3149 0.0337  -0.0086 -0.0395 706  TRP A CZ3 
5250  C CH2 . TRP A 708  ? 0.4322 0.3904 0.4440 0.0316  -0.0112 -0.0394 706  TRP A CH2 
5251  N N   . ASN A 709  ? 0.2735 0.2531 0.2636 0.0378  -0.0040 -0.0409 707  ASN A N   
5252  C CA  . ASN A 709  ? 0.2870 0.2636 0.2768 0.0353  -0.0021 -0.0354 707  ASN A CA  
5253  C C   . ASN A 709  ? 0.2906 0.2713 0.2747 0.0353  0.0009  -0.0315 707  ASN A C   
5254  O O   . ASN A 709  ? 0.3131 0.2930 0.2968 0.0342  0.0026  -0.0277 707  ASN A O   
5255  C CB  . ASN A 709  ? 0.2606 0.2311 0.2530 0.0320  -0.0033 -0.0327 707  ASN A CB  
5256  C CG  . ASN A 709  ? 0.3241 0.2954 0.3133 0.0308  -0.0030 -0.0313 707  ASN A CG  
5257  O OD1 . ASN A 709  ? 0.3533 0.3282 0.3405 0.0326  -0.0036 -0.0343 707  ASN A OD1 
5258  N ND2 . ASN A 709  ? 0.3903 0.3586 0.3792 0.0279  -0.0022 -0.0268 707  ASN A ND2 
5259  N N   . PHE A 710  ? 0.3019 0.2872 0.2821 0.0364  0.0013  -0.0322 708  PHE A N   
5260  C CA  . PHE A 710  ? 0.2876 0.2777 0.2628 0.0369  0.0040  -0.0289 708  PHE A CA  
5261  C C   . PHE A 710  ? 0.2913 0.2888 0.2639 0.0403  0.0041  -0.0327 708  PHE A C   
5262  O O   . PHE A 710  ? 0.2756 0.2768 0.2451 0.0411  0.0040  -0.0332 708  PHE A O   
5263  C CB  . PHE A 710  ? 0.2897 0.2786 0.2625 0.0348  0.0046  -0.0252 708  PHE A CB  
5264  C CG  . PHE A 710  ? 0.3819 0.3644 0.3570 0.0315  0.0046  -0.0216 708  PHE A CG  
5265  C CD1 . PHE A 710  ? 0.4583 0.4387 0.4348 0.0305  0.0058  -0.0190 708  PHE A CD1 
5266  C CD2 . PHE A 710  ? 0.4343 0.4135 0.4100 0.0296  0.0035  -0.0209 708  PHE A CD2 
5267  C CE1 . PHE A 710  ? 0.4287 0.4041 0.4071 0.0277  0.0058  -0.0159 708  PHE A CE1 
5268  C CE2 . PHE A 710  ? 0.4178 0.3922 0.3954 0.0267  0.0036  -0.0177 708  PHE A CE2 
5269  C CZ  . PHE A 710  ? 0.3990 0.3715 0.3778 0.0258  0.0047  -0.0153 708  PHE A CZ  
5270  N N   . PRO A 711  ? 0.2829 0.2832 0.2570 0.0426  0.0041  -0.0357 709  PRO A N   
5271  C CA  . PRO A 711  ? 0.2868 0.2942 0.2593 0.0461  0.0035  -0.0407 709  PRO A CA  
5272  C C   . PRO A 711  ? 0.2847 0.3004 0.2518 0.0477  0.0059  -0.0386 709  PRO A C   
5273  O O   . PRO A 711  ? 0.2737 0.2962 0.2388 0.0506  0.0055  -0.0425 709  PRO A O   
5274  C CB  . PRO A 711  ? 0.3101 0.3173 0.2864 0.0479  0.0028  -0.0442 709  PRO A CB  
5275  C CG  . PRO A 711  ? 0.2784 0.2821 0.2556 0.0457  0.0046  -0.0391 709  PRO A CG  
5276  C CD  . PRO A 711  ? 0.2675 0.2648 0.2448 0.0421  0.0045  -0.0348 709  PRO A CD  
5277  N N   . LEU A 712  ? 0.3053 0.3211 0.2702 0.0459  0.0083  -0.0325 710  LEU A N   
5278  C CA  . LEU A 712  ? 0.2707 0.2938 0.2308 0.0469  0.0104  -0.0296 710  LEU A CA  
5279  C C   . LEU A 712  ? 0.2510 0.2720 0.2090 0.0448  0.0106  -0.0255 710  LEU A C   
5280  O O   . LEU A 712  ? 0.2711 0.2975 0.2256 0.0460  0.0108  -0.0254 710  LEU A O   
5281  C CB  . LEU A 712  ? 0.2552 0.2813 0.2147 0.0468  0.0130  -0.0255 710  LEU A CB  
5282  C CG  . LEU A 712  ? 0.2701 0.3045 0.2251 0.0479  0.0151  -0.0220 710  LEU A CG  
5283  C CD1 . LEU A 712  ? 0.2579 0.3012 0.2105 0.0515  0.0146  -0.0269 710  LEU A CD1 
5284  C CD2 . LEU A 712  ? 0.2903 0.3270 0.2454 0.0472  0.0176  -0.0173 710  LEU A CD2 
5285  N N   . ALA A 713  ? 0.2532 0.2667 0.2133 0.0417  0.0105  -0.0224 711  ALA A N   
5286  C CA  . ALA A 713  ? 0.2533 0.2653 0.2115 0.0397  0.0110  -0.0181 711  ALA A CA  
5287  C C   . ALA A 713  ? 0.2875 0.2990 0.2450 0.0400  0.0090  -0.0209 711  ALA A C   
5288  O O   . ALA A 713  ? 0.2776 0.2932 0.2319 0.0406  0.0094  -0.0195 711  ALA A O   
5289  C CB  . ALA A 713  ? 0.2715 0.2763 0.2322 0.0366  0.0114  -0.0144 711  ALA A CB  
5290  N N   . ILE A 714  ? 0.2783 0.2847 0.2390 0.0393  0.0068  -0.0245 712  ILE A N   
5291  C CA  . ILE A 714  ? 0.2481 0.2540 0.2086 0.0394  0.0049  -0.0271 712  ILE A CA  
5292  C C   . ILE A 714  ? 0.2799 0.2931 0.2381 0.0427  0.0041  -0.0315 712  ILE A C   
5293  O O   . ILE A 714  ? 0.2747 0.2910 0.2304 0.0433  0.0035  -0.0319 712  ILE A O   
5294  C CB  . ILE A 714  ? 0.2703 0.2691 0.2354 0.0377  0.0027  -0.0295 712  ILE A CB  
5295  C CG1 . ILE A 714  ? 0.3183 0.3113 0.2848 0.0344  0.0035  -0.0247 712  ILE A CG1 
5296  C CG2 . ILE A 714  ? 0.2681 0.2672 0.2337 0.0382  0.0002  -0.0334 712  ILE A CG2 
5297  C CD1 . ILE A 714  ? 0.4196 0.4064 0.3900 0.0324  0.0015  -0.0259 712  ILE A CD1 
5298  N N   . PHE A 715  ? 0.3029 0.3193 0.2620 0.0449  0.0041  -0.0350 713  PHE A N   
5299  C CA  . PHE A 715  ? 0.2591 0.2839 0.2154 0.0484  0.0037  -0.0390 713  PHE A CA  
5300  C C   . PHE A 715  ? 0.2720 0.3038 0.2232 0.0491  0.0057  -0.0350 713  PHE A C   
5301  O O   . PHE A 715  ? 0.2664 0.3029 0.2150 0.0505  0.0048  -0.0368 713  PHE A O   
5302  C CB  . PHE A 715  ? 0.2538 0.2816 0.2116 0.0506  0.0042  -0.0420 713  PHE A CB  
5303  C CG  . PHE A 715  ? 0.2780 0.3154 0.2330 0.0544  0.0041  -0.0463 713  PHE A CG  
5304  C CD1 . PHE A 715  ? 0.3096 0.3484 0.2662 0.0565  0.0013  -0.0533 713  PHE A CD1 
5305  C CD2 . PHE A 715  ? 0.2917 0.3374 0.2427 0.0559  0.0067  -0.0434 713  PHE A CD2 
5306  C CE1 . PHE A 715  ? 0.3293 0.3777 0.2833 0.0602  0.0012  -0.0577 713  PHE A CE1 
5307  C CE2 . PHE A 715  ? 0.2981 0.3538 0.2463 0.0595  0.0067  -0.0473 713  PHE A CE2 
5308  C CZ  . PHE A 715  ? 0.3453 0.4025 0.2948 0.0618  0.0039  -0.0547 713  PHE A CZ  
5309  N N   . THR A 716  ? 0.2608 0.2934 0.2107 0.0481  0.0082  -0.0295 714  THR A N   
5310  C CA  . THR A 716  ? 0.2546 0.2939 0.2002 0.0487  0.0100  -0.0251 714  THR A CA  
5311  C C   . THR A 716  ? 0.2488 0.2854 0.1933 0.0469  0.0094  -0.0223 714  THR A C   
5312  O O   . THR A 716  ? 0.2651 0.3078 0.2062 0.0482  0.0095  -0.0216 714  THR A O   
5313  C CB  . THR A 716  ? 0.2817 0.3216 0.2273 0.0476  0.0127  -0.0197 714  THR A CB  
5314  O OG1 . THR A 716  ? 0.2721 0.3157 0.2186 0.0496  0.0133  -0.0226 714  THR A OG1 
5315  C CG2 . THR A 716  ? 0.3137 0.3602 0.2557 0.0479  0.0145  -0.0144 714  THR A CG2 
5316  N N   . GLY A 717  ? 0.2422 0.2701 0.1895 0.0440  0.0088  -0.0207 715  GLY A N   
5317  C CA  . GLY A 717  ? 0.2603 0.2857 0.2070 0.0423  0.0083  -0.0179 715  GLY A CA  
5318  C C   . GLY A 717  ? 0.2579 0.2862 0.2032 0.0438  0.0063  -0.0219 715  GLY A C   
5319  O O   . GLY A 717  ? 0.2760 0.3083 0.2185 0.0443  0.0065  -0.0198 715  GLY A O   
5320  N N   . GLN A 718  ? 0.2337 0.2600 0.1813 0.0445  0.0042  -0.0277 716  GLN A N   
5321  C CA  . GLN A 718  ? 0.2399 0.2685 0.1869 0.0458  0.0020  -0.0318 716  GLN A CA  
5322  C C   . GLN A 718  ? 0.2586 0.2973 0.2012 0.0489  0.0024  -0.0331 716  GLN A C   
5323  O O   . GLN A 718  ? 0.2591 0.3014 0.1991 0.0495  0.0019  -0.0325 716  GLN A O   
5324  C CB  . GLN A 718  ? 0.2580 0.2827 0.2090 0.0460  -0.0004 -0.0380 716  GLN A CB  
5325  C CG  . GLN A 718  ? 0.2625 0.2778 0.2179 0.0428  -0.0011 -0.0367 716  GLN A CG  
5326  C CD  . GLN A 718  ? 0.2867 0.2982 0.2467 0.0428  -0.0039 -0.0422 716  GLN A CD  
5327  O OE1 . GLN A 718  ? 0.3005 0.3065 0.2635 0.0407  -0.0053 -0.0422 716  GLN A OE1 
5328  N NE2 . GLN A 718  ? 0.2648 0.2793 0.2258 0.0453  -0.0047 -0.0470 716  GLN A NE2 
5329  N N   . ILE A 719  ? 0.2763 0.3201 0.2180 0.0511  0.0034  -0.0347 717  ILE A N   
5330  C CA  . ILE A 719  ? 0.2447 0.2992 0.1823 0.0543  0.0039  -0.0363 717  ILE A CA  
5331  C C   . ILE A 719  ? 0.2802 0.3394 0.2139 0.0539  0.0059  -0.0296 717  ILE A C   
5332  O O   . ILE A 719  ? 0.2847 0.3509 0.2149 0.0556  0.0055  -0.0297 717  ILE A O   
5333  C CB  . ILE A 719  ? 0.2889 0.3478 0.2268 0.0566  0.0047  -0.0392 717  ILE A CB  
5334  C CG1 . ILE A 719  ? 0.2809 0.3362 0.2227 0.0575  0.0021  -0.0467 717  ILE A CG1 
5335  C CG2 . ILE A 719  ? 0.3695 0.4405 0.3027 0.0597  0.0059  -0.0393 717  ILE A CG2 
5336  C CD1 . ILE A 719  ? 0.4024 0.4586 0.3462 0.0588  0.0028  -0.0490 717  ILE A CD1 
5337  N N   . ALA A 720  ? 0.2606 0.3161 0.1951 0.0517  0.0079  -0.0236 718  ALA A N   
5338  C CA  . ALA A 720  ? 0.3054 0.3650 0.2372 0.0513  0.0097  -0.0168 718  ALA A CA  
5339  C C   . ALA A 720  ? 0.2470 0.3049 0.1780 0.0502  0.0085  -0.0151 718  ALA A C   
5340  O O   . ALA A 720  ? 0.2738 0.3385 0.2015 0.0514  0.0088  -0.0126 718  ALA A O   
5341  C CB  . ALA A 720  ? 0.2868 0.3417 0.2207 0.0488  0.0117  -0.0112 718  ALA A CB  
5342  N N   . ALA A 721  ? 0.2761 0.3251 0.2101 0.0480  0.0071  -0.0164 719  ALA A N   
5343  C CA  . ALA A 721  ? 0.2451 0.2923 0.1788 0.0471  0.0057  -0.0153 719  ALA A CA  
5344  C C   . ALA A 721  ? 0.2419 0.2960 0.1729 0.0497  0.0041  -0.0195 719  ALA A C   
5345  O O   . ALA A 721  ? 0.2676 0.3265 0.1959 0.0504  0.0040  -0.0168 719  ALA A O   
5346  C CB  . ALA A 721  ? 0.2472 0.2847 0.1849 0.0446  0.0044  -0.0169 719  ALA A CB  
5347  N N   . ALA A 722  ? 0.2536 0.3085 0.1855 0.0513  0.0025  -0.0262 720  ALA A N   
5348  C CA  . ALA A 722  ? 0.2730 0.3343 0.2028 0.0538  0.0006  -0.0310 720  ALA A CA  
5349  C C   . ALA A 722  ? 0.2906 0.3632 0.2154 0.0564  0.0019  -0.0290 720  ALA A C   
5350  O O   . ALA A 722  ? 0.2877 0.3658 0.2097 0.0576  0.0011  -0.0285 720  ALA A O   
5351  C CB  . ALA A 722  ? 0.2621 0.3222 0.1945 0.0550  -0.0014 -0.0388 720  ALA A CB  
5352  N N   . LEU A 723  ? 0.2544 0.3310 0.1783 0.0574  0.0039  -0.0276 721  LEU A N   
5353  C CA  . LEU A 723  ? 0.2547 0.3429 0.1742 0.0599  0.0054  -0.0253 721  LEU A CA  
5354  C C   . LEU A 723  ? 0.2800 0.3701 0.1974 0.0587  0.0065  -0.0176 721  LEU A C   
5355  O O   . LEU A 723  ? 0.2679 0.3668 0.1816 0.0606  0.0063  -0.0165 721  LEU A O   
5356  C CB  . LEU A 723  ? 0.2774 0.3685 0.1969 0.0606  0.0076  -0.0244 721  LEU A CB  
5357  C CG  . LEU A 723  ? 0.2623 0.3550 0.1831 0.0628  0.0067  -0.0319 721  LEU A CG  
5358  C CD1 . LEU A 723  ? 0.3029 0.3970 0.2244 0.0628  0.0092  -0.0293 721  LEU A CD1 
5359  C CD2 . LEU A 723  ? 0.2847 0.3887 0.2019 0.0666  0.0056  -0.0369 721  LEU A CD2 
5360  N N   . VAL A 724  ? 0.2848 0.3670 0.2049 0.0557  0.0076  -0.0122 722  VAL A N   
5361  C CA  . VAL A 724  ? 0.2765 0.3606 0.1953 0.0546  0.0087  -0.0047 722  VAL A CA  
5362  C C   . VAL A 724  ? 0.2821 0.3653 0.2003 0.0544  0.0067  -0.0048 722  VAL A C   
5363  O O   . VAL A 724  ? 0.2763 0.3643 0.1925 0.0547  0.0070  0.0002  722  VAL A O   
5364  C CB  . VAL A 724  ? 0.2560 0.3322 0.1782 0.0516  0.0102  0.0007  722  VAL A CB  
5365  C CG1 . VAL A 724  ? 0.2896 0.3548 0.2153 0.0490  0.0089  -0.0001 722  VAL A CG1 
5366  C CG2 . VAL A 724  ? 0.2865 0.3672 0.2076 0.0512  0.0119  0.0088  722  VAL A CG2 
5367  N N   . ALA A 725  ? 0.2834 0.3606 0.2035 0.0539  0.0046  -0.0103 723  ALA A N   
5368  C CA  . ALA A 725  ? 0.2980 0.3753 0.2175 0.0540  0.0025  -0.0115 723  ALA A CA  
5369  C C   . ALA A 725  ? 0.2852 0.3729 0.2007 0.0573  0.0013  -0.0152 723  ALA A C   
5370  O O   . ALA A 725  ? 0.3306 0.4194 0.2454 0.0577  -0.0006 -0.0167 723  ALA A O   
5371  C CB  . ALA A 725  ? 0.2804 0.3483 0.2037 0.0523  0.0007  -0.0161 723  ALA A CB  
5372  N N   . GLY A 726  ? 0.2933 0.3892 0.2063 0.0597  0.0024  -0.0168 724  GLY A N   
5373  C CA  . GLY A 726  ? 0.2817 0.3888 0.1906 0.0630  0.0014  -0.0201 724  GLY A CA  
5374  C C   . GLY A 726  ? 0.3031 0.4115 0.2125 0.0651  -0.0007 -0.0294 724  GLY A C   
5375  O O   . GLY A 726  ? 0.3219 0.4392 0.2282 0.0678  -0.0020 -0.0330 724  GLY A O   
5376  N N   . ASN A 727  ? 0.2796 0.3795 0.1931 0.0638  -0.0012 -0.0333 725  ASN A N   
5377  C CA  . ASN A 727  ? 0.3121 0.4115 0.2275 0.0654  -0.0035 -0.0422 725  ASN A CA  
5378  C C   . ASN A 727  ? 0.2872 0.3911 0.2024 0.0674  -0.0025 -0.0455 725  ASN A C   
5379  O O   . ASN A 727  ? 0.2882 0.3883 0.2048 0.0660  -0.0004 -0.0421 725  ASN A O   
5380  C CB  . ASN A 727  ? 0.2955 0.3824 0.2163 0.0625  -0.0050 -0.0443 725  ASN A CB  
5381  C CG  . ASN A 727  ? 0.2949 0.3768 0.2164 0.0602  -0.0058 -0.0408 725  ASN A CG  
5382  O OD1 . ASN A 727  ? 0.3057 0.3904 0.2264 0.0612  -0.0079 -0.0436 725  ASN A OD1 
5383  N ND2 . ASN A 727  ? 0.2808 0.3555 0.2042 0.0573  -0.0043 -0.0349 725  ASN A ND2 
5384  N N   . PRO A 728  ? 0.2854 0.3970 0.1991 0.0708  -0.0040 -0.0525 726  PRO A N   
5385  C CA  . PRO A 728  ? 0.3290 0.4435 0.2438 0.0728  -0.0035 -0.0571 726  PRO A CA  
5386  C C   . PRO A 728  ? 0.3091 0.4119 0.2300 0.0710  -0.0051 -0.0612 726  PRO A C   
5387  O O   . PRO A 728  ? 0.3120 0.4077 0.2359 0.0694  -0.0074 -0.0635 726  PRO A O   
5388  C CB  . PRO A 728  ? 0.3025 0.4284 0.2143 0.0769  -0.0053 -0.0640 726  PRO A CB  
5389  C CG  . PRO A 728  ? 0.3085 0.4325 0.2204 0.0764  -0.0079 -0.0658 726  PRO A CG  
5390  C CD  . PRO A 728  ? 0.2955 0.4133 0.2072 0.0730  -0.0065 -0.0571 726  PRO A CD  
5391  N N   . VAL A 729  ? 0.2914 0.3926 0.2143 0.0712  -0.0038 -0.0619 727  VAL A N   
5392  C CA  . VAL A 729  ? 0.2696 0.3593 0.1983 0.0689  -0.0047 -0.0638 727  VAL A CA  
5393  C C   . VAL A 729  ? 0.2978 0.3894 0.2294 0.0716  -0.0062 -0.0719 727  VAL A C   
5394  O O   . VAL A 729  ? 0.3075 0.4080 0.2366 0.0745  -0.0049 -0.0735 727  VAL A O   
5395  C CB  . VAL A 729  ? 0.2600 0.3438 0.1897 0.0661  -0.0018 -0.0565 727  VAL A CB  
5396  C CG1 . VAL A 729  ? 0.2749 0.3486 0.2104 0.0643  -0.0026 -0.0588 727  VAL A CG1 
5397  C CG2 . VAL A 729  ? 0.2823 0.3620 0.2107 0.0632  -0.0010 -0.0495 727  VAL A CG2 
5398  N N   . LEU A 730  ? 0.2709 0.3540 0.2080 0.0706  -0.0089 -0.0767 728  LEU A N   
5399  C CA  . LEU A 730  ? 0.2954 0.3767 0.2372 0.0722  -0.0106 -0.0835 728  LEU A CA  
5400  C C   . LEU A 730  ? 0.2921 0.3624 0.2385 0.0688  -0.0097 -0.0798 728  LEU A C   
5401  O O   . LEU A 730  ? 0.2937 0.3548 0.2434 0.0657  -0.0109 -0.0781 728  LEU A O   
5402  C CB  . LEU A 730  ? 0.3101 0.3899 0.2557 0.0733  -0.0147 -0.0916 728  LEU A CB  
5403  C CG  . LEU A 730  ? 0.2694 0.3592 0.2113 0.0764  -0.0163 -0.0962 728  LEU A CG  
5404  C CD1 . LEU A 730  ? 0.2864 0.3891 0.2233 0.0803  -0.0145 -0.0977 728  LEU A CD1 
5405  C CD2 . LEU A 730  ? 0.3010 0.3910 0.2393 0.0746  -0.0159 -0.0910 728  LEU A CD2 
5406  N N   . ALA A 731  ? 0.2949 0.3666 0.2412 0.0695  -0.0076 -0.0784 729  ALA A N   
5407  C CA  . ALA A 731  ? 0.2740 0.3363 0.2239 0.0665  -0.0065 -0.0742 729  ALA A CA  
5408  C C   . ALA A 731  ? 0.2792 0.3366 0.2355 0.0673  -0.0088 -0.0805 729  ALA A C   
5409  O O   . ALA A 731  ? 0.3379 0.4011 0.2947 0.0704  -0.0089 -0.0852 729  ALA A O   
5410  C CB  . ALA A 731  ? 0.2928 0.3594 0.2394 0.0665  -0.0028 -0.0684 729  ALA A CB  
5411  N N   . LYS A 732  ? 0.2789 0.3261 0.2405 0.0644  -0.0108 -0.0805 730  LYS A N   
5412  C CA  . LYS A 732  ? 0.2955 0.3369 0.2640 0.0647  -0.0133 -0.0857 730  LYS A CA  
5413  C C   . LYS A 732  ? 0.2932 0.3263 0.2646 0.0616  -0.0118 -0.0803 730  LYS A C   
5414  O O   . LYS A 732  ? 0.3037 0.3289 0.2774 0.0581  -0.0123 -0.0766 730  LYS A O   
5415  C CB  . LYS A 732  ? 0.2958 0.3323 0.2689 0.0640  -0.0171 -0.0902 730  LYS A CB  
5416  C CG  . LYS A 732  ? 0.3703 0.4065 0.3495 0.0665  -0.0205 -0.0988 730  LYS A CG  
5417  C CD  . LYS A 732  ? 0.3561 0.3857 0.3409 0.0656  -0.0206 -0.0984 730  LYS A CD  
5418  C CE  . LYS A 732  ? 0.4149 0.4334 0.4043 0.0611  -0.0214 -0.0939 730  LYS A CE  
5419  N NZ  . LYS A 732  ? 0.3808 0.3933 0.3757 0.0604  -0.0217 -0.0933 730  LYS A NZ  
5420  N N   . PRO A 733  ? 0.2755 0.3105 0.2468 0.0627  -0.0100 -0.0795 731  PRO A N   
5421  C CA  . PRO A 733  ? 0.2850 0.3124 0.2590 0.0598  -0.0087 -0.0745 731  PRO A CA  
5422  C C   . PRO A 733  ? 0.2799 0.2992 0.2617 0.0589  -0.0117 -0.0780 731  PRO A C   
5423  O O   . PRO A 733  ? 0.3093 0.3296 0.2948 0.0612  -0.0146 -0.0850 731  PRO A O   
5424  C CB  . PRO A 733  ? 0.3196 0.3532 0.2911 0.0618  -0.0060 -0.0734 731  PRO A CB  
5425  C CG  . PRO A 733  ? 0.3144 0.3564 0.2855 0.0662  -0.0074 -0.0809 731  PRO A CG  
5426  C CD  . PRO A 733  ? 0.3187 0.3634 0.2877 0.0668  -0.0091 -0.0835 731  PRO A CD  
5427  N N   . ALA A 734  ? 0.2741 0.2855 0.2585 0.0555  -0.0111 -0.0729 732  ALA A N   
5428  C CA  . ALA A 734  ? 0.3057 0.3095 0.2977 0.0545  -0.0136 -0.0750 732  ALA A CA  
5429  C C   . ALA A 734  ? 0.3206 0.3272 0.3157 0.0579  -0.0147 -0.0808 732  ALA A C   
5430  O O   . ALA A 734  ? 0.3347 0.3474 0.3265 0.0599  -0.0123 -0.0804 732  ALA A O   
5431  C CB  . ALA A 734  ? 0.2894 0.2863 0.2826 0.0509  -0.0121 -0.0682 732  ALA A CB  
5432  N N   . GLU A 735  ? 0.2999 0.3024 0.3020 0.0585  -0.0184 -0.0861 733  GLU A N   
5433  C CA  . GLU A 735  ? 0.3076 0.3122 0.3138 0.0619  -0.0198 -0.0922 733  GLU A CA  
5434  C C   . GLU A 735  ? 0.3371 0.3400 0.3443 0.0613  -0.0178 -0.0885 733  GLU A C   
5435  O O   . GLU A 735  ? 0.3137 0.3216 0.3211 0.0645  -0.0173 -0.0920 733  GLU A O   
5436  C CB  . GLU A 735  ? 0.3714 0.3703 0.3863 0.0620  -0.0244 -0.0978 733  GLU A CB  
5437  C CG  . GLU A 735  ? 0.4899 0.4783 0.5102 0.0577  -0.0258 -0.0931 733  GLU A CG  
5438  C CD  . GLU A 735  ? 0.5512 0.5368 0.5709 0.0550  -0.0267 -0.0911 733  GLU A CD  
5439  O OE1 . GLU A 735  ? 0.5183 0.5093 0.5312 0.0553  -0.0249 -0.0901 733  GLU A OE1 
5440  O OE2 . GLU A 735  ? 0.5329 0.5111 0.5591 0.0524  -0.0294 -0.0905 733  GLU A OE2 
5441  N N   . GLU A 736  ? 0.3334 0.3298 0.3409 0.0575  -0.0165 -0.0815 734  GLU A N   
5442  C CA  . GLU A 736  ? 0.3216 0.3158 0.3303 0.0568  -0.0148 -0.0780 734  GLU A CA  
5443  C C   . GLU A 736  ? 0.3303 0.3318 0.3323 0.0579  -0.0108 -0.0748 734  GLU A C   
5444  O O   . GLU A 736  ? 0.3333 0.3359 0.3364 0.0590  -0.0097 -0.0744 734  GLU A O   
5445  C CB  . GLU A 736  ? 0.3421 0.3277 0.3532 0.0523  -0.0147 -0.0716 734  GLU A CB  
5446  C CG  . GLU A 736  ? 0.3697 0.3478 0.3884 0.0508  -0.0186 -0.0736 734  GLU A CG  
5447  C CD  . GLU A 736  ? 0.4652 0.4418 0.4830 0.0490  -0.0197 -0.0733 734  GLU A CD  
5448  O OE1 . GLU A 736  ? 0.3650 0.3472 0.3766 0.0499  -0.0182 -0.0735 734  GLU A OE1 
5449  O OE2 . GLU A 736  ? 0.4812 0.4511 0.5047 0.0465  -0.0222 -0.0724 734  GLU A OE2 
5450  N N   . THR A 737  ? 0.3218 0.3282 0.3171 0.0577  -0.0088 -0.0724 735  THR A N   
5451  C CA  . THR A 737  ? 0.3009 0.3132 0.2902 0.0579  -0.0049 -0.0678 735  THR A CA  
5452  C C   . THR A 737  ? 0.3147 0.3371 0.2982 0.0607  -0.0038 -0.0699 735  THR A C   
5453  O O   . THR A 737  ? 0.3046 0.3297 0.2828 0.0595  -0.0017 -0.0653 735  THR A O   
5454  C CB  . THR A 737  ? 0.3143 0.3216 0.3014 0.0538  -0.0031 -0.0600 735  THR A CB  
5455  O OG1 . THR A 737  ? 0.3195 0.3247 0.3054 0.0523  -0.0043 -0.0596 735  THR A OG1 
5456  C CG2 . THR A 737  ? 0.3064 0.3053 0.2986 0.0512  -0.0038 -0.0573 735  THR A CG2 
5457  N N   . PRO A 738  ? 0.2826 0.3112 0.2670 0.0647  -0.0051 -0.0769 736  PRO A N   
5458  C CA  . PRO A 738  ? 0.3024 0.3415 0.2811 0.0675  -0.0040 -0.0791 736  PRO A CA  
5459  C C   . PRO A 738  ? 0.3125 0.3601 0.2863 0.0688  -0.0003 -0.0755 736  PRO A C   
5460  O O   . PRO A 738  ? 0.3008 0.3567 0.2689 0.0701  0.0012  -0.0746 736  PRO A O   
5461  C CB  . PRO A 738  ? 0.3130 0.3555 0.2954 0.0714  -0.0071 -0.0884 736  PRO A CB  
5462  C CG  . PRO A 738  ? 0.3046 0.3422 0.2931 0.0716  -0.0079 -0.0899 736  PRO A CG  
5463  C CD  . PRO A 738  ? 0.2664 0.2932 0.2573 0.0669  -0.0077 -0.0833 736  PRO A CD  
5464  N N   . LEU A 739  ? 0.2716 0.3178 0.2475 0.0685  0.0011  -0.0735 737  LEU A N   
5465  C CA  . LEU A 739  ? 0.3122 0.3675 0.2842 0.0701  0.0043  -0.0709 737  LEU A CA  
5466  C C   . LEU A 739  ? 0.2718 0.3282 0.2386 0.0674  0.0073  -0.0627 737  LEU A C   
5467  O O   . LEU A 739  ? 0.2967 0.3626 0.2585 0.0689  0.0094  -0.0611 737  LEU A O   
5468  C CB  . LEU A 739  ? 0.3380 0.3911 0.3140 0.0703  0.0050  -0.0708 737  LEU A CB  
5469  C CG  . LEU A 739  ? 0.3099 0.3619 0.2917 0.0732  0.0020  -0.0787 737  LEU A CG  
5470  C CD1 . LEU A 739  ? 0.2927 0.3420 0.2783 0.0729  0.0029  -0.0773 737  LEU A CD1 
5471  C CD2 . LEU A 739  ? 0.3111 0.3744 0.2909 0.0779  0.0016  -0.0857 737  LEU A CD2 
5472  N N   . ILE A 740  ? 0.2837 0.3308 0.2519 0.0635  0.0074  -0.0574 738  ILE A N   
5473  C CA  . ILE A 740  ? 0.2857 0.3334 0.2496 0.0609  0.0099  -0.0500 738  ILE A CA  
5474  C C   . ILE A 740  ? 0.2917 0.3429 0.2516 0.0613  0.0094  -0.0502 738  ILE A C   
5475  O O   . ILE A 740  ? 0.2990 0.3558 0.2544 0.0610  0.0116  -0.0456 738  ILE A O   
5476  C CB  . ILE A 740  ? 0.3256 0.3628 0.2921 0.0568  0.0100  -0.0448 738  ILE A CB  
5477  C CG1 . ILE A 740  ? 0.2984 0.3366 0.2613 0.0545  0.0126  -0.0373 738  ILE A CG1 
5478  C CG2 . ILE A 740  ? 0.3157 0.3447 0.2851 0.0551  0.0072  -0.0469 738  ILE A CG2 
5479  C CD1 . ILE A 740  ? 0.3178 0.3638 0.2785 0.0556  0.0155  -0.0341 738  ILE A CD1 
5480  N N   . ALA A 741  ? 0.3027 0.3514 0.2644 0.0621  0.0065  -0.0557 739  ALA A N   
5481  C CA  . ALA A 741  ? 0.3461 0.3990 0.3041 0.0629  0.0058  -0.0567 739  ALA A CA  
5482  C C   . ALA A 741  ? 0.2678 0.3334 0.2214 0.0666  0.0070  -0.0589 739  ALA A C   
5483  O O   . ALA A 741  ? 0.3164 0.3878 0.2652 0.0666  0.0083  -0.0554 739  ALA A O   
5484  C CB  . ALA A 741  ? 0.3370 0.3848 0.2985 0.0631  0.0021  -0.0626 739  ALA A CB  
5485  N N   . ALA A 742  ? 0.2709 0.3414 0.2263 0.0698  0.0065  -0.0645 740  ALA A N   
5486  C CA  . ALA A 742  ? 0.2843 0.3680 0.2355 0.0735  0.0078  -0.0669 740  ALA A CA  
5487  C C   . ALA A 742  ? 0.2956 0.3852 0.2428 0.0727  0.0115  -0.0592 740  ALA A C   
5488  O O   . ALA A 742  ? 0.3173 0.4170 0.2596 0.0743  0.0130  -0.0577 740  ALA A O   
5489  C CB  . ALA A 742  ? 0.2872 0.3747 0.2417 0.0771  0.0066  -0.0743 740  ALA A CB  
5490  N N   . GLU A 743  ? 0.2788 0.3624 0.2284 0.0701  0.0131  -0.0543 741  GLU A N   
5491  C CA  . GLU A 743  ? 0.3126 0.4009 0.2591 0.0690  0.0164  -0.0469 741  GLU A CA  
5492  C C   . GLU A 743  ? 0.2994 0.3864 0.2427 0.0664  0.0172  -0.0406 741  GLU A C   
5493  O O   . GLU A 743  ? 0.2866 0.3817 0.2260 0.0668  0.0194  -0.0359 741  GLU A O   
5494  C CB  . GLU A 743  ? 0.3002 0.3821 0.2506 0.0669  0.0175  -0.0437 741  GLU A CB  
5495  C CG  . GLU A 743  ? 0.3299 0.4149 0.2784 0.0651  0.0208  -0.0357 741  GLU A CG  
5496  C CD  . GLU A 743  ? 0.3143 0.4128 0.2599 0.0680  0.0231  -0.0353 741  GLU A CD  
5497  O OE1 . GLU A 743  ? 0.3445 0.4505 0.2893 0.0718  0.0223  -0.0417 741  GLU A OE1 
5498  O OE2 . GLU A 743  ? 0.4157 0.5176 0.3598 0.0665  0.0256  -0.0284 741  GLU A OE2 
5499  N N   . GLY A 744  ? 0.2815 0.3586 0.2264 0.0639  0.0153  -0.0404 742  GLY A N   
5500  C CA  . GLY A 744  ? 0.2755 0.3515 0.2177 0.0618  0.0156  -0.0354 742  GLY A CA  
5501  C C   . GLY A 744  ? 0.2983 0.3840 0.2360 0.0644  0.0153  -0.0372 742  GLY A C   
5502  O O   . GLY A 744  ? 0.2962 0.3868 0.2303 0.0639  0.0169  -0.0317 742  GLY A O   
5503  N N   . VAL A 745  ? 0.2925 0.3812 0.2305 0.0673  0.0131  -0.0450 743  VAL A N   
5504  C CA  . VAL A 745  ? 0.3204 0.4193 0.2541 0.0701  0.0126  -0.0475 743  VAL A CA  
5505  C C   . VAL A 745  ? 0.2852 0.3970 0.2151 0.0725  0.0153  -0.0451 743  VAL A C   
5506  O O   . VAL A 745  ? 0.3304 0.4503 0.2557 0.0732  0.0164  -0.0418 743  VAL A O   
5507  C CB  . VAL A 745  ? 0.3190 0.4181 0.2545 0.0728  0.0094  -0.0570 743  VAL A CB  
5508  C CG1 . VAL A 745  ? 0.3346 0.4467 0.2656 0.0766  0.0091  -0.0608 743  VAL A CG1 
5509  C CG2 . VAL A 745  ? 0.3172 0.4052 0.2557 0.0702  0.0068  -0.0581 743  VAL A CG2 
5510  N N   . ARG A 746  ? 0.3170 0.4312 0.2488 0.0737  0.0165  -0.0465 744  ARG A N   
5511  C CA  . ARG A 746  ? 0.3094 0.4359 0.2379 0.0756  0.0194  -0.0436 744  ARG A CA  
5512  C C   . ARG A 746  ? 0.2932 0.4205 0.2196 0.0728  0.0219  -0.0336 744  ARG A C   
5513  O O   . ARG A 746  ? 0.3293 0.4675 0.2515 0.0741  0.0235  -0.0302 744  ARG A O   
5514  C CB  . ARG A 746  ? 0.3436 0.4706 0.2754 0.0767  0.0203  -0.0459 744  ARG A CB  
5515  C CG  . ARG A 746  ? 0.3182 0.4592 0.2470 0.0792  0.0231  -0.0440 744  ARG A CG  
5516  C CD  . ARG A 746  ? 0.3618 0.5022 0.2940 0.0793  0.0246  -0.0439 744  ARG A CD  
5517  N NE  . ARG A 746  ? 0.3739 0.5055 0.3083 0.0751  0.0260  -0.0362 744  ARG A NE  
5518  C CZ  . ARG A 746  ? 0.3997 0.5348 0.3320 0.0732  0.0285  -0.0278 744  ARG A CZ  
5519  N NH1 . ARG A 746  ? 0.3971 0.5445 0.3249 0.0749  0.0300  -0.0252 744  ARG A NH1 
5520  N NH2 . ARG A 746  ? 0.3647 0.4910 0.2998 0.0695  0.0294  -0.0218 744  ARG A NH2 
5521  N N   . ILE A 747  ? 0.2906 0.4064 0.2199 0.0690  0.0221  -0.0289 745  ILE A N   
5522  C CA  . ILE A 747  ? 0.2995 0.4148 0.2278 0.0661  0.0241  -0.0197 745  ILE A CA  
5523  C C   . ILE A 747  ? 0.2979 0.4152 0.2228 0.0658  0.0234  -0.0172 745  ILE A C   
5524  O O   . ILE A 747  ? 0.2777 0.4024 0.1998 0.0656  0.0251  -0.0111 745  ILE A O   
5525  C CB  . ILE A 747  ? 0.2986 0.4010 0.2311 0.0624  0.0242  -0.0164 745  ILE A CB  
5526  C CG1 . ILE A 747  ? 0.2945 0.3973 0.2299 0.0627  0.0255  -0.0169 745  ILE A CG1 
5527  C CG2 . ILE A 747  ? 0.3054 0.4052 0.2374 0.0593  0.0253  -0.0078 745  ILE A CG2 
5528  C CD1 . ILE A 747  ? 0.3164 0.4067 0.2563 0.0597  0.0250  -0.0158 745  ILE A CD1 
5529  N N   . LEU A 748  ? 0.2997 0.4106 0.2252 0.0655  0.0208  -0.0215 746  LEU A N   
5530  C CA  . LEU A 748  ? 0.2777 0.3905 0.2001 0.0653  0.0199  -0.0195 746  LEU A CA  
5531  C C   . LEU A 748  ? 0.3015 0.4287 0.2192 0.0688  0.0204  -0.0208 746  LEU A C   
5532  O O   . LEU A 748  ? 0.3174 0.4501 0.2320 0.0685  0.0211  -0.0155 746  LEU A O   
5533  C CB  . LEU A 748  ? 0.2848 0.3889 0.2090 0.0646  0.0169  -0.0247 746  LEU A CB  
5534  C CG  . LEU A 748  ? 0.3343 0.4254 0.2619 0.0607  0.0164  -0.0212 746  LEU A CG  
5535  C CD1 . LEU A 748  ? 0.3495 0.4321 0.2799 0.0602  0.0135  -0.0274 746  LEU A CD1 
5536  C CD2 . LEU A 748  ? 0.3354 0.4267 0.2609 0.0589  0.0169  -0.0146 746  LEU A CD2 
5537  N N   . ARG A 749  ? 0.2987 0.4324 0.2159 0.0721  0.0199  -0.0278 747  ARG A N   
5538  C CA  . ARG A 749  ? 0.2901 0.4389 0.2027 0.0757  0.0205  -0.0294 747  ARG A CA  
5539  C C   . ARG A 749  ? 0.3026 0.4607 0.2131 0.0757  0.0238  -0.0219 747  ARG A C   
5540  O O   . ARG A 749  ? 0.3360 0.5046 0.2423 0.0769  0.0247  -0.0182 747  ARG A O   
5541  C CB  . ARG A 749  ? 0.3164 0.4697 0.2296 0.0795  0.0190  -0.0393 747  ARG A CB  
5542  C CG  . ARG A 749  ? 0.3400 0.4887 0.2540 0.0804  0.0155  -0.0468 747  ARG A CG  
5543  C CD  . ARG A 749  ? 0.4303 0.5839 0.3454 0.0843  0.0138  -0.0568 747  ARG A CD  
5544  N NE  . ARG A 749  ? 0.4246 0.5748 0.3409 0.0854  0.0103  -0.0642 747  ARG A NE  
5545  C CZ  . ARG A 749  ? 0.4045 0.5603 0.3214 0.0892  0.0083  -0.0735 747  ARG A CZ  
5546  N NH1 . ARG A 749  ? 0.4003 0.5658 0.3166 0.0924  0.0095  -0.0767 747  ARG A NH1 
5547  N NH2 . ARG A 749  ? 0.3927 0.5449 0.3112 0.0899  0.0049  -0.0799 747  ARG A NH2 
5548  N N   . GLU A 750  ? 0.2933 0.4478 0.2069 0.0742  0.0255  -0.0193 748  GLU A N   
5549  C CA  . GLU A 750  ? 0.3207 0.4832 0.2331 0.0737  0.0287  -0.0115 748  GLU A CA  
5550  C C   . GLU A 750  ? 0.2889 0.4494 0.2004 0.0708  0.0293  -0.0025 748  GLU A C   
5551  O O   . GLU A 750  ? 0.3157 0.4866 0.2245 0.0712  0.0311  0.0035  748  GLU A O   
5552  C CB  . GLU A 750  ? 0.3058 0.4631 0.2223 0.0722  0.0301  -0.0102 748  GLU A CB  
5553  C CG  . GLU A 750  ? 0.3862 0.5527 0.3020 0.0718  0.0333  -0.0026 748  GLU A CG  
5554  C CD  . GLU A 750  ? 0.3684 0.5292 0.2885 0.0700  0.0347  -0.0004 748  GLU A CD  
5555  O OE1 . GLU A 750  ? 0.4981 0.6509 0.4213 0.0701  0.0335  -0.0063 748  GLU A OE1 
5556  O OE2 . GLU A 750  ? 0.4162 0.5805 0.3370 0.0683  0.0370  0.0073  748  GLU A OE2 
5557  N N   . ALA A 751  ? 0.2894 0.4369 0.2034 0.0679  0.0277  -0.0016 749  ALA A N   
5558  C CA  . ALA A 751  ? 0.3094 0.4535 0.2233 0.0651  0.0279  0.0062  749  ALA A CA  
5559  C C   . ALA A 751  ? 0.3113 0.4630 0.2209 0.0667  0.0270  0.0068  749  ALA A C   
5560  O O   . ALA A 751  ? 0.3382 0.4890 0.2475 0.0648  0.0272  0.0136  749  ALA A O   
5561  C CB  . ALA A 751  ? 0.3047 0.4331 0.2224 0.0618  0.0264  0.0060  749  ALA A CB  
5562  N N   . GLY A 752  ? 0.3068 0.4661 0.2134 0.0702  0.0258  -0.0004 750  GLY A N   
5563  C CA  . GLY A 752  ? 0.3461 0.5143 0.2482 0.0721  0.0249  -0.0003 750  GLY A CA  
5564  C C   . GLY A 752  ? 0.3794 0.5430 0.2809 0.0731  0.0218  -0.0076 750  GLY A C   
5565  O O   . GLY A 752  ? 0.3639 0.5351 0.2618 0.0748  0.0208  -0.0081 750  GLY A O   
5566  N N   . ILE A 753  ? 0.3303 0.4822 0.2356 0.0720  0.0201  -0.0132 751  ILE A N   
5567  C CA  . ILE A 753  ? 0.3105 0.4589 0.2157 0.0731  0.0171  -0.0205 751  ILE A CA  
5568  C C   . ILE A 753  ? 0.3146 0.4744 0.2170 0.0775  0.0163  -0.0281 751  ILE A C   
5569  O O   . ILE A 753  ? 0.3426 0.5047 0.2464 0.0790  0.0170  -0.0321 751  ILE A O   
5570  C CB  . ILE A 753  ? 0.3012 0.4350 0.2114 0.0709  0.0154  -0.0244 751  ILE A CB  
5571  C CG1 . ILE A 753  ? 0.2738 0.3969 0.1868 0.0667  0.0163  -0.0171 751  ILE A CG1 
5572  C CG2 . ILE A 753  ? 0.3462 0.4769 0.2567 0.0719  0.0122  -0.0316 751  ILE A CG2 
5573  C CD1 . ILE A 753  ? 0.2850 0.4056 0.1968 0.0652  0.0152  -0.0134 751  ILE A CD1 
5574  N N   . PRO A 754  ? 0.3388 0.5065 0.2375 0.0797  0.0149  -0.0305 752  PRO A N   
5575  C CA  . PRO A 754  ? 0.3880 0.5673 0.2840 0.0841  0.0140  -0.0383 752  PRO A CA  
5576  C C   . PRO A 754  ? 0.2900 0.4622 0.1900 0.0851  0.0115  -0.0482 752  PRO A C   
5577  O O   . PRO A 754  ? 0.3150 0.4743 0.2188 0.0827  0.0096  -0.0498 752  PRO A O   
5578  C CB  . PRO A 754  ? 0.3970 0.5836 0.2889 0.0855  0.0125  -0.0385 752  PRO A CB  
5579  C CG  . PRO A 754  ? 0.3858 0.5677 0.2773 0.0821  0.0135  -0.0287 752  PRO A CG  
5580  C CD  . PRO A 754  ? 0.3263 0.4931 0.2231 0.0783  0.0139  -0.0261 752  PRO A CD  
5581  N N   . ALA A 755  ? 0.3573 0.5384 0.2566 0.0888  0.0115  -0.0548 753  ALA A N   
5582  C CA  . ALA A 755  ? 0.3618 0.5374 0.2653 0.0903  0.0089  -0.0647 753  ALA A CA  
5583  C C   . ALA A 755  ? 0.3587 0.5295 0.2632 0.0904  0.0053  -0.0703 753  ALA A C   
5584  O O   . ALA A 755  ? 0.3600 0.5201 0.2696 0.0895  0.0029  -0.0756 753  ALA A O   
5585  C CB  . ALA A 755  ? 0.3336 0.5219 0.2357 0.0949  0.0093  -0.0713 753  ALA A CB  
5586  N N   . SER A 756  ? 0.3127 0.4915 0.2127 0.0916  0.0047  -0.0692 754  SER A N   
5587  C CA  . SER A 756  ? 0.3247 0.4995 0.2258 0.0917  0.0013  -0.0745 754  SER A CA  
5588  C C   . SER A 756  ? 0.3346 0.4947 0.2389 0.0872  0.0006  -0.0699 754  SER A C   
5589  O O   . SER A 756  ? 0.3517 0.5049 0.2589 0.0866  -0.0024 -0.0748 754  SER A O   
5590  C CB  . SER A 756  ? 0.3606 0.5485 0.2557 0.0943  0.0009  -0.0745 754  SER A CB  
5591  O OG  . SER A 756  ? 0.3689 0.5588 0.2607 0.0921  0.0032  -0.0641 754  SER A OG  
5592  N N   . ALA A 757  ? 0.3237 0.4792 0.2277 0.0840  0.0032  -0.0606 755  ALA A N   
5593  C CA  . ALA A 757  ? 0.2894 0.4318 0.1964 0.0799  0.0028  -0.0560 755  ALA A CA  
5594  C C   . ALA A 757  ? 0.2981 0.4277 0.2109 0.0774  0.0025  -0.0572 755  ALA A C   
5595  O O   . ALA A 757  ? 0.2957 0.4142 0.2116 0.0743  0.0015  -0.0556 755  ALA A O   
5596  C CB  . ALA A 757  ? 0.3091 0.4525 0.2135 0.0776  0.0054  -0.0454 755  ALA A CB  
5597  N N   . LEU A 758  ? 0.2744 0.4057 0.1887 0.0789  0.0035  -0.0601 756  LEU A N   
5598  C CA  . LEU A 758  ? 0.2600 0.3798 0.1798 0.0766  0.0033  -0.0608 756  LEU A CA  
5599  C C   . LEU A 758  ? 0.3092 0.4320 0.2315 0.0797  0.0021  -0.0693 756  LEU A C   
5600  O O   . LEU A 758  ? 0.3409 0.4718 0.2615 0.0819  0.0040  -0.0694 756  LEU A O   
5601  C CB  . LEU A 758  ? 0.3116 0.4286 0.2315 0.0741  0.0066  -0.0524 756  LEU A CB  
5602  C CG  . LEU A 758  ? 0.2864 0.3924 0.2116 0.0719  0.0066  -0.0527 756  LEU A CG  
5603  C CD1 . LEU A 758  ? 0.2756 0.3695 0.2049 0.0694  0.0040  -0.0550 756  LEU A CD1 
5604  C CD2 . LEU A 758  ? 0.3231 0.4267 0.2480 0.0693  0.0097  -0.0441 756  LEU A CD2 
5605  N N   . GLN A 759  ? 0.2846 0.4011 0.2111 0.0800  -0.0012 -0.0763 757  GLN A N   
5606  C CA  . GLN A 759  ? 0.3070 0.4247 0.2371 0.0828  -0.0030 -0.0849 757  GLN A CA  
5607  C C   . GLN A 759  ? 0.3280 0.4324 0.2648 0.0801  -0.0039 -0.0853 757  GLN A C   
5608  O O   . GLN A 759  ? 0.3594 0.4535 0.2988 0.0768  -0.0051 -0.0830 757  GLN A O   
5609  C CB  . GLN A 759  ? 0.3359 0.4577 0.2663 0.0855  -0.0065 -0.0934 757  GLN A CB  
5610  C CG  . GLN A 759  ? 0.3290 0.4653 0.2528 0.0887  -0.0058 -0.0940 757  GLN A CG  
5611  C CD  . GLN A 759  ? 0.3246 0.4642 0.2489 0.0911  -0.0095 -0.1022 757  GLN A CD  
5612  O OE1 . GLN A 759  ? 0.3276 0.4729 0.2534 0.0947  -0.0114 -0.1108 757  GLN A OE1 
5613  N NE2 . GLN A 759  ? 0.3247 0.4604 0.2482 0.0891  -0.0108 -0.0999 757  GLN A NE2 
5614  N N   . LEU A 760  ? 0.3357 0.4408 0.2751 0.0816  -0.0034 -0.0881 758  LEU A N   
5615  C CA  . LEU A 760  ? 0.3161 0.4095 0.2618 0.0794  -0.0042 -0.0885 758  LEU A CA  
5616  C C   . LEU A 760  ? 0.3165 0.4080 0.2677 0.0817  -0.0080 -0.0982 758  LEU A C   
5617  O O   . LEU A 760  ? 0.3232 0.4236 0.2738 0.0857  -0.0086 -0.1045 758  LEU A O   
5618  C CB  . LEU A 760  ? 0.3424 0.4371 0.2881 0.0792  -0.0013 -0.0846 758  LEU A CB  
5619  C CG  . LEU A 760  ? 0.3234 0.4071 0.2755 0.0773  -0.0020 -0.0849 758  LEU A CG  
5620  C CD1 . LEU A 760  ? 0.3182 0.3912 0.2713 0.0724  -0.0011 -0.0774 758  LEU A CD1 
5621  C CD2 . LEU A 760  ? 0.3204 0.4088 0.2728 0.0791  0.0000  -0.0850 758  LEU A CD2 
5622  N N   . LEU A 761  ? 0.3233 0.4034 0.2800 0.0791  -0.0106 -0.0994 759  LEU A N   
5623  C CA  . LEU A 761  ? 0.3390 0.4159 0.3022 0.0808  -0.0146 -0.1082 759  LEU A CA  
5624  C C   . LEU A 761  ? 0.3107 0.3759 0.2809 0.0782  -0.0155 -0.1072 759  LEU A C   
5625  O O   . LEU A 761  ? 0.3423 0.3977 0.3163 0.0750  -0.0171 -0.1053 759  LEU A O   
5626  C CB  . LEU A 761  ? 0.3355 0.4106 0.2994 0.0803  -0.0176 -0.1114 759  LEU A CB  
5627  C CG  . LEU A 761  ? 0.3510 0.4369 0.3088 0.0827  -0.0176 -0.1130 759  LEU A CG  
5628  C CD1 . LEU A 761  ? 0.3080 0.4072 0.2620 0.0874  -0.0166 -0.1175 759  LEU A CD1 
5629  C CD2 . LEU A 761  ? 0.4085 0.4944 0.3605 0.0798  -0.0149 -0.1040 759  LEU A CD2 
5630  N N   . PRO A 762  ? 0.3220 0.3881 0.2941 0.0797  -0.0145 -0.1082 760  PRO A N   
5631  C CA  . PRO A 762  ? 0.3429 0.3982 0.3219 0.0774  -0.0155 -0.1074 760  PRO A CA  
5632  C C   . PRO A 762  ? 0.3951 0.4447 0.3819 0.0781  -0.0202 -0.1147 760  PRO A C   
5633  O O   . PRO A 762  ? 0.3487 0.4040 0.3362 0.0814  -0.0226 -0.1225 760  PRO A O   
5634  C CB  . PRO A 762  ? 0.3057 0.3659 0.2847 0.0797  -0.0135 -0.1079 760  PRO A CB  
5635  C CG  . PRO A 762  ? 0.3180 0.3907 0.2890 0.0820  -0.0105 -0.1063 760  PRO A CG  
5636  C CD  . PRO A 762  ? 0.3108 0.3884 0.2789 0.0833  -0.0122 -0.1098 760  PRO A CD  
5637  N N   . GLY A 763  ? 0.3212 0.3594 0.3140 0.0747  -0.0215 -0.1122 761  GLY A N   
5638  C CA  . GLY A 763  ? 0.4041 0.4358 0.4055 0.0748  -0.0259 -0.1182 761  GLY A CA  
5639  C C   . GLY A 763  ? 0.4552 0.4756 0.4604 0.0700  -0.0269 -0.1128 761  GLY A C   
5640  O O   . GLY A 763  ? 0.4093 0.4271 0.4107 0.0668  -0.0241 -0.1049 761  GLY A O   
5641  N N   . ASP A 764  ? 0.4781 0.4924 0.4913 0.0696  -0.0311 -0.1174 762  ASP A N   
5642  C CA  . ASP A 764  ? 0.5622 0.5659 0.5806 0.0651  -0.0325 -0.1130 762  ASP A CA  
5643  C C   . ASP A 764  ? 0.5413 0.5447 0.5574 0.0632  -0.0332 -0.1117 762  ASP A C   
5644  O O   . ASP A 764  ? 0.4977 0.5086 0.5068 0.0647  -0.0316 -0.1121 762  ASP A O   
5645  C CB  . ASP A 764  ? 0.5945 0.5916 0.6234 0.0655  -0.0366 -0.1180 762  ASP A CB  
5646  C CG  . ASP A 764  ? 0.6152 0.6160 0.6481 0.0689  -0.0406 -0.1277 762  ASP A CG  
5647  O OD1 . ASP A 764  ? 0.6614 0.6678 0.6897 0.0700  -0.0407 -0.1300 762  ASP A OD1 
5648  O OD2 . ASP A 764  ? 0.6984 0.6964 0.7392 0.0707  -0.0438 -0.1333 762  ASP A OD2 
5649  N N   . GLY A 765  ? 0.5511 0.5461 0.5732 0.0598  -0.0355 -0.1099 763  GLY A N   
5650  C CA  . GLY A 765  ? 0.5010 0.4953 0.5216 0.0577  -0.0363 -0.1085 763  GLY A CA  
5651  C C   . GLY A 765  ? 0.5011 0.5007 0.5223 0.0607  -0.0392 -0.1164 763  GLY A C   
5652  O O   . GLY A 765  ? 0.5283 0.5301 0.5460 0.0599  -0.0392 -0.1156 763  GLY A O   
5653  N N   . ARG A 766  ? 0.4789 0.4808 0.5047 0.0642  -0.0418 -0.1243 764  ARG A N   
5654  C CA  . ARG A 766  ? 0.5194 0.5273 0.5456 0.0675  -0.0447 -0.1326 764  ARG A CA  
5655  C C   . ARG A 766  ? 0.5438 0.5627 0.5597 0.0701  -0.0418 -0.1327 764  ARG A C   
5656  O O   . ARG A 766  ? 0.4484 0.4718 0.4619 0.0711  -0.0430 -0.1356 764  ARG A O   
5657  C CB  . ARG A 766  ? 0.4601 0.4685 0.4935 0.0710  -0.0481 -0.1413 764  ARG A CB  
5658  N N   . VAL A 767  ? 0.5004 0.5238 0.5104 0.0712  -0.0379 -0.1292 765  VAL A N   
5659  C CA  . VAL A 767  ? 0.4440 0.4776 0.4442 0.0732  -0.0348 -0.1276 765  VAL A CA  
5660  C C   . VAL A 767  ? 0.4150 0.4467 0.4107 0.0697  -0.0330 -0.1203 765  VAL A C   
5661  O O   . VAL A 767  ? 0.4326 0.4708 0.4230 0.0708  -0.0328 -0.1210 765  VAL A O   
5662  C CB  . VAL A 767  ? 0.3583 0.3966 0.3541 0.0747  -0.0311 -0.1247 765  VAL A CB  
5663  C CG1 . VAL A 767  ? 0.3758 0.4251 0.3620 0.0766  -0.0280 -0.1225 765  VAL A CG1 
5664  C CG2 . VAL A 767  ? 0.4863 0.5267 0.4871 0.0783  -0.0330 -0.1322 765  VAL A CG2 
5665  N N   . GLY A 768  ? 0.4281 0.4510 0.4257 0.0655  -0.0318 -0.1133 766  GLY A N   
5666  C CA  . GLY A 768  ? 0.3647 0.3853 0.3588 0.0622  -0.0303 -0.1068 766  GLY A CA  
5667  C C   . GLY A 768  ? 0.3578 0.3776 0.3542 0.0617  -0.0335 -0.1102 766  GLY A C   
5668  O O   . GLY A 768  ? 0.3491 0.3734 0.3401 0.0616  -0.0326 -0.1085 766  GLY A O   
5669  N N   . ALA A 769  ? 0.3962 0.4107 0.4010 0.0614  -0.0374 -0.1153 767  ALA A N   
5670  C CA  . ALA A 769  ? 0.4517 0.4649 0.4600 0.0606  -0.0407 -0.1186 767  ALA A CA  
5671  C C   . ALA A 769  ? 0.4141 0.4371 0.4184 0.0646  -0.0419 -0.1252 767  ALA A C   
5672  O O   . ALA A 769  ? 0.4283 0.4536 0.4303 0.0640  -0.0427 -0.1251 767  ALA A O   
5673  C CB  . ALA A 769  ? 0.3976 0.4029 0.4167 0.0594  -0.0448 -0.1225 767  ALA A CB  
5674  N N   . ALA A 770  ? 0.4268 0.4562 0.4303 0.0687  -0.0422 -0.1310 768  ALA A N   
5675  C CA  . ALA A 770  ? 0.3735 0.4134 0.3727 0.0728  -0.0432 -0.1374 768  ALA A CA  
5676  C C   . ALA A 770  ? 0.3196 0.3665 0.3090 0.0727  -0.0397 -0.1317 768  ALA A C   
5677  O O   . ALA A 770  ? 0.3627 0.4157 0.3489 0.0741  -0.0408 -0.1342 768  ALA A O   
5678  C CB  . ALA A 770  ? 0.4131 0.4594 0.4127 0.0772  -0.0435 -0.1439 768  ALA A CB  
5679  N N   . LEU A 771  ? 0.3380 0.3840 0.3227 0.0711  -0.0355 -0.1239 769  LEU A N   
5680  C CA  . LEU A 771  ? 0.3212 0.3729 0.2973 0.0707  -0.0322 -0.1177 769  LEU A CA  
5681  C C   . LEU A 771  ? 0.3122 0.3593 0.2886 0.0674  -0.0329 -0.1138 769  LEU A C   
5682  O O   . LEU A 771  ? 0.3473 0.4005 0.3186 0.0682  -0.0326 -0.1133 769  LEU A O   
5683  C CB  . LEU A 771  ? 0.3029 0.3537 0.2755 0.0695  -0.0280 -0.1104 769  LEU A CB  
5684  C CG  . LEU A 771  ? 0.3127 0.3696 0.2840 0.0728  -0.0267 -0.1132 769  LEU A CG  
5685  C CD1 . LEU A 771  ? 0.3389 0.3926 0.3082 0.0708  -0.0229 -0.1055 769  LEU A CD1 
5686  C CD2 . LEU A 771  ? 0.3720 0.4421 0.3367 0.0769  -0.0260 -0.1164 769  LEU A CD2 
5687  N N   . VAL A 772  ? 0.3429 0.3795 0.3251 0.0636  -0.0337 -0.1108 770  VAL A N   
5688  C CA  . VAL A 772  ? 0.3205 0.3525 0.3033 0.0602  -0.0341 -0.1068 770  VAL A CA  
5689  C C   . VAL A 772  ? 0.3531 0.3882 0.3377 0.0616  -0.0377 -0.1130 770  VAL A C   
5690  O O   . VAL A 772  ? 0.3567 0.3938 0.3382 0.0607  -0.0376 -0.1107 770  VAL A O   
5691  C CB  . VAL A 772  ? 0.3176 0.3385 0.3070 0.0562  -0.0345 -0.1031 770  VAL A CB  
5692  C CG1 . VAL A 772  ? 0.3700 0.3865 0.3616 0.0530  -0.0358 -0.1007 770  VAL A CG1 
5693  C CG2 . VAL A 772  ? 0.3524 0.3706 0.3387 0.0545  -0.0306 -0.0958 770  VAL A CG2 
5694  N N   . ALA A 773  ? 0.3655 0.4014 0.3555 0.0639  -0.0411 -0.1212 771  ALA A N   
5695  C CA  . ALA A 773  ? 0.3405 0.3786 0.3336 0.0650  -0.0450 -0.1277 771  ALA A CA  
5696  C C   . ALA A 773  ? 0.4228 0.4728 0.4090 0.0691  -0.0450 -0.1318 771  ALA A C   
5697  O O   . ALA A 773  ? 0.4440 0.4969 0.4316 0.0700  -0.0480 -0.1367 771  ALA A O   
5698  C CB  . ALA A 773  ? 0.3650 0.3987 0.3675 0.0658  -0.0491 -0.1352 771  ALA A CB  
5699  N N   . ALA A 774  ? 0.3962 0.4535 0.3755 0.0715  -0.0418 -0.1300 772  ALA A N   
5700  C CA  . ALA A 774  ? 0.3788 0.4484 0.3518 0.0756  -0.0418 -0.1341 772  ALA A CA  
5701  C C   . ALA A 774  ? 0.3892 0.4623 0.3571 0.0746  -0.0413 -0.1301 772  ALA A C   
5702  O O   . ALA A 774  ? 0.3869 0.4560 0.3522 0.0715  -0.0386 -0.1219 772  ALA A O   
5703  C CB  . ALA A 774  ? 0.3815 0.4583 0.3484 0.0781  -0.0383 -0.1320 772  ALA A CB  
5704  N N   . ALA A 775  ? 0.4009 0.4817 0.3675 0.0774  -0.0439 -0.1363 773  ALA A N   
5705  C CA  . ALA A 775  ? 0.4505 0.5336 0.4138 0.0763  -0.0442 -0.1336 773  ALA A CA  
5706  C C   . ALA A 775  ? 0.3683 0.4565 0.3230 0.0760  -0.0400 -0.1251 773  ALA A C   
5707  O O   . ALA A 775  ? 0.4131 0.4992 0.3661 0.0736  -0.0393 -0.1197 773  ALA A O   
5708  C CB  . ALA A 775  ? 0.4840 0.5756 0.4471 0.0798  -0.0478 -0.1422 773  ALA A CB  
5709  N N   . GLU A 776  ? 0.3611 0.4561 0.3107 0.0784  -0.0372 -0.1238 774  GLU A N   
5710  C CA  . GLU A 776  ? 0.3243 0.4247 0.2662 0.0782  -0.0335 -0.1157 774  GLU A CA  
5711  C C   . GLU A 776  ? 0.2940 0.3857 0.2363 0.0745  -0.0302 -0.1070 774  GLU A C   
5712  O O   . GLU A 776  ? 0.3636 0.4584 0.3006 0.0739  -0.0272 -0.0997 774  GLU A O   
5713  C CB  . GLU A 776  ? 0.3754 0.4882 0.3115 0.0824  -0.0319 -0.1176 774  GLU A CB  
5714  C CG  . GLU A 776  ? 0.4805 0.6037 0.4153 0.0865  -0.0349 -0.1263 774  GLU A CG  
5715  C CD  . GLU A 776  ? 0.5452 0.6688 0.4850 0.0891  -0.0374 -0.1358 774  GLU A CD  
5716  O OE1 . GLU A 776  ? 0.4429 0.5564 0.3889 0.0871  -0.0376 -0.1362 774  GLU A OE1 
5717  O OE2 . GLU A 776  ? 0.6283 0.7626 0.5661 0.0933  -0.0391 -0.1430 774  GLU A OE2 
5718  N N   . THR A 777  ? 0.3217 0.4029 0.2705 0.0721  -0.0309 -0.1075 775  THR A N   
5719  C CA  . THR A 777  ? 0.3511 0.4241 0.3006 0.0685  -0.0281 -0.0996 775  THR A CA  
5720  C C   . THR A 777  ? 0.3092 0.3783 0.2578 0.0654  -0.0276 -0.0937 775  THR A C   
5721  O O   . THR A 777  ? 0.3617 0.4265 0.3144 0.0640  -0.0303 -0.0961 775  THR A O   
5722  C CB  . THR A 777  ? 0.3201 0.3834 0.2771 0.0667  -0.0293 -0.1020 775  THR A CB  
5723  O OG1 . THR A 777  ? 0.3412 0.4084 0.2985 0.0696  -0.0291 -0.1063 775  THR A OG1 
5724  C CG2 . THR A 777  ? 0.3097 0.3641 0.2678 0.0626  -0.0268 -0.0939 775  THR A CG2 
5725  N N   . ALA A 778  ? 0.2969 0.3679 0.2405 0.0646  -0.0243 -0.0862 776  ALA A N   
5726  C CA  . ALA A 778  ? 0.2737 0.3428 0.2155 0.0624  -0.0238 -0.0807 776  ALA A CA  
5727  C C   . ALA A 778  ? 0.3091 0.3682 0.2538 0.0584  -0.0221 -0.0745 776  ALA A C   
5728  O O   . ALA A 778  ? 0.3131 0.3696 0.2575 0.0563  -0.0219 -0.0704 776  ALA A O   
5729  C CB  . ALA A 778  ? 0.3200 0.3985 0.2546 0.0642  -0.0216 -0.0762 776  ALA A CB  
5730  N N   . GLY A 779  ? 0.3046 0.3585 0.2521 0.0574  -0.0210 -0.0741 777  GLY A N   
5731  C CA  . GLY A 779  ? 0.2655 0.3104 0.2156 0.0538  -0.0195 -0.0685 777  GLY A CA  
5732  C C   . GLY A 779  ? 0.2634 0.3043 0.2166 0.0535  -0.0188 -0.0697 777  GLY A C   
5733  O O   . GLY A 779  ? 0.2811 0.3273 0.2329 0.0563  -0.0186 -0.0729 777  GLY A O   
5734  N N   . VAL A 780  ? 0.2872 0.3191 0.2448 0.0503  -0.0187 -0.0672 778  VAL A N   
5735  C CA  . VAL A 780  ? 0.2818 0.3090 0.2430 0.0498  -0.0182 -0.0679 778  VAL A CA  
5736  C C   . VAL A 780  ? 0.2768 0.2985 0.2378 0.0468  -0.0156 -0.0608 778  VAL A C   
5737  O O   . VAL A 780  ? 0.2650 0.2825 0.2269 0.0442  -0.0155 -0.0573 778  VAL A O   
5738  C CB  . VAL A 780  ? 0.2794 0.3010 0.2476 0.0489  -0.0215 -0.0730 778  VAL A CB  
5739  C CG1 . VAL A 780  ? 0.2996 0.3162 0.2718 0.0483  -0.0212 -0.0733 778  VAL A CG1 
5740  C CG2 . VAL A 780  ? 0.3080 0.3353 0.2768 0.0520  -0.0245 -0.0807 778  VAL A CG2 
5741  N N   . MET A 781  ? 0.2735 0.2957 0.2332 0.0473  -0.0134 -0.0587 779  MET A N   
5742  C CA  . MET A 781  ? 0.2522 0.2689 0.2125 0.0447  -0.0111 -0.0529 779  MET A CA  
5743  C C   . MET A 781  ? 0.2529 0.2646 0.2181 0.0442  -0.0119 -0.0552 779  MET A C   
5744  O O   . MET A 781  ? 0.2883 0.3034 0.2533 0.0465  -0.0117 -0.0581 779  MET A O   
5745  C CB  . MET A 781  ? 0.2726 0.2940 0.2277 0.0456  -0.0080 -0.0482 779  MET A CB  
5746  C CG  . MET A 781  ? 0.2499 0.2767 0.2006 0.0463  -0.0076 -0.0460 779  MET A CG  
5747  S SD  . MET A 781  ? 0.2862 0.3201 0.2313 0.0478  -0.0044 -0.0409 779  MET A SD  
5748  C CE  . MET A 781  ? 0.2639 0.2902 0.2105 0.0442  -0.0023 -0.0338 779  MET A CE  
5749  N N   . PHE A 782  ? 0.2640 0.2682 0.2338 0.0412  -0.0128 -0.0538 780  PHE A N   
5750  C CA  . PHE A 782  ? 0.2843 0.2833 0.2595 0.0404  -0.0138 -0.0555 780  PHE A CA  
5751  C C   . PHE A 782  ? 0.3063 0.2998 0.2824 0.0374  -0.0119 -0.0497 780  PHE A C   
5752  O O   . PHE A 782  ? 0.2896 0.2804 0.2653 0.0350  -0.0113 -0.0459 780  PHE A O   
5753  C CB  . PHE A 782  ? 0.2793 0.2744 0.2603 0.0395  -0.0173 -0.0597 780  PHE A CB  
5754  C CG  . PHE A 782  ? 0.2987 0.2877 0.2860 0.0382  -0.0185 -0.0605 780  PHE A CG  
5755  C CD1 . PHE A 782  ? 0.3012 0.2913 0.2909 0.0405  -0.0197 -0.0652 780  PHE A CD1 
5756  C CD2 . PHE A 782  ? 0.2967 0.2793 0.2874 0.0346  -0.0185 -0.0564 780  PHE A CD2 
5757  C CE1 . PHE A 782  ? 0.3431 0.3276 0.3389 0.0394  -0.0210 -0.0658 780  PHE A CE1 
5758  C CE2 . PHE A 782  ? 0.2663 0.2437 0.2629 0.0334  -0.0197 -0.0567 780  PHE A CE2 
5759  C CZ  . PHE A 782  ? 0.3059 0.2839 0.3051 0.0358  -0.0210 -0.0613 780  PHE A CZ  
5760  N N   . THR A 783  ? 0.2546 0.2467 0.2319 0.0377  -0.0110 -0.0493 781  THR A N   
5761  C CA  . THR A 783  ? 0.2908 0.2773 0.2702 0.0350  -0.0097 -0.0448 781  THR A CA  
5762  C C   . THR A 783  ? 0.3001 0.2827 0.2851 0.0350  -0.0115 -0.0476 781  THR A C   
5763  O O   . THR A 783  ? 0.3133 0.2987 0.2985 0.0376  -0.0118 -0.0512 781  THR A O   
5764  C CB  . THR A 783  ? 0.2686 0.2573 0.2436 0.0352  -0.0065 -0.0403 781  THR A CB  
5765  O OG1 . THR A 783  ? 0.3068 0.2991 0.2771 0.0352  -0.0052 -0.0377 781  THR A OG1 
5766  C CG2 . THR A 783  ? 0.3034 0.2866 0.2806 0.0323  -0.0054 -0.0359 781  THR A CG2 
5767  N N   . GLY A 784  ? 0.3092 0.2858 0.2990 0.0322  -0.0127 -0.0461 782  GLY A N   
5768  C CA  . GLY A 784  ? 0.2838 0.2564 0.2799 0.0320  -0.0149 -0.0487 782  GLY A CA  
5769  C C   . GLY A 784  ? 0.2894 0.2564 0.2906 0.0287  -0.0166 -0.0468 782  GLY A C   
5770  O O   . GLY A 784  ? 0.3219 0.2878 0.3212 0.0264  -0.0154 -0.0426 782  GLY A O   
5771  N N   . SER A 785  ? 0.3175 0.2811 0.3252 0.0286  -0.0195 -0.0498 783  SER A N   
5772  C CA  . SER A 785  ? 0.3597 0.3180 0.3730 0.0252  -0.0211 -0.0474 783  SER A CA  
5773  C C   . SER A 785  ? 0.3909 0.3500 0.4045 0.0242  -0.0225 -0.0483 783  SER A C   
5774  O O   . SER A 785  ? 0.3248 0.2875 0.3367 0.0264  -0.0235 -0.0526 783  SER A O   
5775  C CB  . SER A 785  ? 0.3821 0.3366 0.4031 0.0254  -0.0241 -0.0503 783  SER A CB  
5776  O OG  . SER A 785  ? 0.3849 0.3411 0.4085 0.0278  -0.0268 -0.0567 783  SER A OG  
5777  N N   . THR A 786  ? 0.3587 0.3148 0.3746 0.0208  -0.0225 -0.0441 784  THR A N   
5778  C CA  . THR A 786  ? 0.3715 0.3281 0.3885 0.0195  -0.0239 -0.0445 784  THR A CA  
5779  C C   . THR A 786  ? 0.3070 0.2627 0.3300 0.0203  -0.0276 -0.0499 784  THR A C   
5780  O O   . THR A 786  ? 0.3431 0.3012 0.3654 0.0210  -0.0289 -0.0528 784  THR A O   
5781  C CB  . THR A 786  ? 0.3918 0.3456 0.4109 0.0156  -0.0233 -0.0390 784  THR A CB  
5782  O OG1 . THR A 786  ? 0.4077 0.3624 0.4217 0.0151  -0.0200 -0.0345 784  THR A OG1 
5783  C CG2 . THR A 786  ? 0.4118 0.3670 0.4314 0.0143  -0.0243 -0.0391 784  THR A CG2 
5784  N N   . GLU A 787  ? 0.3985 0.3506 0.4278 0.0204  -0.0297 -0.0516 785  GLU A N   
5785  C CA  . GLU A 787  ? 0.3584 0.3091 0.3946 0.0211  -0.0337 -0.0569 785  GLU A CA  
5786  C C   . GLU A 787  ? 0.3118 0.2671 0.3449 0.0251  -0.0344 -0.0635 785  GLU A C   
5787  O O   . GLU A 787  ? 0.3207 0.2772 0.3563 0.0258  -0.0370 -0.0679 785  GLU A O   
5788  C CB  . GLU A 787  ? 0.4251 0.3708 0.4689 0.0204  -0.0357 -0.0571 785  GLU A CB  
5789  N N   . VAL A 788  ? 0.3456 0.3041 0.3733 0.0278  -0.0322 -0.0643 786  VAL A N   
5790  C CA  . VAL A 788  ? 0.3126 0.2766 0.3369 0.0317  -0.0327 -0.0704 786  VAL A CA  
5791  C C   . VAL A 788  ? 0.3041 0.2729 0.3220 0.0321  -0.0313 -0.0698 786  VAL A C   
5792  O O   . VAL A 788  ? 0.3312 0.3037 0.3487 0.0341  -0.0332 -0.0749 786  VAL A O   
5793  C CB  . VAL A 788  ? 0.3170 0.2836 0.3377 0.0344  -0.0306 -0.0711 786  VAL A CB  
5794  C CG1 . VAL A 788  ? 0.3279 0.3019 0.3431 0.0383  -0.0302 -0.0759 786  VAL A CG1 
5795  C CG2 . VAL A 788  ? 0.3758 0.3384 0.4039 0.0349  -0.0329 -0.0738 786  VAL A CG2 
5796  N N   . ALA A 789  ? 0.2916 0.2606 0.3047 0.0301  -0.0283 -0.0637 787  ALA A N   
5797  C CA  . ALA A 789  ? 0.2595 0.2324 0.2673 0.0302  -0.0273 -0.0628 787  ALA A CA  
5798  C C   . ALA A 789  ? 0.2653 0.2373 0.2777 0.0290  -0.0303 -0.0652 787  ALA A C   
5799  O O   . ALA A 789  ? 0.2816 0.2579 0.2912 0.0305  -0.0310 -0.0680 787  ALA A O   
5800  C CB  . ALA A 789  ? 0.2400 0.2121 0.2437 0.0278  -0.0241 -0.0558 787  ALA A CB  
5801  N N   . ARG A 790  ? 0.2699 0.2364 0.2894 0.0261  -0.0322 -0.0640 788  ARG A N   
5802  C CA  . ARG A 790  ? 0.2806 0.2460 0.3052 0.0247  -0.0352 -0.0659 788  ARG A CA  
5803  C C   . ARG A 790  ? 0.2966 0.2641 0.3243 0.0275  -0.0385 -0.0736 788  ARG A C   
5804  O O   . ARG A 790  ? 0.3075 0.2774 0.3356 0.0279  -0.0403 -0.0765 788  ARG A O   
5805  C CB  . ARG A 790  ? 0.3266 0.2860 0.3585 0.0209  -0.0364 -0.0623 788  ARG A CB  
5806  C CG  . ARG A 790  ? 0.3362 0.2942 0.3739 0.0186  -0.0391 -0.0627 788  ARG A CG  
5807  C CD  . ARG A 790  ? 0.3689 0.3217 0.4131 0.0146  -0.0396 -0.0576 788  ARG A CD  
5808  N NE  . ARG A 790  ? 0.3798 0.3330 0.4195 0.0124  -0.0362 -0.0510 788  ARG A NE  
5809  C CZ  . ARG A 790  ? 0.4265 0.3773 0.4659 0.0110  -0.0343 -0.0465 788  ARG A CZ  
5810  N NH1 . ARG A 790  ? 0.4366 0.3842 0.4800 0.0115  -0.0354 -0.0474 788  ARG A NH1 
5811  N NH2 . ARG A 790  ? 0.4035 0.3553 0.4389 0.0092  -0.0314 -0.0411 788  ARG A NH2 
5812  N N   . LEU A 791  ? 0.3079 0.2748 0.3376 0.0297  -0.0394 -0.0772 789  LEU A N   
5813  C CA  . LEU A 791  ? 0.3235 0.2932 0.3558 0.0330  -0.0425 -0.0851 789  LEU A CA  
5814  C C   . LEU A 791  ? 0.3050 0.2824 0.3292 0.0362  -0.0411 -0.0879 789  LEU A C   
5815  O O   . LEU A 791  ? 0.3156 0.2963 0.3409 0.0379  -0.0436 -0.0933 789  LEU A O   
5816  C CB  . LEU A 791  ? 0.3129 0.2807 0.3490 0.0348  -0.0434 -0.0882 789  LEU A CB  
5817  C CG  . LEU A 791  ? 0.3662 0.3264 0.4116 0.0321  -0.0456 -0.0865 789  LEU A CG  
5818  C CD1 . LEU A 791  ? 0.4085 0.3675 0.4561 0.0342  -0.0458 -0.0888 789  LEU A CD1 
5819  C CD2 . LEU A 791  ? 0.3834 0.3412 0.4374 0.0313  -0.0501 -0.0907 789  LEU A CD2 
5820  N N   . ILE A 792  ? 0.2918 0.2724 0.3081 0.0370  -0.0373 -0.0840 790  ILE A N   
5821  C CA  . ILE A 792  ? 0.3219 0.3102 0.3305 0.0398  -0.0359 -0.0856 790  ILE A CA  
5822  C C   . ILE A 792  ? 0.2936 0.2833 0.3007 0.0383  -0.0363 -0.0841 790  ILE A C   
5823  O O   . ILE A 792  ? 0.3166 0.3117 0.3215 0.0405  -0.0376 -0.0883 790  ILE A O   
5824  C CB  . ILE A 792  ? 0.2904 0.2814 0.2917 0.0406  -0.0317 -0.0811 790  ILE A CB  
5825  C CG1 . ILE A 792  ? 0.3146 0.3061 0.3172 0.0429  -0.0316 -0.0839 790  ILE A CG1 
5826  C CG2 . ILE A 792  ? 0.2941 0.2928 0.2874 0.0427  -0.0300 -0.0807 790  ILE A CG2 
5827  C CD1 . ILE A 792  ? 0.3199 0.3127 0.3171 0.0430  -0.0277 -0.0788 790  ILE A CD1 
5828  N N   . GLN A 793  ? 0.2675 0.2527 0.2757 0.0346  -0.0352 -0.0782 791  GLN A N   
5829  C CA  . GLN A 793  ? 0.2550 0.2411 0.2626 0.0330  -0.0356 -0.0767 791  GLN A CA  
5830  C C   . GLN A 793  ? 0.2835 0.2698 0.2967 0.0334  -0.0398 -0.0826 791  GLN A C   
5831  O O   . GLN A 793  ? 0.2940 0.2848 0.3047 0.0345  -0.0406 -0.0847 791  GLN A O   
5832  C CB  . GLN A 793  ? 0.3132 0.2940 0.3229 0.0289  -0.0342 -0.0701 791  GLN A CB  
5833  C CG  . GLN A 793  ? 0.3283 0.3096 0.3382 0.0269  -0.0347 -0.0681 791  GLN A CG  
5834  C CD  . GLN A 793  ? 0.3919 0.3680 0.4060 0.0228  -0.0342 -0.0629 791  GLN A CD  
5835  O OE1 . GLN A 793  ? 0.4371 0.4086 0.4576 0.0211  -0.0356 -0.0627 791  GLN A OE1 
5836  N NE2 . GLN A 793  ? 0.4152 0.3924 0.4260 0.0212  -0.0322 -0.0585 791  GLN A NE2 
5837  N N   . ALA A 794  ? 0.3306 0.3123 0.3519 0.0326  -0.0425 -0.0854 792  ALA A N   
5838  C CA  . ALA A 794  ? 0.3492 0.3306 0.3770 0.0328  -0.0468 -0.0912 792  ALA A CA  
5839  C C   . ALA A 794  ? 0.3319 0.3199 0.3566 0.0372  -0.0483 -0.0985 792  ALA A C   
5840  O O   . ALA A 794  ? 0.3801 0.3712 0.4057 0.0380  -0.0506 -0.1024 792  ALA A O   
5841  C CB  . ALA A 794  ? 0.3559 0.3307 0.3935 0.0311  -0.0496 -0.0925 792  ALA A CB  
5842  N N   . GLN A 795  ? 0.3503 0.3411 0.3715 0.0402  -0.0469 -0.1004 793  GLN A N   
5843  C CA  . GLN A 795  ? 0.3676 0.3659 0.3853 0.0445  -0.0480 -0.1071 793  GLN A CA  
5844  C C   . GLN A 795  ? 0.3409 0.3460 0.3503 0.0456  -0.0461 -0.1055 793  GLN A C   
5845  O O   . GLN A 795  ? 0.3600 0.3705 0.3686 0.0478  -0.0483 -0.1107 793  GLN A O   
5846  C CB  . GLN A 795  ? 0.4214 0.4218 0.4367 0.0474  -0.0465 -0.1088 793  GLN A CB  
5847  N N   . LEU A 796  ? 0.3084 0.3135 0.3120 0.0441  -0.0423 -0.0982 794  LEU A N   
5848  C CA  . LEU A 796  ? 0.3464 0.3578 0.3424 0.0452  -0.0406 -0.0961 794  LEU A CA  
5849  C C   . LEU A 796  ? 0.3289 0.3399 0.3270 0.0435  -0.0426 -0.0963 794  LEU A C   
5850  O O   . LEU A 796  ? 0.3976 0.4150 0.3911 0.0452  -0.0427 -0.0974 794  LEU A O   
5851  C CB  . LEU A 796  ? 0.2783 0.2892 0.2686 0.0439  -0.0363 -0.0883 794  LEU A CB  
5852  C CG  . LEU A 796  ? 0.3114 0.3250 0.2974 0.0460  -0.0337 -0.0875 794  LEU A CG  
5853  C CD1 . LEU A 796  ? 0.2969 0.3095 0.2778 0.0444  -0.0298 -0.0796 794  LEU A CD1 
5854  C CD2 . LEU A 796  ? 0.3235 0.3463 0.3049 0.0504  -0.0343 -0.0927 794  LEU A CD2 
5855  N N   . ALA A 797  ? 0.3457 0.3500 0.3510 0.0401  -0.0442 -0.0951 795  ALA A N   
5856  C CA  . ALA A 797  ? 0.3668 0.3708 0.3746 0.0383  -0.0460 -0.0950 795  ALA A CA  
5857  C C   . ALA A 797  ? 0.3671 0.3755 0.3772 0.0407  -0.0499 -0.1028 795  ALA A C   
5858  O O   . ALA A 797  ? 0.4920 0.5027 0.5020 0.0402  -0.0512 -0.1034 795  ALA A O   
5859  C CB  . ALA A 797  ? 0.4193 0.4156 0.4348 0.0340  -0.0470 -0.0918 795  ALA A CB  
5860  N N   . ASP A 798  ? 0.3858 0.3957 0.3980 0.0435  -0.0517 -0.1090 796  ASP A N   
5861  C CA  . ASP A 798  ? 0.4549 0.4699 0.4687 0.0464  -0.0553 -0.1172 796  ASP A CA  
5862  C C   . ASP A 798  ? 0.5149 0.5394 0.5197 0.0496  -0.0540 -0.1181 796  ASP A C   
5863  O O   . ASP A 798  ? 0.4304 0.4599 0.4357 0.0516  -0.0569 -0.1239 796  ASP A O   
5864  C CB  . ASP A 798  ? 0.3592 0.3737 0.3776 0.0488  -0.0575 -0.1238 796  ASP A CB  
5865  C CG  . ASP A 798  ? 0.6273 0.6332 0.6566 0.0460  -0.0605 -0.1249 796  ASP A CG  
5866  O OD1 . ASP A 798  ? 0.6903 0.6925 0.7245 0.0429  -0.0622 -0.1233 796  ASP A OD1 
5867  O OD2 . ASP A 798  ? 0.5922 0.5951 0.6254 0.0469  -0.0612 -0.1272 796  ASP A OD2 
5868  N N   . ARG A 799  ? 0.4051 0.4322 0.4021 0.0501  -0.0499 -0.1124 797  ARG A N   
5869  C CA  . ARG A 799  ? 0.4457 0.4823 0.4342 0.0536  -0.0485 -0.1132 797  ARG A CA  
5870  C C   . ARG A 799  ? 0.3846 0.4233 0.3674 0.0523  -0.0460 -0.1066 797  ARG A C   
5871  O O   . ARG A 799  ? 0.3394 0.3722 0.3231 0.0489  -0.0442 -0.1003 797  ARG A O   
5872  C CB  . ARG A 799  ? 0.4760 0.5156 0.4601 0.0560  -0.0459 -0.1128 797  ARG A CB  
5873  C CG  . ARG A 799  ? 0.4800 0.5192 0.4692 0.0581  -0.0483 -0.1201 797  ARG A CG  
5874  C CD  . ARG A 799  ? 0.4341 0.4814 0.4174 0.0622  -0.0467 -0.1225 797  ARG A CD  
5875  N NE  . ARG A 799  ? 0.5294 0.5746 0.5091 0.0613  -0.0426 -0.1161 797  ARG A NE  
5876  C CZ  . ARG A 799  ? 0.5125 0.5628 0.4845 0.0618  -0.0391 -0.1105 797  ARG A CZ  
5877  N NH1 . ARG A 799  ? 0.4966 0.5546 0.4630 0.0635  -0.0389 -0.1103 797  ARG A NH1 
5878  N NH2 . ARG A 799  ? 0.4114 0.4590 0.3814 0.0607  -0.0358 -0.1049 797  ARG A NH2 
5879  N N   . LEU A 800  ? 0.3669 0.4142 0.3439 0.0551  -0.0462 -0.1084 798  LEU A N   
5880  C CA  . LEU A 800  ? 0.3663 0.4173 0.3371 0.0548  -0.0439 -0.1024 798  LEU A CA  
5881  C C   . LEU A 800  ? 0.3680 0.4282 0.3308 0.0584  -0.0420 -0.1022 798  LEU A C   
5882  O O   . LEU A 800  ? 0.4103 0.4760 0.3725 0.0616  -0.0433 -0.1083 798  LEU A O   
5883  C CB  . LEU A 800  ? 0.3961 0.4491 0.3681 0.0543  -0.0464 -0.1041 798  LEU A CB  
5884  C CG  . LEU A 800  ? 0.4252 0.4703 0.4046 0.0505  -0.0481 -0.1033 798  LEU A CG  
5885  C CD1 . LEU A 800  ? 0.4602 0.5090 0.4409 0.0509  -0.0512 -0.1067 798  LEU A CD1 
5886  C CD2 . LEU A 800  ? 0.3929 0.4324 0.3715 0.0472  -0.0449 -0.0949 798  LEU A CD2 
5887  N N   . SER A 801  ? 0.4018 0.4638 0.3590 0.0579  -0.0388 -0.0951 799  SER A N   
5888  C CA  . SER A 801  ? 0.4158 0.4874 0.3654 0.0610  -0.0369 -0.0936 799  SER A CA  
5889  C C   . SER A 801  ? 0.4818 0.5622 0.4291 0.0638  -0.0395 -0.0984 799  SER A C   
5890  O O   . SER A 801  ? 0.4454 0.5238 0.3967 0.0628  -0.0424 -0.1016 799  SER A O   
5891  C CB  . SER A 801  ? 0.4624 0.5330 0.4077 0.0594  -0.0335 -0.0846 799  SER A CB  
5892  O OG  . SER A 801  ? 0.4823 0.5524 0.4277 0.0580  -0.0343 -0.0821 799  SER A OG  
5893  N N   . PRO A 802  ? 0.4576 0.5483 0.3984 0.0673  -0.0387 -0.0990 800  PRO A N   
5894  C CA  . PRO A 802  ? 0.4864 0.5863 0.4244 0.0699  -0.0410 -0.1028 800  PRO A CA  
5895  C C   . PRO A 802  ? 0.5157 0.6144 0.4532 0.0680  -0.0414 -0.0984 800  PRO A C   
5896  O O   . PRO A 802  ? 0.5414 0.6440 0.4795 0.0691  -0.0443 -0.1026 800  PRO A O   
5897  C CB  . PRO A 802  ? 0.5765 0.6874 0.5069 0.0734  -0.0390 -0.1015 800  PRO A CB  
5898  C CG  . PRO A 802  ? 0.5639 0.6719 0.4952 0.0734  -0.0369 -0.1011 800  PRO A CG  
5899  C CD  . PRO A 802  ? 0.4850 0.5802 0.4212 0.0691  -0.0357 -0.0966 800  PRO A CD  
5900  N N   . ALA A 803  ? 0.4798 0.5733 0.4163 0.0654  -0.0386 -0.0903 801  ALA A N   
5901  C CA  . ALA A 803  ? 0.5624 0.6534 0.4995 0.0633  -0.0388 -0.0861 801  ALA A CA  
5902  C C   . ALA A 803  ? 0.5402 0.6222 0.4847 0.0602  -0.0410 -0.0884 801  ALA A C   
5903  O O   . ALA A 803  ? 0.4939 0.5741 0.4396 0.0586  -0.0416 -0.0859 801  ALA A O   
5904  C CB  . ALA A 803  ? 0.5069 0.5952 0.4411 0.0616  -0.0352 -0.0769 801  ALA A CB  
5905  N N   . GLY A 804  ? 0.5409 0.6175 0.4907 0.0594  -0.0421 -0.0928 802  GLY A N   
5906  C CA  . GLY A 804  ? 0.4387 0.5072 0.3959 0.0564  -0.0442 -0.0948 802  GLY A CA  
5907  C C   . GLY A 804  ? 0.4520 0.5115 0.4120 0.0526  -0.0419 -0.0884 802  GLY A C   
5908  O O   . GLY A 804  ? 0.4343 0.4889 0.3986 0.0499  -0.0430 -0.0875 802  GLY A O   
5909  N N   . ARG A 805  ? 0.4229 0.4801 0.3805 0.0522  -0.0388 -0.0842 803  ARG A N   
5910  C CA  . ARG A 805  ? 0.4471 0.4963 0.4067 0.0488  -0.0364 -0.0782 803  ARG A CA  
5911  C C   . ARG A 805  ? 0.3251 0.3692 0.2876 0.0481  -0.0356 -0.0791 803  ARG A C   
5912  O O   . ARG A 805  ? 0.3411 0.3886 0.3024 0.0506  -0.0361 -0.0832 803  ARG A O   
5913  C CB  . ARG A 805  ? 0.4151 0.4664 0.3691 0.0489  -0.0333 -0.0710 803  ARG A CB  
5914  C CG  . ARG A 805  ? 0.4391 0.4956 0.3905 0.0497  -0.0342 -0.0696 803  ARG A CG  
5915  C CD  . ARG A 805  ? 0.4628 0.5147 0.4195 0.0471  -0.0361 -0.0704 803  ARG A CD  
5916  N NE  . ARG A 805  ? 0.3860 0.4428 0.3405 0.0479  -0.0371 -0.0692 803  ARG A NE  
5917  C CZ  . ARG A 805  ? 0.4567 0.5181 0.4119 0.0493  -0.0401 -0.0741 803  ARG A CZ  
5918  N NH1 . ARG A 805  ? 0.4333 0.4951 0.3919 0.0501  -0.0427 -0.0810 803  ARG A NH1 
5919  N NH2 . ARG A 805  ? 0.5870 0.6529 0.5398 0.0501  -0.0407 -0.0723 803  ARG A NH2 
5920  N N   . PRO A 806  ? 0.3453 0.3813 0.3116 0.0448  -0.0345 -0.0755 804  PRO A N   
5921  C CA  . PRO A 806  ? 0.3261 0.3570 0.2957 0.0440  -0.0339 -0.0763 804  PRO A CA  
5922  C C   . PRO A 806  ? 0.3395 0.3734 0.3040 0.0459  -0.0312 -0.0742 804  PRO A C   
5923  O O   . PRO A 806  ? 0.3551 0.3920 0.3143 0.0464  -0.0287 -0.0693 804  PRO A O   
5924  C CB  . PRO A 806  ? 0.3477 0.3708 0.3212 0.0400  -0.0328 -0.0715 804  PRO A CB  
5925  C CG  . PRO A 806  ? 0.3731 0.3968 0.3479 0.0388  -0.0342 -0.0710 804  PRO A CG  
5926  C CD  . PRO A 806  ? 0.3392 0.3708 0.3078 0.0417  -0.0340 -0.0712 804  PRO A CD  
5927  N N   . ILE A 807  ? 0.3085 0.3415 0.2751 0.0470  -0.0317 -0.0779 805  ILE A N   
5928  C CA  . ILE A 807  ? 0.3302 0.3656 0.2928 0.0487  -0.0292 -0.0763 805  ILE A CA  
5929  C C   . ILE A 807  ? 0.3094 0.3381 0.2728 0.0458  -0.0264 -0.0699 805  ILE A C   
5930  O O   . ILE A 807  ? 0.2986 0.3202 0.2674 0.0433  -0.0271 -0.0700 805  ILE A O   
5931  C CB  . ILE A 807  ? 0.3067 0.3432 0.2719 0.0508  -0.0308 -0.0828 805  ILE A CB  
5932  C CG1 . ILE A 807  ? 0.3430 0.3865 0.3077 0.0539  -0.0338 -0.0898 805  ILE A CG1 
5933  C CG2 . ILE A 807  ? 0.3039 0.3431 0.2652 0.0525  -0.0280 -0.0809 805  ILE A CG2 
5934  C CD1 . ILE A 807  ? 0.3549 0.4084 0.3120 0.0569  -0.0325 -0.0890 805  ILE A CD1 
5935  N N   . PRO A 808  ? 0.2886 0.3194 0.2469 0.0458  -0.0234 -0.0642 806  PRO A N   
5936  C CA  . PRO A 808  ? 0.2996 0.3242 0.2588 0.0431  -0.0209 -0.0584 806  PRO A CA  
5937  C C   . PRO A 808  ? 0.2699 0.2905 0.2318 0.0428  -0.0204 -0.0595 806  PRO A C   
5938  O O   . PRO A 808  ? 0.2875 0.3121 0.2479 0.0453  -0.0203 -0.0625 806  PRO A O   
5939  C CB  . PRO A 808  ? 0.3179 0.3469 0.2711 0.0441  -0.0182 -0.0531 806  PRO A CB  
5940  C CG  . PRO A 808  ? 0.3535 0.3896 0.3035 0.0462  -0.0195 -0.0549 806  PRO A CG  
5941  C CD  . PRO A 808  ? 0.2956 0.3345 0.2477 0.0482  -0.0223 -0.0625 806  PRO A CD  
5942  N N   . LEU A 809  ? 0.2955 0.3088 0.2616 0.0397  -0.0201 -0.0571 807  LEU A N   
5943  C CA  . LEU A 809  ? 0.2767 0.2855 0.2457 0.0390  -0.0195 -0.0570 807  LEU A CA  
5944  C C   . LEU A 809  ? 0.2874 0.2921 0.2557 0.0365  -0.0168 -0.0506 807  LEU A C   
5945  O O   . LEU A 809  ? 0.3075 0.3087 0.2773 0.0340  -0.0167 -0.0477 807  LEU A O   
5946  C CB  . LEU A 809  ? 0.3160 0.3197 0.2921 0.0375  -0.0223 -0.0608 807  LEU A CB  
5947  C CG  . LEU A 809  ? 0.2995 0.2975 0.2795 0.0360  -0.0218 -0.0598 807  LEU A CG  
5948  C CD1 . LEU A 809  ? 0.3157 0.3166 0.2943 0.0389  -0.0214 -0.0628 807  LEU A CD1 
5949  C CD2 . LEU A 809  ? 0.3513 0.3438 0.3387 0.0339  -0.0247 -0.0622 807  LEU A CD2 
5950  N N   . ILE A 810  ? 0.2568 0.2624 0.2226 0.0373  -0.0145 -0.0484 808  ILE A N   
5951  C CA  . ILE A 810  ? 0.2721 0.2732 0.2381 0.0351  -0.0122 -0.0431 808  ILE A CA  
5952  C C   . ILE A 810  ? 0.2964 0.2931 0.2668 0.0343  -0.0128 -0.0448 808  ILE A C   
5953  O O   . ILE A 810  ? 0.2929 0.2919 0.2629 0.0364  -0.0128 -0.0475 808  ILE A O   
5954  C CB  . ILE A 810  ? 0.2483 0.2531 0.2093 0.0362  -0.0094 -0.0391 808  ILE A CB  
5955  C CG1 . ILE A 810  ? 0.2855 0.2954 0.2425 0.0373  -0.0092 -0.0376 808  ILE A CG1 
5956  C CG2 . ILE A 810  ? 0.2779 0.2779 0.2397 0.0337  -0.0073 -0.0339 808  ILE A CG2 
5957  C CD1 . ILE A 810  ? 0.3515 0.3650 0.3042 0.0382  -0.0065 -0.0329 808  ILE A CD1 
5958  N N   . ALA A 811  ? 0.2703 0.2610 0.2450 0.0314  -0.0133 -0.0432 809  ALA A N   
5959  C CA  . ALA A 811  ? 0.2702 0.2563 0.2498 0.0305  -0.0143 -0.0446 809  ALA A CA  
5960  C C   . ALA A 811  ? 0.2957 0.2775 0.2761 0.0278  -0.0124 -0.0394 809  ALA A C   
5961  O O   . ALA A 811  ? 0.3075 0.2866 0.2894 0.0253  -0.0125 -0.0368 809  ALA A O   
5962  C CB  . ALA A 811  ? 0.3180 0.3015 0.3033 0.0294  -0.0175 -0.0482 809  ALA A CB  
5963  N N   . GLU A 812  ? 0.2746 0.2561 0.2538 0.0284  -0.0107 -0.0380 810  GLU A N   
5964  C CA  . GLU A 812  ? 0.2601 0.2380 0.2398 0.0262  -0.0089 -0.0333 810  GLU A CA  
5965  C C   . GLU A 812  ? 0.2992 0.2730 0.2838 0.0254  -0.0100 -0.0344 810  GLU A C   
5966  O O   . GLU A 812  ? 0.3030 0.2779 0.2881 0.0274  -0.0103 -0.0372 810  GLU A O   
5967  C CB  . GLU A 812  ? 0.3277 0.3085 0.3026 0.0273  -0.0061 -0.0303 810  GLU A CB  
5968  C CG  . GLU A 812  ? 0.3275 0.3124 0.2981 0.0281  -0.0054 -0.0290 810  GLU A CG  
5969  C CD  . GLU A 812  ? 0.4425 0.4251 0.4138 0.0258  -0.0054 -0.0263 810  GLU A CD  
5970  O OE1 . GLU A 812  ? 0.4211 0.4016 0.3920 0.0242  -0.0038 -0.0223 810  GLU A OE1 
5971  O OE2 . GLU A 812  ? 0.3401 0.3232 0.3125 0.0255  -0.0072 -0.0282 810  GLU A OE2 
5972  N N   . THR A 813  ? 0.2919 0.2613 0.2804 0.0226  -0.0107 -0.0324 811  THR A N   
5973  C CA  . THR A 813  ? 0.2635 0.2290 0.2578 0.0216  -0.0126 -0.0337 811  THR A CA  
5974  C C   . THR A 813  ? 0.3129 0.2750 0.3085 0.0191  -0.0112 -0.0291 811  THR A C   
5975  O O   . THR A 813  ? 0.3239 0.2870 0.3157 0.0189  -0.0087 -0.0258 811  THR A O   
5976  C CB  . THR A 813  ? 0.2918 0.2559 0.2906 0.0206  -0.0155 -0.0363 811  THR A CB  
5977  O OG1 . THR A 813  ? 0.3086 0.2730 0.3063 0.0187  -0.0150 -0.0337 811  THR A OG1 
5978  C CG2 . THR A 813  ? 0.2869 0.2547 0.2849 0.0236  -0.0171 -0.0418 811  THR A CG2 
5979  N N   . GLY A 814  ? 0.3299 0.2882 0.3312 0.0173  -0.0129 -0.0287 812  GLY A N   
5980  C CA  . GLY A 814  ? 0.3823 0.3379 0.3851 0.0155  -0.0119 -0.0250 812  GLY A CA  
5981  C C   . GLY A 814  ? 0.3704 0.3257 0.3718 0.0129  -0.0104 -0.0204 812  GLY A C   
5982  O O   . GLY A 814  ? 0.3445 0.3016 0.3437 0.0124  -0.0100 -0.0199 812  GLY A O   
5983  N N   . GLY A 815  ? 0.3135 0.2667 0.3163 0.0113  -0.0096 -0.0171 813  GLY A N   
5984  C CA  . GLY A 815  ? 0.2954 0.2485 0.2975 0.0088  -0.0084 -0.0130 813  GLY A CA  
5985  C C   . GLY A 815  ? 0.2895 0.2400 0.2963 0.0066  -0.0092 -0.0103 813  GLY A C   
5986  O O   . GLY A 815  ? 0.3947 0.3431 0.4048 0.0071  -0.0103 -0.0113 813  GLY A O   
5987  N N   . GLN A 816  ? 0.2870 0.2379 0.2943 0.0041  -0.0087 -0.0071 814  GLN A N   
5988  C CA  . GLN A 816  ? 0.2544 0.2039 0.2653 0.0018  -0.0090 -0.0036 814  GLN A CA  
5989  C C   . GLN A 816  ? 0.2311 0.1827 0.2381 0.0009  -0.0066 -0.0004 814  GLN A C   
5990  O O   . GLN A 816  ? 0.2678 0.2210 0.2752 -0.0011 -0.0063 0.0019  814  GLN A O   
5991  C CB  . GLN A 816  ? 0.2856 0.2345 0.3016 -0.0005 -0.0111 -0.0026 814  GLN A CB  
5992  C CG  . GLN A 816  ? 0.3106 0.2580 0.3313 -0.0028 -0.0119 0.0010  814  GLN A CG  
5993  C CD  . GLN A 816  ? 0.3953 0.3394 0.4197 -0.0017 -0.0135 -0.0005 814  GLN A CD  
5994  O OE1 . GLN A 816  ? 0.3585 0.3022 0.3806 -0.0002 -0.0123 -0.0007 814  GLN A OE1 
5995  N NE2 . GLN A 816  ? 0.3645 0.3064 0.3952 -0.0024 -0.0163 -0.0015 814  GLN A NE2 
5996  N N   . ASN A 817  ? 0.2422 0.1940 0.2457 0.0025  -0.0050 -0.0006 815  ASN A N   
5997  C CA  . ASN A 817  ? 0.2198 0.1737 0.2190 0.0024  -0.0027 0.0011  815  ASN A CA  
5998  C C   . ASN A 817  ? 0.2172 0.1714 0.2174 0.0004  -0.0021 0.0046  815  ASN A C   
5999  O O   . ASN A 817  ? 0.2549 0.2075 0.2574 0.0001  -0.0025 0.0057  815  ASN A O   
6000  C CB  . ASN A 817  ? 0.2482 0.2024 0.2438 0.0048  -0.0014 -0.0002 815  ASN A CB  
6001  C CG  . ASN A 817  ? 0.2441 0.1986 0.2389 0.0070  -0.0021 -0.0038 815  ASN A CG  
6002  O OD1 . ASN A 817  ? 0.2357 0.1915 0.2295 0.0071  -0.0025 -0.0050 815  ASN A OD1 
6003  N ND2 . ASN A 817  ? 0.2354 0.1891 0.2306 0.0087  -0.0024 -0.0056 815  ASN A ND2 
6004  N N   . ALA A 818  ? 0.2174 0.1740 0.2160 -0.0007 -0.0011 0.0063  816  ALA A N   
6005  C CA  . ALA A 818  ? 0.2331 0.1910 0.2323 -0.0026 -0.0005 0.0094  816  ALA A CA  
6006  C C   . ALA A 818  ? 0.2178 0.1773 0.2133 -0.0020 0.0015  0.0099  816  ALA A C   
6007  O O   . ALA A 818  ? 0.2322 0.1922 0.2247 -0.0005 0.0023  0.0084  816  ALA A O   
6008  C CB  . ALA A 818  ? 0.2652 0.2255 0.2662 -0.0047 -0.0010 0.0108  816  ALA A CB  
6009  N N   . MET A 819  ? 0.2506 0.2110 0.2465 -0.0031 0.0020  0.0122  817  MET A N   
6010  C CA  . MET A 819  ? 0.2210 0.1833 0.2142 -0.0029 0.0035  0.0129  817  MET A CA  
6011  C C   . MET A 819  ? 0.2168 0.1823 0.2111 -0.0050 0.0036  0.0153  817  MET A C   
6012  O O   . MET A 819  ? 0.2404 0.2059 0.2374 -0.0064 0.0027  0.0173  817  MET A O   
6013  C CB  . MET A 819  ? 0.2486 0.2095 0.2409 -0.0019 0.0043  0.0131  817  MET A CB  
6014  C CG  . MET A 819  ? 0.2589 0.2218 0.2492 -0.0019 0.0056  0.0138  817  MET A CG  
6015  S SD  . MET A 819  ? 0.2685 0.2299 0.2585 -0.0010 0.0063  0.0144  817  MET A SD  
6016  C CE  . MET A 819  ? 0.2663 0.2256 0.2546 0.0014  0.0068  0.0121  817  MET A CE  
6017  N N   . ILE A 820  ? 0.2187 0.1871 0.2111 -0.0051 0.0044  0.0150  818  ILE A N   
6018  C CA  . ILE A 820  ? 0.2255 0.1981 0.2185 -0.0068 0.0047  0.0168  818  ILE A CA  
6019  C C   . ILE A 820  ? 0.1978 0.1718 0.1889 -0.0063 0.0058  0.0169  818  ILE A C   
6020  O O   . ILE A 820  ? 0.2195 0.1927 0.2087 -0.0048 0.0065  0.0151  818  ILE A O   
6021  C CB  . ILE A 820  ? 0.2355 0.2111 0.2282 -0.0072 0.0047  0.0161  818  ILE A CB  
6022  C CG1 . ILE A 820  ? 0.2447 0.2190 0.2398 -0.0079 0.0034  0.0161  818  ILE A CG1 
6023  C CG2 . ILE A 820  ? 0.2537 0.2347 0.2467 -0.0087 0.0052  0.0177  818  ILE A CG2 
6024  C CD1 . ILE A 820  ? 0.2484 0.2257 0.2435 -0.0084 0.0034  0.0153  818  ILE A CD1 
6025  N N   . VAL A 821  ? 0.2112 0.1874 0.2032 -0.0076 0.0057  0.0191  819  VAL A N   
6026  C CA  . VAL A 821  ? 0.2281 0.2060 0.2188 -0.0072 0.0065  0.0192  819  VAL A CA  
6027  C C   . VAL A 821  ? 0.2397 0.2234 0.2306 -0.0086 0.0067  0.0204  819  VAL A C   
6028  O O   . VAL A 821  ? 0.2581 0.2439 0.2508 -0.0103 0.0060  0.0230  819  VAL A O   
6029  C CB  . VAL A 821  ? 0.2142 0.1897 0.2059 -0.0072 0.0062  0.0206  819  VAL A CB  
6030  C CG1 . VAL A 821  ? 0.2394 0.2171 0.2300 -0.0071 0.0069  0.0208  819  VAL A CG1 
6031  C CG2 . VAL A 821  ? 0.2325 0.2030 0.2240 -0.0057 0.0061  0.0191  819  VAL A CG2 
6032  N N   . ASP A 822  ? 0.2204 0.2070 0.2096 -0.0079 0.0074  0.0187  820  ASP A N   
6033  C CA  . ASP A 822  ? 0.2489 0.2418 0.2380 -0.0090 0.0076  0.0195  820  ASP A CA  
6034  C C   . ASP A 822  ? 0.2234 0.2182 0.2119 -0.0088 0.0079  0.0197  820  ASP A C   
6035  O O   . ASP A 822  ? 0.2478 0.2388 0.2361 -0.0080 0.0079  0.0195  820  ASP A O   
6036  C CB  . ASP A 822  ? 0.2744 0.2704 0.2627 -0.0084 0.0080  0.0172  820  ASP A CB  
6037  C CG  . ASP A 822  ? 0.2515 0.2466 0.2385 -0.0066 0.0085  0.0142  820  ASP A CG  
6038  O OD1 . ASP A 822  ? 0.2628 0.2558 0.2494 -0.0059 0.0087  0.0138  820  ASP A OD1 
6039  O OD2 . ASP A 822  ? 0.2654 0.2619 0.2521 -0.0059 0.0087  0.0121  820  ASP A OD2 
6040  N N   . SER A 823  ? 0.2588 0.2601 0.2470 -0.0096 0.0081  0.0202  821  SER A N   
6041  C CA  . SER A 823  ? 0.2686 0.2727 0.2562 -0.0096 0.0081  0.0205  821  SER A CA  
6042  C C   . SER A 823  ? 0.2805 0.2837 0.2671 -0.0079 0.0085  0.0172  821  SER A C   
6043  O O   . SER A 823  ? 0.3237 0.3291 0.3101 -0.0078 0.0085  0.0170  821  SER A O   
6044  C CB  . SER A 823  ? 0.2704 0.2828 0.2580 -0.0109 0.0082  0.0220  821  SER A CB  
6045  O OG  . SER A 823  ? 0.3192 0.3356 0.3061 -0.0104 0.0086  0.0196  821  SER A OG  
6046  N N   . SER A 824  ? 0.2509 0.2512 0.2373 -0.0066 0.0087  0.0146  822  SER A N   
6047  C CA  . SER A 824  ? 0.2265 0.2252 0.2127 -0.0051 0.0089  0.0118  822  SER A CA  
6048  C C   . SER A 824  ? 0.2690 0.2613 0.2554 -0.0044 0.0089  0.0121  822  SER A C   
6049  O O   . SER A 824  ? 0.2789 0.2699 0.2657 -0.0034 0.0090  0.0104  822  SER A O   
6050  C CB  . SER A 824  ? 0.2670 0.2663 0.2532 -0.0041 0.0090  0.0090  822  SER A CB  
6051  O OG  . SER A 824  ? 0.2592 0.2535 0.2454 -0.0036 0.0090  0.0092  822  SER A OG  
6052  N N   . ALA A 825  ? 0.2518 0.2405 0.2384 -0.0049 0.0089  0.0141  823  ALA A N   
6053  C CA  . ALA A 825  ? 0.2732 0.2565 0.2599 -0.0040 0.0090  0.0143  823  ALA A CA  
6054  C C   . ALA A 825  ? 0.2725 0.2559 0.2598 -0.0042 0.0089  0.0153  823  ALA A C   
6055  O O   . ALA A 825  ? 0.3159 0.3028 0.3034 -0.0053 0.0086  0.0167  823  ALA A O   
6056  C CB  . ALA A 825  ? 0.2695 0.2496 0.2566 -0.0043 0.0088  0.0157  823  ALA A CB  
6057  N N   . LEU A 826  ? 0.2918 0.2716 0.2794 -0.0032 0.0092  0.0148  824  LEU A N   
6058  C CA  . LEU A 826  ? 0.2875 0.2670 0.2757 -0.0033 0.0091  0.0157  824  LEU A CA  
6059  C C   . LEU A 826  ? 0.3286 0.3055 0.3174 -0.0037 0.0090  0.0178  824  LEU A C   
6060  O O   . LEU A 826  ? 0.3190 0.2922 0.3078 -0.0029 0.0092  0.0177  824  LEU A O   
6061  C CB  . LEU A 826  ? 0.3680 0.3452 0.3568 -0.0022 0.0095  0.0143  824  LEU A CB  
6062  C CG  . LEU A 826  ? 0.4720 0.4494 0.4618 -0.0023 0.0094  0.0149  824  LEU A CG  
6063  C CD1 . LEU A 826  ? 0.4678 0.4502 0.4577 -0.0030 0.0088  0.0145  824  LEU A CD1 
6064  C CD2 . LEU A 826  ? 0.4693 0.4445 0.4603 -0.0013 0.0097  0.0137  824  LEU A CD2 
6065  N N   . ALA A 827  ? 0.3130 0.2920 0.3024 -0.0047 0.0084  0.0198  825  ALA A N   
6066  C CA  . ALA A 827  ? 0.2924 0.2692 0.2829 -0.0052 0.0080  0.0219  825  ALA A CA  
6067  C C   . ALA A 827  ? 0.2905 0.2630 0.2816 -0.0040 0.0082  0.0215  825  ALA A C   
6068  O O   . ALA A 827  ? 0.2759 0.2454 0.2676 -0.0036 0.0080  0.0217  825  ALA A O   
6069  C CB  . ALA A 827  ? 0.3122 0.2923 0.3037 -0.0064 0.0073  0.0243  825  ALA A CB  
6070  N N   . GLU A 828  ? 0.2807 0.2533 0.2718 -0.0034 0.0087  0.0209  826  GLU A N   
6071  C CA  . GLU A 828  ? 0.2930 0.2623 0.2847 -0.0023 0.0090  0.0207  826  GLU A CA  
6072  C C   . GLU A 828  ? 0.2809 0.2475 0.2718 -0.0011 0.0096  0.0194  826  GLU A C   
6073  O O   . GLU A 828  ? 0.3084 0.2726 0.2998 -0.0003 0.0097  0.0195  826  GLU A O   
6074  C CB  . GLU A 828  ? 0.3836 0.3538 0.3758 -0.0020 0.0094  0.0203  826  GLU A CB  
6075  C CG  . GLU A 828  ? 0.4129 0.3853 0.4062 -0.0027 0.0088  0.0217  826  GLU A CG  
6076  C CD  . GLU A 828  ? 0.5005 0.4773 0.4931 -0.0038 0.0083  0.0217  826  GLU A CD  
6077  O OE1 . GLU A 828  ? 0.4263 0.4045 0.4179 -0.0039 0.0084  0.0206  826  GLU A OE1 
6078  O OE2 . GLU A 828  ? 0.5965 0.5759 0.5897 -0.0044 0.0077  0.0228  826  GLU A OE2 
6079  N N   . GLN A 829  ? 0.3038 0.2711 0.2937 -0.0009 0.0100  0.0181  827  GLN A N   
6080  C CA  . GLN A 829  ? 0.3022 0.2676 0.2912 0.0001  0.0104  0.0171  827  GLN A CA  
6081  C C   . GLN A 829  ? 0.2698 0.2341 0.2586 0.0000  0.0099  0.0172  827  GLN A C   
6082  O O   . GLN A 829  ? 0.2710 0.2332 0.2595 0.0010  0.0101  0.0167  827  GLN A O   
6083  C CB  . GLN A 829  ? 0.3871 0.3536 0.3753 0.0002  0.0106  0.0158  827  GLN A CB  
6084  C CG  . GLN A 829  ? 0.4862 0.4529 0.4752 0.0007  0.0110  0.0152  827  GLN A CG  
6085  C CD  . GLN A 829  ? 0.5916 0.5589 0.5803 0.0010  0.0109  0.0138  827  GLN A CD  
6086  O OE1 . GLN A 829  ? 0.4197 0.3882 0.4076 0.0007  0.0106  0.0132  827  GLN A OE1 
6087  N NE2 . GLN A 829  ? 0.5984 0.5651 0.5883 0.0016  0.0111  0.0133  827  GLN A NE2 
6088  N N   . VAL A 830  ? 0.2431 0.2091 0.2321 -0.0013 0.0093  0.0178  828  VAL A N   
6089  C CA  . VAL A 830  ? 0.2390 0.2042 0.2286 -0.0017 0.0085  0.0181  828  VAL A CA  
6090  C C   . VAL A 830  ? 0.2910 0.2537 0.2821 -0.0013 0.0080  0.0188  828  VAL A C   
6091  O O   . VAL A 830  ? 0.2527 0.2133 0.2440 -0.0004 0.0077  0.0178  828  VAL A O   
6092  C CB  . VAL A 830  ? 0.2242 0.1923 0.2143 -0.0033 0.0079  0.0193  828  VAL A CB  
6093  C CG1 . VAL A 830  ? 0.2539 0.2209 0.2456 -0.0040 0.0069  0.0202  828  VAL A CG1 
6094  C CG2 . VAL A 830  ? 0.2629 0.2337 0.2517 -0.0035 0.0083  0.0181  828  VAL A CG2 
6095  N N   . VAL A 831  ? 0.2496 0.2128 0.2419 -0.0017 0.0078  0.0202  829  VAL A N   
6096  C CA  . VAL A 831  ? 0.2308 0.1918 0.2251 -0.0013 0.0071  0.0208  829  VAL A CA  
6097  C C   . VAL A 831  ? 0.2384 0.1971 0.2321 0.0006  0.0077  0.0191  829  VAL A C   
6098  O O   . VAL A 831  ? 0.2390 0.1958 0.2339 0.0014  0.0071  0.0184  829  VAL A O   
6099  C CB  . VAL A 831  ? 0.2212 0.1833 0.2168 -0.0021 0.0068  0.0228  829  VAL A CB  
6100  C CG1 . VAL A 831  ? 0.2743 0.2341 0.2723 -0.0013 0.0061  0.0232  829  VAL A CG1 
6101  C CG2 . VAL A 831  ? 0.2879 0.2527 0.2843 -0.0039 0.0060  0.0248  829  VAL A CG2 
6102  N N   . GLY A 832  ? 0.2366 0.1960 0.2289 0.0013  0.0089  0.0186  830  GLY A N   
6103  C CA  . GLY A 832  ? 0.2427 0.2009 0.2345 0.0030  0.0096  0.0174  830  GLY A CA  
6104  C C   . GLY A 832  ? 0.2567 0.2141 0.2473 0.0039  0.0096  0.0158  830  GLY A C   
6105  O O   . GLY A 832  ? 0.2463 0.2027 0.2372 0.0052  0.0095  0.0147  830  GLY A O   
6106  N N   . ASP A 833  ? 0.2340 0.1922 0.2234 0.0032  0.0095  0.0156  831  ASP A N   
6107  C CA  . ASP A 833  ? 0.2314 0.1891 0.2197 0.0040  0.0094  0.0141  831  ASP A CA  
6108  C C   . ASP A 833  ? 0.2410 0.1974 0.2309 0.0037  0.0081  0.0135  831  ASP A C   
6109  O O   . ASP A 833  ? 0.2600 0.2158 0.2496 0.0049  0.0078  0.0119  831  ASP A O   
6110  C CB  . ASP A 833  ? 0.2347 0.1938 0.2217 0.0033  0.0096  0.0139  831  ASP A CB  
6111  C CG  . ASP A 833  ? 0.2693 0.2291 0.2552 0.0039  0.0107  0.0141  831  ASP A CG  
6112  O OD1 . ASP A 833  ? 0.2770 0.2364 0.2628 0.0049  0.0114  0.0143  831  ASP A OD1 
6113  O OD2 . ASP A 833  ? 0.2611 0.2220 0.2465 0.0033  0.0108  0.0139  831  ASP A OD2 
6114  N N   . VAL A 834  ? 0.2271 0.1835 0.2190 0.0022  0.0072  0.0150  832  VAL A N   
6115  C CA  . VAL A 834  ? 0.2331 0.1881 0.2275 0.0018  0.0056  0.0148  832  VAL A CA  
6116  C C   . VAL A 834  ? 0.2394 0.1925 0.2356 0.0032  0.0051  0.0139  832  VAL A C   
6117  O O   . VAL A 834  ? 0.2370 0.1888 0.2344 0.0041  0.0042  0.0121  832  VAL A O   
6118  C CB  . VAL A 834  ? 0.2304 0.1865 0.2267 -0.0003 0.0048  0.0173  832  VAL A CB  
6119  C CG1 . VAL A 834  ? 0.2479 0.2021 0.2478 -0.0009 0.0031  0.0178  832  VAL A CG1 
6120  C CG2 . VAL A 834  ? 0.2463 0.2047 0.2411 -0.0015 0.0052  0.0176  832  VAL A CG2 
6121  N N   . ILE A 835  ? 0.2186 0.1719 0.2153 0.0034  0.0056  0.0150  833  ILE A N   
6122  C CA  . ILE A 835  ? 0.2262 0.1781 0.2248 0.0049  0.0052  0.0140  833  ILE A CA  
6123  C C   . ILE A 835  ? 0.2486 0.2007 0.2454 0.0070  0.0059  0.0113  833  ILE A C   
6124  O O   . ILE A 835  ? 0.2494 0.2003 0.2478 0.0084  0.0050  0.0093  833  ILE A O   
6125  C CB  . ILE A 835  ? 0.2449 0.1975 0.2440 0.0048  0.0059  0.0156  833  ILE A CB  
6126  C CG1 . ILE A 835  ? 0.2629 0.2156 0.2641 0.0029  0.0049  0.0182  833  ILE A CG1 
6127  C CG2 . ILE A 835  ? 0.2837 0.2354 0.2844 0.0067  0.0057  0.0143  833  ILE A CG2 
6128  C CD1 . ILE A 835  ? 0.2998 0.2504 0.3050 0.0028  0.0030  0.0185  833  ILE A CD1 
6129  N N   . THR A 836  ? 0.2273 0.1810 0.2210 0.0075  0.0074  0.0113  834  THR A N   
6130  C CA  . THR A 836  ? 0.2298 0.1844 0.2216 0.0094  0.0081  0.0092  834  THR A CA  
6131  C C   . THR A 836  ? 0.2381 0.1923 0.2298 0.0097  0.0071  0.0073  834  THR A C   
6132  O O   . THR A 836  ? 0.2712 0.2254 0.2634 0.0114  0.0065  0.0049  834  THR A O   
6133  C CB  . THR A 836  ? 0.2938 0.2503 0.2829 0.0095  0.0098  0.0102  834  THR A CB  
6134  O OG1 . THR A 836  ? 0.3226 0.2796 0.3123 0.0094  0.0106  0.0117  834  THR A OG1 
6135  C CG2 . THR A 836  ? 0.2910 0.2491 0.2780 0.0114  0.0105  0.0087  834  THR A CG2 
6136  N N   . SER A 837  ? 0.2364 0.1904 0.2276 0.0082  0.0067  0.0080  835  SER A N   
6137  C CA  . SER A 837  ? 0.2302 0.1840 0.2212 0.0085  0.0057  0.0062  835  SER A CA  
6138  C C   . SER A 837  ? 0.2480 0.1999 0.2425 0.0085  0.0038  0.0048  835  SER A C   
6139  O O   . SER A 837  ? 0.2440 0.1958 0.2387 0.0097  0.0030  0.0023  835  SER A O   
6140  C CB  . SER A 837  ? 0.2244 0.1788 0.2147 0.0067  0.0057  0.0075  835  SER A CB  
6141  O OG  . SER A 837  ? 0.2545 0.2104 0.2420 0.0068  0.0072  0.0083  835  SER A OG  
6142  N N   . ALA A 838  ? 0.2380 0.1885 0.2355 0.0073  0.0030  0.0065  836  ALA A N   
6143  C CA  . ALA A 838  ? 0.2445 0.1928 0.2462 0.0071  0.0008  0.0055  836  ALA A CA  
6144  C C   . ALA A 838  ? 0.2442 0.1917 0.2478 0.0092  0.0003  0.0032  836  ALA A C   
6145  O O   . ALA A 838  ? 0.2580 0.2041 0.2643 0.0101  -0.0015 0.0008  836  ALA A O   
6146  C CB  . ALA A 838  ? 0.2353 0.1827 0.2401 0.0047  -0.0001 0.0087  836  ALA A CB  
6147  N N   . PHE A 839  ? 0.2521 0.2004 0.2545 0.0101  0.0016  0.0039  837  PHE A N   
6148  C CA  . PHE A 839  ? 0.2393 0.1869 0.2442 0.0119  0.0009  0.0021  837  PHE A CA  
6149  C C   . PHE A 839  ? 0.2491 0.1993 0.2512 0.0144  0.0024  0.0000  837  PHE A C   
6150  O O   . PHE A 839  ? 0.2540 0.2044 0.2581 0.0163  0.0019  -0.0022 837  PHE A O   
6151  C CB  . PHE A 839  ? 0.2215 0.1681 0.2289 0.0109  0.0007  0.0048  837  PHE A CB  
6152  C CG  . PHE A 839  ? 0.2211 0.1659 0.2314 0.0084  -0.0007 0.0075  837  PHE A CG  
6153  C CD1 . PHE A 839  ? 0.2543 0.1970 0.2686 0.0080  -0.0030 0.0065  837  PHE A CD1 
6154  C CD2 . PHE A 839  ? 0.2441 0.1899 0.2533 0.0064  0.0001  0.0110  837  PHE A CD2 
6155  C CE1 . PHE A 839  ? 0.2607 0.2023 0.2778 0.0055  -0.0043 0.0094  837  PHE A CE1 
6156  C CE2 . PHE A 839  ? 0.2643 0.2094 0.2760 0.0041  -0.0012 0.0136  837  PHE A CE2 
6157  C CZ  . PHE A 839  ? 0.2539 0.1970 0.2695 0.0036  -0.0033 0.0131  837  PHE A CZ  
6158  N N   . ASP A 840  ? 0.2369 0.1894 0.2347 0.0145  0.0043  0.0007  838  ASP A N   
6159  C CA  . ASP A 840  ? 0.2365 0.1921 0.2317 0.0168  0.0057  -0.0010 838  ASP A CA  
6160  C C   . ASP A 840  ? 0.2396 0.1957 0.2357 0.0188  0.0044  -0.0050 838  ASP A C   
6161  O O   . ASP A 840  ? 0.2625 0.2172 0.2595 0.0182  0.0029  -0.0062 838  ASP A O   
6162  C CB  . ASP A 840  ? 0.2766 0.2343 0.2678 0.0163  0.0074  0.0005  838  ASP A CB  
6163  C CG  . ASP A 840  ? 0.3085 0.2698 0.2970 0.0185  0.0088  -0.0005 838  ASP A CG  
6164  O OD1 . ASP A 840  ? 0.3228 0.2857 0.3104 0.0202  0.0083  -0.0033 838  ASP A OD1 
6165  O OD2 . ASP A 840  ? 0.3752 0.3381 0.3626 0.0185  0.0104  0.0015  838  ASP A OD2 
6166  N N   . SER A 841  ? 0.2644 0.2229 0.2604 0.0213  0.0048  -0.0072 839  SER A N   
6167  C CA  . SER A 841  ? 0.2450 0.2048 0.2419 0.0236  0.0035  -0.0117 839  SER A CA  
6168  C C   . SER A 841  ? 0.2613 0.2171 0.2632 0.0231  0.0007  -0.0134 839  SER A C   
6169  O O   . SER A 841  ? 0.2777 0.2335 0.2808 0.0241  -0.0009 -0.0168 839  SER A O   
6170  C CB  . SER A 841  ? 0.2847 0.2472 0.2779 0.0243  0.0040  -0.0128 839  SER A CB  
6171  O OG  . SER A 841  ? 0.3208 0.2869 0.3099 0.0247  0.0065  -0.0107 839  SER A OG  
6172  N N   . ALA A 842  ? 0.2596 0.2123 0.2648 0.0214  0.0000  -0.0110 840  ALA A N   
6173  C CA  . ALA A 842  ? 0.2129 0.1617 0.2236 0.0204  -0.0027 -0.0116 840  ALA A CA  
6174  C C   . ALA A 842  ? 0.2504 0.1977 0.2613 0.0188  -0.0039 -0.0116 840  ALA A C   
6175  O O   . ALA A 842  ? 0.2708 0.2159 0.2858 0.0189  -0.0063 -0.0139 840  ALA A O   
6176  C CB  . ALA A 842  ? 0.2780 0.2266 0.2926 0.0230  -0.0045 -0.0160 840  ALA A CB  
6177  N N   . GLY A 843  ? 0.2560 0.2046 0.2629 0.0173  -0.0023 -0.0091 841  GLY A N   
6178  C CA  . GLY A 843  ? 0.2437 0.1914 0.2504 0.0158  -0.0032 -0.0089 841  GLY A CA  
6179  C C   . GLY A 843  ? 0.2630 0.2122 0.2690 0.0177  -0.0041 -0.0131 841  GLY A C   
6180  O O   . GLY A 843  ? 0.2760 0.2241 0.2831 0.0166  -0.0054 -0.0136 841  GLY A O   
6181  N N   . GLN A 844  ? 0.2542 0.2062 0.2585 0.0205  -0.0035 -0.0161 842  GLN A N   
6182  C CA  . GLN A 844  ? 0.2534 0.2075 0.2567 0.0226  -0.0043 -0.0204 842  GLN A CA  
6183  C C   . GLN A 844  ? 0.3325 0.2904 0.3299 0.0231  -0.0023 -0.0197 842  GLN A C   
6184  O O   . GLN A 844  ? 0.3519 0.3139 0.3465 0.0255  -0.0015 -0.0221 842  GLN A O   
6185  C CB  . GLN A 844  ? 0.2580 0.2137 0.2630 0.0256  -0.0051 -0.0245 842  GLN A CB  
6186  C CG  . GLN A 844  ? 0.2601 0.2117 0.2718 0.0253  -0.0076 -0.0257 842  GLN A CG  
6187  C CD  . GLN A 844  ? 0.3223 0.2758 0.3359 0.0284  -0.0081 -0.0297 842  GLN A CD  
6188  O OE1 . GLN A 844  ? 0.2689 0.2207 0.2874 0.0297  -0.0107 -0.0336 842  GLN A OE1 
6189  N NE2 . GLN A 844  ? 0.4329 0.3900 0.4428 0.0298  -0.0056 -0.0288 842  GLN A NE2 
6190  N N   . ARG A 845  ? 0.2668 0.2237 0.2625 0.0207  -0.0014 -0.0162 843  ARG A N   
6191  C CA  . ARG A 845  ? 0.2538 0.2135 0.2450 0.0208  -0.0001 -0.0154 843  ARG A CA  
6192  C C   . ARG A 845  ? 0.2655 0.2235 0.2581 0.0192  -0.0017 -0.0157 843  ARG A C   
6193  O O   . ARG A 845  ? 0.2744 0.2291 0.2704 0.0170  -0.0028 -0.0141 843  ARG A O   
6194  C CB  . ARG A 845  ? 0.2681 0.2282 0.2564 0.0194  0.0022  -0.0112 843  ARG A CB  
6195  C CG  . ARG A 845  ? 0.2654 0.2275 0.2524 0.0208  0.0039  -0.0104 843  ARG A CG  
6196  C CD  . ARG A 845  ? 0.3053 0.2677 0.2900 0.0193  0.0058  -0.0064 843  ARG A CD  
6197  N NE  . ARG A 845  ? 0.3709 0.3352 0.3547 0.0203  0.0075  -0.0052 843  ARG A NE  
6198  C CZ  . ARG A 845  ? 0.3249 0.2928 0.3056 0.0214  0.0091  -0.0043 843  ARG A CZ  
6199  N NH1 . ARG A 845  ? 0.3309 0.3009 0.3089 0.0219  0.0094  -0.0045 843  ARG A NH1 
6200  N NH2 . ARG A 845  ? 0.3452 0.3147 0.3257 0.0220  0.0105  -0.0029 843  ARG A NH2 
6201  N N   . CYS A 846  ? 0.2736 0.2341 0.2636 0.0202  -0.0018 -0.0174 844  CYS A N   
6202  C CA  . CYS A 846  ? 0.2888 0.2480 0.2800 0.0185  -0.0031 -0.0174 844  CYS A CA  
6203  C C   . CYS A 846  ? 0.2278 0.1858 0.2182 0.0159  -0.0019 -0.0131 844  CYS A C   
6204  O O   . CYS A 846  ? 0.2543 0.2104 0.2471 0.0139  -0.0030 -0.0122 844  CYS A O   
6205  C CB  . CYS A 846  ? 0.3030 0.2655 0.2910 0.0201  -0.0032 -0.0197 844  CYS A CB  
6206  S SG  . CYS A 846  ? 0.4284 0.3952 0.4105 0.0216  -0.0003 -0.0176 844  CYS A SG  
6207  N N   . SER A 847  ? 0.2667 0.2258 0.2539 0.0160  0.0003  -0.0106 845  SER A N   
6208  C CA  . SER A 847  ? 0.2526 0.2112 0.2388 0.0140  0.0015  -0.0070 845  SER A CA  
6209  C C   . SER A 847  ? 0.2581 0.2143 0.2472 0.0121  0.0015  -0.0047 845  SER A C   
6210  O O   . SER A 847  ? 0.2491 0.2051 0.2374 0.0105  0.0024  -0.0019 845  SER A O   
6211  C CB  . SER A 847  ? 0.2667 0.2277 0.2491 0.0150  0.0037  -0.0054 845  SER A CB  
6212  O OG  . SER A 847  ? 0.3049 0.2665 0.2872 0.0164  0.0044  -0.0058 845  SER A OG  
6213  N N   . ALA A 848  ? 0.2506 0.2051 0.2427 0.0126  0.0004  -0.0058 846  ALA A N   
6214  C CA  . ALA A 848  ? 0.2307 0.1833 0.2252 0.0111  0.0004  -0.0034 846  ALA A CA  
6215  C C   . ALA A 848  ? 0.2426 0.1939 0.2391 0.0084  -0.0002 -0.0009 846  ALA A C   
6216  O O   . ALA A 848  ? 0.2428 0.1938 0.2408 0.0076  -0.0016 -0.0017 846  ALA A O   
6217  C CB  . ALA A 848  ? 0.2194 0.1702 0.2176 0.0121  -0.0010 -0.0053 846  ALA A CB  
6218  N N   . LEU A 849  ? 0.2180 0.1692 0.2146 0.0070  0.0006  0.0021  847  LEU A N   
6219  C CA  . LEU A 849  ? 0.2185 0.1695 0.2170 0.0044  0.0001  0.0047  847  LEU A CA  
6220  C C   . LEU A 849  ? 0.2500 0.1987 0.2536 0.0034  -0.0020 0.0049  847  LEU A C   
6221  O O   . LEU A 849  ? 0.2448 0.1920 0.2506 0.0039  -0.0026 0.0050  847  LEU A O   
6222  C CB  . LEU A 849  ? 0.1927 0.1445 0.1898 0.0035  0.0016  0.0074  847  LEU A CB  
6223  C CG  . LEU A 849  ? 0.2300 0.1826 0.2289 0.0010  0.0012  0.0103  847  LEU A CG  
6224  C CD1 . LEU A 849  ? 0.2389 0.1931 0.2366 0.0000  0.0012  0.0102  847  LEU A CD1 
6225  C CD2 . LEU A 849  ? 0.2262 0.1801 0.2236 0.0004  0.0025  0.0125  847  LEU A CD2 
6226  N N   . ARG A 850  ? 0.2287 0.1773 0.2344 0.0021  -0.0034 0.0050  848  ARG A N   
6227  C CA  . ARG A 850  ? 0.2485 0.1949 0.2598 0.0008  -0.0056 0.0055  848  ARG A CA  
6228  C C   . ARG A 850  ? 0.2306 0.1779 0.2441 -0.0020 -0.0059 0.0096  848  ARG A C   
6229  O O   . ARG A 850  ? 0.2482 0.1939 0.2663 -0.0031 -0.0074 0.0114  848  ARG A O   
6230  C CB  . ARG A 850  ? 0.2521 0.1979 0.2655 0.0012  -0.0074 0.0027  848  ARG A CB  
6231  C CG  . ARG A 850  ? 0.2689 0.2149 0.2798 0.0041  -0.0072 -0.0015 848  ARG A CG  
6232  C CD  . ARG A 850  ? 0.2589 0.2035 0.2708 0.0060  -0.0074 -0.0030 848  ARG A CD  
6233  N NE  . ARG A 850  ? 0.2810 0.2265 0.2910 0.0088  -0.0074 -0.0073 848  ARG A NE  
6234  C CZ  . ARG A 850  ? 0.2870 0.2323 0.2971 0.0110  -0.0074 -0.0095 848  ARG A CZ  
6235  N NH1 . ARG A 850  ? 0.2663 0.2103 0.2783 0.0108  -0.0073 -0.0078 848  ARG A NH1 
6236  N NH2 . ARG A 850  ? 0.2816 0.2287 0.2899 0.0136  -0.0075 -0.0135 848  ARG A NH2 
6237  N N   . VAL A 851  ? 0.2319 0.1820 0.2423 -0.0031 -0.0045 0.0111  849  VAL A N   
6238  C CA  . VAL A 851  ? 0.2223 0.1745 0.2345 -0.0058 -0.0046 0.0149  849  VAL A CA  
6239  C C   . VAL A 851  ? 0.2289 0.1841 0.2368 -0.0060 -0.0025 0.0163  849  VAL A C   
6240  O O   . VAL A 851  ? 0.2472 0.2041 0.2516 -0.0053 -0.0013 0.0149  849  VAL A O   
6241  C CB  . VAL A 851  ? 0.3004 0.2538 0.3145 -0.0072 -0.0056 0.0150  849  VAL A CB  
6242  C CG1 . VAL A 851  ? 0.3079 0.2640 0.3242 -0.0100 -0.0058 0.0193  849  VAL A CG1 
6243  C CG2 . VAL A 851  ? 0.3678 0.3181 0.3862 -0.0068 -0.0080 0.0128  849  VAL A CG2 
6244  N N   . LEU A 852  ? 0.2203 0.1762 0.2287 -0.0068 -0.0021 0.0189  850  LEU A N   
6245  C CA  . LEU A 852  ? 0.2440 0.2031 0.2490 -0.0072 -0.0003 0.0203  850  LEU A CA  
6246  C C   . LEU A 852  ? 0.2308 0.1936 0.2371 -0.0096 -0.0006 0.0233  850  LEU A C   
6247  O O   . LEU A 852  ? 0.2300 0.1928 0.2402 -0.0112 -0.0019 0.0260  850  LEU A O   
6248  C CB  . LEU A 852  ? 0.2176 0.1759 0.2224 -0.0067 0.0001  0.0214  850  LEU A CB  
6249  C CG  . LEU A 852  ? 0.2350 0.1967 0.2369 -0.0071 0.0016  0.0227  850  LEU A CG  
6250  C CD1 . LEU A 852  ? 0.2391 0.2016 0.2371 -0.0057 0.0032  0.0202  850  LEU A CD1 
6251  C CD2 . LEU A 852  ? 0.2549 0.2157 0.2576 -0.0068 0.0017  0.0240  850  LEU A CD2 
6252  N N   . CYS A 853  ? 0.2370 0.2033 0.2404 -0.0098 0.0007  0.0229  851  CYS A N   
6253  C CA  . CYS A 853  ? 0.2291 0.1999 0.2333 -0.0118 0.0007  0.0253  851  CYS A CA  
6254  C C   . CYS A 853  ? 0.2365 0.2112 0.2380 -0.0119 0.0021  0.0262  851  CYS A C   
6255  O O   . CYS A 853  ? 0.2551 0.2305 0.2533 -0.0106 0.0033  0.0239  851  CYS A O   
6256  C CB  . CYS A 853  ? 0.2443 0.2166 0.2479 -0.0119 0.0008  0.0237  851  CYS A CB  
6257  S SG  . CYS A 853  ? 0.2751 0.2430 0.2813 -0.0112 -0.0008 0.0215  851  CYS A SG  
6258  N N   . LEU A 854  ? 0.2366 0.2139 0.2397 -0.0134 0.0018  0.0295  852  LEU A N   
6259  C CA  . LEU A 854  ? 0.2276 0.2087 0.2284 -0.0135 0.0029  0.0303  852  LEU A CA  
6260  C C   . LEU A 854  ? 0.2313 0.2190 0.2321 -0.0152 0.0032  0.0323  852  LEU A C   
6261  O O   . LEU A 854  ? 0.2334 0.2231 0.2373 -0.0171 0.0022  0.0354  852  LEU A O   
6262  C CB  . LEU A 854  ? 0.2422 0.2221 0.2446 -0.0138 0.0023  0.0326  852  LEU A CB  
6263  C CG  . LEU A 854  ? 0.2524 0.2263 0.2551 -0.0120 0.0020  0.0307  852  LEU A CG  
6264  C CD1 . LEU A 854  ? 0.2413 0.2142 0.2461 -0.0124 0.0012  0.0332  852  LEU A CD1 
6265  C CD2 . LEU A 854  ? 0.2536 0.2268 0.2525 -0.0101 0.0035  0.0275  852  LEU A CD2 
6266  N N   . GLN A 855  ? 0.2320 0.2235 0.2298 -0.0145 0.0044  0.0304  853  GLN A N   
6267  C CA  . GLN A 855  ? 0.2132 0.2120 0.2106 -0.0158 0.0048  0.0320  853  GLN A CA  
6268  C C   . GLN A 855  ? 0.2558 0.2580 0.2546 -0.0173 0.0044  0.0359  853  GLN A C   
6269  O O   . GLN A 855  ? 0.2629 0.2632 0.2611 -0.0166 0.0044  0.0361  853  GLN A O   
6270  C CB  . GLN A 855  ? 0.2370 0.2390 0.2312 -0.0144 0.0061  0.0289  853  GLN A CB  
6271  C CG  . GLN A 855  ? 0.2449 0.2549 0.2390 -0.0155 0.0065  0.0297  853  GLN A CG  
6272  C CD  . GLN A 855  ? 0.2946 0.3084 0.2859 -0.0141 0.0075  0.0264  853  GLN A CD  
6273  O OE1 . GLN A 855  ? 0.3012 0.3113 0.2912 -0.0123 0.0078  0.0230  853  GLN A OE1 
6274  N NE2 . GLN A 855  ? 0.3221 0.3435 0.3129 -0.0148 0.0078  0.0275  853  GLN A NE2 
6275  N N   . GLU A 856  ? 0.2455 0.2529 0.2462 -0.0193 0.0040  0.0393  854  GLU A N   
6276  C CA  . GLU A 856  ? 0.2613 0.2715 0.2642 -0.0210 0.0032  0.0439  854  GLU A CA  
6277  C C   . GLU A 856  ? 0.3319 0.3455 0.3323 -0.0203 0.0039  0.0439  854  GLU A C   
6278  O O   . GLU A 856  ? 0.2997 0.3118 0.3014 -0.0207 0.0031  0.0463  854  GLU A O   
6279  C CB  . GLU A 856  ? 0.2847 0.3016 0.2897 -0.0233 0.0030  0.0476  854  GLU A CB  
6280  C CG  . GLU A 856  ? 0.3553 0.3765 0.3625 -0.0252 0.0022  0.0530  854  GLU A CG  
6281  C CD  . GLU A 856  ? 0.4361 0.4507 0.4475 -0.0258 0.0005  0.0556  854  GLU A CD  
6282  O OE1 . GLU A 856  ? 0.3671 0.3755 0.3809 -0.0257 -0.0004 0.0544  854  GLU A OE1 
6283  O OE2 . GLU A 856  ? 0.4210 0.4367 0.4332 -0.0263 0.0000  0.0587  854  GLU A OE2 
6284  N N   . ASP A 857  ? 0.3111 0.3292 0.3082 -0.0193 0.0051  0.0409  855  ASP A N   
6285  C CA  . ASP A 857  ? 0.3234 0.3458 0.3183 -0.0187 0.0055  0.0405  855  ASP A CA  
6286  C C   . ASP A 857  ? 0.3460 0.3623 0.3404 -0.0173 0.0054  0.0390  855  ASP A C   
6287  O O   . ASP A 857  ? 0.3931 0.4121 0.3868 -0.0172 0.0053  0.0398  855  ASP A O   
6288  C CB  . ASP A 857  ? 0.3765 0.4046 0.3686 -0.0176 0.0066  0.0369  855  ASP A CB  
6289  N N   . VAL A 858  ? 0.2661 0.2747 0.2607 -0.0161 0.0053  0.0366  856  VAL A N   
6290  C CA  . VAL A 858  ? 0.2896 0.2928 0.2839 -0.0147 0.0052  0.0353  856  VAL A CA  
6291  C C   . VAL A 858  ? 0.2614 0.2584 0.2585 -0.0150 0.0042  0.0371  856  VAL A C   
6292  O O   . VAL A 858  ? 0.2766 0.2691 0.2738 -0.0138 0.0042  0.0360  856  VAL A O   
6293  C CB  . VAL A 858  ? 0.2658 0.2658 0.2581 -0.0128 0.0061  0.0307  856  VAL A CB  
6294  C CG1 . VAL A 858  ? 0.3312 0.3370 0.3212 -0.0122 0.0068  0.0285  856  VAL A CG1 
6295  C CG2 . VAL A 858  ? 0.2552 0.2520 0.2478 -0.0125 0.0062  0.0293  856  VAL A CG2 
6296  N N   . ALA A 859  ? 0.2533 0.2503 0.2532 -0.0165 0.0033  0.0398  857  ALA A N   
6297  C CA  . ALA A 859  ? 0.2521 0.2427 0.2551 -0.0165 0.0022  0.0405  857  ALA A CA  
6298  C C   . ALA A 859  ? 0.2745 0.2635 0.2795 -0.0166 0.0013  0.0429  857  ALA A C   
6299  O O   . ALA A 859  ? 0.2668 0.2500 0.2729 -0.0154 0.0008  0.0417  857  ALA A O   
6300  C CB  . ALA A 859  ? 0.2571 0.2482 0.2633 -0.0182 0.0011  0.0429  857  ALA A CB  
6301  N N   . ASP A 860  ? 0.2828 0.2771 0.2882 -0.0180 0.0010  0.0464  858  ASP A N   
6302  C CA  . ASP A 860  ? 0.3199 0.3127 0.3274 -0.0181 0.0000  0.0490  858  ASP A CA  
6303  C C   . ASP A 860  ? 0.2792 0.2696 0.2844 -0.0162 0.0008  0.0460  858  ASP A C   
6304  O O   . ASP A 860  ? 0.2981 0.2838 0.3052 -0.0153 0.0001  0.0460  858  ASP A O   
6305  C CB  . ASP A 860  ? 0.3197 0.3195 0.3281 -0.0200 -0.0005 0.0536  858  ASP A CB  
6306  C CG  . ASP A 860  ? 0.3807 0.3822 0.3928 -0.0221 -0.0016 0.0577  858  ASP A CG  
6307  O OD1 . ASP A 860  ? 0.4935 0.4892 0.5092 -0.0223 -0.0027 0.0578  858  ASP A OD1 
6308  O OD2 . ASP A 860  ? 0.5241 0.5330 0.5357 -0.0237 -0.0014 0.0607  858  ASP A OD2 
6309  N N   . ARG A 861  ? 0.2642 0.2579 0.2656 -0.0154 0.0021  0.0434  859  ARG A N   
6310  C CA  . ARG A 861  ? 0.2822 0.2738 0.2819 -0.0137 0.0028  0.0407  859  ARG A CA  
6311  C C   . ARG A 861  ? 0.2424 0.2271 0.2423 -0.0121 0.0030  0.0379  859  ARG A C   
6312  O O   . ARG A 861  ? 0.2914 0.2727 0.2921 -0.0111 0.0029  0.0374  859  ARG A O   
6313  C CB  . ARG A 861  ? 0.3629 0.3592 0.3593 -0.0132 0.0039  0.0382  859  ARG A CB  
6314  C CG  . ARG A 861  ? 0.4364 0.4304 0.4315 -0.0116 0.0045  0.0355  859  ARG A CG  
6315  C CD  . ARG A 861  ? 0.6154 0.6147 0.6082 -0.0112 0.0051  0.0334  859  ARG A CD  
6316  N NE  . ARG A 861  ? 0.7725 0.7690 0.7647 -0.0098 0.0055  0.0309  859  ARG A NE  
6317  C CZ  . ARG A 861  ? 0.6603 0.6539 0.6517 -0.0086 0.0062  0.0277  859  ARG A CZ  
6318  N NH1 . ARG A 861  ? 0.7065 0.6996 0.6971 -0.0084 0.0067  0.0262  859  ARG A NH1 
6319  N NH2 . ARG A 861  ? 0.6243 0.6156 0.6159 -0.0075 0.0065  0.0261  859  ARG A NH2 
6320  N N   . ILE A 862  ? 0.2453 0.2283 0.2445 -0.0118 0.0034  0.0359  860  ILE A N   
6321  C CA  . ILE A 862  ? 0.2574 0.2348 0.2566 -0.0102 0.0037  0.0331  860  ILE A CA  
6322  C C   . ILE A 862  ? 0.2494 0.2224 0.2520 -0.0102 0.0024  0.0344  860  ILE A C   
6323  O O   . ILE A 862  ? 0.2637 0.2328 0.2666 -0.0087 0.0025  0.0329  860  ILE A O   
6324  C CB  . ILE A 862  ? 0.2583 0.2356 0.2560 -0.0100 0.0042  0.0309  860  ILE A CB  
6325  C CG1 . ILE A 862  ? 0.2865 0.2668 0.2811 -0.0093 0.0055  0.0288  860  ILE A CG1 
6326  C CG2 . ILE A 862  ? 0.2750 0.2469 0.2730 -0.0085 0.0042  0.0287  860  ILE A CG2 
6327  C CD1 . ILE A 862  ? 0.3403 0.3217 0.3336 -0.0092 0.0060  0.0269  860  ILE A CD1 
6328  N N   . LEU A 863  ? 0.2568 0.2307 0.2623 -0.0118 0.0011  0.0373  861  LEU A N   
6329  C CA  A LEU A 863  ? 0.2631 0.2327 0.2726 -0.0118 -0.0004 0.0385  861  LEU A CA  
6330  C CA  B LEU A 863  ? 0.2632 0.2328 0.2728 -0.0118 -0.0004 0.0385  861  LEU A CA  
6331  C C   . LEU A 863  ? 0.2486 0.2171 0.2594 -0.0112 -0.0009 0.0396  861  LEU A C   
6332  O O   . LEU A 863  ? 0.2395 0.2036 0.2522 -0.0099 -0.0014 0.0383  861  LEU A O   
6333  C CB  A LEU A 863  ? 0.2862 0.2574 0.2992 -0.0139 -0.0018 0.0419  861  LEU A CB  
6334  C CB  B LEU A 863  ? 0.2863 0.2575 0.2994 -0.0139 -0.0019 0.0420  861  LEU A CB  
6335  C CG  A LEU A 863  ? 0.2778 0.2442 0.2958 -0.0140 -0.0038 0.0427  861  LEU A CG  
6336  C CG  B LEU A 863  ? 0.2987 0.2665 0.3142 -0.0140 -0.0028 0.0407  861  LEU A CG  
6337  C CD1 A LEU A 863  ? 0.3064 0.2682 0.3240 -0.0121 -0.0037 0.0383  861  LEU A CD1 
6338  C CD1 B LEU A 863  ? 0.3334 0.3033 0.3527 -0.0164 -0.0042 0.0448  861  LEU A CD1 
6339  C CD2 A LEU A 863  ? 0.3300 0.2987 0.3516 -0.0164 -0.0051 0.0464  861  LEU A CD2 
6340  C CD2 B LEU A 863  ? 0.3066 0.2684 0.3244 -0.0123 -0.0038 0.0385  861  LEU A CD2 
6341  N N   . THR A 864  ? 0.2694 0.2423 0.2793 -0.0121 -0.0006 0.0420  862  THR A N   
6342  C CA  . THR A 864  ? 0.2810 0.2532 0.2919 -0.0114 -0.0010 0.0429  862  THR A CA  
6343  C C   . THR A 864  ? 0.2251 0.1943 0.2340 -0.0093 0.0001  0.0392  862  THR A C   
6344  O O   . THR A 864  ? 0.2535 0.2194 0.2645 -0.0082 -0.0004 0.0388  862  THR A O   
6345  C CB  . THR A 864  ? 0.2806 0.2589 0.2901 -0.0126 -0.0007 0.0454  862  THR A CB  
6346  O OG1 . THR A 864  ? 0.2881 0.2696 0.3000 -0.0146 -0.0019 0.0496  862  THR A OG1 
6347  C CG2 . THR A 864  ? 0.2790 0.2569 0.2891 -0.0118 -0.0010 0.0460  862  THR A CG2 
6348  N N   . MET A 865  ? 0.2269 0.1975 0.2322 -0.0087 0.0017  0.0366  863  MET A N   
6349  C CA  . MET A 865  ? 0.2293 0.1975 0.2330 -0.0069 0.0027  0.0336  863  MET A CA  
6350  C C   . MET A 865  ? 0.2344 0.1979 0.2393 -0.0055 0.0025  0.0316  863  MET A C   
6351  O O   . MET A 865  ? 0.2342 0.1953 0.2396 -0.0040 0.0028  0.0303  863  MET A O   
6352  C CB  . MET A 865  ? 0.2499 0.2205 0.2501 -0.0066 0.0042  0.0315  863  MET A CB  
6353  C CG  . MET A 865  ? 0.3236 0.2924 0.3223 -0.0050 0.0053  0.0290  863  MET A CG  
6354  S SD  . MET A 865  ? 0.3966 0.3684 0.3923 -0.0050 0.0065  0.0269  863  MET A SD  
6355  C CE  . MET A 865  ? 0.2363 0.2136 0.2319 -0.0069 0.0058  0.0292  863  MET A CE  
6356  N N   . LEU A 866  ? 0.2466 0.2092 0.2521 -0.0060 0.0020  0.0313  864  LEU A N   
6357  C CA  . LEU A 866  ? 0.2249 0.1835 0.2316 -0.0047 0.0016  0.0291  864  LEU A CA  
6358  C C   . LEU A 866  ? 0.2377 0.1934 0.2483 -0.0042 0.0002  0.0298  864  LEU A C   
6359  O O   . LEU A 866  ? 0.2484 0.2016 0.2595 -0.0023 0.0003  0.0275  864  LEU A O   
6360  C CB  . LEU A 866  ? 0.2559 0.2144 0.2630 -0.0056 0.0011  0.0289  864  LEU A CB  
6361  C CG  . LEU A 866  ? 0.3432 0.2983 0.3511 -0.0042 0.0006  0.0261  864  LEU A CG  
6362  C CD1 . LEU A 866  ? 0.2951 0.2497 0.2995 -0.0023 0.0022  0.0232  864  LEU A CD1 
6363  C CD2 . LEU A 866  ? 0.3122 0.2679 0.3206 -0.0054 0.0000  0.0262  864  LEU A CD2 
6364  N N   . LYS A 867  ? 0.2347 0.1912 0.2485 -0.0057 -0.0013 0.0331  865  LYS A N   
6365  C CA  . LYS A 867  ? 0.2218 0.1754 0.2401 -0.0051 -0.0029 0.0340  865  LYS A CA  
6366  C C   . LYS A 867  ? 0.2451 0.1987 0.2628 -0.0037 -0.0022 0.0333  865  LYS A C   
6367  O O   . LYS A 867  ? 0.2457 0.1965 0.2656 -0.0021 -0.0028 0.0316  865  LYS A O   
6368  C CB  . LYS A 867  ? 0.2426 0.1974 0.2646 -0.0072 -0.0047 0.0383  865  LYS A CB  
6369  C CG  . LYS A 867  ? 0.2496 0.2041 0.2735 -0.0087 -0.0057 0.0392  865  LYS A CG  
6370  C CD  . LYS A 867  ? 0.2710 0.2279 0.2982 -0.0111 -0.0071 0.0442  865  LYS A CD  
6371  C CE  . LYS A 867  ? 0.3696 0.3268 0.3988 -0.0127 -0.0080 0.0452  865  LYS A CE  
6372  N NZ  . LYS A 867  ? 0.3839 0.3442 0.4165 -0.0153 -0.0093 0.0507  865  LYS A NZ  
6373  N N   . GLY A 868  ? 0.2481 0.2050 0.2629 -0.0043 -0.0010 0.0344  866  GLY A N   
6374  C CA  . GLY A 868  ? 0.2580 0.2151 0.2723 -0.0031 -0.0003 0.0338  866  GLY A CA  
6375  C C   . GLY A 868  ? 0.2291 0.1843 0.2416 -0.0010 0.0010  0.0302  866  GLY A C   
6376  O O   . GLY A 868  ? 0.2527 0.2066 0.2666 0.0005  0.0010  0.0292  866  GLY A O   
6377  N N   . ALA A 869  ? 0.2213 0.1768 0.2309 -0.0009 0.0021  0.0283  867  ALA A N   
6378  C CA  . ALA A 869  ? 0.2150 0.1694 0.2227 0.0010  0.0033  0.0252  867  ALA A CA  
6379  C C   . ALA A 869  ? 0.2301 0.1815 0.2403 0.0025  0.0023  0.0234  867  ALA A C   
6380  O O   . ALA A 869  ? 0.2323 0.1832 0.2423 0.0044  0.0030  0.0213  867  ALA A O   
6381  C CB  . ALA A 869  ? 0.2240 0.1794 0.2283 0.0008  0.0045  0.0240  867  ALA A CB  
6382  N N   . LEU A 870  ? 0.2286 0.1786 0.2413 0.0017  0.0007  0.0240  868  LEU A N   
6383  C CA  . LEU A 870  ? 0.2297 0.1768 0.2454 0.0030  -0.0006 0.0219  868  LEU A CA  
6384  C C   . LEU A 870  ? 0.2485 0.1946 0.2672 0.0045  -0.0012 0.0216  868  LEU A C   
6385  O O   . LEU A 870  ? 0.2457 0.1907 0.2652 0.0066  -0.0012 0.0186  868  LEU A O   
6386  C CB  . LEU A 870  ? 0.2328 0.1785 0.2519 0.0015  -0.0026 0.0234  868  LEU A CB  
6387  C CG  . LEU A 870  ? 0.2754 0.2180 0.2984 0.0026  -0.0044 0.0211  868  LEU A CG  
6388  C CD1 . LEU A 870  ? 0.3329 0.2754 0.3533 0.0033  -0.0038 0.0181  868  LEU A CD1 
6389  C CD2 . LEU A 870  ? 0.3098 0.2508 0.3381 0.0008  -0.0069 0.0239  868  LEU A CD2 
6390  N N   . HIS A 871  ? 0.2413 0.1881 0.2617 0.0034  -0.0017 0.0246  869  HIS A N   
6391  C CA  . HIS A 871  ? 0.2723 0.2180 0.2961 0.0047  -0.0026 0.0245  869  HIS A CA  
6392  C C   . HIS A 871  ? 0.2673 0.2146 0.2888 0.0064  -0.0008 0.0229  869  HIS A C   
6393  O O   . HIS A 871  ? 0.3087 0.2555 0.3329 0.0078  -0.0013 0.0224  869  HIS A O   
6394  C CB  . HIS A 871  ? 0.2839 0.2301 0.3107 0.0030  -0.0040 0.0285  869  HIS A CB  
6395  C CG  . HIS A 871  ? 0.2805 0.2248 0.3112 0.0016  -0.0062 0.0304  869  HIS A CG  
6396  N ND1 . HIS A 871  ? 0.3362 0.2772 0.3721 0.0027  -0.0083 0.0292  869  HIS A ND1 
6397  C CD2 . HIS A 871  ? 0.2645 0.2100 0.2950 -0.0007 -0.0067 0.0331  869  HIS A CD2 
6398  C CE1 . HIS A 871  ? 0.3398 0.2796 0.3789 0.0010  -0.0101 0.0314  869  HIS A CE1 
6399  N NE2 . HIS A 871  ? 0.2966 0.2394 0.3324 -0.0012 -0.0091 0.0340  869  HIS A NE2 
6400  N N   . GLU A 872  ? 0.2299 0.1792 0.2469 0.0063  0.0013  0.0221  870  GLU A N   
6401  C CA  . GLU A 872  ? 0.2384 0.1893 0.2536 0.0078  0.0030  0.0207  870  GLU A CA  
6402  C C   . GLU A 872  ? 0.2575 0.2082 0.2717 0.0100  0.0038  0.0174  870  GLU A C   
6403  O O   . GLU A 872  ? 0.2661 0.2186 0.2788 0.0113  0.0053  0.0163  870  GLU A O   
6404  C CB  . GLU A 872  ? 0.2444 0.1976 0.2558 0.0066  0.0046  0.0219  870  GLU A CB  
6405  C CG  . GLU A 872  ? 0.2596 0.2141 0.2717 0.0047  0.0040  0.0249  870  GLU A CG  
6406  C CD  . GLU A 872  ? 0.2915 0.2464 0.3062 0.0053  0.0035  0.0259  870  GLU A CD  
6407  O OE1 . GLU A 872  ? 0.3116 0.2665 0.3269 0.0071  0.0043  0.0243  870  GLU A OE1 
6408  O OE2 . GLU A 872  ? 0.3116 0.2673 0.3279 0.0040  0.0024  0.0285  870  GLU A OE2 
6409  N N   . LEU A 873  ? 0.2519 0.2008 0.2670 0.0104  0.0027  0.0157  871  LEU A N   
6410  C CA  . LEU A 873  ? 0.2593 0.2085 0.2734 0.0125  0.0032  0.0122  871  LEU A CA  
6411  C C   . LEU A 873  ? 0.2499 0.1987 0.2675 0.0148  0.0023  0.0101  871  LEU A C   
6412  O O   . LEU A 873  ? 0.2937 0.2404 0.3157 0.0146  0.0004  0.0107  871  LEU A O   
6413  C CB  . LEU A 873  ? 0.2510 0.1986 0.2650 0.0122  0.0021  0.0109  871  LEU A CB  
6414  C CG  . LEU A 873  ? 0.2455 0.1938 0.2563 0.0101  0.0029  0.0126  871  LEU A CG  
6415  C CD1 . LEU A 873  ? 0.2569 0.2036 0.2684 0.0097  0.0015  0.0114  871  LEU A CD1 
6416  C CD2 . LEU A 873  ? 0.2816 0.2324 0.2881 0.0108  0.0051  0.0120  871  LEU A CD2 
6417  N N   . HIS A 874  ? 0.2489 0.2001 0.2648 0.0170  0.0037  0.0076  872  HIS A N   
6418  C CA  . HIS A 874  ? 0.2488 0.2006 0.2676 0.0195  0.0032  0.0049  872  HIS A CA  
6419  C C   . HIS A 874  ? 0.2645 0.2161 0.2834 0.0213  0.0024  0.0010  872  HIS A C   
6420  O O   . HIS A 874  ? 0.2562 0.2100 0.2712 0.0219  0.0038  -0.0002 872  HIS A O   
6421  C CB  . HIS A 874  ? 0.2682 0.2237 0.2850 0.0208  0.0054  0.0049  872  HIS A CB  
6422  C CG  . HIS A 874  ? 0.3028 0.2599 0.3223 0.0236  0.0051  0.0020  872  HIS A CG  
6423  N ND1 . HIS A 874  ? 0.3703 0.3312 0.3892 0.0248  0.0069  0.0022  872  HIS A ND1 
6424  C CD2 . HIS A 874  ? 0.4465 0.4024 0.4697 0.0256  0.0033  -0.0013 872  HIS A CD2 
6425  C CE1 . HIS A 874  ? 0.3774 0.3396 0.3991 0.0274  0.0063  -0.0009 872  HIS A CE1 
6426  N NE2 . HIS A 874  ? 0.3635 0.3226 0.3880 0.0280  0.0040  -0.0032 872  HIS A NE2 
6427  N N   . ILE A 875  ? 0.2616 0.2107 0.2852 0.0222  0.0000  -0.0010 873  ILE A N   
6428  C CA  . ILE A 875  ? 0.2684 0.2172 0.2931 0.0240  -0.0013 -0.0052 873  ILE A CA  
6429  C C   . ILE A 875  ? 0.3066 0.2572 0.3339 0.0272  -0.0017 -0.0090 873  ILE A C   
6430  O O   . ILE A 875  ? 0.2936 0.2430 0.3251 0.0277  -0.0027 -0.0086 873  ILE A O   
6431  C CB  . ILE A 875  ? 0.2736 0.2179 0.3024 0.0225  -0.0041 -0.0049 873  ILE A CB  
6432  C CG1 . ILE A 875  ? 0.3657 0.3093 0.3914 0.0198  -0.0036 -0.0022 873  ILE A CG1 
6433  C CG2 . ILE A 875  ? 0.3048 0.2485 0.3363 0.0247  -0.0059 -0.0099 873  ILE A CG2 
6434  C CD1 . ILE A 875  ? 0.3762 0.3202 0.3995 0.0173  -0.0022 0.0025  873  ILE A CD1 
6435  N N   . GLY A 876  ? 0.2527 0.2068 0.2776 0.0296  -0.0008 -0.0128 874  GLY A N   
6436  C CA  . GLY A 876  ? 0.2657 0.2223 0.2929 0.0329  -0.0011 -0.0170 874  GLY A CA  
6437  C C   . GLY A 876  ? 0.3061 0.2678 0.3295 0.0353  0.0002  -0.0206 874  GLY A C   
6438  O O   . GLY A 876  ? 0.2679 0.2304 0.2870 0.0343  0.0012  -0.0199 874  GLY A O   
6439  N N   . ARG A 877  ? 0.2865 0.2518 0.3114 0.0385  0.0002  -0.0245 875  ARG A N   
6440  C CA  . ARG A 877  ? 0.2963 0.2678 0.3174 0.0411  0.0018  -0.0278 875  ARG A CA  
6441  C C   . ARG A 877  ? 0.2834 0.2586 0.2985 0.0398  0.0051  -0.0238 875  ARG A C   
6442  O O   . ARG A 877  ? 0.2587 0.2341 0.2736 0.0385  0.0065  -0.0201 875  ARG A O   
6443  C CB  . ARG A 877  ? 0.3299 0.3055 0.3538 0.0448  0.0016  -0.0321 875  ARG A CB  
6444  C CG  . ARG A 877  ? 0.3299 0.3115 0.3512 0.0479  0.0020  -0.0371 875  ARG A CG  
6445  C CD  . ARG A 877  ? 0.3474 0.3331 0.3723 0.0517  0.0014  -0.0420 875  ARG A CD  
6446  N NE  . ARG A 877  ? 0.3444 0.3359 0.3670 0.0525  0.0043  -0.0400 875  ARG A NE  
6447  C CZ  . ARG A 877  ? 0.4582 0.4551 0.4828 0.0559  0.0046  -0.0437 875  ARG A CZ  
6448  N NH1 . ARG A 877  ? 0.3978 0.3947 0.4270 0.0588  0.0021  -0.0498 875  ARG A NH1 
6449  N NH2 . ARG A 877  ? 0.4258 0.4283 0.4482 0.0563  0.0075  -0.0412 875  ARG A NH2 
6450  N N   . THR A 878  ? 0.2613 0.2394 0.2719 0.0401  0.0061  -0.0245 876  THR A N   
6451  C CA  . THR A 878  ? 0.2882 0.2682 0.2938 0.0382  0.0086  -0.0202 876  THR A CA  
6452  C C   . THR A 878  ? 0.2708 0.2578 0.2737 0.0397  0.0113  -0.0193 876  THR A C   
6453  O O   . THR A 878  ? 0.2994 0.2886 0.2983 0.0385  0.0133  -0.0160 876  THR A O   
6454  C CB  . THR A 878  ? 0.2584 0.2381 0.2608 0.0375  0.0083  -0.0207 876  THR A CB  
6455  O OG1 . THR A 878  ? 0.3122 0.2958 0.3144 0.0406  0.0075  -0.0259 876  THR A OG1 
6456  C CG2 . THR A 878  ? 0.3122 0.2851 0.3170 0.0351  0.0061  -0.0198 876  THR A CG2 
6457  N N   . ASP A 879  ? 0.2750 0.2657 0.2801 0.0424  0.0114  -0.0221 877  ASP A N   
6458  C CA  . ASP A 879  ? 0.3310 0.3288 0.3338 0.0437  0.0141  -0.0209 877  ASP A CA  
6459  C C   . ASP A 879  ? 0.3036 0.3001 0.3079 0.0418  0.0153  -0.0165 877  ASP A C   
6460  O O   . ASP A 879  ? 0.2772 0.2791 0.2817 0.0432  0.0170  -0.0161 877  ASP A O   
6461  C CB  . ASP A 879  ? 0.2915 0.2953 0.2956 0.0477  0.0139  -0.0261 877  ASP A CB  
6462  C CG  . ASP A 879  ? 0.3579 0.3589 0.3677 0.0489  0.0120  -0.0288 877  ASP A CG  
6463  O OD1 . ASP A 879  ? 0.3840 0.3776 0.3971 0.0470  0.0099  -0.0280 877  ASP A OD1 
6464  O OD2 . ASP A 879  ? 0.3558 0.3625 0.3670 0.0519  0.0126  -0.0318 877  ASP A OD2 
6465  N N   . ARG A 880  ? 0.2869 0.2770 0.2923 0.0388  0.0144  -0.0133 878  ARG A N   
6466  C CA  . ARG A 880  ? 0.2593 0.2480 0.2655 0.0366  0.0155  -0.0089 878  ARG A CA  
6467  C C   . ARG A 880  ? 0.2562 0.2419 0.2595 0.0336  0.0160  -0.0050 878  ARG A C   
6468  O O   . ARG A 880  ? 0.2742 0.2556 0.2773 0.0323  0.0145  -0.0054 878  ARG A O   
6469  C CB  . ARG A 880  ? 0.3067 0.2907 0.3177 0.0361  0.0135  -0.0090 878  ARG A CB  
6470  C CG  . ARG A 880  ? 0.3712 0.3578 0.3858 0.0389  0.0130  -0.0122 878  ARG A CG  
6471  C CD  . ARG A 880  ? 0.3911 0.3721 0.4107 0.0380  0.0108  -0.0117 878  ARG A CD  
6472  N NE  . ARG A 880  ? 0.6245 0.6078 0.6474 0.0394  0.0110  -0.0121 878  ARG A NE  
6473  C CZ  . ARG A 880  ? 0.6197 0.6055 0.6457 0.0427  0.0102  -0.0164 878  ARG A CZ  
6474  N NH1 . ARG A 880  ? 0.6673 0.6542 0.6934 0.0449  0.0091  -0.0210 878  ARG A NH1 
6475  N NH2 . ARG A 880  ? 0.6580 0.6456 0.6873 0.0438  0.0104  -0.0164 878  ARG A NH2 
6476  N N   . LEU A 881  ? 0.2480 0.2362 0.2496 0.0323  0.0181  -0.0013 879  LEU A N   
6477  C CA  . LEU A 881  ? 0.2513 0.2370 0.2508 0.0295  0.0186  0.0022  879  LEU A CA  
6478  C C   . LEU A 881  ? 0.2485 0.2278 0.2499 0.0272  0.0168  0.0034  879  LEU A C   
6479  O O   . LEU A 881  ? 0.2595 0.2359 0.2592 0.0253  0.0164  0.0048  879  LEU A O   
6480  C CB  . LEU A 881  ? 0.2673 0.2565 0.2661 0.0287  0.0207  0.0058  879  LEU A CB  
6481  C CG  . LEU A 881  ? 0.2820 0.2692 0.2789 0.0261  0.0213  0.0094  879  LEU A CG  
6482  C CD1 . LEU A 881  ? 0.3116 0.3001 0.3051 0.0264  0.0216  0.0089  879  LEU A CD1 
6483  C CD2 . LEU A 881  ? 0.2819 0.2722 0.2797 0.0252  0.0230  0.0127  879  LEU A CD2 
6484  N N   . SER A 882  ? 0.2361 0.2136 0.2410 0.0274  0.0157  0.0029  880  SER A N   
6485  C CA  . SER A 882  ? 0.2425 0.2149 0.2494 0.0252  0.0142  0.0045  880  SER A CA  
6486  C C   . SER A 882  ? 0.2727 0.2412 0.2803 0.0249  0.0121  0.0027  880  SER A C   
6487  O O   . SER A 882  ? 0.2887 0.2534 0.2975 0.0229  0.0108  0.0044  880  SER A O   
6488  C CB  . SER A 882  ? 0.2715 0.2435 0.2822 0.0255  0.0135  0.0049  880  SER A CB  
6489  O OG  . SER A 882  ? 0.3291 0.3019 0.3423 0.0281  0.0125  0.0014  880  SER A OG  
6490  N N   . VAL A 883  ? 0.2768 0.2465 0.2838 0.0269  0.0116  -0.0007 881  VAL A N   
6491  C CA  . VAL A 883  ? 0.2563 0.2222 0.2645 0.0266  0.0094  -0.0025 881  VAL A CA  
6492  C C   . VAL A 883  ? 0.2670 0.2318 0.2719 0.0247  0.0098  -0.0010 881  VAL A C   
6493  O O   . VAL A 883  ? 0.2995 0.2674 0.3008 0.0251  0.0114  -0.0009 881  VAL A O   
6494  C CB  . VAL A 883  ? 0.2816 0.2494 0.2910 0.0296  0.0085  -0.0073 881  VAL A CB  
6495  C CG1 . VAL A 883  ? 0.2840 0.2483 0.2942 0.0291  0.0064  -0.0092 881  VAL A CG1 
6496  C CG2 . VAL A 883  ? 0.3012 0.2690 0.3151 0.0313  0.0075  -0.0090 881  VAL A CG2 
6497  N N   . ASP A 884  ? 0.2384 0.1990 0.2445 0.0225  0.0083  0.0005  882  ASP A N   
6498  C CA  . ASP A 884  ? 0.2534 0.2128 0.2568 0.0207  0.0084  0.0017  882  ASP A CA  
6499  C C   . ASP A 884  ? 0.2765 0.2347 0.2803 0.0214  0.0069  -0.0011 882  ASP A C   
6500  O O   . ASP A 884  ? 0.3166 0.2756 0.3173 0.0211  0.0074  -0.0014 882  ASP A O   
6501  C CB  . ASP A 884  ? 0.2565 0.2129 0.2611 0.0180  0.0077  0.0049  882  ASP A CB  
6502  C CG  . ASP A 884  ? 0.2520 0.2097 0.2564 0.0172  0.0090  0.0075  882  ASP A CG  
6503  O OD1 . ASP A 884  ? 0.2997 0.2598 0.3013 0.0172  0.0108  0.0084  882  ASP A OD1 
6504  O OD2 . ASP A 884  ? 0.2522 0.2085 0.2595 0.0166  0.0080  0.0088  882  ASP A OD2 
6505  N N   . VAL A 885  ? 0.2537 0.2096 0.2615 0.0221  0.0048  -0.0032 883  VAL A N   
6506  C CA  . VAL A 885  ? 0.2698 0.2239 0.2792 0.0225  0.0028  -0.0058 883  VAL A CA  
6507  C C   . VAL A 885  ? 0.2446 0.1995 0.2569 0.0254  0.0016  -0.0101 883  VAL A C   
6508  O O   . VAL A 885  ? 0.2473 0.2012 0.2635 0.0260  0.0007  -0.0103 883  VAL A O   
6509  C CB  . VAL A 885  ? 0.2688 0.2186 0.2815 0.0200  0.0009  -0.0037 883  VAL A CB  
6510  C CG1 . VAL A 885  ? 0.2953 0.2431 0.3102 0.0203  -0.0013 -0.0065 883  VAL A CG1 
6511  C CG2 . VAL A 885  ? 0.2841 0.2337 0.2938 0.0173  0.0021  0.0002  883  VAL A CG2 
6512  N N   . GLY A 886  ? 0.2553 0.2126 0.2660 0.0273  0.0016  -0.0137 884  GLY A N   
6513  C CA  . GLY A 886  ? 0.2339 0.1926 0.2471 0.0303  0.0003  -0.0185 884  GLY A CA  
6514  C C   . GLY A 886  ? 0.2580 0.2129 0.2760 0.0303  -0.0028 -0.0212 884  GLY A C   
6515  O O   . GLY A 886  ? 0.2607 0.2114 0.2809 0.0278  -0.0042 -0.0188 884  GLY A O   
6516  N N   . PRO A 887  ? 0.2535 0.2102 0.2733 0.0333  -0.0041 -0.0265 885  PRO A N   
6517  C CA  . PRO A 887  ? 0.2281 0.1812 0.2534 0.0336  -0.0075 -0.0297 885  PRO A CA  
6518  C C   . PRO A 887  ? 0.2512 0.2038 0.2745 0.0326  -0.0081 -0.0305 885  PRO A C   
6519  O O   . PRO A 887  ? 0.2604 0.2164 0.2780 0.0325  -0.0060 -0.0297 885  PRO A O   
6520  C CB  . PRO A 887  ? 0.2415 0.1979 0.2689 0.0375  -0.0083 -0.0356 885  PRO A CB  
6521  C CG  . PRO A 887  ? 0.2549 0.2179 0.2756 0.0391  -0.0052 -0.0359 885  PRO A CG  
6522  C CD  . PRO A 887  ? 0.2862 0.2490 0.3033 0.0365  -0.0026 -0.0298 885  PRO A CD  
6523  N N   . VAL A 888  ? 0.2863 0.2348 0.3149 0.0319  -0.0111 -0.0322 886  VAL A N   
6524  C CA  . VAL A 888  ? 0.2586 0.2073 0.2863 0.0319  -0.0123 -0.0346 886  VAL A CA  
6525  C C   . VAL A 888  ? 0.2594 0.2117 0.2877 0.0357  -0.0133 -0.0414 886  VAL A C   
6526  O O   . VAL A 888  ? 0.2899 0.2436 0.3208 0.0382  -0.0138 -0.0443 886  VAL A O   
6527  C CB  . VAL A 888  ? 0.2628 0.2060 0.2960 0.0292  -0.0151 -0.0332 886  VAL A CB  
6528  C CG1 . VAL A 888  ? 0.2877 0.2287 0.3193 0.0256  -0.0137 -0.0266 886  VAL A CG1 
6529  C CG2 . VAL A 888  ? 0.2957 0.2353 0.3372 0.0302  -0.0183 -0.0357 886  VAL A CG2 
6530  N N   . ILE A 889  ? 0.2600 0.2146 0.2856 0.0363  -0.0136 -0.0439 887  ILE A N   
6531  C CA  . ILE A 889  ? 0.2924 0.2527 0.3159 0.0400  -0.0135 -0.0497 887  ILE A CA  
6532  C C   . ILE A 889  ? 0.3171 0.2762 0.3474 0.0426  -0.0168 -0.0558 887  ILE A C   
6533  O O   . ILE A 889  ? 0.2959 0.2598 0.3256 0.0461  -0.0165 -0.0602 887  ILE A O   
6534  C CB  . ILE A 889  ? 0.2784 0.2417 0.2972 0.0400  -0.0130 -0.0506 887  ILE A CB  
6535  C CG1 . ILE A 889  ? 0.2928 0.2634 0.3081 0.0439  -0.0123 -0.0558 887  ILE A CG1 
6536  C CG2 . ILE A 889  ? 0.2660 0.2247 0.2892 0.0383  -0.0161 -0.0519 887  ILE A CG2 
6537  C CD1 . ILE A 889  ? 0.2844 0.2604 0.2947 0.0452  -0.0089 -0.0537 887  ILE A CD1 
6538  N N   . THR A 890  ? 0.2505 0.2035 0.2877 0.0410  -0.0200 -0.0562 888  THR A N   
6539  C CA  . THR A 890  ? 0.2709 0.2224 0.3156 0.0434  -0.0237 -0.0623 888  THR A CA  
6540  C C   . THR A 890  ? 0.2495 0.1935 0.3023 0.0410  -0.0264 -0.0597 888  THR A C   
6541  O O   . THR A 890  ? 0.2877 0.2281 0.3402 0.0373  -0.0258 -0.0536 888  THR A O   
6542  C CB  . THR A 890  ? 0.2987 0.2513 0.3444 0.0446  -0.0260 -0.0677 888  THR A CB  
6543  O OG1 . THR A 890  ? 0.2981 0.2463 0.3447 0.0409  -0.0268 -0.0639 888  THR A OG1 
6544  C CG2 . THR A 890  ? 0.3173 0.2778 0.3552 0.0471  -0.0237 -0.0706 888  THR A CG2 
6545  N N   . SER A 891  ? 0.2819 0.2239 0.3422 0.0432  -0.0296 -0.0646 889  SER A N   
6546  C CA  A SER A 891  ? 0.3007 0.2356 0.3701 0.0412  -0.0329 -0.0627 889  SER A CA  
6547  C CA  B SER A 891  ? 0.3004 0.2354 0.3698 0.0411  -0.0328 -0.0625 889  SER A CA  
6548  C C   . SER A 891  ? 0.3069 0.2379 0.3791 0.0381  -0.0349 -0.0609 889  SER A C   
6549  O O   . SER A 891  ? 0.3090 0.2349 0.3857 0.0348  -0.0361 -0.0558 889  SER A O   
6550  C CB  A SER A 891  ? 0.3162 0.2500 0.3938 0.0445  -0.0363 -0.0692 889  SER A CB  
6551  C CB  B SER A 891  ? 0.3164 0.2501 0.3938 0.0444  -0.0362 -0.0688 889  SER A CB  
6552  O OG  A SER A 891  ? 0.3129 0.2497 0.3892 0.0470  -0.0347 -0.0701 889  SER A OG  
6553  O OG  B SER A 891  ? 0.3655 0.3009 0.4450 0.0467  -0.0386 -0.0759 889  SER A OG  
6554  N N   . GLU A 892  ? 0.3191 0.2528 0.3890 0.0392  -0.0354 -0.0652 890  GLU A N   
6555  C CA  . GLU A 892  ? 0.3174 0.2478 0.3900 0.0363  -0.0374 -0.0637 890  GLU A CA  
6556  C C   . GLU A 892  ? 0.3322 0.2624 0.3990 0.0325  -0.0344 -0.0561 890  GLU A C   
6557  O O   . GLU A 892  ? 0.3198 0.2457 0.3904 0.0291  -0.0358 -0.0519 890  GLU A O   
6558  C CB  . GLU A 892  ? 0.3602 0.2941 0.4313 0.0386  -0.0386 -0.0702 890  GLU A CB  
6559  C CG  . GLU A 892  ? 0.4764 0.4121 0.5520 0.0429  -0.0411 -0.0786 890  GLU A CG  
6560  C CD  . GLU A 892  ? 0.4469 0.3901 0.5149 0.0466  -0.0380 -0.0817 890  GLU A CD  
6561  O OE1 . GLU A 892  ? 0.7232 0.6720 0.7848 0.0480  -0.0366 -0.0842 890  GLU A OE1 
6562  O OE2 . GLU A 892  ? 0.4195 0.3634 0.4880 0.0480  -0.0370 -0.0813 890  GLU A OE2 
6563  N N   . ALA A 893  ? 0.2976 0.2325 0.3553 0.0332  -0.0305 -0.0544 891  ALA A N   
6564  C CA  . ALA A 893  ? 0.2895 0.2243 0.3419 0.0298  -0.0276 -0.0474 891  ALA A CA  
6565  C C   . ALA A 893  ? 0.3263 0.2570 0.3826 0.0273  -0.0278 -0.0418 891  ALA A C   
6566  O O   . ALA A 893  ? 0.3249 0.2529 0.3824 0.0238  -0.0279 -0.0368 891  ALA A O   
6567  C CB  . ALA A 893  ? 0.2906 0.2311 0.3337 0.0312  -0.0236 -0.0467 891  ALA A CB  
6568  N N   . LYS A 894  ? 0.2877 0.2181 0.3461 0.0291  -0.0278 -0.0427 892  LYS A N   
6569  C CA  . LYS A 894  ? 0.2743 0.2010 0.3369 0.0270  -0.0282 -0.0376 892  LYS A CA  
6570  C C   . LYS A 894  ? 0.3063 0.2276 0.3775 0.0246  -0.0319 -0.0360 892  LYS A C   
6571  O O   . LYS A 894  ? 0.3293 0.2484 0.4015 0.0212  -0.0317 -0.0299 892  LYS A O   
6572  C CB  . LYS A 894  ? 0.2598 0.1871 0.3246 0.0299  -0.0284 -0.0400 892  LYS A CB  
6573  C CG  . LYS A 894  ? 0.2926 0.2162 0.3621 0.0280  -0.0291 -0.0352 892  LYS A CG  
6574  C CD  . LYS A 894  ? 0.3380 0.2627 0.4094 0.0311  -0.0290 -0.0378 892  LYS A CD  
6575  C CE  . LYS A 894  ? 0.3606 0.2814 0.4376 0.0293  -0.0303 -0.0330 892  LYS A CE  
6576  N NZ  . LYS A 894  ? 0.5356 0.4564 0.6171 0.0325  -0.0315 -0.0366 892  LYS A NZ  
6577  N N   . ASP A 895  ? 0.3058 0.2253 0.3834 0.0263  -0.0354 -0.0415 893  ASP A N   
6578  C CA  . ASP A 895  ? 0.3588 0.2730 0.4458 0.0240  -0.0392 -0.0400 893  ASP A CA  
6579  C C   . ASP A 895  ? 0.3019 0.2157 0.3871 0.0204  -0.0387 -0.0358 893  ASP A C   
6580  O O   . ASP A 895  ? 0.3345 0.2450 0.4245 0.0170  -0.0401 -0.0304 893  ASP A O   
6581  C CB  . ASP A 895  ? 0.3316 0.2442 0.4259 0.0267  -0.0431 -0.0475 893  ASP A CB  
6582  C CG  . ASP A 895  ? 0.4707 0.3829 0.5691 0.0301  -0.0444 -0.0515 893  ASP A CG  
6583  O OD1 . ASP A 895  ? 0.5159 0.4274 0.6141 0.0297  -0.0431 -0.0476 893  ASP A OD1 
6584  O OD2 . ASP A 895  ? 0.5054 0.4182 0.6072 0.0334  -0.0467 -0.0590 893  ASP A OD2 
6585  N N   . ASN A 896  ? 0.3107 0.2282 0.3890 0.0210  -0.0369 -0.0380 894  ASN A N   
6586  C CA  . ASN A 896  ? 0.3063 0.2239 0.3830 0.0178  -0.0365 -0.0345 894  ASN A CA  
6587  C C   . ASN A 896  ? 0.3354 0.2535 0.4080 0.0147  -0.0337 -0.0269 894  ASN A C   
6588  O O   . ASN A 896  ? 0.3386 0.2548 0.4142 0.0113  -0.0346 -0.0222 894  ASN A O   
6589  C CB  . ASN A 896  ? 0.3902 0.3120 0.4601 0.0194  -0.0350 -0.0385 894  ASN A CB  
6590  C CG  . ASN A 896  ? 0.5262 0.4485 0.5938 0.0164  -0.0343 -0.0351 894  ASN A CG  
6591  O OD1 . ASN A 896  ? 0.5715 0.4965 0.6320 0.0151  -0.0311 -0.0313 894  ASN A OD1 
6592  N ND2 . ASN A 896  ? 0.5684 0.4883 0.6426 0.0151  -0.0375 -0.0364 894  ASN A ND2 
6593  N N   . ILE A 897  ? 0.3045 0.2254 0.3703 0.0158  -0.0304 -0.0258 895  ILE A N   
6594  C CA  . ILE A 897  ? 0.2967 0.2185 0.3584 0.0132  -0.0278 -0.0192 895  ILE A CA  
6595  C C   . ILE A 897  ? 0.3319 0.2502 0.4005 0.0111  -0.0296 -0.0146 895  ILE A C   
6596  O O   . ILE A 897  ? 0.3155 0.2334 0.3845 0.0078  -0.0293 -0.0090 895  ILE A O   
6597  C CB  . ILE A 897  ? 0.2828 0.2082 0.3368 0.0152  -0.0243 -0.0194 895  ILE A CB  
6598  C CG1 . ILE A 897  ? 0.2850 0.2143 0.3325 0.0171  -0.0225 -0.0233 895  ILE A CG1 
6599  C CG2 . ILE A 897  ? 0.3087 0.2349 0.3591 0.0126  -0.0218 -0.0131 895  ILE A CG2 
6600  C CD1 . ILE A 897  ? 0.2842 0.2169 0.3263 0.0200  -0.0200 -0.0253 895  ILE A CD1 
6601  N N   . GLU A 898  ? 0.3142 0.2300 0.3884 0.0130  -0.0317 -0.0170 896  GLU A N   
6602  C CA  . GLU A 898  ? 0.2932 0.2057 0.3742 0.0112  -0.0336 -0.0125 896  GLU A CA  
6603  C C   . GLU A 898  ? 0.3164 0.2257 0.4048 0.0082  -0.0366 -0.0099 896  GLU A C   
6604  O O   . GLU A 898  ? 0.3339 0.2421 0.4253 0.0053  -0.0371 -0.0037 896  GLU A O   
6605  C CB  . GLU A 898  ? 0.3469 0.2574 0.4331 0.0142  -0.0355 -0.0164 896  GLU A CB  
6606  C CG  . GLU A 898  ? 0.4085 0.3221 0.4886 0.0166  -0.0325 -0.0176 896  GLU A CG  
6607  C CD  . GLU A 898  ? 0.3440 0.2558 0.4300 0.0196  -0.0346 -0.0214 896  GLU A CD  
6608  O OE1 . GLU A 898  ? 0.5018 0.4109 0.5948 0.0210  -0.0380 -0.0258 896  GLU A OE1 
6609  O OE2 . GLU A 898  ? 0.4917 0.4048 0.5755 0.0206  -0.0329 -0.0200 896  GLU A OE2 
6610  N N   . LYS A 899  ? 0.2972 0.2055 0.3890 0.0090  -0.0389 -0.0145 897  LYS A N   
6611  C CA  . LYS A 899  ? 0.2988 0.2042 0.3978 0.0061  -0.0418 -0.0120 897  LYS A CA  
6612  C C   . LYS A 899  ? 0.3455 0.2536 0.4401 0.0025  -0.0396 -0.0058 897  LYS A C   
6613  O O   . LYS A 899  ? 0.3517 0.2583 0.4515 -0.0008 -0.0410 -0.0003 897  LYS A O   
6614  C CB  . LYS A 899  ? 0.3558 0.2603 0.4580 0.0077  -0.0443 -0.0185 897  LYS A CB  
6615  N N   . HIS A 900  ? 0.3063 0.2184 0.3914 0.0031  -0.0361 -0.0067 898  HIS A N   
6616  C CA  . HIS A 900  ? 0.3180 0.2329 0.3985 0.0000  -0.0338 -0.0014 898  HIS A CA  
6617  C C   . HIS A 900  ? 0.3059 0.2214 0.3859 -0.0020 -0.0326 0.0051  898  HIS A C   
6618  O O   . HIS A 900  ? 0.3224 0.2385 0.4048 -0.0052 -0.0329 0.0106  898  HIS A O   
6619  C CB  . HIS A 900  ? 0.2959 0.2148 0.3665 0.0014  -0.0304 -0.0038 898  HIS A CB  
6620  C CG  . HIS A 900  ? 0.3051 0.2272 0.3704 -0.0012 -0.0278 0.0013  898  HIS A CG  
6621  N ND1 . HIS A 900  ? 0.3416 0.2647 0.4083 -0.0037 -0.0284 0.0033  898  HIS A ND1 
6622  C CD2 . HIS A 900  ? 0.3193 0.2442 0.3784 -0.0016 -0.0247 0.0044  898  HIS A CD2 
6623  C CE1 . HIS A 900  ? 0.3125 0.2390 0.3738 -0.0054 -0.0257 0.0074  898  HIS A CE1 
6624  N NE2 . HIS A 900  ? 0.2982 0.2257 0.3548 -0.0042 -0.0235 0.0080  898  HIS A NE2 
6625  N N   . ILE A 901  ? 0.2808 0.1967 0.3578 0.0000  -0.0311 0.0045  899  ILE A N   
6626  C CA  . ILE A 901  ? 0.2902 0.2070 0.3664 -0.0016 -0.0299 0.0102  899  ILE A CA  
6627  C C   . ILE A 901  ? 0.3205 0.2343 0.4060 -0.0039 -0.0331 0.0146  899  ILE A C   
6628  O O   . ILE A 901  ? 0.3440 0.2595 0.4300 -0.0069 -0.0327 0.0208  899  ILE A O   
6629  C CB  . ILE A 901  ? 0.2713 0.1885 0.3441 0.0011  -0.0283 0.0082  899  ILE A CB  
6630  C CG1 . ILE A 901  ? 0.2846 0.2053 0.3482 0.0030  -0.0250 0.0049  899  ILE A CG1 
6631  C CG2 . ILE A 901  ? 0.2888 0.2067 0.3620 -0.0005 -0.0277 0.0139  899  ILE A CG2 
6632  C CD1 . ILE A 901  ? 0.2911 0.2126 0.3514 0.0060  -0.0235 0.0021  899  ILE A CD1 
6633  N N   . GLU A 902  ? 0.3401 0.2498 0.4336 -0.0026 -0.0365 0.0114  900  GLU A N   
6634  C CA  . GLU A 902  ? 0.3662 0.2726 0.4694 -0.0047 -0.0398 0.0157  900  GLU A CA  
6635  C C   . GLU A 902  ? 0.3373 0.2439 0.4445 -0.0081 -0.0413 0.0195  900  GLU A C   
6636  O O   . GLU A 902  ? 0.3902 0.2965 0.5028 -0.0110 -0.0427 0.0258  900  GLU A O   
6637  C CB  . GLU A 902  ? 0.3873 0.2891 0.4986 -0.0021 -0.0433 0.0109  900  GLU A CB  
6638  C CG  . GLU A 902  ? 0.4345 0.3362 0.5433 0.0009  -0.0422 0.0086  900  GLU A CG  
6639  C CD  . GLU A 902  ? 0.5419 0.4456 0.6483 -0.0008 -0.0404 0.0151  900  GLU A CD  
6640  O OE1 . GLU A 902  ? 0.5632 0.4655 0.6758 -0.0035 -0.0424 0.0210  900  GLU A OE1 
6641  O OE2 . GLU A 902  ? 0.5187 0.4254 0.6172 0.0006  -0.0372 0.0144  900  GLU A OE2 
6642  N N   . ARG A 903  ? 0.3570 0.2645 0.4620 -0.0079 -0.0410 0.0158  901  ARG A N   
6643  C CA  . ARG A 903  ? 0.3781 0.2868 0.4858 -0.0113 -0.0418 0.0195  901  ARG A CA  
6644  C C   . ARG A 903  ? 0.4258 0.3393 0.5279 -0.0140 -0.0388 0.0262  901  ARG A C   
6645  O O   . ARG A 903  ? 0.3928 0.3071 0.4997 -0.0173 -0.0400 0.0323  901  ARG A O   
6646  C CB  . ARG A 903  ? 0.4385 0.3479 0.5437 -0.0103 -0.0417 0.0141  901  ARG A CB  
6647  N N   . MET A 904  ? 0.3751 0.2920 0.4673 -0.0127 -0.0351 0.0249  902  MET A N   
6648  C CA  A MET A 904  ? 0.3653 0.2871 0.4520 -0.0148 -0.0323 0.0304  902  MET A CA  
6649  C CA  B MET A 904  ? 0.3652 0.2870 0.4519 -0.0148 -0.0323 0.0304  902  MET A CA  
6650  C C   . MET A 904  ? 0.3659 0.2876 0.4564 -0.0164 -0.0331 0.0363  902  MET A C   
6651  O O   . MET A 904  ? 0.3867 0.3116 0.4783 -0.0194 -0.0329 0.0425  902  MET A O   
6652  C CB  A MET A 904  ? 0.3353 0.2599 0.4116 -0.0127 -0.0286 0.0275  902  MET A CB  
6653  C CB  B MET A 904  ? 0.3347 0.2595 0.4111 -0.0127 -0.0285 0.0275  902  MET A CB  
6654  C CG  A MET A 904  ? 0.3443 0.2705 0.4157 -0.0118 -0.0272 0.0234  902  MET A CG  
6655  C CG  B MET A 904  ? 0.3382 0.2636 0.4101 -0.0111 -0.0275 0.0221  902  MET A CG  
6656  S SD  A MET A 904  ? 0.4108 0.3402 0.4840 -0.0155 -0.0275 0.0277  902  MET A SD  
6657  S SD  B MET A 904  ? 0.4363 0.3650 0.5076 -0.0140 -0.0272 0.0244  902  MET A SD  
6658  C CE  A MET A 904  ? 0.3625 0.2935 0.4292 -0.0138 -0.0258 0.0221  902  MET A CE  
6659  C CE  B MET A 904  ? 0.3630 0.2872 0.4443 -0.0144 -0.0315 0.0220  902  MET A CE  
6660  N N   . ARG A 905  ? 0.3281 0.2467 0.4208 -0.0142 -0.0341 0.0345  903  ARG A N   
6661  C CA  . ARG A 905  ? 0.3596 0.2780 0.4560 -0.0154 -0.0350 0.0400  903  ARG A CA  
6662  C C   . ARG A 905  ? 0.4557 0.3723 0.5622 -0.0183 -0.0384 0.0449  903  ARG A C   
6663  O O   . ARG A 905  ? 0.4133 0.3325 0.5215 -0.0209 -0.0385 0.0518  903  ARG A O   
6664  C CB  . ARG A 905  ? 0.3756 0.2908 0.4732 -0.0123 -0.0356 0.0364  903  ARG A CB  
6665  C CG  . ARG A 905  ? 0.4373 0.3533 0.5364 -0.0130 -0.0357 0.0416  903  ARG A CG  
6666  C CD  . ARG A 905  ? 0.4888 0.4008 0.5914 -0.0101 -0.0372 0.0382  903  ARG A CD  
6667  N NE  . ARG A 905  ? 0.4441 0.3559 0.5411 -0.0066 -0.0354 0.0310  903  ARG A NE  
6668  C CZ  . ARG A 905  ? 0.4111 0.3256 0.5004 -0.0050 -0.0323 0.0297  903  ARG A CZ  
6669  N NH1 . ARG A 905  ? 0.4740 0.3918 0.5596 -0.0064 -0.0305 0.0346  903  ARG A NH1 
6670  N NH2 . ARG A 905  ? 0.5005 0.4147 0.5857 -0.0018 -0.0310 0.0234  903  ARG A NH2 
6671  N N   . GLY A 906  ? 0.3821 0.2945 0.4955 -0.0180 -0.0414 0.0416  904  GLY A N   
6672  C CA  . GLY A 906  ? 0.4129 0.3232 0.5368 -0.0208 -0.0450 0.0461  904  GLY A CA  
6673  C C   . GLY A 906  ? 0.4946 0.4095 0.6177 -0.0245 -0.0441 0.0516  904  GLY A C   
6674  O O   . GLY A 906  ? 0.4900 0.4049 0.6207 -0.0275 -0.0464 0.0579  904  GLY A O   
6675  N N   . LEU A 907  ? 0.4732 0.3922 0.5875 -0.0243 -0.0409 0.0496  905  LEU A N   
6676  C CA  . LEU A 907  ? 0.4481 0.3726 0.5606 -0.0275 -0.0395 0.0545  905  LEU A CA  
6677  C C   . LEU A 907  ? 0.4334 0.3636 0.5408 -0.0290 -0.0370 0.0605  905  LEU A C   
6678  O O   . LEU A 907  ? 0.4893 0.4251 0.5942 -0.0315 -0.0355 0.0646  905  LEU A O   
6679  C CB  . LEU A 907  ? 0.4215 0.3482 0.5268 -0.0266 -0.0372 0.0496  905  LEU A CB  
6680  C CG  . LEU A 907  ? 0.4798 0.4021 0.5899 -0.0254 -0.0397 0.0440  905  LEU A CG  
6681  C CD1 . LEU A 907  ? 0.4678 0.3928 0.5702 -0.0244 -0.0373 0.0396  905  LEU A CD1 
6682  C CD2 . LEU A 907  ? 0.4875 0.4083 0.6084 -0.0286 -0.0432 0.0482  905  LEU A CD2 
6683  N N   . GLY A 908  ? 0.3844 0.3136 0.4902 -0.0275 -0.0366 0.0609  906  GLY A N   
6684  C CA  . GLY A 908  ? 0.4316 0.3662 0.5329 -0.0287 -0.0344 0.0662  906  GLY A CA  
6685  C C   . GLY A 908  ? 0.3985 0.3373 0.4886 -0.0271 -0.0304 0.0633  906  GLY A C   
6686  O O   . GLY A 908  ? 0.3859 0.3299 0.4718 -0.0282 -0.0285 0.0673  906  GLY A O   
6687  N N   . ARG A 909  ? 0.3549 0.2918 0.4404 -0.0247 -0.0292 0.0565  907  ARG A N   
6688  C CA  . ARG A 909  ? 0.3145 0.2548 0.3900 -0.0231 -0.0256 0.0537  907  ARG A CA  
6689  C C   . ARG A 909  ? 0.3872 0.3266 0.4599 -0.0211 -0.0247 0.0530  907  ARG A C   
6690  O O   . ARG A 909  ? 0.3827 0.3173 0.4598 -0.0194 -0.0265 0.0511  907  ARG A O   
6691  C CB  . ARG A 909  ? 0.3171 0.2555 0.3889 -0.0210 -0.0247 0.0471  907  ARG A CB  
6692  C CG  . ARG A 909  ? 0.3756 0.3145 0.4506 -0.0227 -0.0258 0.0471  907  ARG A CG  
6693  C CD  . ARG A 909  ? 0.4067 0.3521 0.4778 -0.0251 -0.0238 0.0509  907  ARG A CD  
6694  N NE  . ARG A 909  ? 0.5157 0.4618 0.5887 -0.0263 -0.0245 0.0499  907  ARG A NE  
6695  C CZ  . ARG A 909  ? 0.6897 0.6371 0.7692 -0.0293 -0.0263 0.0543  907  ARG A CZ  
6696  N NH1 . ARG A 909  ? 0.6154 0.5637 0.7003 -0.0314 -0.0278 0.0604  907  ARG A NH1 
6697  N NH2 . ARG A 909  ? 0.6011 0.5492 0.6818 -0.0301 -0.0268 0.0529  907  ARG A NH2 
6698  N N   . LYS A 910  ? 0.2884 0.2326 0.3542 -0.0211 -0.0219 0.0543  908  LYS A N   
6699  C CA  . LYS A 910  ? 0.3134 0.2572 0.3763 -0.0193 -0.0209 0.0536  908  LYS A CA  
6700  C C   . LYS A 910  ? 0.2921 0.2325 0.3515 -0.0160 -0.0199 0.0468  908  LYS A C   
6701  O O   . LYS A 910  ? 0.3009 0.2426 0.3549 -0.0152 -0.0180 0.0434  908  LYS A O   
6702  C CB  . LYS A 910  ? 0.3283 0.2784 0.3850 -0.0201 -0.0183 0.0563  908  LYS A CB  
6703  C CG  . LYS A 910  ? 0.4494 0.4037 0.5092 -0.0230 -0.0192 0.0634  908  LYS A CG  
6704  C CD  . LYS A 910  ? 0.4780 0.4386 0.5312 -0.0232 -0.0167 0.0650  908  LYS A CD  
6705  C CE  . LYS A 910  ? 0.4985 0.4572 0.5484 -0.0207 -0.0157 0.0620  908  LYS A CE  
6706  N NZ  . LYS A 910  ? 0.6938 0.6586 0.7388 -0.0212 -0.0139 0.0643  908  LYS A NZ  
6707  N N   . VAL A 911  ? 0.2823 0.2189 0.3447 -0.0141 -0.0211 0.0450  909  VAL A N   
6708  C CA  . VAL A 911  ? 0.2914 0.2250 0.3513 -0.0108 -0.0204 0.0388  909  VAL A CA  
6709  C C   . VAL A 911  ? 0.3105 0.2448 0.3676 -0.0093 -0.0192 0.0388  909  VAL A C   
6710  O O   . VAL A 911  ? 0.2928 0.2261 0.3544 -0.0096 -0.0207 0.0417  909  VAL A O   
6711  C CB  . VAL A 911  ? 0.2997 0.2281 0.3666 -0.0096 -0.0234 0.0357  909  VAL A CB  
6712  C CG1 . VAL A 911  ? 0.3135 0.2400 0.3776 -0.0061 -0.0226 0.0292  909  VAL A CG1 
6713  C CG2 . VAL A 911  ? 0.3382 0.2660 0.4083 -0.0113 -0.0249 0.0357  909  VAL A CG2 
6714  N N   . GLU A 912  ? 0.2684 0.2046 0.3185 -0.0077 -0.0164 0.0358  910  GLU A N   
6715  C CA  . GLU A 912  ? 0.2814 0.2183 0.3285 -0.0060 -0.0150 0.0349  910  GLU A CA  
6716  C C   . GLU A 912  ? 0.2819 0.2160 0.3285 -0.0029 -0.0148 0.0292  910  GLU A C   
6717  O O   . GLU A 912  ? 0.2720 0.2062 0.3155 -0.0020 -0.0139 0.0257  910  GLU A O   
6718  C CB  . GLU A 912  ? 0.3144 0.2557 0.3543 -0.0066 -0.0121 0.0357  910  GLU A CB  
6719  C CG  . GLU A 912  ? 0.2957 0.2383 0.3331 -0.0054 -0.0108 0.0359  910  GLU A CG  
6720  C CD  . GLU A 912  ? 0.3365 0.2804 0.3772 -0.0069 -0.0120 0.0408  910  GLU A CD  
6721  O OE1 . GLU A 912  ? 0.3187 0.2633 0.3627 -0.0091 -0.0135 0.0446  910  GLU A OE1 
6722  O OE2 . GLU A 912  ? 0.3756 0.3200 0.4156 -0.0059 -0.0115 0.0410  910  GLU A OE2 
6723  N N   . GLN A 913  ? 0.2698 0.2019 0.3196 -0.0012 -0.0158 0.0284  911  GLN A N   
6724  C CA  . GLN A 913  ? 0.2908 0.2213 0.3399 0.0019  -0.0155 0.0230  911  GLN A CA  
6725  C C   . GLN A 913  ? 0.3146 0.2460 0.3625 0.0035  -0.0144 0.0228  911  GLN A C   
6726  O O   . GLN A 913  ? 0.3339 0.2651 0.3851 0.0027  -0.0155 0.0262  911  GLN A O   
6727  C CB  . GLN A 913  ? 0.2985 0.2250 0.3546 0.0031  -0.0185 0.0203  911  GLN A CB  
6728  C CG  . GLN A 913  ? 0.3413 0.2666 0.3994 0.0019  -0.0198 0.0196  911  GLN A CG  
6729  C CD  . GLN A 913  ? 0.3496 0.2710 0.4144 0.0035  -0.0228 0.0158  911  GLN A CD  
6730  O OE1 . GLN A 913  ? 0.3852 0.3038 0.4570 0.0034  -0.0254 0.0172  911  GLN A OE1 
6731  N NE2 . GLN A 913  ? 0.3298 0.2511 0.3926 0.0052  -0.0226 0.0108  911  GLN A NE2 
6732  N N   . ILE A 914  ? 0.3218 0.2544 0.3653 0.0058  -0.0124 0.0189  912  ILE A N   
6733  C CA  . ILE A 914  ? 0.2903 0.2238 0.3332 0.0075  -0.0115 0.0183  912  ILE A CA  
6734  C C   . ILE A 914  ? 0.3805 0.3112 0.4297 0.0096  -0.0138 0.0158  912  ILE A C   
6735  O O   . ILE A 914  ? 0.3503 0.2787 0.4026 0.0106  -0.0155 0.0127  912  ILE A O   
6736  C CB  . ILE A 914  ? 0.4223 0.3587 0.4589 0.0091  -0.0086 0.0156  912  ILE A CB  
6737  C CG1 . ILE A 914  ? 0.4463 0.3820 0.4832 0.0120  -0.0087 0.0103  912  ILE A CG1 
6738  C CG2 . ILE A 914  ? 0.4527 0.3910 0.4840 0.0074  -0.0068 0.0167  912  ILE A CG2 
6739  C CD1 . ILE A 914  ? 0.5955 0.5329 0.6316 0.0144  -0.0075 0.0084  912  ILE A CD1 
6740  N N   . GLY A 915  ? 0.4077 0.3384 0.4592 0.0103  -0.0142 0.0172  913  GLY A N   
6741  C CA  . GLY A 915  ? 0.3848 0.3131 0.4424 0.0126  -0.0163 0.0145  913  GLY A CA  
6742  C C   . GLY A 915  ? 0.3692 0.2992 0.4241 0.0158  -0.0147 0.0092  913  GLY A C   
6743  O O   . GLY A 915  ? 0.4753 0.4085 0.5247 0.0163  -0.0120 0.0092  913  GLY A O   
6744  N N   . LEU A 916  ? 0.3820 0.3101 0.4408 0.0181  -0.0165 0.0047  914  LEU A N   
6745  C CA  . LEU A 916  ? 0.3729 0.3034 0.4295 0.0214  -0.0152 -0.0006 914  LEU A CA  
6746  C C   . LEU A 916  ? 0.4203 0.3512 0.4806 0.0238  -0.0158 -0.0022 914  LEU A C   
6747  O O   . LEU A 916  ? 0.3998 0.3276 0.4668 0.0237  -0.0185 -0.0011 914  LEU A O   
6748  C CB  . LEU A 916  ? 0.3875 0.3166 0.4461 0.0228  -0.0169 -0.0054 914  LEU A CB  
6749  C CG  . LEU A 916  ? 0.3739 0.3033 0.4286 0.0209  -0.0161 -0.0047 914  LEU A CG  
6750  C CD1 . LEU A 916  ? 0.4302 0.3592 0.4861 0.0230  -0.0174 -0.0103 914  LEU A CD1 
6751  C CD2 . LEU A 916  ? 0.4330 0.3662 0.4795 0.0201  -0.0125 -0.0030 914  LEU A CD2 
6752  N N   . ALA A 917  ? 0.3797 0.3146 0.4359 0.0259  -0.0133 -0.0046 915  ALA A N   
6753  C CA  . ALA A 917  ? 0.3692 0.3053 0.4286 0.0285  -0.0136 -0.0066 915  ALA A CA  
6754  C C   . ALA A 917  ? 0.3738 0.3084 0.4388 0.0315  -0.0161 -0.0122 915  ALA A C   
6755  O O   . ALA A 917  ? 0.3993 0.3335 0.4639 0.0321  -0.0168 -0.0156 915  ALA A O   
6756  C CB  . ALA A 917  ? 0.4210 0.3623 0.4746 0.0299  -0.0102 -0.0076 915  ALA A CB  
6757  N N   . SER A 918  ? 0.4201 0.3541 0.4907 0.0334  -0.0177 -0.0134 916  SER A N   
6758  C CA  . SER A 918  ? 0.4228 0.3554 0.4998 0.0365  -0.0204 -0.0191 916  SER A CA  
6759  C C   . SER A 918  ? 0.3681 0.3052 0.4412 0.0396  -0.0188 -0.0251 916  SER A C   
6760  O O   . SER A 918  ? 0.3628 0.2989 0.4395 0.0415  -0.0210 -0.0302 916  SER A O   
6761  C CB  . SER A 918  ? 0.4501 0.3819 0.5333 0.0382  -0.0220 -0.0193 916  SER A CB  
6762  O OG  . SER A 918  ? 0.5655 0.5023 0.6444 0.0394  -0.0190 -0.0190 916  SER A OG  
6763  N N   . GLU A 919  ? 0.4204 0.3628 0.4866 0.0400  -0.0152 -0.0246 917  GLU A N   
6764  C CA  . GLU A 919  ? 0.4128 0.3606 0.4749 0.0428  -0.0134 -0.0296 917  GLU A CA  
6765  C C   . GLU A 919  ? 0.4513 0.3985 0.5107 0.0423  -0.0137 -0.0315 917  GLU A C   
6766  O O   . GLU A 919  ? 0.4152 0.3664 0.4726 0.0450  -0.0132 -0.0366 917  GLU A O   
6767  C CB  . GLU A 919  ? 0.4331 0.3864 0.4883 0.0427  -0.0094 -0.0274 917  GLU A CB  
6768  C CG  . GLU A 919  ? 0.5873 0.5432 0.6448 0.0443  -0.0087 -0.0271 917  GLU A CG  
6769  C CD  . GLU A 919  ? 0.6590 0.6118 0.7175 0.0413  -0.0087 -0.0210 917  GLU A CD  
6770  O OE1 . GLU A 919  ? 0.5523 0.5006 0.6113 0.0383  -0.0099 -0.0174 917  GLU A OE1 
6771  O OE2 . GLU A 919  ? 0.7476 0.7030 0.8066 0.0421  -0.0075 -0.0199 917  GLU A OE2 
6772  N N   . THR A 920  ? 0.3691 0.3120 0.4282 0.0389  -0.0146 -0.0277 918  THR A N   
6773  C CA  . THR A 920  ? 0.3440 0.2865 0.4009 0.0383  -0.0150 -0.0295 918  THR A CA  
6774  C C   . THR A 920  ? 0.3213 0.2612 0.3847 0.0403  -0.0186 -0.0349 918  THR A C   
6775  O O   . THR A 920  ? 0.3187 0.2593 0.3804 0.0408  -0.0190 -0.0380 918  THR A O   
6776  C CB  . THR A 920  ? 0.3427 0.2818 0.3977 0.0341  -0.0149 -0.0238 918  THR A CB  
6777  O OG1 . THR A 920  ? 0.3626 0.2964 0.4243 0.0324  -0.0177 -0.0210 918  THR A OG1 
6778  C CG2 . THR A 920  ? 0.3050 0.2469 0.3534 0.0323  -0.0114 -0.0192 918  THR A CG2 
6779  N N   . GLY A 921  ? 0.3538 0.2909 0.4249 0.0416  -0.0213 -0.0363 919  GLY A N   
6780  C CA  . GLY A 921  ? 0.3624 0.2965 0.4408 0.0434  -0.0251 -0.0415 919  GLY A CA  
6781  C C   . GLY A 921  ? 0.3301 0.2690 0.4070 0.0474  -0.0250 -0.0491 919  GLY A C   
6782  O O   . GLY A 921  ? 0.3995 0.3364 0.4807 0.0484  -0.0278 -0.0535 919  GLY A O   
6783  N N   . VAL A 922  ? 0.3657 0.3112 0.4368 0.0496  -0.0218 -0.0506 920  VAL A N   
6784  C CA  . VAL A 922  ? 0.3124 0.2637 0.3816 0.0534  -0.0214 -0.0577 920  VAL A CA  
6785  C C   . VAL A 922  ? 0.3419 0.2954 0.4047 0.0525  -0.0201 -0.0581 920  VAL A C   
6786  O O   . VAL A 922  ? 0.3204 0.2787 0.3816 0.0555  -0.0202 -0.0639 920  VAL A O   
6787  C CB  . VAL A 922  ? 0.3094 0.2679 0.3747 0.0562  -0.0184 -0.0590 920  VAL A CB  
6788  C CG1 . VAL A 922  ? 0.3484 0.3058 0.4209 0.0582  -0.0202 -0.0607 920  VAL A CG1 
6789  C CG2 . VAL A 922  ? 0.3337 0.2943 0.3917 0.0535  -0.0145 -0.0524 920  VAL A CG2 
6790  N N   . GLY A 923  ? 0.3032 0.2540 0.3624 0.0486  -0.0189 -0.0521 921  GLY A N   
6791  C CA  . GLY A 923  ? 0.3087 0.2609 0.3624 0.0475  -0.0179 -0.0523 921  GLY A CA  
6792  C C   . GLY A 923  ? 0.3357 0.2815 0.3925 0.0442  -0.0202 -0.0496 921  GLY A C   
6793  O O   . GLY A 923  ? 0.3350 0.2753 0.3992 0.0432  -0.0232 -0.0488 921  GLY A O   
6794  N N   . THR A 924  ? 0.2943 0.2410 0.3459 0.0425  -0.0190 -0.0480 922  THR A N   
6795  C CA  . THR A 924  ? 0.2889 0.2304 0.3431 0.0393  -0.0210 -0.0457 922  THR A CA  
6796  C C   . THR A 924  ? 0.2956 0.2365 0.3445 0.0357  -0.0184 -0.0386 922  THR A C   
6797  O O   . THR A 924  ? 0.2875 0.2314 0.3298 0.0351  -0.0162 -0.0378 922  THR A O   
6798  C CB  . THR A 924  ? 0.3019 0.2447 0.3555 0.0405  -0.0224 -0.0506 922  THR A CB  
6799  O OG1 . THR A 924  ? 0.2699 0.2189 0.3152 0.0417  -0.0192 -0.0513 922  THR A OG1 
6800  C CG2 . THR A 924  ? 0.3183 0.2614 0.3782 0.0441  -0.0254 -0.0579 922  THR A CG2 
6801  N N   . PHE A 925  ? 0.2780 0.2151 0.3299 0.0333  -0.0188 -0.0337 923  PHE A N   
6802  C CA  . PHE A 925  ? 0.2540 0.1909 0.3013 0.0300  -0.0165 -0.0273 923  PHE A CA  
6803  C C   . PHE A 925  ? 0.3060 0.2381 0.3572 0.0266  -0.0185 -0.0233 923  PHE A C   
6804  O O   . PHE A 925  ? 0.3140 0.2421 0.3726 0.0263  -0.0215 -0.0235 923  PHE A O   
6805  C CB  . PHE A 925  ? 0.2614 0.1994 0.3080 0.0300  -0.0147 -0.0242 923  PHE A CB  
6806  C CG  . PHE A 925  ? 0.2853 0.2287 0.3272 0.0328  -0.0121 -0.0266 923  PHE A CG  
6807  C CD1 . PHE A 925  ? 0.2759 0.2212 0.3208 0.0363  -0.0131 -0.0316 923  PHE A CD1 
6808  C CD2 . PHE A 925  ? 0.2763 0.2232 0.3113 0.0318  -0.0088 -0.0237 923  PHE A CD2 
6809  C CE1 . PHE A 925  ? 0.2966 0.2478 0.3374 0.0388  -0.0105 -0.0335 923  PHE A CE1 
6810  C CE2 . PHE A 925  ? 0.2517 0.2039 0.2828 0.0341  -0.0064 -0.0253 923  PHE A CE2 
6811  C CZ  . PHE A 925  ? 0.2442 0.1987 0.2780 0.0376  -0.0072 -0.0301 923  PHE A CZ  
6812  N N   . VAL A 926  ? 0.2979 0.2307 0.3442 0.0240  -0.0167 -0.0195 924  VAL A N   
6813  C CA  . VAL A 926  ? 0.2883 0.2179 0.3369 0.0204  -0.0177 -0.0147 924  VAL A CA  
6814  C C   . VAL A 926  ? 0.2701 0.2013 0.3142 0.0184  -0.0151 -0.0094 924  VAL A C   
6815  O O   . VAL A 926  ? 0.2769 0.2115 0.3144 0.0188  -0.0122 -0.0093 924  VAL A O   
6816  C CB  . VAL A 926  ? 0.2935 0.2229 0.3408 0.0190  -0.0182 -0.0152 924  VAL A CB  
6817  C CG1 . VAL A 926  ? 0.3018 0.2289 0.3511 0.0152  -0.0190 -0.0098 924  VAL A CG1 
6818  C CG2 . VAL A 926  ? 0.3230 0.2508 0.3754 0.0209  -0.0212 -0.0207 924  VAL A CG2 
6819  N N   . PRO A 927  ? 0.2800 0.2091 0.3276 0.0164  -0.0159 -0.0051 925  PRO A N   
6820  C CA  . PRO A 927  ? 0.2913 0.2223 0.3345 0.0147  -0.0135 -0.0004 925  PRO A CA  
6821  C C   . PRO A 927  ? 0.2711 0.2033 0.3099 0.0123  -0.0122 0.0020  925  PRO A C   
6822  O O   . PRO A 927  ? 0.2800 0.2105 0.3212 0.0108  -0.0138 0.0024  925  PRO A O   
6823  C CB  . PRO A 927  ? 0.3213 0.2497 0.3701 0.0131  -0.0154 0.0034  925  PRO A CB  
6824  C CG  . PRO A 927  ? 0.3625 0.2873 0.4182 0.0128  -0.0188 0.0023  925  PRO A CG  
6825  C CD  . PRO A 927  ? 0.3165 0.2416 0.3723 0.0157  -0.0193 -0.0040 925  PRO A CD  
6826  N N   . PRO A 928  ? 0.2611 0.1963 0.2938 0.0119  -0.0093 0.0035  926  PRO A N   
6827  C CA  . PRO A 928  ? 0.2392 0.1757 0.2682 0.0095  -0.0082 0.0063  926  PRO A CA  
6828  C C   . PRO A 928  ? 0.2358 0.1706 0.2685 0.0067  -0.0098 0.0105  926  PRO A C   
6829  O O   . PRO A 928  ? 0.2484 0.1825 0.2843 0.0061  -0.0106 0.0131  926  PRO A O   
6830  C CB  . PRO A 928  ? 0.2548 0.1941 0.2784 0.0097  -0.0053 0.0077  926  PRO A CB  
6831  C CG  . PRO A 928  ? 0.2998 0.2402 0.3226 0.0126  -0.0046 0.0041  926  PRO A CG  
6832  C CD  . PRO A 928  ? 0.2819 0.2196 0.3109 0.0139  -0.0071 0.0023  926  PRO A CD  
6833  N N   . THR A 929  ? 0.2384 0.1733 0.2710 0.0050  -0.0103 0.0113  927  THR A N   
6834  C CA  . THR A 929  ? 0.2409 0.1745 0.2782 0.0024  -0.0122 0.0149  927  THR A CA  
6835  C C   . THR A 929  ? 0.2501 0.1864 0.2836 0.0001  -0.0109 0.0175  927  THR A C   
6836  O O   . THR A 929  ? 0.2486 0.1861 0.2781 0.0006  -0.0096 0.0152  927  THR A O   
6837  C CB  . THR A 929  ? 0.2594 0.1898 0.3025 0.0028  -0.0151 0.0125  927  THR A CB  
6838  O OG1 . THR A 929  ? 0.2817 0.2098 0.3286 0.0051  -0.0165 0.0097  927  THR A OG1 
6839  C CG2 . THR A 929  ? 0.3008 0.2300 0.3493 -0.0002 -0.0172 0.0167  927  THR A CG2 
6840  N N   . ILE A 930  ? 0.2456 0.1830 0.2805 -0.0024 -0.0111 0.0222  928  ILE A N   
6841  C CA  . ILE A 930  ? 0.2420 0.1824 0.2742 -0.0046 -0.0102 0.0248  928  ILE A CA  
6842  C C   . ILE A 930  ? 0.2568 0.1965 0.2948 -0.0070 -0.0125 0.0281  928  ILE A C   
6843  O O   . ILE A 930  ? 0.2783 0.2169 0.3208 -0.0079 -0.0140 0.0311  928  ILE A O   
6844  C CB  . ILE A 930  ? 0.2340 0.1780 0.2622 -0.0055 -0.0082 0.0276  928  ILE A CB  
6845  C CG1 . ILE A 930  ? 0.2510 0.1957 0.2741 -0.0033 -0.0060 0.0247  928  ILE A CG1 
6846  C CG2 . ILE A 930  ? 0.2723 0.2199 0.2984 -0.0078 -0.0074 0.0302  928  ILE A CG2 
6847  C CD1 . ILE A 930  ? 0.2965 0.2441 0.3165 -0.0039 -0.0044 0.0271  928  ILE A CD1 
6848  N N   . ILE A 931  ? 0.2433 0.1836 0.2814 -0.0081 -0.0128 0.0276  929  ILE A N   
6849  C CA  . ILE A 931  ? 0.2616 0.2014 0.3055 -0.0105 -0.0150 0.0308  929  ILE A CA  
6850  C C   . ILE A 931  ? 0.2817 0.2262 0.3227 -0.0128 -0.0136 0.0337  929  ILE A C   
6851  O O   . ILE A 931  ? 0.2650 0.2110 0.3014 -0.0122 -0.0121 0.0313  929  ILE A O   
6852  C CB  . ILE A 931  ? 0.2845 0.2209 0.3327 -0.0098 -0.0171 0.0273  929  ILE A CB  
6853  C CG1 . ILE A 931  ? 0.2769 0.2092 0.3280 -0.0071 -0.0185 0.0236  929  ILE A CG1 
6854  C CG2 . ILE A 931  ? 0.3035 0.2395 0.3582 -0.0125 -0.0195 0.0309  929  ILE A CG2 
6855  C CD1 . ILE A 931  ? 0.2775 0.2067 0.3327 -0.0061 -0.0208 0.0193  929  ILE A CD1 
6856  N N   . GLU A 932  ? 0.2729 0.2199 0.3165 -0.0152 -0.0142 0.0389  930  GLU A N   
6857  C CA  . GLU A 932  ? 0.2680 0.2203 0.3089 -0.0173 -0.0129 0.0418  930  GLU A CA  
6858  C C   . GLU A 932  ? 0.2679 0.2202 0.3135 -0.0193 -0.0146 0.0432  930  GLU A C   
6859  O O   . GLU A 932  ? 0.2993 0.2498 0.3516 -0.0208 -0.0170 0.0463  930  GLU A O   
6860  C CB  . GLU A 932  ? 0.2764 0.2326 0.3170 -0.0189 -0.0125 0.0468  930  GLU A CB  
6861  C CG  . GLU A 932  ? 0.2732 0.2302 0.3087 -0.0170 -0.0105 0.0452  930  GLU A CG  
6862  C CD  . GLU A 932  ? 0.3184 0.2784 0.3543 -0.0182 -0.0106 0.0496  930  GLU A CD  
6863  O OE1 . GLU A 932  ? 0.3736 0.3388 0.4093 -0.0203 -0.0103 0.0535  930  GLU A OE1 
6864  O OE2 . GLU A 932  ? 0.3323 0.2901 0.3688 -0.0168 -0.0108 0.0492  930  GLU A OE2 
6865  N N   . LEU A 933  ? 0.2714 0.2255 0.3138 -0.0192 -0.0135 0.0410  931  LEU A N   
6866  C CA  . LEU A 933  ? 0.3010 0.2554 0.3476 -0.0211 -0.0150 0.0420  931  LEU A CA  
6867  C C   . LEU A 933  ? 0.3328 0.2937 0.3782 -0.0236 -0.0139 0.0462  931  LEU A C   
6868  O O   . LEU A 933  ? 0.3404 0.3056 0.3802 -0.0233 -0.0116 0.0466  931  LEU A O   
6869  C CB  . LEU A 933  ? 0.3067 0.2591 0.3514 -0.0194 -0.0148 0.0366  931  LEU A CB  
6870  C CG  . LEU A 933  ? 0.3641 0.3108 0.4103 -0.0168 -0.0161 0.0320  931  LEU A CG  
6871  C CD1 . LEU A 933  ? 0.3927 0.3384 0.4365 -0.0151 -0.0159 0.0269  931  LEU A CD1 
6872  C CD2 . LEU A 933  ? 0.4019 0.3448 0.4565 -0.0178 -0.0193 0.0336  931  LEU A CD2 
6873  N N   . GLU A 934  ? 0.3283 0.2902 0.3793 -0.0260 -0.0156 0.0493  932  GLU A N   
6874  C CA  . GLU A 934  ? 0.4900 0.4587 0.5402 -0.0284 -0.0146 0.0531  932  GLU A CA  
6875  C C   . GLU A 934  ? 0.4824 0.4532 0.5283 -0.0277 -0.0131 0.0495  932  GLU A C   
6876  O O   . GLU A 934  ? 0.4945 0.4710 0.5356 -0.0279 -0.0109 0.0500  932  GLU A O   
6877  C CB  . GLU A 934  ? 0.5239 0.4932 0.5822 -0.0315 -0.0170 0.0582  932  GLU A CB  
6878  C CG  . GLU A 934  ? 0.6247 0.5919 0.6881 -0.0323 -0.0188 0.0624  932  GLU A CG  
6879  C CD  . GLU A 934  ? 0.7324 0.7053 0.7921 -0.0329 -0.0171 0.0663  932  GLU A CD  
6880  O OE1 . GLU A 934  ? 0.7832 0.7626 0.8439 -0.0354 -0.0168 0.0714  932  GLU A OE1 
6881  O OE2 . GLU A 934  ? 0.6919 0.6630 0.7477 -0.0308 -0.0161 0.0641  932  GLU A OE2 
6882  N N   . LYS A 935  ? 0.4033 0.3698 0.4510 -0.0267 -0.0143 0.0455  933  LYS A N   
6883  C CA  . LYS A 935  ? 0.5255 0.4937 0.5699 -0.0260 -0.0132 0.0422  933  LYS A CA  
6884  C C   . LYS A 935  ? 0.4297 0.3925 0.4723 -0.0231 -0.0135 0.0362  933  LYS A C   
6885  O O   . LYS A 935  ? 0.4371 0.3947 0.4832 -0.0222 -0.0153 0.0349  933  LYS A O   
6886  C CB  . LYS A 935  ? 0.5490 0.5192 0.5987 -0.0285 -0.0147 0.0444  933  LYS A CB  
6887  N N   . LEU A 936  ? 0.4788 0.4431 0.5159 -0.0216 -0.0118 0.0328  934  LEU A N   
6888  C CA  . LEU A 936  ? 0.5246 0.4847 0.5595 -0.0189 -0.0120 0.0274  934  LEU A CA  
6889  C C   . LEU A 936  ? 0.4964 0.4529 0.5372 -0.0191 -0.0147 0.0256  934  LEU A C   
6890  O O   . LEU A 936  ? 0.4794 0.4316 0.5205 -0.0169 -0.0157 0.0217  934  LEU A O   
6891  C CB  . LEU A 936  ? 0.5332 0.4963 0.5622 -0.0176 -0.0100 0.0247  934  LEU A CB  
6892  C CG  . LEU A 936  ? 0.6371 0.5973 0.6622 -0.0146 -0.0095 0.0197  934  LEU A CG  
6893  C CD1 . LEU A 936  ? 0.5243 0.4807 0.5492 -0.0129 -0.0097 0.0183  934  LEU A CD1 
6894  C CD2 . LEU A 936  ? 0.5517 0.5153 0.5707 -0.0136 -0.0070 0.0186  934  LEU A CD2 
6895  N N   . SER A 937  ? 0.5421 0.5003 0.5879 -0.0216 -0.0161 0.0283  935  SER A N   
6896  C CA  . SER A 937  ? 0.4922 0.4470 0.5444 -0.0221 -0.0190 0.0266  935  SER A CA  
6897  C C   . SER A 937  ? 0.4689 0.4189 0.5273 -0.0222 -0.0215 0.0274  935  SER A C   
6898  O O   . SER A 937  ? 0.5018 0.4482 0.5659 -0.0220 -0.0242 0.0251  935  SER A O   
6899  C CB  . SER A 937  ? 0.5806 0.5390 0.6370 -0.0250 -0.0198 0.0297  935  SER A CB  
6900  O OG  . SER A 937  ? 0.5856 0.5472 0.6446 -0.0277 -0.0197 0.0358  935  SER A OG  
6901  N N   . ASP A 938  ? 0.4803 0.4302 0.5382 -0.0224 -0.0208 0.0304  936  ASP A N   
6902  C CA  . ASP A 938  ? 0.4570 0.4021 0.5203 -0.0219 -0.0231 0.0305  936  ASP A CA  
6903  C C   . ASP A 938  ? 0.4168 0.3577 0.4783 -0.0185 -0.0235 0.0243  936  ASP A C   
6904  O O   . ASP A 938  ? 0.4498 0.3863 0.5168 -0.0177 -0.0259 0.0228  936  ASP A O   
6905  C CB  . ASP A 938  ? 0.5000 0.4465 0.5622 -0.0225 -0.0220 0.0348  936  ASP A CB  
6906  C CG  . ASP A 938  ? 0.5601 0.5116 0.6242 -0.0259 -0.0216 0.0413  936  ASP A CG  
6907  O OD1 . ASP A 938  ? 0.5850 0.5379 0.6535 -0.0281 -0.0229 0.0431  936  ASP A OD1 
6908  O OD2 . ASP A 938  ? 0.5997 0.5542 0.6608 -0.0263 -0.0200 0.0446  936  ASP A OD2 
6909  N N   . LEU A 939  ? 0.4748 0.4172 0.5290 -0.0163 -0.0212 0.0206  937  LEU A N   
6910  C CA  . LEU A 939  ? 0.4872 0.4268 0.5389 -0.0130 -0.0213 0.0149  937  LEU A CA  
6911  C C   . LEU A 939  ? 0.5631 0.5025 0.6153 -0.0122 -0.0224 0.0108  937  LEU A C   
6912  O O   . LEU A 939  ? 0.6571 0.5998 0.7055 -0.0128 -0.0209 0.0110  937  LEU A O   
6913  C CB  . LEU A 939  ? 0.4484 0.3900 0.4919 -0.0111 -0.0181 0.0140  937  LEU A CB  
6914  C CG  . LEU A 939  ? 0.5457 0.4852 0.5861 -0.0077 -0.0177 0.0092  937  LEU A CG  
6915  C CD1 . LEU A 939  ? 0.4767 0.4124 0.5226 -0.0069 -0.0198 0.0085  937  LEU A CD1 
6916  C CD2 . LEU A 939  ? 0.4954 0.4373 0.5285 -0.0065 -0.0146 0.0095  937  LEU A CD2 
6917  N N   . GLN A 940  ? 0.5291 0.4649 0.5860 -0.0109 -0.0250 0.0070  938  GLN A N   
6918  C CA  . GLN A 940  ? 0.5791 0.5147 0.6381 -0.0106 -0.0267 0.0033  938  GLN A CA  
6919  C C   . GLN A 940  ? 0.6293 0.5636 0.6857 -0.0070 -0.0271 -0.0032 938  GLN A C   
6920  O O   . GLN A 940  ? 0.7695 0.7035 0.8282 -0.0064 -0.0290 -0.0069 938  GLN A O   
6921  C CB  . GLN A 940  ? 0.6547 0.5877 0.7235 -0.0129 -0.0302 0.0049  938  GLN A CB  
6922  N N   . ARG A 941  ? 0.6183 0.5524 0.6702 -0.0045 -0.0255 -0.0048 939  ARG A N   
6923  C CA  . ARG A 941  ? 0.5783 0.5122 0.6276 -0.0010 -0.0257 -0.0108 939  ARG A CA  
6924  C C   . ARG A 941  ? 0.3866 0.3217 0.4293 0.0010  -0.0228 -0.0107 939  ARG A C   
6925  O O   . ARG A 941  ? 0.5471 0.4815 0.5901 0.0000  -0.0219 -0.0071 939  ARG A O   
6926  C CB  . ARG A 941  ? 0.5993 0.5295 0.6560 0.0001  -0.0292 -0.0144 939  ARG A CB  
6927  N N   . GLU A 942  ? 0.4417 0.3790 0.4788 0.0037  -0.0215 -0.0145 940  GLU A N   
6928  C CA  . GLU A 942  ? 0.4549 0.3936 0.4862 0.0057  -0.0189 -0.0147 940  GLU A CA  
6929  C C   . GLU A 942  ? 0.4366 0.3727 0.4716 0.0072  -0.0202 -0.0163 940  GLU A C   
6930  O O   . GLU A 942  ? 0.4382 0.3730 0.4771 0.0089  -0.0225 -0.0207 940  GLU A O   
6931  C CB  . GLU A 942  ? 0.4268 0.3686 0.4521 0.0084  -0.0176 -0.0184 940  GLU A CB  
6932  C CG  . GLU A 942  ? 0.4357 0.3794 0.4554 0.0105  -0.0150 -0.0185 940  GLU A CG  
6933  C CD  . GLU A 942  ? 0.5158 0.4628 0.5305 0.0134  -0.0142 -0.0224 940  GLU A CD  
6934  O OE1 . GLU A 942  ? 0.5098 0.4570 0.5267 0.0152  -0.0162 -0.0270 940  GLU A OE1 
6935  O OE2 . GLU A 942  ? 0.4239 0.3735 0.4328 0.0139  -0.0116 -0.0209 940  GLU A OE2 
6936  N N   . VAL A 943  ? 0.3461 0.2818 0.3803 0.0065  -0.0187 -0.0128 941  VAL A N   
6937  C CA  . VAL A 943  ? 0.3119 0.2455 0.3492 0.0079  -0.0196 -0.0137 941  VAL A CA  
6938  C C   . VAL A 943  ? 0.3477 0.2840 0.3787 0.0104  -0.0169 -0.0150 941  VAL A C   
6939  O O   . VAL A 943  ? 0.3159 0.2536 0.3426 0.0095  -0.0144 -0.0115 941  VAL A O   
6940  C CB  . VAL A 943  ? 0.3114 0.2428 0.3530 0.0054  -0.0201 -0.0087 941  VAL A CB  
6941  C CG1 . VAL A 943  ? 0.3318 0.2611 0.3767 0.0070  -0.0211 -0.0097 941  VAL A CG1 
6942  C CG2 . VAL A 943  ? 0.3721 0.3015 0.4202 0.0027  -0.0227 -0.0068 941  VAL A CG2 
6943  N N   . PHE A 944  ? 0.3119 0.2490 0.3423 0.0135  -0.0174 -0.0201 942  PHE A N   
6944  C CA  . PHE A 944  ? 0.2891 0.2298 0.3130 0.0159  -0.0148 -0.0216 942  PHE A CA  
6945  C C   . PHE A 944  ? 0.3046 0.2449 0.3294 0.0171  -0.0142 -0.0211 942  PHE A C   
6946  O O   . PHE A 944  ? 0.3010 0.2423 0.3265 0.0199  -0.0147 -0.0251 942  PHE A O   
6947  C CB  . PHE A 944  ? 0.2822 0.2254 0.3047 0.0187  -0.0156 -0.0271 942  PHE A CB  
6948  C CG  . PHE A 944  ? 0.3233 0.2710 0.3384 0.0205  -0.0128 -0.0275 942  PHE A CG  
6949  C CD1 . PHE A 944  ? 0.3317 0.2811 0.3422 0.0190  -0.0110 -0.0247 942  PHE A CD1 
6950  C CD2 . PHE A 944  ? 0.3140 0.2647 0.3271 0.0236  -0.0120 -0.0306 942  PHE A CD2 
6951  C CE1 . PHE A 944  ? 0.3591 0.3125 0.3634 0.0206  -0.0086 -0.0247 942  PHE A CE1 
6952  C CE2 . PHE A 944  ? 0.3495 0.3047 0.3560 0.0250  -0.0094 -0.0304 942  PHE A CE2 
6953  C CZ  . PHE A 944  ? 0.3568 0.3132 0.3592 0.0235  -0.0078 -0.0273 942  PHE A CZ  
6954  N N   . GLY A 945  ? 0.2778 0.2169 0.3024 0.0150  -0.0130 -0.0163 943  GLY A N   
6955  C CA  . GLY A 945  ? 0.2743 0.2127 0.3003 0.0157  -0.0126 -0.0152 943  GLY A CA  
6956  C C   . GLY A 945  ? 0.2854 0.2241 0.3088 0.0135  -0.0105 -0.0099 943  GLY A C   
6957  O O   . GLY A 945  ? 0.2629 0.2027 0.2831 0.0117  -0.0093 -0.0075 943  GLY A O   
6958  N N   . PRO A 946  ? 0.2654 0.2034 0.2903 0.0136  -0.0102 -0.0083 944  PRO A N   
6959  C CA  . PRO A 946  ? 0.2506 0.1894 0.2727 0.0119  -0.0082 -0.0037 944  PRO A CA  
6960  C C   . PRO A 946  ? 0.2404 0.1772 0.2661 0.0088  -0.0095 0.0004  944  PRO A C   
6961  O O   . PRO A 946  ? 0.2445 0.1801 0.2732 0.0080  -0.0101 0.0030  944  PRO A O   
6962  C CB  . PRO A 946  ? 0.2467 0.1860 0.2693 0.0137  -0.0076 -0.0043 944  PRO A CB  
6963  C CG  . PRO A 946  ? 0.2855 0.2225 0.3139 0.0154  -0.0102 -0.0078 944  PRO A CG  
6964  C CD  . PRO A 946  ? 0.2526 0.1895 0.2815 0.0159  -0.0116 -0.0112 944  PRO A CD  
6965  N N   . VAL A 947  ? 0.2408 0.1777 0.2665 0.0071  -0.0100 0.0012  945  VAL A N   
6966  C CA  . VAL A 947  ? 0.2368 0.1724 0.2665 0.0042  -0.0115 0.0050  945  VAL A CA  
6967  C C   . VAL A 947  ? 0.2590 0.1971 0.2845 0.0022  -0.0098 0.0075  945  VAL A C   
6968  O O   . VAL A 947  ? 0.2780 0.2170 0.3020 0.0022  -0.0098 0.0057  945  VAL A O   
6969  C CB  . VAL A 947  ? 0.2860 0.2188 0.3219 0.0039  -0.0146 0.0033  945  VAL A CB  
6970  C CG1 . VAL A 947  ? 0.2908 0.2227 0.3313 0.0007  -0.0160 0.0080  945  VAL A CG1 
6971  C CG2 . VAL A 947  ? 0.2657 0.1961 0.3059 0.0063  -0.0163 -0.0001 945  VAL A CG2 
6972  N N   . LEU A 948  ? 0.2488 0.1884 0.2728 0.0007  -0.0086 0.0113  946  LEU A N   
6973  C CA  . LEU A 948  ? 0.2288 0.1713 0.2492 -0.0011 -0.0070 0.0137  946  LEU A CA  
6974  C C   . LEU A 948  ? 0.2582 0.2010 0.2827 -0.0039 -0.0085 0.0174  946  LEU A C   
6975  O O   . LEU A 948  ? 0.2884 0.2302 0.3166 -0.0050 -0.0096 0.0202  946  LEU A O   
6976  C CB  . LEU A 948  ? 0.2461 0.1907 0.2625 -0.0010 -0.0048 0.0154  946  LEU A CB  
6977  C CG  . LEU A 948  ? 0.2306 0.1785 0.2437 -0.0027 -0.0034 0.0176  946  LEU A CG  
6978  C CD1 . LEU A 948  ? 0.2568 0.2056 0.2665 -0.0018 -0.0025 0.0149  946  LEU A CD1 
6979  C CD2 . LEU A 948  ? 0.2744 0.2240 0.2846 -0.0027 -0.0017 0.0192  946  LEU A CD2 
6980  N N   . HIS A 949  ? 0.2465 0.1908 0.2704 -0.0052 -0.0085 0.0177  947  HIS A N   
6981  C CA  . HIS A 949  ? 0.2197 0.1653 0.2468 -0.0080 -0.0095 0.0215  947  HIS A CA  
6982  C C   . HIS A 949  ? 0.2425 0.1925 0.2652 -0.0093 -0.0074 0.0239  947  HIS A C   
6983  O O   . HIS A 949  ? 0.2664 0.2179 0.2841 -0.0081 -0.0056 0.0218  947  HIS A O   
6984  C CB  . HIS A 949  ? 0.2210 0.1658 0.2512 -0.0088 -0.0111 0.0202  947  HIS A CB  
6985  C CG  . HIS A 949  ? 0.2636 0.2043 0.2981 -0.0072 -0.0133 0.0169  947  HIS A CG  
6986  N ND1 . HIS A 949  ? 0.2757 0.2153 0.3074 -0.0045 -0.0129 0.0121  947  HIS A ND1 
6987  C CD2 . HIS A 949  ? 0.3008 0.2385 0.3423 -0.0079 -0.0161 0.0177  947  HIS A CD2 
6988  C CE1 . HIS A 949  ? 0.2753 0.2117 0.3120 -0.0034 -0.0153 0.0096  947  HIS A CE1 
6989  N NE2 . HIS A 949  ? 0.2964 0.2312 0.3393 -0.0054 -0.0173 0.0128  947  HIS A NE2 
6990  N N   . VAL A 950  ? 0.2405 0.1928 0.2651 -0.0115 -0.0076 0.0283  948  VAL A N   
6991  C CA  . VAL A 950  ? 0.2376 0.1946 0.2583 -0.0125 -0.0058 0.0304  948  VAL A CA  
6992  C C   . VAL A 950  ? 0.2752 0.2355 0.2983 -0.0151 -0.0064 0.0337  948  VAL A C   
6993  O O   . VAL A 950  ? 0.2773 0.2372 0.3056 -0.0168 -0.0082 0.0369  948  VAL A O   
6994  C CB  . VAL A 950  ? 0.2661 0.2242 0.2859 -0.0125 -0.0051 0.0325  948  VAL A CB  
6995  C CG1 . VAL A 950  ? 0.2915 0.2551 0.3076 -0.0136 -0.0034 0.0344  948  VAL A CG1 
6996  C CG2 . VAL A 950  ? 0.2742 0.2295 0.2917 -0.0099 -0.0043 0.0294  948  VAL A CG2 
6997  N N   . ILE A 951  ? 0.2643 0.2283 0.2841 -0.0155 -0.0051 0.0330  949  ILE A N   
6998  C CA  . ILE A 951  ? 0.3042 0.2727 0.3256 -0.0179 -0.0053 0.0363  949  ILE A CA  
6999  C C   . ILE A 951  ? 0.3202 0.2944 0.3371 -0.0182 -0.0032 0.0371  949  ILE A C   
7000  O O   . ILE A 951  ? 0.2691 0.2430 0.2816 -0.0164 -0.0018 0.0344  949  ILE A O   
7001  C CB  . ILE A 951  ? 0.2604 0.2287 0.2832 -0.0183 -0.0059 0.0346  949  ILE A CB  
7002  C CG1 . ILE A 951  ? 0.3396 0.3081 0.3573 -0.0164 -0.0044 0.0304  949  ILE A CG1 
7003  C CG2 . ILE A 951  ? 0.2993 0.2623 0.3274 -0.0182 -0.0083 0.0336  949  ILE A CG2 
7004  C CD1 . ILE A 951  ? 0.4082 0.3766 0.4272 -0.0167 -0.0051 0.0288  949  ILE A CD1 
7005  N N   . ARG A 952  ? 0.2868 0.2663 0.3051 -0.0204 -0.0033 0.0409  950  ARG A N   
7006  C CA  . ARG A 952  ? 0.2856 0.2714 0.3001 -0.0207 -0.0016 0.0417  950  ARG A CA  
7007  C C   . ARG A 952  ? 0.2548 0.2452 0.2689 -0.0217 -0.0011 0.0416  950  ARG A C   
7008  O O   . ARG A 952  ? 0.2992 0.2893 0.3171 -0.0231 -0.0023 0.0431  950  ARG A O   
7009  C CB  . ARG A 952  ? 0.2889 0.2786 0.3049 -0.0223 -0.0019 0.0464  950  ARG A CB  
7010  C CG  . ARG A 952  ? 0.3208 0.3059 0.3384 -0.0216 -0.0028 0.0471  950  ARG A CG  
7011  C CD  . ARG A 952  ? 0.3889 0.3768 0.4103 -0.0238 -0.0040 0.0526  950  ARG A CD  
7012  N NE  . ARG A 952  ? 0.3921 0.3869 0.4105 -0.0242 -0.0028 0.0546  950  ARG A NE  
7013  C CZ  . ARG A 952  ? 0.3672 0.3620 0.3844 -0.0235 -0.0026 0.0552  950  ARG A CZ  
7014  N NH1 . ARG A 952  ? 0.3610 0.3495 0.3799 -0.0224 -0.0035 0.0544  950  ARG A NH1 
7015  N NH2 . ARG A 952  ? 0.3459 0.3475 0.3602 -0.0239 -0.0016 0.0566  950  ARG A NH2 
7016  N N   . TYR A 953  ? 0.2458 0.2405 0.2556 -0.0209 0.0006  0.0397  951  TYR A N   
7017  C CA  . TYR A 953  ? 0.2582 0.2577 0.2676 -0.0216 0.0012  0.0393  951  TYR A CA  
7018  C C   . TYR A 953  ? 0.2635 0.2706 0.2698 -0.0217 0.0027  0.0397  951  TYR A C   
7019  O O   . TYR A 953  ? 0.2756 0.2828 0.2788 -0.0203 0.0035  0.0381  951  TYR A O   
7020  C CB  . TYR A 953  ? 0.2659 0.2619 0.2736 -0.0198 0.0015  0.0348  951  TYR A CB  
7021  C CG  . TYR A 953  ? 0.2509 0.2463 0.2539 -0.0175 0.0029  0.0312  951  TYR A CG  
7022  C CD1 . TYR A 953  ? 0.2222 0.2123 0.2238 -0.0159 0.0030  0.0296  951  TYR A CD1 
7023  C CD2 . TYR A 953  ? 0.2692 0.2695 0.2697 -0.0170 0.0041  0.0294  951  TYR A CD2 
7024  C CE1 . TYR A 953  ? 0.2324 0.2220 0.2305 -0.0139 0.0042  0.0266  951  TYR A CE1 
7025  C CE2 . TYR A 953  ? 0.2285 0.2280 0.2256 -0.0149 0.0052  0.0262  951  TYR A CE2 
7026  C CZ  . TYR A 953  ? 0.2581 0.2522 0.2541 -0.0135 0.0052  0.0250  951  TYR A CZ  
7027  O OH  . TYR A 953  ? 0.2548 0.2481 0.2480 -0.0117 0.0061  0.0222  951  TYR A OH  
7028  N N   . ARG A 954  ? 0.2826 0.2963 0.2900 -0.0233 0.0029  0.0416  952  ARG A N   
7029  C CA  . ARG A 954  ? 0.3210 0.3428 0.3255 -0.0231 0.0043  0.0412  952  ARG A CA  
7030  C C   . ARG A 954  ? 0.2534 0.2749 0.2548 -0.0211 0.0053  0.0362  952  ARG A C   
7031  O O   . ARG A 954  ? 0.2773 0.2952 0.2795 -0.0206 0.0050  0.0343  952  ARG A O   
7032  C CB  . ARG A 954  ? 0.3279 0.3576 0.3349 -0.0256 0.0042  0.0452  952  ARG A CB  
7033  C CG  . ARG A 954  ? 0.4257 0.4557 0.4367 -0.0279 0.0030  0.0508  952  ARG A CG  
7034  C CD  . ARG A 954  ? 0.5094 0.5405 0.5187 -0.0275 0.0032  0.0522  952  ARG A CD  
7035  N NE  . ARG A 954  ? 0.6113 0.6507 0.6168 -0.0269 0.0047  0.0510  952  ARG A NE  
7036  C CZ  . ARG A 954  ? 0.7206 0.7694 0.7265 -0.0285 0.0050  0.0548  952  ARG A CZ  
7037  N NH1 . ARG A 954  ? 0.7600 0.8109 0.7700 -0.0311 0.0040  0.0606  952  ARG A NH1 
7038  N NH2 . ARG A 954  ? 0.7686 0.8252 0.7710 -0.0275 0.0063  0.0527  952  ARG A NH2 
7039  N N   . ARG A 955  ? 0.3208 0.3459 0.3189 -0.0197 0.0064  0.0339  953  ARG A N   
7040  C CA  . ARG A 955  ? 0.3080 0.3322 0.3037 -0.0175 0.0072  0.0291  953  ARG A CA  
7041  C C   . ARG A 955  ? 0.2646 0.2915 0.2612 -0.0179 0.0073  0.0282  953  ARG A C   
7042  O O   . ARG A 955  ? 0.3006 0.3232 0.2967 -0.0165 0.0072  0.0252  953  ARG A O   
7043  C CB  . ARG A 955  ? 0.3883 0.4176 0.3813 -0.0163 0.0081  0.0270  953  ARG A CB  
7044  C CG  . ARG A 955  ? 0.5684 0.5978 0.5596 -0.0142 0.0087  0.0222  953  ARG A CG  
7045  C CD  . ARG A 955  ? 0.5240 0.5444 0.5149 -0.0128 0.0084  0.0201  953  ARG A CD  
7046  N NE  . ARG A 955  ? 0.6881 0.7074 0.6777 -0.0107 0.0087  0.0160  953  ARG A NE  
7047  C CZ  . ARG A 955  ? 0.5847 0.6034 0.5749 -0.0103 0.0086  0.0145  953  ARG A CZ  
7048  N NH1 . ARG A 955  ? 0.4281 0.4480 0.4200 -0.0118 0.0083  0.0165  953  ARG A NH1 
7049  N NH2 . ARG A 955  ? 0.5327 0.5494 0.5219 -0.0083 0.0088  0.0110  953  ARG A NH2 
7050  N N   . ASP A 956  ? 0.3097 0.3443 0.3078 -0.0197 0.0074  0.0310  954  ASP A N   
7051  C CA  . ASP A 956  ? 0.2957 0.3337 0.2950 -0.0201 0.0076  0.0303  954  ASP A CA  
7052  C C   . ASP A 956  ? 0.2692 0.3009 0.2712 -0.0208 0.0064  0.0309  954  ASP A C   
7053  O O   . ASP A 956  ? 0.3304 0.3629 0.3331 -0.0207 0.0064  0.0294  954  ASP A O   
7054  C CB  . ASP A 956  ? 0.2995 0.3475 0.3001 -0.0221 0.0080  0.0336  954  ASP A CB  
7055  C CG  . ASP A 956  ? 0.3725 0.4284 0.3704 -0.0211 0.0092  0.0320  954  ASP A CG  
7056  O OD1 . ASP A 956  ? 0.4130 0.4668 0.4083 -0.0187 0.0096  0.0276  954  ASP A OD1 
7057  O OD2 . ASP A 956  ? 0.4426 0.5072 0.4411 -0.0226 0.0095  0.0353  954  ASP A OD2 
7058  N N   . ASP A 957  ? 0.2764 0.3020 0.2801 -0.0216 0.0054  0.0330  955  ASP A N   
7059  C CA  . ASP A 957  ? 0.2906 0.3102 0.2972 -0.0221 0.0040  0.0333  955  ASP A CA  
7060  C C   . ASP A 957  ? 0.2876 0.2993 0.2923 -0.0198 0.0038  0.0293  955  ASP A C   
7061  O O   . ASP A 957  ? 0.3138 0.3199 0.3207 -0.0199 0.0026  0.0292  955  ASP A O   
7062  C CB  . ASP A 957  ? 0.3278 0.3455 0.3383 -0.0242 0.0027  0.0377  955  ASP A CB  
7063  C CG  . ASP A 957  ? 0.4426 0.4681 0.4559 -0.0269 0.0026  0.0423  955  ASP A CG  
7064  O OD1 . ASP A 957  ? 0.4325 0.4635 0.4461 -0.0275 0.0032  0.0421  955  ASP A OD1 
7065  O OD2 . ASP A 957  ? 0.3910 0.4172 0.4064 -0.0284 0.0020  0.0464  955  ASP A OD2 
7066  N N   . LEU A 958  ? 0.2538 0.2653 0.2548 -0.0176 0.0049  0.0261  956  LEU A N   
7067  C CA  . LEU A 958  ? 0.2374 0.2421 0.2366 -0.0155 0.0048  0.0229  956  LEU A CA  
7068  C C   . LEU A 958  ? 0.2704 0.2726 0.2705 -0.0150 0.0041  0.0211  956  LEU A C   
7069  O O   . LEU A 958  ? 0.2657 0.2620 0.2663 -0.0143 0.0033  0.0200  956  LEU A O   
7070  C CB  . LEU A 958  ? 0.2531 0.2587 0.2489 -0.0135 0.0060  0.0201  956  LEU A CB  
7071  C CG  . LEU A 958  ? 0.2733 0.2728 0.2672 -0.0112 0.0060  0.0170  956  LEU A CG  
7072  C CD1 . LEU A 958  ? 0.2849 0.2785 0.2791 -0.0110 0.0054  0.0178  956  LEU A CD1 
7073  C CD2 . LEU A 958  ? 0.2820 0.2831 0.2734 -0.0096 0.0070  0.0146  956  LEU A CD2 
7074  N N   . ASP A 959  ? 0.2483 0.2555 0.2488 -0.0154 0.0044  0.0205  957  ASP A N   
7075  C CA  . ASP A 959  ? 0.2719 0.2772 0.2732 -0.0149 0.0037  0.0186  957  ASP A CA  
7076  C C   . ASP A 959  ? 0.2741 0.2766 0.2792 -0.0165 0.0022  0.0205  957  ASP A C   
7077  O O   . ASP A 959  ? 0.2828 0.2805 0.2883 -0.0156 0.0012  0.0186  957  ASP A O   
7078  C CB  . ASP A 959  ? 0.2908 0.3023 0.2922 -0.0150 0.0043  0.0177  957  ASP A CB  
7079  C CG  . ASP A 959  ? 0.3091 0.3185 0.3105 -0.0138 0.0037  0.0150  957  ASP A CG  
7080  O OD1 . ASP A 959  ? 0.3016 0.3065 0.3007 -0.0117 0.0038  0.0125  957  ASP A OD1 
7081  O OD2 . ASP A 959  ? 0.3800 0.3924 0.3838 -0.0150 0.0032  0.0157  957  ASP A OD2 
7082  N N   . ARG A 960  ? 0.2544 0.2600 0.2625 -0.0189 0.0018  0.0242  958  ARG A N   
7083  C CA  . ARG A 960  ? 0.2687 0.2712 0.2812 -0.0206 0.0000  0.0262  958  ARG A CA  
7084  C C   . ARG A 960  ? 0.2869 0.2821 0.2994 -0.0195 -0.0008 0.0253  958  ARG A C   
7085  O O   . ARG A 960  ? 0.3065 0.2974 0.3215 -0.0194 -0.0024 0.0242  958  ARG A O   
7086  C CB  . ARG A 960  ? 0.2779 0.2854 0.2939 -0.0235 -0.0003 0.0311  958  ARG A CB  
7087  C CG  . ARG A 960  ? 0.3147 0.3192 0.3364 -0.0255 -0.0024 0.0336  958  ARG A CG  
7088  C CD  . ARG A 960  ? 0.6277 0.6318 0.6517 -0.0270 -0.0029 0.0377  958  ARG A CD  
7089  N NE  . ARG A 960  ? 0.5771 0.5766 0.5979 -0.0250 -0.0024 0.0359  958  ARG A NE  
7090  C CZ  . ARG A 960  ? 0.5831 0.5825 0.6042 -0.0256 -0.0024 0.0387  958  ARG A CZ  
7091  N NH1 . ARG A 960  ? 0.7198 0.7236 0.7443 -0.0281 -0.0029 0.0436  958  ARG A NH1 
7092  N NH2 . ARG A 960  ? 0.5896 0.5849 0.6078 -0.0236 -0.0020 0.0366  958  ARG A NH2 
7093  N N   . LEU A 961  ? 0.2607 0.2549 0.2704 -0.0185 0.0001  0.0253  959  LEU A N   
7094  C CA  . LEU A 961  ? 0.2663 0.2542 0.2758 -0.0173 -0.0005 0.0243  959  LEU A CA  
7095  C C   . LEU A 961  ? 0.2959 0.2796 0.3033 -0.0150 -0.0007 0.0203  959  LEU A C   
7096  O O   . LEU A 961  ? 0.2724 0.2513 0.2815 -0.0144 -0.0019 0.0191  959  LEU A O   
7097  C CB  . LEU A 961  ? 0.2777 0.2660 0.2845 -0.0166 0.0006  0.0250  959  LEU A CB  
7098  C CG  . LEU A 961  ? 0.2838 0.2660 0.2897 -0.0149 0.0003  0.0235  959  LEU A CG  
7099  C CD1 . LEU A 961  ? 0.3761 0.3549 0.3865 -0.0161 -0.0015 0.0254  959  LEU A CD1 
7100  C CD2 . LEU A 961  ? 0.3242 0.3073 0.3272 -0.0142 0.0016  0.0239  959  LEU A CD2 
7101  N N   . VAL A 962  ? 0.2736 0.2591 0.2776 -0.0135 0.0005  0.0180  960  VAL A N   
7102  C CA  . VAL A 962  ? 0.2386 0.2208 0.2407 -0.0114 0.0003  0.0146  960  VAL A CA  
7103  C C   . VAL A 962  ? 0.3240 0.3053 0.3291 -0.0121 -0.0013 0.0139  960  VAL A C   
7104  O O   . VAL A 962  ? 0.2989 0.2762 0.3041 -0.0108 -0.0022 0.0117  960  VAL A O   
7105  C CB  . VAL A 962  ? 0.2610 0.2459 0.2597 -0.0100 0.0017  0.0128  960  VAL A CB  
7106  C CG1 . VAL A 962  ? 0.3167 0.2988 0.3137 -0.0080 0.0014  0.0098  960  VAL A CG1 
7107  C CG2 . VAL A 962  ? 0.2717 0.2568 0.2679 -0.0092 0.0030  0.0130  960  VAL A CG2 
7108  N N   . ASP A 963  ? 0.3048 0.2901 0.3128 -0.0141 -0.0017 0.0157  961  ASP A N   
7109  C CA  . ASP A 963  ? 0.3215 0.3059 0.3334 -0.0151 -0.0035 0.0154  961  ASP A CA  
7110  C C   . ASP A 963  ? 0.3175 0.2971 0.3327 -0.0155 -0.0052 0.0158  961  ASP A C   
7111  O O   . ASP A 963  ? 0.3459 0.3223 0.3626 -0.0147 -0.0067 0.0134  961  ASP A O   
7112  C CB  . ASP A 963  ? 0.3515 0.3413 0.3667 -0.0177 -0.0036 0.0182  961  ASP A CB  
7113  C CG  . ASP A 963  ? 0.4083 0.4030 0.4212 -0.0172 -0.0024 0.0170  961  ASP A CG  
7114  O OD1 . ASP A 963  ? 0.4737 0.4670 0.4834 -0.0149 -0.0020 0.0138  961  ASP A OD1 
7115  O OD2 . ASP A 963  ? 0.4595 0.4599 0.4742 -0.0190 -0.0020 0.0194  961  ASP A OD2 
7116  N N   . ASP A 964  ? 0.3072 0.2866 0.3239 -0.0167 -0.0051 0.0188  962  ASP A N   
7117  C CA  . ASP A 964  ? 0.3639 0.3388 0.3844 -0.0172 -0.0069 0.0194  962  ASP A CA  
7118  C C   . ASP A 964  ? 0.3856 0.3556 0.4036 -0.0144 -0.0070 0.0158  962  ASP A C   
7119  O O   . ASP A 964  ? 0.3593 0.3255 0.3803 -0.0140 -0.0088 0.0142  962  ASP A O   
7120  C CB  . ASP A 964  ? 0.3640 0.3400 0.3859 -0.0187 -0.0066 0.0234  962  ASP A CB  
7121  C CG  . ASP A 964  ? 0.3938 0.3748 0.4193 -0.0217 -0.0068 0.0276  962  ASP A CG  
7122  O OD1 . ASP A 964  ? 0.4624 0.4453 0.4904 -0.0227 -0.0076 0.0275  962  ASP A OD1 
7123  O OD2 . ASP A 964  ? 0.5381 0.5217 0.5640 -0.0230 -0.0063 0.0312  962  ASP A OD2 
7124  N N   . VAL A 965  ? 0.3171 0.2873 0.3299 -0.0126 -0.0051 0.0145  963  VAL A N   
7125  C CA  . VAL A 965  ? 0.3070 0.2735 0.3172 -0.0100 -0.0051 0.0114  963  VAL A CA  
7126  C C   . VAL A 965  ? 0.3503 0.3160 0.3604 -0.0087 -0.0060 0.0081  963  VAL A C   
7127  O O   . VAL A 965  ? 0.3403 0.3029 0.3516 -0.0075 -0.0073 0.0057  963  VAL A O   
7128  C CB  . VAL A 965  ? 0.2952 0.2625 0.3003 -0.0085 -0.0029 0.0110  963  VAL A CB  
7129  C CG1 . VAL A 965  ? 0.2855 0.2498 0.2880 -0.0058 -0.0028 0.0081  963  VAL A CG1 
7130  C CG2 . VAL A 965  ? 0.3013 0.2692 0.3067 -0.0095 -0.0022 0.0140  963  VAL A CG2 
7131  N N   . ASN A 966  ? 0.2798 0.2487 0.2884 -0.0090 -0.0055 0.0077  964  ASN A N   
7132  C CA  . ASN A 966  ? 0.3068 0.2756 0.3152 -0.0078 -0.0064 0.0047  964  ASN A CA  
7133  C C   . ASN A 966  ? 0.3451 0.3123 0.3588 -0.0090 -0.0088 0.0042  964  ASN A C   
7134  O O   . ASN A 966  ? 0.3396 0.3053 0.3537 -0.0076 -0.0101 0.0010  964  ASN A O   
7135  C CB  . ASN A 966  ? 0.3243 0.2971 0.3309 -0.0081 -0.0055 0.0048  964  ASN A CB  
7136  C CG  . ASN A 966  ? 0.3117 0.2855 0.3133 -0.0063 -0.0035 0.0043  964  ASN A CG  
7137  O OD1 . ASN A 966  ? 0.2897 0.2611 0.2886 -0.0045 -0.0029 0.0032  964  ASN A OD1 
7138  N ND2 . ASN A 966  ? 0.3161 0.2938 0.3168 -0.0068 -0.0025 0.0050  964  ASN A ND2 
7139  N N   . ALA A 967  ? 0.3307 0.2984 0.3490 -0.0116 -0.0096 0.0073  965  ALA A N   
7140  C CA  . ALA A 967  ? 0.3637 0.3303 0.3881 -0.0131 -0.0121 0.0074  965  ALA A CA  
7141  C C   . ALA A 967  ? 0.3871 0.3489 0.4142 -0.0120 -0.0140 0.0050  965  ALA A C   
7142  O O   . ALA A 967  ? 0.4022 0.3626 0.4344 -0.0127 -0.0164 0.0038  965  ALA A O   
7143  C CB  . ALA A 967  ? 0.4152 0.3839 0.4440 -0.0163 -0.0124 0.0121  965  ALA A CB  
7144  N N   . THR A 968  ? 0.3138 0.2733 0.3379 -0.0101 -0.0132 0.0041  966  THR A N   
7145  C CA  . THR A 968  ? 0.3033 0.2588 0.3298 -0.0086 -0.0150 0.0012  966  THR A CA  
7146  C C   . THR A 968  ? 0.3332 0.2885 0.3584 -0.0064 -0.0159 -0.0035 966  THR A C   
7147  O O   . THR A 968  ? 0.3625 0.3151 0.3908 -0.0053 -0.0180 -0.0065 966  THR A O   
7148  C CB  . THR A 968  ? 0.3185 0.2723 0.3418 -0.0069 -0.0137 0.0010  966  THR A CB  
7149  O OG1 . THR A 968  ? 0.3289 0.2843 0.3458 -0.0047 -0.0116 -0.0008 966  THR A OG1 
7150  C CG2 . THR A 968  ? 0.3426 0.2971 0.3665 -0.0088 -0.0126 0.0056  966  THR A CG2 
7151  N N   . GLY A 969  ? 0.3337 0.2919 0.3545 -0.0057 -0.0146 -0.0044 967  GLY A N   
7152  C CA  . GLY A 969  ? 0.3582 0.3168 0.3767 -0.0034 -0.0153 -0.0086 967  GLY A CA  
7153  C C   . GLY A 969  ? 0.3140 0.2724 0.3271 -0.0004 -0.0139 -0.0108 967  GLY A C   
7154  O O   . GLY A 969  ? 0.2820 0.2418 0.2922 0.0016  -0.0139 -0.0137 967  GLY A O   
7155  N N   . TYR A 970  ? 0.2727 0.2297 0.2846 -0.0001 -0.0126 -0.0092 968  TYR A N   
7156  C CA  . TYR A 970  ? 0.2647 0.2219 0.2716 0.0025  -0.0110 -0.0105 968  TYR A CA  
7157  C C   . TYR A 970  ? 0.2650 0.2247 0.2669 0.0026  -0.0086 -0.0085 968  TYR A C   
7158  O O   . TYR A 970  ? 0.3183 0.2795 0.3206 0.0008  -0.0080 -0.0062 968  TYR A O   
7159  C CB  . TYR A 970  ? 0.2576 0.2124 0.2656 0.0027  -0.0108 -0.0096 968  TYR A CB  
7160  C CG  . TYR A 970  ? 0.3107 0.2629 0.3235 0.0033  -0.0133 -0.0123 968  TYR A CG  
7161  C CD1 . TYR A 970  ? 0.3408 0.2932 0.3521 0.0062  -0.0138 -0.0165 968  TYR A CD1 
7162  C CD2 . TYR A 970  ? 0.4138 0.3637 0.4327 0.0011  -0.0151 -0.0107 968  TYR A CD2 
7163  C CE1 . TYR A 970  ? 0.4185 0.3686 0.4344 0.0070  -0.0162 -0.0195 968  TYR A CE1 
7164  C CE2 . TYR A 970  ? 0.3592 0.3065 0.3832 0.0018  -0.0176 -0.0133 968  TYR A CE2 
7165  C CZ  . TYR A 970  ? 0.4288 0.3761 0.4513 0.0048  -0.0182 -0.0180 968  TYR A CZ  
7166  O OH  . TYR A 970  ? 0.4917 0.4365 0.5195 0.0056  -0.0209 -0.0211 968  TYR A OH  
7167  N N   . GLY A 971  ? 0.2414 0.2018 0.2389 0.0049  -0.0072 -0.0095 969  GLY A N   
7168  C CA  . GLY A 971  ? 0.2672 0.2296 0.2605 0.0052  -0.0051 -0.0078 969  GLY A CA  
7169  C C   . GLY A 971  ? 0.2354 0.1982 0.2247 0.0075  -0.0038 -0.0084 969  GLY A C   
7170  O O   . GLY A 971  ? 0.2549 0.2197 0.2409 0.0089  -0.0031 -0.0091 969  GLY A O   
7171  N N   . LEU A 972  ? 0.2180 0.1791 0.2076 0.0079  -0.0033 -0.0080 970  LEU A N   
7172  C CA  . LEU A 972  ? 0.2125 0.1744 0.1987 0.0101  -0.0021 -0.0085 970  LEU A CA  
7173  C C   . LEU A 972  ? 0.2599 0.2220 0.2442 0.0096  0.0000  -0.0055 970  LEU A C   
7174  O O   . LEU A 972  ? 0.2459 0.2096 0.2277 0.0099  0.0010  -0.0046 970  LEU A O   
7175  C CB  . LEU A 972  ? 0.2444 0.2050 0.2324 0.0112  -0.0029 -0.0106 970  LEU A CB  
7176  C CG  . LEU A 972  ? 0.2498 0.2121 0.2344 0.0138  -0.0018 -0.0116 970  LEU A CG  
7177  C CD1 . LEU A 972  ? 0.2594 0.2249 0.2405 0.0155  -0.0016 -0.0128 970  LEU A CD1 
7178  C CD2 . LEU A 972  ? 0.2644 0.2259 0.2512 0.0151  -0.0030 -0.0144 970  LEU A CD2 
7179  N N   . THR A 973  ? 0.2264 0.1868 0.2120 0.0088  0.0005  -0.0041 971  THR A N   
7180  C CA  . THR A 973  ? 0.2264 0.1870 0.2105 0.0083  0.0022  -0.0015 971  THR A CA  
7181  C C   . THR A 973  ? 0.2212 0.1813 0.2075 0.0058  0.0020  0.0006  971  THR A C   
7182  O O   . THR A 973  ? 0.2238 0.1829 0.2132 0.0045  0.0007  0.0005  971  THR A O   
7183  C CB  . THR A 973  ? 0.2432 0.2031 0.2267 0.0093  0.0031  -0.0011 971  THR A CB  
7184  O OG1 . THR A 973  ? 0.2412 0.1991 0.2278 0.0087  0.0020  -0.0015 971  THR A OG1 
7185  C CG2 . THR A 973  ? 0.2339 0.1955 0.2149 0.0118  0.0035  -0.0029 971  THR A CG2 
7186  N N   . PHE A 974  ? 0.2173 0.1783 0.2021 0.0053  0.0034  0.0024  972  PHE A N   
7187  C CA  . PHE A 974  ? 0.2158 0.1774 0.2022 0.0032  0.0035  0.0043  972  PHE A CA  
7188  C C   . PHE A 974  ? 0.2113 0.1735 0.1962 0.0032  0.0049  0.0058  972  PHE A C   
7189  O O   . PHE A 974  ? 0.2294 0.1922 0.2122 0.0044  0.0058  0.0055  972  PHE A O   
7190  C CB  . PHE A 974  ? 0.2261 0.1896 0.2128 0.0023  0.0030  0.0041  972  PHE A CB  
7191  C CG  . PHE A 974  ? 0.2067 0.1720 0.1945 0.0004  0.0034  0.0060  972  PHE A CG  
7192  C CD1 . PHE A 974  ? 0.2197 0.1851 0.2104 -0.0014 0.0025  0.0073  972  PHE A CD1 
7193  C CD2 . PHE A 974  ? 0.2173 0.1844 0.2034 0.0006  0.0045  0.0065  972  PHE A CD2 
7194  C CE1 . PHE A 974  ? 0.2573 0.2253 0.2489 -0.0031 0.0029  0.0093  972  PHE A CE1 
7195  C CE2 . PHE A 974  ? 0.2227 0.1922 0.2098 -0.0010 0.0049  0.0079  972  PHE A CE2 
7196  C CZ  . PHE A 974  ? 0.2357 0.2059 0.2251 -0.0028 0.0042  0.0093  972  PHE A CZ  
7197  N N   . GLY A 975  ? 0.2086 0.1707 0.1949 0.0019  0.0051  0.0075  973  GLY A N   
7198  C CA  . GLY A 975  ? 0.2185 0.1814 0.2038 0.0018  0.0063  0.0087  973  GLY A CA  
7199  C C   . GLY A 975  ? 0.1776 0.1428 0.1636 0.0001  0.0064  0.0098  973  GLY A C   
7200  O O   . GLY A 975  ? 0.2063 0.1724 0.1941 -0.0014 0.0056  0.0107  973  GLY A O   
7201  N N   . LEU A 976  ? 0.2105 0.1770 0.1953 0.0004  0.0073  0.0099  974  LEU A N   
7202  C CA  . LEU A 976  ? 0.2029 0.1724 0.1882 -0.0009 0.0074  0.0107  974  LEU A CA  
7203  C C   . LEU A 976  ? 0.1964 0.1661 0.1813 -0.0006 0.0082  0.0111  974  LEU A C   
7204  O O   . LEU A 976  ? 0.2320 0.2006 0.2159 0.0007  0.0087  0.0103  974  LEU A O   
7205  C CB  . LEU A 976  ? 0.2194 0.1912 0.2044 -0.0007 0.0074  0.0095  974  LEU A CB  
7206  C CG  . LEU A 976  ? 0.2217 0.1974 0.2070 -0.0016 0.0077  0.0097  974  LEU A CG  
7207  C CD1 . LEU A 976  ? 0.2418 0.2199 0.2285 -0.0035 0.0073  0.0113  974  LEU A CD1 
7208  C CD2 . LEU A 976  ? 0.2456 0.2229 0.2305 -0.0009 0.0077  0.0081  974  LEU A CD2 
7209  N N   . HIS A 977  ? 0.2090 0.1804 0.1948 -0.0018 0.0082  0.0124  975  HIS A N   
7210  C CA  . HIS A 977  ? 0.2170 0.1893 0.2026 -0.0017 0.0087  0.0126  975  HIS A CA  
7211  C C   . HIS A 977  ? 0.2125 0.1891 0.1983 -0.0026 0.0087  0.0124  975  HIS A C   
7212  O O   . HIS A 977  ? 0.2256 0.2049 0.2121 -0.0040 0.0084  0.0137  975  HIS A O   
7213  C CB  . HIS A 977  ? 0.2143 0.1854 0.2007 -0.0022 0.0086  0.0141  975  HIS A CB  
7214  C CG  . HIS A 977  ? 0.2611 0.2289 0.2471 -0.0009 0.0090  0.0139  975  HIS A CG  
7215  N ND1 . HIS A 977  ? 0.3125 0.2800 0.2985 -0.0004 0.0096  0.0139  975  HIS A ND1 
7216  C CD2 . HIS A 977  ? 0.3578 0.3229 0.3436 0.0001  0.0089  0.0134  975  HIS A CD2 
7217  C CE1 . HIS A 977  ? 0.3222 0.2872 0.3080 0.0007  0.0099  0.0139  975  HIS A CE1 
7218  N NE2 . HIS A 977  ? 0.3214 0.2850 0.3069 0.0011  0.0095  0.0135  975  HIS A NE2 
7219  N N   . THR A 978  ? 0.2132 0.1908 0.1986 -0.0017 0.0090  0.0107  976  THR A N   
7220  C CA  . THR A 978  ? 0.2197 0.2019 0.2053 -0.0021 0.0090  0.0097  976  THR A CA  
7221  C C   . THR A 978  ? 0.2391 0.2208 0.2250 -0.0008 0.0092  0.0078  976  THR A C   
7222  O O   . THR A 978  ? 0.2405 0.2188 0.2263 0.0003  0.0093  0.0074  976  THR A O   
7223  C CB  . THR A 978  ? 0.2362 0.2212 0.2219 -0.0025 0.0088  0.0093  976  THR A CB  
7224  O OG1 . THR A 978  ? 0.2465 0.2367 0.2325 -0.0028 0.0089  0.0081  976  THR A OG1 
7225  C CG2 . THR A 978  ? 0.2322 0.2147 0.2176 -0.0013 0.0088  0.0078  976  THR A CG2 
7226  N N   . ARG A 979  ? 0.2551 0.2405 0.2415 -0.0009 0.0091  0.0067  977  ARG A N   
7227  C CA  . ARG A 979  ? 0.2378 0.2232 0.2252 0.0004  0.0089  0.0044  977  ARG A CA  
7228  C C   . ARG A 979  ? 0.2644 0.2528 0.2523 0.0009  0.0087  0.0023  977  ARG A C   
7229  O O   . ARG A 979  ? 0.2963 0.2845 0.2855 0.0021  0.0083  0.0002  977  ARG A O   
7230  C CB  . ARG A 979  ? 0.2579 0.2456 0.2461 0.0002  0.0088  0.0037  977  ARG A CB  
7231  C CG  . ARG A 979  ? 0.3254 0.3099 0.3136 -0.0001 0.0090  0.0055  977  ARG A CG  
7232  C CD  . ARG A 979  ? 0.4343 0.4215 0.4232 -0.0004 0.0088  0.0050  977  ARG A CD  
7233  N NE  . ARG A 979  ? 0.5250 0.5091 0.5143 -0.0005 0.0089  0.0065  977  ARG A NE  
7234  C CZ  . ARG A 979  ? 0.5756 0.5611 0.5657 -0.0006 0.0086  0.0062  977  ARG A CZ  
7235  N NH1 . ARG A 979  ? 0.4350 0.4253 0.4256 -0.0007 0.0082  0.0043  977  ARG A NH1 
7236  N NH2 . ARG A 979  ? 0.5586 0.5410 0.5491 -0.0007 0.0088  0.0076  977  ARG A NH2 
7237  N N   . LEU A 980  ? 0.2195 0.2105 0.2066 0.0001  0.0088  0.0028  978  LEU A N   
7238  C CA  . LEU A 980  ? 0.2042 0.1999 0.1919 0.0004  0.0086  0.0009  978  LEU A CA  
7239  C C   . LEU A 980  ? 0.2357 0.2293 0.2234 0.0012  0.0084  0.0003  978  LEU A C   
7240  O O   . LEU A 980  ? 0.2369 0.2289 0.2239 0.0005  0.0085  0.0020  978  LEU A O   
7241  C CB  . LEU A 980  ? 0.2246 0.2258 0.2118 -0.0011 0.0088  0.0020  978  LEU A CB  
7242  C CG  . LEU A 980  ? 0.2455 0.2492 0.2323 -0.0020 0.0089  0.0032  978  LEU A CG  
7243  C CD1 . LEU A 980  ? 0.2477 0.2571 0.2342 -0.0036 0.0091  0.0051  978  LEU A CD1 
7244  C CD2 . LEU A 980  ? 0.2514 0.2577 0.2390 -0.0009 0.0087  0.0003  978  LEU A CD2 
7245  N N   . ASP A 981  ? 0.2359 0.2296 0.2249 0.0026  0.0080  -0.0020 979  ASP A N   
7246  C CA  . ASP A 981  ? 0.2250 0.2167 0.2142 0.0035  0.0077  -0.0025 979  ASP A CA  
7247  C C   . ASP A 981  ? 0.2026 0.1978 0.1913 0.0027  0.0078  -0.0022 979  ASP A C   
7248  O O   . ASP A 981  ? 0.2276 0.2205 0.2158 0.0028  0.0077  -0.0015 979  ASP A O   
7249  C CB  . ASP A 981  ? 0.2227 0.2146 0.2140 0.0052  0.0071  -0.0052 979  ASP A CB  
7250  C CG  . ASP A 981  ? 0.2730 0.2606 0.2655 0.0060  0.0068  -0.0050 979  ASP A CG  
7251  O OD1 . ASP A 981  ? 0.3062 0.2902 0.2976 0.0056  0.0072  -0.0027 979  ASP A OD1 
7252  O OD2 . ASP A 981  ? 0.3042 0.2921 0.2992 0.0072  0.0061  -0.0072 979  ASP A OD2 
7253  N N   . GLU A 982  ? 0.2048 0.2058 0.1937 0.0019  0.0080  -0.0028 980  GLU A N   
7254  C CA  . GLU A 982  ? 0.2127 0.2173 0.2015 0.0009  0.0081  -0.0022 980  GLU A CA  
7255  C C   . GLU A 982  ? 0.2247 0.2266 0.2126 -0.0006 0.0082  0.0008  980  GLU A C   
7256  O O   . GLU A 982  ? 0.2354 0.2368 0.2235 -0.0009 0.0079  0.0013  980  GLU A O   
7257  C CB  . GLU A 982  ? 0.2389 0.2511 0.2281 0.0002  0.0084  -0.0028 980  GLU A CB  
7258  C CG  . GLU A 982  ? 0.2591 0.2753 0.2485 -0.0010 0.0085  -0.0017 980  GLU A CG  
7259  C CD  . GLU A 982  ? 0.3491 0.3731 0.3386 -0.0023 0.0090  -0.0010 980  GLU A CD  
7260  O OE1 . GLU A 982  ? 0.3668 0.3917 0.3556 -0.0033 0.0093  0.0007  980  GLU A OE1 
7261  O OE2 . GLU A 982  ? 0.3193 0.3491 0.3096 -0.0023 0.0092  -0.0020 980  GLU A OE2 
7262  N N   . THR A 983  ? 0.2189 0.2188 0.2062 -0.0014 0.0084  0.0025  981  THR A N   
7263  C CA  . THR A 983  ? 0.2222 0.2195 0.2093 -0.0026 0.0083  0.0051  981  THR A CA  
7264  C C   . THR A 983  ? 0.2341 0.2254 0.2206 -0.0016 0.0080  0.0049  981  THR A C   
7265  O O   . THR A 983  ? 0.2308 0.2208 0.2176 -0.0022 0.0076  0.0058  981  THR A O   
7266  C CB  . THR A 983  ? 0.2538 0.2508 0.2406 -0.0036 0.0085  0.0069  981  THR A CB  
7267  O OG1 . THR A 983  ? 0.2662 0.2697 0.2534 -0.0047 0.0087  0.0074  981  THR A OG1 
7268  C CG2 . THR A 983  ? 0.2639 0.2575 0.2510 -0.0047 0.0081  0.0094  981  THR A CG2 
7269  N N   . ILE A 984  ? 0.2276 0.2160 0.2137 -0.0001 0.0081  0.0038  982  ILE A N   
7270  C CA  . ILE A 984  ? 0.2081 0.1919 0.1936 0.0010  0.0079  0.0038  982  ILE A CA  
7271  C C   . ILE A 984  ? 0.2119 0.1966 0.1976 0.0015  0.0074  0.0028  982  ILE A C   
7272  O O   . ILE A 984  ? 0.2331 0.2158 0.2183 0.0015  0.0071  0.0033  982  ILE A O   
7273  C CB  . ILE A 984  ? 0.2226 0.2039 0.2081 0.0024  0.0080  0.0031  982  ILE A CB  
7274  C CG1 . ILE A 984  ? 0.2484 0.2285 0.2338 0.0020  0.0084  0.0042  982  ILE A CG1 
7275  C CG2 . ILE A 984  ? 0.2411 0.2188 0.2259 0.0037  0.0079  0.0034  982  ILE A CG2 
7276  C CD1 . ILE A 984  ? 0.2678 0.2461 0.2539 0.0031  0.0085  0.0036  982  ILE A CD1 
7277  N N   . ALA A 985  ? 0.2222 0.2103 0.2087 0.0020  0.0073  0.0012  983  ALA A N   
7278  C CA  . ALA A 985  ? 0.2409 0.2301 0.2278 0.0026  0.0069  0.0001  983  ALA A CA  
7279  C C   . ALA A 985  ? 0.2551 0.2461 0.2423 0.0011  0.0066  0.0011  983  ALA A C   
7280  O O   . ALA A 985  ? 0.2639 0.2534 0.2509 0.0013  0.0061  0.0011  983  ALA A O   
7281  C CB  . ALA A 985  ? 0.2519 0.2449 0.2402 0.0034  0.0068  -0.0020 983  ALA A CB  
7282  N N   . HIS A 986  ? 0.2418 0.2364 0.2296 -0.0005 0.0069  0.0021  984  HIS A N   
7283  C CA  . HIS A 986  ? 0.2468 0.2434 0.2355 -0.0023 0.0066  0.0035  984  HIS A CA  
7284  C C   . HIS A 986  ? 0.2677 0.2596 0.2563 -0.0027 0.0061  0.0048  984  HIS A C   
7285  O O   . HIS A 986  ? 0.2577 0.2487 0.2468 -0.0028 0.0054  0.0046  984  HIS A O   
7286  C CB  . HIS A 986  ? 0.2488 0.2500 0.2382 -0.0039 0.0071  0.0049  984  HIS A CB  
7287  C CG  . HIS A 986  ? 0.2259 0.2290 0.2168 -0.0060 0.0067  0.0072  984  HIS A CG  
7288  N ND1 . HIS A 986  ? 0.3534 0.3604 0.3451 -0.0078 0.0070  0.0094  984  HIS A ND1 
7289  C CD2 . HIS A 986  ? 0.2825 0.2844 0.2747 -0.0067 0.0059  0.0078  984  HIS A CD2 
7290  C CE1 . HIS A 986  ? 0.3839 0.3917 0.3776 -0.0096 0.0064  0.0115  984  HIS A CE1 
7291  N NE2 . HIS A 986  ? 0.2705 0.2752 0.2647 -0.0090 0.0057  0.0104  984  HIS A NE2 
7292  N N   . VAL A 987  ? 0.2436 0.2326 0.2315 -0.0028 0.0063  0.0058  985  VAL A N   
7293  C CA  . VAL A 987  ? 0.2269 0.2120 0.2150 -0.0032 0.0058  0.0069  985  VAL A CA  
7294  C C   . VAL A 987  ? 0.2541 0.2358 0.2412 -0.0015 0.0054  0.0054  985  VAL A C   
7295  O O   . VAL A 987  ? 0.2598 0.2401 0.2476 -0.0018 0.0045  0.0053  985  VAL A O   
7296  C CB  . VAL A 987  ? 0.2056 0.1888 0.1934 -0.0035 0.0061  0.0082  985  VAL A CB  
7297  C CG1 . VAL A 987  ? 0.2148 0.1938 0.2030 -0.0034 0.0055  0.0087  985  VAL A CG1 
7298  C CG2 . VAL A 987  ? 0.2627 0.2498 0.2518 -0.0054 0.0063  0.0101  985  VAL A CG2 
7299  N N   . THR A 988  ? 0.2360 0.2166 0.2216 0.0001  0.0059  0.0044  986  THR A N   
7300  C CA  . THR A 988  ? 0.2457 0.2236 0.2302 0.0017  0.0055  0.0035  986  THR A CA  
7301  C C   . THR A 988  ? 0.3315 0.3111 0.3164 0.0020  0.0048  0.0023  986  THR A C   
7302  O O   . THR A 988  ? 0.3177 0.2957 0.3020 0.0028  0.0042  0.0017  986  THR A O   
7303  C CB  . THR A 988  ? 0.2773 0.2536 0.2605 0.0033  0.0061  0.0033  986  THR A CB  
7304  O OG1 . THR A 988  ? 0.2886 0.2672 0.2724 0.0037  0.0063  0.0024  986  THR A OG1 
7305  C CG2 . THR A 988  ? 0.2926 0.2671 0.2755 0.0031  0.0067  0.0044  986  THR A CG2 
7306  N N   . SER A 989  ? 0.2515 0.2347 0.2375 0.0013  0.0048  0.0020  987  SER A N   
7307  C CA  . SER A 989  ? 0.2991 0.2842 0.2858 0.0015  0.0041  0.0009  987  SER A CA  
7308  C C   . SER A 989  ? 0.3431 0.3286 0.3313 0.0000  0.0033  0.0014  987  SER A C   
7309  O O   . SER A 989  ? 0.4121 0.3979 0.4008 0.0004  0.0024  0.0004  987  SER A O   
7310  C CB  . SER A 989  ? 0.2872 0.2766 0.2749 0.0015  0.0044  0.0001  987  SER A CB  
7311  O OG  . SER A 989  ? 0.4236 0.4165 0.4126 -0.0003 0.0048  0.0010  987  SER A OG  
7312  N N   . ARG A 990  ? 0.2554 0.2410 0.2448 -0.0017 0.0034  0.0030  988  ARG A N   
7313  C CA  . ARG A 990  ? 0.2853 0.2714 0.2771 -0.0034 0.0024  0.0038  988  ARG A CA  
7314  C C   . ARG A 990  ? 0.2611 0.2430 0.2532 -0.0034 0.0016  0.0039  988  ARG A C   
7315  O O   . ARG A 990  ? 0.2946 0.2761 0.2888 -0.0041 0.0003  0.0036  988  ARG A O   
7316  C CB  . ARG A 990  ? 0.2925 0.2822 0.2862 -0.0056 0.0028  0.0059  988  ARG A CB  
7317  C CG  . ARG A 990  ? 0.4442 0.4390 0.4377 -0.0056 0.0036  0.0055  988  ARG A CG  
7318  C CD  . ARG A 990  ? 0.4632 0.4614 0.4585 -0.0062 0.0030  0.0050  988  ARG A CD  
7319  N NE  . ARG A 990  ? 0.4268 0.4292 0.4247 -0.0086 0.0029  0.0072  988  ARG A NE  
7320  C CZ  . ARG A 990  ? 0.3965 0.4024 0.3968 -0.0098 0.0024  0.0076  988  ARG A CZ  
7321  N NH1 . ARG A 990  ? 0.3908 0.3962 0.3912 -0.0088 0.0017  0.0056  988  ARG A NH1 
7322  N NH2 . ARG A 990  ? 0.3669 0.3773 0.3697 -0.0121 0.0025  0.0101  988  ARG A NH2 
7323  N N   . ILE A 991  ? 0.2505 0.2296 0.2410 -0.0024 0.0021  0.0041  989  ILE A N   
7324  C CA  . ILE A 991  ? 0.2374 0.2128 0.2281 -0.0020 0.0014  0.0037  989  ILE A CA  
7325  C C   . ILE A 991  ? 0.2747 0.2490 0.2644 -0.0003 0.0006  0.0016  989  ILE A C   
7326  O O   . ILE A 991  ? 0.2848 0.2601 0.2725 0.0010  0.0011  0.0006  989  ILE A O   
7327  C CB  . ILE A 991  ? 0.2358 0.2090 0.2250 -0.0013 0.0023  0.0044  989  ILE A CB  
7328  C CG1 . ILE A 991  ? 0.2938 0.2638 0.2840 -0.0012 0.0015  0.0043  989  ILE A CG1 
7329  C CG2 . ILE A 991  ? 0.3037 0.2763 0.2899 0.0008  0.0032  0.0034  989  ILE A CG2 
7330  C CD1 . ILE A 991  ? 0.3139 0.2839 0.3075 -0.0033 0.0006  0.0060  989  ILE A CD1 
7331  N N   . LYS A 992  ? 0.2539 0.2263 0.2451 -0.0003 -0.0006 0.0006  990  LYS A N   
7332  C CA  . LYS A 992  ? 0.2562 0.2278 0.2463 0.0013  -0.0016 -0.0017 990  LYS A CA  
7333  C C   . LYS A 992  ? 0.2395 0.2084 0.2288 0.0026  -0.0018 -0.0027 990  LYS A C   
7334  O O   . LYS A 992  ? 0.3167 0.2841 0.3084 0.0023  -0.0031 -0.0036 990  LYS A O   
7335  C CB  . LYS A 992  ? 0.2576 0.2303 0.2508 0.0002  -0.0032 -0.0026 990  LYS A CB  
7336  C CG  . LYS A 992  ? 0.3067 0.2828 0.3006 -0.0008 -0.0030 -0.0019 990  LYS A CG  
7337  C CD  . LYS A 992  ? 0.4877 0.4650 0.4856 -0.0026 -0.0045 -0.0021 990  LYS A CD  
7338  C CE  . LYS A 992  ? 0.5362 0.5108 0.5365 -0.0027 -0.0064 -0.0035 990  LYS A CE  
7339  N NZ  . LYS A 992  ? 0.6846 0.6604 0.6892 -0.0043 -0.0081 -0.0038 990  LYS A NZ  
7340  N N   . ALA A 993  ? 0.2768 0.2453 0.2630 0.0042  -0.0005 -0.0024 991  ALA A N   
7341  C CA  . ALA A 993  ? 0.2536 0.2203 0.2387 0.0056  -0.0004 -0.0032 991  ALA A CA  
7342  C C   . ALA A 993  ? 0.2588 0.2265 0.2404 0.0078  0.0006  -0.0035 991  ALA A C   
7343  O O   . ALA A 993  ? 0.2757 0.2446 0.2560 0.0079  0.0014  -0.0025 991  ALA A O   
7344  C CB  . ALA A 993  ? 0.2519 0.2169 0.2378 0.0048  0.0003  -0.0015 991  ALA A CB  
7345  N N   . GLY A 994  ? 0.2564 0.2238 0.2367 0.0095  0.0004  -0.0050 992  GLY A N   
7346  C CA  . GLY A 994  ? 0.2411 0.2100 0.2181 0.0115  0.0011  -0.0050 992  GLY A CA  
7347  C C   . GLY A 994  ? 0.2172 0.1858 0.1927 0.0119  0.0028  -0.0029 992  GLY A C   
7348  O O   . GLY A 994  ? 0.2241 0.1940 0.1976 0.0130  0.0036  -0.0019 992  GLY A O   
7349  N N   . ASN A 995  ? 0.2287 0.1954 0.2054 0.0110  0.0033  -0.0020 993  ASN A N   
7350  C CA  . ASN A 995  ? 0.2408 0.2072 0.2164 0.0114  0.0048  -0.0001 993  ASN A CA  
7351  C C   . ASN A 995  ? 0.2338 0.1988 0.2112 0.0095  0.0052  0.0014  993  ASN A C   
7352  O O   . ASN A 995  ? 0.2348 0.1985 0.2141 0.0085  0.0048  0.0014  993  ASN A O   
7353  C CB  . ASN A 995  ? 0.2442 0.2105 0.2192 0.0127  0.0051  -0.0008 993  ASN A CB  
7354  C CG  . ASN A 995  ? 0.2504 0.2192 0.2228 0.0149  0.0053  -0.0015 993  ASN A CG  
7355  O OD1 . ASN A 995  ? 0.2558 0.2258 0.2277 0.0158  0.0042  -0.0037 993  ASN A OD1 
7356  N ND2 . ASN A 995  ? 0.2445 0.2143 0.2153 0.0156  0.0066  0.0005  993  ASN A ND2 
7357  N N   . LEU A 996  ? 0.2257 0.1914 0.2029 0.0090  0.0060  0.0028  994  LEU A N   
7358  C CA  . LEU A 996  ? 0.2039 0.1692 0.1824 0.0074  0.0064  0.0040  994  LEU A CA  
7359  C C   . LEU A 996  ? 0.2091 0.1737 0.1872 0.0077  0.0075  0.0054  994  LEU A C   
7360  O O   . LEU A 996  ? 0.2128 0.1778 0.1897 0.0090  0.0081  0.0059  994  LEU A O   
7361  C CB  . LEU A 996  ? 0.2106 0.1774 0.1896 0.0067  0.0062  0.0041  994  LEU A CB  
7362  C CG  . LEU A 996  ? 0.2437 0.2117 0.2231 0.0066  0.0052  0.0027  994  LEU A CG  
7363  C CD1 . LEU A 996  ? 0.2765 0.2463 0.2565 0.0060  0.0052  0.0028  994  LEU A CD1 
7364  C CD2 . LEU A 996  ? 0.2571 0.2244 0.2384 0.0054  0.0042  0.0022  994  LEU A CD2 
7365  N N   . TYR A 997  ? 0.2080 0.1720 0.1874 0.0065  0.0077  0.0063  995  TYR A N   
7366  C CA  . TYR A 997  ? 0.2083 0.1717 0.1876 0.0066  0.0087  0.0075  995  TYR A CA  
7367  C C   . TYR A 997  ? 0.2081 0.1722 0.1887 0.0051  0.0088  0.0082  995  TYR A C   
7368  O O   . TYR A 997  ? 0.2182 0.1826 0.1999 0.0038  0.0083  0.0084  995  TYR A O   
7369  C CB  . TYR A 997  ? 0.2263 0.1885 0.2058 0.0070  0.0088  0.0076  995  TYR A CB  
7370  C CG  . TYR A 997  ? 0.2246 0.1870 0.2028 0.0087  0.0087  0.0066  995  TYR A CG  
7371  C CD1 . TYR A 997  ? 0.2380 0.2012 0.2148 0.0101  0.0096  0.0073  995  TYR A CD1 
7372  C CD2 . TYR A 997  ? 0.2248 0.1870 0.2033 0.0090  0.0077  0.0049  995  TYR A CD2 
7373  C CE1 . TYR A 997  ? 0.2475 0.2118 0.2227 0.0118  0.0096  0.0065  995  TYR A CE1 
7374  C CE2 . TYR A 997  ? 0.2357 0.1987 0.2129 0.0108  0.0075  0.0036  995  TYR A CE2 
7375  C CZ  . TYR A 997  ? 0.3000 0.2643 0.2753 0.0122  0.0086  0.0044  995  TYR A CZ  
7376  O OH  . TYR A 997  ? 0.2808 0.2468 0.2545 0.0140  0.0085  0.0031  995  TYR A OH  
7377  N N   . ILE A 998  ? 0.2059 0.1704 0.1866 0.0053  0.0094  0.0087  996  ILE A N   
7378  C CA  A ILE A 998  ? 0.2238 0.1896 0.2056 0.0042  0.0094  0.0089  996  ILE A CA  
7379  C CA  B ILE A 998  ? 0.2238 0.1896 0.2056 0.0042  0.0094  0.0089  996  ILE A CA  
7380  C C   . ILE A 998  ? 0.2119 0.1771 0.1943 0.0042  0.0100  0.0098  996  ILE A C   
7381  O O   . ILE A 998  ? 0.2208 0.1851 0.2031 0.0051  0.0104  0.0102  996  ILE A O   
7382  C CB  A ILE A 998  ? 0.2143 0.1816 0.1964 0.0045  0.0093  0.0080  996  ILE A CB  
7383  C CB  B ILE A 998  ? 0.2144 0.1817 0.1965 0.0045  0.0093  0.0080  996  ILE A CB  
7384  C CG1 A ILE A 998  ? 0.2604 0.2284 0.2419 0.0047  0.0087  0.0071  996  ILE A CG1 
7385  C CG1 B ILE A 998  ? 0.2517 0.2200 0.2334 0.0044  0.0086  0.0071  996  ILE A CG1 
7386  C CG2 A ILE A 998  ? 0.2118 0.1814 0.1951 0.0035  0.0092  0.0077  996  ILE A CG2 
7387  C CG2 B ILE A 998  ? 0.2117 0.1811 0.1950 0.0036  0.0093  0.0077  996  ILE A CG2 
7388  C CD1 A ILE A 998  ? 0.2582 0.2275 0.2403 0.0033  0.0082  0.0070  996  ILE A CD1 
7389  C CD1 B ILE A 998  ? 0.2537 0.2237 0.2359 0.0049  0.0084  0.0061  996  ILE A CD1 
7390  N N   . ASN A 999  ? 0.2034 0.1690 0.1865 0.0030  0.0099  0.0104  997  ASN A N   
7391  C CA  . ASN A 999  ? 0.2048 0.1702 0.1886 0.0028  0.0103  0.0112  997  ASN A CA  
7392  C C   . ASN A 999  ? 0.2005 0.1639 0.1840 0.0037  0.0108  0.0119  997  ASN A C   
7393  O O   . ASN A 999  ? 0.2196 0.1827 0.2038 0.0040  0.0113  0.0125  997  ASN A O   
7394  C CB  . ASN A 999  ? 0.2080 0.1747 0.1927 0.0028  0.0104  0.0106  997  ASN A CB  
7395  C CG  . ASN A 999  ? 0.2407 0.2102 0.2257 0.0019  0.0100  0.0097  997  ASN A CG  
7396  O OD1 . ASN A 999  ? 0.2374 0.2083 0.2224 0.0008  0.0098  0.0103  997  ASN A OD1 
7397  N ND2 . ASN A 999  ? 0.2301 0.2009 0.2157 0.0024  0.0098  0.0084  997  ASN A ND2 
7398  N N   . ARG A 1000 ? 0.2094 0.1718 0.1923 0.0043  0.0107  0.0117  998  ARG A N   
7399  C CA  . ARG A 1000 ? 0.2201 0.1813 0.2026 0.0053  0.0112  0.0122  998  ARG A CA  
7400  C C   . ARG A 1000 ? 0.2496 0.2101 0.2322 0.0054  0.0105  0.0115  998  ARG A C   
7401  O O   . ARG A 1000 ? 0.2472 0.2078 0.2303 0.0045  0.0097  0.0111  998  ARG A O   
7402  C CB  . ARG A 1000 ? 0.2253 0.1866 0.2068 0.0067  0.0117  0.0122  998  ARG A CB  
7403  C CG  . ARG A 1000 ? 0.2363 0.1982 0.2168 0.0071  0.0112  0.0113  998  ARG A CG  
7404  C CD  . ARG A 1000 ? 0.2308 0.1931 0.2099 0.0087  0.0117  0.0114  998  ARG A CD  
7405  N NE  . ARG A 1000 ? 0.2219 0.1841 0.2003 0.0095  0.0117  0.0108  998  ARG A NE  
7406  C CZ  . ARG A 1000 ? 0.2387 0.2020 0.2157 0.0111  0.0121  0.0107  998  ARG A CZ  
7407  N NH1 . ARG A 1000 ? 0.2567 0.2213 0.2328 0.0118  0.0124  0.0116  998  ARG A NH1 
7408  N NH2 . ARG A 1000 ? 0.2262 0.1898 0.2029 0.0119  0.0119  0.0096  998  ARG A NH2 
7409  N N   . ASN A 1001 ? 0.2435 0.2033 0.2260 0.0065  0.0108  0.0114  999  ASN A N   
7410  C CA  . ASN A 1001 ? 0.2243 0.1833 0.2072 0.0069  0.0100  0.0103  999  ASN A CA  
7411  C C   . ASN A 1001 ? 0.2509 0.2104 0.2326 0.0077  0.0095  0.0088  999  ASN A C   
7412  O O   . ASN A 1001 ? 0.2250 0.1854 0.2053 0.0081  0.0100  0.0089  999  ASN A O   
7413  C CB  . ASN A 1001 ? 0.2262 0.1848 0.2097 0.0080  0.0103  0.0101  999  ASN A CB  
7414  C CG  . ASN A 1001 ? 0.2863 0.2463 0.2680 0.0098  0.0113  0.0098  999  ASN A CG  
7415  O OD1 . ASN A 1001 ? 0.2645 0.2253 0.2446 0.0106  0.0112  0.0090  999  ASN A OD1 
7416  N ND2 . ASN A 1001 ? 0.2992 0.2597 0.2811 0.0104  0.0122  0.0107  999  ASN A ND2 
7417  N N   . ILE A 1002 ? 0.2030 0.1617 0.1856 0.0080  0.0085  0.0074  1000 ILE A N   
7418  C CA  . ILE A 1002 ? 0.2147 0.1740 0.1964 0.0086  0.0078  0.0057  1000 ILE A CA  
7419  C C   . ILE A 1002 ? 0.2332 0.1930 0.2140 0.0107  0.0077  0.0039  1000 ILE A C   
7420  O O   . ILE A 1002 ? 0.2532 0.2134 0.2338 0.0113  0.0067  0.0020  1000 ILE A O   
7421  C CB  . ILE A 1002 ? 0.2031 0.1616 0.1869 0.0071  0.0064  0.0053  1000 ILE A CB  
7422  C CG1 . ILE A 1002 ? 0.2227 0.1795 0.2091 0.0070  0.0052  0.0046  1000 ILE A CG1 
7423  C CG2 . ILE A 1002 ? 0.2126 0.1717 0.1970 0.0053  0.0066  0.0071  1000 ILE A CG2 
7424  C CD1 . ILE A 1002 ? 0.2399 0.1959 0.2290 0.0055  0.0036  0.0044  1000 ILE A CD1 
7425  N N   . ILE A 1003 ? 0.2272 0.1876 0.2076 0.0117  0.0086  0.0043  1001 ILE A N   
7426  C CA  . ILE A 1003 ? 0.2437 0.2054 0.2233 0.0138  0.0085  0.0023  1001 ILE A CA  
7427  C C   . ILE A 1003 ? 0.2565 0.2209 0.2337 0.0152  0.0100  0.0034  1001 ILE A C   
7428  O O   . ILE A 1003 ? 0.2673 0.2318 0.2438 0.0145  0.0110  0.0056  1001 ILE A O   
7429  C CB  . ILE A 1003 ? 0.2342 0.1948 0.2161 0.0142  0.0081  0.0015  1001 ILE A CB  
7430  C CG1 . ILE A 1003 ? 0.2494 0.2098 0.2316 0.0137  0.0093  0.0038  1001 ILE A CG1 
7431  C CG2 . ILE A 1003 ? 0.2305 0.1885 0.2154 0.0129  0.0063  0.0007  1001 ILE A CG2 
7432  C CD1 . ILE A 1003 ? 0.2598 0.2199 0.2439 0.0147  0.0091  0.0029  1001 ILE A CD1 
7433  N N   . GLY A 1004 ? 0.2572 0.2239 0.2331 0.0172  0.0101  0.0017  1002 GLY A N   
7434  C CA  . GLY A 1004 ? 0.2570 0.2269 0.2307 0.0186  0.0116  0.0030  1002 GLY A CA  
7435  C C   . GLY A 1004 ? 0.2841 0.2555 0.2558 0.0186  0.0119  0.0043  1002 GLY A C   
7436  O O   . GLY A 1004 ? 0.2919 0.2645 0.2630 0.0185  0.0131  0.0069  1002 GLY A O   
7437  N N   . ALA A 1005 ? 0.2445 0.2158 0.2157 0.0187  0.0107  0.0026  1003 ALA A N   
7438  C CA  . ALA A 1005 ? 0.2664 0.2393 0.2358 0.0189  0.0109  0.0036  1003 ALA A CA  
7439  C C   . ALA A 1005 ? 0.2718 0.2488 0.2390 0.0207  0.0120  0.0049  1003 ALA A C   
7440  O O   . ALA A 1005 ? 0.3057 0.2854 0.2720 0.0224  0.0122  0.0033  1003 ALA A O   
7441  C CB  . ALA A 1005 ? 0.2881 0.2611 0.2571 0.0192  0.0093  0.0010  1003 ALA A CB  
7442  N N   . VAL A 1006 ? 0.2602 0.2381 0.2268 0.0204  0.0127  0.0077  1004 VAL A N   
7443  C CA  . VAL A 1006 ? 0.2483 0.2301 0.2134 0.0216  0.0139  0.0101  1004 VAL A CA  
7444  C C   . VAL A 1006 ? 0.2563 0.2410 0.2193 0.0228  0.0134  0.0101  1004 VAL A C   
7445  O O   . VAL A 1006 ? 0.2415 0.2244 0.2049 0.0219  0.0126  0.0105  1004 VAL A O   
7446  C CB  . VAL A 1006 ? 0.2512 0.2317 0.2180 0.0204  0.0149  0.0138  1004 VAL A CB  
7447  C CG1 . VAL A 1006 ? 0.2922 0.2770 0.2580 0.0215  0.0160  0.0169  1004 VAL A CG1 
7448  C CG2 . VAL A 1006 ? 0.2858 0.2642 0.2545 0.0195  0.0154  0.0138  1004 VAL A CG2 
7449  N N   . VAL A 1007 ? 0.2325 0.2221 0.1932 0.0248  0.0137  0.0096  1005 VAL A N   
7450  C CA  . VAL A 1007 ? 0.2192 0.2126 0.1776 0.0261  0.0133  0.0096  1005 VAL A CA  
7451  C C   . VAL A 1007 ? 0.2537 0.2466 0.2127 0.0252  0.0135  0.0136  1005 VAL A C   
7452  O O   . VAL A 1007 ? 0.2360 0.2289 0.1962 0.0247  0.0146  0.0171  1005 VAL A O   
7453  C CB  . VAL A 1007 ? 0.2259 0.2256 0.1818 0.0284  0.0141  0.0095  1005 VAL A CB  
7454  C CG1 . VAL A 1007 ? 0.2592 0.2635 0.2125 0.0298  0.0136  0.0100  1005 VAL A CG1 
7455  C CG2 . VAL A 1007 ? 0.2850 0.2851 0.2408 0.0295  0.0135  0.0050  1005 VAL A CG2 
7456  N N   . GLY A 1008 ? 0.2408 0.2332 0.1993 0.0252  0.0123  0.0129  1006 GLY A N   
7457  C CA  . GLY A 1008 ? 0.2482 0.2404 0.2074 0.0247  0.0123  0.0163  1006 GLY A CA  
7458  C C   . GLY A 1008 ? 0.2527 0.2400 0.2152 0.0227  0.0123  0.0177  1006 GLY A C   
7459  O O   . GLY A 1008 ? 0.2654 0.2520 0.2293 0.0223  0.0120  0.0202  1006 GLY A O   
7460  N N   . VAL A 1009 ? 0.2347 0.2187 0.1986 0.0216  0.0125  0.0161  1007 VAL A N   
7461  C CA  . VAL A 1009 ? 0.2571 0.2369 0.2238 0.0198  0.0125  0.0169  1007 VAL A CA  
7462  C C   . VAL A 1009 ? 0.2542 0.2309 0.2216 0.0187  0.0115  0.0138  1007 VAL A C   
7463  O O   . VAL A 1009 ? 0.2493 0.2240 0.2181 0.0177  0.0109  0.0137  1007 VAL A O   
7464  C CB  . VAL A 1009 ? 0.2648 0.2438 0.2330 0.0192  0.0136  0.0185  1007 VAL A CB  
7465  C CG1 . VAL A 1009 ? 0.2505 0.2256 0.2216 0.0174  0.0134  0.0191  1007 VAL A CG1 
7466  C CG2 . VAL A 1009 ? 0.2496 0.2321 0.2175 0.0201  0.0146  0.0221  1007 VAL A CG2 
7467  N N   . GLN A 1010 ? 0.2468 0.2235 0.2135 0.0189  0.0113  0.0112  1008 GLN A N   
7468  C CA  . GLN A 1010 ? 0.2267 0.2014 0.1938 0.0182  0.0102  0.0083  1008 GLN A CA  
7469  C C   . GLN A 1010 ? 0.2351 0.2124 0.2002 0.0197  0.0094  0.0058  1008 GLN A C   
7470  O O   . GLN A 1010 ? 0.2633 0.2408 0.2284 0.0202  0.0093  0.0039  1008 GLN A O   
7471  C CB  . GLN A 1010 ? 0.2522 0.2242 0.2211 0.0168  0.0102  0.0074  1008 GLN A CB  
7472  C CG  . GLN A 1010 ? 0.2579 0.2279 0.2287 0.0155  0.0109  0.0095  1008 GLN A CG  
7473  C CD  . GLN A 1010 ? 0.2665 0.2370 0.2375 0.0158  0.0121  0.0112  1008 GLN A CD  
7474  O OE1 . GLN A 1010 ? 0.2718 0.2435 0.2419 0.0167  0.0124  0.0103  1008 GLN A OE1 
7475  N NE2 . GLN A 1010 ? 0.2488 0.2185 0.2212 0.0150  0.0127  0.0134  1008 GLN A NE2 
7476  N N   . PRO A 1011 ? 0.2283 0.2078 0.1920 0.0206  0.0088  0.0058  1009 PRO A N   
7477  C CA  . PRO A 1011 ? 0.2641 0.2461 0.2263 0.0220  0.0078  0.0029  1009 PRO A CA  
7478  C C   . PRO A 1011 ? 0.2403 0.2196 0.2042 0.0210  0.0067  -0.0002 1009 PRO A C   
7479  O O   . PRO A 1011 ? 0.2247 0.2011 0.1905 0.0193  0.0063  0.0000  1009 PRO A O   
7480  C CB  . PRO A 1011 ? 0.2631 0.2465 0.2245 0.0223  0.0071  0.0036  1009 PRO A CB  
7481  C CG  . PRO A 1011 ? 0.2538 0.2372 0.2156 0.0221  0.0081  0.0075  1009 PRO A CG  
7482  C CD  . PRO A 1011 ? 0.2378 0.2176 0.2018 0.0204  0.0089  0.0083  1009 PRO A CD  
7483  N N   . PHE A 1012 ? 0.2405 0.2211 0.2040 0.0222  0.0061  -0.0029 1010 PHE A N   
7484  C CA  . PHE A 1012 ? 0.2362 0.2139 0.2022 0.0212  0.0052  -0.0052 1010 PHE A CA  
7485  C C   . PHE A 1012 ? 0.2406 0.2187 0.2073 0.0216  0.0033  -0.0087 1010 PHE A C   
7486  O O   . PHE A 1012 ? 0.2600 0.2414 0.2249 0.0235  0.0027  -0.0108 1010 PHE A O   
7487  C CB  . PHE A 1012 ? 0.2324 0.2104 0.1986 0.0221  0.0058  -0.0059 1010 PHE A CB  
7488  C CG  . PHE A 1012 ? 0.2327 0.2073 0.2021 0.0210  0.0048  -0.0076 1010 PHE A CG  
7489  C CD1 . PHE A 1012 ? 0.2657 0.2368 0.2371 0.0188  0.0052  -0.0056 1010 PHE A CD1 
7490  C CD2 . PHE A 1012 ? 0.2721 0.2470 0.2426 0.0220  0.0033  -0.0113 1010 PHE A CD2 
7491  C CE1 . PHE A 1012 ? 0.2788 0.2470 0.2533 0.0177  0.0042  -0.0067 1010 PHE A CE1 
7492  C CE2 . PHE A 1012 ? 0.2302 0.2016 0.2043 0.0209  0.0022  -0.0127 1010 PHE A CE2 
7493  C CZ  . PHE A 1012 ? 0.2368 0.2050 0.2129 0.0187  0.0027  -0.0101 1010 PHE A CZ  
7494  N N   . GLY A 1013 ? 0.2239 0.1988 0.1934 0.0197  0.0022  -0.0093 1011 GLY A N   
7495  C CA  . GLY A 1013 ? 0.2746 0.2494 0.2457 0.0198  0.0002  -0.0126 1011 GLY A CA  
7496  C C   . GLY A 1013 ? 0.2554 0.2279 0.2289 0.0175  -0.0005 -0.0118 1011 GLY A C   
7497  O O   . GLY A 1013 ? 0.2736 0.2460 0.2465 0.0165  0.0004  -0.0093 1011 GLY A O   
7498  N N   . GLY A 1014 ? 0.2480 0.2190 0.2247 0.0167  -0.0023 -0.0141 1012 GLY A N   
7499  C CA  . GLY A 1014 ? 0.2909 0.2601 0.2704 0.0143  -0.0030 -0.0131 1012 GLY A CA  
7500  C C   . GLY A 1014 ? 0.3133 0.2836 0.2943 0.0142  -0.0049 -0.0155 1012 GLY A C   
7501  O O   . GLY A 1014 ? 0.3099 0.2827 0.2890 0.0161  -0.0055 -0.0176 1012 GLY A O   
7502  N N   . ARG A 1015 ? 0.2486 0.2173 0.2332 0.0120  -0.0058 -0.0149 1013 ARG A N   
7503  C CA  . ARG A 1015 ? 0.2538 0.2234 0.2403 0.0113  -0.0075 -0.0164 1013 ARG A CA  
7504  C C   . ARG A 1015 ? 0.2765 0.2438 0.2681 0.0097  -0.0094 -0.0175 1013 ARG A C   
7505  O O   . ARG A 1015 ? 0.2649 0.2299 0.2585 0.0091  -0.0093 -0.0168 1013 ARG A O   
7506  C CB  . ARG A 1015 ? 0.2618 0.2325 0.2478 0.0099  -0.0066 -0.0140 1013 ARG A CB  
7507  C CG  . ARG A 1015 ? 0.2697 0.2388 0.2577 0.0076  -0.0057 -0.0111 1013 ARG A CG  
7508  C CD  . ARG A 1015 ? 0.3299 0.3007 0.3182 0.0062  -0.0052 -0.0094 1013 ARG A CD  
7509  N NE  . ARG A 1015 ? 0.3857 0.3583 0.3750 0.0063  -0.0066 -0.0112 1013 ARG A NE  
7510  C CZ  . ARG A 1015 ? 0.4438 0.4162 0.4371 0.0048  -0.0083 -0.0121 1013 ARG A CZ  
7511  N NH1 . ARG A 1015 ? 0.4146 0.3850 0.4114 0.0031  -0.0089 -0.0112 1013 ARG A NH1 
7512  N NH2 . ARG A 1015 ? 0.3423 0.3165 0.3363 0.0051  -0.0097 -0.0139 1013 ARG A NH2 
7513  N N   . GLY A 1016 ? 0.2928 0.2608 0.2871 0.0089  -0.0111 -0.0190 1014 GLY A N   
7514  C CA  . GLY A 1016 ? 0.2618 0.2276 0.2618 0.0071  -0.0132 -0.0196 1014 GLY A CA  
7515  C C   . GLY A 1016 ? 0.2971 0.2612 0.2988 0.0086  -0.0146 -0.0227 1014 GLY A C   
7516  O O   . GLY A 1016 ? 0.2847 0.2505 0.2839 0.0112  -0.0150 -0.0259 1014 GLY A O   
7517  N N   . LEU A 1017 ? 0.2611 0.2222 0.2670 0.0072  -0.0153 -0.0217 1015 LEU A N   
7518  C CA  . LEU A 1017 ? 0.2495 0.2088 0.2579 0.0086  -0.0168 -0.0247 1015 LEU A CA  
7519  C C   . LEU A 1017 ? 0.2638 0.2237 0.2675 0.0110  -0.0150 -0.0252 1015 LEU A C   
7520  O O   . LEU A 1017 ? 0.2806 0.2397 0.2857 0.0127  -0.0160 -0.0281 1015 LEU A O   
7521  C CB  . LEU A 1017 ? 0.2729 0.2286 0.2874 0.0063  -0.0181 -0.0229 1015 LEU A CB  
7522  C CG  . LEU A 1017 ? 0.3233 0.2781 0.3436 0.0036  -0.0202 -0.0220 1015 LEU A CG  
7523  C CD1 . LEU A 1017 ? 0.3309 0.2825 0.3567 0.0013  -0.0210 -0.0190 1015 LEU A CD1 
7524  C CD2 . LEU A 1017 ? 0.3168 0.2716 0.3403 0.0048  -0.0231 -0.0268 1015 LEU A CD2 
7525  N N   . SER A 1018 ? 0.2396 0.2012 0.2383 0.0112  -0.0124 -0.0225 1016 SER A N   
7526  C CA  . SER A 1018 ? 0.2460 0.2085 0.2407 0.0132  -0.0106 -0.0223 1016 SER A CA  
7527  C C   . SER A 1018 ? 0.2683 0.2345 0.2584 0.0160  -0.0101 -0.0246 1016 SER A C   
7528  O O   . SER A 1018 ? 0.2749 0.2425 0.2620 0.0178  -0.0088 -0.0247 1016 SER A O   
7529  C CB  . SER A 1018 ? 0.2456 0.2078 0.2379 0.0119  -0.0081 -0.0179 1016 SER A CB  
7530  O OG  . SER A 1018 ? 0.2414 0.2008 0.2375 0.0096  -0.0084 -0.0156 1016 SER A OG  
7531  N N   . GLY A 1019 ? 0.2704 0.2386 0.2600 0.0163  -0.0111 -0.0261 1017 GLY A N   
7532  C CA  . GLY A 1019 ? 0.3149 0.2872 0.3000 0.0189  -0.0107 -0.0280 1017 GLY A CA  
7533  C C   . GLY A 1019 ? 0.2762 0.2510 0.2602 0.0191  -0.0115 -0.0288 1017 GLY A C   
7534  O O   . GLY A 1019 ? 0.2654 0.2390 0.2513 0.0170  -0.0118 -0.0271 1017 GLY A O   
7535  N N   . THR A 1020 ? 0.2680 0.2467 0.2489 0.0217  -0.0118 -0.0314 1018 THR A N   
7536  C CA  . THR A 1020 ? 0.2774 0.2593 0.2562 0.0223  -0.0124 -0.0319 1018 THR A CA  
7537  C C   . THR A 1020 ? 0.2644 0.2484 0.2387 0.0228  -0.0101 -0.0281 1018 THR A C   
7538  O O   . THR A 1020 ? 0.3042 0.2899 0.2773 0.0226  -0.0102 -0.0273 1018 THR A O   
7539  C CB  . THR A 1020 ? 0.2606 0.2464 0.2381 0.0251  -0.0140 -0.0365 1018 THR A CB  
7540  O OG1 . THR A 1020 ? 0.2544 0.2429 0.2283 0.0274  -0.0125 -0.0366 1018 THR A OG1 
7541  C CG2 . THR A 1020 ? 0.3233 0.3070 0.3061 0.0247  -0.0168 -0.0407 1018 THR A CG2 
7542  N N   . GLY A 1021 ? 0.2564 0.2405 0.2283 0.0235  -0.0081 -0.0261 1019 GLY A N   
7543  C CA  . GLY A 1021 ? 0.2728 0.2597 0.2404 0.0246  -0.0063 -0.0232 1019 GLY A CA  
7544  C C   . GLY A 1021 ? 0.2763 0.2686 0.2407 0.0273  -0.0069 -0.0253 1019 GLY A C   
7545  O O   . GLY A 1021 ? 0.2745 0.2683 0.2399 0.0284  -0.0088 -0.0296 1019 GLY A O   
7546  N N   . PRO A 1022 ? 0.2795 0.2750 0.2403 0.0284  -0.0055 -0.0225 1020 PRO A N   
7547  C CA  . PRO A 1022 ? 0.2851 0.2790 0.2449 0.0274  -0.0034 -0.0177 1020 PRO A CA  
7548  C C   . PRO A 1022 ? 0.2672 0.2595 0.2271 0.0273  -0.0019 -0.0165 1020 PRO A C   
7549  O O   . PRO A 1022 ? 0.2990 0.2922 0.2592 0.0284  -0.0022 -0.0191 1020 PRO A O   
7550  C CB  . PRO A 1022 ? 0.2627 0.2615 0.2189 0.0292  -0.0029 -0.0157 1020 PRO A CB  
7551  C CG  . PRO A 1022 ? 0.2663 0.2700 0.2204 0.0317  -0.0038 -0.0193 1020 PRO A CG  
7552  C CD  . PRO A 1022 ? 0.2745 0.2760 0.2318 0.0310  -0.0060 -0.0238 1020 PRO A CD  
7553  N N   . LYS A 1023 ? 0.2540 0.2441 0.2141 0.0260  -0.0002 -0.0126 1021 LYS A N   
7554  C CA  . LYS A 1023 ? 0.2559 0.2442 0.2165 0.0256  0.0012  -0.0111 1021 LYS A CA  
7555  C C   . LYS A 1023 ? 0.2626 0.2552 0.2202 0.0277  0.0023  -0.0105 1021 LYS A C   
7556  O O   . LYS A 1023 ? 0.2527 0.2490 0.2077 0.0289  0.0029  -0.0085 1021 LYS A O   
7557  C CB  . LYS A 1023 ? 0.2652 0.2506 0.2266 0.0238  0.0025  -0.0072 1021 LYS A CB  
7558  C CG  . LYS A 1023 ? 0.2285 0.2097 0.1931 0.0214  0.0019  -0.0074 1021 LYS A CG  
7559  C CD  . LYS A 1023 ? 0.2164 0.1960 0.1814 0.0202  0.0033  -0.0038 1021 LYS A CD  
7560  C CE  . LYS A 1023 ? 0.2481 0.2243 0.2159 0.0179  0.0030  -0.0037 1021 LYS A CE  
7561  N NZ  . LYS A 1023 ? 0.2342 0.2081 0.2034 0.0171  0.0034  -0.0039 1021 LYS A NZ  
7562  N N   . ALA A 1024 ? 0.2663 0.2586 0.2246 0.0283  0.0026  -0.0121 1022 ALA A N   
7563  C CA  . ALA A 1024 ? 0.2738 0.2701 0.2297 0.0300  0.0041  -0.0110 1022 ALA A CA  
7564  C C   . ALA A 1024 ? 0.2598 0.2551 0.2155 0.0290  0.0060  -0.0060 1022 ALA A C   
7565  O O   . ALA A 1024 ? 0.3043 0.2950 0.2623 0.0269  0.0063  -0.0044 1022 ALA A O   
7566  C CB  . ALA A 1024 ? 0.2819 0.2777 0.2392 0.0307  0.0039  -0.0140 1022 ALA A CB  
7567  N N   . GLY A 1025 ? 0.2529 0.2530 0.2060 0.0304  0.0072  -0.0036 1023 GLY A N   
7568  C CA  . GLY A 1025 ? 0.2850 0.2843 0.2385 0.0294  0.0088  0.0012  1023 GLY A CA  
7569  C C   . GLY A 1025 ? 0.2528 0.2497 0.2072 0.0280  0.0085  0.0037  1023 GLY A C   
7570  O O   . GLY A 1025 ? 0.2357 0.2298 0.1916 0.0267  0.0093  0.0069  1023 GLY A O   
7571  N N   . GLY A 1026 ? 0.2361 0.2339 0.1897 0.0285  0.0070  0.0020  1024 GLY A N   
7572  C CA  . GLY A 1026 ? 0.2382 0.2344 0.1927 0.0275  0.0065  0.0039  1024 GLY A CA  
7573  C C   . GLY A 1026 ? 0.2547 0.2558 0.2067 0.0292  0.0059  0.0045  1024 GLY A C   
7574  O O   . GLY A 1026 ? 0.2505 0.2564 0.2000 0.0311  0.0057  0.0028  1024 GLY A O   
7575  N N   . PRO A 1027 ? 0.2477 0.2479 0.2005 0.0287  0.0054  0.0067  1025 PRO A N   
7576  C CA  . PRO A 1027 ? 0.2748 0.2798 0.2256 0.0302  0.0050  0.0085  1025 PRO A CA  
7577  C C   . PRO A 1027 ? 0.2159 0.2234 0.1653 0.0313  0.0033  0.0050  1025 PRO A C   
7578  O O   . PRO A 1027 ? 0.2520 0.2643 0.1992 0.0329  0.0028  0.0062  1025 PRO A O   
7579  C CB  . PRO A 1027 ? 0.2643 0.2664 0.2175 0.0290  0.0050  0.0121  1025 PRO A CB  
7580  C CG  . PRO A 1027 ? 0.2620 0.2583 0.2180 0.0271  0.0047  0.0100  1025 PRO A CG  
7581  C CD  . PRO A 1027 ? 0.2341 0.2292 0.1899 0.0267  0.0055  0.0081  1025 PRO A CD  
7582  N N   . LEU A 1028 ? 0.2370 0.2415 0.1877 0.0305  0.0022  0.0009  1026 LEU A N   
7583  C CA  . LEU A 1028 ? 0.2226 0.2294 0.1724 0.0314  0.0005  -0.0028 1026 LEU A CA  
7584  C C   . LEU A 1028 ? 0.2439 0.2544 0.1918 0.0331  0.0000  -0.0065 1026 LEU A C   
7585  O O   . LEU A 1028 ? 0.2576 0.2709 0.2045 0.0343  -0.0016 -0.0098 1026 LEU A O   
7586  C CB  . LEU A 1028 ? 0.2424 0.2446 0.1953 0.0296  -0.0007 -0.0053 1026 LEU A CB  
7587  C CG  . LEU A 1028 ? 0.2885 0.2879 0.2432 0.0282  -0.0006 -0.0027 1026 LEU A CG  
7588  C CD1 . LEU A 1028 ? 0.3059 0.3016 0.2635 0.0264  -0.0017 -0.0052 1026 LEU A CD1 
7589  C CD2 . LEU A 1028 ? 0.3678 0.3710 0.3211 0.0295  -0.0014 -0.0011 1026 LEU A CD2 
7590  N N   . TYR A 1029 ? 0.2568 0.2677 0.2042 0.0335  0.0014  -0.0061 1027 TYR A N   
7591  C CA  . TYR A 1029 ? 0.2700 0.2833 0.2165 0.0350  0.0009  -0.0103 1027 TYR A CA  
7592  C C   . TYR A 1029 ? 0.2546 0.2756 0.1976 0.0377  0.0003  -0.0116 1027 TYR A C   
7593  O O   . TYR A 1029 ? 0.2673 0.2905 0.2101 0.0389  -0.0014 -0.0164 1027 TYR A O   
7594  C CB  . TYR A 1029 ? 0.2663 0.2786 0.2132 0.0348  0.0026  -0.0091 1027 TYR A CB  
7595  C CG  . TYR A 1029 ? 0.2457 0.2580 0.1935 0.0356  0.0020  -0.0136 1027 TYR A CG  
7596  C CD1 . TYR A 1029 ? 0.2578 0.2648 0.2089 0.0341  0.0007  -0.0167 1027 TYR A CD1 
7597  C CD2 . TYR A 1029 ? 0.2633 0.2809 0.2088 0.0377  0.0029  -0.0144 1027 TYR A CD2 
7598  C CE1 . TYR A 1029 ? 0.2586 0.2651 0.2112 0.0348  0.0001  -0.0207 1027 TYR A CE1 
7599  C CE2 . TYR A 1029 ? 0.2706 0.2880 0.2173 0.0386  0.0023  -0.0187 1027 TYR A CE2 
7600  C CZ  . TYR A 1029 ? 0.2570 0.2686 0.2074 0.0372  0.0008  -0.0218 1027 TYR A CZ  
7601  O OH  . TYR A 1029 ? 0.2873 0.2985 0.2395 0.0381  0.0001  -0.0260 1027 TYR A OH  
7602  N N   . LEU A 1030 ? 0.2571 0.2827 0.1975 0.0387  0.0016  -0.0073 1028 LEU A N   
7603  C CA  . LEU A 1030 ? 0.2532 0.2873 0.1900 0.0414  0.0013  -0.0082 1028 LEU A CA  
7604  C C   . LEU A 1030 ? 0.2747 0.3105 0.2108 0.0420  -0.0008 -0.0104 1028 LEU A C   
7605  O O   . LEU A 1030 ? 0.2782 0.3199 0.2121 0.0442  -0.0019 -0.0140 1028 LEU A O   
7606  C CB  . LEU A 1030 ? 0.2575 0.2962 0.1921 0.0420  0.0031  -0.0023 1028 LEU A CB  
7607  C CG  . LEU A 1030 ? 0.2535 0.2917 0.1885 0.0416  0.0052  0.0002  1028 LEU A CG  
7608  C CD1 . LEU A 1030 ? 0.3051 0.3488 0.2382 0.0423  0.0066  0.0063  1028 LEU A CD1 
7609  C CD2 . LEU A 1030 ? 0.2959 0.3372 0.2299 0.0433  0.0052  -0.0046 1028 LEU A CD2 
7610  N N   . GLY A 1031 ? 0.2571 0.2882 0.1954 0.0402  -0.0014 -0.0086 1029 GLY A N   
7611  C CA  . GLY A 1031 ? 0.2794 0.3123 0.2172 0.0407  -0.0033 -0.0102 1029 GLY A CA  
7612  C C   . GLY A 1031 ? 0.3020 0.3344 0.2409 0.0411  -0.0053 -0.0166 1029 GLY A C   
7613  O O   . GLY A 1031 ? 0.2947 0.3305 0.2326 0.0422  -0.0071 -0.0189 1029 GLY A O   
7614  N N   . ARG A 1032 ? 0.2530 0.2812 0.1942 0.0402  -0.0053 -0.0196 1030 ARG A N   
7615  C CA  . ARG A 1032 ? 0.2513 0.2788 0.1944 0.0405  -0.0074 -0.0257 1030 ARG A CA  
7616  C C   . ARG A 1032 ? 0.2878 0.3224 0.2282 0.0435  -0.0080 -0.0296 1030 ARG A C   
7617  O O   . ARG A 1032 ? 0.2831 0.3186 0.2247 0.0444  -0.0102 -0.0351 1030 ARG A O   
7618  C CB  . ARG A 1032 ? 0.2579 0.2783 0.2049 0.0385  -0.0072 -0.0269 1030 ARG A CB  
7619  C CG  . ARG A 1032 ? 0.2620 0.2800 0.2125 0.0380  -0.0096 -0.0324 1030 ARG A CG  
7620  C CD  . ARG A 1032 ? 0.2960 0.3117 0.2487 0.0365  -0.0111 -0.0326 1030 ARG A CD  
7621  N NE  . ARG A 1032 ? 0.2767 0.2891 0.2337 0.0354  -0.0133 -0.0371 1030 ARG A NE  
7622  C CZ  . ARG A 1032 ? 0.3180 0.3324 0.2763 0.0361  -0.0157 -0.0411 1030 ARG A CZ  
7623  N NH1 . ARG A 1032 ? 0.3421 0.3620 0.2972 0.0378  -0.0164 -0.0414 1030 ARG A NH1 
7624  N NH2 . ARG A 1032 ? 0.3514 0.3621 0.3144 0.0349  -0.0177 -0.0447 1030 ARG A NH2 
7625  N N   . LEU A 1033 ? 0.2735 0.3134 0.2104 0.0452  -0.0063 -0.0269 1031 LEU A N   
7626  C CA  . LEU A 1033 ? 0.2669 0.3142 0.2012 0.0481  -0.0065 -0.0304 1031 LEU A CA  
7627  C C   . LEU A 1033 ? 0.2524 0.3085 0.1823 0.0505  -0.0069 -0.0296 1031 LEU A C   
7628  O O   . LEU A 1033 ? 0.2724 0.3363 0.1992 0.0531  -0.0066 -0.0314 1031 LEU A O   
7629  C CB  . LEU A 1033 ? 0.2723 0.3202 0.2057 0.0484  -0.0041 -0.0281 1031 LEU A CB  
7630  C CG  . LEU A 1033 ? 0.2718 0.3110 0.2094 0.0460  -0.0036 -0.0283 1031 LEU A CG  
7631  C CD1 . LEU A 1033 ? 0.2815 0.3216 0.2184 0.0463  -0.0013 -0.0260 1031 LEU A CD1 
7632  C CD2 . LEU A 1033 ? 0.3187 0.3549 0.2596 0.0461  -0.0060 -0.0349 1031 LEU A CD2 
7633  N N   . VAL A 1034 ? 0.2767 0.3321 0.2064 0.0496  -0.0076 -0.0270 1032 VAL A N   
7634  C CA  . VAL A 1034 ? 0.2751 0.3386 0.2012 0.0517  -0.0083 -0.0261 1032 VAL A CA  
7635  C C   . VAL A 1034 ? 0.2858 0.3471 0.2137 0.0511  -0.0108 -0.0290 1032 VAL A C   
7636  O O   . VAL A 1034 ? 0.3087 0.3623 0.2406 0.0487  -0.0114 -0.0298 1032 VAL A O   
7637  C CB  . VAL A 1034 ? 0.2813 0.3470 0.2053 0.0513  -0.0064 -0.0183 1032 VAL A CB  
7638  C CG1 . VAL A 1034 ? 0.3055 0.3750 0.2276 0.0522  -0.0040 -0.0155 1032 VAL A CG1 
7639  C CG2 . VAL A 1034 ? 0.2791 0.3359 0.2066 0.0483  -0.0059 -0.0144 1032 VAL A CG2 
7640  N N   . THR A 1035 ? 0.3076 0.3766 0.2326 0.0533  -0.0123 -0.0306 1033 THR A N   
7641  C CA  . THR A 1035 ? 0.3190 0.3866 0.2458 0.0529  -0.0148 -0.0339 1033 THR A CA  
7642  C C   . THR A 1035 ? 0.3992 0.4630 0.3273 0.0510  -0.0147 -0.0288 1033 THR A C   
7643  O O   . THR A 1035 ? 0.4330 0.4927 0.3640 0.0497  -0.0164 -0.0310 1033 THR A O   
7644  C CB  . THR A 1035 ? 0.4012 0.4784 0.3246 0.0560  -0.0167 -0.0377 1033 THR A CB  
7645  O OG1 . THR A 1035 ? 0.4727 0.5576 0.3914 0.0577  -0.0153 -0.0326 1033 THR A OG1 
7646  C CG2 . THR A 1035 ? 0.3806 0.4608 0.3039 0.0579  -0.0175 -0.0443 1033 THR A CG2 
7647  N N   . THR A 1036 ? 0.3199 0.3849 0.2461 0.0509  -0.0127 -0.0222 1034 THR A N   
7648  C CA  . THR A 1036 ? 0.3249 0.3860 0.2529 0.0491  -0.0125 -0.0173 1034 THR A CA  
7649  C C   . THR A 1036 ? 0.3263 0.3821 0.2558 0.0473  -0.0100 -0.0123 1034 THR A C   
7650  O O   . THR A 1036 ? 0.3537 0.4133 0.2808 0.0482  -0.0084 -0.0087 1034 THR A O   
7651  C CB  . THR A 1036 ? 0.4358 0.5041 0.3607 0.0509  -0.0130 -0.0137 1034 THR A CB  
7652  O OG1 . THR A 1036 ? 0.4349 0.5081 0.3585 0.0525  -0.0155 -0.0187 1034 THR A OG1 
7653  C CG2 . THR A 1036 ? 0.4493 0.5131 0.3765 0.0492  -0.0128 -0.0086 1034 THR A CG2 
7654  N N   . ALA A 1037 ? 0.3272 0.3748 0.2605 0.0448  -0.0099 -0.0123 1035 ALA A N   
7655  C CA  . ALA A 1037 ? 0.3348 0.3771 0.2699 0.0430  -0.0078 -0.0086 1035 ALA A CA  
7656  C C   . ALA A 1037 ? 0.2962 0.3392 0.2310 0.0429  -0.0068 -0.0020 1035 ALA A C   
7657  O O   . ALA A 1037 ? 0.3218 0.3650 0.2574 0.0428  -0.0079 -0.0006 1035 ALA A O   
7658  C CB  . ALA A 1037 ? 0.3167 0.3508 0.2560 0.0405  -0.0080 -0.0106 1035 ALA A CB  
7659  N N   . PRO A 1038 ? 0.2839 0.3274 0.2180 0.0428  -0.0048 0.0021  1036 PRO A N   
7660  C CA  . PRO A 1038 ? 0.2787 0.3218 0.2137 0.0423  -0.0040 0.0086  1036 PRO A CA  
7661  C C   . PRO A 1038 ? 0.2961 0.3308 0.2355 0.0398  -0.0037 0.0096  1036 PRO A C   
7662  O O   . PRO A 1038 ? 0.2870 0.3166 0.2283 0.0384  -0.0038 0.0060  1036 PRO A O   
7663  C CB  . PRO A 1038 ? 0.2930 0.3395 0.2264 0.0429  -0.0020 0.0119  1036 PRO A CB  
7664  C CG  . PRO A 1038 ? 0.3455 0.3892 0.2790 0.0424  -0.0014 0.0074  1036 PRO A CG  
7665  C CD  . PRO A 1038 ? 0.2856 0.3300 0.2186 0.0431  -0.0033 0.0010  1036 PRO A CD  
7666  N N   . VAL A 1039 ? 0.2690 0.3026 0.2100 0.0394  -0.0034 0.0148  1037 VAL A N   
7667  C CA  . VAL A 1039 ? 0.3044 0.3309 0.2496 0.0373  -0.0031 0.0162  1037 VAL A CA  
7668  C C   . VAL A 1039 ? 0.2478 0.2719 0.1939 0.0364  -0.0011 0.0185  1037 VAL A C   
7669  O O   . VAL A 1039 ? 0.2866 0.3138 0.2320 0.0370  -0.0002 0.0231  1037 VAL A O   
7670  C CB  . VAL A 1039 ? 0.2744 0.3007 0.2218 0.0374  -0.0039 0.0204  1037 VAL A CB  
7671  C CG1 . VAL A 1039 ? 0.2978 0.3171 0.2497 0.0355  -0.0036 0.0213  1037 VAL A CG1 
7672  C CG2 . VAL A 1039 ? 0.3096 0.3387 0.2562 0.0385  -0.0059 0.0181  1037 VAL A CG2 
7673  N N   . PRO A 1040 ? 0.2531 0.2721 0.2007 0.0348  -0.0005 0.0156  1038 PRO A N   
7674  C CA  . PRO A 1040 ? 0.2889 0.3058 0.2373 0.0340  0.0013  0.0176  1038 PRO A CA  
7675  C C   . PRO A 1040 ? 0.2546 0.2686 0.2062 0.0330  0.0018  0.0224  1038 PRO A C   
7676  O O   . PRO A 1040 ? 0.2626 0.2745 0.2166 0.0326  0.0007  0.0232  1038 PRO A O   
7677  C CB  . PRO A 1040 ? 0.2603 0.2721 0.2101 0.0325  0.0014  0.0132  1038 PRO A CB  
7678  C CG  . PRO A 1040 ? 0.3021 0.3148 0.2511 0.0329  -0.0002 0.0087  1038 PRO A CG  
7679  C CD  . PRO A 1040 ? 0.2707 0.2861 0.2195 0.0338  -0.0014 0.0106  1038 PRO A CD  
7680  N N   . PRO A 1041 ? 0.2515 0.2656 0.2036 0.0326  0.0033  0.0257  1039 PRO A N   
7681  C CA  . PRO A 1041 ? 0.2793 0.2897 0.2353 0.0314  0.0036  0.0298  1039 PRO A CA  
7682  C C   . PRO A 1041 ? 0.2584 0.2623 0.2177 0.0298  0.0031  0.0272  1039 PRO A C   
7683  O O   . PRO A 1041 ? 0.2769 0.2783 0.2357 0.0290  0.0034  0.0232  1039 PRO A O   
7684  C CB  . PRO A 1041 ? 0.3184 0.3296 0.2743 0.0311  0.0054  0.0321  1039 PRO A CB  
7685  C CG  . PRO A 1041 ? 0.3301 0.3473 0.2814 0.0327  0.0059  0.0304  1039 PRO A CG  
7686  C CD  . PRO A 1041 ? 0.3182 0.3351 0.2678 0.0332  0.0047  0.0250  1039 PRO A CD  
7687  N N   . GLN A 1042 ? 0.2492 0.2507 0.2121 0.0294  0.0023  0.0296  1040 GLN A N   
7688  C CA  . GLN A 1042 ? 0.2548 0.2508 0.2213 0.0280  0.0019  0.0277  1040 GLN A CA  
7689  C C   . GLN A 1042 ? 0.2815 0.2766 0.2471 0.0278  0.0010  0.0230  1040 GLN A C   
7690  O O   . GLN A 1042 ? 0.2805 0.2718 0.2486 0.0265  0.0008  0.0209  1040 GLN A O   
7691  C CB  . GLN A 1042 ? 0.2858 0.2781 0.2540 0.0265  0.0031  0.0275  1040 GLN A CB  
7692  C CG  . GLN A 1042 ? 0.3655 0.3582 0.3352 0.0264  0.0040  0.0322  1040 GLN A CG  
7693  C CD  . GLN A 1042 ? 0.4445 0.4337 0.4159 0.0249  0.0052  0.0316  1040 GLN A CD  
7694  O OE1 . GLN A 1042 ? 0.5567 0.5423 0.5322 0.0240  0.0049  0.0326  1040 GLN A OE1 
7695  N NE2 . GLN A 1042 ? 0.5036 0.4938 0.4722 0.0248  0.0063  0.0298  1040 GLN A NE2 
7696  N N   . HIS A 1043 ? 0.2446 0.2436 0.2070 0.0289  0.0003  0.0212  1041 HIS A N   
7697  C CA  . HIS A 1043 ? 0.2378 0.2363 0.1996 0.0286  -0.0005 0.0166  1041 HIS A CA  
7698  C C   . HIS A 1043 ? 0.2738 0.2725 0.2373 0.0290  -0.0020 0.0166  1041 HIS A C   
7699  O O   . HIS A 1043 ? 0.2809 0.2834 0.2427 0.0305  -0.0030 0.0172  1041 HIS A O   
7700  C CB  . HIS A 1043 ? 0.2393 0.2417 0.1971 0.0297  -0.0006 0.0143  1041 HIS A CB  
7701  C CG  . HIS A 1043 ? 0.2474 0.2492 0.2051 0.0293  -0.0017 0.0097  1041 HIS A CG  
7702  N ND1 . HIS A 1043 ? 0.2308 0.2297 0.1892 0.0279  -0.0012 0.0066  1041 HIS A ND1 
7703  C CD2 . HIS A 1043 ? 0.2527 0.2567 0.2100 0.0300  -0.0032 0.0077  1041 HIS A CD2 
7704  C CE1 . HIS A 1043 ? 0.2579 0.2571 0.2165 0.0277  -0.0025 0.0032  1041 HIS A CE1 
7705  N NE2 . HIS A 1043 ? 0.2644 0.2667 0.2223 0.0289  -0.0037 0.0036  1041 HIS A NE2 
7706  N N   . SER A 1044 ? 0.2427 0.2377 0.2097 0.0279  -0.0023 0.0158  1042 SER A N   
7707  C CA  . SER A 1044 ? 0.2446 0.2396 0.2137 0.0282  -0.0037 0.0152  1042 SER A CA  
7708  C C   . SER A 1044 ? 0.2447 0.2360 0.2170 0.0267  -0.0035 0.0131  1042 SER A C   
7709  O O   . SER A 1044 ? 0.2610 0.2496 0.2341 0.0255  -0.0024 0.0129  1042 SER A O   
7710  C CB  . SER A 1044 ? 0.2403 0.2365 0.2111 0.0294  -0.0044 0.0193  1042 SER A CB  
7711  O OG  . SER A 1044 ? 0.2473 0.2402 0.2214 0.0287  -0.0038 0.0217  1042 SER A OG  
7712  N N   . SER A 1045 ? 0.2264 0.2179 0.2007 0.0269  -0.0047 0.0116  1043 SER A N   
7713  C CA  . SER A 1045 ? 0.2422 0.2312 0.2197 0.0257  -0.0046 0.0097  1043 SER A CA  
7714  C C   . SER A 1045 ? 0.2248 0.2146 0.2052 0.0266  -0.0060 0.0096  1043 SER A C   
7715  O O   . SER A 1045 ? 0.2427 0.2352 0.2222 0.0275  -0.0071 0.0091  1043 SER A O   
7716  C CB  . SER A 1045 ? 0.2466 0.2355 0.2231 0.0243  -0.0042 0.0061  1043 SER A CB  
7717  O OG  . SER A 1045 ? 0.2495 0.2371 0.2290 0.0232  -0.0041 0.0044  1043 SER A OG  
7718  N N   . VAL A 1046 ? 0.2376 0.2252 0.2218 0.0263  -0.0061 0.0098  1044 VAL A N   
7719  C CA  . VAL A 1046 ? 0.2426 0.2309 0.2302 0.0273  -0.0075 0.0092  1044 VAL A CA  
7720  C C   . VAL A 1046 ? 0.2449 0.2344 0.2334 0.0265  -0.0076 0.0054  1044 VAL A C   
7721  O O   . VAL A 1046 ? 0.2830 0.2736 0.2743 0.0273  -0.0087 0.0044  1044 VAL A O   
7722  C CB  . VAL A 1046 ? 0.2713 0.2571 0.2635 0.0277  -0.0079 0.0107  1044 VAL A CB  
7723  C CG1 . VAL A 1046 ? 0.3121 0.2972 0.3043 0.0285  -0.0080 0.0152  1044 VAL A CG1 
7724  C CG2 . VAL A 1046 ? 0.2559 0.2395 0.2495 0.0263  -0.0067 0.0088  1044 VAL A CG2 
7725  N N   . HIS A 1047 ? 0.2424 0.2318 0.2289 0.0249  -0.0066 0.0034  1045 HIS A N   
7726  C CA  A HIS A 1047 ? 0.2471 0.2379 0.2346 0.0239  -0.0066 0.0003  1045 HIS A CA  
7727  C CA  B HIS A 1047 ? 0.2478 0.2385 0.2352 0.0238  -0.0065 0.0003  1045 HIS A CA  
7728  C C   . HIS A 1047 ? 0.2682 0.2617 0.2538 0.0240  -0.0074 -0.0010 1045 HIS A C   
7729  O O   . HIS A 1047 ? 0.2796 0.2736 0.2622 0.0242  -0.0074 -0.0003 1045 HIS A O   
7730  C CB  A HIS A 1047 ? 0.2707 0.2600 0.2576 0.0221  -0.0051 -0.0007 1045 HIS A CB  
7731  C CB  B HIS A 1047 ? 0.2695 0.2589 0.2560 0.0220  -0.0051 -0.0008 1045 HIS A CB  
7732  C CG  A HIS A 1047 ? 0.2796 0.2664 0.2683 0.0220  -0.0045 0.0004  1045 HIS A CG  
7733  C CG  B HIS A 1047 ? 0.2551 0.2464 0.2418 0.0206  -0.0050 -0.0033 1045 HIS A CG  
7734  N ND1 A HIS A 1047 ? 0.3283 0.3150 0.3207 0.0224  -0.0048 -0.0005 1045 HIS A ND1 
7735  N ND1 B HIS A 1047 ? 0.2675 0.2594 0.2519 0.0197  -0.0050 -0.0041 1045 HIS A ND1 
7736  C CD2 A HIS A 1047 ? 0.3208 0.3052 0.3083 0.0217  -0.0036 0.0023  1045 HIS A CD2 
7737  C CD2 B HIS A 1047 ? 0.2675 0.2606 0.2567 0.0199  -0.0050 -0.0053 1045 HIS A CD2 
7738  C CE1 A HIS A 1047 ? 0.3129 0.2971 0.3064 0.0223  -0.0043 0.0006  1045 HIS A CE1 
7739  C CE1 B HIS A 1047 ? 0.2815 0.2752 0.2672 0.0184  -0.0051 -0.0060 1045 HIS A CE1 
7740  N NE2 A HIS A 1047 ? 0.2928 0.2755 0.2834 0.0218  -0.0035 0.0025  1045 HIS A NE2 
7741  N NE2 B HIS A 1047 ? 0.2804 0.2752 0.2689 0.0184  -0.0050 -0.0066 1045 HIS A NE2 
7742  N N   . THR A 1048 ? 0.2441 0.2398 0.2318 0.0239  -0.0081 -0.0030 1046 THR A N   
7743  C CA  . THR A 1048 ? 0.2378 0.2364 0.2246 0.0239  -0.0091 -0.0045 1046 THR A CA  
7744  C C   . THR A 1048 ? 0.2541 0.2538 0.2420 0.0220  -0.0086 -0.0069 1046 THR A C   
7745  O O   . THR A 1048 ? 0.2709 0.2712 0.2614 0.0215  -0.0082 -0.0079 1046 THR A O   
7746  C CB  . THR A 1048 ? 0.2336 0.2344 0.2222 0.0256  -0.0106 -0.0045 1046 THR A CB  
7747  O OG1 . THR A 1048 ? 0.2683 0.2680 0.2566 0.0273  -0.0111 -0.0017 1046 THR A OG1 
7748  C CG2 . THR A 1048 ? 0.2655 0.2693 0.2528 0.0257  -0.0118 -0.0059 1046 THR A CG2 
7749  N N   . ASP A 1049 ? 0.2388 0.2390 0.2250 0.0210  -0.0087 -0.0079 1047 ASP A N   
7750  C CA  . ASP A 1049 ? 0.2236 0.2249 0.2112 0.0189  -0.0084 -0.0096 1047 ASP A CA  
7751  C C   . ASP A 1049 ? 0.2295 0.2343 0.2200 0.0190  -0.0092 -0.0111 1047 ASP A C   
7752  O O   . ASP A 1049 ? 0.2320 0.2386 0.2225 0.0203  -0.0106 -0.0115 1047 ASP A O   
7753  C CB  . ASP A 1049 ? 0.2078 0.2089 0.1937 0.0180  -0.0088 -0.0104 1047 ASP A CB  
7754  C CG  . ASP A 1049 ? 0.2411 0.2431 0.2290 0.0157  -0.0086 -0.0117 1047 ASP A CG  
7755  O OD1 . ASP A 1049 ? 0.2377 0.2427 0.2278 0.0153  -0.0096 -0.0130 1047 ASP A OD1 
7756  O OD2 . ASP A 1049 ? 0.2662 0.2663 0.2539 0.0143  -0.0076 -0.0112 1047 ASP A OD2 
7757  N N   . PRO A 1050 ? 0.2156 0.2218 0.2085 0.0178  -0.0085 -0.0119 1048 PRO A N   
7758  C CA  . PRO A 1050 ? 0.2234 0.2334 0.2192 0.0181  -0.0092 -0.0133 1048 PRO A CA  
7759  C C   . PRO A 1050 ? 0.2342 0.2470 0.2309 0.0170  -0.0101 -0.0146 1048 PRO A C   
7760  O O   . PRO A 1050 ? 0.2502 0.2662 0.2488 0.0177  -0.0111 -0.0156 1048 PRO A O   
7761  C CB  . PRO A 1050 ? 0.2615 0.2726 0.2593 0.0171  -0.0079 -0.0138 1048 PRO A CB  
7762  C CG  . PRO A 1050 ? 0.2809 0.2895 0.2769 0.0154  -0.0067 -0.0128 1048 PRO A CG  
7763  C CD  . PRO A 1050 ? 0.2529 0.2577 0.2459 0.0163  -0.0070 -0.0115 1048 PRO A CD  
7764  N N   . VAL A 1051 ? 0.2291 0.2407 0.2248 0.0152  -0.0099 -0.0145 1049 VAL A N   
7765  C CA  . VAL A 1051 ? 0.2268 0.2408 0.2239 0.0141  -0.0111 -0.0157 1049 VAL A CA  
7766  C C   . VAL A 1051 ? 0.2100 0.2239 0.2054 0.0158  -0.0127 -0.0162 1049 VAL A C   
7767  O O   . VAL A 1051 ? 0.2432 0.2601 0.2402 0.0159  -0.0140 -0.0175 1049 VAL A O   
7768  C CB  . VAL A 1051 ? 0.2488 0.2612 0.2460 0.0117  -0.0106 -0.0155 1049 VAL A CB  
7769  C CG1 . VAL A 1051 ? 0.2694 0.2840 0.2687 0.0104  -0.0121 -0.0167 1049 VAL A CG1 
7770  C CG2 . VAL A 1051 ? 0.2676 0.2809 0.2663 0.0100  -0.0090 -0.0147 1049 VAL A CG2 
7771  N N   . LEU A 1052 ? 0.2160 0.2270 0.2082 0.0172  -0.0126 -0.0152 1050 LEU A N   
7772  C CA  . LEU A 1052 ? 0.2180 0.2298 0.2083 0.0192  -0.0140 -0.0154 1050 LEU A CA  
7773  C C   . LEU A 1052 ? 0.2262 0.2407 0.2182 0.0207  -0.0148 -0.0154 1050 LEU A C   
7774  O O   . LEU A 1052 ? 0.2208 0.2380 0.2133 0.0215  -0.0164 -0.0165 1050 LEU A O   
7775  C CB  . LEU A 1052 ? 0.2343 0.2433 0.2211 0.0205  -0.0134 -0.0137 1050 LEU A CB  
7776  C CG  . LEU A 1052 ? 0.2188 0.2289 0.2030 0.0228  -0.0146 -0.0131 1050 LEU A CG  
7777  C CD1 . LEU A 1052 ? 0.2381 0.2494 0.2233 0.0246  -0.0150 -0.0117 1050 LEU A CD1 
7778  C CD2 . LEU A 1052 ? 0.2289 0.2417 0.2130 0.0228  -0.0163 -0.0154 1050 LEU A CD2 
7779  N N   . LEU A 1053 ? 0.2269 0.2407 0.2201 0.0213  -0.0139 -0.0144 1051 LEU A N   
7780  C CA  . LEU A 1053 ? 0.2333 0.2495 0.2287 0.0230  -0.0148 -0.0145 1051 LEU A CA  
7781  C C   . LEU A 1053 ? 0.2082 0.2284 0.2066 0.0220  -0.0155 -0.0165 1051 LEU A C   
7782  O O   . LEU A 1053 ? 0.2384 0.2612 0.2379 0.0234  -0.0170 -0.0171 1051 LEU A O   
7783  C CB  . LEU A 1053 ? 0.2474 0.2621 0.2443 0.0236  -0.0138 -0.0136 1051 LEU A CB  
7784  C CG  . LEU A 1053 ? 0.2589 0.2701 0.2537 0.0249  -0.0135 -0.0112 1051 LEU A CG  
7785  C CD1 . LEU A 1053 ? 0.2637 0.2732 0.2607 0.0253  -0.0126 -0.0108 1051 LEU A CD1 
7786  C CD2 . LEU A 1053 ? 0.2557 0.2677 0.2497 0.0271  -0.0150 -0.0099 1051 LEU A CD2 
7787  N N   . ASP A 1054 ? 0.2280 0.2491 0.2280 0.0198  -0.0146 -0.0174 1052 ASP A N   
7788  C CA  . ASP A 1054 ? 0.2394 0.2648 0.2426 0.0186  -0.0152 -0.0190 1052 ASP A CA  
7789  C C   . ASP A 1054 ? 0.2275 0.2540 0.2302 0.0184  -0.0169 -0.0199 1052 ASP A C   
7790  O O   . ASP A 1054 ? 0.2457 0.2758 0.2506 0.0188  -0.0181 -0.0211 1052 ASP A O   
7791  C CB  . ASP A 1054 ? 0.2334 0.2598 0.2383 0.0160  -0.0138 -0.0191 1052 ASP A CB  
7792  C CG  . ASP A 1054 ? 0.3199 0.3467 0.3258 0.0163  -0.0123 -0.0189 1052 ASP A CG  
7793  O OD1 . ASP A 1054 ? 0.2784 0.3051 0.2846 0.0185  -0.0126 -0.0190 1052 ASP A OD1 
7794  O OD2 . ASP A 1054 ? 0.3323 0.3597 0.3388 0.0143  -0.0110 -0.0186 1052 ASP A OD2 
7795  N N   . PHE A 1055 ? 0.2053 0.2289 0.2054 0.0180  -0.0170 -0.0197 1053 PHE A N   
7796  C CA  . PHE A 1055 ? 0.2429 0.2676 0.2426 0.0180  -0.0188 -0.0210 1053 PHE A CA  
7797  C C   . PHE A 1055 ? 0.2286 0.2549 0.2269 0.0206  -0.0203 -0.0211 1053 PHE A C   
7798  O O   . PHE A 1055 ? 0.2420 0.2714 0.2417 0.0209  -0.0220 -0.0226 1053 PHE A O   
7799  C CB  . PHE A 1055 ? 0.2184 0.2397 0.2154 0.0173  -0.0186 -0.0210 1053 PHE A CB  
7800  C CG  . PHE A 1055 ? 0.2101 0.2325 0.2068 0.0175  -0.0206 -0.0229 1053 PHE A CG  
7801  C CD1 . PHE A 1055 ? 0.2777 0.3026 0.2780 0.0159  -0.0219 -0.0246 1053 PHE A CD1 
7802  C CD2 . PHE A 1055 ? 0.2316 0.2528 0.2246 0.0192  -0.0212 -0.0231 1053 PHE A CD2 
7803  C CE1 . PHE A 1055 ? 0.2885 0.3144 0.2889 0.0161  -0.0239 -0.0268 1053 PHE A CE1 
7804  C CE2 . PHE A 1055 ? 0.2542 0.2768 0.2468 0.0196  -0.0231 -0.0253 1053 PHE A CE2 
7805  C CZ  . PHE A 1055 ? 0.2425 0.2673 0.2390 0.0180  -0.0246 -0.0274 1053 PHE A CZ  
7806  N N   . ALA A 1056 ? 0.2386 0.2630 0.2344 0.0226  -0.0198 -0.0193 1054 ALA A N   
7807  C CA  . ALA A 1056 ? 0.2383 0.2645 0.2331 0.0251  -0.0212 -0.0187 1054 ALA A CA  
7808  C C   . ALA A 1056 ? 0.2635 0.2932 0.2618 0.0257  -0.0221 -0.0195 1054 ALA A C   
7809  O O   . ALA A 1056 ? 0.2536 0.2861 0.2521 0.0270  -0.0238 -0.0201 1054 ALA A O   
7810  C CB  . ALA A 1056 ? 0.2570 0.2805 0.2493 0.0268  -0.0204 -0.0161 1054 ALA A CB  
7811  N N   . LYS A 1057 ? 0.2577 0.2876 0.2589 0.0249  -0.0209 -0.0196 1055 LYS A N   
7812  C CA  . LYS A 1057 ? 0.2752 0.3089 0.2800 0.0255  -0.0217 -0.0207 1055 LYS A CA  
7813  C C   . LYS A 1057 ? 0.2704 0.3077 0.2773 0.0240  -0.0227 -0.0227 1055 LYS A C   
7814  O O   . LYS A 1057 ? 0.3243 0.3651 0.3331 0.0250  -0.0242 -0.0236 1055 LYS A O   
7815  C CB  . LYS A 1057 ? 0.3488 0.3827 0.3563 0.0250  -0.0201 -0.0207 1055 LYS A CB  
7816  C CG  . LYS A 1057 ? 0.3196 0.3509 0.3269 0.0270  -0.0198 -0.0192 1055 LYS A CG  
7817  C CD  . LYS A 1057 ? 0.3126 0.3452 0.3232 0.0268  -0.0187 -0.0202 1055 LYS A CD  
7818  C CE  . LYS A 1057 ? 0.3185 0.3508 0.3288 0.0243  -0.0168 -0.0206 1055 LYS A CE  
7819  N NZ  . LYS A 1057 ? 0.3562 0.3890 0.3688 0.0246  -0.0156 -0.0212 1055 LYS A NZ  
7820  N N   . TRP A 1058 ? 0.2570 0.2935 0.2640 0.0215  -0.0221 -0.0233 1056 TRP A N   
7821  C CA  . TRP A 1058 ? 0.2665 0.3061 0.2760 0.0198  -0.0232 -0.0250 1056 TRP A CA  
7822  C C   . TRP A 1058 ? 0.2909 0.3314 0.2989 0.0211  -0.0254 -0.0260 1056 TRP A C   
7823  O O   . TRP A 1058 ? 0.3350 0.3793 0.3455 0.0211  -0.0270 -0.0275 1056 TRP A O   
7824  C CB  . TRP A 1058 ? 0.2669 0.3047 0.2769 0.0169  -0.0223 -0.0250 1056 TRP A CB  
7825  C CG  . TRP A 1058 ? 0.2883 0.3286 0.3015 0.0149  -0.0236 -0.0266 1056 TRP A CG  
7826  C CD1 . TRP A 1058 ? 0.3143 0.3586 0.3319 0.0130  -0.0236 -0.0270 1056 TRP A CD1 
7827  C CD2 . TRP A 1058 ? 0.3272 0.3665 0.3397 0.0145  -0.0253 -0.0279 1056 TRP A CD2 
7828  N NE1 . TRP A 1058 ? 0.3379 0.3834 0.3580 0.0113  -0.0252 -0.0282 1056 TRP A NE1 
7829  C CE2 . TRP A 1058 ? 0.3373 0.3795 0.3543 0.0123  -0.0264 -0.0291 1056 TRP A CE2 
7830  C CE3 . TRP A 1058 ? 0.2933 0.3297 0.3019 0.0159  -0.0261 -0.0284 1056 TRP A CE3 
7831  C CZ2 . TRP A 1058 ? 0.3454 0.3874 0.3636 0.0114  -0.0284 -0.0309 1056 TRP A CZ2 
7832  C CZ3 . TRP A 1058 ? 0.3410 0.3776 0.3504 0.0152  -0.0280 -0.0304 1056 TRP A CZ3 
7833  C CH2 . TRP A 1058 ? 0.3713 0.4104 0.3856 0.0130  -0.0293 -0.0318 1056 TRP A CH2 
7834  N N   . LEU A 1059 ? 0.2577 0.2952 0.2616 0.0222  -0.0256 -0.0254 1057 LEU A N   
7835  C CA  . LEU A 1059 ? 0.2863 0.3253 0.2881 0.0238  -0.0276 -0.0263 1057 LEU A CA  
7836  C C   . LEU A 1059 ? 0.3249 0.3671 0.3275 0.0261  -0.0289 -0.0260 1057 LEU A C   
7837  O O   . LEU A 1059 ? 0.3486 0.3942 0.3520 0.0267  -0.0309 -0.0276 1057 LEU A O   
7838  C CB  . LEU A 1059 ? 0.2842 0.3202 0.2813 0.0250  -0.0273 -0.0252 1057 LEU A CB  
7839  C CG  . LEU A 1059 ? 0.2663 0.2994 0.2623 0.0233  -0.0267 -0.0261 1057 LEU A CG  
7840  C CD1 . LEU A 1059 ? 0.2520 0.2824 0.2434 0.0247  -0.0258 -0.0246 1057 LEU A CD1 
7841  C CD2 . LEU A 1059 ? 0.2967 0.3319 0.2940 0.0226  -0.0288 -0.0291 1057 LEU A CD2 
7842  N N   . ASP A 1060 ? 0.3221 0.3634 0.3246 0.0275  -0.0279 -0.0240 1058 ASP A N   
7843  C CA  . ASP A 1060 ? 0.3683 0.4123 0.3720 0.0298  -0.0293 -0.0235 1058 ASP A CA  
7844  C C   . ASP A 1060 ? 0.3679 0.4160 0.3762 0.0289  -0.0300 -0.0254 1058 ASP A C   
7845  O O   . ASP A 1060 ? 0.4100 0.4616 0.4194 0.0303  -0.0319 -0.0261 1058 ASP A O   
7846  C CB  . ASP A 1060 ? 0.3997 0.4415 0.4035 0.0313  -0.0282 -0.0211 1058 ASP A CB  
7847  C CG  . ASP A 1060 ? 0.3941 0.4341 0.3942 0.0333  -0.0286 -0.0186 1058 ASP A CG  
7848  O OD1 . ASP A 1060 ? 0.4472 0.4895 0.4452 0.0345  -0.0302 -0.0187 1058 ASP A OD1 
7849  O OD2 . ASP A 1060 ? 0.4523 0.4890 0.4516 0.0337  -0.0273 -0.0165 1058 ASP A OD2 
7850  N N   . GLY A 1061 ? 0.3447 0.3929 0.3557 0.0266  -0.0286 -0.0262 1059 GLY A N   
7851  C CA  . GLY A 1061 ? 0.3682 0.4210 0.3838 0.0256  -0.0292 -0.0279 1059 GLY A CA  
7852  C C   . GLY A 1061 ? 0.4432 0.4984 0.4598 0.0244  -0.0310 -0.0298 1059 GLY A C   
7853  O O   . GLY A 1061 ? 0.4092 0.4688 0.4292 0.0244  -0.0322 -0.0311 1059 GLY A O   
7854  N N   . LYS A 1062 ? 0.3752 0.4279 0.3892 0.0235  -0.0313 -0.0302 1060 LYS A N   
7855  C CA  . LYS A 1062 ? 0.3587 0.4134 0.3737 0.0226  -0.0333 -0.0323 1060 LYS A CA  
7856  C C   . LYS A 1062 ? 0.4096 0.4660 0.4221 0.0252  -0.0355 -0.0330 1060 LYS A C   
7857  O O   . LYS A 1062 ? 0.4762 0.5349 0.4897 0.0248  -0.0376 -0.0352 1060 LYS A O   
7858  C CB  . LYS A 1062 ? 0.4048 0.4560 0.4185 0.0206  -0.0329 -0.0329 1060 LYS A CB  
7859  C CG  . LYS A 1062 ? 0.4620 0.5123 0.4790 0.0175  -0.0313 -0.0324 1060 LYS A CG  
7860  C CD  . LYS A 1062 ? 0.5043 0.5588 0.5268 0.0155  -0.0324 -0.0338 1060 LYS A CD  
7861  C CE  . LYS A 1062 ? 0.5757 0.6299 0.6015 0.0123  -0.0308 -0.0327 1060 LYS A CE  
7862  N NZ  . LYS A 1062 ? 0.5450 0.6037 0.5766 0.0100  -0.0317 -0.0335 1060 LYS A NZ  
7863  N N   . GLY A 1063 ? 0.3541 0.4099 0.3638 0.0278  -0.0353 -0.0311 1061 GLY A N   
7864  C CA  . GLY A 1063 ? 0.4057 0.4636 0.4127 0.0304  -0.0373 -0.0311 1061 GLY A CA  
7865  C C   . GLY A 1063 ? 0.4281 0.4838 0.4300 0.0312  -0.0374 -0.0307 1061 GLY A C   
7866  O O   . GLY A 1063 ? 0.3988 0.4569 0.3980 0.0334  -0.0390 -0.0306 1061 GLY A O   
7867  N N   . ALA A 1064 ? 0.3586 0.4103 0.3592 0.0296  -0.0357 -0.0304 1062 ALA A N   
7868  C CA  . ALA A 1064 ? 0.3287 0.3785 0.3247 0.0303  -0.0356 -0.0303 1062 ALA A CA  
7869  C C   . ALA A 1064 ? 0.3858 0.4336 0.3783 0.0322  -0.0342 -0.0269 1062 ALA A C   
7870  O O   . ALA A 1064 ? 0.3020 0.3459 0.2930 0.0316  -0.0323 -0.0254 1062 ALA A O   
7871  C CB  . ALA A 1064 ? 0.3431 0.3896 0.3398 0.0278  -0.0345 -0.0317 1062 ALA A CB  
7872  N N   . ARG A 1065 ? 0.3377 0.3884 0.3294 0.0346  -0.0354 -0.0254 1063 ARG A N   
7873  C CA  . ARG A 1065 ? 0.3360 0.3851 0.3259 0.0364  -0.0345 -0.0216 1063 ARG A CA  
7874  C C   . ARG A 1065 ? 0.3376 0.3852 0.3227 0.0371  -0.0337 -0.0200 1063 ARG A C   
7875  O O   . ARG A 1065 ? 0.3210 0.3651 0.3051 0.0372  -0.0319 -0.0173 1063 ARG A O   
7876  C CB  . ARG A 1065 ? 0.3969 0.4498 0.3876 0.0387  -0.0363 -0.0203 1063 ARG A CB  
7877  N N   . ALA A 1066 ? 0.3186 0.3690 0.3007 0.0379  -0.0350 -0.0218 1064 ALA A N   
7878  C CA  . ALA A 1066 ? 0.2977 0.3473 0.2751 0.0387  -0.0341 -0.0205 1064 ALA A CA  
7879  C C   . ALA A 1066 ? 0.2996 0.3444 0.2772 0.0366  -0.0321 -0.0212 1064 ALA A C   
7880  O O   . ALA A 1066 ? 0.2845 0.3269 0.2597 0.0369  -0.0304 -0.0187 1064 ALA A O   
7881  C CB  . ALA A 1066 ? 0.3351 0.3894 0.3095 0.0400  -0.0361 -0.0230 1064 ALA A CB  
7882  N N   . GLU A 1067 ? 0.3006 0.3442 0.2811 0.0344  -0.0322 -0.0243 1065 GLU A N   
7883  C CA  . GLU A 1067 ? 0.3001 0.3393 0.2810 0.0323  -0.0304 -0.0248 1065 GLU A CA  
7884  C C   . GLU A 1067 ? 0.2698 0.3054 0.2523 0.0315  -0.0283 -0.0219 1065 GLU A C   
7885  O O   . GLU A 1067 ? 0.2693 0.3014 0.2505 0.0307  -0.0265 -0.0207 1065 GLU A O   
7886  C CB  . GLU A 1067 ? 0.2642 0.3031 0.2486 0.0300  -0.0312 -0.0283 1065 GLU A CB  
7887  C CG  . GLU A 1067 ? 0.2618 0.3032 0.2450 0.0305  -0.0333 -0.0318 1065 GLU A CG  
7888  C CD  . GLU A 1067 ? 0.3576 0.4042 0.3410 0.0321  -0.0357 -0.0333 1065 GLU A CD  
7889  O OE1 . GLU A 1067 ? 0.3202 0.3684 0.3052 0.0327  -0.0360 -0.0317 1065 GLU A OE1 
7890  O OE2 . GLU A 1067 ? 0.3790 0.4282 0.3610 0.0330  -0.0376 -0.0363 1065 GLU A OE2 
7891  N N   . ALA A 1068 ? 0.2916 0.3282 0.2770 0.0317  -0.0285 -0.0210 1066 ALA A N   
7892  C CA  . ALA A 1068 ? 0.2733 0.3070 0.2604 0.0313  -0.0268 -0.0187 1066 ALA A CA  
7893  C C   . ALA A 1068 ? 0.2911 0.3231 0.2752 0.0329  -0.0259 -0.0153 1066 ALA A C   
7894  O O   . ALA A 1068 ? 0.2603 0.2887 0.2444 0.0322  -0.0241 -0.0138 1066 ALA A O   
7895  C CB  . ALA A 1068 ? 0.2979 0.3338 0.2889 0.0317  -0.0275 -0.0189 1066 ALA A CB  
7896  N N   . GLU A 1069 ? 0.2777 0.3126 0.2596 0.0352  -0.0272 -0.0139 1067 GLU A N   
7897  C CA  . GLU A 1069 ? 0.2930 0.3269 0.2721 0.0367  -0.0265 -0.0103 1067 GLU A CA  
7898  C C   . GLU A 1069 ? 0.3153 0.3472 0.2911 0.0359  -0.0251 -0.0103 1067 GLU A C   
7899  O O   . GLU A 1069 ? 0.3019 0.3307 0.2769 0.0358  -0.0235 -0.0077 1067 GLU A O   
7900  C CB  . GLU A 1069 ? 0.3164 0.3548 0.2935 0.0391  -0.0284 -0.0087 1067 GLU A CB  
7901  C CG  . GLU A 1069 ? 0.3979 0.4367 0.3715 0.0406  -0.0278 -0.0049 1067 GLU A CG  
7902  C CD  . GLU A 1069 ? 0.6144 0.6508 0.5903 0.0413  -0.0273 -0.0007 1067 GLU A CD  
7903  O OE1 . GLU A 1069 ? 0.6421 0.6759 0.6221 0.0405  -0.0270 -0.0013 1067 GLU A OE1 
7904  O OE2 . GLU A 1069 ? 0.7388 0.7763 0.7127 0.0427  -0.0272 0.0032  1067 GLU A OE2 
7905  N N   . ALA A 1070 ? 0.3093 0.3428 0.2834 0.0354  -0.0258 -0.0134 1068 ALA A N   
7906  C CA  . ALA A 1070 ? 0.2650 0.2968 0.2364 0.0348  -0.0246 -0.0140 1068 ALA A CA  
7907  C C   . ALA A 1070 ? 0.2424 0.2692 0.2158 0.0326  -0.0227 -0.0141 1068 ALA A C   
7908  O O   . ALA A 1070 ? 0.2768 0.3011 0.2484 0.0323  -0.0212 -0.0127 1068 ALA A O   
7909  C CB  . ALA A 1070 ? 0.2917 0.3261 0.2618 0.0348  -0.0261 -0.0180 1068 ALA A CB  
7910  N N   . ALA A 1071 ? 0.2529 0.2787 0.2301 0.0310  -0.0228 -0.0156 1069 ALA A N   
7911  C CA  . ALA A 1071 ? 0.2142 0.2362 0.1935 0.0289  -0.0211 -0.0155 1069 ALA A CA  
7912  C C   . ALA A 1071 ? 0.2693 0.2888 0.2487 0.0294  -0.0196 -0.0122 1069 ALA A C   
7913  O O   . ALA A 1071 ? 0.2451 0.2614 0.2237 0.0286  -0.0180 -0.0112 1069 ALA A O   
7914  C CB  . ALA A 1071 ? 0.2250 0.2477 0.2085 0.0272  -0.0215 -0.0176 1069 ALA A CB  
7915  N N   . ARG A 1072 ? 0.2544 0.2754 0.2350 0.0309  -0.0204 -0.0106 1070 ARG A N   
7916  C CA  . ARG A 1072 ? 0.2475 0.2661 0.2290 0.0316  -0.0193 -0.0075 1070 ARG A CA  
7917  C C   . ARG A 1072 ? 0.2415 0.2590 0.2194 0.0324  -0.0185 -0.0049 1070 ARG A C   
7918  O O   . ARG A 1072 ? 0.2682 0.2825 0.2464 0.0319  -0.0171 -0.0031 1070 ARG A O   
7919  C CB  . ARG A 1072 ? 0.2536 0.2741 0.2375 0.0332  -0.0207 -0.0062 1070 ARG A CB  
7920  C CG  . ARG A 1072 ? 0.2955 0.3165 0.2836 0.0324  -0.0209 -0.0084 1070 ARG A CG  
7921  C CD  . ARG A 1072 ? 0.3357 0.3581 0.3267 0.0342  -0.0221 -0.0071 1070 ARG A CD  
7922  N NE  . ARG A 1072 ? 0.3702 0.3963 0.3598 0.0358  -0.0240 -0.0067 1070 ARG A NE  
7923  C CZ  . ARG A 1072 ? 0.3714 0.4008 0.3621 0.0359  -0.0254 -0.0091 1070 ARG A CZ  
7924  N NH1 . ARG A 1072 ? 0.3814 0.4113 0.3749 0.0343  -0.0251 -0.0119 1070 ARG A NH1 
7925  N NH2 . ARG A 1072 ? 0.3966 0.4296 0.3859 0.0375  -0.0272 -0.0085 1070 ARG A NH2 
7926  N N   . ASN A 1073 ? 0.2566 0.2772 0.2313 0.0337  -0.0195 -0.0047 1071 ASN A N   
7927  C CA  . ASN A 1073 ? 0.2597 0.2804 0.2310 0.0346  -0.0187 -0.0023 1071 ASN A CA  
7928  C C   . ASN A 1073 ? 0.2909 0.3086 0.2608 0.0330  -0.0171 -0.0036 1071 ASN A C   
7929  O O   . ASN A 1073 ? 0.2931 0.3089 0.2619 0.0330  -0.0157 -0.0012 1071 ASN A O   
7930  C CB  . ASN A 1073 ? 0.2970 0.3226 0.2649 0.0364  -0.0202 -0.0023 1071 ASN A CB  
7931  C CG  . ASN A 1073 ? 0.3759 0.4044 0.3447 0.0382  -0.0216 0.0004  1071 ASN A CG  
7932  O OD1 . ASN A 1073 ? 0.4154 0.4416 0.3869 0.0384  -0.0213 0.0031  1071 ASN A OD1 
7933  N ND2 . ASN A 1073 ? 0.3926 0.4259 0.3592 0.0397  -0.0232 -0.0004 1071 ASN A ND2 
7934  N N   . ALA A 1074 ? 0.2522 0.2698 0.2227 0.0316  -0.0174 -0.0073 1072 ALA A N   
7935  C CA  . ALA A 1074 ? 0.2534 0.2680 0.2234 0.0300  -0.0161 -0.0085 1072 ALA A CA  
7936  C C   . ALA A 1074 ? 0.2440 0.2546 0.2163 0.0287  -0.0144 -0.0070 1072 ALA A C   
7937  O O   . ALA A 1074 ? 0.2482 0.2563 0.2194 0.0281  -0.0130 -0.0059 1072 ALA A O   
7938  C CB  . ALA A 1074 ? 0.2793 0.2943 0.2506 0.0286  -0.0170 -0.0125 1072 ALA A CB  
7939  N N   . GLY A 1075 ? 0.2372 0.2475 0.2128 0.0282  -0.0147 -0.0070 1073 GLY A N   
7940  C CA  . GLY A 1075 ? 0.2286 0.2357 0.2065 0.0271  -0.0133 -0.0060 1073 GLY A CA  
7941  C C   . GLY A 1075 ? 0.2626 0.2679 0.2396 0.0281  -0.0124 -0.0026 1073 GLY A C   
7942  O O   . GLY A 1075 ? 0.2688 0.2711 0.2460 0.0271  -0.0110 -0.0019 1073 GLY A O   
7943  N N   . SER A 1076 ? 0.2422 0.2495 0.2183 0.0300  -0.0133 -0.0003 1074 SER A N   
7944  C CA  . SER A 1076 ? 0.2620 0.2680 0.2377 0.0309  -0.0127 0.0034  1074 SER A CA  
7945  C C   . SER A 1076 ? 0.2776 0.2836 0.2496 0.0309  -0.0116 0.0044  1074 SER A C   
7946  O O   . SER A 1076 ? 0.3065 0.3101 0.2787 0.0306  -0.0104 0.0066  1074 SER A O   
7947  C CB  . SER A 1076 ? 0.2888 0.2973 0.2649 0.0329  -0.0141 0.0060  1074 SER A CB  
7948  O OG  . SER A 1076 ? 0.3900 0.3982 0.3701 0.0331  -0.0151 0.0054  1074 SER A OG  
7949  N N   . SER A 1077 ? 0.2593 0.2682 0.2282 0.0314  -0.0122 0.0027  1075 SER A N   
7950  C CA  A SER A 1077 ? 0.2851 0.2949 0.2506 0.0318  -0.0114 0.0033  1075 SER A CA  
7951  C CA  B SER A 1077 ? 0.2851 0.2950 0.2505 0.0318  -0.0114 0.0032  1075 SER A CA  
7952  C C   . SER A 1077 ? 0.2953 0.3016 0.2609 0.0300  -0.0100 0.0015  1075 SER A C   
7953  O O   . SER A 1077 ? 0.3006 0.3065 0.2642 0.0301  -0.0088 0.0028  1075 SER A O   
7954  C CB  A SER A 1077 ? 0.2830 0.2973 0.2454 0.0330  -0.0126 0.0012  1075 SER A CB  
7955  C CB  B SER A 1077 ? 0.2820 0.2963 0.2446 0.0329  -0.0127 0.0009  1075 SER A CB  
7956  O OG  A SER A 1077 ? 0.3234 0.3416 0.2850 0.0349  -0.0138 0.0036  1075 SER A OG  
7957  O OG  B SER A 1077 ? 0.3242 0.3398 0.2835 0.0334  -0.0120 0.0004  1075 SER A OG  
7958  N N   . SER A 1078 ? 0.2494 0.2536 0.2174 0.0284  -0.0100 -0.0010 1076 SER A N   
7959  C CA  . SER A 1078 ? 0.2460 0.2472 0.2145 0.0266  -0.0088 -0.0024 1076 SER A CA  
7960  C C   . SER A 1078 ? 0.2682 0.2665 0.2372 0.0263  -0.0072 0.0004  1076 SER A C   
7961  O O   . SER A 1078 ? 0.2592 0.2567 0.2302 0.0266  -0.0072 0.0025  1076 SER A O   
7962  C CB  . SER A 1078 ? 0.2243 0.2243 0.1958 0.0249  -0.0091 -0.0047 1076 SER A CB  
7963  O OG  . SER A 1078 ? 0.2190 0.2162 0.1911 0.0232  -0.0079 -0.0054 1076 SER A OG  
7964  N N   . ALA A 1079 ? 0.2116 0.2084 0.1792 0.0256  -0.0061 0.0003  1077 ALA A N   
7965  C CA  . ALA A 1079 ? 0.2493 0.2433 0.2178 0.0250  -0.0046 0.0026  1077 ALA A CA  
7966  C C   . ALA A 1079 ? 0.2319 0.2228 0.2024 0.0230  -0.0039 0.0010  1077 ALA A C   
7967  O O   . ALA A 1079 ? 0.2387 0.2272 0.2096 0.0223  -0.0027 0.0022  1077 ALA A O   
7968  C CB  . ALA A 1079 ? 0.2416 0.2362 0.2072 0.0258  -0.0037 0.0041  1077 ALA A CB  
7969  N N   . LEU A 1080 ? 0.2023 0.1937 0.1742 0.0220  -0.0047 -0.0016 1078 LEU A N   
7970  C CA  . LEU A 1080 ? 0.2108 0.2002 0.1849 0.0201  -0.0041 -0.0027 1078 LEU A CA  
7971  C C   . LEU A 1080 ? 0.2298 0.2177 0.2059 0.0200  -0.0033 -0.0010 1078 LEU A C   
7972  O O   . LEU A 1080 ? 0.2398 0.2286 0.2171 0.0210  -0.0040 -0.0002 1078 LEU A O   
7973  C CB  . LEU A 1080 ? 0.2121 0.2031 0.1879 0.0193  -0.0051 -0.0049 1078 LEU A CB  
7974  C CG  . LEU A 1080 ? 0.2176 0.2078 0.1960 0.0173  -0.0046 -0.0058 1078 LEU A CG  
7975  C CD1 . LEU A 1080 ? 0.2809 0.2693 0.2590 0.0158  -0.0040 -0.0063 1078 LEU A CD1 
7976  C CD2 . LEU A 1080 ? 0.2336 0.2264 0.2141 0.0168  -0.0057 -0.0075 1078 LEU A CD2 
7977  N N   . GLY A 1081 ? 0.2175 0.2032 0.1942 0.0188  -0.0022 -0.0006 1079 GLY A N   
7978  C CA  . GLY A 1081 ? 0.2593 0.2436 0.2380 0.0187  -0.0016 0.0006  1079 GLY A CA  
7979  C C   . GLY A 1081 ? 0.2275 0.2102 0.2056 0.0195  -0.0009 0.0032  1079 GLY A C   
7980  O O   . GLY A 1081 ? 0.2518 0.2330 0.2320 0.0193  -0.0005 0.0040  1079 GLY A O   
7981  N N   . LEU A 1082 ? 0.2125 0.1959 0.1880 0.0204  -0.0009 0.0044  1080 LEU A N   
7982  C CA  A LEU A 1082 ? 0.2192 0.2015 0.1941 0.0209  0.0000  0.0070  1080 LEU A CA  
7983  C CA  B LEU A 1082 ? 0.2193 0.2015 0.1941 0.0209  0.0000  0.0070  1080 LEU A CA  
7984  C C   . LEU A 1082 ? 0.2215 0.2012 0.1972 0.0195  0.0011  0.0069  1080 LEU A C   
7985  O O   . LEU A 1082 ? 0.2374 0.2166 0.2125 0.0183  0.0015  0.0051  1080 LEU A O   
7986  C CB  A LEU A 1082 ? 0.2288 0.2129 0.2002 0.0219  0.0001  0.0077  1080 LEU A CB  
7987  C CB  B LEU A 1082 ? 0.2287 0.2129 0.2002 0.0219  0.0001  0.0077  1080 LEU A CB  
7988  C CG  A LEU A 1082 ? 0.2302 0.2142 0.2007 0.0225  0.0011  0.0107  1080 LEU A CG  
7989  C CG  B LEU A 1082 ? 0.2305 0.2146 0.2009 0.0225  0.0011  0.0106  1080 LEU A CG  
7990  C CD1 A LEU A 1082 ? 0.2406 0.2245 0.2134 0.0232  0.0007  0.0138  1080 LEU A CD1 
7991  C CD1 B LEU A 1082 ? 0.2388 0.2265 0.2062 0.0241  0.0008  0.0115  1080 LEU A CD1 
7992  C CD2 A LEU A 1082 ? 0.2405 0.2276 0.2075 0.0237  0.0011  0.0107  1080 LEU A CD2 
7993  C CD2 B LEU A 1082 ? 0.2222 0.2044 0.1921 0.0213  0.0023  0.0098  1080 LEU A CD2 
7994  N N   . ASP A 1083 ? 0.2352 0.2133 0.2127 0.0196  0.0016  0.0089  1081 ASP A N   
7995  C CA  . ASP A 1083 ? 0.2518 0.2278 0.2306 0.0183  0.0025  0.0087  1081 ASP A CA  
7996  C C   . ASP A 1083 ? 0.2764 0.2511 0.2560 0.0188  0.0031  0.0117  1081 ASP A C   
7997  O O   . ASP A 1083 ? 0.3325 0.3065 0.3150 0.0192  0.0025  0.0130  1081 ASP A O   
7998  C CB  . ASP A 1083 ? 0.3022 0.2778 0.2839 0.0176  0.0021  0.0069  1081 ASP A CB  
7999  C CG  . ASP A 1083 ? 0.4532 0.4272 0.4359 0.0163  0.0030  0.0063  1081 ASP A CG  
8000  O OD1 . ASP A 1083 ? 0.4717 0.4447 0.4529 0.0158  0.0039  0.0071  1081 ASP A OD1 
8001  O OD2 . ASP A 1083 ? 0.4714 0.4457 0.4564 0.0158  0.0027  0.0048  1081 ASP A OD2 
8002  N N   . LEU A 1084 ? 0.2523 0.2270 0.2298 0.0186  0.0040  0.0127  1082 LEU A N   
8003  C CA  . LEU A 1084 ? 0.2394 0.2138 0.2174 0.0191  0.0046  0.0159  1082 LEU A CA  
8004  C C   . LEU A 1084 ? 0.2531 0.2256 0.2316 0.0180  0.0057  0.0159  1082 LEU A C   
8005  O O   . LEU A 1084 ? 0.2830 0.2551 0.2603 0.0171  0.0061  0.0138  1082 LEU A O   
8006  C CB  . LEU A 1084 ? 0.2600 0.2372 0.2349 0.0203  0.0049  0.0175  1082 LEU A CB  
8007  C CG  . LEU A 1084 ? 0.3031 0.2828 0.2770 0.0216  0.0038  0.0179  1082 LEU A CG  
8008  C CD1 . LEU A 1084 ? 0.3040 0.2871 0.2744 0.0228  0.0042  0.0190  1082 LEU A CD1 
8009  C CD2 . LEU A 1084 ? 0.3176 0.2967 0.2948 0.0221  0.0030  0.0205  1082 LEU A CD2 
8010  N N   . GLU A 1085 ? 0.2870 0.2585 0.2677 0.0179  0.0060  0.0185  1083 GLU A N   
8011  C CA  . GLU A 1085 ? 0.2589 0.2292 0.2399 0.0171  0.0071  0.0192  1083 GLU A CA  
8012  C C   . GLU A 1085 ? 0.2807 0.2530 0.2601 0.0179  0.0078  0.0221  1083 GLU A C   
8013  O O   . GLU A 1085 ? 0.3174 0.2908 0.2978 0.0187  0.0075  0.0251  1083 GLU A O   
8014  C CB  . GLU A 1085 ? 0.2523 0.2202 0.2374 0.0164  0.0068  0.0197  1083 GLU A CB  
8015  C CG  . GLU A 1085 ? 0.3080 0.2750 0.2934 0.0156  0.0079  0.0207  1083 GLU A CG  
8016  C CD  . GLU A 1085 ? 0.3855 0.3503 0.3748 0.0147  0.0076  0.0203  1083 GLU A CD  
8017  O OE1 . GLU A 1085 ? 0.4158 0.3798 0.4075 0.0146  0.0066  0.0186  1083 GLU A OE1 
8018  O OE2 . GLU A 1085 ? 0.4113 0.3754 0.4014 0.0141  0.0083  0.0216  1083 GLU A OE2 
8019  N N   . LEU A 1086 ? 0.2665 0.2395 0.2434 0.0178  0.0088  0.0214  1084 LEU A N   
8020  C CA  . LEU A 1086 ? 0.2768 0.2525 0.2518 0.0186  0.0097  0.0237  1084 LEU A CA  
8021  C C   . LEU A 1086 ? 0.2957 0.2704 0.2728 0.0179  0.0106  0.0261  1084 LEU A C   
8022  O O   . LEU A 1086 ? 0.2818 0.2540 0.2605 0.0168  0.0108  0.0248  1084 LEU A O   
8023  C CB  . LEU A 1086 ? 0.2775 0.2549 0.2490 0.0191  0.0101  0.0212  1084 LEU A CB  
8024  C CG  . LEU A 1086 ? 0.2869 0.2650 0.2566 0.0196  0.0091  0.0184  1084 LEU A CG  
8025  C CD1 . LEU A 1086 ? 0.2869 0.2665 0.2539 0.0201  0.0093  0.0158  1084 LEU A CD1 
8026  C CD2 . LEU A 1086 ? 0.2961 0.2768 0.2652 0.0209  0.0084  0.0202  1084 LEU A CD2 
8027  N N   . PRO A 1087 ? 0.3022 0.2794 0.2796 0.0186  0.0111  0.0297  1085 PRO A N   
8028  C CA  . PRO A 1087 ? 0.2886 0.2653 0.2682 0.0179  0.0120  0.0323  1085 PRO A CA  
8029  C C   . PRO A 1087 ? 0.2810 0.2579 0.2588 0.0176  0.0131  0.0305  1085 PRO A C   
8030  O O   . PRO A 1087 ? 0.3114 0.2907 0.2857 0.0185  0.0135  0.0288  1085 PRO A O   
8031  C CB  . PRO A 1087 ? 0.2975 0.2782 0.2770 0.0189  0.0124  0.0367  1085 PRO A CB  
8032  C CG  . PRO A 1087 ? 0.3188 0.3007 0.2972 0.0199  0.0113  0.0368  1085 PRO A CG  
8033  C CD  . PRO A 1087 ? 0.2702 0.2509 0.2461 0.0200  0.0108  0.0320  1085 PRO A CD  
8034  N N   . GLY A 1088 ? 0.2775 0.2522 0.2580 0.0164  0.0135  0.0308  1086 GLY A N   
8035  C CA  . GLY A 1088 ? 0.2904 0.2650 0.2697 0.0161  0.0144  0.0295  1086 GLY A CA  
8036  C C   . GLY A 1088 ? 0.2307 0.2034 0.2136 0.0149  0.0148  0.0309  1086 GLY A C   
8037  O O   . GLY A 1088 ? 0.2528 0.2249 0.2391 0.0145  0.0144  0.0336  1086 GLY A O   
8038  N N   . PRO A 1089 ? 0.2734 0.2450 0.2560 0.0143  0.0152  0.0290  1087 PRO A N   
8039  C CA  . PRO A 1089 ? 0.2500 0.2200 0.2358 0.0132  0.0155  0.0301  1087 PRO A CA  
8040  C C   . PRO A 1089 ? 0.3002 0.2670 0.2891 0.0121  0.0144  0.0290  1087 PRO A C   
8041  O O   . PRO A 1089 ? 0.2817 0.2474 0.2699 0.0121  0.0135  0.0267  1087 PRO A O   
8042  C CB  . PRO A 1089 ? 0.2879 0.2579 0.2720 0.0130  0.0162  0.0280  1087 PRO A CB  
8043  C CG  . PRO A 1089 ? 0.3247 0.2943 0.3058 0.0135  0.0156  0.0249  1087 PRO A CG  
8044  C CD  . PRO A 1089 ? 0.3110 0.2827 0.2905 0.0146  0.0154  0.0258  1087 PRO A CD  
8045  N N   . VAL A 1090 ? 0.2554 0.2211 0.2481 0.0112  0.0143  0.0307  1088 VAL A N   
8046  C CA  . VAL A 1090 ? 0.2266 0.1896 0.2226 0.0103  0.0131  0.0290  1088 VAL A CA  
8047  C C   . VAL A 1090 ? 0.2348 0.1969 0.2290 0.0097  0.0131  0.0257  1088 VAL A C   
8048  O O   . VAL A 1090 ? 0.2665 0.2295 0.2581 0.0098  0.0140  0.0251  1088 VAL A O   
8049  C CB  . VAL A 1090 ? 0.2473 0.2094 0.2481 0.0095  0.0129  0.0311  1088 VAL A CB  
8050  C CG1 . VAL A 1090 ? 0.2833 0.2462 0.2866 0.0099  0.0127  0.0350  1088 VAL A CG1 
8051  C CG2 . VAL A 1090 ? 0.2738 0.2368 0.2741 0.0091  0.0141  0.0318  1088 VAL A CG2 
8052  N N   . GLY A 1091 ? 0.2481 0.2088 0.2440 0.0092  0.0121  0.0234  1089 GLY A N   
8053  C CA  . GLY A 1091 ? 0.2540 0.2144 0.2485 0.0085  0.0120  0.0207  1089 GLY A CA  
8054  C C   . GLY A 1091 ? 0.2397 0.2008 0.2305 0.0089  0.0122  0.0190  1089 GLY A C   
8055  O O   . GLY A 1091 ? 0.2342 0.1954 0.2237 0.0083  0.0122  0.0174  1089 GLY A O   
8056  N N   . GLU A 1092 ? 0.2301 0.1919 0.2194 0.0098  0.0121  0.0195  1090 GLU A N   
8057  C CA  . GLU A 1092 ? 0.2605 0.2230 0.2467 0.0101  0.0120  0.0179  1090 GLU A CA  
8058  C C   . GLU A 1092 ? 0.2464 0.2093 0.2327 0.0109  0.0113  0.0180  1090 GLU A C   
8059  O O   . GLU A 1092 ? 0.2748 0.2379 0.2625 0.0115  0.0112  0.0201  1090 GLU A O   
8060  C CB  . GLU A 1092 ? 0.2702 0.2338 0.2537 0.0108  0.0128  0.0185  1090 GLU A CB  
8061  C CG  . GLU A 1092 ? 0.3157 0.2796 0.2968 0.0108  0.0127  0.0164  1090 GLU A CG  
8062  C CD  . GLU A 1092 ? 0.3504 0.3152 0.3296 0.0115  0.0134  0.0167  1090 GLU A CD  
8063  O OE1 . GLU A 1092 ? 0.3053 0.2719 0.2831 0.0127  0.0136  0.0174  1090 GLU A OE1 
8064  O OE2 . GLU A 1092 ? 0.3434 0.3077 0.3229 0.0110  0.0136  0.0161  1090 GLU A OE2 
8065  N N   . ARG A 1093 ? 0.2230 0.1862 0.2081 0.0108  0.0107  0.0158  1091 ARG A N   
8066  C CA  . ARG A 1093 ? 0.2398 0.2036 0.2245 0.0116  0.0100  0.0156  1091 ARG A CA  
8067  C C   . ARG A 1093 ? 0.2655 0.2305 0.2469 0.0121  0.0101  0.0147  1091 ARG A C   
8068  O O   . ARG A 1093 ? 0.2439 0.2089 0.2244 0.0113  0.0101  0.0129  1091 ARG A O   
8069  C CB  . ARG A 1093 ? 0.3156 0.2792 0.3022 0.0112  0.0091  0.0137  1091 ARG A CB  
8070  C CG  . ARG A 1093 ? 0.4515 0.4142 0.4420 0.0113  0.0085  0.0143  1091 ARG A CG  
8071  C CD  . ARG A 1093 ? 0.5474 0.5104 0.5398 0.0112  0.0075  0.0117  1091 ARG A CD  
8072  N NE  . ARG A 1093 ? 0.5659 0.5300 0.5575 0.0119  0.0069  0.0109  1091 ARG A NE  
8073  C CZ  . ARG A 1093 ? 0.7017 0.6673 0.6922 0.0116  0.0066  0.0086  1091 ARG A CZ  
8074  N NH1 . ARG A 1093 ? 0.6765 0.6429 0.6664 0.0105  0.0070  0.0071  1091 ARG A NH1 
8075  N NH2 . ARG A 1093 ? 0.6636 0.6302 0.6538 0.0123  0.0060  0.0080  1091 ARG A NH2 
8076  N N   . ASN A 1094 ? 0.2349 0.2012 0.2149 0.0132  0.0102  0.0160  1092 ASN A N   
8077  C CA  . ASN A 1094 ? 0.2203 0.1880 0.1974 0.0139  0.0102  0.0148  1092 ASN A CA  
8078  C C   . ASN A 1094 ? 0.2438 0.2126 0.2204 0.0146  0.0093  0.0143  1092 ASN A C   
8079  O O   . ASN A 1094 ? 0.2596 0.2292 0.2367 0.0155  0.0091  0.0162  1092 ASN A O   
8080  C CB  . ASN A 1094 ? 0.2236 0.1928 0.1990 0.0148  0.0110  0.0164  1092 ASN A CB  
8081  C CG  . ASN A 1094 ? 0.2405 0.2088 0.2163 0.0141  0.0118  0.0162  1092 ASN A CG  
8082  O OD1 . ASN A 1094 ? 0.2519 0.2195 0.2270 0.0136  0.0116  0.0142  1092 ASN A OD1 
8083  N ND2 . ASN A 1094 ? 0.2573 0.2254 0.2345 0.0140  0.0125  0.0185  1092 ASN A ND2 
8084  N N   . LEU A 1095 ? 0.2376 0.2064 0.2137 0.0141  0.0086  0.0120  1093 LEU A N   
8085  C CA  . LEU A 1095 ? 0.2186 0.1883 0.1947 0.0146  0.0077  0.0111  1093 LEU A CA  
8086  C C   . LEU A 1095 ? 0.2162 0.1875 0.1898 0.0153  0.0073  0.0097  1093 LEU A C   
8087  O O   . LEU A 1095 ? 0.2561 0.2272 0.2287 0.0149  0.0074  0.0085  1093 LEU A O   
8088  C CB  . LEU A 1095 ? 0.2530 0.2221 0.2309 0.0134  0.0072  0.0093  1093 LEU A CB  
8089  C CG  . LEU A 1095 ? 0.2753 0.2431 0.2557 0.0128  0.0075  0.0100  1093 LEU A CG  
8090  C CD1 . LEU A 1095 ? 0.3618 0.3300 0.3437 0.0119  0.0071  0.0080  1093 LEU A CD1 
8091  C CD2 . LEU A 1095 ? 0.3322 0.2996 0.3144 0.0138  0.0072  0.0119  1093 LEU A CD2 
8092  N N   . TYR A 1096 ? 0.2415 0.2143 0.2146 0.0163  0.0065  0.0099  1094 TYR A N   
8093  C CA  . TYR A 1096 ? 0.2349 0.2097 0.2058 0.0171  0.0059  0.0085  1094 TYR A CA  
8094  C C   . TYR A 1096 ? 0.2163 0.1919 0.1880 0.0172  0.0048  0.0074  1094 TYR A C   
8095  O O   . TYR A 1096 ? 0.2412 0.2172 0.2140 0.0179  0.0045  0.0089  1094 TYR A O   
8096  C CB  . TYR A 1096 ? 0.2314 0.2085 0.2002 0.0187  0.0063  0.0102  1094 TYR A CB  
8097  C CG  . TYR A 1096 ? 0.2275 0.2074 0.1940 0.0200  0.0054  0.0086  1094 TYR A CG  
8098  C CD1 . TYR A 1096 ? 0.2581 0.2387 0.2230 0.0203  0.0054  0.0065  1094 TYR A CD1 
8099  C CD2 . TYR A 1096 ? 0.2526 0.2344 0.2187 0.0210  0.0046  0.0093  1094 TYR A CD2 
8100  C CE1 . TYR A 1096 ? 0.2976 0.2809 0.2606 0.0215  0.0045  0.0046  1094 TYR A CE1 
8101  C CE2 . TYR A 1096 ? 0.2617 0.2465 0.2256 0.0222  0.0037  0.0077  1094 TYR A CE2 
8102  C CZ  . TYR A 1096 ? 0.2723 0.2579 0.2346 0.0225  0.0037  0.0053  1094 TYR A CZ  
8103  O OH  . TYR A 1096 ? 0.2566 0.2453 0.2170 0.0238  0.0027  0.0033  1094 TYR A OH  
8104  N N   . THR A 1097 ? 0.2259 0.2018 0.1975 0.0166  0.0041  0.0050  1095 THR A N   
8105  C CA  A THR A 1097 ? 0.2391 0.2160 0.2119 0.0164  0.0032  0.0039  1095 THR A CA  
8106  C CA  B THR A 1097 ? 0.2392 0.2160 0.2119 0.0164  0.0032  0.0038  1095 THR A CA  
8107  C C   . THR A 1097 ? 0.2404 0.2188 0.2119 0.0168  0.0022  0.0018  1095 THR A C   
8108  O O   . THR A 1097 ? 0.2446 0.2227 0.2153 0.0165  0.0021  0.0006  1095 THR A O   
8109  C CB  A THR A 1097 ? 0.2542 0.2300 0.2292 0.0148  0.0033  0.0030  1095 THR A CB  
8110  C CB  B THR A 1097 ? 0.2547 0.2303 0.2297 0.0148  0.0034  0.0030  1095 THR A CB  
8111  O OG1 A THR A 1097 ? 0.2276 0.2026 0.2027 0.0135  0.0035  0.0020  1095 THR A OG1 
8112  O OG1 B THR A 1097 ? 0.2927 0.2669 0.2688 0.0145  0.0042  0.0046  1095 THR A OG1 
8113  C CG2 A THR A 1097 ? 0.2694 0.2439 0.2460 0.0146  0.0039  0.0044  1095 THR A CG2 
8114  C CG2 B THR A 1097 ? 0.2405 0.2175 0.2171 0.0148  0.0026  0.0022  1095 THR A CG2 
8115  N N   . LEU A 1098 ? 0.2383 0.2185 0.2101 0.0174  0.0012  0.0013  1096 LEU A N   
8116  C CA  . LEU A 1098 ? 0.2214 0.2034 0.1926 0.0177  0.0000  -0.0009 1096 LEU A CA  
8117  C C   . LEU A 1098 ? 0.2058 0.1880 0.1793 0.0163  -0.0007 -0.0023 1096 LEU A C   
8118  O O   . LEU A 1098 ? 0.2269 0.2097 0.2018 0.0164  -0.0008 -0.0019 1096 LEU A O   
8119  C CB  . LEU A 1098 ? 0.2331 0.2177 0.2026 0.0196  -0.0008 -0.0004 1096 LEU A CB  
8120  C CG  . LEU A 1098 ? 0.2027 0.1883 0.1696 0.0210  -0.0001 0.0013  1096 LEU A CG  
8121  C CD1 . LEU A 1098 ? 0.2357 0.2246 0.2010 0.0229  -0.0010 0.0019  1096 LEU A CD1 
8122  C CD2 . LEU A 1098 ? 0.2202 0.2055 0.1858 0.0209  0.0001  -0.0005 1096 LEU A CD2 
8123  N N   . HIS A 1099 ? 0.2267 0.2086 0.2010 0.0151  -0.0012 -0.0041 1097 HIS A N   
8124  C CA  . HIS A 1099 ? 0.2487 0.2312 0.2254 0.0135  -0.0017 -0.0052 1097 HIS A CA  
8125  C C   . HIS A 1099 ? 0.2363 0.2204 0.2134 0.0137  -0.0033 -0.0073 1097 HIS A C   
8126  O O   . HIS A 1099 ? 0.2417 0.2263 0.2169 0.0150  -0.0039 -0.0082 1097 HIS A O   
8127  C CB  . HIS A 1099 ? 0.2311 0.2120 0.2094 0.0116  -0.0011 -0.0050 1097 HIS A CB  
8128  C CG  . HIS A 1099 ? 0.3152 0.2947 0.2933 0.0114  0.0003  -0.0033 1097 HIS A CG  
8129  N ND1 . HIS A 1099 ? 0.3320 0.3121 0.3118 0.0103  0.0008  -0.0028 1097 HIS A ND1 
8130  C CD2 . HIS A 1099 ? 0.3108 0.2885 0.2874 0.0121  0.0012  -0.0020 1097 HIS A CD2 
8131  C CE1 . HIS A 1099 ? 0.3366 0.3152 0.3160 0.0104  0.0019  -0.0016 1097 HIS A CE1 
8132  N NE2 . HIS A 1099 ? 0.3167 0.2938 0.2943 0.0114  0.0021  -0.0009 1097 HIS A NE2 
8133  N N   . ALA A 1100 ? 0.2395 0.2248 0.2191 0.0123  -0.0039 -0.0082 1098 ALA A N   
8134  C CA  . ALA A 1100 ? 0.2197 0.2061 0.2004 0.0119  -0.0055 -0.0102 1098 ALA A CA  
8135  C C   . ALA A 1100 ? 0.2680 0.2524 0.2492 0.0112  -0.0059 -0.0111 1098 ALA A C   
8136  O O   . ALA A 1100 ? 0.2806 0.2630 0.2623 0.0102  -0.0049 -0.0099 1098 ALA A O   
8137  C CB  . ALA A 1100 ? 0.2361 0.2243 0.2200 0.0103  -0.0060 -0.0106 1098 ALA A CB  
8138  N N   . ARG A 1101 ? 0.2648 0.2499 0.2463 0.0118  -0.0074 -0.0134 1099 ARG A N   
8139  C CA  A ARG A 1101 ? 0.2756 0.2588 0.2585 0.0111  -0.0082 -0.0147 1099 ARG A CA  
8140  C CA  B ARG A 1101 ? 0.2757 0.2589 0.2586 0.0111  -0.0082 -0.0147 1099 ARG A CA  
8141  C C   . ARG A 1101 ? 0.2483 0.2308 0.2355 0.0085  -0.0089 -0.0145 1099 ARG A C   
8142  O O   . ARG A 1101 ? 0.2800 0.2603 0.2689 0.0073  -0.0087 -0.0140 1099 ARG A O   
8143  C CB  A ARG A 1101 ? 0.2994 0.2838 0.2815 0.0128  -0.0098 -0.0176 1099 ARG A CB  
8144  C CB  B ARG A 1101 ? 0.2994 0.2838 0.2814 0.0129  -0.0098 -0.0176 1099 ARG A CB  
8145  C CG  A ARG A 1101 ? 0.3111 0.2967 0.2889 0.0154  -0.0092 -0.0176 1099 ARG A CG  
8146  C CG  B ARG A 1101 ? 0.3174 0.3026 0.2953 0.0153  -0.0091 -0.0176 1099 ARG A CG  
8147  C CD  A ARG A 1101 ? 0.2527 0.2401 0.2298 0.0171  -0.0109 -0.0209 1099 ARG A CD  
8148  C CD  B ARG A 1101 ? 0.3210 0.3054 0.2989 0.0162  -0.0100 -0.0201 1099 ARG A CD  
8149  N NE  A ARG A 1101 ? 0.2658 0.2514 0.2440 0.0172  -0.0114 -0.0227 1099 ARG A NE  
8150  N NE  B ARG A 1101 ? 0.2845 0.2701 0.2586 0.0184  -0.0089 -0.0197 1099 ARG A NE  
8151  C CZ  A ARG A 1101 ? 0.2836 0.2691 0.2591 0.0186  -0.0104 -0.0225 1099 ARG A CZ  
8152  C CZ  B ARG A 1101 ? 0.3245 0.3106 0.2978 0.0198  -0.0095 -0.0221 1099 ARG A CZ  
8153  N NH1 A ARG A 1101 ? 0.3194 0.3063 0.2913 0.0199  -0.0087 -0.0202 1099 ARG A NH1 
8154  N NH1 B ARG A 1101 ? 0.2920 0.2772 0.2683 0.0194  -0.0114 -0.0253 1099 ARG A NH1 
8155  N NH2 A ARG A 1101 ? 0.2989 0.2829 0.2759 0.0188  -0.0111 -0.0247 1099 ARG A NH2 
8156  N NH2 B ARG A 1101 ? 0.2953 0.2832 0.2649 0.0218  -0.0083 -0.0213 1099 ARG A NH2 
8157  N N   . GLY A 1102 ? 0.2601 0.2448 0.2493 0.0076  -0.0096 -0.0148 1100 GLY A N   
8158  C CA  . GLY A 1102 ? 0.2704 0.2551 0.2641 0.0051  -0.0104 -0.0144 1100 GLY A CA  
8159  C C   . GLY A 1102 ? 0.2574 0.2445 0.2534 0.0048  -0.0122 -0.0162 1100 GLY A C   
8160  O O   . GLY A 1102 ? 0.2616 0.2513 0.2564 0.0057  -0.0121 -0.0164 1100 GLY A O   
8161  N N   . ARG A 1103 ? 0.2557 0.2419 0.2556 0.0035  -0.0140 -0.0175 1101 ARG A N   
8162  C CA  . ARG A 1103 ? 0.2436 0.2320 0.2464 0.0031  -0.0160 -0.0194 1101 ARG A CA  
8163  C C   . ARG A 1103 ? 0.2260 0.2139 0.2275 0.0052  -0.0177 -0.0229 1101 ARG A C   
8164  O O   . ARG A 1103 ? 0.2725 0.2579 0.2749 0.0054  -0.0185 -0.0242 1101 ARG A O   
8165  C CB  . ARG A 1103 ? 0.2751 0.2634 0.2838 0.0000  -0.0172 -0.0186 1101 ARG A CB  
8166  C CG  . ARG A 1103 ? 0.3128 0.3040 0.3247 -0.0006 -0.0190 -0.0200 1101 ARG A CG  
8167  C CD  . ARG A 1103 ? 0.3173 0.3094 0.3353 -0.0039 -0.0198 -0.0183 1101 ARG A CD  
8168  N NE  . ARG A 1103 ? 0.4011 0.3953 0.4189 -0.0054 -0.0176 -0.0148 1101 ARG A NE  
8169  C CZ  . ARG A 1103 ? 0.4461 0.4444 0.4640 -0.0058 -0.0169 -0.0139 1101 ARG A CZ  
8170  N NH1 . ARG A 1103 ? 0.3437 0.3443 0.3621 -0.0050 -0.0181 -0.0160 1101 ARG A NH1 
8171  N NH2 . ARG A 1103 ? 0.5320 0.5324 0.5497 -0.0070 -0.0149 -0.0111 1101 ARG A NH2 
8172  N N   . ILE A 1104 ? 0.2107 0.2013 0.2101 0.0069  -0.0183 -0.0245 1102 ILE A N   
8173  C CA  . ILE A 1104 ? 0.2366 0.2280 0.2344 0.0092  -0.0200 -0.0279 1102 ILE A CA  
8174  C C   . ILE A 1104 ? 0.2431 0.2357 0.2454 0.0083  -0.0227 -0.0306 1102 ILE A C   
8175  O O   . ILE A 1104 ? 0.2313 0.2261 0.2357 0.0071  -0.0230 -0.0299 1102 ILE A O   
8176  C CB  . ILE A 1104 ? 0.2147 0.2087 0.2073 0.0118  -0.0192 -0.0278 1102 ILE A CB  
8177  C CG1 . ILE A 1104 ? 0.2391 0.2318 0.2279 0.0125  -0.0166 -0.0248 1102 ILE A CG1 
8178  C CG2 . ILE A 1104 ? 0.2283 0.2238 0.2186 0.0143  -0.0207 -0.0312 1102 ILE A CG2 
8179  C CD1 . ILE A 1104 ? 0.2592 0.2494 0.2467 0.0131  -0.0159 -0.0250 1102 ILE A CD1 
8180  N N   . LEU A 1105 ? 0.2240 0.2152 0.2282 0.0088  -0.0246 -0.0337 1103 LEU A N   
8181  C CA  . LEU A 1105 ? 0.2588 0.2512 0.2674 0.0083  -0.0276 -0.0370 1103 LEU A CA  
8182  C C   . LEU A 1105 ? 0.2388 0.2351 0.2441 0.0108  -0.0285 -0.0394 1103 LEU A C   
8183  O O   . LEU A 1105 ? 0.2705 0.2678 0.2711 0.0135  -0.0282 -0.0410 1103 LEU A O   
8184  C CB  . LEU A 1105 ? 0.2594 0.2490 0.2714 0.0083  -0.0296 -0.0400 1103 LEU A CB  
8185  C CG  . LEU A 1105 ? 0.2487 0.2392 0.2658 0.0080  -0.0330 -0.0440 1103 LEU A CG  
8186  C CD1 . LEU A 1105 ? 0.2782 0.2687 0.3014 0.0047  -0.0339 -0.0420 1103 LEU A CD1 
8187  C CD2 . LEU A 1105 ? 0.2795 0.2673 0.2996 0.0087  -0.0351 -0.0476 1103 LEU A CD2 
8188  N N   . LEU A 1106 ? 0.2162 0.2151 0.2236 0.0099  -0.0295 -0.0396 1104 LEU A N   
8189  C CA  . LEU A 1106 ? 0.2117 0.2146 0.2166 0.0122  -0.0307 -0.0419 1104 LEU A CA  
8190  C C   . LEU A 1106 ? 0.2825 0.2863 0.2920 0.0119  -0.0341 -0.0462 1104 LEU A C   
8191  O O   . LEU A 1106 ? 0.2644 0.2675 0.2799 0.0093  -0.0353 -0.0460 1104 LEU A O   
8192  C CB  . LEU A 1106 ? 0.2462 0.2518 0.2503 0.0117  -0.0297 -0.0394 1104 LEU A CB  
8193  C CG  . LEU A 1106 ? 0.3294 0.3345 0.3295 0.0121  -0.0266 -0.0354 1104 LEU A CG  
8194  C CD1 . LEU A 1106 ? 0.2631 0.2717 0.2622 0.0127  -0.0263 -0.0343 1104 LEU A CD1 
8195  C CD2 . LEU A 1106 ? 0.3170 0.3214 0.3118 0.0145  -0.0254 -0.0353 1104 LEU A CD2 
8196  N N   . VAL A 1107 ? 0.2393 0.2451 0.2462 0.0147  -0.0356 -0.0500 1105 VAL A N   
8197  C CA  . VAL A 1107 ? 0.2491 0.2563 0.2603 0.0148  -0.0390 -0.0547 1105 VAL A CA  
8198  C C   . VAL A 1107 ? 0.2284 0.2408 0.2358 0.0173  -0.0399 -0.0566 1105 VAL A C   
8199  O O   . VAL A 1107 ? 0.2592 0.2741 0.2625 0.0202  -0.0405 -0.0593 1105 VAL A O   
8200  C CB  . VAL A 1107 ? 0.2419 0.2470 0.2544 0.0159  -0.0406 -0.0586 1105 VAL A CB  
8201  C CG1 . VAL A 1107 ? 0.2676 0.2735 0.2859 0.0156  -0.0445 -0.0636 1105 VAL A CG1 
8202  C CG2 . VAL A 1107 ? 0.2788 0.2788 0.2940 0.0137  -0.0392 -0.0559 1105 VAL A CG2 
8203  N N   . PRO A 1108 ? 0.2351 0.2497 0.2437 0.0162  -0.0400 -0.0550 1106 PRO A N   
8204  C CA  . PRO A 1108 ? 0.2612 0.2809 0.2664 0.0186  -0.0408 -0.0563 1106 PRO A CA  
8205  C C   . PRO A 1108 ? 0.2634 0.2857 0.2724 0.0190  -0.0445 -0.0613 1106 PRO A C   
8206  O O   . PRO A 1108 ? 0.2949 0.3148 0.3103 0.0169  -0.0465 -0.0634 1106 PRO A O   
8207  C CB  . PRO A 1108 ? 0.2629 0.2835 0.2687 0.0171  -0.0393 -0.0523 1106 PRO A CB  
8208  C CG  . PRO A 1108 ? 0.2541 0.2715 0.2666 0.0134  -0.0395 -0.0512 1106 PRO A CG  
8209  C CD  . PRO A 1108 ? 0.2810 0.2940 0.2941 0.0130  -0.0391 -0.0515 1106 PRO A CD  
8210  N N   . ALA A 1109 ? 0.2476 0.2747 0.2527 0.0217  -0.0455 -0.0633 1107 ALA A N   
8211  C CA  . ALA A 1109 ? 0.2733 0.3039 0.2814 0.0223  -0.0491 -0.0681 1107 ALA A CA  
8212  C C   . ALA A 1109 ? 0.3113 0.3460 0.3194 0.0224  -0.0496 -0.0669 1107 ALA A C   
8213  O O   . ALA A 1109 ? 0.3139 0.3501 0.3271 0.0213  -0.0522 -0.0696 1107 ALA A O   
8214  C CB  . ALA A 1109 ? 0.2671 0.3011 0.2710 0.0258  -0.0505 -0.0725 1107 ALA A CB  
8215  N N   . THR A 1110 ? 0.2762 0.3126 0.2790 0.0237  -0.0472 -0.0630 1108 THR A N   
8216  C CA  . THR A 1110 ? 0.2726 0.3128 0.2752 0.0240  -0.0476 -0.0616 1108 THR A CA  
8217  C C   . THR A 1110 ? 0.2831 0.3211 0.2857 0.0223  -0.0446 -0.0563 1108 THR A C   
8218  O O   . THR A 1110 ? 0.2647 0.2991 0.2656 0.0218  -0.0421 -0.0535 1108 THR A O   
8219  C CB  . THR A 1110 ? 0.2766 0.3220 0.2729 0.0276  -0.0480 -0.0622 1108 THR A CB  
8220  O OG1 . THR A 1110 ? 0.2688 0.3131 0.2594 0.0290  -0.0451 -0.0585 1108 THR A OG1 
8221  C CG2 . THR A 1110 ? 0.3095 0.3579 0.3053 0.0296  -0.0508 -0.0678 1108 THR A CG2 
8222  N N   . GLU A 1111 ? 0.2973 0.3379 0.3020 0.0218  -0.0451 -0.0553 1109 GLU A N   
8223  C CA  . GLU A 1111 ? 0.2814 0.3210 0.2862 0.0206  -0.0425 -0.0508 1109 GLU A CA  
8224  C C   . GLU A 1111 ? 0.2947 0.3339 0.2932 0.0228  -0.0402 -0.0476 1109 GLU A C   
8225  O O   . GLU A 1111 ? 0.2663 0.3022 0.2642 0.0218  -0.0376 -0.0444 1109 GLU A O   
8226  C CB  . GLU A 1111 ? 0.3295 0.3729 0.3372 0.0203  -0.0437 -0.0507 1109 GLU A CB  
8227  C CG  . GLU A 1111 ? 0.3345 0.3778 0.3418 0.0199  -0.0413 -0.0466 1109 GLU A CG  
8228  C CD  . GLU A 1111 ? 0.3360 0.3831 0.3472 0.0192  -0.0425 -0.0468 1109 GLU A CD  
8229  O OE1 . GLU A 1111 ? 0.3952 0.4422 0.4121 0.0165  -0.0431 -0.0476 1109 GLU A OE1 
8230  O OE2 . GLU A 1111 ? 0.3873 0.4376 0.3962 0.0214  -0.0428 -0.0461 1109 GLU A OE2 
8231  N N   . SER A 1112 ? 0.2820 0.3248 0.2760 0.0259  -0.0410 -0.0483 1110 SER A N   
8232  C CA  . SER A 1112 ? 0.2504 0.2930 0.2388 0.0279  -0.0390 -0.0449 1110 SER A CA  
8233  C C   . SER A 1112 ? 0.2944 0.3332 0.2805 0.0277  -0.0373 -0.0444 1110 SER A C   
8234  O O   . SER A 1112 ? 0.2738 0.3101 0.2577 0.0277  -0.0348 -0.0408 1110 SER A O   
8235  C CB  . SER A 1112 ? 0.3038 0.3517 0.2880 0.0311  -0.0404 -0.0456 1110 SER A CB  
8236  O OG  . SER A 1112 ? 0.3064 0.3542 0.2860 0.0328  -0.0384 -0.0416 1110 SER A OG  
8237  N N   . GLY A 1113 ? 0.2501 0.2886 0.2370 0.0277  -0.0387 -0.0481 1111 GLY A N   
8238  C CA  . GLY A 1113 ? 0.2216 0.2564 0.2069 0.0274  -0.0372 -0.0478 1111 GLY A CA  
8239  C C   . GLY A 1113 ? 0.2253 0.2550 0.2137 0.0246  -0.0352 -0.0451 1111 GLY A C   
8240  O O   . GLY A 1113 ? 0.2662 0.2932 0.2520 0.0246  -0.0328 -0.0424 1111 GLY A O   
8241  N N   . LEU A 1114 ? 0.2324 0.2613 0.2264 0.0220  -0.0360 -0.0458 1112 LEU A N   
8242  C CA  . LEU A 1114 ? 0.2505 0.2755 0.2475 0.0193  -0.0341 -0.0430 1112 LEU A CA  
8243  C C   . LEU A 1114 ? 0.2366 0.2614 0.2308 0.0198  -0.0316 -0.0388 1112 LEU A C   
8244  O O   . LEU A 1114 ? 0.2447 0.2662 0.2380 0.0189  -0.0294 -0.0364 1112 LEU A O   
8245  C CB  . LEU A 1114 ? 0.2538 0.2793 0.2571 0.0166  -0.0355 -0.0439 1112 LEU A CB  
8246  C CG  . LEU A 1114 ? 0.2859 0.3088 0.2924 0.0138  -0.0336 -0.0408 1112 LEU A CG  
8247  C CD1 . LEU A 1114 ? 0.2488 0.2672 0.2547 0.0128  -0.0322 -0.0398 1112 LEU A CD1 
8248  C CD2 . LEU A 1114 ? 0.3023 0.3265 0.3154 0.0111  -0.0351 -0.0416 1112 LEU A CD2 
8249  N N   . TYR A 1115 ? 0.2540 0.2823 0.2472 0.0211  -0.0320 -0.0381 1113 TYR A N   
8250  C CA  . TYR A 1115 ? 0.2392 0.2672 0.2305 0.0217  -0.0299 -0.0345 1113 TYR A CA  
8251  C C   . TYR A 1115 ? 0.2476 0.2738 0.2339 0.0235  -0.0283 -0.0325 1113 TYR A C   
8252  O O   . TYR A 1115 ? 0.2405 0.2641 0.2263 0.0229  -0.0261 -0.0296 1113 TYR A O   
8253  C CB  . TYR A 1115 ? 0.2357 0.2678 0.2271 0.0232  -0.0310 -0.0342 1113 TYR A CB  
8254  C CG  . TYR A 1115 ? 0.2101 0.2443 0.2066 0.0215  -0.0323 -0.0356 1113 TYR A CG  
8255  C CD1 . TYR A 1115 ? 0.2464 0.2787 0.2473 0.0185  -0.0319 -0.0359 1113 TYR A CD1 
8256  C CD2 . TYR A 1115 ? 0.2645 0.3029 0.2615 0.0228  -0.0340 -0.0364 1113 TYR A CD2 
8257  C CE1 . TYR A 1115 ? 0.2650 0.3000 0.2710 0.0168  -0.0331 -0.0368 1113 TYR A CE1 
8258  C CE2 . TYR A 1115 ? 0.2566 0.2974 0.2585 0.0213  -0.0352 -0.0376 1113 TYR A CE2 
8259  C CZ  . TYR A 1115 ? 0.3082 0.3474 0.3146 0.0183  -0.0347 -0.0378 1113 TYR A CZ  
8260  O OH  . TYR A 1115 ? 0.3347 0.3768 0.3461 0.0167  -0.0359 -0.0388 1113 TYR A OH  
8261  N N   . HIS A 1116 ? 0.2459 0.2739 0.2287 0.0256  -0.0293 -0.0340 1114 HIS A N   
8262  C CA  . HIS A 1116 ? 0.2390 0.2659 0.2173 0.0271  -0.0277 -0.0320 1114 HIS A CA  
8263  C C   . HIS A 1116 ? 0.2504 0.2729 0.2294 0.0254  -0.0262 -0.0318 1114 HIS A C   
8264  O O   . HIS A 1116 ? 0.2431 0.2632 0.2201 0.0256  -0.0241 -0.0289 1114 HIS A O   
8265  C CB  . HIS A 1116 ? 0.2734 0.3042 0.2479 0.0297  -0.0292 -0.0339 1114 HIS A CB  
8266  C CG  . HIS A 1116 ? 0.2879 0.3231 0.2600 0.0319  -0.0299 -0.0323 1114 HIS A CG  
8267  N ND1 . HIS A 1116 ? 0.3443 0.3831 0.3183 0.0324  -0.0320 -0.0342 1114 HIS A ND1 
8268  C CD2 . HIS A 1116 ? 0.2902 0.3268 0.2587 0.0338  -0.0288 -0.0288 1114 HIS A CD2 
8269  C CE1 . HIS A 1116 ? 0.2877 0.3300 0.2590 0.0345  -0.0323 -0.0319 1114 HIS A CE1 
8270  N NE2 . HIS A 1116 ? 0.3192 0.3602 0.2873 0.0354  -0.0304 -0.0285 1114 HIS A NE2 
8271  N N   . GLN A 1117 ? 0.2273 0.2485 0.2094 0.0239  -0.0274 -0.0348 1115 GLN A N   
8272  C CA  . GLN A 1117 ? 0.2105 0.2274 0.1937 0.0223  -0.0262 -0.0345 1115 GLN A CA  
8273  C C   . GLN A 1117 ? 0.2297 0.2439 0.2149 0.0202  -0.0242 -0.0313 1115 GLN A C   
8274  O O   . GLN A 1117 ? 0.2354 0.2467 0.2192 0.0198  -0.0222 -0.0293 1115 GLN A O   
8275  C CB  . GLN A 1117 ? 0.2336 0.2497 0.2209 0.0208  -0.0282 -0.0382 1115 GLN A CB  
8276  C CG  . GLN A 1117 ? 0.2316 0.2499 0.2171 0.0229  -0.0301 -0.0421 1115 GLN A CG  
8277  C CD  . GLN A 1117 ? 0.2745 0.2913 0.2650 0.0214  -0.0323 -0.0458 1115 GLN A CD  
8278  O OE1 . GLN A 1117 ? 0.2626 0.2774 0.2580 0.0187  -0.0326 -0.0452 1115 GLN A OE1 
8279  N NE2 . GLN A 1117 ? 0.2454 0.2634 0.2349 0.0231  -0.0340 -0.0497 1115 GLN A NE2 
8280  N N   . LEU A 1118 ? 0.2254 0.2409 0.2140 0.0189  -0.0247 -0.0311 1116 LEU A N   
8281  C CA  A LEU A 1118 ? 0.2296 0.2434 0.2202 0.0170  -0.0229 -0.0284 1116 LEU A CA  
8282  C CA  B LEU A 1118 ? 0.2298 0.2436 0.2204 0.0170  -0.0229 -0.0284 1116 LEU A CA  
8283  C C   . LEU A 1118 ? 0.2301 0.2435 0.2174 0.0185  -0.0210 -0.0255 1116 LEU A C   
8284  O O   . LEU A 1118 ? 0.2441 0.2549 0.2313 0.0176  -0.0191 -0.0234 1116 LEU A O   
8285  C CB  A LEU A 1118 ? 0.2509 0.2672 0.2457 0.0155  -0.0238 -0.0290 1116 LEU A CB  
8286  C CB  B LEU A 1118 ? 0.2512 0.2677 0.2459 0.0157  -0.0238 -0.0289 1116 LEU A CB  
8287  C CG  A LEU A 1118 ? 0.2326 0.2483 0.2304 0.0133  -0.0223 -0.0269 1116 LEU A CG  
8288  C CG  B LEU A 1118 ? 0.2283 0.2446 0.2279 0.0132  -0.0252 -0.0307 1116 LEU A CG  
8289  C CD1 A LEU A 1118 ? 0.2287 0.2409 0.2276 0.0113  -0.0212 -0.0260 1116 LEU A CD1 
8290  C CD1 B LEU A 1118 ? 0.2427 0.2628 0.2457 0.0126  -0.0265 -0.0315 1116 LEU A CD1 
8291  C CD2 A LEU A 1118 ? 0.2927 0.3115 0.2952 0.0117  -0.0237 -0.0281 1116 LEU A CD2 
8292  C CD2 B LEU A 1118 ? 0.2310 0.2445 0.2328 0.0107  -0.0236 -0.0287 1116 LEU A CD2 
8293  N N   . ALA A 1119 ? 0.2491 0.2651 0.2338 0.0208  -0.0216 -0.0252 1117 ALA A N   
8294  C CA  . ALA A 1119 ? 0.2630 0.2785 0.2452 0.0223  -0.0201 -0.0222 1117 ALA A CA  
8295  C C   . ALA A 1119 ? 0.2513 0.2639 0.2306 0.0226  -0.0186 -0.0209 1117 ALA A C   
8296  O O   . ALA A 1119 ? 0.2593 0.2697 0.2384 0.0222  -0.0169 -0.0185 1117 ALA A O   
8297  C CB  . ALA A 1119 ? 0.2803 0.2994 0.2605 0.0248  -0.0214 -0.0219 1117 ALA A CB  
8298  N N   . ALA A 1120 ? 0.2303 0.2433 0.2076 0.0234  -0.0193 -0.0226 1118 ALA A N   
8299  C CA  . ALA A 1120 ? 0.2260 0.2368 0.2006 0.0238  -0.0179 -0.0215 1118 ALA A CA  
8300  C C   . ALA A 1120 ? 0.2472 0.2540 0.2239 0.0215  -0.0165 -0.0209 1118 ALA A C   
8301  O O   . ALA A 1120 ? 0.2371 0.2416 0.2125 0.0215  -0.0147 -0.0185 1118 ALA A O   
8302  C CB  . ALA A 1120 ? 0.2346 0.2471 0.2070 0.0251  -0.0191 -0.0242 1118 ALA A CB  
8303  N N   . ALA A 1121 ? 0.2156 0.2217 0.1959 0.0195  -0.0174 -0.0228 1119 ALA A N   
8304  C CA  . ALA A 1121 ? 0.2192 0.2220 0.2018 0.0173  -0.0162 -0.0221 1119 ALA A CA  
8305  C C   . ALA A 1121 ? 0.2070 0.2092 0.1907 0.0162  -0.0147 -0.0195 1119 ALA A C   
8306  O O   . ALA A 1121 ? 0.2007 0.2004 0.1841 0.0154  -0.0130 -0.0178 1119 ALA A O   
8307  C CB  . ALA A 1121 ? 0.2406 0.2432 0.2272 0.0153  -0.0178 -0.0244 1119 ALA A CB  
8308  N N   . LEU A 1122 ? 0.2190 0.2237 0.2042 0.0163  -0.0152 -0.0195 1120 LEU A N   
8309  C CA  . LEU A 1122 ? 0.2082 0.2129 0.1949 0.0156  -0.0138 -0.0176 1120 LEU A CA  
8310  C C   . LEU A 1122 ? 0.2165 0.2201 0.2004 0.0173  -0.0126 -0.0154 1120 LEU A C   
8311  O O   . LEU A 1122 ? 0.2349 0.2370 0.2195 0.0166  -0.0111 -0.0139 1120 LEU A O   
8312  C CB  . LEU A 1122 ? 0.2414 0.2495 0.2305 0.0155  -0.0148 -0.0183 1120 LEU A CB  
8313  C CG  . LEU A 1122 ? 0.2400 0.2497 0.2328 0.0135  -0.0161 -0.0201 1120 LEU A CG  
8314  C CD1 . LEU A 1122 ? 0.2780 0.2915 0.2729 0.0139  -0.0170 -0.0207 1120 LEU A CD1 
8315  C CD2 . LEU A 1122 ? 0.2412 0.2495 0.2364 0.0109  -0.0149 -0.0191 1120 LEU A CD2 
8316  N N   . ALA A 1123 ? 0.2239 0.2284 0.2051 0.0195  -0.0132 -0.0151 1121 ALA A N   
8317  C CA  . ALA A 1123 ? 0.2319 0.2354 0.2110 0.0210  -0.0121 -0.0126 1121 ALA A CA  
8318  C C   . ALA A 1123 ? 0.2496 0.2499 0.2274 0.0204  -0.0105 -0.0114 1121 ALA A C   
8319  O O   . ALA A 1123 ? 0.2338 0.2327 0.2112 0.0209  -0.0094 -0.0092 1121 ALA A O   
8320  C CB  . ALA A 1123 ? 0.2136 0.2193 0.1899 0.0233  -0.0131 -0.0122 1121 ALA A CB  
8321  N N   . THR A 1124 ? 0.2023 0.2015 0.1798 0.0193  -0.0106 -0.0128 1122 THR A N   
8322  C CA  . THR A 1124 ? 0.2080 0.2042 0.1844 0.0187  -0.0092 -0.0118 1122 THR A CA  
8323  C C   . THR A 1124 ? 0.2302 0.2246 0.2093 0.0163  -0.0085 -0.0119 1122 THR A C   
8324  O O   . THR A 1124 ? 0.2232 0.2153 0.2019 0.0155  -0.0076 -0.0115 1122 THR A O   
8325  C CB  . THR A 1124 ? 0.2249 0.2214 0.1992 0.0196  -0.0098 -0.0133 1122 THR A CB  
8326  O OG1 . THR A 1124 ? 0.2130 0.2110 0.1888 0.0191  -0.0116 -0.0161 1122 THR A OG1 
8327  C CG2 . THR A 1124 ? 0.2465 0.2451 0.2173 0.0221  -0.0099 -0.0122 1122 THR A CG2 
8328  N N   . GLY A 1125 ? 0.2029 0.1988 0.1847 0.0153  -0.0088 -0.0123 1123 GLY A N   
8329  C CA  . GLY A 1125 ? 0.2288 0.2241 0.2131 0.0131  -0.0078 -0.0118 1123 GLY A CA  
8330  C C   . GLY A 1125 ? 0.2355 0.2306 0.2221 0.0111  -0.0085 -0.0129 1123 GLY A C   
8331  O O   . GLY A 1125 ? 0.2534 0.2483 0.2420 0.0092  -0.0077 -0.0121 1123 GLY A O   
8332  N N   . ASN A 1126 ? 0.2290 0.2244 0.2156 0.0115  -0.0100 -0.0147 1124 ASN A N   
8333  C CA  . ASN A 1126 ? 0.1997 0.1944 0.1890 0.0096  -0.0110 -0.0159 1124 ASN A CA  
8334  C C   . ASN A 1126 ? 0.2191 0.2164 0.2121 0.0080  -0.0120 -0.0165 1124 ASN A C   
8335  O O   . ASN A 1126 ? 0.2285 0.2286 0.2217 0.0088  -0.0125 -0.0169 1124 ASN A O   
8336  C CB  . ASN A 1126 ? 0.1985 0.1925 0.1865 0.0109  -0.0124 -0.0180 1124 ASN A CB  
8337  C CG  . ASN A 1126 ? 0.2087 0.2008 0.1932 0.0124  -0.0114 -0.0174 1124 ASN A CG  
8338  O OD1 . ASN A 1126 ? 0.2516 0.2412 0.2364 0.0115  -0.0105 -0.0165 1124 ASN A OD1 
8339  N ND2 . ASN A 1126 ? 0.2187 0.2122 0.1999 0.0148  -0.0115 -0.0176 1124 ASN A ND2 
8340  N N   . SER A 1127 ? 0.2441 0.2407 0.2405 0.0057  -0.0125 -0.0164 1125 SER A N   
8341  C CA  . SER A 1127 ? 0.2200 0.2189 0.2205 0.0041  -0.0140 -0.0174 1125 SER A CA  
8342  C C   . SER A 1127 ? 0.2487 0.2466 0.2500 0.0047  -0.0162 -0.0200 1125 SER A C   
8343  O O   . SER A 1127 ? 0.2479 0.2437 0.2467 0.0062  -0.0164 -0.0211 1125 SER A O   
8344  C CB  . SER A 1127 ? 0.2660 0.2650 0.2703 0.0012  -0.0135 -0.0155 1125 SER A CB  
8345  O OG  . SER A 1127 ? 0.3298 0.3254 0.3347 0.0004  -0.0137 -0.0151 1125 SER A OG  
8346  N N   . VAL A 1128 ? 0.2592 0.2592 0.2644 0.0035  -0.0180 -0.0213 1126 VAL A N   
8347  C CA  . VAL A 1128 ? 0.2298 0.2293 0.2363 0.0041  -0.0204 -0.0244 1126 VAL A CA  
8348  C C   . VAL A 1128 ? 0.2680 0.2675 0.2808 0.0013  -0.0221 -0.0246 1126 VAL A C   
8349  O O   . VAL A 1128 ? 0.2505 0.2521 0.2665 -0.0009 -0.0216 -0.0226 1126 VAL A O   
8350  C CB  . VAL A 1128 ? 0.2528 0.2553 0.2574 0.0063  -0.0216 -0.0265 1126 VAL A CB  
8351  C CG1 . VAL A 1128 ? 0.2414 0.2441 0.2404 0.0089  -0.0200 -0.0257 1126 VAL A CG1 
8352  C CG2 . VAL A 1128 ? 0.2821 0.2882 0.2899 0.0050  -0.0220 -0.0260 1126 VAL A CG2 
8353  N N   . ALA A 1129 ? 0.2458 0.2434 0.2606 0.0015  -0.0242 -0.0272 1127 ALA A N   
8354  C CA  . ALA A 1129 ? 0.2624 0.2601 0.2836 -0.0006 -0.0266 -0.0285 1127 ALA A CA  
8355  C C   . ALA A 1129 ? 0.2373 0.2365 0.2583 0.0013  -0.0290 -0.0326 1127 ALA A C   
8356  O O   . ALA A 1129 ? 0.2732 0.2710 0.2911 0.0036  -0.0296 -0.0352 1127 ALA A O   
8357  C CB  . ALA A 1129 ? 0.2953 0.2890 0.3201 -0.0022 -0.0273 -0.0280 1127 ALA A CB  
8358  N N   . ILE A 1130 ? 0.2459 0.2483 0.2697 0.0006  -0.0303 -0.0334 1128 ILE A N   
8359  C CA  . ILE A 1130 ? 0.2599 0.2644 0.2833 0.0025  -0.0327 -0.0373 1128 ILE A CA  
8360  C C   . ILE A 1130 ? 0.3034 0.3068 0.3336 0.0009  -0.0358 -0.0400 1128 ILE A C   
8361  O O   . ILE A 1130 ? 0.2869 0.2903 0.3231 -0.0022 -0.0364 -0.0382 1128 ILE A O   
8362  C CB  . ILE A 1130 ? 0.2506 0.2595 0.2731 0.0030  -0.0324 -0.0369 1128 ILE A CB  
8363  C CG1 . ILE A 1130 ? 0.2734 0.2831 0.2906 0.0042  -0.0295 -0.0340 1128 ILE A CG1 
8364  C CG2 . ILE A 1130 ? 0.2484 0.2598 0.2695 0.0054  -0.0347 -0.0409 1128 ILE A CG2 
8365  C CD1 . ILE A 1130 ? 0.2531 0.2670 0.2705 0.0042  -0.0291 -0.0331 1128 ILE A CD1 
8366  N N   . ASP A 1131 ? 0.2520 0.2548 0.2814 0.0030  -0.0379 -0.0443 1129 ASP A N   
8367  C CA  . ASP A 1131 ? 0.2913 0.2930 0.3275 0.0018  -0.0413 -0.0476 1129 ASP A CA  
8368  C C   . ASP A 1131 ? 0.2792 0.2841 0.3204 0.0000  -0.0430 -0.0478 1129 ASP A C   
8369  O O   . ASP A 1131 ? 0.2803 0.2890 0.3191 0.0017  -0.0436 -0.0495 1129 ASP A O   
8370  C CB  . ASP A 1131 ? 0.2743 0.2762 0.3080 0.0050  -0.0433 -0.0528 1129 ASP A CB  
8371  C CG  . ASP A 1131 ? 0.3720 0.3728 0.4129 0.0041  -0.0471 -0.0570 1129 ASP A CG  
8372  O OD1 . ASP A 1131 ? 0.2987 0.2967 0.3466 0.0010  -0.0480 -0.0554 1129 ASP A OD1 
8373  O OD2 . ASP A 1131 ? 0.3195 0.3226 0.3593 0.0065  -0.0493 -0.0618 1129 ASP A OD2 
8374  N N   . ALA A 1132 ? 0.3130 0.3167 0.3616 -0.0035 -0.0438 -0.0457 1130 ALA A N   
8375  C CA  . ALA A 1132 ? 0.3507 0.3576 0.4049 -0.0055 -0.0455 -0.0457 1130 ALA A CA  
8376  C C   . ALA A 1132 ? 0.3616 0.3694 0.4192 -0.0045 -0.0494 -0.0512 1130 ALA A C   
8377  O O   . ALA A 1132 ? 0.3825 0.3939 0.4425 -0.0049 -0.0508 -0.0522 1130 ALA A O   
8378  C CB  . ALA A 1132 ? 0.3215 0.3273 0.3830 -0.0097 -0.0455 -0.0418 1130 ALA A CB  
8379  N N   . ALA A 1133 ? 0.3286 0.3333 0.3864 -0.0029 -0.0512 -0.0550 1131 ALA A N   
8380  C CA  . ALA A 1133 ? 0.3662 0.3721 0.4271 -0.0015 -0.0550 -0.0609 1131 ALA A CA  
8381  C C   . ALA A 1133 ? 0.3841 0.3945 0.4381 0.0019  -0.0549 -0.0637 1131 ALA A C   
8382  O O   . ALA A 1133 ? 0.3904 0.4029 0.4464 0.0032  -0.0580 -0.0686 1131 ALA A O   
8383  C CB  . ALA A 1133 ? 0.3857 0.3876 0.4486 -0.0005 -0.0570 -0.0646 1131 ALA A CB  
8384  N N   . SER A 1134 ? 0.3370 0.3490 0.3833 0.0035  -0.0516 -0.0607 1132 SER A N   
8385  C CA  . SER A 1134 ? 0.3326 0.3492 0.3728 0.0066  -0.0515 -0.0625 1132 SER A CA  
8386  C C   . SER A 1134 ? 0.3452 0.3658 0.3887 0.0055  -0.0528 -0.0626 1132 SER A C   
8387  O O   . SER A 1134 ? 0.3167 0.3414 0.3569 0.0079  -0.0539 -0.0651 1132 SER A O   
8388  C CB  . SER A 1134 ? 0.3190 0.3359 0.3512 0.0082  -0.0477 -0.0587 1132 SER A CB  
8389  O OG  . SER A 1134 ? 0.3213 0.3385 0.3548 0.0058  -0.0455 -0.0539 1132 SER A OG  
8390  N N   . GLY A 1135 ? 0.3318 0.3519 0.3816 0.0019  -0.0527 -0.0596 1133 GLY A N   
8391  C CA  . GLY A 1135 ? 0.3445 0.3688 0.3976 0.0008  -0.0537 -0.0592 1133 GLY A CA  
8392  C C   . GLY A 1135 ? 0.3788 0.4068 0.4261 0.0022  -0.0511 -0.0566 1133 GLY A C   
8393  O O   . GLY A 1135 ? 0.3711 0.4032 0.4200 0.0021  -0.0521 -0.0571 1133 GLY A O   
8394  N N   . LEU A 1136 ? 0.3101 0.3365 0.3509 0.0036  -0.0480 -0.0538 1134 LEU A N   
8395  C CA  . LEU A 1136 ? 0.3149 0.3444 0.3502 0.0054  -0.0458 -0.0516 1134 LEU A CA  
8396  C C   . LEU A 1136 ? 0.3750 0.4050 0.4119 0.0031  -0.0432 -0.0469 1134 LEU A C   
8397  O O   . LEU A 1136 ? 0.3473 0.3785 0.3795 0.0045  -0.0409 -0.0447 1134 LEU A O   
8398  C CB  . LEU A 1136 ? 0.2882 0.3163 0.3156 0.0085  -0.0441 -0.0515 1134 LEU A CB  
8399  C CG  . LEU A 1136 ? 0.3412 0.3707 0.3655 0.0115  -0.0463 -0.0560 1134 LEU A CG  
8400  C CD1 . LEU A 1136 ? 0.2887 0.3167 0.3059 0.0141  -0.0444 -0.0552 1134 LEU A CD1 
8401  C CD2 . LEU A 1136 ? 0.3569 0.3917 0.3801 0.0132  -0.0479 -0.0576 1134 LEU A CD2 
8402  N N   . GLN A 1137 ? 0.3663 0.3956 0.4099 -0.0004 -0.0436 -0.0455 1135 GLN A N   
8403  C CA  . GLN A 1137 ? 0.3669 0.3974 0.4120 -0.0026 -0.0410 -0.0411 1135 GLN A CA  
8404  C C   . GLN A 1137 ? 0.3554 0.3910 0.3992 -0.0016 -0.0403 -0.0404 1135 GLN A C   
8405  O O   . GLN A 1137 ? 0.3351 0.3716 0.3761 -0.0013 -0.0376 -0.0376 1135 GLN A O   
8406  C CB  . GLN A 1137 ? 0.3864 0.4167 0.4397 -0.0066 -0.0420 -0.0396 1135 GLN A CB  
8407  C CG  . GLN A 1137 ? 0.4045 0.4296 0.4594 -0.0081 -0.0419 -0.0386 1135 GLN A CG  
8408  C CD  . GLN A 1137 ? 0.3524 0.3746 0.4097 -0.0074 -0.0451 -0.0429 1135 GLN A CD  
8409  O OE1 . GLN A 1137 ? 0.3835 0.4074 0.4398 -0.0054 -0.0472 -0.0468 1135 GLN A OE1 
8410  N NE2 . GLN A 1137 ? 0.4286 0.4466 0.4894 -0.0091 -0.0457 -0.0422 1135 GLN A NE2 
8411  N N   . ALA A 1138 ? 0.3748 0.4136 0.4208 -0.0010 -0.0428 -0.0432 1136 ALA A N   
8412  C CA  . ALA A 1138 ? 0.3654 0.4092 0.4109 0.0000  -0.0423 -0.0426 1136 ALA A CA  
8413  C C   . ALA A 1138 ? 0.4089 0.4530 0.4470 0.0035  -0.0408 -0.0424 1136 ALA A C   
8414  O O   . ALA A 1138 ? 0.4482 0.4960 0.4856 0.0045  -0.0402 -0.0415 1136 ALA A O   
8415  C CB  . ALA A 1138 ? 0.3478 0.3950 0.3976 -0.0002 -0.0456 -0.0458 1136 ALA A CB  
8416  N N   . SER A 1139 ? 0.3795 0.4199 0.4123 0.0055  -0.0403 -0.0430 1137 SER A N   
8417  C CA  . SER A 1139 ? 0.3615 0.4021 0.3876 0.0087  -0.0389 -0.0422 1137 SER A CA  
8418  C C   . SER A 1139 ? 0.3248 0.3640 0.3488 0.0084  -0.0357 -0.0386 1137 SER A C   
8419  O O   . SER A 1139 ? 0.3521 0.3915 0.3715 0.0108  -0.0345 -0.0375 1137 SER A O   
8420  C CB  . SER A 1139 ? 0.3696 0.4077 0.3911 0.0109  -0.0397 -0.0442 1137 SER A CB  
8421  O OG  . SER A 1139 ? 0.3754 0.4158 0.3979 0.0120  -0.0427 -0.0480 1137 SER A OG  
8422  N N   . LEU A 1140 ? 0.3286 0.3662 0.3558 0.0056  -0.0344 -0.0367 1138 LEU A N   
8423  C CA  . LEU A 1140 ? 0.3604 0.3968 0.3857 0.0052  -0.0314 -0.0335 1138 LEU A CA  
8424  C C   . LEU A 1140 ? 0.3767 0.4167 0.4066 0.0029  -0.0304 -0.0317 1138 LEU A C   
8425  O O   . LEU A 1140 ? 0.4574 0.4965 0.4883 0.0010  -0.0286 -0.0294 1138 LEU A O   
8426  C CB  . LEU A 1140 ? 0.4029 0.4345 0.4269 0.0042  -0.0303 -0.0325 1138 LEU A CB  
8427  C CG  . LEU A 1140 ? 0.4073 0.4354 0.4257 0.0067  -0.0301 -0.0334 1138 LEU A CG  
8428  C CD1 . LEU A 1140 ? 0.4065 0.4304 0.4242 0.0054  -0.0285 -0.0316 1138 LEU A CD1 
8429  C CD2 . LEU A 1140 ? 0.3428 0.3721 0.3564 0.0096  -0.0290 -0.0325 1138 LEU A CD2 
8430  N N   . LYS A 1141 ? 0.3418 0.3864 0.3745 0.0030  -0.0317 -0.0327 1139 LYS A N   
8431  C CA  . LYS A 1141 ? 0.4782 0.5272 0.5154 0.0009  -0.0308 -0.0311 1139 LYS A CA  
8432  C C   . LYS A 1141 ? 0.4294 0.4800 0.4639 0.0024  -0.0283 -0.0295 1139 LYS A C   
8433  O O   . LYS A 1141 ? 0.4027 0.4528 0.4332 0.0054  -0.0282 -0.0301 1139 LYS A O   
8434  C CB  . LYS A 1141 ? 0.4581 0.5118 0.4995 0.0006  -0.0330 -0.0329 1139 LYS A CB  
8435  N N   . ASN A 1142 ? 0.3874 0.4403 0.4244 0.0003  -0.0265 -0.0273 1140 ASN A N   
8436  C CA  . ASN A 1142 ? 0.3446 0.4002 0.3803 0.0016  -0.0244 -0.0263 1140 ASN A CA  
8437  C C   . ASN A 1142 ? 0.3611 0.4122 0.3912 0.0038  -0.0229 -0.0257 1140 ASN A C   
8438  O O   . ASN A 1142 ? 0.3689 0.4208 0.3968 0.0063  -0.0223 -0.0261 1140 ASN A O   
8439  C CB  . ASN A 1142 ? 0.4800 0.5404 0.5169 0.0034  -0.0253 -0.0277 1140 ASN A CB  
8440  C CG  . ASN A 1142 ? 0.6521 0.7168 0.6945 0.0014  -0.0271 -0.0286 1140 ASN A CG  
8441  O OD1 . ASN A 1142 ? 0.6176 0.6824 0.6603 0.0024  -0.0294 -0.0305 1140 ASN A OD1 
8442  N ND2 . ASN A 1142 ? 0.5601 0.6288 0.6070 -0.0014 -0.0262 -0.0270 1140 ASN A ND2 
8443  N N   . LEU A 1143 ? 0.3666 0.4129 0.3947 0.0029  -0.0224 -0.0249 1141 LEU A N   
8444  C CA  . LEU A 1143 ? 0.3517 0.3940 0.3749 0.0047  -0.0209 -0.0241 1141 LEU A CA  
8445  C C   . LEU A 1143 ? 0.4000 0.4444 0.4233 0.0046  -0.0186 -0.0227 1141 LEU A C   
8446  O O   . LEU A 1143 ? 0.3759 0.4240 0.4026 0.0023  -0.0178 -0.0216 1141 LEU A O   
8447  C CB  . LEU A 1143 ? 0.3207 0.3579 0.3423 0.0036  -0.0208 -0.0235 1141 LEU A CB  
8448  C CG  . LEU A 1143 ? 0.3922 0.4261 0.4118 0.0048  -0.0227 -0.0253 1141 LEU A CG  
8449  C CD1 . LEU A 1143 ? 0.3636 0.3932 0.3829 0.0033  -0.0225 -0.0247 1141 LEU A CD1 
8450  C CD2 . LEU A 1143 ? 0.3461 0.3786 0.3607 0.0082  -0.0226 -0.0258 1141 LEU A CD2 
8451  N N   . PRO A 1144 ? 0.3520 0.3946 0.3719 0.0070  -0.0176 -0.0226 1142 PRO A N   
8452  C CA  . PRO A 1144 ? 0.3614 0.4052 0.3811 0.0070  -0.0155 -0.0215 1142 PRO A CA  
8453  C C   . PRO A 1144 ? 0.3327 0.3747 0.3525 0.0044  -0.0143 -0.0198 1142 PRO A C   
8454  O O   . PRO A 1144 ? 0.3285 0.3661 0.3469 0.0037  -0.0148 -0.0194 1142 PRO A O   
8455  C CB  . PRO A 1144 ? 0.3667 0.4069 0.3826 0.0099  -0.0152 -0.0216 1142 PRO A CB  
8456  C CG  . PRO A 1144 ? 0.3767 0.4161 0.3915 0.0118  -0.0172 -0.0227 1142 PRO A CG  
8457  C CD  . PRO A 1144 ? 0.3766 0.4160 0.3928 0.0099  -0.0185 -0.0233 1142 PRO A CD  
8458  N N   . GLN A 1145 ? 0.3620 0.4079 0.3837 0.0031  -0.0127 -0.0188 1143 GLN A N   
8459  C CA  . GLN A 1145 ? 0.3648 0.4098 0.3869 0.0006  -0.0115 -0.0168 1143 GLN A CA  
8460  C C   . GLN A 1145 ? 0.3426 0.3812 0.3606 0.0014  -0.0110 -0.0162 1143 GLN A C   
8461  O O   . GLN A 1145 ? 0.3335 0.3692 0.3515 -0.0003 -0.0110 -0.0150 1143 GLN A O   
8462  C CB  . GLN A 1145 ? 0.4083 0.4591 0.4321 -0.0003 -0.0098 -0.0160 1143 GLN A CB  
8463  N N   . THR A 1146 ? 0.3258 0.3623 0.3407 0.0041  -0.0105 -0.0170 1144 THR A N   
8464  C CA  . THR A 1146 ? 0.3535 0.3843 0.3647 0.0049  -0.0099 -0.0163 1144 THR A CA  
8465  C C   . THR A 1146 ? 0.2773 0.3037 0.2871 0.0049  -0.0112 -0.0165 1144 THR A C   
8466  O O   . THR A 1146 ? 0.3007 0.3232 0.3088 0.0042  -0.0108 -0.0156 1144 THR A O   
8467  C CB  . THR A 1146 ? 0.3872 0.4167 0.3962 0.0078  -0.0095 -0.0170 1144 THR A CB  
8468  O OG1 . THR A 1146 ? 0.3322 0.3624 0.3414 0.0096  -0.0111 -0.0183 1144 THR A OG1 
8469  C CG2 . THR A 1146 ? 0.3739 0.4070 0.3842 0.0081  -0.0082 -0.0172 1144 THR A CG2 
8470  N N   . VAL A 1147 ? 0.3080 0.3353 0.3184 0.0057  -0.0130 -0.0179 1145 VAL A N   
8471  C CA  . VAL A 1147 ? 0.2661 0.2901 0.2753 0.0059  -0.0144 -0.0186 1145 VAL A CA  
8472  C C   . VAL A 1147 ? 0.2613 0.2855 0.2738 0.0031  -0.0152 -0.0184 1145 VAL A C   
8473  O O   . VAL A 1147 ? 0.2907 0.3112 0.3025 0.0024  -0.0156 -0.0183 1145 VAL A O   
8474  C CB  . VAL A 1147 ? 0.2661 0.2913 0.2746 0.0080  -0.0162 -0.0203 1145 VAL A CB  
8475  C CG1 . VAL A 1147 ? 0.2772 0.2995 0.2840 0.0085  -0.0177 -0.0215 1145 VAL A CG1 
8476  C CG2 . VAL A 1147 ? 0.2894 0.3143 0.2953 0.0108  -0.0156 -0.0201 1145 VAL A CG2 
8477  N N   . GLY A 1148 ? 0.2910 0.3198 0.3077 0.0013  -0.0154 -0.0182 1146 GLY A N   
8478  C CA  . GLY A 1148 ? 0.2780 0.3073 0.2987 -0.0017 -0.0162 -0.0175 1146 GLY A CA  
8479  C C   . GLY A 1148 ? 0.3046 0.3312 0.3250 -0.0034 -0.0150 -0.0154 1146 GLY A C   
8480  O O   . GLY A 1148 ? 0.3329 0.3570 0.3554 -0.0051 -0.0160 -0.0150 1146 GLY A O   
8481  N N   . LEU A 1149 ? 0.2919 0.3187 0.3100 -0.0028 -0.0129 -0.0141 1147 LEU A N   
8482  C CA  . LEU A 1149 ? 0.3147 0.3390 0.3321 -0.0042 -0.0117 -0.0121 1147 LEU A CA  
8483  C C   . LEU A 1149 ? 0.3026 0.3209 0.3176 -0.0034 -0.0124 -0.0127 1147 LEU A C   
8484  O O   . LEU A 1149 ? 0.3515 0.3672 0.3672 -0.0049 -0.0122 -0.0114 1147 LEU A O   
8485  C CB  . LEU A 1149 ? 0.3638 0.3895 0.3788 -0.0033 -0.0095 -0.0113 1147 LEU A CB  
8486  C CG  . LEU A 1149 ? 0.5027 0.5349 0.5200 -0.0042 -0.0084 -0.0105 1147 LEU A CG  
8487  C CD1 . LEU A 1149 ? 0.4774 0.5103 0.4922 -0.0031 -0.0065 -0.0101 1147 LEU A CD1 
8488  C CD2 . LEU A 1149 ? 0.5158 0.5512 0.5374 -0.0076 -0.0085 -0.0083 1147 LEU A CD2 
8489  N N   . ARG A 1150 ? 0.2996 0.3158 0.3116 -0.0008 -0.0132 -0.0147 1148 ARG A N   
8490  C CA  . ARG A 1150 ? 0.2651 0.2764 0.2743 0.0003  -0.0137 -0.0155 1148 ARG A CA  
8491  C C   . ARG A 1150 ? 0.2560 0.2663 0.2674 -0.0001 -0.0161 -0.0174 1148 ARG A C   
8492  O O   . ARG A 1150 ? 0.3041 0.3109 0.3137 0.0009  -0.0167 -0.0185 1148 ARG A O   
8493  C CB  . ARG A 1150 ? 0.2534 0.2636 0.2581 0.0034  -0.0133 -0.0163 1148 ARG A CB  
8494  C CG  . ARG A 1150 ? 0.2789 0.2886 0.2814 0.0041  -0.0112 -0.0148 1148 ARG A CG  
8495  C CD  . ARG A 1150 ? 0.3027 0.3085 0.3011 0.0060  -0.0108 -0.0147 1148 ARG A CD  
8496  N NE  . ARG A 1150 ? 0.3068 0.3123 0.3033 0.0071  -0.0091 -0.0135 1148 ARG A NE  
8497  C CZ  . ARG A 1150 ? 0.2964 0.3002 0.2899 0.0093  -0.0089 -0.0134 1148 ARG A CZ  
8498  N NH1 . ARG A 1150 ? 0.2497 0.2523 0.2411 0.0108  -0.0099 -0.0143 1148 ARG A NH1 
8499  N NH2 . ARG A 1150 ? 0.2616 0.2650 0.2543 0.0101  -0.0076 -0.0124 1148 ARG A NH2 
8500  N N   . VAL A 1151 ? 0.2726 0.2862 0.2881 -0.0014 -0.0174 -0.0180 1149 VAL A N   
8501  C CA  . VAL A 1151 ? 0.2421 0.2552 0.2599 -0.0015 -0.0200 -0.0204 1149 VAL A CA  
8502  C C   . VAL A 1151 ? 0.3362 0.3494 0.3598 -0.0047 -0.0210 -0.0194 1149 VAL A C   
8503  O O   . VAL A 1151 ? 0.3365 0.3531 0.3635 -0.0069 -0.0204 -0.0174 1149 VAL A O   
8504  C CB  . VAL A 1151 ? 0.2628 0.2796 0.2808 -0.0002 -0.0211 -0.0222 1149 VAL A CB  
8505  C CG1 . VAL A 1151 ? 0.2902 0.3072 0.3116 -0.0007 -0.0239 -0.0247 1149 VAL A CG1 
8506  C CG2 . VAL A 1151 ? 0.2736 0.2899 0.2862 0.0031  -0.0205 -0.0230 1149 VAL A CG2 
8507  N N   . SER A 1152 ? 0.2824 0.2920 0.3076 -0.0051 -0.0226 -0.0207 1150 SER A N   
8508  C CA  . SER A 1152 ? 0.3477 0.3571 0.3794 -0.0080 -0.0244 -0.0203 1150 SER A CA  
8509  C C   . SER A 1152 ? 0.3273 0.3353 0.3607 -0.0070 -0.0273 -0.0241 1150 SER A C   
8510  O O   . SER A 1152 ? 0.3149 0.3216 0.3439 -0.0042 -0.0277 -0.0268 1150 SER A O   
8511  C CB  . SER A 1152 ? 0.3238 0.3298 0.3570 -0.0098 -0.0238 -0.0179 1150 SER A CB  
8512  O OG  . SER A 1152 ? 0.4021 0.4035 0.4323 -0.0079 -0.0242 -0.0198 1150 SER A OG  
8513  N N   . TRP A 1153 ? 0.2918 0.3008 0.3318 -0.0094 -0.0295 -0.0244 1151 TRP A N   
8514  C CA  . TRP A 1153 ? 0.3497 0.3573 0.3926 -0.0088 -0.0327 -0.0283 1151 TRP A CA  
8515  C C   . TRP A 1153 ? 0.3564 0.3599 0.4044 -0.0107 -0.0342 -0.0281 1151 TRP A C   
8516  O O   . TRP A 1153 ? 0.3910 0.3945 0.4433 -0.0137 -0.0337 -0.0245 1151 TRP A O   
8517  C CB  . TRP A 1153 ? 0.3135 0.3253 0.3609 -0.0099 -0.0344 -0.0292 1151 TRP A CB  
8518  C CG  . TRP A 1153 ? 0.3623 0.3778 0.4050 -0.0076 -0.0336 -0.0303 1151 TRP A CG  
8519  C CD1 . TRP A 1153 ? 0.3432 0.3622 0.3839 -0.0076 -0.0313 -0.0278 1151 TRP A CD1 
8520  C CD2 . TRP A 1153 ? 0.3270 0.3433 0.3667 -0.0047 -0.0352 -0.0342 1151 TRP A CD2 
8521  N NE1 . TRP A 1153 ? 0.3537 0.3753 0.3907 -0.0050 -0.0314 -0.0298 1151 TRP A NE1 
8522  C CE2 . TRP A 1153 ? 0.3276 0.3477 0.3638 -0.0032 -0.0337 -0.0335 1151 TRP A CE2 
8523  C CE3 . TRP A 1153 ? 0.3103 0.3248 0.3501 -0.0031 -0.0377 -0.0383 1151 TRP A CE3 
8524  C CZ2 . TRP A 1153 ? 0.3048 0.3268 0.3375 -0.0003 -0.0348 -0.0363 1151 TRP A CZ2 
8525  C CZ3 . TRP A 1153 ? 0.2947 0.3118 0.3308 -0.0002 -0.0387 -0.0413 1151 TRP A CZ3 
8526  C CH2 . TRP A 1153 ? 0.3458 0.3665 0.3784 0.0011  -0.0372 -0.0400 1151 TRP A CH2 
8527  N N   . SER A 1154 ? 0.2922 0.2926 0.3398 -0.0089 -0.0362 -0.0319 1152 SER A N   
8528  C CA  . SER A 1154 ? 0.2987 0.2946 0.3506 -0.0101 -0.0376 -0.0321 1152 SER A CA  
8529  C C   . SER A 1154 ? 0.3487 0.3439 0.4064 -0.0102 -0.0415 -0.0364 1152 SER A C   
8530  O O   . SER A 1154 ? 0.3321 0.3280 0.3866 -0.0073 -0.0428 -0.0409 1152 SER A O   
8531  C CB  . SER A 1154 ? 0.3236 0.3162 0.3698 -0.0077 -0.0362 -0.0329 1152 SER A CB  
8532  O OG  . SER A 1154 ? 0.3486 0.3369 0.3993 -0.0088 -0.0377 -0.0331 1152 SER A OG  
8533  N N   . LYS A 1155 ? 0.3388 0.3327 0.4049 -0.0134 -0.0435 -0.0351 1153 LYS A N   
8534  C CA  . LYS A 1155 ? 0.3661 0.3582 0.4388 -0.0135 -0.0476 -0.0393 1153 LYS A CA  
8535  C C   . LYS A 1155 ? 0.3988 0.3856 0.4736 -0.0130 -0.0488 -0.0409 1153 LYS A C   
8536  O O   . LYS A 1155 ? 0.5713 0.5564 0.6483 -0.0114 -0.0518 -0.0461 1153 LYS A O   
8537  C CB  . LYS A 1155 ? 0.3563 0.3500 0.4383 -0.0174 -0.0495 -0.0372 1153 LYS A CB  
8538  N N   . ASP A 1156 ? 0.3608 0.3452 0.4346 -0.0142 -0.0467 -0.0367 1154 ASP A N   
8539  C CA  . ASP A 1156 ? 0.3559 0.3353 0.4319 -0.0139 -0.0476 -0.0374 1154 ASP A CA  
8540  C C   . ASP A 1156 ? 0.3719 0.3507 0.4389 -0.0115 -0.0441 -0.0363 1154 ASP A C   
8541  O O   . ASP A 1156 ? 0.3414 0.3202 0.4069 -0.0131 -0.0415 -0.0313 1154 ASP A O   
8542  C CB  . ASP A 1156 ? 0.3961 0.3734 0.4807 -0.0179 -0.0485 -0.0328 1154 ASP A CB  
8543  C CG  . ASP A 1156 ? 0.5336 0.5056 0.6213 -0.0178 -0.0496 -0.0331 1154 ASP A CG  
8544  O OD1 . ASP A 1156 ? 0.5501 0.5201 0.6332 -0.0145 -0.0497 -0.0372 1154 ASP A OD1 
8545  O OD2 . ASP A 1156 ? 0.6119 0.5819 0.7066 -0.0210 -0.0505 -0.0291 1154 ASP A OD2 
8546  N N   . TRP A 1157 ? 0.3211 0.2998 0.3824 -0.0079 -0.0442 -0.0408 1155 TRP A N   
8547  C CA  . TRP A 1157 ? 0.3046 0.2833 0.3573 -0.0056 -0.0409 -0.0397 1155 TRP A CA  
8548  C C   . TRP A 1157 ? 0.3379 0.3127 0.3916 -0.0065 -0.0398 -0.0368 1155 TRP A C   
8549  O O   . TRP A 1157 ? 0.3437 0.3188 0.3923 -0.0064 -0.0367 -0.0334 1155 TRP A O   
8550  C CB  . TRP A 1157 ? 0.3217 0.3012 0.3690 -0.0016 -0.0415 -0.0449 1155 TRP A CB  
8551  C CG  . TRP A 1157 ? 0.3043 0.2878 0.3500 -0.0001 -0.0427 -0.0481 1155 TRP A CG  
8552  C CD1 . TRP A 1157 ? 0.3321 0.3188 0.3794 -0.0017 -0.0428 -0.0466 1155 TRP A CD1 
8553  C CD2 . TRP A 1157 ? 0.2782 0.2635 0.3203 0.0034  -0.0441 -0.0535 1155 TRP A CD2 
8554  N NE1 . TRP A 1157 ? 0.3270 0.3169 0.3720 0.0005  -0.0442 -0.0506 1155 TRP A NE1 
8555  C CE2 . TRP A 1157 ? 0.2931 0.2825 0.3348 0.0037  -0.0450 -0.0548 1155 TRP A CE2 
8556  C CE3 . TRP A 1157 ? 0.3532 0.3376 0.3924 0.0064  -0.0446 -0.0573 1155 TRP A CE3 
8557  C CZ2 . TRP A 1157 ? 0.3270 0.3197 0.3653 0.0069  -0.0465 -0.0597 1155 TRP A CZ2 
8558  C CZ3 . TRP A 1157 ? 0.3009 0.2889 0.3367 0.0095  -0.0459 -0.0622 1155 TRP A CZ3 
8559  C CH2 . TRP A 1157 ? 0.3296 0.3217 0.3650 0.0097  -0.0469 -0.0633 1155 TRP A CH2 
8560  N N   . ALA A 1158 ? 0.3115 0.2827 0.3721 -0.0074 -0.0426 -0.0384 1156 ALA A N   
8561  C CA  . ALA A 1158 ? 0.3200 0.2874 0.3820 -0.0082 -0.0418 -0.0357 1156 ALA A CA  
8562  C C   . ALA A 1158 ? 0.3701 0.3380 0.4340 -0.0117 -0.0399 -0.0291 1156 ALA A C   
8563  O O   . ALA A 1158 ? 0.4904 0.4568 0.5520 -0.0119 -0.0379 -0.0260 1156 ALA A O   
8564  C CB  . ALA A 1158 ? 0.4183 0.3816 0.4882 -0.0084 -0.0455 -0.0389 1156 ALA A CB  
8565  N N   . ALA A 1159 ? 0.3383 0.3088 0.4065 -0.0143 -0.0406 -0.0270 1157 ALA A N   
8566  C CA  . ALA A 1159 ? 0.4173 0.3894 0.4876 -0.0176 -0.0389 -0.0207 1157 ALA A CA  
8567  C C   . ALA A 1159 ? 0.4210 0.3969 0.4833 -0.0169 -0.0350 -0.0182 1157 ALA A C   
8568  O O   . ALA A 1159 ? 0.4396 0.4166 0.5016 -0.0188 -0.0330 -0.0133 1157 ALA A O   
8569  C CB  . ALA A 1159 ? 0.3965 0.3707 0.4747 -0.0208 -0.0410 -0.0191 1157 ALA A CB  
8570  N N   . ASP A 1160 ? 0.4211 0.3990 0.4770 -0.0140 -0.0341 -0.0214 1158 ASP A N   
8571  C CA  . ASP A 1160 ? 0.4107 0.3922 0.4599 -0.0133 -0.0309 -0.0193 1158 ASP A CA  
8572  C C   . ASP A 1160 ? 0.3477 0.3278 0.3893 -0.0106 -0.0285 -0.0198 1158 ASP A C   
8573  O O   . ASP A 1160 ? 0.3856 0.3682 0.4216 -0.0096 -0.0261 -0.0186 1158 ASP A O   
8574  C CB  . ASP A 1160 ? 0.4095 0.3948 0.4575 -0.0124 -0.0315 -0.0217 1158 ASP A CB  
8575  C CG  . ASP A 1160 ? 0.4123 0.3997 0.4679 -0.0154 -0.0335 -0.0206 1158 ASP A CG  
8576  O OD1 . ASP A 1160 ? 0.5472 0.5343 0.6079 -0.0184 -0.0335 -0.0167 1158 ASP A OD1 
8577  O OD2 . ASP A 1160 ? 0.4117 0.4012 0.4683 -0.0147 -0.0351 -0.0235 1158 ASP A OD2 
8578  N N   . GLY A 1161 ? 0.3390 0.3152 0.3806 -0.0093 -0.0293 -0.0216 1159 GLY A N   
8579  C CA  . GLY A 1161 ? 0.3521 0.3270 0.3870 -0.0069 -0.0271 -0.0218 1159 GLY A CA  
8580  C C   . GLY A 1161 ? 0.4261 0.4002 0.4605 -0.0086 -0.0250 -0.0172 1159 GLY A C   
8581  O O   . GLY A 1161 ? 0.4575 0.4330 0.4958 -0.0114 -0.0248 -0.0135 1159 GLY A O   
8582  N N   . PRO A 1162 ? 0.3702 0.3425 0.3999 -0.0067 -0.0233 -0.0172 1160 PRO A N   
8583  C CA  . PRO A 1162 ? 0.3799 0.3513 0.4048 -0.0033 -0.0231 -0.0209 1160 PRO A CA  
8584  C C   . PRO A 1162 ? 0.3828 0.3576 0.4019 -0.0014 -0.0217 -0.0218 1160 PRO A C   
8585  O O   . PRO A 1162 ? 0.3610 0.3380 0.3777 -0.0021 -0.0198 -0.0191 1160 PRO A O   
8586  C CB  . PRO A 1162 ? 0.3754 0.3444 0.3978 -0.0028 -0.0214 -0.0191 1160 PRO A CB  
8587  C CG  . PRO A 1162 ? 0.4874 0.4576 0.5100 -0.0052 -0.0195 -0.0143 1160 PRO A CG  
8588  C CD  . PRO A 1162 ? 0.4249 0.3965 0.4537 -0.0080 -0.0212 -0.0131 1160 PRO A CD  
8589  N N   . PHE A 1163 ? 0.2856 0.2609 0.3024 0.0011  -0.0228 -0.0257 1161 PHE A N   
8590  C CA  . PHE A 1163 ? 0.2558 0.2341 0.2669 0.0033  -0.0216 -0.0264 1161 PHE A CA  
8591  C C   . PHE A 1163 ? 0.2719 0.2495 0.2775 0.0056  -0.0196 -0.0262 1161 PHE A C   
8592  O O   . PHE A 1163 ? 0.2854 0.2603 0.2915 0.0058  -0.0195 -0.0263 1161 PHE A O   
8593  C CB  . PHE A 1163 ? 0.2492 0.2296 0.2610 0.0048  -0.0239 -0.0305 1161 PHE A CB  
8594  C CG  . PHE A 1163 ? 0.2805 0.2615 0.2983 0.0024  -0.0260 -0.0308 1161 PHE A CG  
8595  C CD1 . PHE A 1163 ? 0.3132 0.2965 0.3318 0.0006  -0.0250 -0.0279 1161 PHE A CD1 
8596  C CD2 . PHE A 1163 ? 0.2699 0.2493 0.2930 0.0020  -0.0290 -0.0339 1161 PHE A CD2 
8597  C CE1 . PHE A 1163 ? 0.3233 0.3077 0.3479 -0.0017 -0.0268 -0.0279 1161 PHE A CE1 
8598  C CE2 . PHE A 1163 ? 0.3083 0.2884 0.3377 -0.0003 -0.0310 -0.0339 1161 PHE A CE2 
8599  C CZ  . PHE A 1163 ? 0.3287 0.3113 0.3587 -0.0023 -0.0299 -0.0307 1161 PHE A CZ  
8600  N N   . ALA A 1164 ? 0.2598 0.2398 0.2603 0.0072  -0.0181 -0.0256 1162 ALA A N   
8601  C CA  . ALA A 1164 ? 0.2824 0.2622 0.2778 0.0093  -0.0162 -0.0249 1162 ALA A CA  
8602  C C   . ALA A 1164 ? 0.2700 0.2525 0.2616 0.0122  -0.0167 -0.0276 1162 ALA A C   
8603  O O   . ALA A 1164 ? 0.3021 0.2853 0.2892 0.0141  -0.0152 -0.0267 1162 ALA A O   
8604  C CB  . ALA A 1164 ? 0.3113 0.2915 0.3043 0.0086  -0.0137 -0.0212 1162 ALA A CB  
8605  N N   . GLY A 1165 ? 0.2469 0.2311 0.2402 0.0127  -0.0190 -0.0306 1163 GLY A N   
8606  C CA  . GLY A 1165 ? 0.2704 0.2579 0.2603 0.0155  -0.0198 -0.0334 1163 GLY A CA  
8607  C C   . GLY A 1165 ? 0.2599 0.2494 0.2527 0.0152  -0.0222 -0.0361 1163 GLY A C   
8608  O O   . GLY A 1165 ? 0.2553 0.2437 0.2527 0.0127  -0.0230 -0.0353 1163 GLY A O   
8609  N N   . ALA A 1166 ? 0.2563 0.2492 0.2465 0.0177  -0.0234 -0.0391 1164 ALA A N   
8610  C CA  . ALA A 1166 ? 0.2583 0.2535 0.2511 0.0176  -0.0259 -0.0418 1164 ALA A CA  
8611  C C   . ALA A 1166 ? 0.2664 0.2663 0.2543 0.0203  -0.0260 -0.0428 1164 ALA A C   
8612  O O   . ALA A 1166 ? 0.2883 0.2901 0.2715 0.0226  -0.0250 -0.0429 1164 ALA A O   
8613  C CB  . ALA A 1166 ? 0.2542 0.2484 0.2516 0.0176  -0.0287 -0.0464 1164 ALA A CB  
8614  N N   . LEU A 1167 ? 0.2377 0.2400 0.2270 0.0199  -0.0272 -0.0433 1165 LEU A N   
8615  C CA  . LEU A 1167 ? 0.2176 0.2248 0.2033 0.0223  -0.0280 -0.0447 1165 LEU A CA  
8616  C C   . LEU A 1167 ? 0.2641 0.2732 0.2536 0.0223  -0.0313 -0.0492 1165 LEU A C   
8617  O O   . LEU A 1167 ? 0.2771 0.2845 0.2719 0.0198  -0.0324 -0.0493 1165 LEU A O   
8618  C CB  . LEU A 1167 ? 0.2725 0.2812 0.2564 0.0220  -0.0266 -0.0409 1165 LEU A CB  
8619  C CG  . LEU A 1167 ? 0.2386 0.2453 0.2196 0.0218  -0.0236 -0.0365 1165 LEU A CG  
8620  C CD1 . LEU A 1167 ? 0.2642 0.2719 0.2448 0.0214  -0.0226 -0.0334 1165 LEU A CD1 
8621  C CD2 . LEU A 1167 ? 0.2647 0.2731 0.2403 0.0245  -0.0226 -0.0362 1165 LEU A CD2 
8622  N N   . VAL A 1168 ? 0.2287 0.2416 0.2156 0.0250  -0.0328 -0.0529 1166 VAL A N   
8623  C CA  . VAL A 1168 ? 0.2261 0.2409 0.2166 0.0254  -0.0361 -0.0580 1166 VAL A CA  
8624  C C   . VAL A 1168 ? 0.2334 0.2543 0.2200 0.0279  -0.0371 -0.0595 1166 VAL A C   
8625  O O   . VAL A 1168 ? 0.2574 0.2815 0.2380 0.0304  -0.0358 -0.0584 1166 VAL A O   
8626  C CB  . VAL A 1168 ? 0.2688 0.2824 0.2609 0.0264  -0.0376 -0.0624 1166 VAL A CB  
8627  C CG1 . VAL A 1168 ? 0.2507 0.2662 0.2472 0.0268  -0.0415 -0.0682 1166 VAL A CG1 
8628  C CG2 . VAL A 1168 ? 0.2752 0.2827 0.2712 0.0240  -0.0366 -0.0605 1166 VAL A CG2 
8629  N N   . GLU A 1169 ? 0.2329 0.2555 0.2229 0.0273  -0.0395 -0.0617 1167 GLU A N   
8630  C CA  . GLU A 1169 ? 0.2421 0.2708 0.2292 0.0296  -0.0411 -0.0637 1167 GLU A CA  
8631  C C   . GLU A 1169 ? 0.2824 0.3129 0.2733 0.0303  -0.0447 -0.0701 1167 GLU A C   
8632  O O   . GLU A 1169 ? 0.2713 0.2985 0.2689 0.0278  -0.0465 -0.0718 1167 GLU A O   
8633  C CB  . GLU A 1169 ? 0.2432 0.2730 0.2312 0.0284  -0.0408 -0.0607 1167 GLU A CB  
8634  C CG  . GLU A 1169 ? 0.2666 0.3026 0.2520 0.0307  -0.0425 -0.0625 1167 GLU A CG  
8635  C CD  . GLU A 1169 ? 0.2686 0.3054 0.2566 0.0292  -0.0428 -0.0604 1167 GLU A CD  
8636  O OE1 . GLU A 1169 ? 0.2682 0.3009 0.2605 0.0263  -0.0420 -0.0583 1167 GLU A OE1 
8637  O OE2 . GLU A 1169 ? 0.2716 0.3134 0.2573 0.0310  -0.0439 -0.0609 1167 GLU A OE2 
8638  N N   . GLY A 1170 ? 0.2603 0.2962 0.2473 0.0335  -0.0460 -0.0737 1168 GLY A N   
8639  C CA  . GLY A 1170 ? 0.2563 0.2947 0.2468 0.0344  -0.0497 -0.0802 1168 GLY A CA  
8640  C C   . GLY A 1170 ? 0.2677 0.3124 0.2529 0.0384  -0.0505 -0.0840 1168 GLY A C   
8641  O O   . GLY A 1170 ? 0.3153 0.3621 0.2942 0.0402  -0.0480 -0.0813 1168 GLY A O   
8642  N N   . ASP A 1171 ? 0.3023 0.3502 0.2903 0.0396  -0.0541 -0.0905 1169 ASP A N   
8643  C CA  . ASP A 1171 ? 0.2865 0.3406 0.2701 0.0435  -0.0551 -0.0951 1169 ASP A CA  
8644  C C   . ASP A 1171 ? 0.3128 0.3636 0.2976 0.0439  -0.0546 -0.0973 1169 ASP A C   
8645  O O   . ASP A 1171 ? 0.2759 0.3195 0.2647 0.0411  -0.0535 -0.0950 1169 ASP A O   
8646  C CB  . ASP A 1171 ? 0.3028 0.3621 0.2888 0.0450  -0.0592 -0.1017 1169 ASP A CB  
8647  C CG  . ASP A 1171 ? 0.4080 0.4625 0.4033 0.0428  -0.0626 -0.1066 1169 ASP A CG  
8648  O OD1 . ASP A 1171 ? 0.3251 0.3734 0.3248 0.0411  -0.0622 -0.1067 1169 ASP A OD1 
8649  O OD2 . ASP A 1171 ? 0.4762 0.5335 0.4747 0.0430  -0.0658 -0.1106 1169 ASP A OD2 
8650  N N   . ALA A 1172 ? 0.3274 0.3840 0.3084 0.0474  -0.0554 -0.1018 1170 ALA A N   
8651  C CA  . ALA A 1172 ? 0.3190 0.3734 0.2999 0.0483  -0.0544 -0.1033 1170 ALA A CA  
8652  C C   . ALA A 1172 ? 0.3285 0.3759 0.3183 0.0460  -0.0567 -0.1069 1170 ALA A C   
8653  O O   . ALA A 1172 ? 0.3198 0.3612 0.3116 0.0444  -0.0549 -0.1044 1170 ALA A O   
8654  C CB  . ALA A 1172 ? 0.3669 0.4298 0.3427 0.0527  -0.0552 -0.1082 1170 ALA A CB  
8655  N N   . GLU A 1173 ? 0.3445 0.3923 0.3401 0.0458  -0.0606 -0.1125 1171 GLU A N   
8656  C CA  . GLU A 1173 ? 0.3583 0.3995 0.3630 0.0437  -0.0631 -0.1159 1171 GLU A CA  
8657  C C   . GLU A 1173 ? 0.3315 0.3649 0.3412 0.0392  -0.0619 -0.1099 1171 GLU A C   
8658  O O   . GLU A 1173 ? 0.3691 0.3961 0.3848 0.0371  -0.0622 -0.1098 1171 GLU A O   
8659  C CB  . GLU A 1173 ? 0.4212 0.4652 0.4314 0.0449  -0.0679 -0.1239 1171 GLU A CB  
8660  C CG  . GLU A 1173 ? 0.4725 0.5234 0.4792 0.0494  -0.0695 -0.1310 1171 GLU A CG  
8661  C CD  . GLU A 1173 ? 0.5699 0.6183 0.5761 0.0506  -0.0680 -0.1317 1171 GLU A CD  
8662  O OE1 . GLU A 1173 ? 0.4984 0.5390 0.5116 0.0481  -0.0685 -0.1313 1171 GLU A OE1 
8663  O OE2 . GLU A 1173 ? 0.5183 0.5731 0.5172 0.0540  -0.0662 -0.1325 1171 GLU A OE2 
8664  N N   . ARG A 1174 ? 0.2882 0.3226 0.2957 0.0376  -0.0604 -0.1050 1172 ARG A N   
8665  C CA  . ARG A 1174 ? 0.2985 0.3265 0.3098 0.0335  -0.0587 -0.0989 1172 ARG A CA  
8666  C C   . ARG A 1174 ? 0.3134 0.3376 0.3212 0.0329  -0.0549 -0.0938 1172 ARG A C   
8667  O O   . ARG A 1174 ? 0.2871 0.3050 0.2999 0.0301  -0.0543 -0.0913 1172 ARG A O   
8668  C CB  . ARG A 1174 ? 0.2966 0.3271 0.3058 0.0325  -0.0579 -0.0951 1172 ARG A CB  
8669  C CG  . ARG A 1174 ? 0.3060 0.3312 0.3179 0.0286  -0.0556 -0.0885 1172 ARG A CG  
8670  C CD  . ARG A 1174 ? 0.3323 0.3524 0.3540 0.0253  -0.0580 -0.0898 1172 ARG A CD  
8671  N NE  . ARG A 1174 ? 0.3035 0.3196 0.3278 0.0217  -0.0559 -0.0836 1172 ARG A NE  
8672  C CZ  . ARG A 1174 ? 0.3249 0.3357 0.3565 0.0184  -0.0566 -0.0824 1172 ARG A CZ  
8673  N NH1 . ARG A 1174 ? 0.3414 0.3495 0.3790 0.0182  -0.0594 -0.0868 1172 ARG A NH1 
8674  N NH2 . ARG A 1174 ? 0.2937 0.3021 0.3268 0.0154  -0.0544 -0.0766 1172 ARG A NH2 
8675  N N   . ILE A 1175 ? 0.2797 0.3081 0.2793 0.0356  -0.0524 -0.0921 1173 ILE A N   
8676  C CA  . ILE A 1175 ? 0.3037 0.3291 0.2999 0.0353  -0.0488 -0.0875 1173 ILE A CA  
8677  C C   . ILE A 1175 ? 0.2534 0.2749 0.2537 0.0354  -0.0497 -0.0907 1173 ILE A C   
8678  O O   . ILE A 1175 ? 0.3114 0.3270 0.3141 0.0331  -0.0481 -0.0872 1173 ILE A O   
8679  C CB  . ILE A 1175 ? 0.2640 0.2954 0.2512 0.0384  -0.0464 -0.0856 1173 ILE A CB  
8680  C CG1 . ILE A 1175 ? 0.2795 0.3134 0.2632 0.0379  -0.0451 -0.0810 1173 ILE A CG1 
8681  C CG2 . ILE A 1175 ? 0.2738 0.3027 0.2580 0.0386  -0.0433 -0.0822 1173 ILE A CG2 
8682  C CD1 . ILE A 1175 ? 0.3064 0.3469 0.2819 0.0410  -0.0434 -0.0792 1173 ILE A CD1 
8683  N N   . ARG A 1176 ? 0.3358 0.3607 0.3370 0.0381  -0.0524 -0.0976 1174 ARG A N   
8684  C CA  . ARG A 1176 ? 0.2796 0.3009 0.2852 0.0385  -0.0537 -0.1013 1174 ARG A CA  
8685  C C   . ARG A 1176 ? 0.2553 0.2691 0.2703 0.0347  -0.0554 -0.1007 1174 ARG A C   
8686  O O   . ARG A 1176 ? 0.2951 0.3036 0.3130 0.0333  -0.0544 -0.0987 1174 ARG A O   
8687  C CB  . ARG A 1176 ? 0.2732 0.3000 0.2791 0.0421  -0.0568 -0.1097 1174 ARG A CB  
8688  C CG  . ARG A 1176 ? 0.3455 0.3702 0.3537 0.0436  -0.0573 -0.1133 1174 ARG A CG  
8689  C CD  . ARG A 1176 ? 0.3609 0.3895 0.3724 0.0466  -0.0613 -0.1226 1174 ARG A CD  
8690  N NE  . ARG A 1176 ? 0.3771 0.4152 0.3820 0.0501  -0.0617 -0.1256 1174 ARG A NE  
8691  C CZ  . ARG A 1176 ? 0.4676 0.5125 0.4651 0.0537  -0.0600 -0.1269 1174 ARG A CZ  
8692  N NH1 . ARG A 1176 ? 0.3789 0.4224 0.3747 0.0545  -0.0577 -0.1254 1174 ARG A NH1 
8693  N NH2 . ARG A 1176 ? 0.4504 0.5043 0.4424 0.0566  -0.0607 -0.1295 1174 ARG A NH2 
8694  N N   . ALA A 1177 ? 0.2698 0.2833 0.2898 0.0330  -0.0580 -0.1020 1175 ALA A N   
8695  C CA  . ALA A 1177 ? 0.3395 0.3464 0.3690 0.0292  -0.0598 -0.1010 1175 ALA A CA  
8696  C C   . ALA A 1177 ? 0.3139 0.3162 0.3430 0.0259  -0.0564 -0.0930 1175 ALA A C   
8697  O O   . ALA A 1177 ? 0.3285 0.3251 0.3631 0.0236  -0.0565 -0.0912 1175 ALA A O   
8698  C CB  . ALA A 1177 ? 0.3088 0.3173 0.3433 0.0279  -0.0630 -0.1034 1175 ALA A CB  
8699  N N   . VAL A 1178 ? 0.2933 0.2982 0.3160 0.0257  -0.0535 -0.0882 1176 VAL A N   
8700  C CA  . VAL A 1178 ? 0.2562 0.2574 0.2781 0.0229  -0.0503 -0.0811 1176 VAL A CA  
8701  C C   . VAL A 1178 ? 0.3207 0.3192 0.3398 0.0236  -0.0478 -0.0791 1176 VAL A C   
8702  O O   . VAL A 1178 ? 0.2981 0.2916 0.3204 0.0209  -0.0467 -0.0753 1176 VAL A O   
8703  C CB  . VAL A 1178 ? 0.2745 0.2794 0.2903 0.0230  -0.0479 -0.0770 1176 VAL A CB  
8704  C CG1 . VAL A 1178 ? 0.2425 0.2441 0.2568 0.0207  -0.0444 -0.0702 1176 VAL A CG1 
8705  C CG2 . VAL A 1178 ? 0.2857 0.2926 0.3053 0.0218  -0.0503 -0.0783 1176 VAL A CG2 
8706  N N   . ASN A 1179 ? 0.2961 0.2984 0.3091 0.0271  -0.0470 -0.0815 1177 ASN A N   
8707  C CA  . ASN A 1179 ? 0.2878 0.2882 0.2980 0.0279  -0.0446 -0.0798 1177 ASN A CA  
8708  C C   . ASN A 1179 ? 0.3278 0.3228 0.3453 0.0268  -0.0465 -0.0821 1177 ASN A C   
8709  O O   . ASN A 1179 ? 0.3273 0.3182 0.3454 0.0254  -0.0447 -0.0785 1177 ASN A O   
8710  C CB  . ASN A 1179 ? 0.3754 0.3817 0.3785 0.0321  -0.0438 -0.0826 1177 ASN A CB  
8711  C CG  . ASN A 1179 ? 0.4282 0.4341 0.4258 0.0328  -0.0402 -0.0785 1177 ASN A CG  
8712  O OD1 . ASN A 1179 ? 0.4352 0.4372 0.4329 0.0304  -0.0378 -0.0730 1177 ASN A OD1 
8713  N ND2 . ASN A 1179 ? 0.3797 0.3903 0.3727 0.0362  -0.0397 -0.0814 1177 ASN A ND2 
8714  N N   . LYS A 1180 ? 0.3175 0.3125 0.3410 0.0273  -0.0505 -0.0880 1178 LYS A N   
8715  C CA  . LYS A 1180 ? 0.3351 0.3248 0.3669 0.0261  -0.0528 -0.0903 1178 LYS A CA  
8716  C C   . LYS A 1180 ? 0.3229 0.3070 0.3608 0.0216  -0.0527 -0.0849 1178 LYS A C   
8717  O O   . LYS A 1180 ? 0.3283 0.3075 0.3698 0.0201  -0.0522 -0.0826 1178 LYS A O   
8718  C CB  . LYS A 1180 ? 0.3351 0.3263 0.3725 0.0277  -0.0574 -0.0980 1178 LYS A CB  
8719  C CG  . LYS A 1180 ? 0.3935 0.3903 0.4262 0.0323  -0.0580 -0.1042 1178 LYS A CG  
8720  C CD  . LYS A 1180 ? 0.3832 0.3821 0.4215 0.0337  -0.0627 -0.1121 1178 LYS A CD  
8721  C CE  . LYS A 1180 ? 0.6102 0.6131 0.6467 0.0381  -0.0641 -0.1191 1178 LYS A CE  
8722  N NZ  . LYS A 1180 ? 0.6171 0.6277 0.6428 0.0413  -0.0613 -0.1187 1178 LYS A NZ  
8723  N N   . ALA A 1181 ? 0.3028 0.2879 0.3421 0.0195  -0.0530 -0.0828 1179 ALA A N   
8724  C CA  . ALA A 1181 ? 0.3245 0.3055 0.3690 0.0152  -0.0525 -0.0773 1179 ALA A CA  
8725  C C   . ALA A 1181 ? 0.3195 0.2988 0.3592 0.0141  -0.0484 -0.0708 1179 ALA A C   
8726  O O   . ALA A 1181 ? 0.3266 0.3017 0.3708 0.0112  -0.0479 -0.0669 1179 ALA A O   
8727  C CB  . ALA A 1181 ? 0.2933 0.2769 0.3391 0.0136  -0.0534 -0.0763 1179 ALA A CB  
8728  N N   . ILE A 1182 ? 0.2767 0.2595 0.3075 0.0162  -0.0454 -0.0693 1180 ILE A N   
8729  C CA  . ILE A 1182 ? 0.2763 0.2576 0.3027 0.0152  -0.0416 -0.0634 1180 ILE A CA  
8730  C C   . ILE A 1182 ? 0.3380 0.3159 0.3652 0.0159  -0.0411 -0.0637 1180 ILE A C   
8731  O O   . ILE A 1182 ? 0.3147 0.2891 0.3433 0.0136  -0.0395 -0.0591 1180 ILE A O   
8732  C CB  . ILE A 1182 ? 0.2500 0.2358 0.2674 0.0174  -0.0388 -0.0619 1180 ILE A CB  
8733  C CG1 . ILE A 1182 ? 0.2913 0.2798 0.3086 0.0162  -0.0390 -0.0603 1180 ILE A CG1 
8734  C CG2 . ILE A 1182 ? 0.2917 0.2760 0.3046 0.0171  -0.0352 -0.0569 1180 ILE A CG2 
8735  C CD1 . ILE A 1182 ? 0.3075 0.3008 0.3168 0.0185  -0.0370 -0.0594 1180 ILE A CD1 
8736  N N   . ALA A 1183 ? 0.2765 0.2558 0.3030 0.0189  -0.0425 -0.0690 1181 ALA A N   
8737  C CA  . ALA A 1183 ? 0.3119 0.2882 0.3396 0.0197  -0.0423 -0.0697 1181 ALA A CA  
8738  C C   . ALA A 1183 ? 0.3598 0.3304 0.3967 0.0168  -0.0443 -0.0687 1181 ALA A C   
8739  O O   . ALA A 1183 ? 0.3404 0.3076 0.3785 0.0161  -0.0433 -0.0663 1181 ALA A O   
8740  C CB  . ALA A 1183 ? 0.2936 0.2731 0.3197 0.0237  -0.0439 -0.0763 1181 ALA A CB  
8741  N N   . ALA A 1184 ? 0.3153 0.2850 0.3588 0.0148  -0.0472 -0.0699 1182 ALA A N   
8742  C CA  . ALA A 1184 ? 0.3204 0.2849 0.3735 0.0118  -0.0495 -0.0686 1182 ALA A CA  
8743  C C   . ALA A 1184 ? 0.3471 0.3095 0.4010 0.0080  -0.0472 -0.0611 1182 ALA A C   
8744  O O   . ALA A 1184 ? 0.3437 0.3020 0.4050 0.0053  -0.0487 -0.0589 1182 ALA A O   
8745  C CB  . ALA A 1184 ? 0.3138 0.2782 0.3745 0.0109  -0.0537 -0.0727 1182 ALA A CB  
8746  N N   . LEU A 1185 ? 0.2881 0.2533 0.3349 0.0078  -0.0439 -0.0573 1183 LEU A N   
8747  C CA  . LEU A 1185 ? 0.3502 0.3141 0.3976 0.0045  -0.0418 -0.0506 1183 LEU A CA  
8748  C C   . LEU A 1185 ? 0.3579 0.3186 0.4050 0.0041  -0.0401 -0.0476 1183 LEU A C   
8749  O O   . LEU A 1185 ? 0.3468 0.3078 0.3887 0.0067  -0.0386 -0.0491 1183 LEU A O   
8750  C CB  . LEU A 1185 ? 0.2863 0.2542 0.3263 0.0047  -0.0387 -0.0478 1183 LEU A CB  
8751  C CG  . LEU A 1185 ? 0.3233 0.2949 0.3630 0.0052  -0.0401 -0.0503 1183 LEU A CG  
8752  C CD1 . LEU A 1185 ? 0.2988 0.2741 0.3309 0.0059  -0.0370 -0.0476 1183 LEU A CD1 
8753  C CD2 . LEU A 1185 ? 0.3185 0.2892 0.3665 0.0018  -0.0425 -0.0492 1183 LEU A CD2 
8754  N N   . PRO A 1186 ? 0.3491 0.3069 0.4018 0.0008  -0.0403 -0.0432 1184 PRO A N   
8755  C CA  . PRO A 1186 ? 0.3150 0.2699 0.3675 0.0003  -0.0388 -0.0401 1184 PRO A CA  
8756  C C   . PRO A 1186 ? 0.2923 0.2494 0.3362 0.0010  -0.0347 -0.0366 1184 PRO A C   
8757  O O   . PRO A 1186 ? 0.3360 0.2963 0.3756 0.0007  -0.0329 -0.0350 1184 PRO A O   
8758  C CB  . PRO A 1186 ? 0.4410 0.3934 0.5013 -0.0037 -0.0399 -0.0355 1184 PRO A CB  
8759  C CG  . PRO A 1186 ? 0.5133 0.4666 0.5797 -0.0050 -0.0430 -0.0377 1184 PRO A CG  
8760  C CD  . PRO A 1186 ? 0.4026 0.3601 0.4623 -0.0027 -0.0420 -0.0407 1184 PRO A CD  
8761  N N   . GLY A 1187 ? 0.2832 0.2384 0.3248 0.0020  -0.0332 -0.0356 1185 GLY A N   
8762  C CA  . GLY A 1187 ? 0.3277 0.2844 0.3625 0.0022  -0.0295 -0.0320 1185 GLY A CA  
8763  C C   . GLY A 1187 ? 0.2949 0.2541 0.3221 0.0057  -0.0279 -0.0347 1185 GLY A C   
8764  O O   . GLY A 1187 ? 0.3406 0.2994 0.3675 0.0083  -0.0290 -0.0388 1185 GLY A O   
8765  N N   . PRO A 1188 ? 0.2856 0.2476 0.3068 0.0060  -0.0253 -0.0324 1186 PRO A N   
8766  C CA  . PRO A 1188 ? 0.3056 0.2699 0.3197 0.0089  -0.0233 -0.0336 1186 PRO A CA  
8767  C C   . PRO A 1188 ? 0.2919 0.2590 0.3043 0.0116  -0.0249 -0.0386 1186 PRO A C   
8768  O O   . PRO A 1188 ? 0.2972 0.2654 0.3122 0.0111  -0.0268 -0.0405 1186 PRO A O   
8769  C CB  . PRO A 1188 ? 0.3323 0.2986 0.3419 0.0080  -0.0206 -0.0296 1186 PRO A CB  
8770  C CG  . PRO A 1188 ? 0.3416 0.3083 0.3551 0.0055  -0.0217 -0.0283 1186 PRO A CG  
8771  C CD  . PRO A 1188 ? 0.2961 0.2596 0.3171 0.0036  -0.0242 -0.0286 1186 PRO A CD  
8772  N N   . LEU A 1189 ? 0.2740 0.2427 0.2820 0.0145  -0.0240 -0.0407 1187 LEU A N   
8773  C CA  . LEU A 1189 ? 0.2610 0.2337 0.2656 0.0174  -0.0248 -0.0448 1187 LEU A CA  
8774  C C   . LEU A 1189 ? 0.3198 0.2957 0.3198 0.0173  -0.0231 -0.0423 1187 LEU A C   
8775  O O   . LEU A 1189 ? 0.4136 0.3895 0.4099 0.0168  -0.0205 -0.0383 1187 LEU A O   
8776  C CB  . LEU A 1189 ? 0.3012 0.2756 0.3020 0.0204  -0.0238 -0.0469 1187 LEU A CB  
8777  C CG  . LEU A 1189 ? 0.3386 0.3114 0.3438 0.0217  -0.0261 -0.0514 1187 LEU A CG  
8778  C CD1 . LEU A 1189 ? 0.3341 0.3017 0.3441 0.0195  -0.0261 -0.0488 1187 LEU A CD1 
8779  C CD2 . LEU A 1189 ? 0.4222 0.3988 0.4227 0.0253  -0.0252 -0.0542 1187 LEU A CD2 
8780  N N   . LEU A 1190 ? 0.2775 0.2560 0.2780 0.0177  -0.0248 -0.0448 1188 LEU A N   
8781  C CA  . LEU A 1190 ? 0.2514 0.2328 0.2481 0.0177  -0.0236 -0.0426 1188 LEU A CA  
8782  C C   . LEU A 1190 ? 0.2846 0.2706 0.2753 0.0210  -0.0230 -0.0443 1188 LEU A C   
8783  O O   . LEU A 1190 ? 0.2965 0.2847 0.2872 0.0232  -0.0247 -0.0488 1188 LEU A O   
8784  C CB  . LEU A 1190 ? 0.2767 0.2587 0.2774 0.0162  -0.0258 -0.0438 1188 LEU A CB  
8785  C CG  . LEU A 1190 ? 0.3195 0.2980 0.3266 0.0127  -0.0266 -0.0417 1188 LEU A CG  
8786  C CD1 . LEU A 1190 ? 0.3331 0.3134 0.3426 0.0113  -0.0279 -0.0418 1188 LEU A CD1 
8787  C CD2 . LEU A 1190 ? 0.3579 0.3344 0.3635 0.0110  -0.0238 -0.0365 1188 LEU A CD2 
8788  N N   . LEU A 1191 ? 0.2704 0.2581 0.2563 0.0214  -0.0205 -0.0407 1189 LEU A N   
8789  C CA  . LEU A 1191 ? 0.2752 0.2677 0.2555 0.0242  -0.0199 -0.0414 1189 LEU A CA  
8790  C C   . LEU A 1191 ? 0.2675 0.2629 0.2483 0.0243  -0.0216 -0.0429 1189 LEU A C   
8791  O O   . LEU A 1191 ? 0.2885 0.2835 0.2699 0.0227  -0.0211 -0.0401 1189 LEU A O   
8792  C CB  . LEU A 1191 ? 0.2613 0.2543 0.2374 0.0243  -0.0169 -0.0366 1189 LEU A CB  
8793  C CG  . LEU A 1191 ? 0.2465 0.2442 0.2170 0.0272  -0.0159 -0.0363 1189 LEU A CG  
8794  C CD1 . LEU A 1191 ? 0.2741 0.2709 0.2418 0.0269  -0.0130 -0.0315 1189 LEU A CD1 
8795  C CD2 . LEU A 1191 ? 0.2637 0.2657 0.2322 0.0284  -0.0169 -0.0370 1189 LEU A CD2 
8796  N N   . VAL A 1192 ? 0.2671 0.2657 0.2479 0.0263  -0.0238 -0.0476 1190 VAL A N   
8797  C CA  . VAL A 1192 ? 0.2598 0.2613 0.2416 0.0266  -0.0260 -0.0500 1190 VAL A CA  
8798  C C   . VAL A 1192 ? 0.2328 0.2402 0.2087 0.0294  -0.0254 -0.0498 1190 VAL A C   
8799  O O   . VAL A 1192 ? 0.2958 0.3064 0.2680 0.0319  -0.0249 -0.0512 1190 VAL A O   
8800  C CB  . VAL A 1192 ? 0.3055 0.3069 0.2919 0.0271  -0.0292 -0.0558 1190 VAL A CB  
8801  C CG1 . VAL A 1192 ? 0.3207 0.3252 0.3083 0.0273  -0.0316 -0.0584 1190 VAL A CG1 
8802  C CG2 . VAL A 1192 ? 0.3189 0.3144 0.3117 0.0243  -0.0300 -0.0555 1190 VAL A CG2 
8803  N N   . GLN A 1193 ? 0.2646 0.2738 0.2397 0.0290  -0.0255 -0.0481 1191 GLN A N   
8804  C CA  . GLN A 1193 ? 0.2239 0.2390 0.1942 0.0314  -0.0256 -0.0480 1191 GLN A CA  
8805  C C   . GLN A 1193 ? 0.2517 0.2693 0.2243 0.0316  -0.0284 -0.0516 1191 GLN A C   
8806  O O   . GLN A 1193 ? 0.2506 0.2658 0.2273 0.0293  -0.0292 -0.0510 1191 GLN A O   
8807  C CB  . GLN A 1193 ? 0.2362 0.2514 0.2036 0.0311  -0.0233 -0.0425 1191 GLN A CB  
8808  C CG  . GLN A 1193 ? 0.2800 0.2926 0.2454 0.0307  -0.0205 -0.0388 1191 GLN A CG  
8809  C CD  . GLN A 1193 ? 0.2755 0.2894 0.2379 0.0310  -0.0187 -0.0339 1191 GLN A CD  
8810  O OE1 . GLN A 1193 ? 0.2994 0.3181 0.2578 0.0333  -0.0186 -0.0331 1191 GLN A OE1 
8811  N NE2 . GLN A 1193 ? 0.2885 0.2984 0.2528 0.0288  -0.0173 -0.0306 1191 GLN A NE2 
8812  N N   . ALA A 1194 ? 0.2499 0.2731 0.2199 0.0344  -0.0299 -0.0552 1192 ALA A N   
8813  C CA  . ALA A 1194 ? 0.2434 0.2696 0.2153 0.0349  -0.0329 -0.0591 1192 ALA A CA  
8814  C C   . ALA A 1194 ? 0.2684 0.3013 0.2351 0.0374  -0.0328 -0.0582 1192 ALA A C   
8815  O O   . ALA A 1194 ? 0.2871 0.3234 0.2486 0.0394  -0.0311 -0.0561 1192 ALA A O   
8816  C CB  . ALA A 1194 ? 0.2522 0.2792 0.2270 0.0360  -0.0355 -0.0656 1192 ALA A CB  
8817  N N   . ALA A 1195 ? 0.2506 0.2856 0.2189 0.0372  -0.0348 -0.0595 1193 ALA A N   
8818  C CA  . ALA A 1195 ? 0.2827 0.3243 0.2467 0.0395  -0.0353 -0.0590 1193 ALA A CA  
8819  C C   . ALA A 1195 ? 0.2406 0.2846 0.2079 0.0395  -0.0386 -0.0634 1193 ALA A C   
8820  O O   . ALA A 1195 ? 0.2864 0.3262 0.2594 0.0369  -0.0398 -0.0646 1193 ALA A O   
8821  C CB  . ALA A 1195 ? 0.2584 0.2994 0.2202 0.0388  -0.0331 -0.0526 1193 ALA A CB  
8822  N N   . SER A 1196 ? 0.2686 0.3197 0.2323 0.0423  -0.0401 -0.0656 1194 SER A N   
8823  C CA  . SER A 1196 ? 0.2958 0.3499 0.2620 0.0425  -0.0431 -0.0692 1194 SER A CA  
8824  C C   . SER A 1196 ? 0.2895 0.3435 0.2559 0.0413  -0.0425 -0.0647 1194 SER A C   
8825  O O   . SER A 1196 ? 0.2805 0.3335 0.2440 0.0411  -0.0399 -0.0591 1194 SER A O   
8826  C CB  . SER A 1196 ? 0.2984 0.3608 0.2605 0.0461  -0.0450 -0.0731 1194 SER A CB  
8827  O OG  . SER A 1196 ? 0.3014 0.3687 0.2574 0.0479  -0.0432 -0.0684 1194 SER A OG  
8828  N N   . SER A 1197 ? 0.2590 0.3142 0.2292 0.0406  -0.0450 -0.0673 1195 SER A N   
8829  C CA  . SER A 1197 ? 0.2617 0.3178 0.2322 0.0398  -0.0448 -0.0637 1195 SER A CA  
8830  C C   . SER A 1197 ? 0.2906 0.3525 0.2547 0.0427  -0.0440 -0.0606 1195 SER A C   
8831  O O   . SER A 1197 ? 0.2694 0.3304 0.2324 0.0422  -0.0422 -0.0554 1195 SER A O   
8832  C CB  . SER A 1197 ? 0.3141 0.3717 0.2895 0.0390  -0.0480 -0.0676 1195 SER A CB  
8833  O OG  . SER A 1197 ? 0.3123 0.3643 0.2942 0.0360  -0.0487 -0.0696 1195 SER A OG  
8834  N N   . GLY A 1198 ? 0.3421 0.4105 0.3024 0.0456  -0.0453 -0.0638 1196 GLY A N   
8835  C CA  . GLY A 1198 ? 0.2892 0.3639 0.2434 0.0483  -0.0447 -0.0605 1196 GLY A CA  
8836  C C   . GLY A 1198 ? 0.3236 0.3964 0.2742 0.0485  -0.0413 -0.0549 1196 GLY A C   
8837  O O   . GLY A 1198 ? 0.2974 0.3722 0.2453 0.0492  -0.0401 -0.0497 1196 GLY A O   
8838  N N   . GLU A 1199 ? 0.2912 0.3602 0.2422 0.0478  -0.0399 -0.0558 1197 GLU A N   
8839  C CA  . GLU A 1199 ? 0.2958 0.3625 0.2439 0.0476  -0.0367 -0.0507 1197 GLU A CA  
8840  C C   . GLU A 1199 ? 0.3049 0.3657 0.2556 0.0452  -0.0350 -0.0455 1197 GLU A C   
8841  O O   . GLU A 1199 ? 0.2983 0.3594 0.2463 0.0457  -0.0330 -0.0401 1197 GLU A O   
8842  C CB  . GLU A 1199 ? 0.3214 0.3848 0.2703 0.0472  -0.0359 -0.0533 1197 GLU A CB  
8843  C CG  . GLU A 1199 ? 0.3911 0.4530 0.3368 0.0474  -0.0328 -0.0487 1197 GLU A CG  
8844  C CD  . GLU A 1199 ? 0.5256 0.5847 0.4724 0.0471  -0.0322 -0.0519 1197 GLU A CD  
8845  O OE1 . GLU A 1199 ? 0.4513 0.5098 0.4012 0.0470  -0.0345 -0.0577 1197 GLU A OE1 
8846  O OE2 . GLU A 1199 ? 0.5840 0.6414 0.5289 0.0470  -0.0297 -0.0485 1197 GLU A OE2 
8847  N N   . ILE A 1200 ? 0.2791 0.3349 0.2351 0.0426  -0.0357 -0.0471 1198 ILE A N   
8848  C CA  . ILE A 1200 ? 0.2477 0.2988 0.2063 0.0405  -0.0342 -0.0428 1198 ILE A CA  
8849  C C   . ILE A 1200 ? 0.3194 0.3745 0.2763 0.0418  -0.0346 -0.0396 1198 ILE A C   
8850  O O   . ILE A 1200 ? 0.3078 0.3610 0.2642 0.0415  -0.0329 -0.0346 1198 ILE A O   
8851  C CB  . ILE A 1200 ? 0.2556 0.3020 0.2202 0.0376  -0.0352 -0.0453 1198 ILE A CB  
8852  C CG1 . ILE A 1200 ? 0.2730 0.3146 0.2395 0.0361  -0.0344 -0.0470 1198 ILE A CG1 
8853  C CG2 . ILE A 1200 ? 0.2557 0.2991 0.2229 0.0358  -0.0340 -0.0414 1198 ILE A CG2 
8854  C CD1 . ILE A 1200 ? 0.2766 0.3143 0.2494 0.0333  -0.0356 -0.0496 1198 ILE A CD1 
8855  N N   . ALA A 1201 ? 0.2889 0.3497 0.2451 0.0434  -0.0371 -0.0424 1199 ALA A N   
8856  C CA  . ALA A 1201 ? 0.3137 0.3785 0.2686 0.0448  -0.0378 -0.0394 1199 ALA A CA  
8857  C C   . ALA A 1201 ? 0.3244 0.3932 0.2739 0.0471  -0.0365 -0.0351 1199 ALA A C   
8858  O O   . ALA A 1201 ? 0.3088 0.3781 0.2579 0.0475  -0.0359 -0.0303 1199 ALA A O   
8859  C CB  . ALA A 1201 ? 0.3295 0.3996 0.2851 0.0459  -0.0410 -0.0437 1199 ALA A CB  
8860  N N   . ARG A 1202 ? 0.2809 0.3527 0.2268 0.0486  -0.0361 -0.0365 1200 ARG A N   
8861  C CA  . ARG A 1202 ? 0.3185 0.3954 0.2592 0.0509  -0.0351 -0.0324 1200 ARG A CA  
8862  C C   . ARG A 1202 ? 0.3429 0.4153 0.2830 0.0500  -0.0321 -0.0274 1200 ARG A C   
8863  O O   . ARG A 1202 ? 0.3500 0.4246 0.2878 0.0510  -0.0310 -0.0220 1200 ARG A O   
8864  C CB  . ARG A 1202 ? 0.2827 0.3665 0.2195 0.0533  -0.0361 -0.0363 1200 ARG A CB  
8865  C CG  . ARG A 1202 ? 0.2960 0.3865 0.2322 0.0551  -0.0392 -0.0406 1200 ARG A CG  
8866  C CD  . ARG A 1202 ? 0.3467 0.4449 0.2783 0.0578  -0.0400 -0.0442 1200 ARG A CD  
8867  N NE  . ARG A 1202 ? 0.3800 0.4745 0.3129 0.0571  -0.0395 -0.0485 1200 ARG A NE  
8868  C CZ  . ARG A 1202 ? 0.3893 0.4830 0.3253 0.0567  -0.0417 -0.0554 1200 ARG A CZ  
8869  N NH1 . ARG A 1202 ? 0.3494 0.4462 0.2870 0.0572  -0.0446 -0.0592 1200 ARG A NH1 
8870  N NH2 . ARG A 1202 ? 0.3733 0.4626 0.3111 0.0558  -0.0410 -0.0586 1200 ARG A NH2 
8871  N N   . ASN A 1203 ? 0.2956 0.3619 0.2380 0.0480  -0.0307 -0.0290 1201 ASN A N   
8872  C CA  . ASN A 1203 ? 0.3257 0.3884 0.2670 0.0473  -0.0280 -0.0250 1201 ASN A CA  
8873  C C   . ASN A 1203 ? 0.3807 0.4354 0.3264 0.0445  -0.0267 -0.0232 1201 ASN A C   
8874  O O   . ASN A 1203 ? 0.3193 0.3695 0.2681 0.0426  -0.0268 -0.0266 1201 ASN A O   
8875  C CB  . ASN A 1203 ? 0.3320 0.3953 0.2716 0.0478  -0.0274 -0.0283 1201 ASN A CB  
8876  C CG  . ASN A 1203 ? 0.3670 0.4270 0.3056 0.0471  -0.0246 -0.0243 1201 ASN A CG  
8877  O OD1 . ASN A 1203 ? 0.3678 0.4256 0.3068 0.0465  -0.0232 -0.0189 1201 ASN A OD1 
8878  N ND2 . ASN A 1203 ? 0.3705 0.4303 0.3080 0.0474  -0.0239 -0.0270 1201 ASN A ND2 
8879  N N   . PRO A 1204 ? 0.3460 0.3989 0.2922 0.0442  -0.0255 -0.0178 1202 PRO A N   
8880  C CA  . PRO A 1204 ? 0.3847 0.4306 0.3349 0.0418  -0.0242 -0.0163 1202 PRO A CA  
8881  C C   . PRO A 1204 ? 0.3557 0.3968 0.3064 0.0403  -0.0224 -0.0170 1202 PRO A C   
8882  O O   . PRO A 1204 ? 0.3638 0.3995 0.3179 0.0381  -0.0217 -0.0173 1202 PRO A O   
8883  C CB  . PRO A 1204 ? 0.4218 0.4677 0.3719 0.0424  -0.0234 -0.0105 1202 PRO A CB  
8884  C CG  . PRO A 1204 ? 0.4984 0.5515 0.4453 0.0449  -0.0248 -0.0092 1202 PRO A CG  
8885  C CD  . PRO A 1204 ? 0.3751 0.4326 0.3185 0.0462  -0.0253 -0.0129 1202 PRO A CD  
8886  N N   . ASP A 1205 ? 0.3523 0.3957 0.2996 0.0414  -0.0216 -0.0171 1203 ASP A N   
8887  C CA  . ASP A 1205 ? 0.3632 0.4025 0.3109 0.0402  -0.0199 -0.0179 1203 ASP A CA  
8888  C C   . ASP A 1205 ? 0.3686 0.4086 0.3165 0.0403  -0.0211 -0.0236 1203 ASP A C   
8889  O O   . ASP A 1205 ? 0.3811 0.4200 0.3281 0.0403  -0.0201 -0.0246 1203 ASP A O   
8890  C CB  . ASP A 1205 ? 0.4056 0.4468 0.3500 0.0414  -0.0180 -0.0139 1203 ASP A CB  
8891  C CG  . ASP A 1205 ? 0.4772 0.5167 0.4223 0.0411  -0.0169 -0.0081 1203 ASP A CG  
8892  O OD1 . ASP A 1205 ? 0.4380 0.4733 0.3867 0.0395  -0.0170 -0.0074 1203 ASP A OD1 
8893  O OD2 . ASP A 1205 ? 0.4915 0.5343 0.4340 0.0424  -0.0160 -0.0043 1203 ASP A OD2 
8894  N N   . ALA A 1206 ? 0.2894 0.3313 0.2388 0.0404  -0.0234 -0.0275 1204 ALA A N   
8895  C CA  . ALA A 1206 ? 0.3120 0.3543 0.2625 0.0405  -0.0250 -0.0332 1204 ALA A CA  
8896  C C   . ALA A 1206 ? 0.3251 0.3609 0.2786 0.0382  -0.0239 -0.0341 1204 ALA A C   
8897  O O   . ALA A 1206 ? 0.3563 0.3921 0.3095 0.0387  -0.0240 -0.0372 1204 ALA A O   
8898  C CB  . ALA A 1206 ? 0.3034 0.3471 0.2566 0.0402  -0.0276 -0.0367 1204 ALA A CB  
8899  N N   . TYR A 1207 ? 0.3050 0.3356 0.2615 0.0359  -0.0228 -0.0315 1205 TYR A N   
8900  C CA  . TYR A 1207 ? 0.2571 0.2820 0.2161 0.0337  -0.0214 -0.0311 1205 TYR A CA  
8901  C C   . TYR A 1207 ? 0.3004 0.3235 0.2574 0.0337  -0.0188 -0.0261 1205 TYR A C   
8902  O O   . TYR A 1207 ? 0.4014 0.4244 0.3585 0.0335  -0.0182 -0.0227 1205 TYR A O   
8903  C CB  . TYR A 1207 ? 0.2656 0.2865 0.2296 0.0311  -0.0220 -0.0319 1205 TYR A CB  
8904  C CG  . TYR A 1207 ? 0.2759 0.2982 0.2426 0.0308  -0.0247 -0.0366 1205 TYR A CG  
8905  C CD1 . TYR A 1207 ? 0.3035 0.3254 0.2712 0.0311  -0.0259 -0.0407 1205 TYR A CD1 
8906  C CD2 . TYR A 1207 ? 0.2414 0.2655 0.2102 0.0304  -0.0262 -0.0371 1205 TYR A CD2 
8907  C CE1 . TYR A 1207 ? 0.2767 0.2998 0.2478 0.0308  -0.0286 -0.0452 1205 TYR A CE1 
8908  C CE2 . TYR A 1207 ? 0.2621 0.2875 0.2339 0.0301  -0.0288 -0.0415 1205 TYR A CE2 
8909  C CZ  . TYR A 1207 ? 0.2719 0.2967 0.2449 0.0302  -0.0300 -0.0455 1205 TYR A CZ  
8910  O OH  . TYR A 1207 ? 0.2696 0.2956 0.2463 0.0299  -0.0328 -0.0500 1205 TYR A OH  
8911  N N   . CYS A 1208 ? 0.2815 0.3034 0.2372 0.0339  -0.0174 -0.0258 1206 CYS A N   
8912  C CA  . CYS A 1208 ? 0.2982 0.3188 0.2522 0.0339  -0.0151 -0.0211 1206 CYS A CA  
8913  C C   . CYS A 1208 ? 0.2985 0.3129 0.2557 0.0313  -0.0138 -0.0195 1206 CYS A C   
8914  O O   . CYS A 1208 ? 0.2713 0.2825 0.2309 0.0298  -0.0139 -0.0217 1206 CYS A O   
8915  C CB  . CYS A 1208 ? 0.3123 0.3351 0.2632 0.0354  -0.0142 -0.0215 1206 CYS A CB  
8916  S SG  . CYS A 1208 ? 0.3307 0.3519 0.2801 0.0352  -0.0113 -0.0159 1206 CYS A SG  
8917  N N   . LEU A 1209 ? 0.2346 0.2478 0.1923 0.0308  -0.0128 -0.0156 1207 LEU A N   
8918  C CA  . LEU A 1209 ? 0.2335 0.2416 0.1942 0.0285  -0.0116 -0.0142 1207 LEU A CA  
8919  C C   . LEU A 1209 ? 0.2519 0.2570 0.2121 0.0278  -0.0098 -0.0129 1207 LEU A C   
8920  O O   . LEU A 1209 ? 0.2455 0.2467 0.2083 0.0259  -0.0090 -0.0125 1207 LEU A O   
8921  C CB  . LEU A 1209 ? 0.2333 0.2412 0.1950 0.0284  -0.0113 -0.0110 1207 LEU A CB  
8922  C CG  . LEU A 1209 ? 0.2649 0.2757 0.2275 0.0290  -0.0131 -0.0122 1207 LEU A CG  
8923  C CD1 . LEU A 1209 ? 0.2817 0.2915 0.2461 0.0288  -0.0127 -0.0092 1207 LEU A CD1 
8924  C CD2 . LEU A 1209 ? 0.2785 0.2886 0.2437 0.0276  -0.0144 -0.0159 1207 LEU A CD2 
8925  N N   . ASN A 1210 ? 0.2660 0.2734 0.2232 0.0294  -0.0091 -0.0122 1208 ASN A N   
8926  C CA  . ASN A 1210 ? 0.2861 0.2910 0.2430 0.0289  -0.0075 -0.0112 1208 ASN A CA  
8927  C C   . ASN A 1210 ? 0.2378 0.2394 0.1971 0.0273  -0.0079 -0.0144 1208 ASN A C   
8928  O O   . ASN A 1210 ? 0.2790 0.2771 0.2397 0.0260  -0.0067 -0.0133 1208 ASN A O   
8929  C CB  . ASN A 1210 ? 0.2819 0.2908 0.2352 0.0310  -0.0070 -0.0108 1208 ASN A CB  
8930  C CG  . ASN A 1210 ? 0.3280 0.3404 0.2791 0.0325  -0.0064 -0.0068 1208 ASN A CG  
8931  O OD1 . ASN A 1210 ? 0.3981 0.4099 0.3503 0.0321  -0.0067 -0.0047 1208 ASN A OD1 
8932  N ND2 . ASN A 1210 ? 0.4300 0.4463 0.3780 0.0342  -0.0056 -0.0058 1208 ASN A ND2 
8933  N N   . TRP A 1211 ? 0.2517 0.2547 0.2119 0.0276  -0.0098 -0.0182 1209 TRP A N   
8934  C CA  . TRP A 1211 ? 0.2475 0.2478 0.2104 0.0264  -0.0105 -0.0212 1209 TRP A CA  
8935  C C   . TRP A 1211 ? 0.2567 0.2539 0.2236 0.0239  -0.0112 -0.0216 1209 TRP A C   
8936  O O   . TRP A 1211 ? 0.3003 0.2952 0.2702 0.0226  -0.0120 -0.0238 1209 TRP A O   
8937  C CB  . TRP A 1211 ? 0.2723 0.2758 0.2345 0.0281  -0.0123 -0.0256 1209 TRP A CB  
8938  C CG  . TRP A 1211 ? 0.2637 0.2722 0.2215 0.0308  -0.0118 -0.0252 1209 TRP A CG  
8939  C CD1 . TRP A 1211 ? 0.2729 0.2867 0.2283 0.0329  -0.0132 -0.0270 1209 TRP A CD1 
8940  C CD2 . TRP A 1211 ? 0.2640 0.2732 0.2190 0.0317  -0.0098 -0.0225 1209 TRP A CD2 
8941  N NE1 . TRP A 1211 ? 0.2990 0.3172 0.2503 0.0351  -0.0121 -0.0254 1209 TRP A NE1 
8942  C CE2 . TRP A 1211 ? 0.2550 0.2704 0.2062 0.0343  -0.0100 -0.0226 1209 TRP A CE2 
8943  C CE3 . TRP A 1211 ? 0.2635 0.2691 0.2192 0.0305  -0.0079 -0.0199 1209 TRP A CE3 
8944  C CZ2 . TRP A 1211 ? 0.3012 0.3193 0.2493 0.0357  -0.0082 -0.0199 1209 TRP A CZ2 
8945  C CZ3 . TRP A 1211 ? 0.2974 0.3054 0.2502 0.0319  -0.0063 -0.0176 1209 TRP A CZ3 
8946  C CH2 . TRP A 1211 ? 0.2926 0.3068 0.2417 0.0344  -0.0064 -0.0175 1209 TRP A CH2 
8947  N N   . LEU A 1212 ? 0.2294 0.2267 0.1968 0.0233  -0.0109 -0.0194 1210 LEU A N   
8948  C CA  . LEU A 1212 ? 0.2167 0.2121 0.1878 0.0210  -0.0113 -0.0194 1210 LEU A CA  
8949  C C   . LEU A 1212 ? 0.2190 0.2116 0.1910 0.0195  -0.0094 -0.0163 1210 LEU A C   
8950  O O   . LEU A 1212 ? 0.2314 0.2230 0.2062 0.0177  -0.0095 -0.0159 1210 LEU A O   
8951  C CB  . LEU A 1212 ? 0.2222 0.2206 0.1937 0.0216  -0.0125 -0.0199 1210 LEU A CB  
8952  C CG  . LEU A 1212 ? 0.2306 0.2313 0.2025 0.0223  -0.0148 -0.0237 1210 LEU A CG  
8953  C CD1 . LEU A 1212 ? 0.2433 0.2479 0.2143 0.0237  -0.0160 -0.0239 1210 LEU A CD1 
8954  C CD2 . LEU A 1212 ? 0.2485 0.2470 0.2251 0.0200  -0.0160 -0.0258 1210 LEU A CD2 
8955  N N   . VAL A 1213 ? 0.2382 0.2300 0.2080 0.0203  -0.0078 -0.0141 1211 VAL A N   
8956  C CA  . VAL A 1213 ? 0.2317 0.2207 0.2025 0.0189  -0.0062 -0.0116 1211 VAL A CA  
8957  C C   . VAL A 1213 ? 0.2321 0.2187 0.2028 0.0184  -0.0055 -0.0119 1211 VAL A C   
8958  O O   . VAL A 1213 ? 0.2522 0.2397 0.2215 0.0196  -0.0059 -0.0136 1211 VAL A O   
8959  C CB  . VAL A 1213 ? 0.2356 0.2250 0.2046 0.0200  -0.0050 -0.0086 1211 VAL A CB  
8960  C CG1 . VAL A 1213 ? 0.2703 0.2615 0.2402 0.0203  -0.0057 -0.0082 1211 VAL A CG1 
8961  C CG2 . VAL A 1213 ? 0.2390 0.2303 0.2048 0.0220  -0.0046 -0.0078 1211 VAL A CG2 
8962  N N   . GLU A 1214 ? 0.2321 0.2162 0.2044 0.0168  -0.0043 -0.0103 1212 GLU A N   
8963  C CA  . GLU A 1214 ? 0.2837 0.2654 0.2564 0.0161  -0.0036 -0.0101 1212 GLU A CA  
8964  C C   . GLU A 1214 ? 0.2291 0.2099 0.2003 0.0164  -0.0018 -0.0074 1212 GLU A C   
8965  O O   . GLU A 1214 ? 0.2388 0.2192 0.2107 0.0158  -0.0011 -0.0056 1212 GLU A O   
8966  C CB  . GLU A 1214 ? 0.3010 0.2807 0.2771 0.0137  -0.0039 -0.0104 1212 GLU A CB  
8967  C CG  . GLU A 1214 ? 0.4500 0.4272 0.4269 0.0128  -0.0032 -0.0099 1212 GLU A CG  
8968  C CD  . GLU A 1214 ? 0.4260 0.4018 0.4064 0.0104  -0.0036 -0.0095 1212 GLU A CD  
8969  O OE1 . GLU A 1214 ? 0.5407 0.5171 0.5234 0.0095  -0.0050 -0.0109 1212 GLU A OE1 
8970  O OE2 . GLU A 1214 ? 0.6598 0.6341 0.6407 0.0093  -0.0024 -0.0077 1212 GLU A OE2 
8971  N N   . GLU A 1215 ? 0.2342 0.2147 0.2036 0.0175  -0.0011 -0.0071 1213 GLU A N   
8972  C CA  . GLU A 1215 ? 0.2172 0.1969 0.1857 0.0177  0.0005  -0.0045 1213 GLU A CA  
8973  C C   . GLU A 1215 ? 0.2290 0.2057 0.1994 0.0158  0.0012  -0.0039 1213 GLU A C   
8974  O O   . GLU A 1215 ? 0.2423 0.2178 0.2139 0.0151  0.0007  -0.0054 1213 GLU A O   
8975  C CB  . GLU A 1215 ? 0.2232 0.2045 0.1891 0.0195  0.0010  -0.0043 1213 GLU A CB  
8976  C CG  . GLU A 1215 ? 0.2337 0.2188 0.1973 0.0215  0.0004  -0.0046 1213 GLU A CG  
8977  C CD  . GLU A 1215 ? 0.2543 0.2419 0.2155 0.0232  0.0007  -0.0052 1213 GLU A CD  
8978  O OE1 . GLU A 1215 ? 0.2615 0.2497 0.2228 0.0237  -0.0002 -0.0083 1213 GLU A OE1 
8979  O OE2 . GLU A 1215 ? 0.2634 0.2524 0.2230 0.0241  0.0020  -0.0025 1213 GLU A OE2 
8980  N N   . VAL A 1216 ? 0.2206 0.1963 0.1915 0.0152  0.0023  -0.0017 1214 VAL A N   
8981  C CA  . VAL A 1216 ? 0.2198 0.1933 0.1922 0.0137  0.0031  -0.0009 1214 VAL A CA  
8982  C C   . VAL A 1216 ? 0.2291 0.2020 0.2006 0.0142  0.0044  0.0013  1214 VAL A C   
8983  O O   . VAL A 1216 ? 0.2214 0.1950 0.1928 0.0148  0.0047  0.0028  1214 VAL A O   
8984  C CB  . VAL A 1216 ? 0.2339 0.2071 0.2085 0.0119  0.0029  -0.0008 1214 VAL A CB  
8985  C CG1 . VAL A 1216 ? 0.2468 0.2184 0.2227 0.0105  0.0038  0.0003  1214 VAL A CG1 
8986  C CG2 . VAL A 1216 ? 0.2321 0.2060 0.2081 0.0111  0.0016  -0.0027 1214 VAL A CG2 
8987  N N   . SER A 1217 ? 0.2373 0.2090 0.2089 0.0140  0.0051  0.0017  1215 SER A N   
8988  C CA  . SER A 1217 ? 0.2170 0.1880 0.1883 0.0142  0.0063  0.0038  1215 SER A CA  
8989  C C   . SER A 1217 ? 0.2186 0.1877 0.1918 0.0125  0.0067  0.0043  1215 SER A C   
8990  O O   . SER A 1217 ? 0.2339 0.2022 0.2082 0.0114  0.0063  0.0032  1215 SER A O   
8991  C CB  . SER A 1217 ? 0.2559 0.2275 0.2258 0.0153  0.0068  0.0037  1215 SER A CB  
8992  O OG  . SER A 1217 ? 0.2869 0.2576 0.2571 0.0151  0.0080  0.0056  1215 SER A OG  
8993  N N   . ALA A 1218 ? 0.2024 0.1711 0.1764 0.0122  0.0074  0.0059  1216 ALA A N   
8994  C CA  . ALA A 1218 ? 0.2123 0.1798 0.1879 0.0108  0.0078  0.0063  1216 ALA A CA  
8995  C C   . ALA A 1218 ? 0.2329 0.1996 0.2087 0.0111  0.0088  0.0081  1216 ALA A C   
8996  O O   . ALA A 1218 ? 0.2541 0.2213 0.2301 0.0120  0.0090  0.0093  1216 ALA A O   
8997  C CB  . ALA A 1218 ? 0.2316 0.1997 0.2087 0.0099  0.0074  0.0058  1216 ALA A CB  
8998  N N   . SER A 1219 ? 0.2267 0.1925 0.2031 0.0104  0.0093  0.0084  1217 SER A N   
8999  C CA  . SER A 1219 ? 0.2317 0.1968 0.2085 0.0106  0.0101  0.0100  1217 SER A CA  
9000  C C   . SER A 1219 ? 0.2134 0.1778 0.1921 0.0092  0.0102  0.0100  1217 SER A C   
9001  O O   . SER A 1219 ? 0.2229 0.1870 0.2018 0.0082  0.0101  0.0095  1217 SER A O   
9002  C CB  . SER A 1219 ? 0.2602 0.2254 0.2361 0.0112  0.0107  0.0103  1217 SER A CB  
9003  O OG  . SER A 1219 ? 0.2385 0.2033 0.2152 0.0113  0.0116  0.0120  1217 SER A OG  
9004  N N   . ILE A 1220 ? 0.2109 0.1752 0.1910 0.0091  0.0103  0.0107  1218 ILE A N   
9005  C CA  . ILE A 1220 ? 0.2205 0.1848 0.2024 0.0080  0.0102  0.0103  1218 ILE A CA  
9006  C C   . ILE A 1220 ? 0.2161 0.1794 0.1991 0.0080  0.0108  0.0116  1218 ILE A C   
9007  O O   . ILE A 1220 ? 0.2237 0.1867 0.2077 0.0087  0.0109  0.0129  1218 ILE A O   
9008  C CB  . ILE A 1220 ? 0.2630 0.2281 0.2462 0.0080  0.0096  0.0093  1218 ILE A CB  
9009  C CG1 . ILE A 1220 ? 0.3082 0.2745 0.2903 0.0080  0.0091  0.0081  1218 ILE A CG1 
9010  C CG2 . ILE A 1220 ? 0.3032 0.2690 0.2880 0.0070  0.0095  0.0085  1218 ILE A CG2 
9011  C CD1 . ILE A 1220 ? 0.4751 0.4418 0.4576 0.0091  0.0085  0.0079  1218 ILE A CD1 
9012  N N   . ASN A 1221 ? 0.2315 0.1946 0.2148 0.0071  0.0111  0.0116  1219 ASN A N   
9013  C CA  . ASN A 1221 ? 0.2202 0.1827 0.2050 0.0069  0.0115  0.0127  1219 ASN A CA  
9014  C C   . ASN A 1221 ? 0.2361 0.1990 0.2232 0.0065  0.0110  0.0120  1219 ASN A C   
9015  O O   . ASN A 1221 ? 0.2783 0.2423 0.2658 0.0057  0.0107  0.0107  1219 ASN A O   
9016  C CB  . ASN A 1221 ? 0.2456 0.2080 0.2301 0.0062  0.0118  0.0129  1219 ASN A CB  
9017  C CG  . ASN A 1221 ? 0.2383 0.2003 0.2244 0.0059  0.0122  0.0138  1219 ASN A CG  
9018  O OD1 . ASN A 1221 ? 0.2458 0.2075 0.2335 0.0063  0.0123  0.0146  1219 ASN A OD1 
9019  N ND2 . ASN A 1221 ? 0.2617 0.2238 0.2479 0.0052  0.0123  0.0139  1219 ASN A ND2 
9020  N N   . THR A 1222 ? 0.2199 0.1822 0.2089 0.0071  0.0108  0.0127  1220 THR A N   
9021  C CA  . THR A 1222 ? 0.2453 0.2078 0.2371 0.0070  0.0101  0.0116  1220 THR A CA  
9022  C C   . THR A 1222 ? 0.2759 0.2379 0.2700 0.0065  0.0101  0.0120  1220 THR A C   
9023  O O   . THR A 1222 ? 0.3529 0.3151 0.3498 0.0064  0.0093  0.0107  1220 THR A O   
9024  C CB  . THR A 1222 ? 0.2807 0.2425 0.2741 0.0079  0.0095  0.0121  1220 THR A CB  
9025  O OG1 . THR A 1222 ? 0.2857 0.2464 0.2797 0.0084  0.0100  0.0147  1220 THR A OG1 
9026  C CG2 . THR A 1222 ? 0.2755 0.2381 0.2667 0.0085  0.0093  0.0114  1220 THR A CG2 
9027  N N   . ALA A 1223 ? 0.2342 0.1958 0.2274 0.0062  0.0109  0.0134  1221 ALA A N   
9028  C CA  . ALA A 1223 ? 0.3127 0.2742 0.3078 0.0055  0.0109  0.0136  1221 ALA A CA  
9029  C C   . ALA A 1223 ? 0.3880 0.3508 0.3820 0.0047  0.0108  0.0124  1221 ALA A C   
9030  O O   . ALA A 1223 ? 0.4266 0.3897 0.4219 0.0041  0.0108  0.0125  1221 ALA A O   
9031  C CB  . ALA A 1223 ? 0.3072 0.2679 0.3024 0.0058  0.0118  0.0161  1221 ALA A CB  
9032  N N   . ALA A 1224 ? 0.3950 0.3589 0.3868 0.0045  0.0108  0.0114  1222 ALA A N   
9033  C CA  . ALA A 1224 ? 0.4331 0.3984 0.4237 0.0036  0.0108  0.0111  1222 ALA A CA  
9034  C C   . ALA A 1224 ? 0.4621 0.4295 0.4543 0.0029  0.0102  0.0098  1222 ALA A C   
9035  O O   . ALA A 1224 ? 0.4949 0.4633 0.4869 0.0022  0.0103  0.0102  1222 ALA A O   
9036  C CB  . ALA A 1224 ? 0.4237 0.3900 0.4123 0.0033  0.0107  0.0105  1222 ALA A CB  
9037  N N   . ALA A 1225 ? 0.4163 0.3844 0.4103 0.0033  0.0095  0.0081  1223 ALA A N   
9038  C CA  . ALA A 1225 ? 0.4665 0.4372 0.4621 0.0029  0.0089  0.0062  1223 ALA A CA  
9039  C C   . ALA A 1225 ? 0.5314 0.5011 0.5291 0.0027  0.0087  0.0068  1223 ALA A C   
9040  O O   . ALA A 1225 ? 0.5388 0.5109 0.5376 0.0023  0.0081  0.0053  1223 ALA A O   
9041  C CB  . ALA A 1225 ? 0.4406 0.4124 0.4381 0.0036  0.0080  0.0038  1223 ALA A CB  
9042  N N   . GLY A 1226 ? 0.4707 0.4376 0.4689 0.0030  0.0093  0.0088  1224 GLY A N   
9043  C CA  . GLY A 1226 ? 0.4475 0.4137 0.4480 0.0027  0.0093  0.0097  1224 GLY A CA  
9044  C C   . GLY A 1226 ? 0.4717 0.4357 0.4753 0.0032  0.0090  0.0105  1224 GLY A C   
9045  O O   . GLY A 1226 ? 0.4687 0.4321 0.4747 0.0029  0.0090  0.0115  1224 GLY A O   
9046  N N   . GLY A 1227 ? 0.3567 0.3198 0.3609 0.0039  0.0088  0.0104  1225 GLY A N   
9047  C CA  . GLY A 1227 ? 0.4223 0.3834 0.4299 0.0043  0.0085  0.0117  1225 GLY A CA  
9048  C C   . GLY A 1227 ? 0.4311 0.3913 0.4380 0.0051  0.0084  0.0122  1225 GLY A C   
9049  O O   . GLY A 1227 ? 0.4100 0.3711 0.4141 0.0053  0.0085  0.0110  1225 GLY A O   
9050  N N   . ASN A 1228 ? 0.3496 0.3082 0.3595 0.0054  0.0082  0.0142  1226 ASN A N   
9051  C CA  . ASN A 1228 ? 0.4256 0.3834 0.4353 0.0062  0.0081  0.0154  1226 ASN A CA  
9052  C C   . ASN A 1228 ? 0.4699 0.4266 0.4844 0.0066  0.0065  0.0141  1226 ASN A C   
9053  O O   . ASN A 1228 ? 0.4460 0.4014 0.4651 0.0063  0.0057  0.0153  1226 ASN A O   
9054  C CB  . ASN A 1228 ? 0.4535 0.4108 0.4628 0.0064  0.0091  0.0192  1226 ASN A CB  
9055  C CG  . ASN A 1228 ? 0.4822 0.4393 0.4906 0.0073  0.0092  0.0208  1226 ASN A CG  
9056  O OD1 . ASN A 1228 ? 0.4860 0.4424 0.4965 0.0077  0.0080  0.0199  1226 ASN A OD1 
9057  N ND2 . ASN A 1228 ? 0.4464 0.4044 0.4516 0.0076  0.0104  0.0230  1226 ASN A ND2 
9058  N N   . ALA A 1229 ? 0.4141 0.3715 0.4280 0.0072  0.0058  0.0117  1227 ALA A N   
9059  C CA  . ALA A 1229 ? 0.3901 0.3467 0.4088 0.0077  0.0040  0.0098  1227 ALA A CA  
9060  C C   . ALA A 1229 ? 0.4296 0.3841 0.4517 0.0082  0.0034  0.0129  1227 ALA A C   
9061  O O   . ALA A 1229 ? 0.4757 0.4286 0.5035 0.0082  0.0020  0.0129  1227 ALA A O   
9062  C CB  . ALA A 1229 ? 0.4232 0.3816 0.4402 0.0084  0.0035  0.0066  1227 ALA A CB  
9063  N N   . SER A 1230 ? 0.4418 0.3964 0.4607 0.0085  0.0045  0.0156  1228 SER A N   
9064  C CA  . SER A 1230 ? 0.5024 0.4556 0.5242 0.0090  0.0040  0.0192  1228 SER A CA  
9065  C C   . SER A 1230 ? 0.5665 0.5187 0.5921 0.0082  0.0041  0.0222  1228 SER A C   
9066  O O   . SER A 1230 ? 0.5648 0.5154 0.5958 0.0082  0.0028  0.0241  1228 SER A O   
9067  C CB  . SER A 1230 ? 0.5666 0.5209 0.5835 0.0095  0.0053  0.0214  1228 SER A CB  
9068  O OG  . SER A 1230 ? 0.6904 0.6455 0.7051 0.0103  0.0049  0.0190  1228 SER A OG  
9069  N N   . LEU A 1231 ? 0.4553 0.4084 0.4784 0.0075  0.0054  0.0229  1229 LEU A N   
9070  C CA  . LEU A 1231 ? 0.4960 0.4486 0.5225 0.0067  0.0056  0.0259  1229 LEU A CA  
9071  C C   . LEU A 1231 ? 0.5638 0.5151 0.5961 0.0060  0.0041  0.0239  1229 LEU A C   
9072  O O   . LEU A 1231 ? 0.6341 0.5847 0.6705 0.0053  0.0039  0.0265  1229 LEU A O   
9073  C CB  . LEU A 1231 ? 0.5136 0.4679 0.5356 0.0063  0.0076  0.0273  1229 LEU A CB  
9074  C CG  . LEU A 1231 ? 0.4914 0.4473 0.5111 0.0067  0.0090  0.0314  1229 LEU A CG  
9075  C CD1 . LEU A 1231 ? 0.5958 0.5520 0.6129 0.0078  0.0088  0.0316  1229 LEU A CD1 
9076  C CD2 . LEU A 1231 ? 0.4211 0.3789 0.4362 0.0066  0.0108  0.0316  1229 LEU A CD2 
9077  N N   . MET A 1232 ? 0.5518 0.5030 0.5845 0.0063  0.0030  0.0194  1230 MET A N   
9078  C CA  . MET A 1232 ? 0.5566 0.5067 0.5953 0.0060  0.0011  0.0170  1230 MET A CA  
9079  C C   . MET A 1232 ? 0.5369 0.4847 0.5826 0.0062  -0.0007 0.0186  1230 MET A C   
9080  O O   . MET A 1232 ? 0.5327 0.4791 0.5847 0.0057  -0.0023 0.0178  1230 MET A O   
9081  C CB  . MET A 1232 ? 0.4934 0.4450 0.5309 0.0065  0.0003  0.0116  1230 MET A CB  
9082  C CG  . MET A 1232 ? 0.5074 0.4613 0.5396 0.0059  0.0016  0.0100  1230 MET A CG  
9083  S SD  . MET A 1232 ? 0.6894 0.6461 0.7199 0.0065  0.0008  0.0043  1230 MET A SD  
9084  C CE  . MET A 1232 ? 0.6190 0.5752 0.6571 0.0067  -0.0017 0.0009  1230 MET A CE  
9085  N N   . ALA A 1233 ? 0.5874 0.5347 0.6325 0.0069  -0.0007 0.0208  1231 ALA A N   
9086  C CA  . ALA A 1233 ? 0.6636 0.6087 0.7154 0.0072  -0.0025 0.0230  1231 ALA A CA  
9087  C C   . ALA A 1233 ? 0.6939 0.6388 0.7473 0.0065  -0.0017 0.0292  1231 ALA A C   
9088  O O   . ALA A 1233 ? 0.7634 0.7067 0.8221 0.0066  -0.0030 0.0322  1231 ALA A O   
9089  C CB  . ALA A 1233 ? 0.5868 0.5318 0.6374 0.0085  -0.0031 0.0221  1231 ALA A CB  
9090  N N   . ILE A 1234 ? 0.6831 0.6298 0.7323 0.0058  0.0004  0.0313  1232 ILE A N   
9091  C CA  . ILE A 1234 ? 0.6695 0.6171 0.7194 0.0051  0.0015  0.0371  1232 ILE A CA  
9092  C C   . ILE A 1234 ? 0.6550 0.6024 0.7090 0.0038  0.0014  0.0380  1232 ILE A C   
9093  O O   . ILE A 1234 ? 0.5333 0.4819 0.5838 0.0035  0.0026  0.0361  1232 ILE A O   
9094  C CB  . ILE A 1234 ? 0.5671 0.5177 0.6090 0.0056  0.0040  0.0388  1232 ILE A CB  
9095  C CG1 . ILE A 1234 ? 0.6238 0.5747 0.6623 0.0069  0.0039  0.0381  1232 ILE A CG1 
9096  C CG2 . ILE A 1234 ? 0.4859 0.4385 0.5284 0.0051  0.0053  0.0446  1232 ILE A CG2 
9097  C CD1 . ILE A 1234 ? 0.5309 0.4846 0.5635 0.0075  0.0058  0.0411  1232 ILE A CD1 
9098  N N   . GLY A 1235 ? 0.5885 0.5343 0.6503 0.0031  -0.0001 0.0409  1233 GLY A N   
9099  C CA  . GLY A 1235 ? 0.5074 0.4530 0.5742 0.0018  -0.0004 0.0424  1233 GLY A CA  
9100  C C   . GLY A 1235 ? 0.5274 0.4731 0.5998 0.0010  -0.0006 0.0489  1233 GLY A C   
9101  O O   . GLY A 1235 ? 0.3710 0.3183 0.4446 -0.0001 0.0004  0.0523  1233 GLY A O   
9102  O OXT . GLY A 1235 ? 0.5117 0.4562 0.5876 0.0013  -0.0019 0.0511  1233 GLY A OXT 
9103  N N   . ALA B 16   ? 0.6955 0.5514 0.6328 0.0974  -0.0648 -0.0487 14   ALA B N   
9104  C CA  . ALA B 16   ? 0.7266 0.5889 0.6681 0.0891  -0.0622 -0.0458 14   ALA B CA  
9105  C C   . ALA B 16   ? 0.6992 0.5492 0.6321 0.0825  -0.0638 -0.0441 14   ALA B C   
9106  O O   . ALA B 16   ? 0.7289 0.5690 0.6544 0.0834  -0.0652 -0.0458 14   ALA B O   
9107  C CB  . ALA B 16   ? 0.5944 0.4711 0.5443 0.0885  -0.0572 -0.0468 14   ALA B CB  
9108  N N   . PRO B 17   ? 0.6508 0.5016 0.5846 0.0757  -0.0636 -0.0407 15   PRO B N   
9109  C CA  . PRO B 17   ? 0.5732 0.4143 0.4997 0.0686  -0.0647 -0.0388 15   PRO B CA  
9110  C C   . PRO B 17   ? 0.5721 0.4178 0.5002 0.0657  -0.0615 -0.0398 15   PRO B C   
9111  O O   . PRO B 17   ? 0.6114 0.4705 0.5480 0.0657  -0.0575 -0.0402 15   PRO B O   
9112  C CB  . PRO B 17   ? 0.6425 0.4876 0.5720 0.0628  -0.0642 -0.0352 15   PRO B CB  
9113  C CG  . PRO B 17   ? 0.7201 0.5723 0.6554 0.0676  -0.0645 -0.0354 15   PRO B CG  
9114  C CD  . PRO B 17   ? 0.6626 0.5229 0.6035 0.0742  -0.0626 -0.0386 15   PRO B CD  
9115  N N   . ALA B 18   ? 0.5202 0.3544 0.4398 0.0632  -0.0634 -0.0401 16   ALA B N   
9116  C CA  . ALA B 18   ? 0.4861 0.3233 0.4060 0.0603  -0.0608 -0.0411 16   ALA B CA  
9117  C C   . ALA B 18   ? 0.4727 0.3199 0.3986 0.0532  -0.0577 -0.0383 16   ALA B C   
9118  O O   . ALA B 18   ? 0.4551 0.3008 0.3804 0.0486  -0.0586 -0.0353 16   ALA B O   
9119  C CB  . ALA B 18   ? 0.5078 0.3299 0.4169 0.0579  -0.0640 -0.0415 16   ALA B CB  
9120  N N   . PRO B 19   ? 0.4262 0.2839 0.3579 0.0524  -0.0539 -0.0391 17   PRO B N   
9121  C CA  . PRO B 19   ? 0.4217 0.2888 0.3591 0.0463  -0.0509 -0.0366 17   PRO B CA  
9122  C C   . PRO B 19   ? 0.4215 0.2808 0.3528 0.0390  -0.0526 -0.0341 17   PRO B C   
9123  O O   . PRO B 19   ? 0.4267 0.2769 0.3509 0.0374  -0.0544 -0.0348 17   PRO B O   
9124  C CB  . PRO B 19   ? 0.4133 0.2896 0.3554 0.0473  -0.0473 -0.0384 17   PRO B CB  
9125  C CG  . PRO B 19   ? 0.4597 0.3368 0.4027 0.0551  -0.0474 -0.0415 17   PRO B CG  
9126  C CD  . PRO B 19   ? 0.4652 0.3279 0.3994 0.0579  -0.0519 -0.0424 17   PRO B CD  
9127  N N   . PHE B 20   ? 0.4209 0.2841 0.3549 0.0346  -0.0521 -0.0311 18   PHE B N   
9128  C CA  . PHE B 20   ? 0.3878 0.2471 0.3180 0.0272  -0.0529 -0.0282 18   PHE B CA  
9129  C C   . PHE B 20   ? 0.4467 0.2906 0.3667 0.0257  -0.0574 -0.0275 18   PHE B C   
9130  O O   . PHE B 20   ? 0.4505 0.2899 0.3662 0.0193  -0.0584 -0.0254 18   PHE B O   
9131  C CB  . PHE B 20   ? 0.3955 0.2596 0.3270 0.0231  -0.0506 -0.0283 18   PHE B CB  
9132  C CG  . PHE B 20   ? 0.3701 0.2486 0.3110 0.0241  -0.0463 -0.0286 18   PHE B CG  
9133  C CD1 . PHE B 20   ? 0.3421 0.2292 0.2886 0.0211  -0.0442 -0.0263 18   PHE B CD1 
9134  C CD2 . PHE B 20   ? 0.3414 0.2244 0.2851 0.0281  -0.0444 -0.0313 18   PHE B CD2 
9135  C CE1 . PHE B 20   ? 0.3664 0.2659 0.3211 0.0219  -0.0405 -0.0266 18   PHE B CE1 
9136  C CE2 . PHE B 20   ? 0.3541 0.2499 0.3060 0.0287  -0.0406 -0.0314 18   PHE B CE2 
9137  C CZ  . PHE B 20   ? 0.3684 0.2721 0.3258 0.0256  -0.0387 -0.0291 18   PHE B CZ  
9138  N N   . ALA B 21   ? 0.4865 0.3223 0.4026 0.0314  -0.0601 -0.0292 19   ALA B N   
9139  C CA  . ALA B 21   ? 0.5198 0.3398 0.4257 0.0303  -0.0647 -0.0285 19   ALA B CA  
9140  C C   . ALA B 21   ? 0.5149 0.3320 0.4185 0.0249  -0.0661 -0.0247 19   ALA B C   
9141  O O   . ALA B 21   ? 0.5554 0.3606 0.4505 0.0209  -0.0693 -0.0231 19   ALA B O   
9142  C CB  . ALA B 21   ? 0.5596 0.3727 0.4626 0.0384  -0.0673 -0.0310 19   ALA B CB  
9143  N N   . ASP B 22   ? 0.4439 0.2715 0.3545 0.0245  -0.0638 -0.0231 20   ASP B N   
9144  C CA  . ASP B 22   ? 0.4398 0.2659 0.3486 0.0197  -0.0648 -0.0196 20   ASP B CA  
9145  C C   . ASP B 22   ? 0.3910 0.2305 0.3072 0.0153  -0.0608 -0.0178 20   ASP B C   
9146  O O   . ASP B 22   ? 0.4378 0.2827 0.3574 0.0146  -0.0600 -0.0161 20   ASP B O   
9147  C CB  . ASP B 22   ? 0.5286 0.3519 0.4370 0.0244  -0.0669 -0.0194 20   ASP B CB  
9148  N N   . PHE B 23   ? 0.3538 0.1987 0.2725 0.0124  -0.0584 -0.0183 21   PHE B N   
9149  C CA  . PHE B 23   ? 0.3604 0.2189 0.2869 0.0095  -0.0544 -0.0172 21   PHE B CA  
9150  C C   . PHE B 23   ? 0.3472 0.2064 0.2722 0.0034  -0.0544 -0.0136 21   PHE B C   
9151  O O   . PHE B 23   ? 0.3448 0.2119 0.2747 0.0034  -0.0527 -0.0125 21   PHE B O   
9152  C CB  . PHE B 23   ? 0.3514 0.2145 0.2799 0.0076  -0.0522 -0.0184 21   PHE B CB  
9153  C CG  . PHE B 23   ? 0.3627 0.2386 0.2983 0.0044  -0.0485 -0.0171 21   PHE B CG  
9154  C CD1 . PHE B 23   ? 0.3197 0.2059 0.2632 0.0077  -0.0458 -0.0177 21   PHE B CD1 
9155  C CD2 . PHE B 23   ? 0.3406 0.2180 0.2748 -0.0020 -0.0478 -0.0151 21   PHE B CD2 
9156  C CE1 . PHE B 23   ? 0.3010 0.1983 0.2506 0.0049  -0.0425 -0.0165 21   PHE B CE1 
9157  C CE2 . PHE B 23   ? 0.3733 0.2626 0.3140 -0.0045 -0.0444 -0.0139 21   PHE B CE2 
9158  C CZ  . PHE B 23   ? 0.3350 0.2337 0.2831 -0.0009 -0.0418 -0.0147 21   PHE B CZ  
9159  N N   . ALA B 24   ? 0.3490 0.2005 0.2672 -0.0021 -0.0564 -0.0118 22   ALA B N   
9160  C CA  . ALA B 24   ? 0.3437 0.1964 0.2602 -0.0084 -0.0563 -0.0082 22   ALA B CA  
9161  C C   . ALA B 24   ? 0.3594 0.1991 0.2661 -0.0131 -0.0599 -0.0063 22   ALA B C   
9162  O O   . ALA B 24   ? 0.3887 0.2296 0.2939 -0.0195 -0.0594 -0.0044 22   ALA B O   
9163  C CB  . ALA B 24   ? 0.3703 0.2352 0.2928 -0.0124 -0.0525 -0.0073 22   ALA B CB  
9164  N N   . PRO B 25   ? 0.4086 0.2360 0.3087 -0.0104 -0.0636 -0.0067 23   PRO B N   
9165  C CA  . PRO B 25   ? 0.4396 0.2536 0.3298 -0.0151 -0.0674 -0.0047 23   PRO B CA  
9166  C C   . PRO B 25   ? 0.3999 0.2159 0.2884 -0.0220 -0.0671 -0.0006 23   PRO B C   
9167  O O   . PRO B 25   ? 0.3929 0.2148 0.2847 -0.0210 -0.0658 0.0007  23   PRO B O   
9168  C CB  . PRO B 25   ? 0.4665 0.2682 0.3510 -0.0095 -0.0712 -0.0059 23   PRO B CB  
9169  C CG  . PRO B 25   ? 0.4245 0.2350 0.3160 -0.0041 -0.0693 -0.0068 23   PRO B CG  
9170  C CD  . PRO B 25   ? 0.3987 0.2242 0.3000 -0.0033 -0.0647 -0.0083 23   PRO B CD  
9171  N N   . PRO B 26   ? 0.3916 0.2035 0.2751 -0.0291 -0.0681 0.0017  24   PRO B N   
9172  C CA  . PRO B 26   ? 0.4283 0.2428 0.3102 -0.0359 -0.0676 0.0058  24   PRO B CA  
9173  C C   . PRO B 26   ? 0.4249 0.2287 0.2996 -0.0357 -0.0710 0.0079  24   PRO B C   
9174  O O   . PRO B 26   ? 0.4417 0.2326 0.3103 -0.0320 -0.0746 0.0066  24   PRO B O   
9175  C CB  . PRO B 26   ? 0.4386 0.2500 0.3163 -0.0432 -0.0686 0.0073  24   PRO B CB  
9176  C CG  . PRO B 26   ? 0.4525 0.2525 0.3255 -0.0402 -0.0715 0.0044  24   PRO B CG  
9177  C CD  . PRO B 26   ? 0.4539 0.2592 0.3333 -0.0315 -0.0698 0.0005  24   PRO B CD  
9178  N N   . VAL B 27   ? 0.4311 0.2403 0.3063 -0.0396 -0.0697 0.0111  25   VAL B N   
9179  C CA  . VAL B 27   ? 0.4288 0.2281 0.2967 -0.0404 -0.0727 0.0137  25   VAL B CA  
9180  C C   . VAL B 27   ? 0.4551 0.2381 0.3122 -0.0444 -0.0772 0.0152  25   VAL B C   
9181  O O   . VAL B 27   ? 0.4708 0.2407 0.3208 -0.0417 -0.0811 0.0154  25   VAL B O   
9182  C CB  . VAL B 27   ? 0.4235 0.2319 0.2931 -0.0451 -0.0703 0.0172  25   VAL B CB  
9183  C CG1 . VAL B 27   ? 0.4627 0.2602 0.3236 -0.0468 -0.0736 0.0203  25   VAL B CG1 
9184  C CG2 . VAL B 27   ? 0.4246 0.2469 0.3037 -0.0403 -0.0665 0.0154  25   VAL B CG2 
9185  N N   . ARG B 28   ? 0.4392 0.2225 0.2949 -0.0508 -0.0770 0.0162  26   ARG B N   
9186  C CA  . ARG B 28   ? 0.4677 0.2354 0.3131 -0.0555 -0.0813 0.0177  26   ARG B CA  
9187  C C   . ARG B 28   ? 0.5124 0.2819 0.3591 -0.0586 -0.0808 0.0162  26   ARG B C   
9188  O O   . ARG B 28   ? 0.4452 0.2291 0.3004 -0.0590 -0.0768 0.0153  26   ARG B O   
9189  C CB  . ARG B 28   ? 0.5241 0.2887 0.3634 -0.0635 -0.0825 0.0228  26   ARG B CB  
9190  C CG  . ARG B 28   ? 0.4942 0.2729 0.3386 -0.0708 -0.0787 0.0253  26   ARG B CG  
9191  C CD  . ARG B 28   ? 0.5272 0.3044 0.3662 -0.0780 -0.0793 0.0304  26   ARG B CD  
9192  N NE  . ARG B 28   ? 0.5546 0.3366 0.3957 -0.0744 -0.0779 0.0312  26   ARG B NE  
9193  C CZ  . ARG B 28   ? 0.6811 0.4517 0.5152 -0.0723 -0.0811 0.0325  26   ARG B CZ  
9194  N NH1 . ARG B 28   ? 0.6445 0.3975 0.4686 -0.0734 -0.0860 0.0332  26   ARG B NH1 
9195  N NH2 . ARG B 28   ? 0.5880 0.3645 0.4247 -0.0689 -0.0795 0.0330  26   ARG B NH2 
9196  N N   . PRO B 29   ? 0.5129 0.2676 0.3511 -0.0605 -0.0849 0.0159  27   PRO B N   
9197  C CA  . PRO B 29   ? 0.5124 0.2684 0.3509 -0.0647 -0.0848 0.0150  27   PRO B CA  
9198  C C   . PRO B 29   ? 0.4971 0.2636 0.3382 -0.0738 -0.0825 0.0187  27   PRO B C   
9199  O O   . PRO B 29   ? 0.5247 0.2890 0.3616 -0.0794 -0.0833 0.0228  27   PRO B O   
9200  C CB  . PRO B 29   ? 0.5340 0.2697 0.3607 -0.0661 -0.0904 0.0147  27   PRO B CB  
9201  C CG  . PRO B 29   ? 0.5825 0.3079 0.4051 -0.0588 -0.0929 0.0136  27   PRO B CG  
9202  C CD  . PRO B 29   ? 0.5680 0.3037 0.3956 -0.0586 -0.0901 0.0161  27   PRO B CD  
9203  N N   . GLN B 30   ? 0.4814 0.2599 0.3296 -0.0751 -0.0795 0.0174  28   GLN B N   
9204  C CA  . GLN B 30   ? 0.5055 0.2972 0.3581 -0.0825 -0.0766 0.0205  28   GLN B CA  
9205  C C   . GLN B 30   ? 0.4860 0.2695 0.3312 -0.0917 -0.0798 0.0231  28   GLN B C   
9206  O O   . GLN B 30   ? 0.5060 0.2834 0.3485 -0.0924 -0.0818 0.0211  28   GLN B O   
9207  C CB  . GLN B 30   ? 0.4794 0.2873 0.3426 -0.0799 -0.0723 0.0180  28   GLN B CB  
9208  C CG  . GLN B 30   ? 0.4243 0.2402 0.2949 -0.0712 -0.0692 0.0154  28   GLN B CG  
9209  C CD  . GLN B 30   ? 0.4239 0.2477 0.2974 -0.0717 -0.0669 0.0180  28   GLN B CD  
9210  O OE1 . GLN B 30   ? 0.4297 0.2670 0.3088 -0.0752 -0.0635 0.0198  28   GLN B OE1 
9211  N NE2 . GLN B 30   ? 0.4352 0.2508 0.3047 -0.0681 -0.0687 0.0183  28   GLN B NE2 
9212  N N   . SER B 31   ? 0.4929 0.2764 0.3345 -0.0987 -0.0802 0.0277  29   SER B N   
9213  C CA  . SER B 31   ? 0.4564 0.2334 0.2913 -0.1084 -0.0831 0.0309  29   SER B CA  
9214  C C   . SER B 31   ? 0.4954 0.2864 0.3370 -0.1132 -0.0805 0.0309  29   SER B C   
9215  O O   . SER B 31   ? 0.4637 0.2701 0.3151 -0.1094 -0.0762 0.0291  29   SER B O   
9216  C CB  . SER B 31   ? 0.5005 0.2763 0.3308 -0.1148 -0.0835 0.0360  29   SER B CB  
9217  O OG  . SER B 31   ? 0.4887 0.2835 0.3275 -0.1168 -0.0786 0.0380  29   SER B OG  
9218  N N   . THR B 32   ? 0.5104 0.2957 0.3464 -0.1218 -0.0833 0.0332  30   THR B N   
9219  C CA  . THR B 32   ? 0.4702 0.2689 0.3120 -0.1275 -0.0813 0.0339  30   THR B CA  
9220  C C   . THR B 32   ? 0.4682 0.2865 0.3187 -0.1292 -0.0762 0.0364  30   THR B C   
9221  O O   . THR B 32   ? 0.4821 0.3159 0.3419 -0.1273 -0.0725 0.0349  30   THR B O   
9222  C CB  . THR B 32   ? 0.5413 0.3305 0.3750 -0.1376 -0.0854 0.0368  30   THR B CB  
9223  O OG1 . THR B 32   ? 0.6267 0.3982 0.4527 -0.1353 -0.0900 0.0338  30   THR B OG1 
9224  C CG2 . THR B 32   ? 0.6291 0.4336 0.4692 -0.1442 -0.0833 0.0380  30   THR B CG2 
9225  N N   . LEU B 33   ? 0.4696 0.2873 0.3171 -0.1323 -0.0760 0.0402  31   LEU B N   
9226  C CA  . LEU B 33   ? 0.4666 0.3025 0.3216 -0.1339 -0.0712 0.0426  31   LEU B CA  
9227  C C   . LEU B 33   ? 0.4513 0.2972 0.3147 -0.1243 -0.0672 0.0394  31   LEU B C   
9228  O O   . LEU B 33   ? 0.4493 0.3124 0.3214 -0.1238 -0.0630 0.0393  31   LEU B O   
9229  C CB  . LEU B 33   ? 0.4665 0.2982 0.3152 -0.1393 -0.0721 0.0473  31   LEU B CB  
9230  C CG  . LEU B 33   ? 0.5247 0.3506 0.3666 -0.1503 -0.0753 0.0513  31   LEU B CG  
9231  C CD1 . LEU B 33   ? 0.5383 0.3566 0.3723 -0.1552 -0.0768 0.0559  31   LEU B CD1 
9232  C CD2 . LEU B 33   ? 0.5515 0.3955 0.4008 -0.1563 -0.0722 0.0529  31   LEU B CD2 
9233  N N   . ARG B 34   ? 0.4236 0.2590 0.2844 -0.1166 -0.0687 0.0367  32   ARG B N   
9234  C CA  . ARG B 34   ? 0.4071 0.2516 0.2759 -0.1077 -0.0651 0.0334  32   ARG B CA  
9235  C C   . ARG B 34   ? 0.4272 0.2802 0.3034 -0.1045 -0.0632 0.0299  32   ARG B C   
9236  O O   . ARG B 34   ? 0.3782 0.2456 0.2631 -0.1009 -0.0591 0.0287  32   ARG B O   
9237  C CB  . ARG B 34   ? 0.4114 0.2430 0.2760 -0.1004 -0.0674 0.0313  32   ARG B CB  
9238  C CG  . ARG B 34   ? 0.4466 0.2720 0.3053 -0.1020 -0.0686 0.0346  32   ARG B CG  
9239  C CD  . ARG B 34   ? 0.4286 0.2688 0.2941 -0.1000 -0.0642 0.0356  32   ARG B CD  
9240  N NE  . ARG B 34   ? 0.4156 0.2614 0.2881 -0.0909 -0.0619 0.0316  32   ARG B NE  
9241  C CZ  . ARG B 34   ? 0.4491 0.2890 0.3203 -0.0846 -0.0627 0.0302  32   ARG B CZ  
9242  N NH1 . ARG B 34   ? 0.4315 0.2592 0.2943 -0.0857 -0.0659 0.0324  32   ARG B NH1 
9243  N NH2 . ARG B 34   ? 0.4022 0.2486 0.2805 -0.0770 -0.0605 0.0267  32   ARG B NH2 
9244  N N   . ARG B 35   ? 0.4013 0.2451 0.2735 -0.1057 -0.0663 0.0282  33   ARG B N   
9245  C CA  . ARG B 35   ? 0.4098 0.2615 0.2885 -0.1031 -0.0646 0.0250  33   ARG B CA  
9246  C C   . ARG B 35   ? 0.3620 0.2303 0.2472 -0.1085 -0.0615 0.0270  33   ARG B C   
9247  O O   . ARG B 35   ? 0.3808 0.2611 0.2740 -0.1048 -0.0584 0.0249  33   ARG B O   
9248  C CB  . ARG B 35   ? 0.4319 0.2699 0.3040 -0.1039 -0.0687 0.0230  33   ARG B CB  
9249  C CG  . ARG B 35   ? 0.5255 0.3491 0.3928 -0.0966 -0.0712 0.0199  33   ARG B CG  
9250  C CD  . ARG B 35   ? 0.5443 0.3555 0.4056 -0.0970 -0.0750 0.0174  33   ARG B CD  
9251  N NE  . ARG B 35   ? 0.7705 0.5667 0.6258 -0.0904 -0.0778 0.0148  33   ARG B NE  
9252  C CZ  . ARG B 35   ? 0.8260 0.6243 0.6857 -0.0813 -0.0761 0.0111  33   ARG B CZ  
9253  N NH1 . ARG B 35   ? 0.7941 0.6078 0.6636 -0.0778 -0.0717 0.0096  33   ARG B NH1 
9254  N NH2 . ARG B 35   ? 0.7635 0.5480 0.6173 -0.0756 -0.0789 0.0090  33   ARG B NH2 
9255  N N   . ALA B 36   ? 0.3845 0.2541 0.2665 -0.1171 -0.0624 0.0312  34   ALA B N   
9256  C CA  . ALA B 36   ? 0.4032 0.2896 0.2917 -0.1222 -0.0595 0.0331  34   ALA B CA  
9257  C C   . ALA B 36   ? 0.4096 0.3114 0.3063 -0.1180 -0.0545 0.0333  34   ALA B C   
9258  O O   . ALA B 36   ? 0.3784 0.2952 0.2830 -0.1175 -0.0514 0.0328  34   ALA B O   
9259  C CB  . ALA B 36   ? 0.4259 0.3106 0.3090 -0.1326 -0.0615 0.0378  34   ALA B CB  
9260  N N   . ILE B 37   ? 0.3638 0.2618 0.2585 -0.1148 -0.0540 0.0339  35   ILE B N   
9261  C CA  . ILE B 37   ? 0.3394 0.2502 0.2412 -0.1098 -0.0497 0.0335  35   ILE B CA  
9262  C C   . ILE B 37   ? 0.3717 0.2876 0.2805 -0.1018 -0.0477 0.0291  35   ILE B C   
9263  O O   . ILE B 37   ? 0.3332 0.2636 0.2497 -0.1001 -0.0441 0.0285  35   ILE B O   
9264  C CB  . ILE B 37   ? 0.3256 0.2291 0.2228 -0.1075 -0.0502 0.0346  35   ILE B CB  
9265  C CG1 . ILE B 37   ? 0.3209 0.2222 0.2120 -0.1158 -0.0514 0.0394  35   ILE B CG1 
9266  C CG2 . ILE B 37   ? 0.3308 0.2451 0.2351 -0.1007 -0.0462 0.0331  35   ILE B CG2 
9267  C CD1 . ILE B 37   ? 0.3321 0.2219 0.2165 -0.1141 -0.0533 0.0406  35   ILE B CD1 
9268  N N   . THR B 38   ? 0.3331 0.2369 0.2388 -0.0967 -0.0500 0.0261  36   THR B N   
9269  C CA  . THR B 38   ? 0.3344 0.2423 0.2463 -0.0889 -0.0481 0.0221  36   THR B CA  
9270  C C   . THR B 38   ? 0.3183 0.2354 0.2353 -0.0903 -0.0468 0.0210  36   THR B C   
9271  O O   . THR B 38   ? 0.3303 0.2582 0.2548 -0.0859 -0.0436 0.0191  36   THR B O   
9272  C CB  . THR B 38   ? 0.3615 0.2546 0.2686 -0.0838 -0.0511 0.0193  36   THR B CB  
9273  O OG1 . THR B 38   ? 0.3447 0.2289 0.2466 -0.0829 -0.0527 0.0206  36   THR B OG1 
9274  C CG2 . THR B 38   ? 0.3371 0.2352 0.2508 -0.0757 -0.0488 0.0154  36   THR B CG2 
9275  N N   . ALA B 39   ? 0.3329 0.2457 0.2458 -0.0967 -0.0495 0.0222  37   ALA B N   
9276  C CA  . ALA B 39   ? 0.3383 0.2592 0.2554 -0.0985 -0.0487 0.0212  37   ALA B CA  
9277  C C   . ALA B 39   ? 0.3671 0.3063 0.2921 -0.1000 -0.0448 0.0229  37   ALA B C   
9278  O O   . ALA B 39   ? 0.3437 0.2920 0.2744 -0.0986 -0.0432 0.0213  37   ALA B O   
9279  C CB  . ALA B 39   ? 0.3682 0.2807 0.2787 -0.1060 -0.0526 0.0227  37   ALA B CB  
9280  N N   . ALA B 40   ? 0.3207 0.2655 0.2461 -0.1026 -0.0432 0.0258  38   ALA B N   
9281  C CA  . ALA B 40   ? 0.3388 0.3009 0.2711 -0.1040 -0.0394 0.0275  38   ALA B CA  
9282  C C   . ALA B 40   ? 0.2858 0.2559 0.2243 -0.0964 -0.0357 0.0256  38   ALA B C   
9283  O O   . ALA B 40   ? 0.3176 0.3019 0.2620 -0.0964 -0.0325 0.0265  38   ALA B O   
9284  C CB  . ALA B 40   ? 0.3248 0.2898 0.2541 -0.1112 -0.0395 0.0318  38   ALA B CB  
9285  N N   . TYR B 41   ? 0.3140 0.2752 0.2512 -0.0901 -0.0362 0.0231  39   TYR B N   
9286  C CA  . TYR B 41   ? 0.2696 0.2363 0.2113 -0.0837 -0.0333 0.0218  39   TYR B CA  
9287  C C   . TYR B 41   ? 0.3283 0.3102 0.2782 -0.0812 -0.0296 0.0208  39   TYR B C   
9288  O O   . TYR B 41   ? 0.2779 0.2698 0.2314 -0.0804 -0.0268 0.0219  39   TYR B O   
9289  C CB  . TYR B 41   ? 0.2720 0.2279 0.2121 -0.0772 -0.0346 0.0186  39   TYR B CB  
9290  C CG  . TYR B 41   ? 0.2800 0.2360 0.2217 -0.0715 -0.0331 0.0176  39   TYR B CG  
9291  C CD1 . TYR B 41   ? 0.2884 0.2562 0.2352 -0.0699 -0.0296 0.0182  39   TYR B CD1 
9292  C CD2 . TYR B 41   ? 0.3156 0.2599 0.2537 -0.0674 -0.0352 0.0159  39   TYR B CD2 
9293  C CE1 . TYR B 41   ? 0.2686 0.2359 0.2165 -0.0647 -0.0285 0.0172  39   TYR B CE1 
9294  C CE2 . TYR B 41   ? 0.2963 0.2407 0.2360 -0.0623 -0.0340 0.0150  39   TYR B CE2 
9295  C CZ  . TYR B 41   ? 0.2869 0.2427 0.2314 -0.0611 -0.0307 0.0156  39   TYR B CZ  
9296  O OH  . TYR B 41   ? 0.2996 0.2553 0.2455 -0.0562 -0.0298 0.0146  39   TYR B OH  
9297  N N   . ARG B 42   ? 0.3051 0.2889 0.2578 -0.0800 -0.0299 0.0189  40   ARG B N   
9298  C CA  . ARG B 42   ? 0.2701 0.2673 0.2304 -0.0771 -0.0268 0.0178  40   ARG B CA  
9299  C C   . ARG B 42   ? 0.2896 0.2929 0.2514 -0.0819 -0.0274 0.0187  40   ARG B C   
9300  O O   . ARG B 42   ? 0.3005 0.3100 0.2669 -0.0793 -0.0263 0.0170  40   ARG B O   
9301  C CB  . ARG B 42   ? 0.2952 0.2902 0.2586 -0.0697 -0.0259 0.0143  40   ARG B CB  
9302  C CG  . ARG B 42   ? 0.2975 0.2900 0.2610 -0.0651 -0.0247 0.0137  40   ARG B CG  
9303  C CD  . ARG B 42   ? 0.2969 0.2854 0.2625 -0.0583 -0.0244 0.0105  40   ARG B CD  
9304  N NE  . ARG B 42   ? 0.2741 0.2560 0.2372 -0.0556 -0.0248 0.0103  40   ARG B NE  
9305  C CZ  . ARG B 42   ? 0.2910 0.2783 0.2568 -0.0528 -0.0226 0.0105  40   ARG B CZ  
9306  N NH1 . ARG B 42   ? 0.2973 0.2964 0.2683 -0.0520 -0.0197 0.0107  40   ARG B NH1 
9307  N NH2 . ARG B 42   ? 0.2726 0.2530 0.2357 -0.0506 -0.0235 0.0103  40   ARG B NH2 
9308  N N   . ARG B 43   ? 0.2947 0.2967 0.2526 -0.0892 -0.0292 0.0215  41   ARG B N   
9309  C CA  . ARG B 43   ? 0.3126 0.3201 0.2714 -0.0947 -0.0302 0.0227  41   ARG B CA  
9310  C C   . ARG B 43   ? 0.3177 0.3425 0.2843 -0.0935 -0.0268 0.0230  41   ARG B C   
9311  O O   . ARG B 43   ? 0.2965 0.3297 0.2661 -0.0919 -0.0240 0.0241  41   ARG B O   
9312  C CB  . ARG B 43   ? 0.2962 0.3001 0.2495 -0.1031 -0.0325 0.0261  41   ARG B CB  
9313  C CG  . ARG B 43   ? 0.2969 0.3075 0.2511 -0.1101 -0.0338 0.0279  41   ARG B CG  
9314  C CD  . ARG B 43   ? 0.3317 0.3336 0.2786 -0.1183 -0.0371 0.0308  41   ARG B CD  
9315  N NE  . ARG B 43   ? 0.3715 0.3550 0.3110 -0.1173 -0.0407 0.0291  41   ARG B NE  
9316  C CZ  . ARG B 43   ? 0.3648 0.3359 0.2966 -0.1213 -0.0434 0.0309  41   ARG B CZ  
9317  N NH1 . ARG B 43   ? 0.3728 0.3476 0.3029 -0.1269 -0.0429 0.0347  41   ARG B NH1 
9318  N NH2 . ARG B 43   ? 0.3680 0.3226 0.2934 -0.1195 -0.0467 0.0289  41   ARG B NH2 
9319  N N   . PRO B 44   ? 0.2999 0.3304 0.2699 -0.0937 -0.0270 0.0220  42   PRO B N   
9320  C CA  . PRO B 44   ? 0.2745 0.3215 0.2518 -0.0924 -0.0240 0.0224  42   PRO B CA  
9321  C C   . PRO B 44   ? 0.2708 0.3283 0.2493 -0.0977 -0.0227 0.0259  42   PRO B C   
9322  O O   . PRO B 44   ? 0.2739 0.3280 0.2480 -0.1048 -0.0248 0.0285  42   PRO B O   
9323  C CB  . PRO B 44   ? 0.3121 0.3611 0.2908 -0.0939 -0.0257 0.0214  42   PRO B CB  
9324  C CG  . PRO B 44   ? 0.3561 0.3894 0.3298 -0.0914 -0.0282 0.0188  42   PRO B CG  
9325  C CD  . PRO B 44   ? 0.3169 0.3387 0.2841 -0.0941 -0.0300 0.0201  42   PRO B CD  
9326  N N   . GLU B 45   ? 0.2867 0.3568 0.2708 -0.0941 -0.0192 0.0261  43   GLU B N   
9327  C CA  . GLU B 45   ? 0.2907 0.3722 0.2763 -0.0980 -0.0173 0.0292  43   GLU B CA  
9328  C C   . GLU B 45   ? 0.2716 0.3613 0.2584 -0.1054 -0.0185 0.0316  43   GLU B C   
9329  O O   . GLU B 45   ? 0.3145 0.4073 0.2992 -0.1119 -0.0188 0.0348  43   GLU B O   
9330  C CB  . GLU B 45   ? 0.3491 0.4426 0.3408 -0.0916 -0.0133 0.0282  43   GLU B CB  
9331  C CG  . GLU B 45   ? 0.3582 0.4584 0.3496 -0.0930 -0.0110 0.0305  43   GLU B CG  
9332  C CD  . GLU B 45   ? 0.2399 0.3439 0.2342 -0.0853 -0.0078 0.0287  43   GLU B CD  
9333  O OE1 . GLU B 45   ? 0.2529 0.3526 0.2489 -0.0790 -0.0076 0.0257  43   GLU B OE1 
9334  O OE2 . GLU B 45   ? 0.2765 0.3878 0.2710 -0.0859 -0.0056 0.0303  43   GLU B OE2 
9335  N N   . THR B 46   ? 0.2915 0.3845 0.2814 -0.1049 -0.0195 0.0302  44   THR B N   
9336  C CA  . THR B 46   ? 0.2619 0.3626 0.2529 -0.1120 -0.0211 0.0323  44   THR B CA  
9337  C C   . THR B 46   ? 0.3043 0.3929 0.2881 -0.1198 -0.0250 0.0340  44   THR B C   
9338  O O   . THR B 46   ? 0.3303 0.4251 0.3141 -0.1273 -0.0263 0.0367  44   THR B O   
9339  C CB  . THR B 46   ? 0.3197 0.4254 0.3150 -0.1093 -0.0216 0.0303  44   THR B CB  
9340  O OG1 . THR B 46   ? 0.3151 0.4066 0.3070 -0.1054 -0.0235 0.0272  44   THR B OG1 
9341  C CG2 . THR B 46   ? 0.3357 0.4558 0.3384 -0.1029 -0.0179 0.0294  44   THR B CG2 
9342  N N   . GLU B 47   ? 0.2923 0.3638 0.2699 -0.1181 -0.0272 0.0323  45   GLU B N   
9343  C CA  . GLU B 47   ? 0.2841 0.3430 0.2542 -0.1252 -0.0310 0.0339  45   GLU B CA  
9344  C C   . GLU B 47   ? 0.3118 0.3684 0.2780 -0.1288 -0.0305 0.0369  45   GLU B C   
9345  O O   . GLU B 47   ? 0.3477 0.4000 0.3091 -0.1369 -0.0330 0.0397  45   GLU B O   
9346  C CB  . GLU B 47   ? 0.3066 0.3478 0.2712 -0.1217 -0.0338 0.0308  45   GLU B CB  
9347  C CG  . GLU B 47   ? 0.3804 0.4222 0.3475 -0.1189 -0.0347 0.0280  45   GLU B CG  
9348  C CD  . GLU B 47   ? 0.4766 0.5023 0.4389 -0.1141 -0.0367 0.0247  45   GLU B CD  
9349  O OE1 . GLU B 47   ? 0.5297 0.5420 0.4854 -0.1154 -0.0387 0.0250  45   GLU B OE1 
9350  O OE2 . GLU B 47   ? 0.5494 0.5761 0.5145 -0.1090 -0.0362 0.0219  45   GLU B OE2 
9351  N N   . CYS B 48   ? 0.3019 0.3611 0.2699 -0.1233 -0.0274 0.0365  46   CYS B N   
9352  C CA  . CYS B 48   ? 0.3158 0.3723 0.2797 -0.1262 -0.0269 0.0392  46   CYS B CA  
9353  C C   . CYS B 48   ? 0.3241 0.3952 0.2905 -0.1328 -0.0252 0.0430  46   CYS B C   
9354  O O   . CYS B 48   ? 0.3336 0.4011 0.2950 -0.1394 -0.0264 0.0463  46   CYS B O   
9355  C CB  . CYS B 48   ? 0.2945 0.3507 0.2598 -0.1184 -0.0240 0.0375  46   CYS B CB  
9356  S SG  . CYS B 48   ? 0.3217 0.3607 0.2835 -0.1109 -0.0256 0.0335  46   CYS B SG  
9357  N N   . LEU B 49   ? 0.3183 0.4063 0.2924 -0.1310 -0.0225 0.0428  47   LEU B N   
9358  C CA  . LEU B 49   ? 0.3035 0.4074 0.2808 -0.1353 -0.0200 0.0462  47   LEU B CA  
9359  C C   . LEU B 49   ? 0.2978 0.4055 0.2737 -0.1457 -0.0223 0.0497  47   LEU B C   
9360  O O   . LEU B 49   ? 0.3087 0.4222 0.2832 -0.1513 -0.0213 0.0533  47   LEU B O   
9361  C CB  . LEU B 49   ? 0.3366 0.4578 0.3227 -0.1295 -0.0162 0.0448  47   LEU B CB  
9362  C CG  . LEU B 49   ? 0.3019 0.4275 0.2896 -0.1230 -0.0124 0.0441  47   LEU B CG  
9363  C CD1 . LEU B 49   ? 0.3103 0.4414 0.2955 -0.1284 -0.0110 0.0479  47   LEU B CD1 
9364  C CD2 . LEU B 49   ? 0.2704 0.3800 0.2541 -0.1168 -0.0132 0.0412  47   LEU B CD2 
9365  N N   . PRO B 50   ? 0.3437 0.4488 0.3197 -0.1490 -0.0253 0.0491  48   PRO B N   
9366  C CA  . PRO B 50   ? 0.3481 0.4590 0.3234 -0.1593 -0.0273 0.0526  48   PRO B CA  
9367  C C   . PRO B 50   ? 0.3632 0.4629 0.3302 -0.1670 -0.0297 0.0559  48   PRO B C   
9368  O O   . PRO B 50   ? 0.3954 0.5049 0.3629 -0.1745 -0.0290 0.0599  48   PRO B O   
9369  C CB  . PRO B 50   ? 0.3352 0.4409 0.3106 -0.1602 -0.0308 0.0505  48   PRO B CB  
9370  C CG  . PRO B 50   ? 0.3262 0.4351 0.3068 -0.1500 -0.0286 0.0465  48   PRO B CG  
9371  C CD  . PRO B 50   ? 0.3315 0.4325 0.3097 -0.1434 -0.0265 0.0452  48   PRO B CD  
9372  N N   . PRO B 51   ? 0.3434 0.4230 0.3027 -0.1657 -0.0324 0.0546  49   PRO B N   
9373  C CA  . PRO B 51   ? 0.3459 0.4150 0.2969 -0.1730 -0.0345 0.0581  49   PRO B CA  
9374  C C   . PRO B 51   ? 0.3729 0.4487 0.3240 -0.1724 -0.0310 0.0605  49   PRO B C   
9375  O O   . PRO B 51   ? 0.3683 0.4430 0.3149 -0.1802 -0.0319 0.0645  49   PRO B O   
9376  C CB  . PRO B 51   ? 0.4234 0.4698 0.3667 -0.1700 -0.0382 0.0555  49   PRO B CB  
9377  C CG  . PRO B 51   ? 0.4013 0.4481 0.3493 -0.1595 -0.0364 0.0508  49   PRO B CG  
9378  C CD  . PRO B 51   ? 0.3526 0.4177 0.3096 -0.1586 -0.0341 0.0503  49   PRO B CD  
9379  N N   . LEU B 52   ? 0.3494 0.4320 0.3054 -0.1634 -0.0272 0.0582  50   LEU B N   
9380  C CA  . LEU B 52   ? 0.3159 0.4064 0.2722 -0.1627 -0.0236 0.0603  50   LEU B CA  
9381  C C   . LEU B 52   ? 0.4164 0.5279 0.3785 -0.1677 -0.0208 0.0635  50   LEU B C   
9382  O O   . LEU B 52   ? 0.3656 0.4819 0.3253 -0.1730 -0.0196 0.0673  50   LEU B O   
9383  C CB  . LEU B 52   ? 0.3194 0.4110 0.2790 -0.1517 -0.0205 0.0567  50   LEU B CB  
9384  C CG  . LEU B 52   ? 0.3490 0.4214 0.3035 -0.1460 -0.0228 0.0536  50   LEU B CG  
9385  C CD1 . LEU B 52   ? 0.3358 0.4123 0.2954 -0.1355 -0.0196 0.0499  50   LEU B CD1 
9386  C CD2 . LEU B 52   ? 0.3648 0.4243 0.3107 -0.1493 -0.0244 0.0559  50   LEU B CD2 
9387  N N   . VAL B 53   ? 0.3455 0.4703 0.3153 -0.1661 -0.0198 0.0621  51   VAL B N   
9388  C CA  . VAL B 53   ? 0.3326 0.4782 0.3084 -0.1710 -0.0174 0.0651  51   VAL B CA  
9389  C C   . VAL B 53   ? 0.3963 0.5385 0.3667 -0.1810 -0.0204 0.0689  51   VAL B C   
9390  O O   . VAL B 53   ? 0.3923 0.5440 0.3624 -0.1836 -0.0186 0.0717  51   VAL B O   
9391  C CB  . VAL B 53   ? 0.3326 0.4901 0.3166 -0.1678 -0.0170 0.0628  51   VAL B CB  
9392  C CG1 . VAL B 53   ? 0.3667 0.5424 0.3553 -0.1720 -0.0158 0.0653  51   VAL B CG1 
9393  C CG2 . VAL B 53   ? 0.3222 0.4845 0.3114 -0.1563 -0.0136 0.0589  51   VAL B CG2 
9394  N N   . GLU B 54   ? 0.3895 0.5163 0.3544 -0.1851 -0.0251 0.0685  52   GLU B N   
9395  C CA  . GLU B 54   ? 0.4051 0.5262 0.3637 -0.1928 -0.0284 0.0714  52   GLU B CA  
9396  C C   . GLU B 54   ? 0.4576 0.5708 0.4089 -0.1960 -0.0284 0.0743  52   GLU B C   
9397  O O   . GLU B 54   ? 0.4273 0.5468 0.3769 -0.2009 -0.0283 0.0775  52   GLU B O   
9398  C CB  . GLU B 54   ? 0.4656 0.5702 0.4191 -0.1956 -0.0336 0.0699  52   GLU B CB  
9399  N N   . ALA B 55   ? 0.3944 0.4940 0.3413 -0.1931 -0.0286 0.0733  53   ALA B N   
9400  C CA  . ALA B 55   ? 0.4421 0.5334 0.3817 -0.1955 -0.0287 0.0760  53   ALA B CA  
9401  C C   . ALA B 55   ? 0.4152 0.5237 0.3589 -0.1939 -0.0237 0.0779  53   ALA B C   
9402  O O   . ALA B 55   ? 0.4404 0.5481 0.3792 -0.1979 -0.0238 0.0810  53   ALA B O   
9403  C CB  . ALA B 55   ? 0.4416 0.5149 0.3760 -0.1920 -0.0300 0.0743  53   ALA B CB  
9404  N N   . ALA B 56   ? 0.3884 0.5124 0.3408 -0.1878 -0.0196 0.0759  54   ALA B N   
9405  C CA  . ALA B 56   ? 0.4196 0.5597 0.3759 -0.1849 -0.0147 0.0770  54   ALA B CA  
9406  C C   . ALA B 56   ? 0.4246 0.5823 0.3853 -0.1879 -0.0135 0.0788  54   ALA B C   
9407  O O   . ALA B 56   ? 0.4436 0.6142 0.4065 -0.1863 -0.0098 0.0801  54   ALA B O   
9408  C CB  . ALA B 56   ? 0.3942 0.5427 0.3575 -0.1765 -0.0109 0.0739  54   ALA B CB  
9409  N N   . THR B 57   ? 0.4083 0.5666 0.3700 -0.1921 -0.0164 0.0790  55   THR B N   
9410  C CA  . THR B 57   ? 0.4718 0.6475 0.4383 -0.1947 -0.0154 0.0806  55   THR B CA  
9411  C C   . THR B 57   ? 0.5043 0.6815 0.4658 -0.2007 -0.0155 0.0845  55   THR B C   
9412  O O   . THR B 57   ? 0.4762 0.6377 0.4292 -0.2061 -0.0188 0.0864  55   THR B O   
9413  C CB  . THR B 57   ? 0.4433 0.6169 0.4108 -0.1983 -0.0191 0.0800  55   THR B CB  
9414  O OG1 . THR B 57   ? 0.4529 0.6310 0.4271 -0.1921 -0.0181 0.0765  55   THR B OG1 
9415  C CG2 . THR B 57   ? 0.4202 0.6086 0.3904 -0.2031 -0.0190 0.0825  55   THR B CG2 
9416  N N   . GLN B 58   ? 0.4633 0.6593 0.4299 -0.1996 -0.0118 0.0856  56   GLN B N   
9417  C CA  . GLN B 58   ? 0.4813 0.6822 0.4444 -0.2051 -0.0115 0.0893  56   GLN B CA  
9418  C C   . GLN B 58   ? 0.4734 0.6927 0.4424 -0.2076 -0.0108 0.0905  56   GLN B C   
9419  O O   . GLN B 58   ? 0.4896 0.7206 0.4663 -0.2031 -0.0093 0.0883  56   GLN B O   
9420  C CB  . GLN B 58   ? 0.4987 0.7045 0.4613 -0.2011 -0.0074 0.0897  56   GLN B CB  
9421  C CG  . GLN B 58   ? 0.4827 0.6730 0.4407 -0.1971 -0.0073 0.0881  56   GLN B CG  
9422  C CD  . GLN B 58   ? 0.5814 0.7721 0.5355 -0.1961 -0.0047 0.0898  56   GLN B CD  
9423  O OE1 . GLN B 58   ? 0.5628 0.7473 0.5102 -0.2021 -0.0064 0.0929  56   GLN B OE1 
9424  N NE2 . GLN B 58   ? 0.5345 0.7324 0.4923 -0.1883 -0.0005 0.0876  56   GLN B NE2 
9425  N N   . SER B 59   ? 0.5247 0.7464 0.4900 -0.2147 -0.0118 0.0941  57   SER B N   
9426  C CA  . SER B 59   ? 0.5572 0.7965 0.5276 -0.2178 -0.0112 0.0958  57   SER B CA  
9427  C C   . SER B 59   ? 0.5553 0.8153 0.5340 -0.2108 -0.0060 0.0946  57   SER B C   
9428  O O   . SER B 59   ? 0.5145 0.7754 0.4936 -0.2049 -0.0028 0.0933  57   SER B O   
9429  C CB  . SER B 59   ? 0.5506 0.7885 0.5150 -0.2267 -0.0130 0.1001  57   SER B CB  
9430  O OG  . SER B 59   ? 0.5328 0.7744 0.4953 -0.2254 -0.0099 0.1015  57   SER B OG  
9431  N N   . LYS B 60   ? 0.5000 0.7766 0.4850 -0.2114 -0.0054 0.0949  58   LYS B N   
9432  C CA  . LYS B 60   ? 0.5194 0.8161 0.5119 -0.2048 -0.0007 0.0939  58   LYS B CA  
9433  C C   . LYS B 60   ? 0.4721 0.7748 0.4621 -0.2060 0.0021  0.0963  58   LYS B C   
9434  O O   . LYS B 60   ? 0.5331 0.8458 0.5268 -0.1989 0.0062  0.0948  58   LYS B O   
9435  C CB  . LYS B 60   ? 0.5053 0.8182 0.5044 -0.2059 -0.0010 0.0943  58   LYS B CB  
9436  N N   . GLU B 61   ? 0.5105 0.8070 0.4940 -0.2147 -0.0002 0.0999  59   GLU B N   
9437  C CA  . GLU B 61   ? 0.4603 0.7619 0.4410 -0.2162 0.0022  0.1024  59   GLU B CA  
9438  C C   . GLU B 61   ? 0.5645 0.8551 0.5410 -0.2113 0.0040  0.1010  59   GLU B C   
9439  O O   . GLU B 61   ? 0.5180 0.8181 0.4965 -0.2061 0.0081  0.1004  59   GLU B O   
9440  C CB  . GLU B 61   ? 0.5361 0.8318 0.5102 -0.2270 -0.0011 0.1067  59   GLU B CB  
9441  N N   . ILE B 62   ? 0.5225 0.7928 0.4931 -0.2127 0.0009  0.1003  60   ILE B N   
9442  C CA  . ILE B 62   ? 0.4903 0.7494 0.4569 -0.2081 0.0023  0.0990  60   ILE B CA  
9443  C C   . ILE B 62   ? 0.4330 0.7002 0.4063 -0.1978 0.0060  0.0950  60   ILE B C   
9444  O O   . ILE B 62   ? 0.5314 0.8017 0.5045 -0.1924 0.0095  0.0941  60   ILE B O   
9445  C CB  . ILE B 62   ? 0.5527 0.7882 0.5115 -0.2117 -0.0022 0.0990  60   ILE B CB  
9446  N N   . ARG B 63   ? 0.4859 0.7567 0.4652 -0.1948 0.0052  0.0925  61   ARG B N   
9447  C CA  . ARG B 63   ? 0.4704 0.7496 0.4564 -0.1850 0.0085  0.0888  61   ARG B CA  
9448  C C   . ARG B 63   ? 0.4474 0.7460 0.4383 -0.1804 0.0131  0.0887  61   ARG B C   
9449  O O   . ARG B 63   ? 0.4679 0.7695 0.4603 -0.1727 0.0165  0.0865  61   ARG B O   
9450  C CB  . ARG B 63   ? 0.5173 0.7991 0.5089 -0.1835 0.0068  0.0866  61   ARG B CB  
9451  C CG  . ARG B 63   ? 0.4740 0.7373 0.4624 -0.1842 0.0034  0.0851  61   ARG B CG  
9452  C CD  . ARG B 63   ? 0.5742 0.8397 0.5666 -0.1858 0.0007  0.0841  61   ARG B CD  
9453  N NE  . ARG B 63   ? 0.5590 0.8433 0.5602 -0.1800 0.0035  0.0824  61   ARG B NE  
9454  C CZ  . ARG B 63   ? 0.5932 0.8861 0.5988 -0.1819 0.0020  0.0826  61   ARG B CZ  
9455  N NH1 . ARG B 63   ? 0.5488 0.8337 0.5508 -0.1897 -0.0022 0.0843  61   ARG B NH1 
9456  N NH2 . ARG B 63   ? 0.6589 0.9685 0.6722 -0.1758 0.0046  0.0809  61   ARG B NH2 
9457  N N   . ASP B 64   ? 0.4779 0.7897 0.4711 -0.1848 0.0131  0.0911  62   ASP B N   
9458  C CA  . ASP B 64   ? 0.5054 0.8355 0.5029 -0.1805 0.0173  0.0911  62   ASP B CA  
9459  C C   . ASP B 64   ? 0.3692 0.6959 0.3610 -0.1806 0.0195  0.0925  62   ASP B C   
9460  O O   . ASP B 64   ? 0.3979 0.7327 0.3919 -0.1732 0.0235  0.0907  62   ASP B O   
9461  C CB  . ASP B 64   ? 0.4547 0.7995 0.4556 -0.1860 0.0167  0.0937  62   ASP B CB  
9462  C CG  . ASP B 64   ? 0.5310 0.8828 0.5385 -0.1842 0.0153  0.0920  62   ASP B CG  
9463  O OD1 . ASP B 64   ? 0.5330 0.8832 0.5441 -0.1768 0.0161  0.0884  62   ASP B OD1 
9464  O OD2 . ASP B 64   ? 0.5259 0.8849 0.5349 -0.1903 0.0134  0.0942  62   ASP B OD2 
9465  N N   . ALA B 65   ? 0.4431 0.7575 0.4274 -0.1886 0.0169  0.0957  63   ALA B N   
9466  C CA  . ALA B 65   ? 0.4311 0.7410 0.4092 -0.1891 0.0187  0.0972  63   ALA B CA  
9467  C C   . ALA B 65   ? 0.4738 0.7743 0.4500 -0.1815 0.0204  0.0942  63   ALA B C   
9468  O O   . ALA B 65   ? 0.5149 0.8192 0.4896 -0.1773 0.0238  0.0939  63   ALA B O   
9469  C CB  . ALA B 65   ? 0.4949 0.7909 0.4647 -0.1991 0.0149  0.1010  63   ALA B CB  
9470  N N   . ALA B 66   ? 0.4746 0.7628 0.4508 -0.1797 0.0182  0.0920  64   ALA B N   
9471  C CA  . ALA B 66   ? 0.4653 0.7441 0.4395 -0.1728 0.0197  0.0893  64   ALA B CA  
9472  C C   . ALA B 66   ? 0.4435 0.7361 0.4245 -0.1628 0.0239  0.0858  64   ALA B C   
9473  O O   . ALA B 66   ? 0.4876 0.7789 0.4667 -0.1569 0.0267  0.0842  64   ALA B O   
9474  C CB  . ALA B 66   ? 0.4346 0.6966 0.4068 -0.1740 0.0160  0.0880  64   ALA B CB  
9475  N N   . ALA B 67   ? 0.4295 0.7351 0.4183 -0.1606 0.0243  0.0844  65   ALA B N   
9476  C CA  . ALA B 67   ? 0.3833 0.7020 0.3785 -0.1508 0.0280  0.0810  65   ALA B CA  
9477  C C   . ALA B 67   ? 0.4879 0.8193 0.4831 -0.1483 0.0318  0.0818  65   ALA B C   
9478  O O   . ALA B 67   ? 0.5306 0.8674 0.5276 -0.1397 0.0351  0.0790  65   ALA B O   
9479  C CB  . ALA B 67   ? 0.4348 0.7645 0.4378 -0.1494 0.0273  0.0798  65   ALA B CB  
9480  N N   . SER B 68   ? 0.4989 0.8349 0.4916 -0.1556 0.0312  0.0855  66   SER B N   
9481  C CA  . SER B 68   ? 0.4373 0.7837 0.4288 -0.1539 0.0347  0.0865  66   SER B CA  
9482  C C   . SER B 68   ? 0.4884 0.8229 0.4726 -0.1522 0.0359  0.0864  66   SER B C   
9483  O O   . SER B 68   ? 0.5734 0.9134 0.5577 -0.1449 0.0395  0.0844  66   SER B O   
9484  C CB  . SER B 68   ? 0.5405 0.8943 0.5311 -0.1628 0.0336  0.0907  66   SER B CB  
9485  N N   . THR B 69   ? 0.5181 0.8356 0.4954 -0.1587 0.0327  0.0885  67   THR B N   
9486  C CA  . THR B 69   ? 0.4197 0.7244 0.3894 -0.1574 0.0333  0.0886  67   THR B CA  
9487  C C   . THR B 69   ? 0.4465 0.7482 0.4176 -0.1477 0.0354  0.0844  67   THR B C   
9488  O O   . THR B 69   ? 0.4967 0.7980 0.4643 -0.1428 0.0381  0.0834  67   THR B O   
9489  C CB  . THR B 69   ? 0.5198 0.8053 0.4823 -0.1654 0.0289  0.0911  67   THR B CB  
9490  O OG1 . THR B 69   ? 0.4970 0.7847 0.4570 -0.1744 0.0272  0.0952  67   THR B OG1 
9491  C CG2 . THR B 69   ? 0.4308 0.7017 0.3853 -0.1634 0.0292  0.0910  67   THR B CG2 
9492  N N   . ALA B 70   ? 0.4340 0.7334 0.4098 -0.1447 0.0341  0.0818  68   ALA B N   
9493  C CA  . ALA B 70   ? 0.4811 0.7779 0.4584 -0.1355 0.0360  0.0777  68   ALA B CA  
9494  C C   . ALA B 70   ? 0.4945 0.8073 0.4765 -0.1270 0.0402  0.0752  68   ALA B C   
9495  O O   . ALA B 70   ? 0.4809 0.7915 0.4608 -0.1200 0.0426  0.0727  68   ALA B O   
9496  C CB  . ALA B 70   ? 0.4669 0.7591 0.4488 -0.1345 0.0336  0.0757  68   ALA B CB  
9497  N N   . ARG B 71   ? 0.5003 0.8289 0.4884 -0.1274 0.0411  0.0757  69   ARG B N   
9498  C CA  . ARG B 71   ? 0.4819 0.8257 0.4744 -0.1191 0.0449  0.0733  69   ARG B CA  
9499  C C   . ARG B 71   ? 0.3990 0.7448 0.3862 -0.1178 0.0477  0.0741  69   ARG B C   
9500  O O   . ARG B 71   ? 0.4962 0.8456 0.4833 -0.1093 0.0507  0.0710  69   ARG B O   
9501  C CB  . ARG B 71   ? 0.5507 0.9107 0.5502 -0.1206 0.0449  0.0741  69   ARG B CB  
9502  C CG  . ARG B 71   ? 0.5525 0.9285 0.5563 -0.1123 0.0486  0.0718  69   ARG B CG  
9503  C CD  . ARG B 71   ? 0.6125 1.0046 0.6233 -0.1136 0.0484  0.0727  69   ARG B CD  
9504  N NE  . ARG B 71   ? 0.5573 0.9507 0.5741 -0.1093 0.0471  0.0701  69   ARG B NE  
9505  C CZ  . ARG B 71   ? 0.5816 0.9799 0.6022 -0.0993 0.0491  0.0662  69   ARG B CZ  
9506  N NH1 . ARG B 71   ? 0.5410 0.9428 0.5598 -0.0922 0.0524  0.0642  69   ARG B NH1 
9507  N NH2 . ARG B 71   ? 0.6008 1.0002 0.6268 -0.0963 0.0476  0.0642  69   ARG B NH2 
9508  N N   . LYS B 72   ? 0.4584 0.8013 0.4405 -0.1261 0.0467  0.0781  70   LYS B N   
9509  C CA  . LYS B 72   ? 0.4157 0.7590 0.3918 -0.1254 0.0492  0.0791  70   LYS B CA  
9510  C C   . LYS B 72   ? 0.5089 0.8378 0.4787 -0.1210 0.0495  0.0772  70   LYS B C   
9511  O O   . LYS B 72   ? 0.4969 0.8286 0.4641 -0.1149 0.0525  0.0754  70   LYS B O   
9512  C CB  . LYS B 72   ? 0.4937 0.8352 0.4653 -0.1358 0.0475  0.0840  70   LYS B CB  
9513  N N   . LEU B 73   ? 0.5358 0.8491 0.5028 -0.1240 0.0464  0.0773  71   LEU B N   
9514  C CA  . LEU B 73   ? 0.5248 0.8243 0.4857 -0.1199 0.0465  0.0755  71   LEU B CA  
9515  C C   . LEU B 73   ? 0.5230 0.8270 0.4878 -0.1091 0.0489  0.0706  71   LEU B C   
9516  O O   . LEU B 73   ? 0.4967 0.7969 0.4570 -0.1035 0.0508  0.0687  71   LEU B O   
9517  C CB  . LEU B 73   ? 0.4668 0.7490 0.4242 -0.1254 0.0424  0.0768  71   LEU B CB  
9518  C CG  . LEU B 73   ? 0.5268 0.8005 0.4787 -0.1359 0.0393  0.0814  71   LEU B CG  
9519  C CD1 . LEU B 73   ? 0.4316 0.6884 0.3809 -0.1401 0.0351  0.0820  71   LEU B CD1 
9520  C CD2 . LEU B 73   ? 0.5383 0.8076 0.4819 -0.1372 0.0404  0.0835  71   LEU B CD2 
9521  N N   . ILE B 74   ? 0.5224 0.8341 0.4953 -0.1061 0.0488  0.0686  72   ILE B N   
9522  C CA  . ILE B 74   ? 0.4674 0.7824 0.4441 -0.0959 0.0507  0.0639  72   ILE B CA  
9523  C C   . ILE B 74   ? 0.5168 0.8452 0.4948 -0.0892 0.0545  0.0622  72   ILE B C   
9524  O O   . ILE B 74   ? 0.5787 0.9058 0.5550 -0.0809 0.0565  0.0587  72   ILE B O   
9525  C CB  . ILE B 74   ? 0.5351 0.8536 0.5196 -0.0949 0.0492  0.0625  72   ILE B CB  
9526  C CG1 . ILE B 74   ? 0.5215 0.8245 0.5039 -0.0993 0.0458  0.0631  72   ILE B CG1 
9527  C CG2 . ILE B 74   ? 0.5001 0.8256 0.4895 -0.0841 0.0514  0.0579  72   ILE B CG2 
9528  C CD1 . ILE B 74   ? 0.4445 0.7499 0.4335 -0.1017 0.0435  0.0630  72   ILE B CD1 
9529  N N   . GLU B 75   ? 0.5467 0.8880 0.5274 -0.0926 0.0553  0.0645  73   GLU B N   
9530  C CA  . GLU B 75   ? 0.5396 0.8935 0.5209 -0.0869 0.0589  0.0632  73   GLU B CA  
9531  C C   . GLU B 75   ? 0.5301 0.8768 0.5028 -0.0855 0.0605  0.0633  73   GLU B C   
9532  O O   . GLU B 75   ? 0.5295 0.8774 0.5008 -0.0769 0.0629  0.0598  73   GLU B O   
9533  C CB  . GLU B 75   ? 0.5055 0.8738 0.4905 -0.0923 0.0593  0.0664  73   GLU B CB  
9534  N N   . ALA B 76   ? 0.5141 0.8524 0.4806 -0.0937 0.0590  0.0671  74   ALA B N   
9535  C CA  . ALA B 76   ? 0.4469 0.7766 0.4045 -0.0929 0.0600  0.0674  74   ALA B CA  
9536  C C   . ALA B 76   ? 0.5482 0.8666 0.5027 -0.0858 0.0599  0.0635  74   ALA B C   
9537  O O   . ALA B 76   ? 0.6099 0.9281 0.5602 -0.0793 0.0622  0.0611  74   ALA B O   
9538  C CB  . ALA B 76   ? 0.4632 0.7826 0.4146 -0.1032 0.0574  0.0721  74   ALA B CB  
9539  N N   . LEU B 77   ? 0.5190 0.8280 0.4752 -0.0868 0.0573  0.0628  75   LEU B N   
9540  C CA  . LEU B 77   ? 0.5417 0.8402 0.4952 -0.0803 0.0571  0.0592  75   LEU B CA  
9541  C C   . LEU B 77   ? 0.4919 0.7992 0.4491 -0.0695 0.0599  0.0545  75   LEU B C   
9542  O O   . LEU B 77   ? 0.5772 0.8795 0.5295 -0.0632 0.0612  0.0517  75   LEU B O   
9543  C CB  . LEU B 77   ? 0.4423 0.7316 0.3984 -0.0831 0.0540  0.0592  75   LEU B CB  
9544  C CG  . LEU B 77   ? 0.5195 0.7927 0.4687 -0.0906 0.0508  0.0622  75   LEU B CG  
9545  C CD1 . LEU B 77   ? 0.5137 0.7797 0.4666 -0.0931 0.0479  0.0621  75   LEU B CD1 
9546  C CD2 . LEU B 77   ? 0.5278 0.7903 0.4686 -0.0866 0.0512  0.0608  75   LEU B CD2 
9547  N N   . ARG B 78   ? 0.4557 0.7756 0.4213 -0.0672 0.0607  0.0535  76   ARG B N   
9548  C CA  . ARG B 78   ? 0.4574 0.7845 0.4268 -0.0568 0.0629  0.0489  76   ARG B CA  
9549  C C   . ARG B 78   ? 0.5800 0.9174 0.5476 -0.0526 0.0660  0.0482  76   ARG B C   
9550  O O   . ARG B 78   ? 0.4788 0.8196 0.4473 -0.0434 0.0678  0.0442  76   ARG B O   
9551  C CB  . ARG B 78   ? 0.5709 0.9068 0.5497 -0.0556 0.0622  0.0480  76   ARG B CB  
9552  C CG  . ARG B 78   ? 0.5341 0.8601 0.5151 -0.0561 0.0596  0.0470  76   ARG B CG  
9553  C CD  . ARG B 78   ? 0.5776 0.9128 0.5676 -0.0551 0.0588  0.0463  76   ARG B CD  
9554  N NE  . ARG B 78   ? 0.5174 0.8454 0.5099 -0.0504 0.0576  0.0433  76   ARG B NE  
9555  C CZ  . ARG B 78   ? 0.5993 0.9325 0.5990 -0.0484 0.0566  0.0421  76   ARG B CZ  
9556  N NH1 . ARG B 78   ? 0.6063 0.9520 0.6115 -0.0509 0.0565  0.0438  76   ARG B NH1 
9557  N NH2 . ARG B 78   ? 0.5477 0.8737 0.5491 -0.0438 0.0557  0.0392  76   ARG B NH2 
9558  N N   . GLY B 79   ? 0.5843 0.9262 0.5492 -0.0591 0.0666  0.0520  77   GLY B N   
9559  C CA  . GLY B 79   ? 0.5647 0.9156 0.5271 -0.0553 0.0697  0.0514  77   GLY B CA  
9560  C C   . GLY B 79   ? 0.6799 1.0210 0.6335 -0.0511 0.0707  0.0495  77   GLY B C   
9561  O O   . GLY B 79   ? 0.5665 0.9130 0.5182 -0.0441 0.0733  0.0469  77   GLY B O   
9562  N N   . LYS B 80   ? 0.6347 0.9609 0.5823 -0.0551 0.0686  0.0507  78   LYS B N   
9563  C CA  . LYS B 80   ? 0.6428 0.9583 0.5813 -0.0519 0.0689  0.0492  78   LYS B CA  
9564  C C   . LYS B 80   ? 0.6751 0.9875 0.6136 -0.0413 0.0696  0.0436  78   LYS B C   
9565  O O   . LYS B 80   ? 0.7010 1.0020 0.6380 -0.0398 0.0677  0.0419  78   LYS B O   
9566  C CB  . LYS B 80   ? 0.6151 0.9152 0.5475 -0.0590 0.0659  0.0520  78   LYS B CB  
9567  C CG  . LYS B 80   ? 0.5863 0.8875 0.5181 -0.0697 0.0647  0.0576  78   LYS B CG  
9568  C CD  . LYS B 80   ? 0.5970 0.8828 0.5246 -0.0767 0.0610  0.0602  78   LYS B CD  
9569  C CE  . LYS B 80   ? 0.6437 0.9294 0.5695 -0.0871 0.0596  0.0656  78   LYS B CE  
9570  N NZ  . LYS B 80   ? 0.5236 0.7926 0.4435 -0.0937 0.0559  0.0684  78   LYS B NZ  
9571  N N   . SER B 84   ? 0.8045 1.0396 0.7237 -0.0030 0.0591  0.0179  82   SER B N   
9572  C CA  . SER B 84   ? 0.6722 0.8882 0.5876 -0.0021 0.0549  0.0159  82   SER B CA  
9573  C C   . SER B 84   ? 0.6645 0.8758 0.5724 0.0046  0.0553  0.0122  82   SER B C   
9574  O O   . SER B 84   ? 0.6419 0.8620 0.5497 0.0113  0.0582  0.0093  82   SER B O   
9575  C CB  . SER B 84   ? 0.5233 0.7312 0.4455 0.0004  0.0520  0.0134  82   SER B CB  
9576  N N   . GLY B 85   ? 0.5445 0.7418 0.4461 0.0030  0.0523  0.0122  83   GLY B N   
9577  C CA  . GLY B 85   ? 0.5808 0.7713 0.4755 0.0093  0.0518  0.0082  83   GLY B CA  
9578  C C   . GLY B 85   ? 0.5114 0.6950 0.4095 0.0166  0.0502  0.0032  83   GLY B C   
9579  O O   . GLY B 85   ? 0.5357 0.7200 0.4303 0.0236  0.0514  -0.0007 83   GLY B O   
9580  N N   . VAL B 86   ? 0.5243 0.7010 0.4290 0.0150  0.0474  0.0031  84   VAL B N   
9581  C CA  . VAL B 86   ? 0.5060 0.6756 0.4139 0.0213  0.0456  -0.0013 84   VAL B CA  
9582  C C   . VAL B 86   ? 0.5209 0.7033 0.4334 0.0268  0.0490  -0.0032 84   VAL B C   
9583  O O   . VAL B 86   ? 0.5432 0.7230 0.4546 0.0342  0.0490  -0.0075 84   VAL B O   
9584  C CB  . VAL B 86   ? 0.5024 0.6614 0.4159 0.0178  0.0418  -0.0006 84   VAL B CB  
9585  C CG1 . VAL B 86   ? 0.6163 0.7837 0.5363 0.0121  0.0428  0.0032  84   VAL B CG1 
9586  C CG2 . VAL B 86   ? 0.5438 0.6958 0.4607 0.0241  0.0401  -0.0050 84   VAL B CG2 
9587  N N   . GLU B 87   ? 0.5564 0.7527 0.4737 0.0234  0.0517  -0.0001 85   GLU B N   
9588  C CA  . GLU B 87   ? 0.5466 0.7566 0.4682 0.0287  0.0551  -0.0016 85   GLU B CA  
9589  C C   . GLU B 87   ? 0.4847 0.7009 0.3999 0.0351  0.0581  -0.0043 85   GLU B C   
9590  O O   . GLU B 87   ? 0.4768 0.6957 0.3929 0.0428  0.0592  -0.0081 85   GLU B O   
9591  C CB  . GLU B 87   ? 0.5833 0.8080 0.5108 0.0230  0.0574  0.0027  85   GLU B CB  
9592  N N   . GLY B 88   ? 0.5086 0.7269 0.4169 0.0320  0.0594  -0.0023 86   GLY B N   
9593  C CA  . GLY B 88   ? 0.4748 0.6987 0.3762 0.0380  0.0622  -0.0048 86   GLY B CA  
9594  C C   . GLY B 88   ? 0.4638 0.6733 0.3595 0.0445  0.0596  -0.0098 86   GLY B C   
9595  O O   . GLY B 88   ? 0.4478 0.6608 0.3398 0.0520  0.0615  -0.0135 86   GLY B O   
9596  N N   . LEU B 89   ? 0.4713 0.6647 0.3661 0.0417  0.0552  -0.0100 87   LEU B N   
9597  C CA  . LEU B 89   ? 0.4709 0.6502 0.3611 0.0472  0.0523  -0.0146 87   LEU B CA  
9598  C C   . LEU B 89   ? 0.4343 0.6124 0.3295 0.0539  0.0519  -0.0184 87   LEU B C   
9599  O O   . LEU B 89   ? 0.4147 0.5895 0.3055 0.0612  0.0520  -0.0228 87   LEU B O   
9600  C CB  . LEU B 89   ? 0.4705 0.6342 0.3596 0.0422  0.0477  -0.0135 87   LEU B CB  
9601  C CG  . LEU B 89   ? 0.4863 0.6342 0.3723 0.0463  0.0438  -0.0177 87   LEU B CG  
9602  C CD1 . LEU B 89   ? 0.5532 0.6988 0.4295 0.0507  0.0444  -0.0205 87   LEU B CD1 
9603  C CD2 . LEU B 89   ? 0.5565 0.6918 0.4439 0.0404  0.0396  -0.0158 87   LEU B CD2 
9604  N N   . VAL B 90   ? 0.4444 0.6249 0.3484 0.0514  0.0514  -0.0167 88   VAL B N   
9605  C CA  . VAL B 90   ? 0.4411 0.6211 0.3503 0.0571  0.0510  -0.0197 88   VAL B CA  
9606  C C   . VAL B 90   ? 0.5264 0.7194 0.4346 0.0642  0.0550  -0.0219 88   VAL B C   
9607  O O   . VAL B 90   ? 0.4486 0.6375 0.3553 0.0718  0.0546  -0.0262 88   VAL B O   
9608  C CB  . VAL B 90   ? 0.4275 0.6097 0.3460 0.0524  0.0501  -0.0169 88   VAL B CB  
9609  C CG1 . VAL B 90   ? 0.4572 0.6427 0.3814 0.0583  0.0506  -0.0194 88   VAL B CG1 
9610  C CG2 . VAL B 90   ? 0.3926 0.5598 0.3119 0.0473  0.0458  -0.0159 88   VAL B CG2 
9611  N N   . GLN B 91   ? 0.4582 0.6671 0.3671 0.0619  0.0589  -0.0190 89   GLN B N   
9612  C CA  . GLN B 91   ? 0.5157 0.7386 0.4240 0.0688  0.0629  -0.0209 89   GLN B CA  
9613  C C   . GLN B 91   ? 0.4885 0.7066 0.3875 0.0745  0.0633  -0.0245 89   GLN B C   
9614  O O   . GLN B 91   ? 0.5149 0.7328 0.4138 0.0819  0.0635  -0.0279 89   GLN B O   
9615  C CB  . GLN B 91   ? 0.5454 0.7849 0.4583 0.0635  0.0660  -0.0163 89   GLN B CB  
9616  N N   . GLU B 92   ? 0.4256 0.6380 0.3170 0.0709  0.0627  -0.0235 90   GLU B N   
9617  C CA  . GLU B 92   ? 0.4845 0.6927 0.3671 0.0757  0.0629  -0.0266 90   GLU B CA  
9618  C C   . GLU B 92   ? 0.4312 0.6254 0.3097 0.0830  0.0601  -0.0321 90   GLU B C   
9619  O O   . GLU B 92   ? 0.4503 0.6424 0.3249 0.0894  0.0603  -0.0356 90   GLU B O   
9620  C CB  . GLU B 92   ? 0.5091 0.7141 0.3839 0.0701  0.0627  -0.0242 90   GLU B CB  
9621  C CG  . GLU B 92   ? 0.5644 0.7649 0.4301 0.0746  0.0628  -0.0271 90   GLU B CG  
9622  C CD  . GLU B 92   ? 0.5542 0.7501 0.4116 0.0693  0.0621  -0.0250 90   GLU B CD  
9623  O OE1 . GLU B 92   ? 0.5868 0.7824 0.4468 0.0613  0.0611  -0.0205 90   GLU B OE1 
9624  O OE2 . GLU B 92   ? 0.5292 0.7198 0.3785 0.0727  0.0617  -0.0275 90   GLU B OE2 
9625  N N   . TYR B 93   ? 0.4599 0.6409 0.3417 0.0805  0.0560  -0.0324 91   TYR B N   
9626  C CA  . TYR B 93   ? 0.4494 0.6155 0.3282 0.0861  0.0526  -0.0371 91   TYR B CA  
9627  C C   . TYR B 93   ? 0.4195 0.5847 0.3056 0.0896  0.0518  -0.0386 91   TYR B C   
9628  O O   . TYR B 93   ? 0.4162 0.5681 0.3011 0.0930  0.0485  -0.0419 91   TYR B O   
9629  C CB  . TYR B 93   ? 0.4181 0.5682 0.2942 0.0811  0.0481  -0.0367 91   TYR B CB  
9630  C CG  . TYR B 93   ? 0.4123 0.5607 0.2791 0.0797  0.0484  -0.0365 91   TYR B CG  
9631  C CD1 . TYR B 93   ? 0.3939 0.5354 0.2518 0.0858  0.0476  -0.0410 91   TYR B CD1 
9632  C CD2 . TYR B 93   ? 0.4492 0.6030 0.3157 0.0724  0.0494  -0.0319 91   TYR B CD2 
9633  C CE1 . TYR B 93   ? 0.4408 0.5811 0.2898 0.0848  0.0479  -0.0409 91   TYR B CE1 
9634  C CE2 . TYR B 93   ? 0.4849 0.6372 0.3424 0.0712  0.0496  -0.0315 91   TYR B CE2 
9635  C CZ  . TYR B 93   ? 0.4662 0.6120 0.3150 0.0775  0.0489  -0.0361 91   TYR B CZ  
9636  O OH  . TYR B 93   ? 0.4816 0.6260 0.3212 0.0764  0.0491  -0.0358 91   TYR B OH  
9637  N N   . SER B 94   ? 0.3715 0.5508 0.2650 0.0889  0.0547  -0.0362 92   SER B N   
9638  C CA  . SER B 94   ? 0.3623 0.5427 0.2628 0.0926  0.0542  -0.0374 92   SER B CA  
9639  C C   . SER B 94   ? 0.4095 0.5746 0.3136 0.0894  0.0497  -0.0374 92   SER B C   
9640  O O   . SER B 94   ? 0.4074 0.5638 0.3120 0.0943  0.0476  -0.0406 92   SER B O   
9641  C CB  . SER B 94   ? 0.4241 0.6044 0.3213 0.1023  0.0550  -0.0419 92   SER B CB  
9642  O OG  . SER B 94   ? 0.4752 0.6670 0.3720 0.1035  0.0578  -0.0409 92   SER B OG  
9643  N N   . LEU B 95   ? 0.3312 0.4928 0.2375 0.0811  0.0481  -0.0338 93   LEU B N   
9644  C CA  . LEU B 95   ? 0.3453 0.4931 0.2548 0.0777  0.0439  -0.0336 93   LEU B CA  
9645  C C   . LEU B 95   ? 0.3258 0.4780 0.2446 0.0765  0.0439  -0.0320 93   LEU B C   
9646  O O   . LEU B 95   ? 0.3772 0.5427 0.3009 0.0738  0.0465  -0.0290 93   LEU B O   
9647  C CB  . LEU B 95   ? 0.3352 0.4776 0.2436 0.0697  0.0420  -0.0305 93   LEU B CB  
9648  C CG  . LEU B 95   ? 0.3575 0.4949 0.2566 0.0699  0.0416  -0.0316 93   LEU B CG  
9649  C CD1 . LEU B 95   ? 0.3563 0.4870 0.2547 0.0622  0.0392  -0.0285 93   LEU B CD1 
9650  C CD2 . LEU B 95   ? 0.3611 0.4865 0.2544 0.0763  0.0393  -0.0366 93   LEU B CD2 
9651  N N   . SER B 96   ? 0.3053 0.4461 0.2264 0.0781  0.0408  -0.0339 94   SER B N   
9652  C CA  . SER B 96   ? 0.2988 0.4407 0.2283 0.0751  0.0399  -0.0318 94   SER B CA  
9653  C C   . SER B 96   ? 0.3306 0.4694 0.2628 0.0664  0.0383  -0.0280 94   SER B C   
9654  O O   . SER B 96   ? 0.3207 0.4543 0.2480 0.0631  0.0373  -0.0274 94   SER B O   
9655  C CB  . SER B 96   ? 0.3473 0.4772 0.2779 0.0790  0.0370  -0.0347 94   SER B CB  
9656  O OG  . SER B 96   ? 0.3033 0.4188 0.2306 0.0764  0.0335  -0.0355 94   SER B OG  
9657  N N   . SER B 97   ? 0.2875 0.4290 0.2272 0.0628  0.0379  -0.0257 95   SER B N   
9658  C CA  . SER B 97   ? 0.2657 0.4032 0.2079 0.0549  0.0361  -0.0224 95   SER B CA  
9659  C C   . SER B 97   ? 0.3068 0.4283 0.2461 0.0538  0.0323  -0.0238 95   SER B C   
9660  O O   . SER B 97   ? 0.2838 0.4010 0.2202 0.0492  0.0311  -0.0222 95   SER B O   
9661  C CB  . SER B 97   ? 0.3297 0.4716 0.2802 0.0521  0.0359  -0.0202 95   SER B CB  
9662  O OG  . SER B 97   ? 0.4229 0.5804 0.3763 0.0514  0.0392  -0.0180 95   SER B OG  
9663  N N   . GLN B 98   ? 0.3001 0.4129 0.2400 0.0580  0.0303  -0.0267 96   GLN B N   
9664  C CA  . GLN B 98   ? 0.2798 0.3780 0.2174 0.0569  0.0267  -0.0281 96   GLN B CA  
9665  C C   . GLN B 98   ? 0.2611 0.3547 0.1907 0.0581  0.0261  -0.0298 96   GLN B C   
9666  O O   . GLN B 98   ? 0.2783 0.3630 0.2057 0.0547  0.0235  -0.0294 96   GLN B O   
9667  C CB  . GLN B 98   ? 0.2874 0.3778 0.2269 0.0612  0.0248  -0.0309 96   GLN B CB  
9668  C CG  . GLN B 98   ? 0.2725 0.3642 0.2196 0.0590  0.0244  -0.0292 96   GLN B CG  
9669  C CD  . GLN B 98   ? 0.3053 0.3911 0.2552 0.0525  0.0221  -0.0268 96   GLN B CD  
9670  O OE1 . GLN B 98   ? 0.3320 0.4233 0.2834 0.0476  0.0229  -0.0238 96   GLN B OE1 
9671  N NE2 . GLN B 98   ? 0.2929 0.3672 0.2433 0.0524  0.0190  -0.0282 96   GLN B NE2 
9672  N N   . GLU B 99   ? 0.2411 0.3406 0.1659 0.0631  0.0285  -0.0317 97   GLU B N   
9673  C CA  . GLU B 99   ? 0.2618 0.3578 0.1784 0.0642  0.0283  -0.0332 97   GLU B CA  
9674  C C   . GLU B 99   ? 0.3098 0.4105 0.2249 0.0581  0.0291  -0.0296 97   GLU B C   
9675  O O   . GLU B 99   ? 0.2968 0.3902 0.2071 0.0559  0.0271  -0.0296 97   GLU B O   
9676  C CB  . GLU B 99   ? 0.3221 0.4239 0.2337 0.0712  0.0309  -0.0361 97   GLU B CB  
9677  C CG  . GLU B 99   ? 0.2868 0.3801 0.1970 0.0777  0.0292  -0.0403 97   GLU B CG  
9678  C CD  . GLU B 99   ? 0.3255 0.4262 0.2323 0.0852  0.0321  -0.0429 97   GLU B CD  
9679  O OE1 . GLU B 99   ? 0.3239 0.4374 0.2299 0.0853  0.0356  -0.0415 97   GLU B OE1 
9680  O OE2 . GLU B 99   ? 0.3296 0.4232 0.2343 0.0909  0.0308  -0.0465 97   GLU B OE2 
9681  N N   . GLY B 100  ? 0.2787 0.3915 0.1981 0.0551  0.0319  -0.0264 98   GLY B N   
9682  C CA  . GLY B 100  ? 0.3005 0.4171 0.2185 0.0488  0.0325  -0.0226 98   GLY B CA  
9683  C C   . GLY B 100  ? 0.3041 0.4103 0.2239 0.0432  0.0289  -0.0209 98   GLY B C   
9684  O O   . GLY B 100  ? 0.3159 0.4174 0.2311 0.0400  0.0276  -0.0198 98   GLY B O   
9685  N N   . VAL B 101  ? 0.2796 0.3816 0.2059 0.0424  0.0272  -0.0209 99   VAL B N   
9686  C CA  . VAL B 101  ? 0.2551 0.3474 0.1835 0.0377  0.0238  -0.0195 99   VAL B CA  
9687  C C   . VAL B 101  ? 0.2941 0.3743 0.2174 0.0393  0.0207  -0.0221 99   VAL B C   
9688  O O   . VAL B 101  ? 0.2961 0.3703 0.2169 0.0355  0.0186  -0.0207 99   VAL B O   
9689  C CB  . VAL B 101  ? 0.2624 0.3532 0.1985 0.0372  0.0229  -0.0193 99   VAL B CB  
9690  C CG1 . VAL B 101  ? 0.2652 0.3455 0.2031 0.0333  0.0193  -0.0185 99   VAL B CG1 
9691  C CG2 . VAL B 101  ? 0.2739 0.3767 0.2150 0.0348  0.0255  -0.0165 99   VAL B CG2 
9692  N N   . ALA B 102  ? 0.2715 0.3476 0.1930 0.0450  0.0203  -0.0258 100  ALA B N   
9693  C CA  . ALA B 102  ? 0.2812 0.3458 0.1979 0.0466  0.0171  -0.0285 100  ALA B CA  
9694  C C   . ALA B 102  ? 0.3138 0.3783 0.2226 0.0459  0.0173  -0.0283 100  ALA B C   
9695  O O   . ALA B 102  ? 0.2916 0.3476 0.1975 0.0438  0.0143  -0.0284 100  ALA B O   
9696  C CB  . ALA B 102  ? 0.3059 0.3667 0.2212 0.0530  0.0169  -0.0325 100  ALA B CB  
9697  N N   . LEU B 103  ? 0.2855 0.3600 0.1910 0.0476  0.0208  -0.0279 101  LEU B N   
9698  C CA  . LEU B 103  ? 0.3149 0.3901 0.2125 0.0470  0.0213  -0.0275 101  LEU B CA  
9699  C C   . LEU B 103  ? 0.3063 0.3804 0.2041 0.0402  0.0201  -0.0236 101  LEU B C   
9700  O O   . LEU B 103  ? 0.3249 0.3926 0.2170 0.0388  0.0179  -0.0236 101  LEU B O   
9701  C CB  . LEU B 103  ? 0.3340 0.4217 0.2289 0.0499  0.0256  -0.0275 101  LEU B CB  
9702  C CG  . LEU B 103  ? 0.3038 0.3942 0.1904 0.0492  0.0268  -0.0268 101  LEU B CG  
9703  C CD1 . LEU B 103  ? 0.3227 0.4027 0.2018 0.0530  0.0243  -0.0306 101  LEU B CD1 
9704  C CD2 . LEU B 103  ? 0.3195 0.4240 0.2048 0.0519  0.0316  -0.0264 101  LEU B CD2 
9705  N N   . MET B 104  ? 0.2731 0.3528 0.1770 0.0360  0.0211  -0.0202 102  MET B N   
9706  C CA  . MET B 104  ? 0.3323 0.4102 0.2360 0.0295  0.0198  -0.0165 102  MET B CA  
9707  C C   . MET B 104  ? 0.3068 0.3722 0.2117 0.0278  0.0154  -0.0170 102  MET B C   
9708  O O   . MET B 104  ? 0.3286 0.3891 0.2299 0.0244  0.0134  -0.0153 102  MET B O   
9709  C CB  . MET B 104  ? 0.3142 0.4006 0.2240 0.0255  0.0218  -0.0130 102  MET B CB  
9710  C CG  . MET B 104  ? 0.3105 0.4107 0.2192 0.0264  0.0262  -0.0119 102  MET B CG  
9711  S SD  . MET B 104  ? 0.4352 0.5389 0.3342 0.0254  0.0278  -0.0106 102  MET B SD  
9712  C CE  . MET B 104  ? 0.5727 0.6733 0.4717 0.0168  0.0260  -0.0055 102  MET B CE  
9713  N N   . CYS B 105  ? 0.2688 0.3291 0.1785 0.0303  0.0138  -0.0194 103  CYS B N   
9714  C CA  . CYS B 105  ? 0.2782 0.3272 0.1889 0.0292  0.0097  -0.0203 103  CYS B CA  
9715  C C   . CYS B 105  ? 0.3232 0.3654 0.2265 0.0311  0.0076  -0.0225 103  CYS B C   
9716  O O   . CYS B 105  ? 0.3363 0.3717 0.2378 0.0285  0.0046  -0.0217 103  CYS B O   
9717  C CB  . CYS B 105  ? 0.2630 0.3085 0.1797 0.0316  0.0087  -0.0225 103  CYS B CB  
9718  S SG  . CYS B 105  ? 0.2951 0.3464 0.2207 0.0288  0.0102  -0.0199 103  CYS B SG  
9719  N N   . LEU B 106  ? 0.3021 0.3458 0.2012 0.0361  0.0090  -0.0255 104  LEU B N   
9720  C CA  . LEU B 106  ? 0.2855 0.3231 0.1768 0.0381  0.0071  -0.0278 104  LEU B CA  
9721  C C   . LEU B 106  ? 0.3339 0.3735 0.2195 0.0347  0.0074  -0.0251 104  LEU B C   
9722  O O   . LEU B 106  ? 0.3462 0.3785 0.2276 0.0335  0.0043  -0.0252 104  LEU B O   
9723  C CB  . LEU B 106  ? 0.2892 0.3291 0.1761 0.0441  0.0090  -0.0313 104  LEU B CB  
9724  C CG  . LEU B 106  ? 0.3061 0.3405 0.1839 0.0462  0.0073  -0.0338 104  LEU B CG  
9725  C CD1 . LEU B 106  ? 0.3885 0.4110 0.2667 0.0462  0.0027  -0.0359 104  LEU B CD1 
9726  C CD2 . LEU B 106  ? 0.3576 0.3960 0.2301 0.0521  0.0100  -0.0369 104  LEU B CD2 
9727  N N   . ALA B 107  ? 0.2936 0.3433 0.1789 0.0331  0.0110  -0.0224 105  ALA B N   
9728  C CA  . ALA B 107  ? 0.3395 0.3915 0.2190 0.0296  0.0115  -0.0194 105  ALA B CA  
9729  C C   . ALA B 107  ? 0.3449 0.3904 0.2262 0.0243  0.0083  -0.0165 105  ALA B C   
9730  O O   . ALA B 107  ? 0.3754 0.4157 0.2508 0.0227  0.0061  -0.0157 105  ALA B O   
9731  C CB  . ALA B 107  ? 0.3401 0.4048 0.2199 0.0284  0.0160  -0.0169 105  ALA B CB  
9732  N N   . GLU B 108  ? 0.3417 0.3872 0.2309 0.0219  0.0078  -0.0150 106  GLU B N   
9733  C CA  . GLU B 108  ? 0.3343 0.3731 0.2256 0.0176  0.0046  -0.0127 106  GLU B CA  
9734  C C   . GLU B 108  ? 0.4012 0.4295 0.2901 0.0189  0.0004  -0.0150 106  GLU B C   
9735  O O   . GLU B 108  ? 0.3858 0.4088 0.2712 0.0162  -0.0021 -0.0133 106  GLU B O   
9736  C CB  . GLU B 108  ? 0.3462 0.3860 0.2464 0.0159  0.0047  -0.0118 106  GLU B CB  
9737  C CG  . GLU B 108  ? 0.3699 0.4019 0.2731 0.0126  0.0012  -0.0102 106  GLU B CG  
9738  C CD  . GLU B 108  ? 0.4382 0.4697 0.3500 0.0124  0.0009  -0.0106 106  GLU B CD  
9739  O OE1 . GLU B 108  ? 0.4173 0.4555 0.3328 0.0140  0.0037  -0.0112 106  GLU B OE1 
9740  O OE2 . GLU B 108  ? 0.4596 0.4842 0.3743 0.0110  -0.0022 -0.0104 106  GLU B OE2 
9741  N N   . ALA B 109  ? 0.3547 0.3796 0.2452 0.0230  -0.0005 -0.0187 107  ALA B N   
9742  C CA  . ALA B 109  ? 0.4096 0.4249 0.2984 0.0240  -0.0046 -0.0209 107  ALA B CA  
9743  C C   . ALA B 109  ? 0.4159 0.4290 0.2953 0.0248  -0.0056 -0.0215 107  ALA B C   
9744  O O   . ALA B 109  ? 0.4076 0.4141 0.2844 0.0232  -0.0091 -0.0210 107  ALA B O   
9745  C CB  . ALA B 109  ? 0.4070 0.4192 0.2991 0.0279  -0.0053 -0.0247 107  ALA B CB  
9746  N N   . LEU B 110  ? 0.3535 0.3725 0.2277 0.0273  -0.0025 -0.0225 108  LEU B N   
9747  C CA  . LEU B 110  ? 0.3534 0.3706 0.2181 0.0283  -0.0031 -0.0231 108  LEU B CA  
9748  C C   . LEU B 110  ? 0.4032 0.4209 0.2643 0.0237  -0.0036 -0.0190 108  LEU B C   
9749  O O   . LEU B 110  ? 0.4468 0.4596 0.3011 0.0233  -0.0060 -0.0190 108  LEU B O   
9750  C CB  . LEU B 110  ? 0.3588 0.3830 0.2187 0.0322  0.0007  -0.0249 108  LEU B CB  
9751  C CG  . LEU B 110  ? 0.3627 0.3840 0.2234 0.0375  0.0004  -0.0296 108  LEU B CG  
9752  C CD1 . LEU B 110  ? 0.3791 0.4089 0.2368 0.0415  0.0047  -0.0311 108  LEU B CD1 
9753  C CD2 . LEU B 110  ? 0.4124 0.4239 0.2673 0.0392  -0.0037 -0.0326 108  LEU B CD2 
9754  N N   . LEU B 111  ? 0.3943 0.4173 0.2596 0.0200  -0.0016 -0.0153 109  LEU B N   
9755  C CA  . LEU B 111  ? 0.4448 0.4675 0.3066 0.0153  -0.0022 -0.0112 109  LEU B CA  
9756  C C   . LEU B 111  ? 0.4936 0.5070 0.3574 0.0129  -0.0068 -0.0102 109  LEU B C   
9757  O O   . LEU B 111  ? 0.4947 0.5056 0.3542 0.0096  -0.0082 -0.0071 109  LEU B O   
9758  C CB  . LEU B 111  ? 0.4433 0.4745 0.3086 0.0120  0.0013  -0.0077 109  LEU B CB  
9759  C CG  . LEU B 111  ? 0.4037 0.4455 0.2655 0.0136  0.0060  -0.0077 109  LEU B CG  
9760  C CD1 . LEU B 111  ? 0.4393 0.4899 0.3065 0.0104  0.0092  -0.0046 109  LEU B CD1 
9761  C CD2 . LEU B 111  ? 0.4256 0.4678 0.2774 0.0127  0.0063  -0.0063 109  LEU B CD2 
9762  N N   . ARG B 112  ? 0.4407 0.4492 0.3107 0.0145  -0.0092 -0.0125 110  ARG B N   
9763  C CA  . ARG B 112  ? 0.4881 0.4880 0.3596 0.0131  -0.0137 -0.0122 110  ARG B CA  
9764  C C   . ARG B 112  ? 0.5397 0.5337 0.4039 0.0147  -0.0168 -0.0140 110  ARG B C   
9765  O O   . ARG B 112  ? 0.5577 0.5452 0.4217 0.0134  -0.0208 -0.0133 110  ARG B O   
9766  C CB  . ARG B 112  ? 0.4428 0.4402 0.3232 0.0143  -0.0151 -0.0142 110  ARG B CB  
9767  C CG  . ARG B 112  ? 0.4851 0.4876 0.3725 0.0124  -0.0125 -0.0124 110  ARG B CG  
9768  C CD  . ARG B 112  ? 0.6200 0.6188 0.5157 0.0126  -0.0144 -0.0134 110  ARG B CD  
9769  N NE  . ARG B 112  ? 0.5651 0.5636 0.4639 0.0163  -0.0142 -0.0171 110  ARG B NE  
9770  C CZ  . ARG B 112  ? 0.6594 0.6626 0.5632 0.0176  -0.0115 -0.0180 110  ARG B CZ  
9771  N NH1 . ARG B 112  ? 0.6801 0.6892 0.5869 0.0156  -0.0087 -0.0156 110  ARG B NH1 
9772  N NH2 . ARG B 112  ? 0.7253 0.7268 0.6310 0.0210  -0.0118 -0.0213 110  ARG B NH2 
9773  N N   . ILE B 113  ? 0.4522 0.4485 0.3106 0.0177  -0.0153 -0.0163 111  ILE B N   
9774  C CA  . ILE B 113  ? 0.4935 0.4850 0.3435 0.0190  -0.0179 -0.0176 111  ILE B CA  
9775  C C   . ILE B 113  ? 0.5388 0.5326 0.3816 0.0161  -0.0168 -0.0139 111  ILE B C   
9776  O O   . ILE B 113  ? 0.5510 0.5522 0.3907 0.0160  -0.0127 -0.0128 111  ILE B O   
9777  C CB  . ILE B 113  ? 0.4985 0.4911 0.3445 0.0236  -0.0166 -0.0218 111  ILE B CB  
9778  C CG1 . ILE B 113  ? 0.4964 0.4862 0.3494 0.0261  -0.0177 -0.0252 111  ILE B CG1 
9779  C CG2 . ILE B 113  ? 0.4704 0.4579 0.3069 0.0248  -0.0194 -0.0232 111  ILE B CG2 
9780  C CD1 . ILE B 113  ? 0.5077 0.4982 0.3570 0.0307  -0.0162 -0.0293 111  ILE B CD1 
9781  N N   . PRO B 114  ? 0.5844 0.5722 0.4242 0.0138  -0.0205 -0.0118 112  PRO B N   
9782  C CA  . PRO B 114  ? 0.6091 0.5984 0.4425 0.0104  -0.0196 -0.0077 112  PRO B CA  
9783  C C   . PRO B 114  ? 0.5546 0.5460 0.3776 0.0118  -0.0183 -0.0082 112  PRO B C   
9784  O O   . PRO B 114  ? 0.6128 0.6096 0.4311 0.0095  -0.0153 -0.0051 112  PRO B O   
9785  C CB  . PRO B 114  ? 0.5125 0.4935 0.3460 0.0082  -0.0245 -0.0058 112  PRO B CB  
9786  C CG  . PRO B 114  ? 0.6114 0.5884 0.4533 0.0101  -0.0272 -0.0087 112  PRO B CG  
9787  C CD  . PRO B 114  ? 0.5674 0.5470 0.4100 0.0139  -0.0255 -0.0130 112  PRO B CD  
9788  N N   . ASP B 115  ? 0.6362 0.6236 0.4553 0.0153  -0.0205 -0.0119 113  ASP B N   
9789  C CA  . ASP B 115  ? 0.6665 0.6546 0.4748 0.0168  -0.0199 -0.0126 113  ASP B CA  
9790  C C   . ASP B 115  ? 0.5971 0.5929 0.4040 0.0200  -0.0152 -0.0150 113  ASP B C   
9791  O O   . ASP B 115  ? 0.5883 0.5836 0.3990 0.0236  -0.0151 -0.0190 113  ASP B O   
9792  C CB  . ASP B 115  ? 0.6670 0.6467 0.4714 0.0190  -0.0249 -0.0156 113  ASP B CB  
9793  C CG  . ASP B 115  ? 0.7082 0.6885 0.5018 0.0215  -0.0243 -0.0176 113  ASP B CG  
9794  O OD1 . ASP B 115  ? 0.8084 0.7920 0.5946 0.0198  -0.0223 -0.0147 113  ASP B OD1 
9795  O OD2 . ASP B 115  ? 0.7160 0.6931 0.5082 0.0252  -0.0258 -0.0220 113  ASP B OD2 
9796  N N   . THR B 116  ? 0.5999 0.6029 0.4011 0.0188  -0.0114 -0.0126 114  THR B N   
9797  C CA  . THR B 116  ? 0.6555 0.6672 0.4552 0.0220  -0.0064 -0.0145 114  THR B CA  
9798  C C   . THR B 116  ? 0.6472 0.6557 0.4423 0.0275  -0.0074 -0.0198 114  THR B C   
9799  O O   . THR B 116  ? 0.6293 0.6412 0.4275 0.0313  -0.0052 -0.0231 114  THR B O   
9800  C CB  . THR B 116  ? 0.7332 0.7527 0.5260 0.0196  -0.0027 -0.0108 114  THR B CB  
9801  O OG1 . THR B 116  ? 0.7942 0.8169 0.5919 0.0144  -0.0016 -0.0060 114  THR B OG1 
9802  C CG2 . THR B 116  ? 0.7400 0.7693 0.5307 0.0234  0.0024  -0.0130 114  THR B CG2 
9803  N N   . ALA B 117  ? 0.6591 0.6606 0.4462 0.0280  -0.0110 -0.0208 115  ALA B N   
9804  C CA  . ALA B 117  ? 0.6688 0.6668 0.4502 0.0330  -0.0122 -0.0259 115  ALA B CA  
9805  C C   . ALA B 117  ? 0.5940 0.5862 0.3829 0.0353  -0.0149 -0.0298 115  ALA B C   
9806  O O   . ALA B 117  ? 0.6483 0.6405 0.4361 0.0398  -0.0139 -0.0340 115  ALA B O   
9807  C CB  . ALA B 117  ? 0.6810 0.6727 0.4524 0.0327  -0.0158 -0.0260 115  ALA B CB  
9808  N N   . THR B 118  ? 0.5863 0.5733 0.3825 0.0324  -0.0184 -0.0283 116  THR B N   
9809  C CA  . THR B 118  ? 0.5728 0.5548 0.3765 0.0341  -0.0209 -0.0315 116  THR B CA  
9810  C C   . THR B 118  ? 0.5522 0.5402 0.3633 0.0356  -0.0170 -0.0322 116  THR B C   
9811  O O   . THR B 118  ? 0.5854 0.5711 0.3989 0.0390  -0.0173 -0.0361 116  THR B O   
9812  C CB  . THR B 118  ? 0.5563 0.5325 0.3661 0.0306  -0.0252 -0.0295 116  THR B CB  
9813  O OG1 . THR B 118  ? 0.6451 0.6154 0.4477 0.0297  -0.0293 -0.0291 116  THR B OG1 
9814  C CG2 . THR B 118  ? 0.5373 0.5090 0.3551 0.0319  -0.0276 -0.0325 116  THR B CG2 
9815  N N   . ARG B 119  ? 0.5770 0.5725 0.3918 0.0330  -0.0134 -0.0285 117  ARG B N   
9816  C CA  . ARG B 119  ? 0.5517 0.5539 0.3734 0.0343  -0.0095 -0.0288 117  ARG B CA  
9817  C C   . ARG B 119  ? 0.5591 0.5663 0.3757 0.0392  -0.0060 -0.0319 117  ARG B C   
9818  O O   . ARG B 119  ? 0.5359 0.5430 0.3561 0.0428  -0.0053 -0.0352 117  ARG B O   
9819  C CB  . ARG B 119  ? 0.5069 0.5164 0.3327 0.0300  -0.0066 -0.0239 117  ARG B CB  
9820  C CG  . ARG B 119  ? 0.4108 0.4278 0.2443 0.0309  -0.0028 -0.0239 117  ARG B CG  
9821  C CD  . ARG B 119  ? 0.4987 0.5240 0.3334 0.0269  0.0005  -0.0192 117  ARG B CD  
9822  N NE  . ARG B 119  ? 0.5295 0.5501 0.3656 0.0218  -0.0023 -0.0155 117  ARG B NE  
9823  C CZ  . ARG B 119  ? 0.6245 0.6476 0.4561 0.0179  -0.0015 -0.0115 117  ARG B CZ  
9824  N NH1 . ARG B 119  ? 0.5433 0.5743 0.3689 0.0181  0.0023  -0.0104 117  ARG B NH1 
9825  N NH2 . ARG B 119  ? 0.5893 0.6069 0.4224 0.0137  -0.0045 -0.0084 117  ARG B NH2 
9826  N N   . ASP B 120  ? 0.5559 0.5675 0.3636 0.0396  -0.0039 -0.0310 118  ASP B N   
9827  C CA  . ASP B 120  ? 0.5686 0.5856 0.3706 0.0445  -0.0004 -0.0340 118  ASP B CA  
9828  C C   . ASP B 120  ? 0.5907 0.5997 0.3888 0.0494  -0.0032 -0.0395 118  ASP B C   
9829  O O   . ASP B 120  ? 0.5414 0.5529 0.3385 0.0543  -0.0009 -0.0428 118  ASP B O   
9830  C CB  . ASP B 120  ? 0.5953 0.6180 0.3879 0.0436  0.0021  -0.0318 118  ASP B CB  
9831  C CG  . ASP B 120  ? 0.6851 0.7177 0.4812 0.0393  0.0058  -0.0266 118  ASP B CG  
9832  O OD1 . ASP B 120  ? 0.7159 0.7510 0.5215 0.0374  0.0067  -0.0251 118  ASP B OD1 
9833  O OD2 . ASP B 120  ? 0.7392 0.7768 0.5282 0.0376  0.0079  -0.0241 118  ASP B OD2 
9834  N N   . ALA B 121  ? 0.5786 0.5776 0.3742 0.0482  -0.0083 -0.0404 119  ALA B N   
9835  C CA  . ALA B 121  ? 0.6366 0.6271 0.4286 0.0521  -0.0115 -0.0455 119  ALA B CA  
9836  C C   . ALA B 121  ? 0.6041 0.5917 0.4050 0.0536  -0.0122 -0.0477 119  ALA B C   
9837  O O   . ALA B 121  ? 0.5843 0.5697 0.3832 0.0582  -0.0119 -0.0519 119  ALA B O   
9838  C CB  . ALA B 121  ? 0.6287 0.6100 0.4165 0.0500  -0.0170 -0.0457 119  ALA B CB  
9839  N N   . LEU B 122  ? 0.5205 0.5080 0.3312 0.0497  -0.0133 -0.0449 120  LEU B N   
9840  C CA  . LEU B 122  ? 0.5888 0.5741 0.4081 0.0507  -0.0138 -0.0465 120  LEU B CA  
9841  C C   . LEU B 122  ? 0.5447 0.5374 0.3657 0.0545  -0.0090 -0.0477 120  LEU B C   
9842  O O   . LEU B 122  ? 0.5852 0.5746 0.4081 0.0579  -0.0094 -0.0510 120  LEU B O   
9843  C CB  . LEU B 122  ? 0.5487 0.5341 0.3777 0.0459  -0.0151 -0.0429 120  LEU B CB  
9844  C CG  . LEU B 122  ? 0.5745 0.5566 0.4126 0.0463  -0.0163 -0.0443 120  LEU B CG  
9845  C CD1 . LEU B 122  ? 0.6503 0.6221 0.4868 0.0471  -0.0213 -0.0476 120  LEU B CD1 
9846  C CD2 . LEU B 122  ? 0.5140 0.4987 0.3614 0.0420  -0.0161 -0.0405 120  LEU B CD2 
9847  N N   . ILE B 123  ? 0.5222 0.5250 0.3422 0.0538  -0.0046 -0.0449 121  ILE B N   
9848  C CA  . ILE B 123  ? 0.5405 0.5519 0.3624 0.0573  0.0001  -0.0456 121  ILE B CA  
9849  C C   . ILE B 123  ? 0.6723 0.6819 0.4862 0.0636  0.0008  -0.0504 121  ILE B C   
9850  O O   . ILE B 123  ? 0.6225 0.6319 0.4388 0.0678  0.0018  -0.0532 121  ILE B O   
9851  C CB  . ILE B 123  ? 0.4512 0.4742 0.2733 0.0547  0.0044  -0.0413 121  ILE B CB  
9852  C CG1 . ILE B 123  ? 0.3874 0.4118 0.2183 0.0488  0.0039  -0.0369 121  ILE B CG1 
9853  C CG2 . ILE B 123  ? 0.4639 0.4971 0.2865 0.0589  0.0095  -0.0424 121  ILE B CG2 
9854  C CD1 . ILE B 123  ? 0.4336 0.4676 0.2637 0.0450  0.0072  -0.0323 121  ILE B CD1 
9855  N N   . ARG B 124  ? 0.5487 0.5566 0.3525 0.0646  0.0001  -0.0514 122  ARG B N   
9856  C CA  . ARG B 124  ? 0.6132 0.6198 0.4083 0.0708  0.0010  -0.0560 122  ARG B CA  
9857  C C   . ARG B 124  ? 0.6838 0.6781 0.4779 0.0735  -0.0035 -0.0605 122  ARG B C   
9858  O O   . ARG B 124  ? 0.7301 0.7227 0.5215 0.0790  -0.0026 -0.0645 122  ARG B O   
9859  C CB  . ARG B 124  ? 0.6926 0.7009 0.4770 0.0708  0.0015  -0.0556 122  ARG B CB  
9860  N N   . ASP B 125  ? 0.6887 0.6741 0.4847 0.0696  -0.0083 -0.0600 123  ASP B N   
9861  C CA  . ASP B 125  ? 0.7366 0.7100 0.5301 0.0714  -0.0131 -0.0642 123  ASP B CA  
9862  C C   . ASP B 125  ? 0.6235 0.5921 0.4267 0.0702  -0.0151 -0.0645 123  ASP B C   
9863  O O   . ASP B 125  ? 0.7207 0.6800 0.5222 0.0721  -0.0185 -0.0682 123  ASP B O   
9864  C CB  . ASP B 125  ? 0.7793 0.7458 0.5676 0.0682  -0.0176 -0.0638 123  ASP B CB  
9865  C CG  . ASP B 125  ? 0.8021 0.7729 0.5803 0.0689  -0.0158 -0.0632 123  ASP B CG  
9866  O OD1 . ASP B 125  ? 0.8102 0.7857 0.5823 0.0736  -0.0123 -0.0653 123  ASP B OD1 
9867  O OD2 . ASP B 125  ? 0.8635 0.8332 0.6398 0.0649  -0.0180 -0.0606 123  ASP B OD2 
9868  N N   . LYS B 126  ? 0.6567 0.6312 0.4697 0.0670  -0.0133 -0.0609 124  LYS B N   
9869  C CA  . LYS B 126  ? 0.6539 0.6238 0.4758 0.0659  -0.0153 -0.0611 124  LYS B CA  
9870  C C   . LYS B 126  ? 0.6612 0.6391 0.4910 0.0667  -0.0112 -0.0595 124  LYS B C   
9871  O O   . LYS B 126  ? 0.7206 0.6952 0.5540 0.0690  -0.0115 -0.0615 124  LYS B O   
9872  C CB  . LYS B 126  ? 0.6937 0.6597 0.5211 0.0601  -0.0190 -0.0585 124  LYS B CB  
9873  N N   . ILE B 127  ? 0.6137 0.6018 0.4462 0.0646  -0.0075 -0.0557 125  ILE B N   
9874  C CA  . ILE B 127  ? 0.5859 0.5818 0.4265 0.0647  -0.0040 -0.0538 125  ILE B CA  
9875  C C   . ILE B 127  ? 0.6026 0.6037 0.4398 0.0707  -0.0004 -0.0564 125  ILE B C   
9876  O O   . ILE B 127  ? 0.6006 0.6027 0.4430 0.0731  0.0007  -0.0574 125  ILE B O   
9877  C CB  . ILE B 127  ? 0.4891 0.4938 0.3337 0.0599  -0.0017 -0.0488 125  ILE B CB  
9878  C CG1 . ILE B 127  ? 0.5297 0.5288 0.3767 0.0544  -0.0055 -0.0464 125  ILE B CG1 
9879  C CG2 . ILE B 127  ? 0.4880 0.5001 0.3416 0.0595  0.0014  -0.0469 125  ILE B CG2 
9880  C CD1 . ILE B 127  ? 0.5534 0.5450 0.4074 0.0530  -0.0089 -0.0471 125  ILE B CD1 
9881  N N   . ALA B 128  ? 0.5463 0.5514 0.3748 0.0734  0.0017  -0.0574 126  ALA B N   
9882  C CA  . ALA B 128  ? 0.5576 0.5692 0.3828 0.0795  0.0056  -0.0598 126  ALA B CA  
9883  C C   . ALA B 128  ? 0.6655 0.6681 0.4883 0.0850  0.0036  -0.0646 126  ALA B C   
9884  O O   . ALA B 128  ? 0.6805 0.6876 0.5032 0.0902  0.0064  -0.0665 126  ALA B O   
9885  C CB  . ALA B 128  ? 0.5923 0.6093 0.4078 0.0814  0.0079  -0.0601 126  ALA B CB  
9886  N N   . ASP B 129  ? 0.7399 0.7301 0.5608 0.0838  -0.0014 -0.0667 127  ASP B N   
9887  C CA  . ASP B 129  ? 0.8178 0.7978 0.6370 0.0878  -0.0040 -0.0710 127  ASP B CA  
9888  C C   . ASP B 129  ? 0.8132 0.7908 0.6426 0.0858  -0.0051 -0.0698 127  ASP B C   
9889  O O   . ASP B 129  ? 0.9426 0.9098 0.7717 0.0869  -0.0085 -0.0724 127  ASP B O   
9890  C CB  . ASP B 129  ? 0.8211 0.7890 0.6331 0.0871  -0.0090 -0.0738 127  ASP B CB  
9891  N N   . GLY B 130  ? 0.8088 0.7957 0.6468 0.0827  -0.0024 -0.0657 128  GLY B N   
9892  C CA  . GLY B 130  ? 0.7518 0.7374 0.5993 0.0808  -0.0030 -0.0643 128  GLY B CA  
9893  C C   . GLY B 130  ? 0.8187 0.7961 0.6708 0.0754  -0.0074 -0.0631 128  GLY B C   
9894  O O   . GLY B 130  ? 0.7812 0.7590 0.6419 0.0730  -0.0076 -0.0613 128  GLY B O   
9895  N N   . ASN B 131  ? 0.9084 0.8788 0.7552 0.0735  -0.0108 -0.0641 129  ASN B N   
9896  C CA  . ASN B 131  ? 0.8749 0.8380 0.7261 0.0687  -0.0152 -0.0632 129  ASN B CA  
9897  C C   . ASN B 131  ? 0.8414 0.8108 0.6995 0.0632  -0.0144 -0.0585 129  ASN B C   
9898  O O   . ASN B 131  ? 0.9230 0.8892 0.7807 0.0595  -0.0173 -0.0574 129  ASN B O   
9899  C CB  . ASN B 131  ? 0.8996 0.8538 0.7428 0.0685  -0.0192 -0.0657 129  ASN B CB  
9900  N N   . TRP B 132  ? 0.7462 0.7243 0.6105 0.0628  -0.0108 -0.0560 130  TRP B N   
9901  C CA  . TRP B 132  ? 0.6530 0.6371 0.5231 0.0579  -0.0098 -0.0516 130  TRP B CA  
9902  C C   . TRP B 132  ? 0.6708 0.6505 0.5492 0.0540  -0.0126 -0.0502 130  TRP B C   
9903  O O   . TRP B 132  ? 0.7392 0.7195 0.6204 0.0497  -0.0138 -0.0474 130  TRP B O   
9904  C CB  . TRP B 132  ? 0.6241 0.6195 0.4973 0.0586  -0.0049 -0.0494 130  TRP B CB  
9905  C CG  . TRP B 132  ? 0.5454 0.5426 0.4248 0.0608  -0.0034 -0.0499 130  TRP B CG  
9906  C CD1 . TRP B 132  ? 0.5200 0.5186 0.3970 0.0663  -0.0015 -0.0526 130  TRP B CD1 
9907  C CD2 . TRP B 132  ? 0.5079 0.5058 0.3965 0.0577  -0.0037 -0.0476 130  TRP B CD2 
9908  N NE1 . TRP B 132  ? 0.4987 0.4986 0.3829 0.0667  -0.0007 -0.0520 130  TRP B NE1 
9909  C CE2 . TRP B 132  ? 0.4655 0.4651 0.3569 0.0614  -0.0019 -0.0490 130  TRP B CE2 
9910  C CE3 . TRP B 132  ? 0.4672 0.4643 0.3616 0.0525  -0.0053 -0.0447 130  TRP B CE3 
9911  C CZ2 . TRP B 132  ? 0.4124 0.4130 0.3121 0.0597  -0.0018 -0.0474 130  TRP B CZ2 
9912  C CZ3 . TRP B 132  ? 0.4193 0.4176 0.3221 0.0510  -0.0050 -0.0433 130  TRP B CZ3 
9913  C CH2 . TRP B 132  ? 0.3975 0.3975 0.3027 0.0545  -0.0032 -0.0445 130  TRP B CH2 
9914  N N   . LYS B 133  ? 0.6958 0.6710 0.5778 0.0556  -0.0135 -0.0519 131  LYS B N   
9915  C CA  . LYS B 133  ? 0.7598 0.7315 0.6497 0.0520  -0.0159 -0.0506 131  LYS B CA  
9916  C C   . LYS B 133  ? 0.8457 0.8104 0.7341 0.0490  -0.0203 -0.0509 131  LYS B C   
9917  O O   . LYS B 133  ? 0.8447 0.8096 0.7390 0.0450  -0.0218 -0.0485 131  LYS B O   
9918  C CB  . LYS B 133  ? 0.6564 0.6239 0.5493 0.0544  -0.0162 -0.0526 131  LYS B CB  
9919  N N   . SER B 134  ? 0.9270 0.8859 0.8076 0.0510  -0.0225 -0.0538 132  SER B N   
9920  C CA  . SER B 134  ? 0.9398 0.8918 0.8185 0.0485  -0.0270 -0.0545 132  SER B CA  
9921  C C   . SER B 134  ? 0.8908 0.8452 0.7639 0.0473  -0.0272 -0.0533 132  SER B C   
9922  O O   . SER B 134  ? 1.0163 0.9656 0.8824 0.0480  -0.0299 -0.0554 132  SER B O   
9923  C CB  . SER B 134  ? 0.8029 0.7459 0.6763 0.0510  -0.0299 -0.0587 132  SER B CB  
9924  N N   . HIS B 135  ? 0.8392 0.8011 0.7150 0.0453  -0.0246 -0.0498 133  HIS B N   
9925  C CA  . HIS B 135  ? 0.8678 0.8319 0.7379 0.0440  -0.0247 -0.0483 133  HIS B CA  
9926  C C   . HIS B 135  ? 0.8686 0.8394 0.7436 0.0406  -0.0226 -0.0440 133  HIS B C   
9927  O O   . HIS B 135  ? 0.8816 0.8535 0.7530 0.0386  -0.0232 -0.0420 133  HIS B O   
9928  C CB  . HIS B 135  ? 0.7440 0.7105 0.6051 0.0479  -0.0221 -0.0501 133  HIS B CB  
9929  N N   . LEU B 136  ? 0.8310 0.8059 0.7137 0.0399  -0.0204 -0.0424 134  LEU B N   
9930  C CA  . LEU B 136  ? 0.7130 0.6937 0.6005 0.0366  -0.0187 -0.0385 134  LEU B CA  
9931  C C   . LEU B 136  ? 0.6861 0.6666 0.5831 0.0349  -0.0190 -0.0374 134  LEU B C   
9932  O O   . LEU B 136  ? 0.7249 0.7090 0.6265 0.0320  -0.0180 -0.0344 134  LEU B O   
9933  C CB  . LEU B 136  ? 0.6224 0.6116 0.5076 0.0377  -0.0140 -0.0370 134  LEU B CB  
9934  C CG  . LEU B 136  ? 0.6061 0.5977 0.4821 0.0387  -0.0128 -0.0371 134  LEU B CG  
9935  C CD1 . LEU B 136  ? 0.5204 0.5214 0.3955 0.0401  -0.0079 -0.0359 134  LEU B CD1 
9936  C CD2 . LEU B 136  ? 0.6339 0.6239 0.5074 0.0349  -0.0149 -0.0343 134  LEU B CD2 
9937  N N   . ARG B 140  ? 0.5422 0.5197 0.4757 0.0243  -0.0240 -0.0312 138  ARG B N   
9938  C CA  . ARG B 140  ? 0.6490 0.6325 0.5838 0.0235  -0.0206 -0.0288 138  ARG B CA  
9939  C C   . ARG B 140  ? 0.6513 0.6386 0.5828 0.0262  -0.0174 -0.0298 138  ARG B C   
9940  O O   . ARG B 140  ? 0.4811 0.4679 0.4061 0.0280  -0.0172 -0.0312 138  ARG B O   
9941  C CB  . ARG B 140  ? 0.6010 0.5854 0.5326 0.0213  -0.0211 -0.0263 138  ARG B CB  
9942  N N   . SER B 141  ? 0.4725 0.4641 0.4086 0.0265  -0.0147 -0.0292 139  SER B N   
9943  C CA  . SER B 141  ? 0.3811 0.3772 0.3150 0.0293  -0.0116 -0.0301 139  SER B CA  
9944  C C   . SER B 141  ? 0.4368 0.4380 0.3654 0.0290  -0.0095 -0.0286 139  SER B C   
9945  O O   . SER B 141  ? 0.4072 0.4104 0.3361 0.0259  -0.0094 -0.0259 139  SER B O   
9946  C CB  . SER B 141  ? 0.4351 0.4355 0.3754 0.0294  -0.0093 -0.0291 139  SER B CB  
9947  O OG  . SER B 141  ? 0.4642 0.4702 0.4027 0.0321  -0.0061 -0.0296 139  SER B OG  
9948  N N   . LEU B 142  ? 0.3770 0.3800 0.3003 0.0323  -0.0079 -0.0305 140  LEU B N   
9949  C CA  . LEU B 142  ? 0.3430 0.3525 0.2616 0.0322  -0.0052 -0.0290 140  LEU B CA  
9950  C C   . LEU B 142  ? 0.3365 0.3540 0.2597 0.0304  -0.0022 -0.0263 140  LEU B C   
9951  O O   . LEU B 142  ? 0.3132 0.3363 0.2338 0.0286  -0.0003 -0.0240 140  LEU B O   
9952  C CB  . LEU B 142  ? 0.3675 0.3784 0.2806 0.0368  -0.0036 -0.0319 140  LEU B CB  
9953  C CG  . LEU B 142  ? 0.4194 0.4339 0.3250 0.0371  -0.0021 -0.0313 140  LEU B CG  
9954  C CD1 . LEU B 142  ? 0.4551 0.4621 0.3553 0.0365  -0.0056 -0.0324 140  LEU B CD1 
9955  C CD2 . LEU B 142  ? 0.4640 0.4830 0.3660 0.0418  0.0007  -0.0336 140  LEU B CD2 
9956  N N   . PHE B 143  ? 0.2904 0.3087 0.2201 0.0306  -0.0017 -0.0263 141  PHE B N   
9957  C CA  . PHE B 143  ? 0.2822 0.3086 0.2162 0.0297  0.0013  -0.0243 141  PHE B CA  
9958  C C   . PHE B 143  ? 0.3130 0.3391 0.2525 0.0254  0.0004  -0.0216 141  PHE B C   
9959  O O   . PHE B 143  ? 0.2942 0.3255 0.2382 0.0246  0.0023  -0.0202 141  PHE B O   
9960  C CB  . PHE B 143  ? 0.2682 0.2963 0.2050 0.0336  0.0027  -0.0264 141  PHE B CB  
9961  C CG  . PHE B 143  ? 0.2729 0.3003 0.2040 0.0383  0.0034  -0.0294 141  PHE B CG  
9962  C CD1 . PHE B 143  ? 0.2727 0.3065 0.1986 0.0395  0.0058  -0.0291 141  PHE B CD1 
9963  C CD2 . PHE B 143  ? 0.2855 0.3057 0.2159 0.0413  0.0014  -0.0324 141  PHE B CD2 
9964  C CE1 . PHE B 143  ? 0.3014 0.3343 0.2215 0.0441  0.0064  -0.0321 141  PHE B CE1 
9965  C CE2 . PHE B 143  ? 0.2754 0.2940 0.1999 0.0457  0.0017  -0.0353 141  PHE B CE2 
9966  C CZ  . PHE B 143  ? 0.2925 0.3174 0.2118 0.0474  0.0042  -0.0353 141  PHE B CZ  
9967  N N   . VAL B 144  ? 0.3273 0.3475 0.2660 0.0228  -0.0024 -0.0208 142  VAL B N   
9968  C CA  A VAL B 144  ? 0.3332 0.3521 0.2765 0.0192  -0.0035 -0.0185 142  VAL B CA  
9969  C CA  B VAL B 144  ? 0.3332 0.3522 0.2767 0.0192  -0.0035 -0.0185 142  VAL B CA  
9970  C C   . VAL B 144  ? 0.2998 0.3258 0.2440 0.0164  -0.0010 -0.0155 142  VAL B C   
9971  O O   . VAL B 144  ? 0.3490 0.3767 0.2983 0.0146  -0.0007 -0.0142 142  VAL B O   
9972  C CB  A VAL B 144  ? 0.3424 0.3546 0.2834 0.0172  -0.0069 -0.0180 142  VAL B CB  
9973  C CB  B VAL B 144  ? 0.3432 0.3552 0.2847 0.0173  -0.0069 -0.0181 142  VAL B CB  
9974  C CG1 A VAL B 144  ? 0.3527 0.3637 0.2975 0.0137  -0.0079 -0.0155 142  VAL B CG1 
9975  C CG1 B VAL B 144  ? 0.4105 0.4162 0.3528 0.0195  -0.0095 -0.0208 142  VAL B CG1 
9976  C CG2 A VAL B 144  ? 0.4136 0.4192 0.3552 0.0194  -0.0095 -0.0208 142  VAL B CG2 
9977  C CG2 B VAL B 144  ? 0.3499 0.3624 0.2843 0.0163  -0.0069 -0.0170 142  VAL B CG2 
9978  N N   . ASN B 145  ? 0.3147 0.3451 0.2536 0.0160  0.0006  -0.0145 143  ASN B N   
9979  C CA  . ASN B 145  ? 0.3217 0.3590 0.2609 0.0127  0.0028  -0.0114 143  ASN B CA  
9980  C C   . ASN B 145  ? 0.3343 0.3811 0.2744 0.0148  0.0064  -0.0117 143  ASN B C   
9981  O O   . ASN B 145  ? 0.3164 0.3703 0.2550 0.0125  0.0086  -0.0094 143  ASN B O   
9982  C CB  . ASN B 145  ? 0.3402 0.3767 0.2731 0.0099  0.0023  -0.0093 143  ASN B CB  
9983  C CG  . ASN B 145  ? 0.4222 0.4509 0.3552 0.0069  -0.0010 -0.0079 143  ASN B CG  
9984  O OD1 . ASN B 145  ? 0.4842 0.5116 0.4220 0.0048  -0.0018 -0.0067 143  ASN B OD1 
9985  N ND2 . ASN B 145  ? 0.4048 0.4284 0.3324 0.0069  -0.0031 -0.0080 143  ASN B ND2 
9986  N N   . ALA B 146  ? 0.3127 0.3598 0.2552 0.0190  0.0070  -0.0144 144  ALA B N   
9987  C CA  . ALA B 146  ? 0.3144 0.3704 0.2573 0.0217  0.0103  -0.0150 144  ALA B CA  
9988  C C   . ALA B 146  ? 0.2611 0.3247 0.2093 0.0192  0.0122  -0.0126 144  ALA B C   
9989  O O   . ALA B 146  ? 0.3186 0.3917 0.2668 0.0202  0.0152  -0.0120 144  ALA B O   
9990  C CB  . ALA B 146  ? 0.3052 0.3585 0.2491 0.0270  0.0101  -0.0185 144  ALA B CB  
9991  N N   . ALA B 147  ? 0.3163 0.3765 0.2691 0.0162  0.0106  -0.0113 145  ALA B N   
9992  C CA  . ALA B 147  ? 0.2830 0.3502 0.2402 0.0134  0.0122  -0.0090 145  ALA B CA  
9993  C C   . ALA B 147  ? 0.3362 0.4092 0.2901 0.0094  0.0136  -0.0059 145  ALA B C   
9994  O O   . ALA B 147  ? 0.3121 0.3948 0.2679 0.0084  0.0161  -0.0044 145  ALA B O   
9995  C CB  . ALA B 147  ? 0.3111 0.3726 0.2728 0.0108  0.0100  -0.0082 145  ALA B CB  
9996  N N   . THR B 148  ? 0.3203 0.3878 0.2693 0.0071  0.0120  -0.0050 146  THR B N   
9997  C CA  . THR B 148  ? 0.3124 0.3846 0.2576 0.0031  0.0131  -0.0019 146  THR B CA  
9998  C C   . THR B 148  ? 0.3290 0.4105 0.2711 0.0056  0.0163  -0.0024 146  THR B C   
9999  O O   . THR B 148  ? 0.3640 0.4552 0.3068 0.0034  0.0189  -0.0002 146  THR B O   
10000 C CB  . THR B 148  ? 0.4018 0.4652 0.3420 0.0007  0.0104  -0.0009 146  THR B CB  
10001 O OG1 . THR B 148  ? 0.4242 0.4800 0.3677 -0.0014 0.0076  -0.0005 146  THR B OG1 
10002 C CG2 . THR B 148  ? 0.4139 0.4816 0.3494 -0.0037 0.0115  0.0025  146  THR B CG2 
10003 N N   . TRP B 149  ? 0.3010 0.3800 0.2396 0.0103  0.0163  -0.0053 147  TRP B N   
10004 C CA  . TRP B 149  ? 0.2831 0.3707 0.2184 0.0134  0.0194  -0.0061 147  TRP B CA  
10005 C C   . TRP B 149  ? 0.2893 0.3864 0.2298 0.0161  0.0221  -0.0069 147  TRP B C   
10006 O O   . TRP B 149  ? 0.3040 0.4117 0.2434 0.0169  0.0252  -0.0061 147  TRP B O   
10007 C CB  . TRP B 149  ? 0.3082 0.3901 0.2383 0.0181  0.0185  -0.0094 147  TRP B CB  
10008 C CG  . TRP B 149  ? 0.3111 0.3853 0.2355 0.0155  0.0161  -0.0085 147  TRP B CG  
10009 C CD1 . TRP B 149  ? 0.3023 0.3654 0.2257 0.0159  0.0126  -0.0100 147  TRP B CD1 
10010 C CD2 . TRP B 149  ? 0.3538 0.4312 0.2729 0.0119  0.0170  -0.0057 147  TRP B CD2 
10011 N NE1 . TRP B 149  ? 0.3188 0.3778 0.2364 0.0131  0.0111  -0.0084 147  TRP B NE1 
10012 C CE2 . TRP B 149  ? 0.3499 0.4171 0.2645 0.0106  0.0138  -0.0057 147  TRP B CE2 
10013 C CE3 . TRP B 149  ? 0.3798 0.4679 0.2973 0.0096  0.0203  -0.0030 147  TRP B CE3 
10014 C CZ2 . TRP B 149  ? 0.3924 0.4592 0.3008 0.0072  0.0136  -0.0031 147  TRP B CZ2 
10015 C CZ3 . TRP B 149  ? 0.3992 0.4870 0.3104 0.0059  0.0202  -0.0004 147  TRP B CZ3 
10016 C CH2 . TRP B 149  ? 0.4208 0.4976 0.3274 0.0048  0.0168  -0.0004 147  TRP B CH2 
10017 N N   . GLY B 150  ? 0.2608 0.3544 0.2068 0.0176  0.0209  -0.0082 148  GLY B N   
10018 C CA  . GLY B 150  ? 0.3011 0.4036 0.2525 0.0197  0.0231  -0.0085 148  GLY B CA  
10019 C C   . GLY B 150  ? 0.3267 0.4391 0.2806 0.0148  0.0249  -0.0049 148  GLY B C   
10020 O O   . GLY B 150  ? 0.3195 0.4433 0.2751 0.0163  0.0278  -0.0045 148  GLY B O   
10021 N N   . LEU B 151  ? 0.3287 0.4369 0.2829 0.0090  0.0231  -0.0022 149  LEU B N   
10022 C CA  A LEU B 151  ? 0.3589 0.4755 0.3147 0.0036  0.0245  0.0015  149  LEU B CA  
10023 C CA  B LEU B 151  ? 0.3590 0.4756 0.3148 0.0036  0.0245  0.0015  149  LEU B CA  
10024 C C   . LEU B 151  ? 0.3822 0.5074 0.3332 0.0027  0.0272  0.0030  149  LEU B C   
10025 O O   . LEU B 151  ? 0.3992 0.5365 0.3524 0.0014  0.0299  0.0047  149  LEU B O   
10026 C CB  A LEU B 151  ? 0.3971 0.5056 0.3528 -0.0023 0.0218  0.0039  149  LEU B CB  
10027 C CB  B LEU B 151  ? 0.3971 0.5054 0.3528 -0.0022 0.0217  0.0038  149  LEU B CB  
10028 C CG  A LEU B 151  ? 0.4120 0.5209 0.3738 -0.0049 0.0209  0.0050  149  LEU B CG  
10029 C CG  B LEU B 151  ? 0.4509 0.5641 0.4102 -0.0078 0.0219  0.0070  149  LEU B CG  
10030 C CD1 A LEU B 151  ? 0.4663 0.5658 0.4268 -0.0101 0.0179  0.0069  149  LEU B CD1 
10031 C CD1 B LEU B 151  ? 0.4370 0.5593 0.4026 -0.0056 0.0237  0.0062  149  LEU B CD1 
10032 C CD2 A LEU B 151  ? 0.4394 0.5617 0.4042 -0.0072 0.0236  0.0071  149  LEU B CD2 
10033 C CD2 B LEU B 151  ? 0.4665 0.5684 0.4266 -0.0111 0.0185  0.0077  149  LEU B CD2 
10034 N N   . VAL B 152  ? 0.3355 0.4552 0.2801 0.0035  0.0265  0.0023  150  VAL B N   
10035 C CA  . VAL B 152  ? 0.3742 0.5016 0.3136 0.0027  0.0290  0.0037  150  VAL B CA  
10036 C C   . VAL B 152  ? 0.3875 0.5263 0.3278 0.0081  0.0325  0.0018  150  VAL B C   
10037 O O   . VAL B 152  ? 0.4399 0.5910 0.3801 0.0066  0.0356  0.0038  150  VAL B O   
10038 C CB  . VAL B 152  ? 0.3374 0.4555 0.2694 0.0033  0.0273  0.0029  150  VAL B CB  
10039 C CG1 . VAL B 152  ? 0.4395 0.5658 0.3656 0.0039  0.0302  0.0037  150  VAL B CG1 
10040 C CG2 . VAL B 152  ? 0.4269 0.5356 0.3574 -0.0025 0.0242  0.0055  150  VAL B CG2 
10041 N N   . VAL B 153  ? 0.3531 0.4881 0.2945 0.0145  0.0321  -0.0021 151  VAL B N   
10042 C CA  . VAL B 153  ? 0.3433 0.4872 0.2841 0.0207  0.0350  -0.0045 151  VAL B CA  
10043 C C   . VAL B 153  ? 0.3269 0.4815 0.2748 0.0218  0.0370  -0.0041 151  VAL B C   
10044 O O   . VAL B 153  ? 0.3655 0.5331 0.3138 0.0238  0.0403  -0.0038 151  VAL B O   
10045 C CB  . VAL B 153  ? 0.3450 0.4791 0.2831 0.0271  0.0334  -0.0089 151  VAL B CB  
10046 C CG1 . VAL B 153  ? 0.3606 0.5027 0.2984 0.0342  0.0361  -0.0118 151  VAL B CG1 
10047 C CG2 . VAL B 153  ? 0.3184 0.4438 0.2492 0.0263  0.0317  -0.0093 151  VAL B CG2 
10048 N N   . THR B 154  ? 0.3273 0.4771 0.2808 0.0207  0.0349  -0.0041 152  THR B N   
10049 C CA  . THR B 154  ? 0.3631 0.5216 0.3233 0.0224  0.0362  -0.0041 152  THR B CA  
10050 C C   . THR B 154  ? 0.3839 0.5480 0.3489 0.0158  0.0362  -0.0004 152  THR B C   
10051 O O   . THR B 154  ? 0.4444 0.6186 0.4146 0.0165  0.0378  0.0001  152  THR B O   
10052 C CB  . THR B 154  ? 0.3721 0.5215 0.3353 0.0267  0.0341  -0.0071 152  THR B CB  
10053 O OG1 . THR B 154  ? 0.3728 0.5124 0.3380 0.0221  0.0310  -0.0059 152  THR B OG1 
10054 C CG2 . THR B 154  ? 0.4251 0.5662 0.3832 0.0325  0.0333  -0.0108 152  THR B CG2 
10055 N N   . GLY B 155  ? 0.3213 0.4786 0.2846 0.0095  0.0342  0.0021  153  GLY B N   
10056 C CA  . GLY B 155  ? 0.3458 0.5058 0.3132 0.0031  0.0335  0.0053  153  GLY B CA  
10057 C C   . GLY B 155  ? 0.4389 0.5920 0.4114 0.0032  0.0311  0.0044  153  GLY B C   
10058 O O   . GLY B 155  ? 0.4544 0.6090 0.4302 -0.0018 0.0303  0.0068  153  GLY B O   
10059 N N   . LYS B 156  ? 0.3734 0.5187 0.3462 0.0087  0.0299  0.0010  154  LYS B N   
10060 C CA  . LYS B 156  ? 0.3955 0.5339 0.3727 0.0091  0.0277  0.0001  154  LYS B CA  
10061 C C   . LYS B 156  ? 0.3872 0.5110 0.3617 0.0088  0.0247  -0.0011 154  LYS B C   
10062 O O   . LYS B 156  ? 0.3470 0.4656 0.3166 0.0110  0.0243  -0.0026 154  LYS B O   
10063 C CB  . LYS B 156  ? 0.4479 0.5898 0.4284 0.0156  0.0287  -0.0027 154  LYS B CB  
10064 N N   . LEU B 157  ? 0.3873 0.5046 0.3648 0.0060  0.0224  -0.0005 155  LEU B N   
10065 C CA  . LEU B 157  ? 0.4246 0.5288 0.4005 0.0055  0.0195  -0.0015 155  LEU B CA  
10066 C C   . LEU B 157  ? 0.5153 0.6145 0.4948 0.0097  0.0184  -0.0041 155  LEU B C   
10067 O O   . LEU B 157  ? 0.5183 0.6216 0.5024 0.0100  0.0189  -0.0039 155  LEU B O   
10068 C CB  . LEU B 157  ? 0.5077 0.6076 0.4840 -0.0006 0.0176  0.0011  155  LEU B CB  
10069 C CG  . LEU B 157  ? 0.5209 0.6079 0.4962 -0.0011 0.0144  0.0002  155  LEU B CG  
10070 C CD1 . LEU B 157  ? 0.5330 0.6145 0.5025 -0.0002 0.0137  -0.0004 155  LEU B CD1 
10071 C CD2 . LEU B 157  ? 0.5808 0.6641 0.5572 -0.0064 0.0126  0.0025  155  LEU B CD2 
10072 N N   . THR B 158  ? 0.5243 0.6148 0.5013 0.0127  0.0169  -0.0064 156  THR B N   
10073 C CA  . THR B 158  ? 0.5584 0.6418 0.5382 0.0154  0.0153  -0.0084 156  THR B CA  
10074 C C   . THR B 158  ? 0.5287 0.6017 0.5075 0.0128  0.0125  -0.0083 156  THR B C   
10075 O O   . THR B 158  ? 0.5624 0.6322 0.5370 0.0109  0.0117  -0.0076 156  THR B O   
10076 C CB  . THR B 158  ? 0.6559 0.7378 0.6340 0.0213  0.0158  -0.0115 156  THR B CB  
10077 O OG1 . THR B 158  ? 0.6483 0.7232 0.6214 0.0218  0.0144  -0.0126 156  THR B OG1 
10078 C CG2 . THR B 158  ? 0.5757 0.6683 0.5532 0.0242  0.0187  -0.0116 156  THR B CG2 
10079 N N   . SER B 159  ? 0.4338 0.5016 0.4163 0.0128  0.0109  -0.0089 157  SER B N   
10080 C CA  . SER B 159  ? 0.4201 0.4789 0.4022 0.0106  0.0083  -0.0088 157  SER B CA  
10081 C C   . SER B 159  ? 0.4324 0.4839 0.4119 0.0136  0.0068  -0.0111 157  SER B C   
10082 O O   . SER B 159  ? 0.4133 0.4588 0.3905 0.0120  0.0049  -0.0109 157  SER B O   
10083 C CB  . SER B 159  ? 0.5455 0.6020 0.5324 0.0095  0.0073  -0.0085 157  SER B CB  
10084 O OG  . SER B 159  ? 0.5726 0.6344 0.5628 0.0120  0.0089  -0.0091 157  SER B OG  
10085 N N   . THR B 160  ? 0.4009 0.4528 0.3808 0.0178  0.0075  -0.0133 158  THR B N   
10086 C CA  . THR B 160  ? 0.3047 0.3499 0.2821 0.0205  0.0060  -0.0156 158  THR B CA  
10087 C C   . THR B 160  ? 0.2961 0.3451 0.2699 0.0243  0.0078  -0.0171 158  THR B C   
10088 O O   . THR B 160  ? 0.3446 0.4018 0.3188 0.0253  0.0102  -0.0165 158  THR B O   
10089 C CB  . THR B 160  ? 0.3236 0.3633 0.3045 0.0221  0.0047  -0.0171 158  THR B CB  
10090 O OG1 . THR B 160  ? 0.3705 0.4149 0.3543 0.0244  0.0063  -0.0174 158  THR B OG1 
10091 C CG2 . THR B 160  ? 0.3616 0.3975 0.3458 0.0187  0.0030  -0.0158 158  THR B CG2 
10092 N N   . VAL B 161  ? 0.2393 0.2823 0.2094 0.0265  0.0064  -0.0192 159  VAL B N   
10093 C CA  . VAL B 161  ? 0.3071 0.3521 0.2721 0.0298  0.0076  -0.0208 159  VAL B CA  
10094 C C   . VAL B 161  ? 0.2708 0.3120 0.2356 0.0344  0.0071  -0.0236 159  VAL B C   
10095 O O   . VAL B 161  ? 0.2768 0.3102 0.2428 0.0343  0.0048  -0.0247 159  VAL B O   
10096 C CB  . VAL B 161  ? 0.3407 0.3814 0.3006 0.0283  0.0061  -0.0208 159  VAL B CB  
10097 C CG1 . VAL B 161  ? 0.4112 0.4500 0.3655 0.0322  0.0062  -0.0234 159  VAL B CG1 
10098 C CG2 . VAL B 161  ? 0.4666 0.5128 0.4252 0.0245  0.0072  -0.0179 159  VAL B CG2 
10099 N N   . ASN B 162  ? 0.2594 0.3058 0.2227 0.0383  0.0093  -0.0247 160  ASN B N   
10100 C CA  . ASN B 162  ? 0.2607 0.3022 0.2224 0.0430  0.0086  -0.0276 160  ASN B CA  
10101 C C   . ASN B 162  ? 0.2449 0.2814 0.2001 0.0447  0.0075  -0.0297 160  ASN B C   
10102 O O   . ASN B 162  ? 0.2437 0.2842 0.1945 0.0477  0.0092  -0.0308 160  ASN B O   
10103 C CB  . ASN B 162  ? 0.2696 0.3181 0.2323 0.0471  0.0111  -0.0282 160  ASN B CB  
10104 C CG  . ASN B 162  ? 0.2488 0.2910 0.2097 0.0520  0.0101  -0.0311 160  ASN B CG  
10105 O OD1 . ASN B 162  ? 0.2738 0.3073 0.2311 0.0527  0.0079  -0.0331 160  ASN B OD1 
10106 N ND2 . ASN B 162  ? 0.3054 0.3516 0.2685 0.0553  0.0115  -0.0315 160  ASN B ND2 
10107 N N   . ASP B 163  ? 0.2605 0.2882 0.2150 0.0428  0.0046  -0.0304 161  ASP B N   
10108 C CA  . ASP B 163  ? 0.2598 0.2824 0.2081 0.0438  0.0030  -0.0322 161  ASP B CA  
10109 C C   . ASP B 163  ? 0.2477 0.2661 0.1919 0.0489  0.0027  -0.0355 161  ASP B C   
10110 O O   . ASP B 163  ? 0.2618 0.2781 0.1996 0.0507  0.0024  -0.0372 161  ASP B O   
10111 C CB  . ASP B 163  ? 0.2716 0.2865 0.2207 0.0402  -0.0002 -0.0318 161  ASP B CB  
10112 C CG  . ASP B 163  ? 0.2835 0.2931 0.2377 0.0396  -0.0020 -0.0322 161  ASP B CG  
10113 O OD1 . ASP B 163  ? 0.2722 0.2852 0.2312 0.0394  -0.0007 -0.0311 161  ASP B OD1 
10114 O OD2 . ASP B 163  ? 0.3350 0.3370 0.2880 0.0392  -0.0048 -0.0336 161  ASP B OD2 
10115 N N   . ARG B 164  ? 0.2406 0.2571 0.1874 0.0513  0.0027  -0.0364 162  ARG B N   
10116 C CA  . ARG B 164  ? 0.2396 0.2519 0.1817 0.0566  0.0025  -0.0396 162  ARG B CA  
10117 C C   . ARG B 164  ? 0.2166 0.2374 0.1556 0.0606  0.0057  -0.0402 162  ARG B C   
10118 O O   . ARG B 164  ? 0.2323 0.2509 0.1649 0.0645  0.0057  -0.0427 162  ARG B O   
10119 C CB  . ARG B 164  ? 0.2344 0.2417 0.1797 0.0581  0.0014  -0.0404 162  ARG B CB  
10120 C CG  . ARG B 164  ? 0.2593 0.2583 0.2073 0.0545  -0.0018 -0.0401 162  ARG B CG  
10121 C CD  . ARG B 164  ? 0.3780 0.3701 0.3212 0.0534  -0.0044 -0.0416 162  ARG B CD  
10122 N NE  . ARG B 164  ? 0.4762 0.4641 0.4122 0.0579  -0.0048 -0.0448 162  ARG B NE  
10123 C CZ  . ARG B 164  ? 0.5228 0.5072 0.4530 0.0580  -0.0062 -0.0463 162  ARG B CZ  
10124 N NH1 . ARG B 164  ? 0.5167 0.5015 0.4475 0.0539  -0.0073 -0.0449 162  ARG B NH1 
10125 N NH2 . ARG B 164  ? 0.4931 0.4735 0.4165 0.0625  -0.0065 -0.0494 162  ARG B NH2 
10126 N N   . SER B 165  ? 0.2503 0.2810 0.1938 0.0597  0.0083  -0.0378 163  SER B N   
10127 C CA  . SER B 165  ? 0.2214 0.2619 0.1627 0.0631  0.0116  -0.0380 163  SER B CA  
10128 C C   . SER B 165  ? 0.2343 0.2777 0.1704 0.0620  0.0123  -0.0378 163  SER B C   
10129 O O   . SER B 165  ? 0.2376 0.2840 0.1684 0.0661  0.0139  -0.0396 163  SER B O   
10130 C CB  . SER B 165  ? 0.2177 0.2685 0.1654 0.0614  0.0139  -0.0352 163  SER B CB  
10131 O OG  . SER B 165  ? 0.2466 0.3084 0.1928 0.0636  0.0171  -0.0348 163  SER B OG  
10132 N N   . LEU B 166  ? 0.2505 0.2927 0.1877 0.0565  0.0112  -0.0356 164  LEU B N   
10133 C CA  . LEU B 166  ? 0.2356 0.2798 0.1675 0.0550  0.0117  -0.0351 164  LEU B CA  
10134 C C   . LEU B 166  ? 0.2443 0.2800 0.1692 0.0578  0.0096  -0.0382 164  LEU B C   
10135 O O   . LEU B 166  ? 0.2545 0.2931 0.1734 0.0596  0.0109  -0.0391 164  LEU B O   
10136 C CB  . LEU B 166  ? 0.2391 0.2828 0.1738 0.0487  0.0105  -0.0320 164  LEU B CB  
10137 C CG  . LEU B 166  ? 0.2777 0.3310 0.2178 0.0458  0.0129  -0.0288 164  LEU B CG  
10138 C CD1 . LEU B 166  ? 0.3089 0.3600 0.2518 0.0399  0.0113  -0.0260 164  LEU B CD1 
10139 C CD2 . LEU B 166  ? 0.2712 0.3352 0.2082 0.0470  0.0163  -0.0280 164  LEU B CD2 
10140 N N   . ALA B 167  ? 0.2388 0.2640 0.1642 0.0577  0.0064  -0.0399 165  ALA B N   
10141 C CA  . ALA B 167  ? 0.2633 0.2799 0.1818 0.0602  0.0041  -0.0431 165  ALA B CA  
10142 C C   . ALA B 167  ? 0.2643 0.2822 0.1780 0.0667  0.0058  -0.0460 165  ALA B C   
10143 O O   . ALA B 167  ? 0.2816 0.2983 0.1880 0.0692  0.0059  -0.0481 165  ALA B O   
10144 C CB  . ALA B 167  ? 0.2821 0.2879 0.2028 0.0588  0.0004  -0.0441 165  ALA B CB  
10145 N N   . ALA B 168  ? 0.2656 0.2860 0.1829 0.0696  0.0071  -0.0464 166  ALA B N   
10146 C CA  . ALA B 168  ? 0.2655 0.2878 0.1786 0.0762  0.0088  -0.0491 166  ALA B CA  
10147 C C   . ALA B 168  ? 0.2481 0.2816 0.1580 0.0779  0.0123  -0.0485 166  ALA B C   
10148 O O   . ALA B 168  ? 0.2755 0.3089 0.1787 0.0827  0.0131  -0.0513 166  ALA B O   
10149 C CB  . ALA B 168  ? 0.2803 0.3045 0.1988 0.0786  0.0096  -0.0489 166  ALA B CB  
10150 N N   . ALA B 169  ? 0.2494 0.2929 0.1643 0.0738  0.0145  -0.0450 167  ALA B N   
10151 C CA  . ALA B 169  ? 0.2495 0.3048 0.1621 0.0746  0.0181  -0.0439 167  ALA B CA  
10152 C C   . ALA B 169  ? 0.2828 0.3355 0.1880 0.0737  0.0175  -0.0445 167  ALA B C   
10153 O O   . ALA B 169  ? 0.2748 0.3330 0.1744 0.0773  0.0198  -0.0458 167  ALA B O   
10154 C CB  . ALA B 169  ? 0.2636 0.3288 0.1831 0.0696  0.0200  -0.0396 167  ALA B CB  
10155 N N   . LEU B 170  ? 0.2741 0.3187 0.1789 0.0690  0.0145  -0.0437 168  LEU B N   
10156 C CA  . LEU B 170  ? 0.2542 0.2961 0.1518 0.0680  0.0136  -0.0442 168  LEU B CA  
10157 C C   . LEU B 170  ? 0.2845 0.3190 0.1743 0.0736  0.0123  -0.0486 168  LEU B C   
10158 O O   . LEU B 170  ? 0.2931 0.3304 0.1758 0.0759  0.0137  -0.0498 168  LEU B O   
10159 C CB  . LEU B 170  ? 0.2860 0.3207 0.1854 0.0621  0.0103  -0.0423 168  LEU B CB  
10160 C CG  . LEU B 170  ? 0.2776 0.3100 0.1702 0.0601  0.0092  -0.0421 168  LEU B CG  
10161 C CD1 . LEU B 170  ? 0.3108 0.3546 0.2013 0.0591  0.0129  -0.0396 168  LEU B CD1 
10162 C CD2 . LEU B 170  ? 0.3534 0.3793 0.2492 0.0547  0.0059  -0.0401 168  LEU B CD2 
10163 N N   . THR B 171  ? 0.2909 0.3157 0.1815 0.0757  0.0096  -0.0511 169  THR B N   
10164 C CA  . THR B 171  ? 0.3136 0.3308 0.1966 0.0812  0.0082  -0.0555 169  THR B CA  
10165 C C   . THR B 171  ? 0.3051 0.3305 0.1845 0.0875  0.0119  -0.0572 169  THR B C   
10166 O O   . THR B 171  ? 0.2975 0.3220 0.1687 0.0913  0.0123  -0.0598 169  THR B O   
10167 C CB  . THR B 171  ? 0.3404 0.3468 0.2257 0.0822  0.0050  -0.0574 169  THR B CB  
10168 O OG1 . THR B 171  ? 0.3720 0.3710 0.2601 0.0766  0.0015  -0.0561 169  THR B OG1 
10169 C CG2 . THR B 171  ? 0.3372 0.3352 0.2144 0.0881  0.0036  -0.0620 169  THR B CG2 
10170 N N   . ARG B 172  ? 0.2990 0.3331 0.1846 0.0887  0.0146  -0.0557 170  ARG B N   
10171 C CA  . ARG B 172  ? 0.2942 0.3370 0.1771 0.0951  0.0181  -0.0573 170  ARG B CA  
10172 C C   . ARG B 172  ? 0.2830 0.3360 0.1617 0.0947  0.0212  -0.0562 170  ARG B C   
10173 O O   . ARG B 172  ? 0.3098 0.3648 0.1814 0.1002  0.0228  -0.0590 170  ARG B O   
10174 C CB  . ARG B 172  ? 0.2748 0.3259 0.1659 0.0958  0.0203  -0.0555 170  ARG B CB  
10175 C CG  . ARG B 172  ? 0.2778 0.3366 0.1667 0.1035  0.0233  -0.0577 170  ARG B CG  
10176 C CD  . ARG B 172  ? 0.2906 0.3591 0.1880 0.1038  0.0255  -0.0554 170  ARG B CD  
10177 N NE  . ARG B 172  ? 0.2716 0.3323 0.1751 0.1008  0.0227  -0.0544 170  ARG B NE  
10178 C CZ  . ARG B 172  ? 0.2611 0.3245 0.1717 0.0941  0.0224  -0.0507 170  ARG B CZ  
10179 N NH1 . ARG B 172  ? 0.2668 0.3394 0.1792 0.0894  0.0244  -0.0475 170  ARG B NH1 
10180 N NH2 . ARG B 172  ? 0.2668 0.3230 0.1823 0.0921  0.0200  -0.0501 170  ARG B NH2 
10181 N N   . LEU B 173  ? 0.2991 0.3584 0.1817 0.0882  0.0221  -0.0521 171  LEU B N   
10182 C CA  . LEU B 173  ? 0.3082 0.3782 0.1870 0.0876  0.0254  -0.0506 171  LEU B CA  
10183 C C   . LEU B 173  ? 0.3248 0.3881 0.1941 0.0882  0.0239  -0.0527 171  LEU B C   
10184 O O   . LEU B 173  ? 0.3280 0.3980 0.1912 0.0913  0.0265  -0.0536 171  LEU B O   
10185 C CB  . LEU B 173  ? 0.3288 0.4069 0.2139 0.0804  0.0267  -0.0455 171  LEU B CB  
10186 C CG  . LEU B 173  ? 0.3305 0.4015 0.2166 0.0733  0.0237  -0.0430 171  LEU B CG  
10187 C CD1 . LEU B 173  ? 0.3237 0.3957 0.2023 0.0714  0.0241  -0.0423 171  LEU B CD1 
10188 C CD2 . LEU B 173  ? 0.3334 0.4103 0.2282 0.0676  0.0244  -0.0388 171  LEU B CD2 
10189 N N   . ILE B 174  ? 0.3137 0.3641 0.1815 0.0854  0.0196  -0.0534 172  ILE B N   
10190 C CA  . ILE B 174  ? 0.3015 0.3451 0.1601 0.0860  0.0177  -0.0554 172  ILE B CA  
10191 C C   . ILE B 174  ? 0.3189 0.3576 0.1701 0.0936  0.0175  -0.0605 172  ILE B C   
10192 O O   . ILE B 174  ? 0.3460 0.3860 0.1886 0.0965  0.0186  -0.0624 172  ILE B O   
10193 C CB  . ILE B 174  ? 0.3237 0.3554 0.1832 0.0809  0.0130  -0.0549 172  ILE B CB  
10194 C CG1 . ILE B 174  ? 0.3244 0.3608 0.1897 0.0737  0.0132  -0.0500 172  ILE B CG1 
10195 C CG2 . ILE B 174  ? 0.3434 0.3671 0.1930 0.0822  0.0106  -0.0576 172  ILE B CG2 
10196 C CD1 . ILE B 174  ? 0.3418 0.3676 0.2098 0.0690  0.0087  -0.0492 172  ILE B CD1 
10197 N N   . SER B 175  ? 0.3396 0.3719 0.1934 0.0971  0.0160  -0.0629 173  SER B N   
10198 C CA  . SER B 175  ? 0.3506 0.3774 0.1970 0.1046  0.0156  -0.0678 173  SER B CA  
10199 C C   . SER B 175  ? 0.3256 0.3650 0.1694 0.1104  0.0204  -0.0686 173  SER B C   
10200 O O   . SER B 175  ? 0.3829 0.4199 0.2183 0.1166  0.0208  -0.0725 173  SER B O   
10201 C CB  . SER B 175  ? 0.3630 0.3801 0.2126 0.1068  0.0129  -0.0698 173  SER B CB  
10202 O OG  . SER B 175  ? 0.4327 0.4377 0.2837 0.1020  0.0084  -0.0696 173  SER B OG  
10203 N N   . ARG B 176  ? 0.3387 0.3918 0.1898 0.1086  0.0241  -0.0651 174  ARG B N   
10204 C CA  . ARG B 176  ? 0.3282 0.3949 0.1778 0.1139  0.0288  -0.0656 174  ARG B CA  
10205 C C   . ARG B 176  ? 0.3893 0.4649 0.2335 0.1123  0.0315  -0.0641 174  ARG B C   
10206 O O   . ARG B 176  ? 0.3942 0.4755 0.2319 0.1181  0.0342  -0.0666 174  ARG B O   
10207 C CB  . ARG B 176  ? 0.3650 0.4429 0.2249 0.1126  0.0314  -0.0624 174  ARG B CB  
10208 C CG  . ARG B 176  ? 0.3632 0.4559 0.2230 0.1187  0.0361  -0.0631 174  ARG B CG  
10209 C CD  . ARG B 176  ? 0.3456 0.4477 0.2159 0.1173  0.0378  -0.0601 174  ARG B CD  
10210 N NE  . ARG B 176  ? 0.3566 0.4686 0.2330 0.1095  0.0395  -0.0550 174  ARG B NE  
10211 C CZ  . ARG B 176  ? 0.3671 0.4764 0.2509 0.1028  0.0376  -0.0517 174  ARG B CZ  
10212 N NH1 . ARG B 176  ? 0.3267 0.4248 0.2140 0.1027  0.0343  -0.0527 174  ARG B NH1 
10213 N NH2 . ARG B 176  ? 0.4069 0.5250 0.2946 0.0961  0.0392  -0.0473 174  ARG B NH2 
10214 N N   . CYS B 177  ? 0.3491 0.4258 0.1957 0.1045  0.0309  -0.0602 175  CYS B N   
10215 C CA  . CYS B 177  ? 0.3471 0.4342 0.1902 0.1019  0.0339  -0.0576 175  CYS B CA  
10216 C C   . CYS B 177  ? 0.4126 0.4910 0.2484 0.0985  0.0312  -0.0577 175  CYS B C   
10217 O O   . CYS B 177  ? 0.4332 0.5185 0.2633 0.0979  0.0336  -0.0567 175  CYS B O   
10218 C CB  . CYS B 177  ? 0.3495 0.4480 0.2014 0.0954  0.0362  -0.0522 175  CYS B CB  
10219 S SG  . CYS B 177  ? 0.4427 0.5537 0.3037 0.0989  0.0396  -0.0516 175  CYS B SG  
10220 N N   . GLY B 178  ? 0.4146 0.4786 0.2505 0.0961  0.0264  -0.0587 176  GLY B N   
10221 C CA  . GLY B 178  ? 0.4192 0.4740 0.2474 0.0940  0.0233  -0.0596 176  GLY B CA  
10222 C C   . GLY B 178  ? 0.4307 0.4900 0.2597 0.0867  0.0237  -0.0549 176  GLY B C   
10223 O O   . GLY B 178  ? 0.4048 0.4708 0.2415 0.0818  0.0250  -0.0507 176  GLY B O   
10224 N N   . GLU B 179  ? 0.4429 0.4978 0.2630 0.0862  0.0223  -0.0557 177  GLU B N   
10225 C CA  . GLU B 179  ? 0.4776 0.5347 0.2970 0.0795  0.0220  -0.0514 177  GLU B CA  
10226 C C   . GLU B 179  ? 0.4102 0.4825 0.2325 0.0768  0.0269  -0.0471 177  GLU B C   
10227 O O   . GLU B 179  ? 0.3884 0.4625 0.2154 0.0702  0.0264  -0.0426 177  GLU B O   
10228 C CB  . GLU B 179  ? 0.4929 0.5437 0.3011 0.0804  0.0201  -0.0533 177  GLU B CB  
10229 C CG  . GLU B 179  ? 0.5373 0.5897 0.3436 0.0738  0.0196  -0.0489 177  GLU B CG  
10230 C CD  . GLU B 179  ? 0.7542 0.7978 0.5503 0.0739  0.0165  -0.0506 177  GLU B CD  
10231 O OE1 . GLU B 179  ? 0.7417 0.7791 0.5313 0.0794  0.0151  -0.0554 177  GLU B OE1 
10232 O OE2 . GLU B 179  ? 0.7561 0.7987 0.5505 0.0686  0.0151  -0.0472 177  GLU B OE2 
10233 N N   . PRO B 180  ? 0.3869 0.4707 0.2069 0.0814  0.0315  -0.0481 178  PRO B N   
10234 C CA  . PRO B 180  ? 0.4395 0.5385 0.2624 0.0780  0.0360  -0.0436 178  PRO B CA  
10235 C C   . PRO B 180  ? 0.4413 0.5445 0.2754 0.0729  0.0362  -0.0397 178  PRO B C   
10236 O O   . PRO B 180  ? 0.4080 0.5177 0.2442 0.0667  0.0376  -0.0350 178  PRO B O   
10237 C CB  . PRO B 180  ? 0.4482 0.5580 0.2682 0.0852  0.0404  -0.0463 178  PRO B CB  
10238 C CG  . PRO B 180  ? 0.4282 0.5280 0.2385 0.0912  0.0384  -0.0515 178  PRO B CG  
10239 C CD  . PRO B 180  ? 0.4577 0.5412 0.2704 0.0897  0.0327  -0.0532 178  PRO B CD  
10240 N N   . VAL B 181  ? 0.3527 0.4519 0.1938 0.0750  0.0348  -0.0414 179  VAL B N   
10241 C CA  . VAL B 181  ? 0.3205 0.4237 0.1719 0.0701  0.0350  -0.0377 179  VAL B CA  
10242 C C   . VAL B 181  ? 0.3397 0.4330 0.1933 0.0634  0.0309  -0.0352 179  VAL B C   
10243 O O   . VAL B 181  ? 0.3418 0.4392 0.2011 0.0575  0.0314  -0.0309 179  VAL B O   
10244 C CB  . VAL B 181  ? 0.3590 0.4617 0.2172 0.0744  0.0349  -0.0401 179  VAL B CB  
10245 C CG1 . VAL B 181  ? 0.4089 0.4958 0.2669 0.0759  0.0302  -0.0433 179  VAL B CG1 
10246 C CG2 . VAL B 181  ? 0.4026 0.5130 0.2708 0.0698  0.0362  -0.0362 179  VAL B CG2 
10247 N N   . ILE B 182  ? 0.3613 0.4412 0.2102 0.0642  0.0269  -0.0377 180  ILE B N   
10248 C CA  . ILE B 182  ? 0.3604 0.4312 0.2110 0.0583  0.0229  -0.0355 180  ILE B CA  
10249 C C   . ILE B 182  ? 0.3843 0.4596 0.2308 0.0531  0.0239  -0.0314 180  ILE B C   
10250 O O   . ILE B 182  ? 0.3807 0.4562 0.2318 0.0471  0.0231  -0.0275 180  ILE B O   
10251 C CB  . ILE B 182  ? 0.3808 0.4375 0.2269 0.0604  0.0183  -0.0392 180  ILE B CB  
10252 C CG1 . ILE B 182  ? 0.3590 0.4104 0.2094 0.0647  0.0170  -0.0427 180  ILE B CG1 
10253 C CG2 . ILE B 182  ? 0.3940 0.4423 0.2418 0.0546  0.0143  -0.0368 180  ILE B CG2 
10254 C CD1 . ILE B 182  ? 0.4130 0.4521 0.2573 0.0681  0.0133  -0.0471 180  ILE B CD1 
10255 N N   . ARG B 183  ? 0.3847 0.4635 0.2223 0.0555  0.0257  -0.0324 181  ARG B N   
10256 C CA  . ARG B 183  ? 0.4179 0.5015 0.2507 0.0508  0.0270  -0.0285 181  ARG B CA  
10257 C C   . ARG B 183  ? 0.4423 0.5379 0.2813 0.0463  0.0305  -0.0239 181  ARG B C   
10258 O O   . ARG B 183  ? 0.4439 0.5388 0.2841 0.0399  0.0295  -0.0196 181  ARG B O   
10259 C CB  . ARG B 183  ? 0.4459 0.5330 0.2683 0.0549  0.0291  -0.0306 181  ARG B CB  
10260 C CG  . ARG B 183  ? 0.5778 0.6735 0.3949 0.0509  0.0319  -0.0265 181  ARG B CG  
10261 C CD  . ARG B 183  ? 0.6426 0.7316 0.4594 0.0437  0.0287  -0.0224 181  ARG B CD  
10262 N NE  . ARG B 183  ? 0.6786 0.7530 0.4921 0.0444  0.0235  -0.0249 181  ARG B NE  
10263 C CZ  . ARG B 183  ? 0.6195 0.6853 0.4355 0.0395  0.0195  -0.0226 181  ARG B CZ  
10264 N NH1 . ARG B 183  ? 0.5324 0.6015 0.3537 0.0337  0.0200  -0.0180 181  ARG B NH1 
10265 N NH2 . ARG B 183  ? 0.6979 0.7516 0.5107 0.0406  0.0149  -0.0251 181  ARG B NH2 
10266 N N   . ARG B 184  ? 0.4205 0.5269 0.2636 0.0497  0.0343  -0.0247 182  ARG B N   
10267 C CA  . ARG B 184  ? 0.4275 0.5461 0.2768 0.0455  0.0375  -0.0204 182  ARG B CA  
10268 C C   . ARG B 184  ? 0.4261 0.5397 0.2839 0.0403  0.0349  -0.0179 182  ARG B C   
10269 O O   . ARG B 184  ? 0.4171 0.5352 0.2775 0.0340  0.0356  -0.0133 182  ARG B O   
10270 C CB  . ARG B 184  ? 0.4360 0.5668 0.2885 0.0508  0.0417  -0.0222 182  ARG B CB  
10271 C CG  . ARG B 184  ? 0.5131 0.6537 0.3579 0.0545  0.0456  -0.0232 182  ARG B CG  
10272 C CD  . ARG B 184  ? 0.5808 0.7357 0.4264 0.0493  0.0495  -0.0182 182  ARG B CD  
10273 N NE  . ARG B 184  ? 0.5788 0.7473 0.4322 0.0505  0.0531  -0.0174 182  ARG B NE  
10274 C CZ  . ARG B 184  ? 0.5340 0.7086 0.3953 0.0447  0.0537  -0.0133 182  ARG B CZ  
10275 N NH1 . ARG B 184  ? 0.5645 0.7326 0.4268 0.0372  0.0511  -0.0095 182  ARG B NH1 
10276 N NH2 . ARG B 184  ? 0.4804 0.6676 0.3483 0.0466  0.0569  -0.0131 182  ARG B NH2 
10277 N N   . GLY B 185  ? 0.3862 0.4905 0.2484 0.0427  0.0319  -0.0207 183  GLY B N   
10278 C CA  . GLY B 185  ? 0.3474 0.4467 0.2174 0.0382  0.0294  -0.0186 183  GLY B CA  
10279 C C   . GLY B 185  ? 0.3798 0.4704 0.2473 0.0325  0.0260  -0.0159 183  GLY B C   
10280 O O   . GLY B 185  ? 0.3771 0.4682 0.2492 0.0269  0.0254  -0.0122 183  GLY B O   
10281 N N   . VAL B 186  ? 0.3747 0.4571 0.2346 0.0339  0.0236  -0.0177 184  VAL B N   
10282 C CA  . VAL B 186  ? 0.4037 0.4779 0.2606 0.0289  0.0203  -0.0152 184  VAL B CA  
10283 C C   . VAL B 186  ? 0.4172 0.4990 0.2714 0.0236  0.0226  -0.0103 184  VAL B C   
10284 O O   . VAL B 186  ? 0.4087 0.4877 0.2655 0.0180  0.0209  -0.0067 184  VAL B O   
10285 C CB  . VAL B 186  ? 0.3692 0.4341 0.2181 0.0319  0.0174  -0.0183 184  VAL B CB  
10286 C CG1 . VAL B 186  ? 0.4034 0.4621 0.2474 0.0270  0.0146  -0.0152 184  VAL B CG1 
10287 C CG2 . VAL B 186  ? 0.4123 0.4677 0.2648 0.0352  0.0141  -0.0222 184  VAL B CG2 
10288 N N   . ASP B 187  ? 0.4390 0.5305 0.2879 0.0253  0.0264  -0.0102 185  ASP B N   
10289 C CA  . ASP B 187  ? 0.4497 0.5492 0.2958 0.0200  0.0289  -0.0054 185  ASP B CA  
10290 C C   . ASP B 187  ? 0.4924 0.5987 0.3469 0.0154  0.0304  -0.0019 185  ASP B C   
10291 O O   . ASP B 187  ? 0.4373 0.5435 0.2915 0.0090  0.0298  0.0026  185  ASP B O   
10292 C CB  . ASP B 187  ? 0.4494 0.5597 0.2891 0.0232  0.0332  -0.0061 185  ASP B CB  
10293 C CG  . ASP B 187  ? 0.5103 0.6138 0.3401 0.0266  0.0317  -0.0088 185  ASP B CG  
10294 O OD1 . ASP B 187  ? 0.5653 0.6564 0.3929 0.0253  0.0272  -0.0092 185  ASP B OD1 
10295 O OD2 . ASP B 187  ? 0.4879 0.5987 0.3120 0.0306  0.0349  -0.0106 185  ASP B OD2 
10296 N N   . MET B 188  ? 0.4344 0.5461 0.2963 0.0187  0.0320  -0.0039 186  MET B N   
10297 C CA  . MET B 188  ? 0.4209 0.5396 0.2910 0.0147  0.0334  -0.0010 186  MET B CA  
10298 C C   . MET B 188  ? 0.4080 0.5162 0.2825 0.0102  0.0294  0.0008  186  MET B C   
10299 O O   . MET B 188  ? 0.5155 0.6261 0.3923 0.0041  0.0294  0.0049  186  MET B O   
10300 C CB  . MET B 188  ? 0.4569 0.5826 0.3334 0.0200  0.0357  -0.0040 186  MET B CB  
10301 C CG  . MET B 188  ? 0.4959 0.6295 0.3810 0.0165  0.0371  -0.0012 186  MET B CG  
10302 S SD  . MET B 188  ? 0.6618 0.8105 0.5452 0.0108  0.0413  0.0039  186  MET B SD  
10303 C CE  . MET B 188  ? 0.5774 0.7359 0.4543 0.0177  0.0453  0.0009  186  MET B CE  
10304 N N   . ALA B 189  ? 0.4275 0.5242 0.3031 0.0131  0.0258  -0.0024 187  ALA B N   
10305 C CA  . ALA B 189  ? 0.4389 0.5259 0.3186 0.0093  0.0219  -0.0010 187  ALA B CA  
10306 C C   . ALA B 189  ? 0.4431 0.5241 0.3170 0.0042  0.0197  0.0024  187  ALA B C   
10307 O O   . ALA B 189  ? 0.4197 0.4973 0.2964 -0.0008 0.0180  0.0054  187  ALA B O   
10308 C CB  . ALA B 189  ? 0.4537 0.5305 0.3356 0.0136  0.0187  -0.0051 187  ALA B CB  
10309 N N   . MET B 190  ? 0.4191 0.4985 0.2844 0.0055  0.0197  0.0019  188  MET B N   
10310 C CA  . MET B 190  ? 0.4425 0.5163 0.3015 0.0009  0.0175  0.0052  188  MET B CA  
10311 C C   . MET B 190  ? 0.5310 0.6124 0.3900 -0.0053 0.0199  0.0103  188  MET B C   
10312 O O   . MET B 190  ? 0.4444 0.5200 0.3028 -0.0105 0.0175  0.0137  188  MET B O   
10313 C CB  . MET B 190  ? 0.4499 0.5218 0.2994 0.0037  0.0174  0.0036  188  MET B CB  
10314 C CG  . MET B 190  ? 0.5530 0.6174 0.3954 -0.0004 0.0146  0.0066  188  MET B CG  
10315 S SD  . MET B 190  ? 0.6183 0.6828 0.4488 0.0027  0.0152  0.0052  188  MET B SD  
10316 C CE  . MET B 190  ? 0.5263 0.5847 0.3583 0.0102  0.0132  -0.0014 188  MET B CE  
10317 N N   . ARG B 191  ? 0.4221 0.5167 0.2818 -0.0048 0.0245  0.0109  189  ARG B N   
10318 C CA  . ARG B 191  ? 0.4882 0.5913 0.3484 -0.0110 0.0269  0.0158  189  ARG B CA  
10319 C C   . ARG B 191  ? 0.4911 0.5927 0.3597 -0.0147 0.0256  0.0175  189  ARG B C   
10320 O O   . ARG B 191  ? 0.4464 0.5449 0.3142 -0.0210 0.0242  0.0216  189  ARG B O   
10321 C CB  . ARG B 191  ? 0.4485 0.5672 0.3085 -0.0091 0.0322  0.0157  189  ARG B CB  
10322 N N   . MET B 192  ? 0.4201 0.5234 0.2963 -0.0109 0.0259  0.0144  190  MET B N   
10323 C CA  . MET B 192  ? 0.3808 0.4835 0.2649 -0.0141 0.0249  0.0158  190  MET B CA  
10324 C C   . MET B 192  ? 0.4213 0.5101 0.3050 -0.0171 0.0202  0.0169  190  MET B C   
10325 O O   . MET B 192  ? 0.4324 0.5197 0.3178 -0.0227 0.0192  0.0203  190  MET B O   
10326 C CB  . MET B 192  ? 0.4392 0.5453 0.3309 -0.0089 0.0259  0.0121  190  MET B CB  
10327 C CG  . MET B 192  ? 0.4636 0.5839 0.3563 -0.0055 0.0305  0.0110  190  MET B CG  
10328 S SD  . MET B 192  ? 0.6291 0.7521 0.5306 0.0003  0.0311  0.0070  190  MET B SD  
10329 C CE  . MET B 192  ? 0.4573 0.5829 0.3666 -0.0060 0.0306  0.0106  190  MET B CE  
10330 N N   . MET B 193  ? 0.4143 0.4930 0.2958 -0.0133 0.0173  0.0139  191  MET B N   
10331 C CA  . MET B 193  ? 0.4399 0.5062 0.3220 -0.0153 0.0128  0.0144  191  MET B CA  
10332 C C   . MET B 193  ? 0.4253 0.4857 0.2996 -0.0197 0.0108  0.0179  191  MET B C   
10333 O O   . MET B 193  ? 0.4520 0.5032 0.3267 -0.0226 0.0074  0.0195  191  MET B O   
10334 C CB  . MET B 193  ? 0.4632 0.5213 0.3466 -0.0099 0.0102  0.0100  191  MET B CB  
10335 C CG  . MET B 193  ? 0.5074 0.5672 0.3994 -0.0069 0.0106  0.0072  191  MET B CG  
10336 S SD  . MET B 193  ? 0.5608 0.6094 0.4543 -0.0020 0.0068  0.0029  191  MET B SD  
10337 C CE  . MET B 193  ? 0.4125 0.4645 0.3002 0.0034  0.0086  -0.0005 191  MET B CE  
10338 N N   . GLY B 194  ? 0.4258 0.4913 0.2930 -0.0201 0.0129  0.0192  192  GLY B N   
10339 C CA  . GLY B 194  ? 0.4249 0.4847 0.2840 -0.0242 0.0111  0.0226  192  GLY B CA  
10340 C C   . GLY B 194  ? 0.4830 0.5492 0.3402 -0.0308 0.0132  0.0277  192  GLY B C   
10341 O O   . GLY B 194  ? 0.4595 0.5192 0.3112 -0.0355 0.0110  0.0313  192  GLY B O   
10342 N N   . GLU B 195  ? 0.4415 0.5204 0.3029 -0.0314 0.0173  0.0282  193  GLU B N   
10343 C CA  . GLU B 195  ? 0.4873 0.5747 0.3465 -0.0377 0.0200  0.0330  193  GLU B CA  
10344 C C   . GLU B 195  ? 0.4398 0.5354 0.3071 -0.0406 0.0219  0.0343  193  GLU B C   
10345 O O   . GLU B 195  ? 0.4103 0.5097 0.2763 -0.0472 0.0227  0.0388  193  GLU B O   
10346 C CB  . GLU B 195  ? 0.4812 0.5796 0.3349 -0.0361 0.0241  0.0332  193  GLU B CB  
10347 C CG  . GLU B 195  ? 0.5712 0.6630 0.4159 -0.0335 0.0226  0.0321  193  GLU B CG  
10348 C CD  . GLU B 195  ? 0.6589 0.7621 0.4986 -0.0310 0.0269  0.0315  193  GLU B CD  
10349 O OE1 . GLU B 195  ? 0.6914 0.8078 0.5332 -0.0333 0.0310  0.0336  193  GLU B OE1 
10350 O OE2 . GLU B 195  ? 0.7810 0.8801 0.6146 -0.0266 0.0262  0.0289  193  GLU B OE2 
10351 N N   . GLN B 196  ? 0.4708 0.5693 0.3460 -0.0362 0.0225  0.0307  194  GLN B N   
10352 C CA  . GLN B 196  ? 0.4389 0.5457 0.3218 -0.0387 0.0243  0.0318  194  GLN B CA  
10353 C C   . GLN B 196  ? 0.4562 0.5531 0.3445 -0.0400 0.0206  0.0314  194  GLN B C   
10354 O O   . GLN B 196  ? 0.4751 0.5722 0.3654 -0.0458 0.0200  0.0347  194  GLN B O   
10355 C CB  . GLN B 196  ? 0.4443 0.5628 0.3324 -0.0329 0.0279  0.0284  194  GLN B CB  
10356 N N   . PHE B 197  ? 0.4252 0.5134 0.3156 -0.0348 0.0182  0.0275  195  PHE B N   
10357 C CA  . PHE B 197  ? 0.4514 0.5303 0.3467 -0.0356 0.0148  0.0270  195  PHE B CA  
10358 C C   . PHE B 197  ? 0.4494 0.5166 0.3397 -0.0402 0.0110  0.0299  195  PHE B C   
10359 O O   . PHE B 197  ? 0.4543 0.5153 0.3477 -0.0430 0.0087  0.0309  195  PHE B O   
10360 C CB  . PHE B 197  ? 0.4417 0.5151 0.3406 -0.0289 0.0133  0.0221  195  PHE B CB  
10361 C CG  . PHE B 197  ? 0.4295 0.5127 0.3340 -0.0243 0.0164  0.0191  195  PHE B CG  
10362 C CD1 . PHE B 197  ? 0.5089 0.6032 0.4180 -0.0264 0.0193  0.0206  195  PHE B CD1 
10363 C CD2 . PHE B 197  ? 0.4929 0.5739 0.3978 -0.0178 0.0163  0.0148  195  PHE B CD2 
10364 C CE1 . PHE B 197  ? 0.5613 0.6645 0.4756 -0.0218 0.0220  0.0179  195  PHE B CE1 
10365 C CE2 . PHE B 197  ? 0.5027 0.5918 0.4123 -0.0133 0.0189  0.0121  195  PHE B CE2 
10366 C CZ  . PHE B 197  ? 0.5010 0.6012 0.4153 -0.0151 0.0218  0.0137  195  PHE B CZ  
10367 N N   . VAL B 198  ? 0.4259 0.4893 0.3080 -0.0408 0.0103  0.0312  196  VAL B N   
10368 C CA  . VAL B 198  ? 0.3981 0.4508 0.2744 -0.0453 0.0069  0.0344  196  VAL B CA  
10369 C C   . VAL B 198  ? 0.4317 0.4895 0.3003 -0.0495 0.0088  0.0382  196  VAL B C   
10370 O O   . VAL B 198  ? 0.4522 0.5193 0.3187 -0.0472 0.0122  0.0374  196  VAL B O   
10371 C CB  . VAL B 198  ? 0.3922 0.4323 0.2658 -0.0415 0.0028  0.0320  196  VAL B CB  
10372 C CG1 . VAL B 198  ? 0.4266 0.4618 0.3079 -0.0379 0.0009  0.0285  196  VAL B CG1 
10373 C CG2 . VAL B 198  ? 0.4485 0.4908 0.3174 -0.0370 0.0040  0.0297  196  VAL B CG2 
10374 N N   . THR B 199  ? 0.4148 0.4664 0.2789 -0.0556 0.0067  0.0425  197  THR B N   
10375 C CA  . THR B 199  ? 0.4108 0.4654 0.2665 -0.0600 0.0081  0.0465  197  THR B CA  
10376 C C   . THR B 199  ? 0.4505 0.4985 0.2987 -0.0566 0.0064  0.0454  197  THR B C   
10377 O O   . THR B 199  ? 0.4817 0.5358 0.3239 -0.0570 0.0089  0.0466  197  THR B O   
10378 C CB  . THR B 199  ? 0.4540 0.5029 0.3067 -0.0677 0.0060  0.0515  197  THR B CB  
10379 O OG1 . THR B 199  ? 0.4904 0.5457 0.3506 -0.0706 0.0074  0.0520  197  THR B OG1 
10380 C CG2 . THR B 199  ? 0.4432 0.4964 0.2876 -0.0730 0.0078  0.0561  197  THR B CG2 
10381 N N   . GLY B 200  ? 0.4253 0.4613 0.2738 -0.0531 0.0024  0.0429  198  GLY B N   
10382 C CA  . GLY B 200  ? 0.4334 0.4633 0.2760 -0.0491 0.0005  0.0411  198  GLY B CA  
10383 C C   . GLY B 200  ? 0.4116 0.4316 0.2584 -0.0445 -0.0033 0.0373  198  GLY B C   
10384 O O   . GLY B 200  ? 0.3905 0.4066 0.2434 -0.0452 -0.0050 0.0370  198  GLY B O   
10385 N N   . GLU B 201  ? 0.5143 0.5305 0.3578 -0.0398 -0.0048 0.0346  199  GLU B N   
10386 C CA  . GLU B 201  ? 0.5115 0.5187 0.3586 -0.0355 -0.0085 0.0311  199  GLU B CA  
10387 C C   . GLU B 201  ? 0.4463 0.4411 0.2902 -0.0380 -0.0133 0.0335  199  GLU B C   
10388 O O   . GLU B 201  ? 0.5072 0.4955 0.3564 -0.0363 -0.0161 0.0318  199  GLU B O   
10389 C CB  . GLU B 201  ? 0.4945 0.5016 0.3388 -0.0300 -0.0088 0.0275  199  GLU B CB  
10390 C CG  . GLU B 201  ? 0.6442 0.6449 0.4937 -0.0252 -0.0119 0.0234  199  GLU B CG  
10391 C CD  . GLU B 201  ? 0.6874 0.6861 0.5326 -0.0207 -0.0130 0.0203  199  GLU B CD  
10392 O OE1 . GLU B 201  ? 0.6780 0.6801 0.5157 -0.0211 -0.0114 0.0214  199  GLU B OE1 
10393 O OE2 . GLU B 201  ? 0.7711 0.7650 0.6203 -0.0169 -0.0156 0.0169  199  GLU B OE2 
10394 N N   . THR B 202  ? 0.4240 0.4154 0.2592 -0.0419 -0.0142 0.0375  200  THR B N   
10395 C CA  . THR B 202  ? 0.4408 0.4202 0.2717 -0.0446 -0.0187 0.0402  200  THR B CA  
10396 C C   . THR B 202  ? 0.5171 0.4971 0.3443 -0.0516 -0.0177 0.0454  200  THR B C   
10397 O O   . THR B 202  ? 0.4509 0.4411 0.2772 -0.0545 -0.0135 0.0472  200  THR B O   
10398 C CB  . THR B 202  ? 0.5005 0.4731 0.3228 -0.0428 -0.0215 0.0405  200  THR B CB  
10399 O OG1 . THR B 202  ? 0.5097 0.4880 0.3242 -0.0456 -0.0188 0.0433  200  THR B OG1 
10400 C CG2 . THR B 202  ? 0.5439 0.5166 0.3693 -0.0363 -0.0224 0.0354  200  THR B CG2 
10401 N N   . ILE B 203  ? 0.4490 0.4179 0.2735 -0.0545 -0.0216 0.0480  201  ILE B N   
10402 C CA  . ILE B 203  ? 0.4372 0.4051 0.2575 -0.0616 -0.0212 0.0531  201  ILE B CA  
10403 C C   . ILE B 203  ? 0.4524 0.4229 0.2629 -0.0649 -0.0198 0.0567  201  ILE B C   
10404 O O   . ILE B 203  ? 0.4392 0.4163 0.2474 -0.0705 -0.0169 0.0604  201  ILE B O   
10405 C CB  . ILE B 203  ? 0.4389 0.3931 0.2579 -0.0635 -0.0261 0.0548  201  ILE B CB  
10406 C CG1 . ILE B 203  ? 0.4372 0.3906 0.2529 -0.0712 -0.0256 0.0598  201  ILE B CG1 
10407 C CG2 . ILE B 203  ? 0.4615 0.4042 0.2729 -0.0613 -0.0306 0.0553  201  ILE B CG2 
10408 C CD1 . ILE B 203  ? 0.4063 0.3705 0.2300 -0.0734 -0.0217 0.0592  201  ILE B CD1 
10409 N N   . ARG B 204  ? 0.4768 0.4428 0.2813 -0.0615 -0.0217 0.0558  202  ARG B N   
10410 C CA  . ARG B 204  ? 0.5393 0.5080 0.3341 -0.0640 -0.0203 0.0589  202  ARG B CA  
10411 C C   . ARG B 204  ? 0.4617 0.4460 0.2583 -0.0645 -0.0144 0.0585  202  ARG B C   
10412 O O   . ARG B 204  ? 0.5150 0.5050 0.3065 -0.0698 -0.0118 0.0626  202  ARG B O   
10413 C CB  . ARG B 204  ? 0.5292 0.4914 0.3185 -0.0592 -0.0233 0.0569  202  ARG B CB  
10414 C CG  . ARG B 204  ? 0.6879 0.6464 0.4652 -0.0621 -0.0243 0.0609  202  ARG B CG  
10415 C CD  . ARG B 204  ? 0.6568 0.6084 0.4297 -0.0568 -0.0278 0.0584  202  ARG B CD  
10416 N NE  . ARG B 204  ? 0.5376 0.4976 0.3150 -0.0511 -0.0253 0.0533  202  ARG B NE  
10417 C CZ  . ARG B 204  ? 0.6662 0.6355 0.4397 -0.0505 -0.0215 0.0529  202  ARG B CZ  
10418 N NH1 . ARG B 204  ? 0.6888 0.6609 0.4536 -0.0551 -0.0196 0.0573  202  ARG B NH1 
10419 N NH2 . ARG B 204  ? 0.6959 0.6719 0.4741 -0.0451 -0.0195 0.0479  202  ARG B NH2 
10420 N N   . GLU B 205  ? 0.4615 0.4531 0.2656 -0.0590 -0.0122 0.0535  203  GLU B N   
10421 C CA  . GLU B 205  ? 0.4766 0.4830 0.2829 -0.0585 -0.0067 0.0526  203  GLU B CA  
10422 C C   . GLU B 205  ? 0.4422 0.4566 0.2538 -0.0636 -0.0037 0.0551  203  GLU B C   
10423 O O   . GLU B 205  ? 0.4652 0.4905 0.2747 -0.0668 0.0004  0.0575  203  GLU B O   
10424 C CB  . GLU B 205  ? 0.5134 0.5239 0.3262 -0.0511 -0.0057 0.0466  203  GLU B CB  
10425 C CG  . GLU B 205  ? 0.5852 0.6102 0.3996 -0.0491 -0.0003 0.0449  203  GLU B CG  
10426 C CD  . GLU B 205  ? 0.6623 0.6893 0.4822 -0.0417 0.0001  0.0390  203  GLU B CD  
10427 O OE1 . GLU B 205  ? 0.6512 0.6775 0.4799 -0.0398 -0.0005 0.0365  203  GLU B OE1 
10428 O OE2 . GLU B 205  ? 0.7680 0.7969 0.5831 -0.0378 0.0010  0.0367  203  GLU B OE2 
10429 N N   . ALA B 206  ? 0.4450 0.4542 0.2632 -0.0644 -0.0058 0.0546  204  ALA B N   
10430 C CA  . ALA B 206  ? 0.4328 0.4487 0.2559 -0.0695 -0.0036 0.0570  204  ALA B CA  
10431 C C   . ALA B 206  ? 0.4691 0.4838 0.2845 -0.0775 -0.0036 0.0631  204  ALA B C   
10432 O O   . ALA B 206  ? 0.4456 0.4716 0.2620 -0.0818 0.0002  0.0656  204  ALA B O   
10433 C CB  . ALA B 206  ? 0.4152 0.4237 0.2456 -0.0688 -0.0065 0.0553  204  ALA B CB  
10434 N N   . LEU B 207  ? 0.4070 0.4084 0.2148 -0.0795 -0.0079 0.0656  205  LEU B N   
10435 C CA  . LEU B 207  ? 0.4679 0.4664 0.2677 -0.0873 -0.0084 0.0717  205  LEU B CA  
10436 C C   . LEU B 207  ? 0.4771 0.4865 0.2708 -0.0893 -0.0043 0.0740  205  LEU B C   
10437 O O   . LEU B 207  ? 0.5010 0.5171 0.2926 -0.0961 -0.0018 0.0785  205  LEU B O   
10438 C CB  . LEU B 207  ? 0.4582 0.4394 0.2505 -0.0880 -0.0141 0.0735  205  LEU B CB  
10439 C CG  . LEU B 207  ? 0.5090 0.4789 0.3057 -0.0881 -0.0182 0.0727  205  LEU B CG  
10440 C CD1 . LEU B 207  ? 0.5263 0.4796 0.3161 -0.0868 -0.0239 0.0736  205  LEU B CD1 
10441 C CD2 . LEU B 207  ? 0.4483 0.4197 0.2462 -0.0957 -0.0174 0.0766  205  LEU B CD2 
10442 N N   . LYS B 208  ? 0.4642 0.4756 0.2549 -0.0837 -0.0035 0.0712  206  LYS B N   
10443 C CA  . LYS B 208  ? 0.4958 0.5178 0.2804 -0.0849 0.0006  0.0731  206  LYS B CA  
10444 C C   . LYS B 208  ? 0.5266 0.5662 0.3180 -0.0856 0.0063  0.0724  206  LYS B C   
10445 O O   . LYS B 208  ? 0.5574 0.6068 0.3451 -0.0906 0.0098  0.0763  206  LYS B O   
10446 C CB  . LYS B 208  ? 0.5215 0.5417 0.3018 -0.0781 0.0000  0.0695  206  LYS B CB  
10447 N N   . ARG B 209  ? 0.4912 0.5353 0.2926 -0.0806 0.0073  0.0677  207  ARG B N   
10448 C CA  . ARG B 209  ? 0.4732 0.5340 0.2815 -0.0805 0.0126  0.0668  207  ARG B CA  
10449 C C   . ARG B 209  ? 0.5669 0.6321 0.3790 -0.0880 0.0135  0.0708  207  ARG B C   
10450 O O   . ARG B 209  ? 0.5225 0.6026 0.3393 -0.0892 0.0179  0.0712  207  ARG B O   
10451 C CB  . ARG B 209  ? 0.4931 0.5565 0.3105 -0.0728 0.0131  0.0606  207  ARG B CB  
10452 C CG  . ARG B 209  ? 0.4920 0.5540 0.3063 -0.0654 0.0130  0.0563  207  ARG B CG  
10453 C CD  . ARG B 209  ? 0.4946 0.5578 0.3179 -0.0585 0.0131  0.0506  207  ARG B CD  
10454 N NE  . ARG B 209  ? 0.6175 0.6806 0.4382 -0.0515 0.0134  0.0462  207  ARG B NE  
10455 C CZ  . ARG B 209  ? 0.6719 0.7345 0.4988 -0.0451 0.0130  0.0410  207  ARG B CZ  
10456 N NH1 . ARG B 209  ? 0.5532 0.6156 0.3893 -0.0445 0.0125  0.0394  207  ARG B NH1 
10457 N NH2 . ARG B 209  ? 0.7021 0.7641 0.5255 -0.0392 0.0131  0.0374  207  ARG B NH2 
10458 N N   . SER B 210  ? 0.4695 0.5220 0.2793 -0.0929 0.0093  0.0738  208  SER B N   
10459 C CA  . SER B 210  ? 0.4533 0.5085 0.2664 -0.1002 0.0095  0.0775  208  SER B CA  
10460 C C   . SER B 210  ? 0.4697 0.5305 0.2755 -0.1084 0.0115  0.0836  208  SER B C   
10461 O O   . SER B 210  ? 0.5097 0.5777 0.3189 -0.1147 0.0132  0.0867  208  SER B O   
10462 C CB  . SER B 210  ? 0.4190 0.4576 0.2323 -0.1020 0.0040  0.0779  208  SER B CB  
10463 O OG  . SER B 210  ? 0.4708 0.5060 0.2920 -0.0951 0.0026  0.0725  208  SER B OG  
10464 N N   . LYS B 211  ? 0.4648 0.5225 0.2608 -0.1087 0.0114  0.0856  209  LYS B N   
10465 C CA  . LYS B 211  ? 0.4663 0.5278 0.2545 -0.1170 0.0129  0.0920  209  LYS B CA  
10466 C C   . LYS B 211  ? 0.4892 0.5713 0.2821 -0.1198 0.0189  0.0933  209  LYS B C   
10467 O O   . LYS B 211  ? 0.5229 0.6088 0.3170 -0.1267 0.0196  0.0972  209  LYS B O   
10468 C CB  . LYS B 211  ? 0.4803 0.5364 0.2575 -0.1155 0.0121  0.0931  209  LYS B CB  
10469 N N   . GLU B 212  ? 0.4852 0.5796 0.2840 -0.1127 0.0227  0.0885  210  GLU B N   
10470 C CA  . GLU B 212  ? 0.5565 0.6709 0.3605 -0.1136 0.0284  0.0890  210  GLU B CA  
10471 C C   . GLU B 212  ? 0.5347 0.6549 0.3475 -0.1191 0.0288  0.0907  210  GLU B C   
10472 O O   . GLU B 212  ? 0.5287 0.6564 0.3434 -0.1247 0.0305  0.0939  210  GLU B O   
10473 C CB  . GLU B 212  ? 0.5896 0.7146 0.3980 -0.1046 0.0319  0.0833  210  GLU B CB  
10474 C CG  . GLU B 212  ? 0.7076 0.8526 0.5233 -0.1041 0.0375  0.0828  210  GLU B CG  
10475 C CD  . GLU B 212  ? 0.7964 0.9517 0.6166 -0.0951 0.0408  0.0773  210  GLU B CD  
10476 O OE1 . GLU B 212  ? 0.8635 1.0131 0.6785 -0.0888 0.0401  0.0740  210  GLU B OE1 
10477 O OE2 . GLU B 212  ? 0.8880 1.0561 0.7176 -0.0939 0.0436  0.0758  210  GLU B OE2 
10478 N N   . LEU B 213  ? 0.5218 0.6385 0.3408 -0.1172 0.0271  0.0882  211  LEU B N   
10479 C CA  . LEU B 213  ? 0.5143 0.6372 0.3409 -0.1226 0.0275  0.0899  211  LEU B CA  
10480 C C   . LEU B 213  ? 0.4440 0.5540 0.2668 -0.1310 0.0233  0.0945  211  LEU B C   
10481 O O   . LEU B 213  ? 0.4701 0.5861 0.2981 -0.1369 0.0237  0.0968  211  LEU B O   
10482 C CB  . LEU B 213  ? 0.4092 0.5308 0.2458 -0.1164 0.0265  0.0845  211  LEU B CB  
10483 C CG  . LEU B 213  ? 0.5132 0.6490 0.3562 -0.1081 0.0308  0.0796  211  LEU B CG  
10484 C CD1 . LEU B 213  ? 0.4731 0.6080 0.3261 -0.1029 0.0298  0.0749  211  LEU B CD1 
10485 C CD2 . LEU B 213  ? 0.5269 0.6832 0.3716 -0.1112 0.0363  0.0821  211  LEU B CD2 
10486 N N   . GLU B 214  ? 0.4377 0.5301 0.2515 -0.1316 0.0189  0.0958  212  GLU B N   
10487 C CA  . GLU B 214  ? 0.4724 0.5519 0.2817 -0.1393 0.0148  0.1002  212  GLU B CA  
10488 C C   . GLU B 214  ? 0.5086 0.5959 0.3165 -0.1449 0.0168  0.1038  212  GLU B C   
10489 O O   . GLU B 214  ? 0.5169 0.6029 0.3264 -0.1521 0.0154  0.1069  212  GLU B O   
10490 C CB  . GLU B 214  ? 0.4774 0.5370 0.2769 -0.1379 0.0098  0.1007  212  GLU B CB  
10491 C CG  . GLU B 214  ? 0.4931 0.5406 0.2982 -0.1324 0.0058  0.0961  212  GLU B CG  
10492 C CD  . GLU B 214  ? 0.5031 0.5305 0.3005 -0.1306 0.0003  0.0962  212  GLU B CD  
10493 O OE1 . GLU B 214  ? 0.5340 0.5571 0.3217 -0.1323 -0.0002 0.0991  212  GLU B OE1 
10494 O OE2 . GLU B 214  ? 0.5002 0.5163 0.3012 -0.1274 -0.0035 0.0933  212  GLU B OE2 
10495 N N   . GLU B 215  ? 0.4972 0.5927 0.3019 -0.1417 0.0202  0.1034  213  GLU B N   
10496 C CA  . GLU B 215  ? 0.4911 0.5954 0.2946 -0.1466 0.0225  0.1068  213  GLU B CA  
10497 C C   . GLU B 215  ? 0.5846 0.7059 0.3981 -0.1497 0.0259  0.1071  213  GLU B C   
10498 O O   . GLU B 215  ? 0.5435 0.6697 0.3568 -0.1561 0.0264  0.1106  213  GLU B O   
10499 C CB  . GLU B 215  ? 0.5366 0.6471 0.3350 -0.1415 0.0257  0.1056  213  GLU B CB  
10500 N N   . LYS B 216  ? 0.5035 0.6341 0.3257 -0.1453 0.0279  0.1034  214  LYS B N   
10501 C CA  . LYS B 216  ? 0.5776 0.7237 0.4098 -0.1479 0.0305  0.1034  214  LYS B CA  
10502 C C   . LYS B 216  ? 0.6295 0.7684 0.4650 -0.1544 0.0267  0.1053  214  LYS B C   
10503 O O   . LYS B 216  ? 0.5323 0.6827 0.3752 -0.1582 0.0280  0.1061  214  LYS B O   
10504 C CB  . LYS B 216  ? 0.5319 0.6913 0.3721 -0.1400 0.0342  0.0986  214  LYS B CB  
10505 C CG  . LYS B 216  ? 0.5746 0.7447 0.4131 -0.1335 0.0386  0.0964  214  LYS B CG  
10506 C CD  . LYS B 216  ? 0.6866 0.8661 0.5319 -0.1249 0.0414  0.0911  214  LYS B CD  
10507 C CE  . LYS B 216  ? 0.7558 0.9442 0.5986 -0.1179 0.0453  0.0885  214  LYS B CE  
10508 N NZ  . LYS B 216  ? 0.8391 1.0266 0.6832 -0.1089 0.0460  0.0832  214  LYS B NZ  
10509 N N   . GLY B 217  ? 0.5163 0.6363 0.3464 -0.1557 0.0219  0.1058  215  GLY B N   
10510 C CA  . GLY B 217  ? 0.4467 0.5579 0.2790 -0.1615 0.0180  0.1074  215  GLY B CA  
10511 C C   . GLY B 217  ? 0.5251 0.6291 0.3607 -0.1576 0.0160  0.1042  215  GLY B C   
10512 O O   . GLY B 217  ? 0.5118 0.6085 0.3494 -0.1619 0.0128  0.1051  215  GLY B O   
10513 N N   . PHE B 218  ? 0.4434 0.5495 0.2796 -0.1496 0.0179  0.1005  216  PHE B N   
10514 C CA  . PHE B 218  ? 0.4757 0.5731 0.3136 -0.1458 0.0156  0.0977  216  PHE B CA  
10515 C C   . PHE B 218  ? 0.4666 0.5416 0.2962 -0.1459 0.0101  0.0983  216  PHE B C   
10516 O O   . PHE B 218  ? 0.4681 0.5359 0.2884 -0.1483 0.0089  0.1013  216  PHE B O   
10517 C CB  . PHE B 218  ? 0.4467 0.5519 0.2898 -0.1355 0.0185  0.0920  216  PHE B CB  
10518 C CG  . PHE B 218  ? 0.4900 0.6160 0.3422 -0.1339 0.0235  0.0905  216  PHE B CG  
10519 C CD1 . PHE B 218  ? 0.4819 0.6232 0.3346 -0.1343 0.0278  0.0916  216  PHE B CD1 
10520 C CD2 . PHE B 218  ? 0.4792 0.6084 0.3413 -0.1302 0.0234  0.0867  216  PHE B CD2 
10521 C CE1 . PHE B 218  ? 0.4687 0.6284 0.3308 -0.1315 0.0320  0.0895  216  PHE B CE1 
10522 C CE2 . PHE B 218  ? 0.5086 0.6567 0.3788 -0.1284 0.0278  0.0853  216  PHE B CE2 
10523 C CZ  . PHE B 218  ? 0.4754 0.6391 0.3455 -0.1291 0.0322  0.0868  216  PHE B CZ  
10524 N N   . SER B 219  ? 0.4275 0.4915 0.2614 -0.1425 0.0065  0.0949  217  SER B N   
10525 C CA  . SER B 219  ? 0.4316 0.4753 0.2599 -0.1398 0.0013  0.0938  217  SER B CA  
10526 C C   . SER B 219  ? 0.4095 0.4508 0.2447 -0.1298 0.0007  0.0873  217  SER B C   
10527 O O   . SER B 219  ? 0.4206 0.4749 0.2643 -0.1256 0.0041  0.0839  217  SER B O   
10528 C CB  . SER B 219  ? 0.4167 0.4463 0.2419 -0.1466 -0.0034 0.0968  217  SER B CB  
10529 O OG  . SER B 219  ? 0.4636 0.4968 0.2978 -0.1466 -0.0035 0.0946  217  SER B OG  
10530 N N   . TYR B 220  ? 0.3950 0.4196 0.2265 -0.1261 -0.0037 0.0855  218  TYR B N   
10531 C CA  . TYR B 220  ? 0.3830 0.4051 0.2201 -0.1167 -0.0043 0.0796  218  TYR B CA  
10532 C C   . TYR B 220  ? 0.3551 0.3611 0.1931 -0.1153 -0.0094 0.0779  218  TYR B C   
10533 O O   . TYR B 220  ? 0.3856 0.3785 0.2169 -0.1199 -0.0132 0.0810  218  TYR B O   
10534 C CB  . TYR B 220  ? 0.3497 0.3700 0.1818 -0.1111 -0.0040 0.0780  218  TYR B CB  
10535 C CG  . TYR B 220  ? 0.3830 0.4204 0.2175 -0.1085 0.0014  0.0769  218  TYR B CG  
10536 C CD1 . TYR B 220  ? 0.4217 0.4687 0.2511 -0.1140 0.0046  0.0812  218  TYR B CD1 
10537 C CD2 . TYR B 220  ? 0.3355 0.3796 0.1773 -0.1005 0.0034  0.0715  218  TYR B CD2 
10538 C CE1 . TYR B 220  ? 0.4047 0.4680 0.2364 -0.1111 0.0097  0.0799  218  TYR B CE1 
10539 C CE2 . TYR B 220  ? 0.4167 0.4760 0.2605 -0.0977 0.0083  0.0702  218  TYR B CE2 
10540 C CZ  . TYR B 220  ? 0.3851 0.4542 0.2239 -0.1028 0.0114  0.0743  218  TYR B CZ  
10541 O OH  . TYR B 220  ? 0.4425 0.5269 0.2831 -0.0994 0.0163  0.0728  218  TYR B OH  
10542 N N   . SER B 221  ? 0.3550 0.3624 0.2011 -0.1086 -0.0092 0.0728  219  SER B N   
10543 C CA  . SER B 221  ? 0.3377 0.3312 0.1854 -0.1048 -0.0135 0.0700  219  SER B CA  
10544 C C   . SER B 221  ? 0.3611 0.3564 0.2132 -0.0957 -0.0127 0.0647  219  SER B C   
10545 O O   . SER B 221  ? 0.3611 0.3681 0.2210 -0.0922 -0.0094 0.0617  219  SER B O   
10546 C CB  . SER B 221  ? 0.3809 0.3744 0.2350 -0.1071 -0.0142 0.0693  219  SER B CB  
10547 O OG  . SER B 221  ? 0.3732 0.3538 0.2286 -0.1029 -0.0181 0.0663  219  SER B OG  
10548 N N   . TYR B 222  ? 0.3718 0.3559 0.2192 -0.0919 -0.0159 0.0637  220  TYR B N   
10549 C CA  . TYR B 222  ? 0.3439 0.3294 0.1946 -0.0837 -0.0153 0.0590  220  TYR B CA  
10550 C C   . TYR B 222  ? 0.3491 0.3290 0.2068 -0.0788 -0.0175 0.0549  220  TYR B C   
10551 O O   . TYR B 222  ? 0.3762 0.3446 0.2326 -0.0800 -0.0213 0.0554  220  TYR B O   
10552 C CB  . TYR B 222  ? 0.3285 0.3059 0.1708 -0.0820 -0.0176 0.0599  220  TYR B CB  
10553 C CG  . TYR B 222  ? 0.3363 0.3206 0.1720 -0.0863 -0.0150 0.0637  220  TYR B CG  
10554 C CD1 . TYR B 222  ? 0.3734 0.3712 0.2111 -0.0838 -0.0105 0.0622  220  TYR B CD1 
10555 C CD2 . TYR B 222  ? 0.3513 0.3290 0.1786 -0.0932 -0.0168 0.0689  220  TYR B CD2 
10556 C CE1 . TYR B 222  ? 0.3672 0.3725 0.1991 -0.0876 -0.0078 0.0656  220  TYR B CE1 
10557 C CE2 . TYR B 222  ? 0.3891 0.3740 0.2103 -0.0976 -0.0141 0.0726  220  TYR B CE2 
10558 C CZ  . TYR B 222  ? 0.3848 0.3839 0.2084 -0.0946 -0.0095 0.0709  220  TYR B CZ  
10559 O OH  . TYR B 222  ? 0.4028 0.4100 0.2206 -0.0987 -0.0065 0.0745  220  TYR B OH  
10560 N N   . ASP B 223  ? 0.3484 0.3364 0.2132 -0.0731 -0.0151 0.0507  221  ASP B N   
10561 C CA  . ASP B 223  ? 0.3879 0.3734 0.2603 -0.0681 -0.0162 0.0465  221  ASP B CA  
10562 C C   . ASP B 223  ? 0.4174 0.4003 0.2899 -0.0613 -0.0171 0.0430  221  ASP B C   
10563 O O   . ASP B 223  ? 0.4233 0.4152 0.2977 -0.0581 -0.0141 0.0411  221  ASP B O   
10564 C CB  . ASP B 223  ? 0.3992 0.3971 0.2799 -0.0678 -0.0125 0.0449  221  ASP B CB  
10565 C CG  . ASP B 223  ? 0.4461 0.4437 0.3347 -0.0618 -0.0128 0.0403  221  ASP B CG  
10566 O OD1 . ASP B 223  ? 0.4564 0.4432 0.3449 -0.0592 -0.0163 0.0387  221  ASP B OD1 
10567 O OD2 . ASP B 223  ? 0.5063 0.5146 0.4011 -0.0595 -0.0096 0.0382  221  ASP B OD2 
10568 N N   . MET B 224  ? 0.3970 0.3677 0.2672 -0.0591 -0.0212 0.0422  222  MET B N   
10569 C CA  . MET B 224  ? 0.4362 0.4039 0.3059 -0.0533 -0.0226 0.0394  222  MET B CA  
10570 C C   . MET B 224  ? 0.4655 0.4368 0.3439 -0.0475 -0.0218 0.0346  222  MET B C   
10571 O O   . MET B 224  ? 0.6120 0.5793 0.4909 -0.0427 -0.0237 0.0319  222  MET B O   
10572 C CB  . MET B 224  ? 0.4971 0.4510 0.3610 -0.0530 -0.0275 0.0405  222  MET B CB  
10573 C CG  . MET B 224  ? 0.4939 0.4429 0.3480 -0.0586 -0.0287 0.0454  222  MET B CG  
10574 S SD  . MET B 224  ? 0.5078 0.4658 0.3560 -0.0598 -0.0253 0.0471  222  MET B SD  
10575 C CE  . MET B 224  ? 0.4751 0.4289 0.3226 -0.0525 -0.0276 0.0434  222  MET B CE  
10576 N N   . LEU B 225  ? 0.5539 0.5327 0.4392 -0.0480 -0.0192 0.0336  223  LEU B N   
10577 C CA  . LEU B 225  ? 0.4086 0.3930 0.3018 -0.0430 -0.0175 0.0294  223  LEU B CA  
10578 C C   . LEU B 225  ? 0.7041 0.6802 0.6008 -0.0388 -0.0208 0.0266  223  LEU B C   
10579 O O   . LEU B 225  ? 0.8022 0.7799 0.7027 -0.0340 -0.0206 0.0232  223  LEU B O   
10580 C CB  . LEU B 225  ? 0.4610 0.4532 0.3537 -0.0397 -0.0149 0.0276  223  LEU B CB  
10581 C CG  . LEU B 225  ? 0.5357 0.5396 0.4281 -0.0426 -0.0106 0.0294  223  LEU B CG  
10582 C CD1 . LEU B 225  ? 0.5185 0.5297 0.4101 -0.0387 -0.0080 0.0272  223  LEU B CD1 
10583 C CD2 . LEU B 225  ? 0.4862 0.4966 0.3858 -0.0441 -0.0086 0.0291  223  LEU B CD2 
10584 N N   . GLY B 226  ? 0.6102 0.5772 0.5054 -0.0408 -0.0239 0.0280  224  GLY B N   
10585 C CA  . GLY B 226  ? 0.5506 0.5105 0.4496 -0.0372 -0.0268 0.0255  224  GLY B CA  
10586 C C   . GLY B 226  ? 0.4759 0.4368 0.3804 -0.0384 -0.0262 0.0250  224  GLY B C   
10587 O O   . GLY B 226  ? 0.4685 0.4297 0.3711 -0.0433 -0.0257 0.0277  224  GLY B O   
10588 N N   . GLU B 227  ? 0.5090 0.4706 0.4203 -0.0342 -0.0263 0.0216  225  GLU B N   
10589 C CA  . GLU B 227  ? 0.4739 0.4352 0.3901 -0.0349 -0.0262 0.0209  225  GLU B CA  
10590 C C   . GLU B 227  ? 0.4045 0.3648 0.3270 -0.0297 -0.0270 0.0173  225  GLU B C   
10591 O O   . GLU B 227  ? 0.4172 0.3795 0.3414 -0.0259 -0.0268 0.0152  225  GLU B O   
10592 C CB  . GLU B 227  ? 0.5085 0.4798 0.4281 -0.0376 -0.0226 0.0216  225  GLU B CB  
10593 C CG  . GLU B 227  ? 0.4387 0.4194 0.3642 -0.0340 -0.0195 0.0188  225  GLU B CG  
10594 C CD  . GLU B 227  ? 0.5975 0.5881 0.5257 -0.0367 -0.0161 0.0198  225  GLU B CD  
10595 O OE1 . GLU B 227  ? 0.4979 0.4944 0.4229 -0.0389 -0.0141 0.0216  225  GLU B OE1 
10596 O OE2 . GLU B 227  ? 0.4731 0.4660 0.4066 -0.0365 -0.0154 0.0187  225  GLU B OE2 
10597 N N   . ALA B 228  ? 0.3595 0.3165 0.2852 -0.0297 -0.0280 0.0166  226  ALA B N   
10598 C CA  . ALA B 228  ? 0.3434 0.3007 0.2757 -0.0253 -0.0283 0.0133  226  ALA B CA  
10599 C C   . ALA B 228  ? 0.3935 0.3464 0.3255 -0.0211 -0.0306 0.0116  226  ALA B C   
10600 O O   . ALA B 228  ? 0.4123 0.3697 0.3484 -0.0178 -0.0296 0.0092  226  ALA B O   
10601 C CB  . ALA B 228  ? 0.3773 0.3446 0.3158 -0.0241 -0.0247 0.0115  226  ALA B CB  
10602 N N   . ALA B 229  ? 0.3387 0.2828 0.2655 -0.0215 -0.0340 0.0129  227  ALA B N   
10603 C CA  . ALA B 229  ? 0.3293 0.2688 0.2563 -0.0174 -0.0368 0.0113  227  ALA B CA  
10604 C C   . ALA B 229  ? 0.2797 0.2211 0.2143 -0.0135 -0.0366 0.0082  227  ALA B C   
10605 O O   . ALA B 229  ? 0.3396 0.2802 0.2770 -0.0139 -0.0364 0.0077  227  ALA B O   
10606 C CB  . ALA B 229  ? 0.3243 0.2534 0.2450 -0.0181 -0.0406 0.0132  227  ALA B CB  
10607 N N   . THR B 230  ? 0.3177 0.2618 0.2555 -0.0100 -0.0368 0.0060  228  THR B N   
10608 C CA  . THR B 230  ? 0.3141 0.2603 0.2590 -0.0064 -0.0368 0.0032  228  THR B CA  
10609 C C   . THR B 230  ? 0.3171 0.2572 0.2620 -0.0034 -0.0404 0.0023  228  THR B C   
10610 O O   . THR B 230  ? 0.3047 0.2445 0.2543 -0.0011 -0.0409 0.0007  228  THR B O   
10611 C CB  . THR B 230  ? 0.3179 0.2711 0.2669 -0.0046 -0.0348 0.0012  228  THR B CB  
10612 O OG1 . THR B 230  ? 0.4001 0.3592 0.3488 -0.0070 -0.0315 0.0020  228  THR B OG1 
10613 C CG2 . THR B 230  ? 0.3251 0.2810 0.2816 -0.0016 -0.0344 -0.0014 228  THR B CG2 
10614 N N   . THR B 231  ? 0.3059 0.2414 0.2454 -0.0031 -0.0430 0.0035  229  THR B N   
10615 C CA  . THR B 231  ? 0.2650 0.1950 0.2041 0.0001  -0.0466 0.0028  229  THR B CA  
10616 C C   . THR B 231  ? 0.3155 0.2368 0.2466 -0.0015 -0.0495 0.0054  229  THR B C   
10617 O O   . THR B 231  ? 0.2858 0.2060 0.2113 -0.0053 -0.0486 0.0078  229  THR B O   
10618 C CB  . THR B 231  ? 0.2936 0.2264 0.2343 0.0026  -0.0477 0.0013  229  THR B CB  
10619 O OG1 . THR B 231  ? 0.3347 0.2661 0.2686 0.0007  -0.0481 0.0031  229  THR B OG1 
10620 C CG2 . THR B 231  ? 0.2957 0.2367 0.2433 0.0036  -0.0448 -0.0010 229  THR B CG2 
10621 N N   . ALA B 232  ? 0.2878 0.2033 0.2184 0.0015  -0.0530 0.0049  230  ALA B N   
10622 C CA  . ALA B 232  ? 0.3295 0.2357 0.2520 0.0006  -0.0563 0.0073  230  ALA B CA  
10623 C C   . ALA B 232  ? 0.3540 0.2600 0.2706 -0.0011 -0.0568 0.0091  230  ALA B C   
10624 O O   . ALA B 232  ? 0.3457 0.2462 0.2547 -0.0043 -0.0576 0.0120  230  ALA B O   
10625 C CB  . ALA B 232  ? 0.3302 0.2311 0.2536 0.0051  -0.0600 0.0060  230  ALA B CB  
10626 N N   . ALA B 233  ? 0.3215 0.2330 0.2411 0.0009  -0.0564 0.0075  231  ALA B N   
10627 C CA  . ALA B 233  ? 0.3350 0.2463 0.2488 -0.0003 -0.0570 0.0089  231  ALA B CA  
10628 C C   . ALA B 233  ? 0.3456 0.2602 0.2559 -0.0048 -0.0535 0.0108  231  ALA B C   
10629 O O   . ALA B 233  ? 0.3477 0.2593 0.2505 -0.0073 -0.0542 0.0134  231  ALA B O   
10630 C CB  . ALA B 233  ? 0.3202 0.2370 0.2383 0.0027  -0.0572 0.0064  231  ALA B CB  
10631 N N   . ASP B 234  ? 0.3000 0.2213 0.2158 -0.0059 -0.0499 0.0097  232  ASP B N   
10632 C CA  . ASP B 234  ? 0.3060 0.2314 0.2193 -0.0100 -0.0465 0.0115  232  ASP B CA  
10633 C C   . ASP B 234  ? 0.3174 0.2363 0.2241 -0.0139 -0.0475 0.0148  232  ASP B C   
10634 O O   . ASP B 234  ? 0.3355 0.2544 0.2361 -0.0174 -0.0467 0.0174  232  ASP B O   
10635 C CB  . ASP B 234  ? 0.3235 0.2562 0.2441 -0.0102 -0.0430 0.0097  232  ASP B CB  
10636 C CG  . ASP B 234  ? 0.4053 0.3446 0.3317 -0.0072 -0.0415 0.0068  232  ASP B CG  
10637 O OD1 . ASP B 234  ? 0.4084 0.3486 0.3327 -0.0059 -0.0422 0.0062  232  ASP B OD1 
10638 O OD2 . ASP B 234  ? 0.4017 0.3455 0.3347 -0.0063 -0.0395 0.0050  232  ASP B OD2 
10639 N N   . ALA B 235  ? 0.2928 0.2065 0.2008 -0.0137 -0.0491 0.0148  233  ALA B N   
10640 C CA  . ALA B 235  ? 0.3026 0.2096 0.2045 -0.0177 -0.0500 0.0178  233  ALA B CA  
10641 C C   . ALA B 235  ? 0.3425 0.2412 0.2357 -0.0184 -0.0534 0.0203  233  ALA B C   
10642 O O   . ALA B 235  ? 0.3343 0.2299 0.2207 -0.0229 -0.0534 0.0236  233  ALA B O   
10643 C CB  . ALA B 235  ? 0.3174 0.2197 0.2222 -0.0165 -0.0513 0.0168  233  ALA B CB  
10644 N N   . GLU B 236  ? 0.3261 0.2212 0.2193 -0.0141 -0.0565 0.0190  234  GLU B N   
10645 C CA  . GLU B 236  ? 0.3478 0.2351 0.2326 -0.0144 -0.0599 0.0213  234  GLU B CA  
10646 C C   . GLU B 236  ? 0.3421 0.2336 0.2222 -0.0171 -0.0582 0.0232  234  GLU B C   
10647 O O   . GLU B 236  ? 0.3565 0.2425 0.2281 -0.0203 -0.0594 0.0265  234  GLU B O   
10648 C CB  . GLU B 236  ? 0.3573 0.2414 0.2441 -0.0088 -0.0635 0.0193  234  GLU B CB  
10649 C CG  . GLU B 236  ? 0.3985 0.2729 0.2766 -0.0085 -0.0678 0.0217  234  GLU B CG  
10650 C CD  . GLU B 236  ? 0.5671 0.4392 0.4475 -0.0028 -0.0714 0.0195  234  GLU B CD  
10651 O OE1 . GLU B 236  ? 0.6158 0.4942 0.5049 0.0007  -0.0705 0.0162  234  GLU B OE1 
10652 O OE2 . GLU B 236  ? 0.5781 0.4425 0.4518 -0.0018 -0.0752 0.0213  234  GLU B OE2 
10653 N N   . ARG B 237  ? 0.3239 0.2250 0.2090 -0.0159 -0.0552 0.0210  235  ARG B N   
10654 C CA  . ARG B 237  ? 0.3555 0.2611 0.2362 -0.0181 -0.0532 0.0224  235  ARG B CA  
10655 C C   . ARG B 237  ? 0.3432 0.2510 0.2204 -0.0237 -0.0503 0.0254  235  ARG B C   
10656 O O   . ARG B 237  ? 0.3570 0.2630 0.2265 -0.0270 -0.0504 0.0284  235  ARG B O   
10657 C CB  . ARG B 237  ? 0.3523 0.2672 0.2390 -0.0154 -0.0507 0.0192  235  ARG B CB  
10658 C CG  . ARG B 237  ? 0.3981 0.3176 0.2799 -0.0171 -0.0487 0.0203  235  ARG B CG  
10659 C CD  . ARG B 237  ? 0.4955 0.4244 0.3830 -0.0152 -0.0455 0.0173  235  ARG B CD  
10660 N NE  . ARG B 237  ? 0.5616 0.4942 0.4432 -0.0166 -0.0438 0.0184  235  ARG B NE  
10661 C CZ  . ARG B 237  ? 0.5638 0.5022 0.4470 -0.0144 -0.0422 0.0160  235  ARG B CZ  
10662 N NH1 . ARG B 237  ? 0.5945 0.5359 0.4850 -0.0109 -0.0420 0.0125  235  ARG B NH1 
10663 N NH2 . ARG B 237  ? 0.4958 0.4369 0.3726 -0.0156 -0.0407 0.0171  235  ARG B NH2 
10664 N N   . TYR B 238  ? 0.3246 0.2368 0.2074 -0.0251 -0.0477 0.0246  236  TYR B N   
10665 C CA  . TYR B 238  ? 0.3187 0.2339 0.1990 -0.0306 -0.0450 0.0274  236  TYR B CA  
10666 C C   . TYR B 238  ? 0.3402 0.2454 0.2123 -0.0344 -0.0479 0.0312  236  TYR B C   
10667 O O   . TYR B 238  ? 0.3237 0.2298 0.1898 -0.0392 -0.0466 0.0345  236  TYR B O   
10668 C CB  . TYR B 238  ? 0.3160 0.2364 0.2038 -0.0310 -0.0425 0.0258  236  TYR B CB  
10669 C CG  . TYR B 238  ? 0.3560 0.2872 0.2512 -0.0284 -0.0390 0.0227  236  TYR B CG  
10670 C CD1 . TYR B 238  ? 0.4340 0.3720 0.3277 -0.0283 -0.0367 0.0226  236  TYR B CD1 
10671 C CD2 . TYR B 238  ? 0.3512 0.2851 0.2543 -0.0259 -0.0382 0.0199  236  TYR B CD2 
10672 C CE1 . TYR B 238  ? 0.5003 0.4470 0.4003 -0.0257 -0.0338 0.0197  236  TYR B CE1 
10673 C CE2 . TYR B 238  ? 0.4191 0.3619 0.3286 -0.0236 -0.0352 0.0173  236  TYR B CE2 
10674 C CZ  . TYR B 238  ? 0.5447 0.4936 0.4526 -0.0234 -0.0331 0.0171  236  TYR B CZ  
10675 O OH  . TYR B 238  ? 0.4849 0.4417 0.3986 -0.0208 -0.0304 0.0144  236  TYR B OH  
10676 N N   . TYR B 239  ? 0.3269 0.2224 0.1981 -0.0324 -0.0517 0.0308  237  TYR B N   
10677 C CA  . TYR B 239  ? 0.3266 0.2110 0.1892 -0.0356 -0.0550 0.0343  237  TYR B CA  
10678 C C   . TYR B 239  ? 0.3605 0.2420 0.2148 -0.0367 -0.0563 0.0369  237  TYR B C   
10679 O O   . TYR B 239  ? 0.3655 0.2437 0.2123 -0.0419 -0.0564 0.0408  237  TYR B O   
10680 C CB  . TYR B 239  ? 0.3496 0.2241 0.2129 -0.0318 -0.0591 0.0329  237  TYR B CB  
10681 C CG  . TYR B 239  ? 0.3861 0.2476 0.2397 -0.0340 -0.0632 0.0362  237  TYR B CG  
10682 C CD1 . TYR B 239  ? 0.4067 0.2627 0.2562 -0.0392 -0.0634 0.0389  237  TYR B CD1 
10683 C CD2 . TYR B 239  ? 0.4987 0.3531 0.3470 -0.0311 -0.0669 0.0368  237  TYR B CD2 
10684 C CE1 . TYR B 239  ? 0.3832 0.2264 0.2233 -0.0414 -0.0674 0.0421  237  TYR B CE1 
10685 C CE2 . TYR B 239  ? 0.5564 0.3983 0.3955 -0.0330 -0.0708 0.0400  237  TYR B CE2 
10686 C CZ  . TYR B 239  ? 0.4992 0.3352 0.3341 -0.0382 -0.0710 0.0426  237  TYR B CZ  
10687 O OH  . TYR B 239  ? 0.5666 0.3892 0.3916 -0.0402 -0.0751 0.0459  237  TYR B OH  
10688 N N   . ARG B 240  ? 0.3690 0.2515 0.2242 -0.0320 -0.0576 0.0349  238  ARG B N   
10689 C CA  . ARG B 240  ? 0.3936 0.2731 0.2406 -0.0327 -0.0592 0.0372  238  ARG B CA  
10690 C C   . ARG B 240  ? 0.3535 0.2416 0.1979 -0.0367 -0.0551 0.0390  238  ARG B C   
10691 O O   . ARG B 240  ? 0.3807 0.2654 0.2163 -0.0401 -0.0558 0.0425  238  ARG B O   
10692 C CB  . ARG B 240  ? 0.3893 0.2688 0.2384 -0.0268 -0.0614 0.0343  238  ARG B CB  
10693 C CG  . ARG B 240  ? 0.3848 0.2554 0.2350 -0.0226 -0.0660 0.0330  238  ARG B CG  
10694 C CD  . ARG B 240  ? 0.4700 0.3282 0.3104 -0.0246 -0.0699 0.0367  238  ARG B CD  
10695 N NE  . ARG B 240  ? 0.5219 0.3717 0.3637 -0.0205 -0.0740 0.0354  238  ARG B NE  
10696 C CZ  . ARG B 240  ? 0.6395 0.4773 0.4742 -0.0213 -0.0778 0.0379  238  ARG B CZ  
10697 N NH1 . ARG B 240  ? 0.5619 0.3939 0.3871 -0.0266 -0.0782 0.0422  238  ARG B NH1 
10698 N NH2 . ARG B 240  ? 0.6921 0.5233 0.5288 -0.0166 -0.0813 0.0361  238  ARG B NH2 
10699 N N   . ASP B 241  ? 0.3666 0.2658 0.2182 -0.0364 -0.0509 0.0367  239  ASP B N   
10700 C CA  . ASP B 241  ? 0.3807 0.2890 0.2303 -0.0398 -0.0468 0.0382  239  ASP B CA  
10701 C C   . ASP B 241  ? 0.3461 0.2535 0.1915 -0.0465 -0.0455 0.0423  239  ASP B C   
10702 O O   . ASP B 241  ? 0.3849 0.2948 0.2239 -0.0504 -0.0441 0.0454  239  ASP B O   
10703 C CB  . ASP B 241  ? 0.3825 0.3023 0.2411 -0.0373 -0.0428 0.0346  239  ASP B CB  
10704 C CG  . ASP B 241  ? 0.4685 0.3907 0.3298 -0.0317 -0.0435 0.0311  239  ASP B CG  
10705 O OD1 . ASP B 241  ? 0.5121 0.4284 0.3677 -0.0302 -0.0465 0.0316  239  ASP B OD1 
10706 O OD2 . ASP B 241  ? 0.5668 0.4964 0.4355 -0.0291 -0.0410 0.0278  239  ASP B OD2 
10707 N N   . TYR B 242  ? 0.3712 0.2751 0.2198 -0.0481 -0.0462 0.0424  240  TYR B N   
10708 C CA  . TYR B 242  ? 0.3823 0.2837 0.2263 -0.0547 -0.0459 0.0464  240  TYR B CA  
10709 C C   . TYR B 242  ? 0.3855 0.2756 0.2187 -0.0576 -0.0495 0.0504  240  TYR B C   
10710 O O   . TYR B 242  ? 0.3568 0.2477 0.1836 -0.0634 -0.0484 0.0544  240  TYR B O   
10711 C CB  . TYR B 242  ? 0.3422 0.2399 0.1909 -0.0553 -0.0468 0.0454  240  TYR B CB  
10712 C CG  . TYR B 242  ? 0.3229 0.2316 0.1810 -0.0547 -0.0429 0.0428  240  TYR B CG  
10713 C CD1 . TYR B 242  ? 0.3540 0.2752 0.2144 -0.0569 -0.0384 0.0432  240  TYR B CD1 
10714 C CD2 . TYR B 242  ? 0.3224 0.2289 0.1870 -0.0517 -0.0439 0.0399  240  TYR B CD2 
10715 C CE1 . TYR B 242  ? 0.3683 0.2992 0.2373 -0.0560 -0.0351 0.0408  240  TYR B CE1 
10716 C CE2 . TYR B 242  ? 0.3465 0.2625 0.2193 -0.0512 -0.0406 0.0376  240  TYR B CE2 
10717 C CZ  . TYR B 242  ? 0.3709 0.2988 0.2459 -0.0533 -0.0363 0.0381  240  TYR B CZ  
10718 O OH  . TYR B 242  ? 0.3611 0.2979 0.2443 -0.0524 -0.0333 0.0358  240  TYR B OH  
10719 N N   . GLU B 243  ? 0.3581 0.2377 0.1892 -0.0535 -0.0540 0.0494  241  GLU B N   
10720 C CA  . GLU B 243  ? 0.3696 0.2373 0.1902 -0.0555 -0.0579 0.0530  241  GLU B CA  
10721 C C   . GLU B 243  ? 0.3935 0.2653 0.2076 -0.0573 -0.0566 0.0553  241  GLU B C   
10722 O O   . GLU B 243  ? 0.3914 0.2589 0.1968 -0.0627 -0.0571 0.0599  241  GLU B O   
10723 C CB  . GLU B 243  ? 0.3827 0.2406 0.2034 -0.0495 -0.0627 0.0508  241  GLU B CB  
10724 C CG  . GLU B 243  ? 0.4499 0.2947 0.2600 -0.0505 -0.0673 0.0542  241  GLU B CG  
10725 C CD  . GLU B 243  ? 0.5274 0.3647 0.3384 -0.0436 -0.0717 0.0516  241  GLU B CD  
10726 O OE1 . GLU B 243  ? 0.5153 0.3597 0.3339 -0.0384 -0.0708 0.0476  241  GLU B OE1 
10727 O OE2 . GLU B 243  ? 0.5644 0.3888 0.3686 -0.0434 -0.0762 0.0536  241  GLU B OE2 
10728 N N   . SER B 244  ? 0.3625 0.2423 0.1805 -0.0528 -0.0548 0.0523  242  SER B N   
10729 C CA  . SER B 244  ? 0.3673 0.2512 0.1791 -0.0539 -0.0535 0.0540  242  SER B CA  
10730 C C   . SER B 244  ? 0.3750 0.2681 0.1852 -0.0599 -0.0489 0.0568  242  SER B C   
10731 O O   . SER B 244  ? 0.3778 0.2699 0.1793 -0.0640 -0.0486 0.0607  242  SER B O   
10732 C CB  . SER B 244  ? 0.4007 0.2915 0.2177 -0.0478 -0.0525 0.0497  242  SER B CB  
10733 O OG  . SER B 244  ? 0.4826 0.3783 0.2938 -0.0487 -0.0508 0.0509  242  SER B OG  
10734 N N   . ALA B 245  ? 0.3896 0.2918 0.2079 -0.0607 -0.0453 0.0551  243  ALA B N   
10735 C CA  . ALA B 245  ? 0.3577 0.2698 0.1755 -0.0663 -0.0409 0.0576  243  ALA B CA  
10736 C C   . ALA B 245  ? 0.3977 0.3028 0.2084 -0.0735 -0.0423 0.0628  243  ALA B C   
10737 O O   . ALA B 245  ? 0.3925 0.3024 0.1978 -0.0788 -0.0400 0.0665  243  ALA B O   
10738 C CB  . ALA B 245  ? 0.3586 0.2812 0.1868 -0.0652 -0.0372 0.0546  243  ALA B CB  
10739 N N   . ILE B 246  ? 0.3726 0.2665 0.1830 -0.0740 -0.0460 0.0632  244  ILE B N   
10740 C CA  . ILE B 246  ? 0.3996 0.2853 0.2027 -0.0811 -0.0479 0.0681  244  ILE B CA  
10741 C C   . ILE B 246  ? 0.4129 0.2915 0.2045 -0.0835 -0.0500 0.0721  244  ILE B C   
10742 O O   . ILE B 246  ? 0.4398 0.3189 0.2250 -0.0905 -0.0490 0.0768  244  ILE B O   
10743 C CB  . ILE B 246  ? 0.3866 0.2602 0.1910 -0.0802 -0.0519 0.0672  244  ILE B CB  
10744 C CG1 . ILE B 246  ? 0.4136 0.2949 0.2281 -0.0799 -0.0493 0.0643  244  ILE B CG1 
10745 C CG2 . ILE B 246  ? 0.4247 0.2866 0.2194 -0.0869 -0.0549 0.0723  244  ILE B CG2 
10746 C CD1 . ILE B 246  ? 0.4306 0.3011 0.2472 -0.0781 -0.0529 0.0626  244  ILE B CD1 
10747 N N   . HIS B 247  ? 0.4166 0.2891 0.2054 -0.0780 -0.0530 0.0706  245  HIS B N   
10748 C CA  . HIS B 247  ? 0.4212 0.2875 0.1989 -0.0800 -0.0549 0.0743  245  HIS B CA  
10749 C C   . HIS B 247  ? 0.4139 0.2927 0.1892 -0.0832 -0.0502 0.0762  245  HIS B C   
10750 O O   . HIS B 247  ? 0.4523 0.3290 0.2188 -0.0891 -0.0501 0.0811  245  HIS B O   
10751 C CB  . HIS B 247  ? 0.4256 0.2849 0.2017 -0.0730 -0.0588 0.0718  245  HIS B CB  
10752 C CG  . HIS B 247  ? 0.4227 0.2674 0.1976 -0.0706 -0.0642 0.0714  245  HIS B CG  
10753 N ND1 . HIS B 247  ? 0.4733 0.3045 0.2386 -0.0747 -0.0680 0.0758  245  HIS B ND1 
10754 C CD2 . HIS B 247  ? 0.4401 0.2816 0.2219 -0.0643 -0.0665 0.0671  245  HIS B CD2 
10755 C CE1 . HIS B 247  ? 0.5078 0.3280 0.2741 -0.0707 -0.0725 0.0740  245  HIS B CE1 
10756 N NE2 . HIS B 247  ? 0.4972 0.3238 0.2737 -0.0644 -0.0715 0.0688  245  HIS B NE2 
10757 N N   . ALA B 248  ? 0.4014 0.2935 0.1845 -0.0795 -0.0461 0.0724  246  ALA B N   
10758 C CA  . ALA B 248  ? 0.4012 0.3058 0.1822 -0.0817 -0.0415 0.0737  246  ALA B CA  
10759 C C   . ALA B 248  ? 0.4236 0.3354 0.2048 -0.0893 -0.0380 0.0773  246  ALA B C   
10760 O O   . ALA B 248  ? 0.4464 0.3620 0.2205 -0.0943 -0.0361 0.0814  246  ALA B O   
10761 C CB  . ALA B 248  ? 0.3990 0.3150 0.1883 -0.0755 -0.0383 0.0684  246  ALA B CB  
10762 N N   . ILE B 249  ? 0.4114 0.3257 0.2006 -0.0902 -0.0372 0.0758  247  ILE B N   
10763 C CA  . ILE B 249  ? 0.4322 0.3537 0.2224 -0.0974 -0.0341 0.0790  247  ILE B CA  
10764 C C   . ILE B 249  ? 0.4413 0.3516 0.2218 -0.1047 -0.0372 0.0847  247  ILE B C   
10765 O O   . ILE B 249  ? 0.4497 0.3657 0.2257 -0.1116 -0.0347 0.0891  247  ILE B O   
10766 C CB  . ILE B 249  ? 0.3896 0.3152 0.1904 -0.0963 -0.0331 0.0758  247  ILE B CB  
10767 C CG1 . ILE B 249  ? 0.3779 0.3155 0.1879 -0.0897 -0.0296 0.0706  247  ILE B CG1 
10768 C CG2 . ILE B 249  ? 0.4327 0.3644 0.2342 -0.1044 -0.0307 0.0795  247  ILE B CG2 
10769 C CD1 . ILE B 249  ? 0.3939 0.3319 0.2139 -0.0863 -0.0300 0.0666  247  ILE B CD1 
10770 N N   . GLY B 250  ? 0.4455 0.3396 0.2221 -0.1033 -0.0426 0.0848  248  GLY B N   
10771 C CA  . GLY B 250  ? 0.4385 0.3201 0.2054 -0.1099 -0.0461 0.0902  248  GLY B CA  
10772 C C   . GLY B 250  ? 0.5247 0.4048 0.2807 -0.1131 -0.0461 0.0946  248  GLY B C   
10773 O O   . GLY B 250  ? 0.5146 0.3927 0.2635 -0.1211 -0.0460 0.1000  248  GLY B O   
10774 N N   . LYS B 251  ? 0.4740 0.3549 0.2282 -0.1072 -0.0464 0.0925  249  LYS B N   
10775 C CA  . LYS B 251  ? 0.5069 0.3872 0.2506 -0.1100 -0.0461 0.0965  249  LYS B CA  
10776 C C   . LYS B 251  ? 0.4974 0.3944 0.2418 -0.1147 -0.0401 0.0985  249  LYS B C   
10777 O O   . LYS B 251  ? 0.5249 0.4217 0.2606 -0.1214 -0.0394 0.1039  249  LYS B O   
10778 C CB  . LYS B 251  ? 0.5359 0.4135 0.2777 -0.1022 -0.0480 0.0933  249  LYS B CB  
10779 N N   . ALA B 252  ? 0.4678 0.3793 0.2225 -0.1114 -0.0356 0.0944  250  ALA B N   
10780 C CA  . ALA B 252  ? 0.4838 0.4123 0.2402 -0.1152 -0.0297 0.0959  250  ALA B CA  
10781 C C   . ALA B 252  ? 0.4959 0.4264 0.2518 -0.1243 -0.0286 0.1005  250  ALA B C   
10782 O O   . ALA B 252  ? 0.5241 0.4641 0.2763 -0.1302 -0.0251 0.1045  250  ALA B O   
10783 C CB  . ALA B 252  ? 0.4840 0.4264 0.2517 -0.1091 -0.0257 0.0902  250  ALA B CB  
10784 N N   . SER B 253  ? 0.4794 0.4018 0.2392 -0.1256 -0.0314 0.1000  251  SER B N   
10785 C CA  . SER B 253  ? 0.4770 0.3996 0.2357 -0.1347 -0.0311 0.1044  251  SER B CA  
10786 C C   . SER B 253  ? 0.5102 0.4246 0.2562 -0.1421 -0.0330 0.1110  251  SER B C   
10787 O O   . SER B 253  ? 0.5374 0.4602 0.2843 -0.1488 -0.0303 0.1140  251  SER B O   
10788 C CB  . SER B 253  ? 0.4844 0.3961 0.2475 -0.1344 -0.0349 0.1027  251  SER B CB  
10789 O OG  . SER B 253  ? 0.5052 0.4166 0.2667 -0.1434 -0.0349 0.1070  251  SER B OG  
10790 N N   . ALA B 254  ? 0.4978 0.3970 0.2354 -0.1396 -0.0377 0.1118  252  ALA B N   
10791 C CA  . ALA B 254  ? 0.5767 0.4690 0.3062 -0.1435 -0.0394 0.1155  252  ALA B CA  
10792 C C   . ALA B 254  ? 0.5729 0.4620 0.3028 -0.1517 -0.0403 0.1187  252  ALA B C   
10793 O O   . ALA B 254  ? 0.5951 0.4893 0.3225 -0.1573 -0.0385 0.1220  252  ALA B O   
10794 C CB  . ALA B 254  ? 0.5841 0.4898 0.3116 -0.1434 -0.0348 0.1165  252  ALA B CB  
10795 N N   . GLY B 255  ? 0.5991 0.4796 0.3321 -0.1524 -0.0433 0.1177  253  GLY B N   
10796 C CA  . GLY B 255  ? 0.5939 0.4686 0.3263 -0.1597 -0.0453 0.1202  253  GLY B CA  
10797 C C   . GLY B 255  ? 0.6131 0.5038 0.3530 -0.1657 -0.0408 0.1211  253  GLY B C   
10798 O O   . GLY B 255  ? 0.6586 0.5461 0.3976 -0.1725 -0.0422 0.1235  253  GLY B O   
10799 N N   . ARG B 256  ? 0.5337 0.4415 0.2808 -0.1632 -0.0356 0.1190  254  ARG B N   
10800 C CA  . ARG B 256  ? 0.5787 0.5031 0.3335 -0.1682 -0.0312 0.1196  254  ARG B CA  
10801 C C   . ARG B 256  ? 0.5912 0.5116 0.3513 -0.1709 -0.0332 0.1186  254  ARG B C   
10802 O O   . ARG B 256  ? 0.5821 0.5141 0.3480 -0.1762 -0.0306 0.1196  254  ARG B O   
10803 C CB  . ARG B 256  ? 0.5058 0.4491 0.2670 -0.1639 -0.0254 0.1172  254  ARG B CB  
10804 C CG  . ARG B 256  ? 0.5531 0.5072 0.3112 -0.1643 -0.0216 0.1189  254  ARG B CG  
10805 C CD  . ARG B 256  ? 0.5512 0.5232 0.3154 -0.1594 -0.0160 0.1160  254  ARG B CD  
10806 N NE  . ARG B 256  ? 0.5690 0.5352 0.3310 -0.1513 -0.0173 0.1127  254  ARG B NE  
10807 C CZ  . ARG B 256  ? 0.5121 0.4901 0.2791 -0.1458 -0.0137 0.1093  254  ARG B CZ  
10808 N NH1 . ARG B 256  ? 0.5432 0.5394 0.3181 -0.1468 -0.0085 0.1084  254  ARG B NH1 
10809 N NH2 . ARG B 256  ? 0.5504 0.5223 0.3179 -0.1371 -0.0155 0.1048  254  ARG B NH2 
10810 N N   . GLY B 257  ? 0.5529 0.4578 0.3112 -0.1671 -0.0377 0.1167  255  GLY B N   
10811 C CA  . GLY B 257  ? 0.5296 0.4295 0.2923 -0.1692 -0.0399 0.1155  255  GLY B CA  
10812 C C   . GLY B 257  ? 0.5081 0.4200 0.2800 -0.1658 -0.0365 0.1124  255  GLY B C   
10813 O O   . GLY B 257  ? 0.5273 0.4525 0.3028 -0.1618 -0.0322 0.1109  255  GLY B O   
10814 N N   . ILE B 258  ? 0.4873 0.3946 0.2633 -0.1674 -0.0384 0.1112  256  ILE B N   
10815 C CA  . ILE B 258  ? 0.4897 0.4059 0.2765 -0.1617 -0.0362 0.1062  256  ILE B CA  
10816 C C   . ILE B 258  ? 0.4754 0.4131 0.2705 -0.1647 -0.0305 0.1064  256  ILE B C   
10817 O O   . ILE B 258  ? 0.4676 0.4159 0.2726 -0.1585 -0.0277 0.1016  256  ILE B O   
10818 C CB  . ILE B 258  ? 0.5694 0.4724 0.3580 -0.1611 -0.0406 0.1040  256  ILE B CB  
10819 C CG1 . ILE B 258  ? 0.5349 0.4351 0.3202 -0.1716 -0.0420 0.1085  256  ILE B CG1 
10820 C CG2 . ILE B 258  ? 0.4844 0.3673 0.2658 -0.1563 -0.0460 0.1029  256  ILE B CG2 
10821 C CD1 . ILE B 258  ? 0.5371 0.4236 0.3229 -0.1716 -0.0465 0.1066  256  ILE B CD1 
10822 N N   . TYR B 259  ? 0.5021 0.4476 0.2954 -0.1727 -0.0287 0.1106  257  TYR B N   
10823 C CA  . TYR B 259  ? 0.4920 0.4588 0.2942 -0.1751 -0.0235 0.1104  257  TYR B CA  
10824 C C   . TYR B 259  ? 0.5229 0.5050 0.3258 -0.1723 -0.0184 0.1105  257  TYR B C   
10825 O O   . TYR B 259  ? 0.4897 0.4859 0.2993 -0.1681 -0.0142 0.1080  257  TYR B O   
10826 C CB  . TYR B 259  ? 0.5059 0.4747 0.3090 -0.1837 -0.0246 0.1130  257  TYR B CB  
10827 C CG  . TYR B 259  ? 0.5024 0.4552 0.3039 -0.1860 -0.0299 0.1126  257  TYR B CG  
10828 C CD1 . TYR B 259  ? 0.5326 0.4864 0.3406 -0.1837 -0.0299 0.1097  257  TYR B CD1 
10829 C CD2 . TYR B 259  ? 0.5672 0.5033 0.3603 -0.1901 -0.0348 0.1148  257  TYR B CD2 
10830 C CE1 . TYR B 259  ? 0.5792 0.5180 0.3855 -0.1853 -0.0347 0.1089  257  TYR B CE1 
10831 C CE2 . TYR B 259  ? 0.5035 0.4245 0.2948 -0.1916 -0.0398 0.1140  257  TYR B CE2 
10832 C CZ  . TYR B 259  ? 0.5674 0.4898 0.3653 -0.1891 -0.0397 0.1110  257  TYR B CZ  
10833 O OH  . TYR B 259  ? 0.5743 0.4816 0.3701 -0.1902 -0.0445 0.1099  257  TYR B OH  
10834 N N   . GLU B 260  ? 0.4881 0.4673 0.2840 -0.1744 -0.0188 0.1132  258  GLU B N   
10835 C CA  . GLU B 260  ? 0.5210 0.5133 0.3166 -0.1712 -0.0142 0.1131  258  GLU B CA  
10836 C C   . GLU B 260  ? 0.5076 0.4943 0.2999 -0.1630 -0.0146 0.1104  258  GLU B C   
10837 O O   . GLU B 260  ? 0.5476 0.5475 0.3433 -0.1582 -0.0103 0.1083  258  GLU B O   
10838 C CB  . GLU B 260  ? 0.5103 0.5012 0.2992 -0.1762 -0.0146 0.1170  258  GLU B CB  
10839 C CG  . GLU B 260  ? 0.6525 0.6552 0.4399 -0.1727 -0.0102 0.1169  258  GLU B CG  
10840 C CD  . GLU B 260  ? 0.6747 0.6731 0.4541 -0.1769 -0.0111 0.1207  258  GLU B CD  
10841 O OE1 . GLU B 260  ? 0.6832 0.6714 0.4589 -0.1833 -0.0147 0.1236  258  GLU B OE1 
10842 O OE2 . GLU B 260  ? 0.7028 0.7076 0.4791 -0.1738 -0.0083 0.1207  258  GLU B OE2 
10843 N N   . GLY B 261  ? 0.5394 0.5067 0.3252 -0.1611 -0.0198 0.1103  259  GLY B N   
10844 C CA  . GLY B 261  ? 0.4947 0.4558 0.2792 -0.1521 -0.0210 0.1065  259  GLY B CA  
10845 C C   . GLY B 261  ? 0.4972 0.4612 0.2924 -0.1437 -0.0206 0.1000  259  GLY B C   
10846 O O   . GLY B 261  ? 0.4441 0.4097 0.2461 -0.1449 -0.0208 0.0985  259  GLY B O   
10847 N N   . PRO B 262  ? 0.4214 0.3853 0.2177 -0.1352 -0.0202 0.0959  260  PRO B N   
10848 C CA  . PRO B 262  ? 0.4454 0.4130 0.2518 -0.1270 -0.0195 0.0897  260  PRO B CA  
10849 C C   . PRO B 262  ? 0.4346 0.3867 0.2422 -0.1245 -0.0245 0.0875  260  PRO B C   
10850 O O   . PRO B 262  ? 0.4746 0.4112 0.2744 -0.1270 -0.0291 0.0900  260  PRO B O   
10851 C CB  . PRO B 262  ? 0.4175 0.3878 0.2224 -0.1197 -0.0183 0.0869  260  PRO B CB  
10852 C CG  . PRO B 262  ? 0.4335 0.3926 0.2264 -0.1229 -0.0212 0.0910  260  PRO B CG  
10853 C CD  . PRO B 262  ? 0.4268 0.3877 0.2148 -0.1331 -0.0205 0.0971  260  PRO B CD  
10854 N N   . GLY B 263  ? 0.3845 0.3409 0.2018 -0.1192 -0.0237 0.0826  261  GLY B N   
10855 C CA  . GLY B 263  ? 0.3850 0.3286 0.2047 -0.1155 -0.0279 0.0797  261  GLY B CA  
10856 C C   . GLY B 263  ? 0.3732 0.3200 0.2004 -0.1061 -0.0271 0.0738  261  GLY B C   
10857 O O   . GLY B 263  ? 0.3927 0.3502 0.2223 -0.1025 -0.0237 0.0720  261  GLY B O   
10858 N N   . ILE B 264  ? 0.3742 0.3120 0.2051 -0.1024 -0.0301 0.0707  262  ILE B N   
10859 C CA  . ILE B 264  ? 0.3735 0.3135 0.2118 -0.0939 -0.0298 0.0652  262  ILE B CA  
10860 C C   . ILE B 264  ? 0.4033 0.3446 0.2498 -0.0932 -0.0297 0.0626  262  ILE B C   
10861 O O   . ILE B 264  ? 0.3859 0.3205 0.2307 -0.0979 -0.0319 0.0646  262  ILE B O   
10862 C CB  . ILE B 264  ? 0.4359 0.3626 0.2700 -0.0888 -0.0340 0.0637  262  ILE B CB  
10863 C CG1 . ILE B 264  ? 0.3771 0.3085 0.2182 -0.0805 -0.0330 0.0585  262  ILE B CG1 
10864 C CG2 . ILE B 264  ? 0.3847 0.2966 0.2166 -0.0896 -0.0387 0.0641  262  ILE B CG2 
10865 C CD1 . ILE B 264  ? 0.3829 0.3034 0.2200 -0.0754 -0.0369 0.0571  262  ILE B CD1 
10866 N N   . SER B 265  ? 0.3404 0.2905 0.1955 -0.0874 -0.0272 0.0583  263  SER B N   
10867 C CA  . SER B 265  ? 0.3316 0.2834 0.1949 -0.0855 -0.0271 0.0553  263  SER B CA  
10868 C C   . SER B 265  ? 0.3604 0.3063 0.2272 -0.0777 -0.0290 0.0508  263  SER B C   
10869 O O   . SER B 265  ? 0.4063 0.3541 0.2730 -0.0731 -0.0284 0.0491  263  SER B O   
10870 C CB  . SER B 265  ? 0.4079 0.3761 0.2787 -0.0858 -0.0223 0.0542  263  SER B CB  
10871 O OG  . SER B 265  ? 0.4026 0.3768 0.2717 -0.0933 -0.0207 0.0581  263  SER B OG  
10872 N N   . ILE B 266  ? 0.3272 0.2656 0.1968 -0.0764 -0.0315 0.0491  264  ILE B N   
10873 C CA  . ILE B 266  ? 0.3221 0.2555 0.1957 -0.0693 -0.0334 0.0450  264  ILE B CA  
10874 C C   . ILE B 266  ? 0.3356 0.2732 0.2177 -0.0674 -0.0322 0.0419  264  ILE B C   
10875 O O   . ILE B 266  ? 0.3193 0.2601 0.2030 -0.0718 -0.0313 0.0432  264  ILE B O   
10876 C CB  . ILE B 266  ? 0.3305 0.2481 0.1979 -0.0684 -0.0384 0.0456  264  ILE B CB  
10877 C CG1 . ILE B 266  ? 0.3549 0.2645 0.2204 -0.0727 -0.0407 0.0472  264  ILE B CG1 
10878 C CG2 . ILE B 266  ? 0.3643 0.2770 0.2227 -0.0705 -0.0398 0.0489  264  ILE B CG2 
10879 C CD1 . ILE B 266  ? 0.4366 0.3306 0.2974 -0.0704 -0.0457 0.0468  264  ILE B CD1 
10880 N N   . LYS B 267  ? 0.3208 0.2584 0.2083 -0.0609 -0.0325 0.0380  265  LYS B N   
10881 C CA  . LYS B 267  ? 0.2860 0.2262 0.1812 -0.0583 -0.0319 0.0349  265  LYS B CA  
10882 C C   . LYS B 267  ? 0.2937 0.2223 0.1884 -0.0543 -0.0357 0.0329  265  LYS B C   
10883 O O   . LYS B 267  ? 0.3179 0.2425 0.2114 -0.0501 -0.0373 0.0316  265  LYS B O   
10884 C CB  . LYS B 267  ? 0.3315 0.2834 0.2341 -0.0540 -0.0283 0.0318  265  LYS B CB  
10885 C CG  . LYS B 267  ? 0.3457 0.3099 0.2495 -0.0575 -0.0243 0.0335  265  LYS B CG  
10886 C CD  . LYS B 267  ? 0.4609 0.4359 0.3723 -0.0530 -0.0210 0.0302  265  LYS B CD  
10887 C CE  . LYS B 267  ? 0.5065 0.4942 0.4195 -0.0561 -0.0170 0.0318  265  LYS B CE  
10888 N NZ  . LYS B 267  ? 0.4935 0.4828 0.3997 -0.0597 -0.0164 0.0350  265  LYS B NZ  
10889 N N   . LEU B 268  ? 0.2976 0.2210 0.1932 -0.0557 -0.0373 0.0326  266  LEU B N   
10890 C CA  . LEU B 268  ? 0.3169 0.2295 0.2120 -0.0516 -0.0408 0.0306  266  LEU B CA  
10891 C C   . LEU B 268  ? 0.2920 0.2089 0.1943 -0.0448 -0.0399 0.0265  266  LEU B C   
10892 O O   . LEU B 268  ? 0.2999 0.2099 0.2013 -0.0405 -0.0426 0.0251  266  LEU B O   
10893 C CB  . LEU B 268  ? 0.2992 0.2058 0.1937 -0.0542 -0.0425 0.0308  266  LEU B CB  
10894 C CG  . LEU B 268  ? 0.3364 0.2369 0.2232 -0.0614 -0.0440 0.0350  266  LEU B CG  
10895 C CD1 . LEU B 268  ? 0.3494 0.2431 0.2357 -0.0633 -0.0460 0.0346  266  LEU B CD1 
10896 C CD2 . LEU B 268  ? 0.3755 0.2654 0.2537 -0.0618 -0.0473 0.0373  266  LEU B CD2 
10897 N N   . SER B 269  ? 0.2807 0.2090 0.1900 -0.0437 -0.0363 0.0248  267  SER B N   
10898 C CA  . SER B 269  ? 0.2821 0.2143 0.1979 -0.0377 -0.0355 0.0211  267  SER B CA  
10899 C C   . SER B 269  ? 0.2790 0.2107 0.1929 -0.0346 -0.0362 0.0207  267  SER B C   
10900 O O   . SER B 269  ? 0.3194 0.2512 0.2373 -0.0296 -0.0368 0.0179  267  SER B O   
10901 C CB  . SER B 269  ? 0.2848 0.2288 0.2076 -0.0373 -0.0315 0.0197  267  SER B CB  
10902 O OG  . SER B 269  ? 0.3104 0.2622 0.2320 -0.0391 -0.0289 0.0211  267  SER B OG  
10903 N N   . ALA B 270  ? 0.2646 0.1960 0.1723 -0.0376 -0.0362 0.0235  268  ALA B N   
10904 C CA  . ALA B 270  ? 0.2805 0.2103 0.1853 -0.0348 -0.0373 0.0232  268  ALA B CA  
10905 C C   . ALA B 270  ? 0.3123 0.2306 0.2133 -0.0326 -0.0417 0.0232  268  ALA B C   
10906 O O   . ALA B 270  ? 0.3058 0.2225 0.2061 -0.0290 -0.0432 0.0221  268  ALA B O   
10907 C CB  . ALA B 270  ? 0.3052 0.2377 0.2038 -0.0388 -0.0360 0.0263  268  ALA B CB  
10908 N N   . LEU B 271  ? 0.3067 0.2168 0.2047 -0.0346 -0.0440 0.0245  269  LEU B N   
10909 C CA  . LEU B 271  ? 0.3302 0.2283 0.2225 -0.0331 -0.0485 0.0252  269  LEU B CA  
10910 C C   . LEU B 271  ? 0.3008 0.1949 0.1978 -0.0280 -0.0505 0.0221  269  LEU B C   
10911 O O   . LEU B 271  ? 0.3448 0.2295 0.2378 -0.0257 -0.0542 0.0222  269  LEU B O   
10912 C CB  . LEU B 271  ? 0.3267 0.2165 0.2111 -0.0386 -0.0503 0.0289  269  LEU B CB  
10913 C CG  . LEU B 271  ? 0.3553 0.2480 0.2339 -0.0436 -0.0489 0.0325  269  LEU B CG  
10914 C CD1 . LEU B 271  ? 0.3972 0.2822 0.2683 -0.0498 -0.0505 0.0363  269  LEU B CD1 
10915 C CD2 . LEU B 271  ? 0.3974 0.2878 0.2719 -0.0410 -0.0505 0.0329  269  LEU B CD2 
10916 N N   . HIS B 272  ? 0.2903 0.1916 0.1953 -0.0259 -0.0481 0.0193  270  HIS B N   
10917 C CA  . HIS B 272  ? 0.3233 0.2219 0.2330 -0.0210 -0.0496 0.0163  270  HIS B CA  
10918 C C   . HIS B 272  ? 0.2892 0.1982 0.2078 -0.0187 -0.0463 0.0134  270  HIS B C   
10919 O O   . HIS B 272  ? 0.3273 0.2430 0.2483 -0.0216 -0.0432 0.0138  270  HIS B O   
10920 C CB  . HIS B 272  ? 0.3426 0.2329 0.2498 -0.0223 -0.0516 0.0167  270  HIS B CB  
10921 C CG  . HIS B 272  ? 0.3422 0.2272 0.2515 -0.0169 -0.0541 0.0142  270  HIS B CG  
10922 N ND1 . HIS B 272  ? 0.3507 0.2416 0.2681 -0.0132 -0.0525 0.0109  270  HIS B ND1 
10923 C CD2 . HIS B 272  ? 0.3978 0.2726 0.3024 -0.0143 -0.0582 0.0144  270  HIS B CD2 
10924 C CE1 . HIS B 272  ? 0.3819 0.2670 0.2997 -0.0086 -0.0553 0.0092  270  HIS B CE1 
10925 N NE2 . HIS B 272  ? 0.4133 0.2885 0.3234 -0.0091 -0.0588 0.0112  270  HIS B NE2 
10926 N N   . PRO B 273  ? 0.2908 0.2015 0.2146 -0.0136 -0.0469 0.0106  271  PRO B N   
10927 C CA  . PRO B 273  ? 0.2866 0.2068 0.2187 -0.0116 -0.0438 0.0081  271  PRO B CA  
10928 C C   . PRO B 273  ? 0.2779 0.1989 0.2140 -0.0116 -0.0427 0.0068  271  PRO B C   
10929 O O   . PRO B 273  ? 0.2940 0.2229 0.2363 -0.0109 -0.0399 0.0052  271  PRO B O   
10930 C CB  . PRO B 273  ? 0.3263 0.2469 0.2617 -0.0065 -0.0454 0.0058  271  PRO B CB  
10931 C CG  . PRO B 273  ? 0.3409 0.2517 0.2715 -0.0050 -0.0495 0.0065  271  PRO B CG  
10932 C CD  . PRO B 273  ? 0.3132 0.2181 0.2354 -0.0095 -0.0504 0.0099  271  PRO B CD  
10933 N N   . ARG B 274  ? 0.2727 0.1857 0.2053 -0.0122 -0.0450 0.0074  272  ARG B N   
10934 C CA  . ARG B 274  ? 0.2719 0.1852 0.2078 -0.0122 -0.0441 0.0061  272  ARG B CA  
10935 C C   . ARG B 274  ? 0.3174 0.2260 0.2478 -0.0173 -0.0445 0.0085  272  ARG B C   
10936 O O   . ARG B 274  ? 0.3217 0.2227 0.2494 -0.0173 -0.0466 0.0083  272  ARG B O   
10937 C CB  . ARG B 274  ? 0.2932 0.2014 0.2308 -0.0074 -0.0465 0.0039  272  ARG B CB  
10938 C CG  . ARG B 274  ? 0.3020 0.2158 0.2459 -0.0026 -0.0460 0.0014  272  ARG B CG  
10939 C CD  . ARG B 274  ? 0.2946 0.2189 0.2457 -0.0027 -0.0422 0.0000  272  ARG B CD  
10940 N NE  . ARG B 274  ? 0.3160 0.2416 0.2696 -0.0034 -0.0407 -0.0008 272  ARG B NE  
10941 C CZ  . ARG B 274  ? 0.3011 0.2261 0.2583 -0.0001 -0.0411 -0.0030 272  ARG B CZ  
10942 N NH1 . ARG B 274  ? 0.3117 0.2349 0.2705 0.0042  -0.0430 -0.0045 272  ARG B NH1 
10943 N NH2 . ARG B 274  ? 0.2959 0.2228 0.2552 -0.0011 -0.0394 -0.0037 272  ARG B NH2 
10944 N N   . TYR B 275  ? 0.2964 0.2096 0.2250 -0.0218 -0.0425 0.0107  273  TYR B N   
10945 C CA  . TYR B 275  ? 0.3148 0.2246 0.2385 -0.0273 -0.0428 0.0133  273  TYR B CA  
10946 C C   . TYR B 275  ? 0.2884 0.2036 0.2169 -0.0285 -0.0405 0.0121  273  TYR B C   
10947 O O   . TYR B 275  ? 0.2930 0.2179 0.2254 -0.0302 -0.0373 0.0123  273  TYR B O   
10948 C CB  . TYR B 275  ? 0.2850 0.1985 0.2050 -0.0317 -0.0415 0.0163  273  TYR B CB  
10949 C CG  . TYR B 275  ? 0.2921 0.2040 0.2077 -0.0380 -0.0414 0.0191  273  TYR B CG  
10950 C CD1 . TYR B 275  ? 0.3199 0.2209 0.2300 -0.0401 -0.0445 0.0202  273  TYR B CD1 
10951 C CD2 . TYR B 275  ? 0.3039 0.2254 0.2211 -0.0419 -0.0381 0.0206  273  TYR B CD2 
10952 C CE1 . TYR B 275  ? 0.3436 0.2431 0.2497 -0.0464 -0.0446 0.0229  273  TYR B CE1 
10953 C CE2 . TYR B 275  ? 0.2974 0.2183 0.2110 -0.0480 -0.0380 0.0234  273  TYR B CE2 
10954 C CZ  . TYR B 275  ? 0.3170 0.2269 0.2252 -0.0505 -0.0413 0.0245  273  TYR B CZ  
10955 O OH  . TYR B 275  ? 0.3297 0.2390 0.2344 -0.0570 -0.0414 0.0273  273  TYR B OH  
10956 N N   . SER B 276  ? 0.2801 0.1891 0.2083 -0.0273 -0.0423 0.0108  274  SER B N   
10957 C CA  . SER B 276  ? 0.2802 0.1935 0.2126 -0.0281 -0.0405 0.0096  274  SER B CA  
10958 C C   . SER B 276  ? 0.2831 0.1864 0.2117 -0.0281 -0.0434 0.0090  274  SER B C   
10959 O O   . SER B 276  ? 0.3124 0.2062 0.2369 -0.0257 -0.0465 0.0087  274  SER B O   
10960 C CB  . SER B 276  ? 0.3470 0.2685 0.2876 -0.0234 -0.0382 0.0066  274  SER B CB  
10961 O OG  . SER B 276  ? 0.3760 0.2923 0.3175 -0.0184 -0.0401 0.0044  274  SER B OG  
10962 N N   . ARG B 277  ? 0.2698 0.1753 0.1997 -0.0308 -0.0424 0.0088  275  ARG B N   
10963 C CA  . ARG B 277  ? 0.2879 0.1840 0.2141 -0.0309 -0.0450 0.0080  275  ARG B CA  
10964 C C   . ARG B 277  ? 0.2968 0.1896 0.2255 -0.0243 -0.0460 0.0048  275  ARG B C   
10965 O O   . ARG B 277  ? 0.3184 0.2006 0.2422 -0.0228 -0.0492 0.0042  275  ARG B O   
10966 C CB  . ARG B 277  ? 0.2846 0.1850 0.2126 -0.0346 -0.0435 0.0081  275  ARG B CB  
10967 C CG  . ARG B 277  ? 0.3182 0.2097 0.2429 -0.0343 -0.0459 0.0066  275  ARG B CG  
10968 C CD  . ARG B 277  ? 0.3179 0.1959 0.2334 -0.0369 -0.0499 0.0085  275  ARG B CD  
10969 N NE  . ARG B 277  ? 0.3284 0.1972 0.2403 -0.0363 -0.0524 0.0069  275  ARG B NE  
10970 C CZ  . ARG B 277  ? 0.3404 0.2026 0.2516 -0.0305 -0.0542 0.0041  275  ARG B CZ  
10971 N NH1 . ARG B 277  ? 0.3497 0.2139 0.2642 -0.0248 -0.0538 0.0027  275  ARG B NH1 
10972 N NH2 . ARG B 277  ? 0.3481 0.2014 0.2550 -0.0304 -0.0565 0.0028  275  ARG B NH2 
10973 N N   . ALA B 278  ? 0.3195 0.2213 0.2557 -0.0203 -0.0435 0.0027  276  ALA B N   
10974 C CA  . ALA B 278  ? 0.2996 0.1997 0.2387 -0.0142 -0.0442 -0.0002 276  ALA B CA  
10975 C C   . ALA B 278  ? 0.3063 0.1986 0.2416 -0.0111 -0.0473 -0.0002 276  ALA B C   
10976 O O   . ALA B 278  ? 0.3412 0.2284 0.2763 -0.0065 -0.0490 -0.0023 276  ALA B O   
10977 C CB  . ALA B 278  ? 0.2928 0.2040 0.2404 -0.0111 -0.0410 -0.0021 276  ALA B CB  
10978 N N   . GLN B 279  ? 0.3062 0.1973 0.2382 -0.0132 -0.0480 0.0021  277  GLN B N   
10979 C CA  . GLN B 279  ? 0.2883 0.1719 0.2161 -0.0106 -0.0511 0.0025  277  GLN B CA  
10980 C C   . GLN B 279  ? 0.3474 0.2203 0.2659 -0.0148 -0.0540 0.0054  277  GLN B C   
10981 O O   . GLN B 279  ? 0.3497 0.2185 0.2640 -0.0151 -0.0558 0.0072  277  GLN B O   
10982 C CB  . GLN B 279  ? 0.3220 0.2124 0.2531 -0.0091 -0.0499 0.0029  277  GLN B CB  
10983 C CG  . GLN B 279  ? 0.3151 0.2154 0.2550 -0.0052 -0.0473 0.0002  277  GLN B CG  
10984 C CD  . GLN B 279  ? 0.3836 0.2809 0.3258 0.0004  -0.0488 -0.0025 277  GLN B CD  
10985 O OE1 . GLN B 279  ? 0.4314 0.3200 0.3690 0.0027  -0.0522 -0.0025 277  GLN B OE1 
10986 N NE2 . GLN B 279  ? 0.2937 0.1984 0.2429 0.0028  -0.0465 -0.0048 277  GLN B NE2 
10987 N N   . ALA B 280  ? 0.3222 0.1901 0.2372 -0.0181 -0.0547 0.0059  278  ALA B N   
10988 C CA  . ALA B 280  ? 0.3260 0.1839 0.2321 -0.0232 -0.0574 0.0089  278  ALA B CA  
10989 C C   . ALA B 280  ? 0.3545 0.2004 0.2541 -0.0201 -0.0616 0.0092  278  ALA B C   
10990 O O   . ALA B 280  ? 0.3559 0.1957 0.2488 -0.0236 -0.0635 0.0122  278  ALA B O   
10991 C CB  . ALA B 280  ? 0.3582 0.2116 0.2616 -0.0266 -0.0580 0.0088  278  ALA B CB  
10992 N N   . ALA B 281  ? 0.3442 0.1869 0.2456 -0.0137 -0.0631 0.0063  279  ALA B N   
10993 C CA  . ALA B 281  ? 0.3950 0.2261 0.2901 -0.0103 -0.0673 0.0064  279  ALA B CA  
10994 C C   . ALA B 281  ? 0.3861 0.2198 0.2811 -0.0095 -0.0675 0.0080  279  ALA B C   
10995 O O   . ALA B 281  ? 0.3969 0.2211 0.2843 -0.0107 -0.0707 0.0103  279  ALA B O   
10996 C CB  . ALA B 281  ? 0.4246 0.2535 0.3226 -0.0030 -0.0684 0.0027  279  ALA B CB  
10997 N N   . ARG B 282  ? 0.3669 0.2128 0.2699 -0.0076 -0.0644 0.0069  280  ARG B N   
10998 C CA  . ARG B 282  ? 0.3489 0.1978 0.2518 -0.0071 -0.0646 0.0082  280  ARG B CA  
10999 C C   . ARG B 282  ? 0.3548 0.2038 0.2527 -0.0139 -0.0638 0.0119  280  ARG B C   
11000 O O   . ARG B 282  ? 0.3810 0.2260 0.2739 -0.0146 -0.0656 0.0141  280  ARG B O   
11001 C CB  . ARG B 282  ? 0.3996 0.2615 0.3120 -0.0039 -0.0614 0.0060  280  ARG B CB  
11002 C CG  . ARG B 282  ? 0.3976 0.2608 0.3154 0.0029  -0.0621 0.0026  280  ARG B CG  
11003 C CD  . ARG B 282  ? 0.3771 0.2519 0.3030 0.0055  -0.0596 0.0011  280  ARG B CD  
11004 N NE  . ARG B 282  ? 0.3536 0.2282 0.2771 0.0055  -0.0610 0.0026  280  ARG B NE  
11005 C CZ  . ARG B 282  ? 0.3827 0.2665 0.3112 0.0059  -0.0590 0.0022  280  ARG B CZ  
11006 N NH1 . ARG B 282  ? 0.3295 0.2231 0.2655 0.0061  -0.0555 0.0005  280  ARG B NH1 
11007 N NH2 . ARG B 282  ? 0.3825 0.2649 0.3077 0.0059  -0.0606 0.0036  280  ARG B NH2 
11008 N N   . VAL B 283  ? 0.3466 0.2005 0.2458 -0.0188 -0.0611 0.0128  281  VAL B N   
11009 C CA  . VAL B 283  ? 0.3280 0.1829 0.2229 -0.0255 -0.0602 0.0164  281  VAL B CA  
11010 C C   . VAL B 283  ? 0.3528 0.1940 0.2373 -0.0285 -0.0642 0.0192  281  VAL B C   
11011 O O   . VAL B 283  ? 0.3974 0.2362 0.2767 -0.0310 -0.0651 0.0221  281  VAL B O   
11012 C CB  . VAL B 283  ? 0.3264 0.1893 0.2250 -0.0299 -0.0569 0.0166  281  VAL B CB  
11013 C CG1 . VAL B 283  ? 0.3527 0.2150 0.2457 -0.0372 -0.0565 0.0205  281  VAL B CG1 
11014 C CG2 . VAL B 283  ? 0.3345 0.2114 0.2423 -0.0275 -0.0528 0.0146  281  VAL B CG2 
11015 N N   . MET B 284  ? 0.3547 0.1862 0.2357 -0.0283 -0.0667 0.0185  282  MET B N   
11016 C CA  . MET B 284  ? 0.3825 0.1996 0.2530 -0.0313 -0.0708 0.0212  282  MET B CA  
11017 C C   . MET B 284  ? 0.4228 0.2319 0.2890 -0.0265 -0.0743 0.0213  282  MET B C   
11018 O O   . MET B 284  ? 0.4377 0.2375 0.2954 -0.0295 -0.0770 0.0245  282  MET B O   
11019 C CB  . MET B 284  ? 0.3679 0.1759 0.2354 -0.0317 -0.0729 0.0200  282  MET B CB  
11020 C CG  . MET B 284  ? 0.4100 0.2252 0.2810 -0.0367 -0.0699 0.0200  282  MET B CG  
11021 S SD  . MET B 284  ? 0.4386 0.2569 0.3053 -0.0465 -0.0685 0.0250  282  MET B SD  
11022 C CE  . MET B 284  ? 0.4939 0.2928 0.3476 -0.0506 -0.0740 0.0279  282  MET B CE  
11023 N N   . GLY B 285  ? 0.4023 0.2148 0.2743 -0.0192 -0.0743 0.0180  283  GLY B N   
11024 C CA  . GLY B 285  ? 0.4223 0.2275 0.2908 -0.0142 -0.0778 0.0178  283  GLY B CA  
11025 C C   . GLY B 285  ? 0.4365 0.2476 0.3056 -0.0143 -0.0771 0.0194  283  GLY B C   
11026 O O   . GLY B 285  ? 0.4518 0.2548 0.3146 -0.0129 -0.0805 0.0210  283  GLY B O   
11027 N N   . GLU B 286  ? 0.3884 0.2129 0.2643 -0.0159 -0.0728 0.0190  284  GLU B N   
11028 C CA  . GLU B 286  ? 0.3441 0.1755 0.2218 -0.0150 -0.0718 0.0197  284  GLU B CA  
11029 C C   . GLU B 286  ? 0.3977 0.2350 0.2736 -0.0214 -0.0690 0.0226  284  GLU B C   
11030 O O   . GLU B 286  ? 0.4429 0.2793 0.3144 -0.0226 -0.0699 0.0249  284  GLU B O   
11031 C CB  . GLU B 286  ? 0.3724 0.2152 0.2605 -0.0098 -0.0694 0.0160  284  GLU B CB  
11032 C CG  . GLU B 286  ? 0.3952 0.2342 0.2861 -0.0031 -0.0717 0.0129  284  GLU B CG  
11033 C CD  . GLU B 286  ? 0.4500 0.3007 0.3515 0.0010  -0.0689 0.0095  284  GLU B CD  
11034 O OE1 . GLU B 286  ? 0.4531 0.3136 0.3590 -0.0001 -0.0661 0.0095  284  GLU B OE1 
11035 O OE2 . GLU B 286  ? 0.4933 0.3431 0.3983 0.0053  -0.0696 0.0068  284  GLU B OE2 
11036 N N   . LEU B 287  ? 0.3872 0.2312 0.2665 -0.0254 -0.0657 0.0227  285  LEU B N   
11037 C CA  . LEU B 287  ? 0.3786 0.2294 0.2567 -0.0314 -0.0628 0.0255  285  LEU B CA  
11038 C C   . LEU B 287  ? 0.3862 0.2274 0.2544 -0.0375 -0.0650 0.0295  285  LEU B C   
11039 O O   . LEU B 287  ? 0.3818 0.2233 0.2451 -0.0407 -0.0649 0.0325  285  LEU B O   
11040 C CB  . LEU B 287  ? 0.3788 0.2404 0.2642 -0.0333 -0.0587 0.0241  285  LEU B CB  
11041 C CG  . LEU B 287  ? 0.4003 0.2740 0.2885 -0.0369 -0.0546 0.0254  285  LEU B CG  
11042 C CD1 . LEU B 287  ? 0.3622 0.2457 0.2584 -0.0369 -0.0510 0.0232  285  LEU B CD1 
11043 C CD2 . LEU B 287  ? 0.3908 0.2620 0.2716 -0.0440 -0.0546 0.0297  285  LEU B CD2 
11044 N N   . LEU B 288  ? 0.3984 0.2308 0.2633 -0.0393 -0.0670 0.0298  286  LEU B N   
11045 C CA  . LEU B 288  ? 0.3956 0.2182 0.2509 -0.0457 -0.0693 0.0338  286  LEU B CA  
11046 C C   . LEU B 288  ? 0.3987 0.2121 0.2455 -0.0455 -0.0726 0.0365  286  LEU B C   
11047 O O   . LEU B 288  ? 0.4063 0.2192 0.2473 -0.0515 -0.0723 0.0404  286  LEU B O   
11048 C CB  . LEU B 288  ? 0.4286 0.2412 0.2814 -0.0462 -0.0718 0.0329  286  LEU B CB  
11049 C CG  . LEU B 288  ? 0.4797 0.2790 0.3216 -0.0523 -0.0752 0.0368  286  LEU B CG  
11050 C CD1 . LEU B 288  ? 0.4600 0.2661 0.3003 -0.0607 -0.0725 0.0406  286  LEU B CD1 
11051 C CD2 . LEU B 288  ? 0.5367 0.3255 0.3760 -0.0520 -0.0779 0.0354  286  LEU B CD2 
11052 N N   . PRO B 289  ? 0.4257 0.2324 0.2714 -0.0391 -0.0758 0.0347  287  PRO B N   
11053 C CA  . PRO B 289  ? 0.4217 0.2198 0.2590 -0.0391 -0.0790 0.0375  287  PRO B CA  
11054 C C   . PRO B 289  ? 0.4141 0.2218 0.2519 -0.0412 -0.0764 0.0394  287  PRO B C   
11055 O O   . PRO B 289  ? 0.4635 0.2654 0.2930 -0.0444 -0.0781 0.0430  287  PRO B O   
11056 C CB  . PRO B 289  ? 0.5091 0.3018 0.3479 -0.0308 -0.0822 0.0345  287  PRO B CB  
11057 C CG  . PRO B 289  ? 0.5403 0.3323 0.3841 -0.0280 -0.0820 0.0311  287  PRO B CG  
11058 C CD  . PRO B 289  ? 0.4843 0.2891 0.3351 -0.0319 -0.0771 0.0305  287  PRO B CD  
11059 N N   . ARG B 290  ? 0.4055 0.2273 0.2523 -0.0392 -0.0723 0.0369  288  ARG B N   
11060 C CA  . ARG B 290  ? 0.4121 0.2430 0.2590 -0.0412 -0.0696 0.0385  288  ARG B CA  
11061 C C   . ARG B 290  ? 0.3979 0.2320 0.2410 -0.0493 -0.0673 0.0422  288  ARG B C   
11062 O O   . ARG B 290  ? 0.4030 0.2368 0.2400 -0.0527 -0.0672 0.0455  288  ARG B O   
11063 C CB  . ARG B 290  ? 0.3918 0.2362 0.2490 -0.0371 -0.0660 0.0348  288  ARG B CB  
11064 C CG  . ARG B 290  ? 0.4486 0.2913 0.3089 -0.0297 -0.0684 0.0319  288  ARG B CG  
11065 C CD  . ARG B 290  ? 0.5130 0.3672 0.3840 -0.0258 -0.0652 0.0279  288  ARG B CD  
11066 N NE  . ARG B 290  ? 0.5633 0.4194 0.4369 -0.0202 -0.0666 0.0258  288  ARG B NE  
11067 C CZ  . ARG B 290  ? 0.6094 0.4737 0.4918 -0.0159 -0.0649 0.0223  288  ARG B CZ  
11068 N NH1 . ARG B 290  ? 0.5721 0.4434 0.4615 -0.0162 -0.0617 0.0204  288  ARG B NH1 
11069 N NH2 . ARG B 290  ? 0.5261 0.3917 0.4102 -0.0114 -0.0664 0.0208  288  ARG B NH2 
11070 N N   . VAL B 291  ? 0.4026 0.2396 0.2490 -0.0526 -0.0654 0.0419  289  VAL B N   
11071 C CA  . VAL B 291  ? 0.3715 0.2121 0.2147 -0.0606 -0.0633 0.0455  289  VAL B CA  
11072 C C   . VAL B 291  ? 0.3951 0.2221 0.2269 -0.0653 -0.0671 0.0498  289  VAL B C   
11073 O O   . VAL B 291  ? 0.4163 0.2453 0.2429 -0.0710 -0.0660 0.0537  289  VAL B O   
11074 C CB  . VAL B 291  ? 0.3926 0.2385 0.2415 -0.0631 -0.0611 0.0443  289  VAL B CB  
11075 C CG1 . VAL B 291  ? 0.4238 0.2751 0.2701 -0.0714 -0.0587 0.0481  289  VAL B CG1 
11076 C CG2 . VAL B 291  ? 0.3824 0.2404 0.2420 -0.0580 -0.0577 0.0401  289  VAL B CG2 
11077 N N   . LYS B 292  ? 0.3989 0.2120 0.2265 -0.0631 -0.0715 0.0492  290  LYS B N   
11078 C CA  . LYS B 292  ? 0.4027 0.2015 0.2188 -0.0675 -0.0755 0.0533  290  LYS B CA  
11079 C C   . LYS B 292  ? 0.4399 0.2369 0.2500 -0.0671 -0.0765 0.0558  290  LYS B C   
11080 O O   . LYS B 292  ? 0.4527 0.2456 0.2546 -0.0734 -0.0772 0.0604  290  LYS B O   
11081 C CB  . LYS B 292  ? 0.4490 0.2326 0.2614 -0.0639 -0.0803 0.0518  290  LYS B CB  
11082 C CG  . LYS B 292  ? 0.5076 0.2748 0.3075 -0.0688 -0.0848 0.0561  290  LYS B CG  
11083 C CD  . LYS B 292  ? 0.5877 0.3450 0.3810 -0.0644 -0.0887 0.0569  290  LYS B CD  
11084 C CE  . LYS B 292  ? 0.6031 0.3431 0.3834 -0.0693 -0.0934 0.0613  290  LYS B CE  
11085 N NZ  . LYS B 292  ? 0.6175 0.3445 0.3950 -0.0684 -0.0969 0.0599  290  LYS B NZ  
11086 N N   . ALA B 293  ? 0.4315 0.2320 0.2456 -0.0600 -0.0766 0.0530  291  ALA B N   
11087 C CA  . ALA B 293  ? 0.4861 0.2852 0.2946 -0.0593 -0.0778 0.0551  291  ALA B CA  
11088 C C   . ALA B 293  ? 0.4422 0.2523 0.2499 -0.0650 -0.0736 0.0579  291  ALA B C   
11089 O O   . ALA B 293  ? 0.4536 0.2593 0.2526 -0.0688 -0.0748 0.0619  291  ALA B O   
11090 C CB  . ALA B 293  ? 0.4658 0.2686 0.2801 -0.0508 -0.0783 0.0511  291  ALA B CB  
11091 N N   . LEU B 294  ? 0.4099 0.2345 0.2265 -0.0654 -0.0688 0.0558  292  LEU B N   
11092 C CA  . LEU B 294  ? 0.4269 0.2632 0.2436 -0.0702 -0.0646 0.0581  292  LEU B CA  
11093 C C   . LEU B 294  ? 0.4235 0.2567 0.2337 -0.0790 -0.0645 0.0628  292  LEU B C   
11094 O O   . LEU B 294  ? 0.4452 0.2809 0.2497 -0.0838 -0.0633 0.0666  292  LEU B O   
11095 C CB  . LEU B 294  ? 0.3817 0.2336 0.2095 -0.0681 -0.0598 0.0546  292  LEU B CB  
11096 C CG  . LEU B 294  ? 0.3792 0.2357 0.2138 -0.0600 -0.0594 0.0501  292  LEU B CG  
11097 C CD1 . LEU B 294  ? 0.3614 0.2315 0.2065 -0.0585 -0.0550 0.0469  292  LEU B CD1 
11098 C CD2 . LEU B 294  ? 0.3965 0.2548 0.2270 -0.0583 -0.0595 0.0510  292  LEU B CD2 
11099 N N   . ALA B 295  ? 0.4427 0.2705 0.2537 -0.0814 -0.0657 0.0626  293  ALA B N   
11100 C CA  . ALA B 295  ? 0.4211 0.2455 0.2262 -0.0902 -0.0659 0.0671  293  ALA B CA  
11101 C C   . ALA B 295  ? 0.4787 0.2886 0.2713 -0.0934 -0.0701 0.0715  293  ALA B C   
11102 O O   . ALA B 295  ? 0.4853 0.2958 0.2718 -0.1010 -0.0694 0.0761  293  ALA B O   
11103 C CB  . ALA B 295  ? 0.4206 0.2408 0.2288 -0.0915 -0.0670 0.0655  293  ALA B CB  
11104 N N   . LEU B 296  ? 0.4498 0.2471 0.2387 -0.0878 -0.0746 0.0701  294  LEU B N   
11105 C CA  . LEU B 296  ? 0.4744 0.2574 0.2512 -0.0900 -0.0789 0.0742  294  LEU B CA  
11106 C C   . LEU B 296  ? 0.5435 0.3333 0.3165 -0.0919 -0.0768 0.0770  294  LEU B C   
11107 O O   . LEU B 296  ? 0.5381 0.3224 0.3016 -0.0983 -0.0779 0.0821  294  LEU B O   
11108 C CB  . LEU B 296  ? 0.5342 0.3043 0.3090 -0.0822 -0.0838 0.0716  294  LEU B CB  
11109 C CG  . LEU B 296  ? 0.5998 0.3529 0.3620 -0.0833 -0.0891 0.0752  294  LEU B CG  
11110 C CD1 . LEU B 296  ? 0.6457 0.3887 0.3998 -0.0918 -0.0909 0.0795  294  LEU B CD1 
11111 C CD2 . LEU B 296  ? 0.7111 0.4532 0.4732 -0.0747 -0.0937 0.0719  294  LEU B CD2 
11112 N N   . LEU B 297  ? 0.4749 0.2765 0.2547 -0.0864 -0.0740 0.0739  295  LEU B N   
11113 C CA  . LEU B 297  ? 0.4688 0.2781 0.2454 -0.0880 -0.0715 0.0762  295  LEU B CA  
11114 C C   . LEU B 297  ? 0.4876 0.3074 0.2638 -0.0962 -0.0672 0.0796  295  LEU B C   
11115 O O   . LEU B 297  ? 0.4726 0.2919 0.2408 -0.1014 -0.0669 0.0841  295  LEU B O   
11116 C CB  . LEU B 297  ? 0.4345 0.2548 0.2191 -0.0806 -0.0692 0.0717  295  LEU B CB  
11117 C CG  . LEU B 297  ? 0.5585 0.3705 0.3427 -0.0727 -0.0732 0.0689  295  LEU B CG  
11118 C CD1 . LEU B 297  ? 0.5340 0.3582 0.3283 -0.0662 -0.0704 0.0640  295  LEU B CD1 
11119 C CD2 . LEU B 297  ? 0.5566 0.3599 0.3299 -0.0733 -0.0764 0.0725  295  LEU B CD2 
11120 N N   . ALA B 298  ? 0.4577 0.2878 0.2427 -0.0975 -0.0638 0.0775  296  ALA B N   
11121 C CA  . ALA B 298  ? 0.4372 0.2779 0.2227 -0.1053 -0.0598 0.0807  296  ALA B CA  
11122 C C   . ALA B 298  ? 0.5263 0.3559 0.3018 -0.1137 -0.0625 0.0862  296  ALA B C   
11123 O O   . ALA B 298  ? 0.5099 0.3445 0.2804 -0.1205 -0.0605 0.0906  296  ALA B O   
11124 C CB  . ALA B 298  ? 0.4137 0.2653 0.2100 -0.1050 -0.0565 0.0775  296  ALA B CB  
11125 N N   . LYS B 299  ? 0.4726 0.2869 0.2447 -0.1135 -0.0673 0.0860  297  LYS B N   
11126 C CA  . LYS B 299  ? 0.5337 0.3351 0.2953 -0.1213 -0.0706 0.0912  297  LYS B CA  
11127 C C   . LYS B 299  ? 0.6203 0.4147 0.3710 -0.1233 -0.0725 0.0955  297  LYS B C   
11128 O O   . LYS B 299  ? 0.5929 0.3864 0.3363 -0.1316 -0.0721 0.1008  297  LYS B O   
11129 C CB  . LYS B 299  ? 0.5615 0.3462 0.3208 -0.1193 -0.0758 0.0896  297  LYS B CB  
11130 C CG  . LYS B 299  ? 0.6379 0.4064 0.3849 -0.1268 -0.0801 0.0949  297  LYS B CG  
11131 C CD  . LYS B 299  ? 0.7221 0.4712 0.4642 -0.1225 -0.0861 0.0933  297  LYS B CD  
11132 C CE  . LYS B 299  ? 0.7077 0.4428 0.4400 -0.1297 -0.0899 0.0971  297  LYS B CE  
11133 N NZ  . LYS B 299  ? 0.7954 0.5312 0.5212 -0.1334 -0.0898 0.1008  297  LYS B NZ  
11134 N N   . ASN B 300  ? 0.5429 0.3320 0.2920 -0.1157 -0.0747 0.0933  298  ASN B N   
11135 C CA  . ASN B 300  ? 0.5561 0.3373 0.2943 -0.1170 -0.0771 0.0973  298  ASN B CA  
11136 C C   . ASN B 300  ? 0.5276 0.3226 0.2643 -0.1220 -0.0723 0.1005  298  ASN B C   
11137 O O   . ASN B 300  ? 0.5679 0.3573 0.2943 -0.1276 -0.0735 0.1058  298  ASN B O   
11138 C CB  . ASN B 300  ? 0.5848 0.3604 0.3230 -0.1075 -0.0800 0.0940  298  ASN B CB  
11139 C CG  . ASN B 300  ? 0.6876 0.4473 0.4246 -0.1028 -0.0854 0.0917  298  ASN B CG  
11140 O OD1 . ASN B 300  ? 0.7196 0.4684 0.4520 -0.1074 -0.0880 0.0938  298  ASN B OD1 
11141 N ND2 . ASN B 300  ? 0.7966 0.5551 0.5377 -0.0937 -0.0871 0.0874  298  ASN B ND2 
11142 N N   . TYR B 301  ? 0.4807 0.2938 0.2275 -0.1201 -0.0670 0.0975  299  TYR B N   
11143 C CA  . TYR B 301  ? 0.5336 0.3613 0.2799 -0.1243 -0.0620 0.1000  299  TYR B CA  
11144 C C   . TYR B 301  ? 0.4928 0.3290 0.2409 -0.1331 -0.0588 0.1031  299  TYR B C   
11145 O O   . TYR B 301  ? 0.5107 0.3595 0.2581 -0.1374 -0.0545 0.1057  299  TYR B O   
11146 C CB  . TYR B 301  ? 0.4910 0.3338 0.2468 -0.1172 -0.0579 0.0951  299  TYR B CB  
11147 C CG  . TYR B 301  ? 0.4704 0.3085 0.2238 -0.1096 -0.0601 0.0928  299  TYR B CG  
11148 C CD1 . TYR B 301  ? 0.5247 0.3604 0.2686 -0.1110 -0.0607 0.0963  299  TYR B CD1 
11149 C CD2 . TYR B 301  ? 0.4648 0.3017 0.2257 -0.1011 -0.0615 0.0873  299  TYR B CD2 
11150 C CE1 . TYR B 301  ? 0.5042 0.3359 0.2460 -0.1041 -0.0630 0.0941  299  TYR B CE1 
11151 C CE2 . TYR B 301  ? 0.4982 0.3316 0.2574 -0.0943 -0.0636 0.0851  299  TYR B CE2 
11152 C CZ  . TYR B 301  ? 0.5325 0.3632 0.2822 -0.0959 -0.0645 0.0885  299  TYR B CZ  
11153 O OH  . TYR B 301  ? 0.5110 0.3383 0.2590 -0.0893 -0.0668 0.0864  299  TYR B OH  
11154 N N   . ASP B 302  ? 0.4824 0.3125 0.2329 -0.1357 -0.0607 0.1027  300  ASP B N   
11155 C CA  . ASP B 302  ? 0.5149 0.3534 0.2688 -0.1435 -0.0580 0.1048  300  ASP B CA  
11156 C C   . ASP B 302  ? 0.4730 0.3334 0.2372 -0.1423 -0.0515 0.1024  300  ASP B C   
11157 O O   . ASP B 302  ? 0.5028 0.3751 0.2664 -0.1486 -0.0477 0.1058  300  ASP B O   
11158 C CB  . ASP B 302  ? 0.5364 0.3706 0.2815 -0.1529 -0.0589 0.1107  300  ASP B CB  
11159 C CG  . ASP B 302  ? 0.5386 0.3761 0.2877 -0.1600 -0.0583 0.1115  300  ASP B CG  
11160 O OD1 . ASP B 302  ? 0.5842 0.4175 0.3375 -0.1586 -0.0598 0.1092  300  ASP B OD1 
11161 O OD2 . ASP B 302  ? 0.5998 0.4445 0.3481 -0.1670 -0.0564 0.1145  300  ASP B OD2 
11162 N N   . ILE B 303  ? 0.4440 0.3098 0.2176 -0.1339 -0.0503 0.0966  301  ILE B N   
11163 C CA  . ILE B 303  ? 0.4362 0.3211 0.2205 -0.1318 -0.0448 0.0936  301  ILE B CA  
11164 C C   . ILE B 303  ? 0.4583 0.3438 0.2514 -0.1301 -0.0451 0.0899  301  ILE B C   
11165 O O   . ILE B 303  ? 0.4468 0.3183 0.2385 -0.1282 -0.0495 0.0885  301  ILE B O   
11166 C CB  . ILE B 303  ? 0.4267 0.3194 0.2148 -0.1235 -0.0425 0.0897  301  ILE B CB  
11167 C CG1 . ILE B 303  ? 0.4624 0.3466 0.2548 -0.1148 -0.0456 0.0845  301  ILE B CG1 
11168 C CG2 . ILE B 303  ? 0.4341 0.3244 0.2126 -0.1247 -0.0428 0.0931  301  ILE B CG2 
11169 C CD1 . ILE B 303  ? 0.4500 0.3431 0.2479 -0.1068 -0.0432 0.0802  301  ILE B CD1 
11170 N N   . GLY B 304  ? 0.4114 0.3135 0.2135 -0.1304 -0.0404 0.0882  302  GLY B N   
11171 C CA  . GLY B 304  ? 0.4065 0.3110 0.2176 -0.1282 -0.0402 0.0845  302  GLY B CA  
11172 C C   . GLY B 304  ? 0.4147 0.3193 0.2325 -0.1181 -0.0403 0.0786  302  GLY B C   
11173 O O   . GLY B 304  ? 0.4396 0.3503 0.2587 -0.1130 -0.0383 0.0768  302  GLY B O   
11174 N N   . LEU B 305  ? 0.3804 0.2777 0.2020 -0.1154 -0.0428 0.0757  303  LEU B N   
11175 C CA  . LEU B 305  ? 0.4060 0.3044 0.2351 -0.1064 -0.0427 0.0701  303  LEU B CA  
11176 C C   . LEU B 305  ? 0.4155 0.3200 0.2532 -0.1065 -0.0413 0.0676  303  LEU B C   
11177 O O   . LEU B 305  ? 0.3990 0.2945 0.2350 -0.1094 -0.0441 0.0682  303  LEU B O   
11178 C CB  . LEU B 305  ? 0.4440 0.3257 0.2685 -0.1017 -0.0478 0.0687  303  LEU B CB  
11179 C CG  . LEU B 305  ? 0.4134 0.2962 0.2455 -0.0926 -0.0479 0.0631  303  LEU B CG  
11180 C CD1 . LEU B 305  ? 0.4870 0.3608 0.3143 -0.0874 -0.0509 0.0624  303  LEU B CD1 
11181 C CD2 . LEU B 305  ? 0.4561 0.3328 0.2922 -0.0912 -0.0499 0.0606  303  LEU B CD2 
11182 N N   . ASN B 306  ? 0.3581 0.2776 0.2045 -0.1033 -0.0370 0.0648  304  ASN B N   
11183 C CA  . ASN B 306  ? 0.3784 0.3062 0.2331 -0.1036 -0.0349 0.0627  304  ASN B CA  
11184 C C   . ASN B 306  ? 0.3426 0.2699 0.2046 -0.0954 -0.0352 0.0574  304  ASN B C   
11185 O O   . ASN B 306  ? 0.3623 0.2926 0.2265 -0.0894 -0.0341 0.0549  304  ASN B O   
11186 C CB  . ASN B 306  ? 0.4071 0.3530 0.2667 -0.1061 -0.0298 0.0636  304  ASN B CB  
11187 C CG  . ASN B 306  ? 0.4237 0.3788 0.2924 -0.1054 -0.0277 0.0611  304  ASN B CG  
11188 O OD1 . ASN B 306  ? 0.4114 0.3661 0.2802 -0.1110 -0.0284 0.0629  304  ASN B OD1 
11189 N ND2 . ASN B 306  ? 0.3511 0.3140 0.2273 -0.0984 -0.0253 0.0569  304  ASN B ND2 
11190 N N   . ILE B 307  ? 0.3444 0.2680 0.2100 -0.0954 -0.0366 0.0556  305  ILE B N   
11191 C CA  . ILE B 307  ? 0.3217 0.2462 0.1948 -0.0882 -0.0364 0.0507  305  ILE B CA  
11192 C C   . ILE B 307  ? 0.3468 0.2868 0.2286 -0.0881 -0.0321 0.0491  305  ILE B C   
11193 O O   . ILE B 307  ? 0.3367 0.2802 0.2203 -0.0928 -0.0316 0.0503  305  ILE B O   
11194 C CB  . ILE B 307  ? 0.3458 0.2571 0.2174 -0.0875 -0.0404 0.0494  305  ILE B CB  
11195 C CG1 . ILE B 307  ? 0.4133 0.3091 0.2764 -0.0865 -0.0448 0.0507  305  ILE B CG1 
11196 C CG2 . ILE B 307  ? 0.3365 0.2509 0.2166 -0.0808 -0.0396 0.0446  305  ILE B CG2 
11197 C CD1 . ILE B 307  ? 0.4517 0.3335 0.3118 -0.0864 -0.0490 0.0499  305  ILE B CD1 
11198 N N   . ASP B 308  ? 0.3213 0.2704 0.2082 -0.0826 -0.0292 0.0465  306  ASP B N   
11199 C CA  . ASP B 308  ? 0.3205 0.2838 0.2158 -0.0813 -0.0253 0.0446  306  ASP B CA  
11200 C C   . ASP B 308  ? 0.3098 0.2709 0.2108 -0.0790 -0.0263 0.0417  306  ASP B C   
11201 O O   . ASP B 308  ? 0.3293 0.2797 0.2294 -0.0758 -0.0293 0.0398  306  ASP B O   
11202 C CB  . ASP B 308  ? 0.3236 0.2947 0.2226 -0.0752 -0.0227 0.0420  306  ASP B CB  
11203 C CG  . ASP B 308  ? 0.3456 0.3225 0.2400 -0.0773 -0.0206 0.0446  306  ASP B CG  
11204 O OD1 . ASP B 308  ? 0.3313 0.3084 0.2207 -0.0839 -0.0207 0.0486  306  ASP B OD1 
11205 O OD2 . ASP B 308  ? 0.3796 0.3607 0.2753 -0.0724 -0.0191 0.0426  306  ASP B OD2 
11206 N N   . ALA B 309  ? 0.2882 0.2602 0.1951 -0.0805 -0.0236 0.0412  307  ALA B N   
11207 C CA  . ALA B 309  ? 0.2697 0.2412 0.1823 -0.0785 -0.0241 0.0385  307  ALA B CA  
11208 C C   . ALA B 309  ? 0.2999 0.2794 0.2200 -0.0716 -0.0215 0.0347  307  ALA B C   
11209 O O   . ALA B 309  ? 0.2767 0.2669 0.1993 -0.0704 -0.0183 0.0346  307  ALA B O   
11210 C CB  . ALA B 309  ? 0.2967 0.2748 0.2112 -0.0844 -0.0231 0.0404  307  ALA B CB  
11211 N N   . GLU B 310  ? 0.2731 0.2468 0.1962 -0.0671 -0.0230 0.0315  308  GLU B N   
11212 C CA  . GLU B 310  ? 0.2613 0.2405 0.1909 -0.0605 -0.0211 0.0279  308  GLU B CA  
11213 C C   . GLU B 310  ? 0.2518 0.2351 0.1877 -0.0595 -0.0203 0.0259  308  GLU B C   
11214 O O   . GLU B 310  ? 0.2508 0.2403 0.1879 -0.0637 -0.0192 0.0274  308  GLU B O   
11215 C CB  . GLU B 310  ? 0.2691 0.2388 0.1968 -0.0555 -0.0235 0.0260  308  GLU B CB  
11216 C CG  . GLU B 310  ? 0.2945 0.2609 0.2157 -0.0567 -0.0242 0.0282  308  GLU B CG  
11217 C CD  . GLU B 310  ? 0.3222 0.2809 0.2421 -0.0516 -0.0264 0.0263  308  GLU B CD  
11218 O OE1 . GLU B 310  ? 0.3212 0.2850 0.2453 -0.0468 -0.0248 0.0238  308  GLU B OE1 
11219 O OE2 . GLU B 310  ? 0.2945 0.2420 0.2089 -0.0523 -0.0298 0.0274  308  GLU B OE2 
11220 N N   . GLU B 311  ? 0.2326 0.2127 0.1722 -0.0541 -0.0209 0.0226  309  GLU B N   
11221 C CA  . GLU B 311  ? 0.2235 0.2081 0.1691 -0.0526 -0.0199 0.0206  309  GLU B CA  
11222 C C   . GLU B 311  ? 0.2673 0.2458 0.2106 -0.0567 -0.0222 0.0216  309  GLU B C   
11223 O O   . GLU B 311  ? 0.2729 0.2410 0.2102 -0.0592 -0.0252 0.0230  309  GLU B O   
11224 C CB  . GLU B 311  ? 0.2362 0.2183 0.1859 -0.0461 -0.0201 0.0171  309  GLU B CB  
11225 C CG  . GLU B 311  ? 0.2958 0.2841 0.2483 -0.0419 -0.0179 0.0157  309  GLU B CG  
11226 C CD  . GLU B 311  ? 0.3294 0.3113 0.2774 -0.0403 -0.0195 0.0160  309  GLU B CD  
11227 O OE1 . GLU B 311  ? 0.2927 0.2665 0.2347 -0.0432 -0.0220 0.0179  309  GLU B OE1 
11228 O OE2 . GLU B 311  ? 0.3799 0.3646 0.3302 -0.0362 -0.0184 0.0142  309  GLU B OE2 
11229 N N   . ALA B 312  ? 0.2297 0.2143 0.1777 -0.0574 -0.0209 0.0208  310  ALA B N   
11230 C CA  . ALA B 312  ? 0.2697 0.2495 0.2156 -0.0616 -0.0230 0.0216  310  ALA B CA  
11231 C C   . ALA B 312  ? 0.2553 0.2219 0.1981 -0.0594 -0.0263 0.0200  310  ALA B C   
11232 O O   . ALA B 312  ? 0.2830 0.2411 0.2206 -0.0633 -0.0291 0.0214  310  ALA B O   
11233 C CB  . ALA B 312  ? 0.2466 0.2357 0.1985 -0.0617 -0.0211 0.0206  310  ALA B CB  
11234 N N   . ASP B 313  ? 0.2640 0.2285 0.2096 -0.0531 -0.0262 0.0171  311  ASP B N   
11235 C CA  . ASP B 313  ? 0.2624 0.2154 0.2056 -0.0505 -0.0292 0.0154  311  ASP B CA  
11236 C C   . ASP B 313  ? 0.2874 0.2300 0.2240 -0.0506 -0.0319 0.0166  311  ASP B C   
11237 O O   . ASP B 313  ? 0.3043 0.2371 0.2385 -0.0480 -0.0346 0.0152  311  ASP B O   
11238 C CB  . ASP B 313  ? 0.2633 0.2185 0.2123 -0.0439 -0.0281 0.0119  311  ASP B CB  
11239 C CG  . ASP B 313  ? 0.2982 0.2573 0.2498 -0.0398 -0.0266 0.0110  311  ASP B CG  
11240 O OD1 . ASP B 313  ? 0.3024 0.2617 0.2508 -0.0413 -0.0265 0.0129  311  ASP B OD1 
11241 O OD2 . ASP B 313  ? 0.3354 0.2971 0.2919 -0.0351 -0.0255 0.0084  311  ASP B OD2 
11242 N N   . ARG B 314  ? 0.2571 0.2016 0.1905 -0.0537 -0.0315 0.0192  312  ARG B N   
11243 C CA  . ARG B 314  ? 0.2857 0.2200 0.2119 -0.0548 -0.0343 0.0210  312  ARG B CA  
11244 C C   . ARG B 314  ? 0.2889 0.2187 0.2086 -0.0620 -0.0359 0.0245  312  ARG B C   
11245 O O   . ARG B 314  ? 0.2790 0.1989 0.1918 -0.0635 -0.0387 0.0263  312  ARG B O   
11246 C CB  . ARG B 314  ? 0.2916 0.2302 0.2180 -0.0527 -0.0328 0.0215  312  ARG B CB  
11247 C CG  . ARG B 314  ? 0.2861 0.2246 0.2167 -0.0457 -0.0327 0.0182  312  ARG B CG  
11248 C CD  . ARG B 314  ? 0.2993 0.2452 0.2319 -0.0436 -0.0304 0.0181  312  ARG B CD  
11249 N NE  . ARG B 314  ? 0.2980 0.2412 0.2328 -0.0376 -0.0313 0.0155  312  ARG B NE  
11250 C CZ  . ARG B 314  ? 0.3110 0.2594 0.2480 -0.0347 -0.0298 0.0146  312  ARG B CZ  
11251 N NH1 . ARG B 314  ? 0.2856 0.2429 0.2236 -0.0363 -0.0270 0.0156  312  ARG B NH1 
11252 N NH2 . ARG B 314  ? 0.3160 0.2607 0.2542 -0.0299 -0.0313 0.0126  312  ARG B NH2 
11253 N N   . LEU B 315  ? 0.2764 0.2131 0.1981 -0.0666 -0.0345 0.0257  313  LEU B N   
11254 C CA  . LEU B 315  ? 0.2929 0.2267 0.2087 -0.0742 -0.0359 0.0294  313  LEU B CA  
11255 C C   . LEU B 315  ? 0.3291 0.2473 0.2379 -0.0758 -0.0403 0.0298  313  LEU B C   
11256 O O   . LEU B 315  ? 0.3293 0.2390 0.2308 -0.0790 -0.0426 0.0324  313  LEU B O   
11257 C CB  . LEU B 315  ? 0.2937 0.2381 0.2138 -0.0784 -0.0338 0.0301  313  LEU B CB  
11258 C CG  . LEU B 315  ? 0.2908 0.2387 0.2073 -0.0867 -0.0336 0.0343  313  LEU B CG  
11259 C CD1 . LEU B 315  ? 0.3057 0.2662 0.2283 -0.0892 -0.0312 0.0343  313  LEU B CD1 
11260 C CD2 . LEU B 315  ? 0.3657 0.2997 0.2738 -0.0919 -0.0378 0.0365  313  LEU B CD2 
11261 N N   . GLU B 316  ? 0.3173 0.2310 0.2277 -0.0735 -0.0416 0.0271  314  GLU B N   
11262 C CA  . GLU B 316  ? 0.3158 0.2146 0.2190 -0.0754 -0.0459 0.0274  314  GLU B CA  
11263 C C   . GLU B 316  ? 0.3305 0.2178 0.2290 -0.0709 -0.0486 0.0267  314  GLU B C   
11264 O O   . GLU B 316  ? 0.3641 0.2391 0.2544 -0.0737 -0.0521 0.0286  314  GLU B O   
11265 C CB  . GLU B 316  ? 0.3593 0.2567 0.2651 -0.0741 -0.0465 0.0247  314  GLU B CB  
11266 C CG  . GLU B 316  ? 0.3132 0.2195 0.2214 -0.0803 -0.0450 0.0263  314  GLU B CG  
11267 C CD  . GLU B 316  ? 0.3627 0.2680 0.2731 -0.0795 -0.0457 0.0238  314  GLU B CD  
11268 O OE1 . GLU B 316  ? 0.3882 0.2807 0.2936 -0.0784 -0.0491 0.0224  314  GLU B OE1 
11269 O OE2 . GLU B 316  ? 0.3552 0.2725 0.2721 -0.0799 -0.0430 0.0231  314  GLU B OE2 
11270 N N   . LEU B 317  ? 0.3227 0.2140 0.2261 -0.0641 -0.0470 0.0242  315  LEU B N   
11271 C CA  . LEU B 317  ? 0.3575 0.2396 0.2570 -0.0598 -0.0494 0.0237  315  LEU B CA  
11272 C C   . LEU B 317  ? 0.3610 0.2397 0.2539 -0.0641 -0.0505 0.0275  315  LEU B C   
11273 O O   . LEU B 317  ? 0.3584 0.2243 0.2439 -0.0642 -0.0541 0.0286  315  LEU B O   
11274 C CB  . LEU B 317  ? 0.3420 0.2314 0.2485 -0.0528 -0.0472 0.0208  315  LEU B CB  
11275 C CG  . LEU B 317  ? 0.3570 0.2389 0.2607 -0.0479 -0.0494 0.0201  315  LEU B CG  
11276 C CD1 . LEU B 317  ? 0.4470 0.3146 0.3451 -0.0461 -0.0536 0.0191  315  LEU B CD1 
11277 C CD2 . LEU B 317  ? 0.3561 0.2461 0.2674 -0.0416 -0.0472 0.0170  315  LEU B CD2 
11278 N N   . SER B 318  ? 0.3250 0.2148 0.2201 -0.0676 -0.0473 0.0296  316  SER B N   
11279 C CA  . SER B 318  ? 0.3172 0.2045 0.2060 -0.0716 -0.0480 0.0334  316  SER B CA  
11280 C C   . SER B 318  ? 0.3165 0.1930 0.1967 -0.0784 -0.0513 0.0366  316  SER B C   
11281 O O   . SER B 318  ? 0.3709 0.2390 0.2437 -0.0804 -0.0536 0.0393  316  SER B O   
11282 C CB  . SER B 318  ? 0.3290 0.2312 0.2219 -0.0740 -0.0438 0.0349  316  SER B CB  
11283 O OG  . SER B 318  ? 0.3382 0.2471 0.2325 -0.0801 -0.0423 0.0366  316  SER B OG  
11284 N N   . LEU B 319  ? 0.3397 0.2155 0.2206 -0.0819 -0.0518 0.0364  317  LEU B N   
11285 C CA  . LEU B 319  ? 0.3597 0.2243 0.2322 -0.0886 -0.0552 0.0393  317  LEU B CA  
11286 C C   . LEU B 319  ? 0.3684 0.2154 0.2336 -0.0856 -0.0600 0.0386  317  LEU B C   
11287 O O   . LEU B 319  ? 0.3816 0.2173 0.2379 -0.0904 -0.0632 0.0417  317  LEU B O   
11288 C CB  . LEU B 319  ? 0.3567 0.2242 0.2317 -0.0924 -0.0550 0.0388  317  LEU B CB  
11289 C CG  . LEU B 319  ? 0.3675 0.2524 0.2496 -0.0959 -0.0507 0.0397  317  LEU B CG  
11290 C CD1 . LEU B 319  ? 0.3308 0.2169 0.2151 -0.0987 -0.0512 0.0386  317  LEU B CD1 
11291 C CD2 . LEU B 319  ? 0.3634 0.2525 0.2416 -0.1031 -0.0498 0.0445  317  LEU B CD2 
11292 N N   . ASP B 320  ? 0.3670 0.2112 0.2355 -0.0777 -0.0605 0.0346  318  ASP B N   
11293 C CA  . ASP B 320  ? 0.4203 0.2484 0.2820 -0.0741 -0.0650 0.0337  318  ASP B CA  
11294 C C   . ASP B 320  ? 0.4165 0.2395 0.2727 -0.0735 -0.0664 0.0361  318  ASP B C   
11295 O O   . ASP B 320  ? 0.4538 0.2621 0.3014 -0.0740 -0.0706 0.0374  318  ASP B O   
11296 C CB  . ASP B 320  ? 0.4030 0.2311 0.2702 -0.0656 -0.0649 0.0289  318  ASP B CB  
11297 C CG  . ASP B 320  ? 0.4083 0.2357 0.2776 -0.0660 -0.0650 0.0266  318  ASP B CG  
11298 O OD1 . ASP B 320  ? 0.4493 0.2655 0.3115 -0.0702 -0.0683 0.0278  318  ASP B OD1 
11299 O OD2 . ASP B 320  ? 0.4231 0.2608 0.3006 -0.0625 -0.0620 0.0238  318  ASP B OD2 
11300 N N   . LEU B 321  ? 0.3660 0.2008 0.2268 -0.0724 -0.0630 0.0366  319  LEU B N   
11301 C CA  . LEU B 321  ? 0.3826 0.2133 0.2378 -0.0727 -0.0643 0.0393  319  LEU B CA  
11302 C C   . LEU B 321  ? 0.4048 0.2324 0.2525 -0.0815 -0.0650 0.0443  319  LEU B C   
11303 O O   . LEU B 321  ? 0.4382 0.2539 0.2770 -0.0832 -0.0684 0.0469  319  LEU B O   
11304 C CB  . LEU B 321  ? 0.3787 0.2224 0.2405 -0.0688 -0.0606 0.0382  319  LEU B CB  
11305 C CG  . LEU B 321  ? 0.3812 0.2257 0.2484 -0.0599 -0.0607 0.0339  319  LEU B CG  
11306 C CD1 . LEU B 321  ? 0.3853 0.2390 0.2618 -0.0570 -0.0579 0.0303  319  LEU B CD1 
11307 C CD2 . LEU B 321  ? 0.4332 0.2842 0.3021 -0.0570 -0.0591 0.0341  319  LEU B CD2 
11308 N N   . LEU B 322  ? 0.3809 0.2192 0.2320 -0.0874 -0.0620 0.0458  320  LEU B N   
11309 C CA  . LEU B 322  ? 0.3934 0.2301 0.2380 -0.0964 -0.0625 0.0507  320  LEU B CA  
11310 C C   . LEU B 322  ? 0.4218 0.2407 0.2569 -0.1001 -0.0676 0.0523  320  LEU B C   
11311 O O   . LEU B 322  ? 0.4541 0.2646 0.2805 -0.1052 -0.0699 0.0563  320  LEU B O   
11312 C CB  . LEU B 322  ? 0.3707 0.2221 0.2215 -0.1016 -0.0586 0.0514  320  LEU B CB  
11313 C CG  . LEU B 322  ? 0.4286 0.2814 0.2739 -0.1113 -0.0585 0.0567  320  LEU B CG  
11314 C CD1 . LEU B 322  ? 0.4344 0.2907 0.2765 -0.1118 -0.0571 0.0595  320  LEU B CD1 
11315 C CD2 . LEU B 322  ? 0.4109 0.2786 0.2631 -0.1159 -0.0550 0.0570  320  LEU B CD2 
11316 N N   . GLU B 323  ? 0.4137 0.2265 0.2502 -0.0975 -0.0694 0.0491  321  GLU B N   
11317 C CA  . GLU B 323  ? 0.4438 0.2388 0.2712 -0.1001 -0.0745 0.0500  321  GLU B CA  
11318 C C   . GLU B 323  ? 0.4350 0.2152 0.2539 -0.0971 -0.0785 0.0511  321  GLU B C   
11319 O O   . GLU B 323  ? 0.4935 0.2614 0.3024 -0.1026 -0.0819 0.0547  321  GLU B O   
11320 C CB  . GLU B 323  ? 0.4819 0.2738 0.3130 -0.0957 -0.0755 0.0455  321  GLU B CB  
11321 C CG  . GLU B 323  ? 0.5320 0.3044 0.3537 -0.0969 -0.0809 0.0455  321  GLU B CG  
11322 C CD  . GLU B 323  ? 0.5942 0.3642 0.4124 -0.1060 -0.0820 0.0478  321  GLU B CD  
11323 O OE1 . GLU B 323  ? 0.5384 0.3230 0.3630 -0.1104 -0.0784 0.0487  321  GLU B OE1 
11324 O OE2 . GLU B 323  ? 0.5790 0.3323 0.3877 -0.1088 -0.0867 0.0488  321  GLU B OE2 
11325 N N   . VAL B 324  ? 0.4373 0.2183 0.2597 -0.0883 -0.0782 0.0479  322  VAL B N   
11326 C CA  . VAL B 324  ? 0.5032 0.2707 0.3181 -0.0845 -0.0821 0.0486  322  VAL B CA  
11327 C C   . VAL B 324  ? 0.4945 0.2620 0.3034 -0.0896 -0.0821 0.0534  322  VAL B C   
11328 O O   . VAL B 324  ? 0.5059 0.2587 0.3044 -0.0920 -0.0862 0.0563  322  VAL B O   
11329 C CB  . VAL B 324  ? 0.5116 0.2827 0.3329 -0.0742 -0.0815 0.0442  322  VAL B CB  
11330 C CG1 . VAL B 324  ? 0.5387 0.2979 0.3529 -0.0702 -0.0853 0.0451  322  VAL B CG1 
11331 C CG2 . VAL B 324  ? 0.5161 0.2852 0.3418 -0.0692 -0.0820 0.0396  322  VAL B CG2 
11332 N N   . LEU B 325  ? 0.4853 0.2689 0.3002 -0.0912 -0.0775 0.0544  323  LEU B N   
11333 C CA  . LEU B 325  ? 0.5310 0.3160 0.3406 -0.0955 -0.0770 0.0588  323  LEU B CA  
11334 C C   . LEU B 325  ? 0.5008 0.2788 0.3018 -0.1055 -0.0787 0.0638  323  LEU B C   
11335 O O   . LEU B 325  ? 0.5087 0.2775 0.3005 -0.1087 -0.0812 0.0676  323  LEU B O   
11336 C CB  . LEU B 325  ? 0.4930 0.2972 0.3110 -0.0951 -0.0714 0.0584  323  LEU B CB  
11337 C CG  . LEU B 325  ? 0.4495 0.2603 0.2752 -0.0857 -0.0698 0.0539  323  LEU B CG  
11338 C CD1 . LEU B 325  ? 0.4548 0.2845 0.2896 -0.0855 -0.0643 0.0529  323  LEU B CD1 
11339 C CD2 . LEU B 325  ? 0.4569 0.2593 0.2766 -0.0818 -0.0726 0.0548  323  LEU B CD2 
11340 N N   . CYS B 326  ? 0.4867 0.2689 0.2904 -0.1109 -0.0776 0.0639  324  CYS B N   
11341 C CA  . CYS B 326  ? 0.4880 0.2643 0.2840 -0.1210 -0.0792 0.0688  324  CYS B CA  
11342 C C   . CYS B 326  ? 0.5040 0.2583 0.2890 -0.1221 -0.0854 0.0699  324  CYS B C   
11343 O O   . CYS B 326  ? 0.5273 0.2733 0.3032 -0.1301 -0.0877 0.0747  324  CYS B O   
11344 C CB  . CYS B 326  ? 0.5084 0.2957 0.3105 -0.1265 -0.0765 0.0686  324  CYS B CB  
11345 S SG  . CYS B 326  ? 0.5092 0.3220 0.3221 -0.1274 -0.0695 0.0689  324  CYS B SG  
11346 N N   . LEU B 327  ? 0.4908 0.2353 0.2760 -0.1144 -0.0882 0.0657  325  LEU B N   
11347 C CA  . LEU B 327  ? 0.5239 0.2467 0.2985 -0.1140 -0.0943 0.0661  325  LEU B CA  
11348 C C   . LEU B 327  ? 0.5565 0.2690 0.3250 -0.1082 -0.0972 0.0665  325  LEU B C   
11349 O O   . LEU B 327  ? 0.5998 0.2936 0.3588 -0.1074 -0.1025 0.0672  325  LEU B O   
11350 C CB  . LEU B 327  ? 0.5074 0.2249 0.2850 -0.1090 -0.0959 0.0612  325  LEU B CB  
11351 C CG  . LEU B 327  ? 0.5597 0.2820 0.3401 -0.1157 -0.0947 0.0613  325  LEU B CG  
11352 C CD1 . LEU B 327  ? 0.6327 0.3549 0.4189 -0.1094 -0.0948 0.0557  325  LEU B CD1 
11353 C CD2 . LEU B 327  ? 0.7065 0.4140 0.4755 -0.1248 -0.0989 0.0655  325  LEU B CD2 
11354 N N   . ASP B 328  ? 0.5372 0.2611 0.3108 -0.1043 -0.0941 0.0662  326  ASP B N   
11355 C CA  . ASP B 328  ? 0.5482 0.2639 0.3169 -0.0984 -0.0968 0.0664  326  ASP B CA  
11356 C C   . ASP B 328  ? 0.5397 0.2458 0.2968 -0.1055 -0.0992 0.0724  326  ASP B C   
11357 O O   . ASP B 328  ? 0.6225 0.3393 0.3802 -0.1112 -0.0960 0.0758  326  ASP B O   
11358 C CB  . ASP B 328  ? 0.5469 0.2785 0.3250 -0.0923 -0.0926 0.0640  326  ASP B CB  
11359 C CG  . ASP B 328  ? 0.6076 0.3317 0.3822 -0.0849 -0.0954 0.0632  326  ASP B CG  
11360 O OD1 . ASP B 328  ? 0.6157 0.3246 0.3794 -0.0865 -0.0999 0.0663  326  ASP B OD1 
11361 O OD2 . ASP B 328  ? 0.6501 0.3840 0.4330 -0.0777 -0.0933 0.0596  326  ASP B OD2 
11362 N N   . GLY B 329  ? 0.6391 0.3251 0.3854 -0.1049 -0.1050 0.0736  327  GLY B N   
11363 C CA  . GLY B 329  ? 0.6269 0.3071 0.3645 -0.1102 -0.1070 0.0775  327  GLY B CA  
11364 C C   . GLY B 329  ? 0.6009 0.2858 0.3367 -0.1092 -0.1057 0.0802  327  GLY B C   
11365 O O   . GLY B 329  ? 0.6355 0.3212 0.3660 -0.1154 -0.1055 0.0840  327  GLY B O   
11366 N N   . ASP B 330  ? 0.6026 0.2921 0.3433 -0.1012 -0.1047 0.0778  328  ASP B N   
11367 C CA  . ASP B 330  ? 0.5983 0.2949 0.3385 -0.1000 -0.1030 0.0797  328  ASP B CA  
11368 C C   . ASP B 330  ? 0.6342 0.3473 0.3780 -0.1074 -0.0976 0.0827  328  ASP B C   
11369 O O   . ASP B 330  ? 0.6488 0.3650 0.3885 -0.1094 -0.0967 0.0860  328  ASP B O   
11370 C CB  . ASP B 330  ? 0.6367 0.3407 0.3854 -0.0893 -0.1019 0.0747  328  ASP B CB  
11371 C CG  . ASP B 330  ? 0.6883 0.3766 0.4326 -0.0815 -0.1073 0.0724  328  ASP B CG  
11372 O OD1 . ASP B 330  ? 0.7125 0.3837 0.4457 -0.0839 -0.1121 0.0752  328  ASP B OD1 
11373 O OD2 . ASP B 330  ? 0.6390 0.3324 0.3911 -0.0728 -0.1068 0.0676  328  ASP B OD2 
11374 N N   . LEU B 331  ? 0.5796 0.3034 0.3306 -0.1113 -0.0941 0.0816  329  LEU B N   
11375 C CA  . LEU B 331  ? 0.5511 0.2914 0.3061 -0.1181 -0.0889 0.0842  329  LEU B CA  
11376 C C   . LEU B 331  ? 0.5514 0.2866 0.2990 -0.1292 -0.0899 0.0894  329  LEU B C   
11377 O O   . LEU B 331  ? 0.5634 0.3125 0.3153 -0.1355 -0.0857 0.0912  329  LEU B O   
11378 C CB  . LEU B 331  ? 0.5073 0.2647 0.2758 -0.1151 -0.0841 0.0797  329  LEU B CB  
11379 C CG  . LEU B 331  ? 0.4853 0.2482 0.2617 -0.1044 -0.0831 0.0744  329  LEU B CG  
11380 C CD1 . LEU B 331  ? 0.4990 0.2774 0.2880 -0.1020 -0.0787 0.0703  329  LEU B CD1 
11381 C CD2 . LEU B 331  ? 0.5551 0.3239 0.3301 -0.1023 -0.0816 0.0758  329  LEU B CD2 
11382 N N   . SER B 332  ? 0.6056 0.3244 0.3447 -0.1305 -0.0949 0.0902  330  SER B N   
11383 C CA  . SER B 332  ? 0.5714 0.2880 0.3066 -0.1391 -0.0959 0.0925  330  SER B CA  
11384 C C   . SER B 332  ? 0.6464 0.3760 0.3814 -0.1469 -0.0921 0.0969  330  SER B C   
11385 O O   . SER B 332  ? 0.7196 0.4512 0.4513 -0.1460 -0.0913 0.0990  330  SER B O   
11386 C CB  . SER B 332  ? 0.6366 0.3349 0.3622 -0.1376 -0.1017 0.0925  330  SER B CB  
11387 O OG  . SER B 332  ? 0.7815 0.4768 0.5024 -0.1461 -0.1031 0.0950  330  SER B OG  
11388 N N   . GLY B 333  ? 0.5878 0.3265 0.3263 -0.1544 -0.0897 0.0982  331  GLY B N   
11389 C CA  . GLY B 333  ? 0.7291 0.4804 0.4676 -0.1623 -0.0863 0.1022  331  GLY B CA  
11390 C C   . GLY B 333  ? 0.7247 0.4946 0.4701 -0.1618 -0.0803 0.1029  331  GLY B C   
11391 O O   . GLY B 333  ? 0.6401 0.4226 0.3865 -0.1680 -0.0769 0.1060  331  GLY B O   
11392 N N   . TRP B 334  ? 0.5968 0.3693 0.3469 -0.1545 -0.0790 0.1002  332  TRP B N   
11393 C CA  . TRP B 334  ? 0.6386 0.4284 0.3948 -0.1532 -0.0735 0.1005  332  TRP B CA  
11394 C C   . TRP B 334  ? 0.5390 0.3439 0.3055 -0.1556 -0.0695 0.0986  332  TRP B C   
11395 O O   . TRP B 334  ? 0.6063 0.4091 0.3785 -0.1517 -0.0705 0.0944  332  TRP B O   
11396 C CB  . TRP B 334  ? 0.5795 0.3691 0.3400 -0.1418 -0.0736 0.0956  332  TRP B CB  
11397 C CG  . TRP B 334  ? 0.5693 0.3788 0.3398 -0.1374 -0.0679 0.0928  332  TRP B CG  
11398 C CD1 . TRP B 334  ? 0.5801 0.4022 0.3503 -0.1400 -0.0640 0.0954  332  TRP B CD1 
11399 C CD2 . TRP B 334  ? 0.5399 0.3580 0.3215 -0.1293 -0.0657 0.0868  332  TRP B CD2 
11400 N NE1 . TRP B 334  ? 0.5092 0.3469 0.2896 -0.1338 -0.0596 0.0912  332  TRP B NE1 
11401 C CE2 . TRP B 334  ? 0.4757 0.3112 0.2633 -0.1274 -0.0606 0.0861  332  TRP B CE2 
11402 C CE3 . TRP B 334  ? 0.5216 0.3346 0.3085 -0.1235 -0.0676 0.0822  332  TRP B CE3 
11403 C CZ2 . TRP B 334  ? 0.4289 0.2758 0.2273 -0.1201 -0.0575 0.0808  332  TRP B CZ2 
11404 C CZ3 . TRP B 334  ? 0.5362 0.3611 0.3339 -0.1165 -0.0644 0.0772  332  TRP B CZ3 
11405 C CH2 . TRP B 334  ? 0.5295 0.3709 0.3328 -0.1150 -0.0595 0.0766  332  TRP B CH2 
11406 N N   . ASN B 335  ? 0.5546 0.3751 0.3236 -0.1621 -0.0651 0.1017  333  ASN B N   
11407 C CA  . ASN B 335  ? 0.5523 0.3886 0.3312 -0.1646 -0.0613 0.1002  333  ASN B CA  
11408 C C   . ASN B 335  ? 0.5094 0.3644 0.2990 -0.1579 -0.0559 0.0964  333  ASN B C   
11409 O O   . ASN B 335  ? 0.5128 0.3839 0.3104 -0.1602 -0.0518 0.0959  333  ASN B O   
11410 C CB  . ASN B 335  ? 0.5277 0.3721 0.3055 -0.1745 -0.0598 0.1043  333  ASN B CB  
11411 C CG  . ASN B 335  ? 0.6463 0.4762 0.4183 -0.1791 -0.0649 0.1050  333  ASN B CG  
11412 O OD1 . ASN B 335  ? 0.5733 0.3900 0.3441 -0.1763 -0.0688 0.1025  333  ASN B OD1 
11413 N ND2 . ASN B 335  ? 0.6368 0.4691 0.4049 -0.1861 -0.0651 0.1084  333  ASN B ND2 
11414 N N   . GLY B 336  ? 0.5123 0.3655 0.3020 -0.1497 -0.0559 0.0938  334  GLY B N   
11415 C CA  . GLY B 336  ? 0.4745 0.3443 0.2732 -0.1435 -0.0510 0.0904  334  GLY B CA  
11416 C C   . GLY B 336  ? 0.4628 0.3358 0.2713 -0.1355 -0.0504 0.0843  334  GLY B C   
11417 O O   . GLY B 336  ? 0.4436 0.3297 0.2597 -0.1301 -0.0466 0.0813  334  GLY B O   
11418 N N   . MET B 337  ? 0.4684 0.3298 0.2769 -0.1344 -0.0540 0.0824  335  MET B N   
11419 C CA  A MET B 337  ? 0.4367 0.3018 0.2546 -0.1272 -0.0533 0.0768  335  MET B CA  
11420 C CA  B MET B 337  ? 0.4381 0.3030 0.2559 -0.1273 -0.0533 0.0768  335  MET B CA  
11421 C C   . MET B 337  ? 0.4783 0.3609 0.3055 -0.1295 -0.0487 0.0759  335  MET B C   
11422 O O   . MET B 337  ? 0.4735 0.3580 0.2999 -0.1370 -0.0487 0.0785  335  MET B O   
11423 C CB  A MET B 337  ? 0.4768 0.3256 0.2919 -0.1259 -0.0581 0.0751  335  MET B CB  
11424 C CB  B MET B 337  ? 0.4774 0.3259 0.2921 -0.1266 -0.0582 0.0754  335  MET B CB  
11425 C CG  A MET B 337  ? 0.4366 0.2874 0.2604 -0.1175 -0.0577 0.0692  335  MET B CG  
11426 C CG  B MET B 337  ? 0.4972 0.3495 0.3211 -0.1212 -0.0575 0.0703  335  MET B CG  
11427 S SD  A MET B 337  ? 0.5431 0.3924 0.3685 -0.1072 -0.0580 0.0658  335  MET B SD  
11428 S SD  B MET B 337  ? 0.4434 0.2971 0.2731 -0.1093 -0.0569 0.0649  335  MET B SD  
11429 C CE  A MET B 337  ? 0.4266 0.2972 0.2647 -0.1031 -0.0519 0.0623  335  MET B CE  
11430 C CE  B MET B 337  ? 0.5413 0.3749 0.3599 -0.1070 -0.0625 0.0663  335  MET B CE  
11431 N N   . GLY B 338  ? 0.4232 0.3186 0.2589 -0.1232 -0.0449 0.0723  336  GLY B N   
11432 C CA  . GLY B 338  ? 0.4167 0.3295 0.2615 -0.1241 -0.0404 0.0711  336  GLY B CA  
11433 C C   . GLY B 338  ? 0.4245 0.3395 0.2780 -0.1174 -0.0400 0.0658  336  GLY B C   
11434 O O   . GLY B 338  ? 0.4004 0.3082 0.2547 -0.1102 -0.0417 0.0625  336  GLY B O   
11435 N N   . PHE B 339  ? 0.3824 0.3077 0.2425 -0.1198 -0.0377 0.0651  337  PHE B N   
11436 C CA  . PHE B 339  ? 0.3558 0.2830 0.2238 -0.1142 -0.0374 0.0604  337  PHE B CA  
11437 C C   . PHE B 339  ? 0.3680 0.3130 0.2445 -0.1155 -0.0331 0.0599  337  PHE B C   
11438 O O   . PHE B 339  ? 0.3699 0.3208 0.2457 -0.1228 -0.0322 0.0631  337  PHE B O   
11439 C CB  . PHE B 339  ? 0.3673 0.2805 0.2322 -0.1160 -0.0418 0.0600  337  PHE B CB  
11440 C CG  . PHE B 339  ? 0.3310 0.2434 0.2025 -0.1095 -0.0421 0.0551  337  PHE B CG  
11441 C CD1 . PHE B 339  ? 0.3909 0.2944 0.2621 -0.1020 -0.0440 0.0518  337  PHE B CD1 
11442 C CD2 . PHE B 339  ? 0.3361 0.2569 0.2141 -0.1110 -0.0405 0.0538  337  PHE B CD2 
11443 C CE1 . PHE B 339  ? 0.3413 0.2445 0.2186 -0.0963 -0.0441 0.0475  337  PHE B CE1 
11444 C CE2 . PHE B 339  ? 0.3674 0.2873 0.2511 -0.1052 -0.0407 0.0494  337  PHE B CE2 
11445 C CZ  . PHE B 339  ? 0.3813 0.2926 0.2647 -0.0979 -0.0424 0.0463  337  PHE B CZ  
11446 N N   . VAL B 340  ? 0.3298 0.2834 0.2140 -0.1084 -0.0304 0.0559  338  VAL B N   
11447 C CA  . VAL B 340  ? 0.2982 0.2685 0.1907 -0.1083 -0.0262 0.0549  338  VAL B CA  
11448 C C   . VAL B 340  ? 0.3523 0.3221 0.2497 -0.1084 -0.0273 0.0528  338  VAL B C   
11449 O O   . VAL B 340  ? 0.3303 0.2903 0.2281 -0.1039 -0.0297 0.0498  338  VAL B O   
11450 C CB  . VAL B 340  ? 0.2985 0.2777 0.1964 -0.1007 -0.0230 0.0517  338  VAL B CB  
11451 C CG1 . VAL B 340  ? 0.3137 0.3093 0.2200 -0.1000 -0.0191 0.0505  338  VAL B CG1 
11452 C CG2 . VAL B 340  ? 0.3075 0.2878 0.2003 -0.1007 -0.0220 0.0537  338  VAL B CG2 
11453 N N   . VAL B 341  ? 0.3041 0.2850 0.2053 -0.1132 -0.0253 0.0543  339  VAL B N   
11454 C CA  . VAL B 341  ? 0.3124 0.2961 0.2194 -0.1127 -0.0255 0.0520  339  VAL B CA  
11455 C C   . VAL B 341  ? 0.2857 0.2879 0.2011 -0.1108 -0.0209 0.0509  339  VAL B C   
11456 O O   . VAL B 341  ? 0.3129 0.3263 0.2286 -0.1142 -0.0182 0.0536  339  VAL B O   
11457 C CB  . VAL B 341  ? 0.3678 0.3458 0.2709 -0.1209 -0.0284 0.0547  339  VAL B CB  
11458 C CG1 . VAL B 341  ? 0.4103 0.3688 0.3046 -0.1219 -0.0331 0.0554  339  VAL B CG1 
11459 C CG2 . VAL B 341  ? 0.4905 0.4788 0.3923 -0.1289 -0.0265 0.0593  339  VAL B CG2 
11460 N N   . GLN B 342  ? 0.2899 0.2951 0.2120 -0.1052 -0.0202 0.0471  340  GLN B N   
11461 C CA  . GLN B 342  ? 0.2721 0.2931 0.2024 -0.1015 -0.0162 0.0453  340  GLN B CA  
11462 C C   . GLN B 342  ? 0.2852 0.3143 0.2200 -0.1055 -0.0158 0.0458  340  GLN B C   
11463 O O   . GLN B 342  ? 0.2727 0.2959 0.2090 -0.1045 -0.0179 0.0438  340  GLN B O   
11464 C CB  . GLN B 342  ? 0.2625 0.2813 0.1969 -0.0926 -0.0156 0.0408  340  GLN B CB  
11465 C CG  . GLN B 342  ? 0.2658 0.2784 0.1967 -0.0883 -0.0158 0.0400  340  GLN B CG  
11466 C CD  . GLN B 342  ? 0.2648 0.2686 0.1974 -0.0814 -0.0174 0.0362  340  GLN B CD  
11467 O OE1 . GLN B 342  ? 0.2829 0.2780 0.2149 -0.0816 -0.0200 0.0351  340  GLN B OE1 
11468 N NE2 . GLN B 342  ? 0.2572 0.2635 0.1919 -0.0753 -0.0157 0.0339  340  GLN B NE2 
11469 N N   . ALA B 343  ? 0.2773 0.3206 0.2146 -0.1095 -0.0130 0.0483  341  ALA B N   
11470 C CA  . ALA B 343  ? 0.2574 0.3096 0.1989 -0.1140 -0.0127 0.0492  341  ALA B CA  
11471 C C   . ALA B 343  ? 0.2624 0.3226 0.2121 -0.1079 -0.0110 0.0455  341  ALA B C   
11472 O O   . ALA B 343  ? 0.2903 0.3548 0.2433 -0.1106 -0.0116 0.0455  341  ALA B O   
11473 C CB  . ALA B 343  ? 0.2907 0.3570 0.2328 -0.1199 -0.0102 0.0530  341  ALA B CB  
11474 N N   . TYR B 344  ? 0.2670 0.3288 0.2197 -0.0999 -0.0090 0.0424  342  TYR B N   
11475 C CA  . TYR B 344  ? 0.2532 0.3200 0.2127 -0.0944 -0.0080 0.0390  342  TYR B CA  
11476 C C   . TYR B 344  ? 0.2398 0.2937 0.1983 -0.0929 -0.0113 0.0368  342  TYR B C   
11477 O O   . TYR B 344  ? 0.2550 0.3119 0.2186 -0.0890 -0.0108 0.0341  342  TYR B O   
11478 C CB  . TYR B 344  ? 0.2515 0.3241 0.2147 -0.0865 -0.0050 0.0364  342  TYR B CB  
11479 C CG  . TYR B 344  ? 0.2517 0.3131 0.2122 -0.0808 -0.0059 0.0340  342  TYR B CG  
11480 C CD1 . TYR B 344  ? 0.2430 0.2893 0.1976 -0.0822 -0.0092 0.0343  342  TYR B CD1 
11481 C CD2 . TYR B 344  ? 0.2063 0.2726 0.1703 -0.0739 -0.0034 0.0314  342  TYR B CD2 
11482 C CE1 . TYR B 344  ? 0.2407 0.2779 0.1935 -0.0767 -0.0101 0.0321  342  TYR B CE1 
11483 C CE2 . TYR B 344  ? 0.2502 0.3071 0.2121 -0.0688 -0.0043 0.0293  342  TYR B CE2 
11484 C CZ  . TYR B 344  ? 0.2570 0.3000 0.2136 -0.0703 -0.0076 0.0296  342  TYR B CZ  
11485 O OH  . TYR B 344  ? 0.2471 0.2819 0.2021 -0.0652 -0.0085 0.0275  342  TYR B OH  
11486 N N   . GLY B 345  ? 0.2557 0.2953 0.2075 -0.0959 -0.0146 0.0378  343  GLY B N   
11487 C CA  . GLY B 345  ? 0.2932 0.3199 0.2433 -0.0941 -0.0178 0.0355  343  GLY B CA  
11488 C C   . GLY B 345  ? 0.2691 0.2937 0.2179 -0.1005 -0.0202 0.0369  343  GLY B C   
11489 O O   . GLY B 345  ? 0.2871 0.3128 0.2325 -0.1078 -0.0210 0.0404  343  GLY B O   
11490 N N   . LYS B 346  ? 0.2481 0.2692 0.1994 -0.0978 -0.0214 0.0342  344  LYS B N   
11491 C CA  . LYS B 346  ? 0.2633 0.2822 0.2134 -0.1034 -0.0239 0.0350  344  LYS B CA  
11492 C C   . LYS B 346  ? 0.2972 0.3009 0.2388 -0.1085 -0.0279 0.0367  344  LYS B C   
11493 O O   . LYS B 346  ? 0.3135 0.3158 0.2527 -0.1152 -0.0301 0.0385  344  LYS B O   
11494 C CB  . LYS B 346  ? 0.2717 0.2896 0.2258 -0.0987 -0.0243 0.0314  344  LYS B CB  
11495 C CG  . LYS B 346  ? 0.2734 0.3062 0.2357 -0.0944 -0.0207 0.0300  344  LYS B CG  
11496 C CD  . LYS B 346  ? 0.2721 0.3029 0.2377 -0.0895 -0.0211 0.0266  344  LYS B CD  
11497 C CE  . LYS B 346  ? 0.2552 0.3011 0.2285 -0.0861 -0.0178 0.0257  344  LYS B CE  
11498 N NZ  . LYS B 346  ? 0.2593 0.3037 0.2360 -0.0807 -0.0178 0.0224  344  LYS B NZ  
11499 N N   . ARG B 347  ? 0.2922 0.2842 0.2290 -0.1055 -0.0292 0.0361  345  ARG B N   
11500 C CA  . ARG B 347  ? 0.3075 0.2839 0.2357 -0.1097 -0.0333 0.0376  345  ARG B CA  
11501 C C   . ARG B 347  ? 0.3422 0.3188 0.2653 -0.1165 -0.0336 0.0420  345  ARG B C   
11502 O O   . ARG B 347  ? 0.3427 0.3065 0.2581 -0.1211 -0.0371 0.0438  345  ARG B O   
11503 C CB  . ARG B 347  ? 0.2809 0.2443 0.2061 -0.1031 -0.0349 0.0349  345  ARG B CB  
11504 C CG  . ARG B 347  ? 0.2796 0.2410 0.2087 -0.0973 -0.0352 0.0308  345  ARG B CG  
11505 C CD  . ARG B 347  ? 0.2966 0.2496 0.2248 -0.0900 -0.0357 0.0281  345  ARG B CD  
11506 N NE  . ARG B 347  ? 0.2820 0.2447 0.2155 -0.0850 -0.0321 0.0273  345  ARG B NE  
11507 C CZ  . ARG B 347  ? 0.2951 0.2530 0.2284 -0.0791 -0.0321 0.0255  345  ARG B CZ  
11508 N NH1 . ARG B 347  ? 0.2882 0.2325 0.2168 -0.0768 -0.0352 0.0242  345  ARG B NH1 
11509 N NH2 . ARG B 347  ? 0.2583 0.2252 0.1960 -0.0753 -0.0290 0.0250  345  ARG B NH2 
11510 N N   . CYS B 348  ? 0.3144 0.3053 0.2414 -0.1173 -0.0300 0.0438  346  CYS B N   
11511 C CA  . CYS B 348  ? 0.3197 0.3114 0.2419 -0.1226 -0.0296 0.0478  346  CYS B CA  
11512 C C   . CYS B 348  ? 0.3395 0.3248 0.2553 -0.1321 -0.0327 0.0515  346  CYS B C   
11513 O O   . CYS B 348  ? 0.3491 0.3228 0.2571 -0.1349 -0.0351 0.0537  346  CYS B O   
11514 C CB  . CYS B 348  ? 0.2756 0.2860 0.2038 -0.1222 -0.0249 0.0489  346  CYS B CB  
11515 S SG  . CYS B 348  ? 0.3837 0.3958 0.3061 -0.1266 -0.0237 0.0533  346  CYS B SG  
11516 N N   . PRO B 349  ? 0.3284 0.3203 0.2469 -0.1375 -0.0332 0.0525  347  PRO B N   
11517 C CA  . PRO B 349  ? 0.3633 0.3481 0.2751 -0.1472 -0.0365 0.0562  347  PRO B CA  
11518 C C   . PRO B 349  ? 0.3636 0.3271 0.2672 -0.1472 -0.0414 0.0552  347  PRO B C   
11519 O O   . PRO B 349  ? 0.3758 0.3290 0.2713 -0.1535 -0.0443 0.0584  347  PRO B O   
11520 C CB  . PRO B 349  ? 0.3439 0.3404 0.2613 -0.1516 -0.0360 0.0565  347  PRO B CB  
11521 C CG  . PRO B 349  ? 0.3189 0.3224 0.2440 -0.1436 -0.0338 0.0522  347  PRO B CG  
11522 C CD  . PRO B 349  ? 0.3130 0.3180 0.2400 -0.1354 -0.0310 0.0503  347  PRO B CD  
11523 N N   . PHE B 350  ? 0.3616 0.3183 0.2668 -0.1401 -0.0424 0.0508  348  PHE B N   
11524 C CA  . PHE B 350  ? 0.3709 0.3079 0.2687 -0.1392 -0.0470 0.0493  348  PHE B CA  
11525 C C   . PHE B 350  ? 0.3865 0.3124 0.2785 -0.1356 -0.0479 0.0497  348  PHE B C   
11526 O O   . PHE B 350  ? 0.3826 0.2924 0.2658 -0.1383 -0.0520 0.0509  348  PHE B O   
11527 C CB  . PHE B 350  ? 0.3492 0.2843 0.2511 -0.1326 -0.0473 0.0446  348  PHE B CB  
11528 C CG  . PHE B 350  ? 0.3807 0.3278 0.2888 -0.1354 -0.0461 0.0442  348  PHE B CG  
11529 C CD1 . PHE B 350  ? 0.4223 0.3646 0.3265 -0.1429 -0.0494 0.0457  348  PHE B CD1 
11530 C CD2 . PHE B 350  ? 0.3448 0.3080 0.2621 -0.1308 -0.0420 0.0425  348  PHE B CD2 
11531 C CE1 . PHE B 350  ? 0.4495 0.4033 0.3593 -0.1458 -0.0485 0.0454  348  PHE B CE1 
11532 C CE2 . PHE B 350  ? 0.3678 0.3423 0.2907 -0.1335 -0.0411 0.0423  348  PHE B CE2 
11533 C CZ  . PHE B 350  ? 0.4053 0.3753 0.3245 -0.1409 -0.0444 0.0438  348  PHE B CZ  
11534 N N   . VAL B 351  ? 0.3447 0.2790 0.2413 -0.1297 -0.0444 0.0486  349  VAL B N   
11535 C CA  . VAL B 351  ? 0.3402 0.2663 0.2316 -0.1269 -0.0450 0.0494  349  VAL B CA  
11536 C C   . VAL B 351  ? 0.3837 0.3075 0.2683 -0.1353 -0.0461 0.0546  349  VAL B C   
11537 O O   . VAL B 351  ? 0.3892 0.2986 0.2654 -0.1362 -0.0492 0.0560  349  VAL B O   
11538 C CB  . VAL B 351  ? 0.3394 0.2767 0.2376 -0.1196 -0.0409 0.0474  349  VAL B CB  
11539 C CG1 . VAL B 351  ? 0.3747 0.3048 0.2675 -0.1174 -0.0415 0.0486  349  VAL B CG1 
11540 C CG2 . VAL B 351  ? 0.3462 0.2834 0.2501 -0.1115 -0.0404 0.0425  349  VAL B CG2 
11541 N N   . LEU B 352  ? 0.3527 0.2905 0.2404 -0.1415 -0.0436 0.0575  350  LEU B N   
11542 C CA  . LEU B 352  ? 0.3465 0.2833 0.2280 -0.1501 -0.0444 0.0627  350  LEU B CA  
11543 C C   . LEU B 352  ? 0.3876 0.3083 0.2605 -0.1568 -0.0495 0.0646  350  LEU B C   
11544 O O   . LEU B 352  ? 0.4275 0.3377 0.2917 -0.1613 -0.0519 0.0680  350  LEU B O   
11545 C CB  . LEU B 352  ? 0.3869 0.3434 0.2744 -0.1551 -0.0405 0.0652  350  LEU B CB  
11546 C CG  . LEU B 352  ? 0.4294 0.4008 0.3232 -0.1494 -0.0355 0.0643  350  LEU B CG  
11547 C CD1 . LEU B 352  ? 0.4011 0.3922 0.3013 -0.1537 -0.0318 0.0663  350  LEU B CD1 
11548 C CD2 . LEU B 352  ? 0.3999 0.3653 0.2870 -0.1492 -0.0355 0.0666  350  LEU B CD2 
11549 N N   . ASP B 353  ? 0.4217 0.3399 0.2963 -0.1578 -0.0514 0.0626  351  ASP B N   
11550 C CA  . ASP B 353  ? 0.4310 0.3320 0.2970 -0.1632 -0.0567 0.0636  351  ASP B CA  
11551 C C   . ASP B 353  ? 0.4254 0.3069 0.2836 -0.1583 -0.0602 0.0622  351  ASP B C   
11552 O O   . ASP B 353  ? 0.4619 0.3288 0.3103 -0.1635 -0.0641 0.0651  351  ASP B O   
11553 C CB  . ASP B 353  ? 0.4325 0.3338 0.3021 -0.1630 -0.0580 0.0606  351  ASP B CB  
11554 C CG  . ASP B 353  ? 0.4890 0.4070 0.3647 -0.1697 -0.0559 0.0626  351  ASP B CG  
11555 O OD1 . ASP B 353  ? 0.4872 0.4132 0.3621 -0.1769 -0.0546 0.0670  351  ASP B OD1 
11556 O OD2 . ASP B 353  ? 0.5113 0.4348 0.3927 -0.1676 -0.0555 0.0596  351  ASP B OD2 
11557 N N   . PHE B 354  ? 0.4195 0.3003 0.2816 -0.1483 -0.0590 0.0579  352  PHE B N   
11558 C CA  . PHE B 354  ? 0.4454 0.3093 0.3010 -0.1427 -0.0621 0.0564  352  PHE B CA  
11559 C C   . PHE B 354  ? 0.4650 0.3252 0.3146 -0.1447 -0.0622 0.0601  352  PHE B C   
11560 O O   . PHE B 354  ? 0.4477 0.2911 0.2878 -0.1462 -0.0664 0.0616  352  PHE B O   
11561 C CB  . PHE B 354  ? 0.4320 0.2988 0.2942 -0.1319 -0.0602 0.0513  352  PHE B CB  
11562 C CG  . PHE B 354  ? 0.4191 0.2720 0.2759 -0.1256 -0.0626 0.0499  352  PHE B CG  
11563 C CD1 . PHE B 354  ? 0.4829 0.3186 0.3335 -0.1233 -0.0670 0.0479  352  PHE B CD1 
11564 C CD2 . PHE B 354  ? 0.4254 0.2823 0.2831 -0.1218 -0.0605 0.0505  352  PHE B CD2 
11565 C CE1 . PHE B 354  ? 0.4507 0.2740 0.2965 -0.1173 -0.0694 0.0466  352  PHE B CE1 
11566 C CE2 . PHE B 354  ? 0.4595 0.3039 0.3123 -0.1161 -0.0630 0.0493  352  PHE B CE2 
11567 C CZ  . PHE B 354  ? 0.4792 0.3071 0.3263 -0.1138 -0.0674 0.0474  352  PHE B CZ  
11568 N N   . ILE B 355  ? 0.3926 0.2682 0.2474 -0.1444 -0.0578 0.0615  353  ILE B N   
11569 C CA  . ILE B 355  ? 0.4106 0.2840 0.2599 -0.1458 -0.0576 0.0649  353  ILE B CA  
11570 C C   . ILE B 355  ? 0.4394 0.3066 0.2804 -0.1565 -0.0600 0.0703  353  ILE B C   
11571 O O   . ILE B 355  ? 0.4658 0.3201 0.2977 -0.1581 -0.0628 0.0728  353  ILE B O   
11572 C CB  . ILE B 355  ? 0.4193 0.3114 0.2762 -0.1431 -0.0521 0.0649  353  ILE B CB  
11573 C CG1 . ILE B 355  ? 0.4429 0.3388 0.3069 -0.1325 -0.0502 0.0598  353  ILE B CG1 
11574 C CG2 . ILE B 355  ? 0.4392 0.3300 0.2899 -0.1459 -0.0517 0.0689  353  ILE B CG2 
11575 C CD1 . ILE B 355  ? 0.4006 0.3147 0.2724 -0.1296 -0.0449 0.0593  353  ILE B CD1 
11576 N N   . ILE B 356  ? 0.4210 0.2977 0.2648 -0.1640 -0.0590 0.0723  354  ILE B N   
11577 C CA  . ILE B 356  ? 0.4889 0.3606 0.3250 -0.1749 -0.0613 0.0777  354  ILE B CA  
11578 C C   . ILE B 356  ? 0.4732 0.3218 0.2991 -0.1769 -0.0675 0.0778  354  ILE B C   
11579 O O   . ILE B 356  ? 0.4929 0.3304 0.3093 -0.1819 -0.0703 0.0814  354  ILE B O   
11580 C CB  . ILE B 356  ? 0.4566 0.3437 0.2986 -0.1823 -0.0591 0.0794  354  ILE B CB  
11581 C CG1 . ILE B 356  ? 0.4952 0.4046 0.3456 -0.1814 -0.0532 0.0803  354  ILE B CG1 
11582 C CG2 . ILE B 356  ? 0.4591 0.3397 0.2937 -0.1922 -0.0625 0.0835  354  ILE B CG2 
11583 C CD1 . ILE B 356  ? 0.4554 0.3822 0.3139 -0.1860 -0.0506 0.0807  354  ILE B CD1 
11584 N N   . ASP B 357  ? 0.4842 0.3258 0.3118 -0.1723 -0.0695 0.0734  355  ASP B N   
11585 C CA  . ASP B 357  ? 0.5200 0.3392 0.3378 -0.1727 -0.0754 0.0728  355  ASP B CA  
11586 C C   . ASP B 357  ? 0.5242 0.3297 0.3354 -0.1666 -0.0775 0.0724  355  ASP B C   
11587 O O   . ASP B 357  ? 0.4887 0.2783 0.2898 -0.1692 -0.0818 0.0743  355  ASP B O   
11588 C CB  . ASP B 357  ? 0.5102 0.3261 0.3317 -0.1679 -0.0767 0.0677  355  ASP B CB  
11589 C CG  . ASP B 357  ? 0.5379 0.3305 0.3495 -0.1664 -0.0826 0.0663  355  ASP B CG  
11590 O OD1 . ASP B 357  ? 0.5706 0.3570 0.3761 -0.1714 -0.0857 0.0678  355  ASP B OD1 
11591 O OD2 . ASP B 357  ? 0.5254 0.3106 0.3370 -0.1570 -0.0834 0.0624  355  ASP B OD2 
11592 N N   . LEU B 358  ? 0.4948 0.3077 0.3123 -0.1574 -0.0744 0.0693  356  LEU B N   
11593 C CA  . LEU B 358  ? 0.5037 0.3053 0.3158 -0.1514 -0.0762 0.0689  356  LEU B CA  
11594 C C   . LEU B 358  ? 0.4928 0.2912 0.2971 -0.1578 -0.0768 0.0745  356  LEU B C   
11595 O O   . LEU B 358  ? 0.5126 0.2938 0.3071 -0.1576 -0.0809 0.0760  356  LEU B O   
11596 C CB  . LEU B 358  ? 0.4323 0.2454 0.2534 -0.1415 -0.0722 0.0651  356  LEU B CB  
11597 C CG  . LEU B 358  ? 0.4655 0.2706 0.2828 -0.1347 -0.0733 0.0645  356  LEU B CG  
11598 C CD1 . LEU B 358  ? 0.4795 0.2633 0.2885 -0.1314 -0.0789 0.0629  356  LEU B CD1 
11599 C CD2 . LEU B 358  ? 0.4236 0.2416 0.2510 -0.1257 -0.0693 0.0604  356  LEU B CD2 
11600 N N   . ALA B 359  ? 0.4682 0.2831 0.2767 -0.1634 -0.0727 0.0777  357  ALA B N   
11601 C CA  . ALA B 359  ? 0.4698 0.2833 0.2711 -0.1699 -0.0728 0.0833  357  ALA B CA  
11602 C C   . ALA B 359  ? 0.5425 0.3442 0.3354 -0.1765 -0.0774 0.0854  357  ALA B C   
11603 O O   . ALA B 359  ? 0.5478 0.3388 0.3323 -0.1770 -0.0801 0.0874  357  ALA B O   
11604 C CB  . ALA B 359  ? 0.5754 0.4112 0.3840 -0.1741 -0.0672 0.0856  357  ALA B CB  
11605 N N   . ARG B 360  ? 0.5594 0.3639 0.3548 -0.1805 -0.0782 0.0844  358  ARG B N   
11606 C CA  . ARG B 360  ? 0.6019 0.3962 0.3898 -0.1858 -0.0825 0.0857  358  ARG B CA  
11607 C C   . ARG B 360  ? 0.5707 0.3427 0.3493 -0.1808 -0.0879 0.0838  358  ARG B C   
11608 O O   . ARG B 360  ? 0.5883 0.3499 0.3582 -0.1836 -0.0912 0.0860  358  ARG B O   
11609 C CB  . ARG B 360  ? 0.5593 0.3596 0.3517 -0.1896 -0.0827 0.0843  358  ARG B CB  
11610 C CG  . ARG B 360  ? 0.6086 0.4266 0.4055 -0.1976 -0.0796 0.0876  358  ARG B CG  
11611 C CD  . ARG B 360  ? 0.6335 0.4532 0.4321 -0.2019 -0.0813 0.0866  358  ARG B CD  
11612 N NE  . ARG B 360  ? 0.7141 0.5530 0.5238 -0.2025 -0.0769 0.0857  358  ARG B NE  
11613 C CZ  . ARG B 360  ? 0.7032 0.5606 0.5184 -0.2080 -0.0733 0.0885  358  ARG B CZ  
11614 N NH1 . ARG B 360  ? 0.8049 0.6646 0.6157 -0.2136 -0.0734 0.0924  358  ARG B NH1 
11615 N NH2 . ARG B 360  ? 0.7711 0.6453 0.5964 -0.2077 -0.0696 0.0871  358  ARG B NH2 
11616 N N   . ARG B 361  ? 0.5224 0.2871 0.3030 -0.1733 -0.0890 0.0796  359  ARG B N   
11617 C CA  . ARG B 361  ? 0.6396 0.3838 0.4117 -0.1682 -0.0942 0.0773  359  ARG B CA  
11618 C C   . ARG B 361  ? 0.6091 0.3451 0.3766 -0.1626 -0.0951 0.0778  359  ARG B C   
11619 O O   . ARG B 361  ? 0.5678 0.2873 0.3271 -0.1595 -0.0997 0.0770  359  ARG B O   
11620 C CB  . ARG B 361  ? 0.6401 0.3793 0.4156 -0.1621 -0.0953 0.0723  359  ARG B CB  
11621 C CG  . ARG B 361  ? 0.6402 0.3857 0.4235 -0.1552 -0.0921 0.0696  359  ARG B CG  
11622 C CD  . ARG B 361  ? 0.5857 0.3283 0.3729 -0.1506 -0.0929 0.0647  359  ARG B CD  
11623 N NE  . ARG B 361  ? 0.5032 0.2612 0.3018 -0.1453 -0.0882 0.0618  359  ARG B NE  
11624 C CZ  . ARG B 361  ? 0.5046 0.2636 0.3073 -0.1351 -0.0870 0.0580  359  ARG B CZ  
11625 N NH1 . ARG B 361  ? 0.5692 0.3126 0.3650 -0.1297 -0.0906 0.0571  359  ARG B NH1 
11626 N NH2 . ARG B 361  ? 0.4537 0.2299 0.2677 -0.1301 -0.0822 0.0551  359  ARG B NH2 
11627 N N   . SER B 362  ? 0.5747 0.3217 0.3471 -0.1612 -0.0911 0.0792  360  SER B N   
11628 C CA  . SER B 362  ? 0.5874 0.3273 0.3556 -0.1558 -0.0919 0.0798  360  SER B CA  
11629 C C   . SER B 362  ? 0.5621 0.3039 0.3248 -0.1612 -0.0917 0.0845  360  SER B C   
11630 O O   . SER B 362  ? 0.5729 0.3074 0.3306 -0.1573 -0.0930 0.0852  360  SER B O   
11631 C CB  . SER B 362  ? 0.6088 0.3582 0.3846 -0.1500 -0.0880 0.0784  360  SER B CB  
11632 O OG  . SER B 362  ? 0.5149 0.2845 0.2978 -0.1542 -0.0826 0.0803  360  SER B OG  
11633 N N   . GLY B 363  ? 0.5254 0.2772 0.2889 -0.1699 -0.0900 0.0875  361  GLY B N   
11634 C CA  . GLY B 363  ? 0.5850 0.3396 0.3438 -0.1751 -0.0894 0.0919  361  GLY B CA  
11635 C C   . GLY B 363  ? 0.5545 0.3218 0.3174 -0.1733 -0.0848 0.0935  361  GLY B C   
11636 O O   . GLY B 363  ? 0.5960 0.3617 0.3537 -0.1743 -0.0849 0.0963  361  GLY B O   
11637 N N   . ARG B 364  ? 0.5646 0.3443 0.3366 -0.1705 -0.0807 0.0917  362  ARG B N   
11638 C CA  . ARG B 364  ? 0.6257 0.4191 0.4022 -0.1685 -0.0759 0.0930  362  ARG B CA  
11639 C C   . ARG B 364  ? 0.5584 0.3722 0.3431 -0.1742 -0.0708 0.0943  362  ARG B C   
11640 O O   . ARG B 364  ? 0.6023 0.4208 0.3929 -0.1751 -0.0702 0.0922  362  ARG B O   
11641 C CB  . ARG B 364  ? 0.5675 0.3610 0.3494 -0.1581 -0.0749 0.0883  362  ARG B CB  
11642 C CG  . ARG B 364  ? 0.5910 0.3657 0.3663 -0.1514 -0.0798 0.0865  362  ARG B CG  
11643 C CD  . ARG B 364  ? 0.5569 0.3273 0.3252 -0.1506 -0.0804 0.0895  362  ARG B CD  
11644 N NE  . ARG B 364  ? 0.5923 0.3438 0.3535 -0.1445 -0.0855 0.0880  362  ARG B NE  
11645 C CZ  . ARG B 364  ? 0.5571 0.3082 0.3231 -0.1341 -0.0857 0.0832  362  ARG B CZ  
11646 N NH1 . ARG B 364  ? 0.5440 0.3116 0.3214 -0.1287 -0.0811 0.0794  362  ARG B NH1 
11647 N NH2 . ARG B 364  ? 0.6006 0.3342 0.3598 -0.1291 -0.0907 0.0821  362  ARG B NH2 
11648 N N   . ARG B 365  ? 0.5246 0.3512 0.3099 -0.1776 -0.0673 0.0974  363  ARG B N   
11649 C CA  . ARG B 365  ? 0.5400 0.3880 0.3343 -0.1809 -0.0618 0.0981  363  ARG B CA  
11650 C C   . ARG B 365  ? 0.4455 0.3039 0.2478 -0.1720 -0.0580 0.0943  363  ARG B C   
11651 O O   . ARG B 365  ? 0.4821 0.3424 0.2830 -0.1677 -0.0566 0.0944  363  ARG B O   
11652 C CB  . ARG B 365  ? 0.5306 0.3900 0.3236 -0.1871 -0.0594 0.1020  363  ARG B CB  
11653 C CG  . ARG B 365  ? 0.5061 0.3880 0.3085 -0.1907 -0.0541 0.1026  363  ARG B CG  
11654 C CD  . ARG B 365  ? 0.5884 0.4805 0.3893 -0.1975 -0.0523 0.1064  363  ARG B CD  
11655 N NE  . ARG B 365  ? 0.6126 0.5256 0.4225 -0.2012 -0.0480 0.1067  363  ARG B NE  
11656 C CZ  . ARG B 365  ? 0.6249 0.5561 0.4393 -0.2016 -0.0429 0.1081  363  ARG B CZ  
11657 N NH1 . ARG B 365  ? 0.5691 0.5006 0.3794 -0.1992 -0.0413 0.1095  363  ARG B NH1 
11658 N NH2 . ARG B 365  ? 0.5250 0.4748 0.3480 -0.2043 -0.0394 0.1079  363  ARG B NH2 
11659 N N   . ILE B 366  ? 0.4510 0.3162 0.2625 -0.1678 -0.0567 0.0899  364  ILE B N   
11660 C CA  . ILE B 366  ? 0.4811 0.3565 0.3016 -0.1579 -0.0533 0.0849  364  ILE B CA  
11661 C C   . ILE B 366  ? 0.4577 0.3554 0.2858 -0.1595 -0.0474 0.0857  364  ILE B C   
11662 O O   . ILE B 366  ? 0.4659 0.3738 0.2974 -0.1660 -0.0457 0.0876  364  ILE B O   
11663 C CB  . ILE B 366  ? 0.4378 0.3101 0.2644 -0.1526 -0.0546 0.0798  364  ILE B CB  
11664 C CG1 . ILE B 366  ? 0.4791 0.3293 0.2978 -0.1504 -0.0604 0.0788  364  ILE B CG1 
11665 C CG2 . ILE B 366  ? 0.4082 0.2920 0.2445 -0.1430 -0.0510 0.0750  364  ILE B CG2 
11666 C CD1 . ILE B 366  ? 0.5078 0.3534 0.3310 -0.1460 -0.0621 0.0742  364  ILE B CD1 
11667 N N   . MET B 367  ? 0.4476 0.3529 0.2782 -0.1534 -0.0445 0.0844  365  MET B N   
11668 C CA  . MET B 367  ? 0.4415 0.3676 0.2796 -0.1530 -0.0388 0.0842  365  MET B CA  
11669 C C   . MET B 367  ? 0.4584 0.3933 0.3073 -0.1467 -0.0367 0.0790  365  MET B C   
11670 O O   . MET B 367  ? 0.4151 0.3440 0.2663 -0.1386 -0.0379 0.0748  365  MET B O   
11671 C CB  . MET B 367  ? 0.4407 0.3704 0.2766 -0.1487 -0.0367 0.0845  365  MET B CB  
11672 C CG  . MET B 367  ? 0.4351 0.3537 0.2596 -0.1538 -0.0393 0.0893  365  MET B CG  
11673 S SD  . MET B 367  ? 0.4921 0.4142 0.3130 -0.1489 -0.0371 0.0897  365  MET B SD  
11674 C CE  . MET B 367  ? 0.6349 0.5784 0.4581 -0.1550 -0.0313 0.0933  365  MET B CE  
11675 N N   . VAL B 368  ? 0.3863 0.3354 0.2418 -0.1504 -0.0339 0.0794  366  VAL B N   
11676 C CA  . VAL B 368  ? 0.3697 0.3267 0.2350 -0.1452 -0.0323 0.0749  366  VAL B CA  
11677 C C   . VAL B 368  ? 0.3661 0.3435 0.2391 -0.1429 -0.0267 0.0742  366  VAL B C   
11678 O O   . VAL B 368  ? 0.3776 0.3675 0.2522 -0.1491 -0.0242 0.0772  366  VAL B O   
11679 C CB  . VAL B 368  ? 0.4179 0.3729 0.2847 -0.1507 -0.0343 0.0753  366  VAL B CB  
11680 C CG1 . VAL B 368  ? 0.4191 0.3815 0.2956 -0.1445 -0.0327 0.0704  366  VAL B CG1 
11681 C CG2 . VAL B 368  ? 0.4344 0.3684 0.2925 -0.1531 -0.0400 0.0762  366  VAL B CG2 
11682 N N   . ARG B 369  ? 0.3775 0.3584 0.2552 -0.1340 -0.0248 0.0701  367  ARG B N   
11683 C CA  . ARG B 369  ? 0.3520 0.3512 0.2369 -0.1308 -0.0198 0.0688  367  ARG B CA  
11684 C C   . ARG B 369  ? 0.3856 0.3929 0.2796 -0.1285 -0.0186 0.0657  367  ARG B C   
11685 O O   . ARG B 369  ? 0.3609 0.3618 0.2580 -0.1224 -0.0200 0.0616  367  ARG B O   
11686 C CB  . ARG B 369  ? 0.3544 0.3537 0.2396 -0.1226 -0.0183 0.0660  367  ARG B CB  
11687 C CG  . ARG B 369  ? 0.3678 0.3854 0.2598 -0.1192 -0.0132 0.0646  367  ARG B CG  
11688 C CD  . ARG B 369  ? 0.3483 0.3653 0.2424 -0.1101 -0.0122 0.0606  367  ARG B CD  
11689 N NE  . ARG B 369  ? 0.3388 0.3478 0.2250 -0.1096 -0.0134 0.0621  367  ARG B NE  
11690 C CZ  . ARG B 369  ? 0.3596 0.3612 0.2448 -0.1028 -0.0146 0.0591  367  ARG B CZ  
11691 N NH1 . ARG B 369  ? 0.3106 0.3114 0.2021 -0.0962 -0.0148 0.0546  367  ARG B NH1 
11692 N NH2 . ARG B 369  ? 0.3711 0.3662 0.2489 -0.1029 -0.0158 0.0609  367  ARG B NH2 
11693 N N   . LEU B 370  ? 0.3321 0.3534 0.2303 -0.1335 -0.0161 0.0676  368  LEU B N   
11694 C CA  . LEU B 370  ? 0.3276 0.3586 0.2346 -0.1314 -0.0146 0.0649  368  LEU B CA  
11695 C C   . LEU B 370  ? 0.3203 0.3658 0.2339 -0.1246 -0.0101 0.0623  368  LEU B C   
11696 O O   . LEU B 370  ? 0.3616 0.4192 0.2754 -0.1262 -0.0068 0.0644  368  LEU B O   
11697 C CB  . LEU B 370  ? 0.3146 0.3539 0.2230 -0.1402 -0.0144 0.0683  368  LEU B CB  
11698 C CG  . LEU B 370  ? 0.3317 0.3813 0.2489 -0.1387 -0.0132 0.0659  368  LEU B CG  
11699 C CD1 . LEU B 370  ? 0.3322 0.3682 0.2495 -0.1358 -0.0168 0.0627  368  LEU B CD1 
11700 C CD2 . LEU B 370  ? 0.3304 0.3905 0.2489 -0.1479 -0.0126 0.0698  368  LEU B CD2 
11701 N N   . VAL B 371  ? 0.2812 0.3249 0.1998 -0.1168 -0.0100 0.0577  369  VAL B N   
11702 C CA  . VAL B 371  ? 0.2841 0.3400 0.2092 -0.1098 -0.0062 0.0547  369  VAL B CA  
11703 C C   . VAL B 371  ? 0.3068 0.3695 0.2398 -0.1078 -0.0055 0.0522  369  VAL B C   
11704 O O   . VAL B 371  ? 0.3097 0.3660 0.2429 -0.1108 -0.0083 0.0523  369  VAL B O   
11705 C CB  . VAL B 371  ? 0.2709 0.3186 0.1946 -0.1020 -0.0066 0.0515  369  VAL B CB  
11706 C CG1 . VAL B 371  ? 0.2880 0.3276 0.2033 -0.1042 -0.0079 0.0541  369  VAL B CG1 
11707 C CG2 . VAL B 371  ? 0.2836 0.3190 0.2086 -0.0982 -0.0098 0.0483  369  VAL B CG2 
11708 N N   . LYS B 372  ? 0.2669 0.3421 0.2063 -0.1023 -0.0020 0.0499  370  LYS B N   
11709 C CA  . LYS B 372  ? 0.2949 0.3746 0.2416 -0.0990 -0.0017 0.0470  370  LYS B CA  
11710 C C   . LYS B 372  ? 0.2711 0.3392 0.2184 -0.0921 -0.0035 0.0429  370  LYS B C   
11711 O O   . LYS B 372  ? 0.2883 0.3479 0.2360 -0.0926 -0.0063 0.0419  370  LYS B O   
11712 C CB  . LYS B 372  ? 0.2928 0.3906 0.2459 -0.0963 0.0026  0.0463  370  LYS B CB  
11713 C CG  . LYS B 372  ? 0.2897 0.3994 0.2431 -0.1041 0.0039  0.0505  370  LYS B CG  
11714 C CD  . LYS B 372  ? 0.3196 0.4484 0.2794 -0.1019 0.0081  0.0502  370  LYS B CD  
11715 C CE  . LYS B 372  ? 0.3312 0.4713 0.2903 -0.1102 0.0093  0.0547  370  LYS B CE  
11716 N NZ  . LYS B 372  ? 0.3181 0.4778 0.2831 -0.1077 0.0137  0.0546  370  LYS B NZ  
11717 N N   . GLY B 373  ? 0.2779 0.3453 0.2251 -0.0858 -0.0022 0.0408  371  GLY B N   
11718 C CA  . GLY B 373  ? 0.2675 0.3235 0.2147 -0.0799 -0.0041 0.0374  371  GLY B CA  
11719 C C   . GLY B 373  ? 0.2520 0.3131 0.2028 -0.0724 -0.0017 0.0342  371  GLY B C   
11720 O O   . GLY B 373  ? 0.2935 0.3672 0.2494 -0.0704 0.0013  0.0335  371  GLY B O   
11721 N N   . ALA B 374  ? 0.2471 0.2986 0.1953 -0.0680 -0.0030 0.0323  372  ALA B N   
11722 C CA  . ALA B 374  ? 0.2511 0.3064 0.2013 -0.0615 -0.0010 0.0297  372  ALA B CA  
11723 C C   . ALA B 374  ? 0.2551 0.3076 0.2103 -0.0554 -0.0013 0.0258  372  ALA B C   
11724 O O   . ALA B 374  ? 0.2825 0.3375 0.2393 -0.0500 0.0001  0.0235  372  ALA B O   
11725 C CB  . ALA B 374  ? 0.2667 0.3145 0.2106 -0.0608 -0.0021 0.0303  372  ALA B CB  
11726 N N   . TYR B 375  ? 0.2261 0.2734 0.1836 -0.0560 -0.0033 0.0250  373  TYR B N   
11727 C CA  . TYR B 375  ? 0.2321 0.2751 0.1935 -0.0505 -0.0040 0.0216  373  TYR B CA  
11728 C C   . TYR B 375  ? 0.2453 0.2950 0.2127 -0.0497 -0.0029 0.0204  373  TYR B C   
11729 O O   . TYR B 375  ? 0.2318 0.2766 0.2019 -0.0469 -0.0041 0.0182  373  TYR B O   
11730 C CB  . TYR B 375  ? 0.2691 0.2983 0.2274 -0.0505 -0.0075 0.0210  373  TYR B CB  
11731 C CG  . TYR B 375  ? 0.2476 0.2690 0.1995 -0.0512 -0.0092 0.0222  373  TYR B CG  
11732 C CD1 . TYR B 375  ? 0.2618 0.2811 0.2082 -0.0570 -0.0101 0.0257  373  TYR B CD1 
11733 C CD2 . TYR B 375  ? 0.2879 0.3039 0.2394 -0.0463 -0.0099 0.0201  373  TYR B CD2 
11734 C CE1 . TYR B 375  ? 0.2696 0.2815 0.2098 -0.0576 -0.0117 0.0269  373  TYR B CE1 
11735 C CE2 . TYR B 375  ? 0.3073 0.3163 0.2529 -0.0468 -0.0116 0.0212  373  TYR B CE2 
11736 C CZ  . TYR B 375  ? 0.3127 0.3195 0.2526 -0.0523 -0.0125 0.0246  373  TYR B CZ  
11737 O OH  . TYR B 375  ? 0.3648 0.3643 0.2984 -0.0529 -0.0143 0.0259  373  TYR B OH  
11738 N N   . TRP B 376  ? 0.2318 0.2933 0.2016 -0.0518 -0.0005 0.0218  374  TRP B N   
11739 C CA  . TRP B 376  ? 0.2225 0.2902 0.1974 -0.0524 0.0000  0.0214  374  TRP B CA  
11740 C C   . TRP B 376  ? 0.2168 0.2847 0.1966 -0.0460 0.0007  0.0180  374  TRP B C   
11741 O O   . TRP B 376  ? 0.2264 0.2903 0.2083 -0.0457 -0.0007 0.0169  374  TRP B O   
11742 C CB  . TRP B 376  ? 0.2271 0.3088 0.2040 -0.0551 0.0027  0.0234  374  TRP B CB  
11743 C CG  . TRP B 376  ? 0.2202 0.3083 0.2023 -0.0558 0.0029  0.0230  374  TRP B CG  
11744 C CD1 . TRP B 376  ? 0.2450 0.3311 0.2269 -0.0609 0.0010  0.0245  374  TRP B CD1 
11745 C CD2 . TRP B 376  ? 0.2449 0.3420 0.2327 -0.0511 0.0050  0.0211  374  TRP B CD2 
11746 N NE1 . TRP B 376  ? 0.2334 0.3272 0.2208 -0.0597 0.0018  0.0235  374  TRP B NE1 
11747 C CE2 . TRP B 376  ? 0.2453 0.3460 0.2364 -0.0536 0.0043  0.0215  374  TRP B CE2 
11748 C CE3 . TRP B 376  ? 0.2778 0.3800 0.2680 -0.0449 0.0074  0.0190  374  TRP B CE3 
11749 C CZ2 . TRP B 376  ? 0.2460 0.3552 0.2426 -0.0501 0.0058  0.0201  374  TRP B CZ2 
11750 C CZ3 . TRP B 376  ? 0.2355 0.3457 0.2311 -0.0413 0.0088  0.0175  374  TRP B CZ3 
11751 C CH2 . TRP B 376  ? 0.2560 0.3698 0.2548 -0.0439 0.0080  0.0181  374  TRP B CH2 
11752 N N   . ASP B 377  ? 0.2228 0.2951 0.2042 -0.0410 0.0027  0.0163  375  ASP B N   
11753 C CA  A ASP B 377  ? 0.2260 0.2985 0.2118 -0.0353 0.0033  0.0133  375  ASP B CA  
11754 C CA  B ASP B 377  ? 0.2268 0.2994 0.2127 -0.0356 0.0033  0.0134  375  ASP B CA  
11755 C C   . ASP B 377  ? 0.1954 0.2561 0.1805 -0.0336 0.0008  0.0116  375  ASP B C   
11756 O O   . ASP B 377  ? 0.2331 0.2926 0.2218 -0.0312 0.0005  0.0099  375  ASP B O   
11757 C CB  A ASP B 377  ? 0.2789 0.3554 0.2649 -0.0304 0.0054  0.0118  375  ASP B CB  
11758 C CB  B ASP B 377  ? 0.2778 0.3568 0.2652 -0.0306 0.0058  0.0118  375  ASP B CB  
11759 C CG  A ASP B 377  ? 0.3352 0.4244 0.3223 -0.0307 0.0082  0.0129  375  ASP B CG  
11760 C CG  B ASP B 377  ? 0.3092 0.3841 0.2920 -0.0296 0.0057  0.0118  375  ASP B CG  
11761 O OD1 A ASP B 377  ? 0.4683 0.5653 0.4591 -0.0319 0.0091  0.0135  375  ASP B OD1 
11762 O OD1 B ASP B 377  ? 0.3679 0.4326 0.3479 -0.0297 0.0035  0.0114  375  ASP B OD1 
11763 O OD2 A ASP B 377  ? 0.4828 0.5745 0.4672 -0.0297 0.0096  0.0131  375  ASP B OD2 
11764 O OD2 B ASP B 377  ? 0.4030 0.4854 0.3850 -0.0285 0.0079  0.0121  375  ASP B OD2 
11765 N N   . ALA B 378  ? 0.2207 0.2727 0.2012 -0.0346 -0.0009 0.0121  376  ALA B N   
11766 C CA  . ALA B 378  ? 0.2222 0.2635 0.2021 -0.0327 -0.0033 0.0105  376  ALA B CA  
11767 C C   . ALA B 378  ? 0.2386 0.2754 0.2186 -0.0357 -0.0052 0.0110  376  ALA B C   
11768 O O   . ALA B 378  ? 0.2305 0.2621 0.2124 -0.0331 -0.0063 0.0091  376  ALA B O   
11769 C CB  . ALA B 378  ? 0.2341 0.2678 0.2088 -0.0331 -0.0049 0.0111  376  ALA B CB  
11770 N N   . GLU B 379  ? 0.2149 0.2537 0.1928 -0.0410 -0.0056 0.0135  377  GLU B N   
11771 C CA  . GLU B 379  ? 0.2105 0.2446 0.1879 -0.0442 -0.0077 0.0139  377  GLU B CA  
11772 C C   . GLU B 379  ? 0.2392 0.2792 0.2219 -0.0425 -0.0066 0.0125  377  GLU B C   
11773 O O   . GLU B 379  ? 0.2246 0.2592 0.2079 -0.0421 -0.0082 0.0114  377  GLU B O   
11774 C CB  . GLU B 379  ? 0.2212 0.2558 0.1946 -0.0509 -0.0086 0.0171  377  GLU B CB  
11775 C CG  . GLU B 379  ? 0.2450 0.2724 0.2122 -0.0532 -0.0100 0.0189  377  GLU B CG  
11776 C CD  . GLU B 379  ? 0.2716 0.2854 0.2352 -0.0520 -0.0131 0.0179  377  GLU B CD  
11777 O OE1 . GLU B 379  ? 0.2654 0.2750 0.2312 -0.0497 -0.0142 0.0158  377  GLU B OE1 
11778 O OE2 . GLU B 379  ? 0.2544 0.2618 0.2127 -0.0534 -0.0146 0.0193  377  GLU B OE2 
11779 N N   . ILE B 380  ? 0.2075 0.2587 0.1939 -0.0414 -0.0040 0.0126  378  ILE B N   
11780 C CA  . ILE B 380  ? 0.1986 0.2555 0.1900 -0.0393 -0.0030 0.0113  378  ILE B CA  
11781 C C   . ILE B 380  ? 0.2072 0.2589 0.2008 -0.0339 -0.0032 0.0085  378  ILE B C   
11782 O O   . ILE B 380  ? 0.2093 0.2581 0.2045 -0.0331 -0.0042 0.0074  378  ILE B O   
11783 C CB  . ILE B 380  ? 0.2266 0.2964 0.2213 -0.0384 -0.0002 0.0119  378  ILE B CB  
11784 C CG1 . ILE B 380  ? 0.2087 0.2849 0.2016 -0.0441 0.0002  0.0149  378  ILE B CG1 
11785 C CG2 . ILE B 380  ? 0.2164 0.2916 0.2161 -0.0359 0.0006  0.0106  378  ILE B CG2 
11786 C CD1 . ILE B 380  ? 0.2437 0.3195 0.2364 -0.0494 -0.0016 0.0164  378  ILE B CD1 
11787 N N   . LYS B 381  ? 0.2097 0.2602 0.2031 -0.0301 -0.0024 0.0074  379  LYS B N   
11788 C CA  . LYS B 381  ? 0.1958 0.2418 0.1913 -0.0253 -0.0026 0.0049  379  LYS B CA  
11789 C C   . LYS B 381  ? 0.1995 0.2354 0.1933 -0.0257 -0.0050 0.0042  379  LYS B C   
11790 O O   . LYS B 381  ? 0.2044 0.2384 0.2008 -0.0235 -0.0053 0.0026  379  LYS B O   
11791 C CB  . LYS B 381  ? 0.2026 0.2481 0.1973 -0.0220 -0.0017 0.0039  379  LYS B CB  
11792 C CG  . LYS B 381  ? 0.2150 0.2556 0.2118 -0.0175 -0.0021 0.0016  379  LYS B CG  
11793 C CD  . LYS B 381  ? 0.1905 0.2315 0.1866 -0.0144 -0.0013 0.0006  379  LYS B CD  
11794 C CE  . LYS B 381  ? 0.2322 0.2695 0.2309 -0.0103 -0.0015 -0.0017 379  LYS B CE  
11795 N NZ  . LYS B 381  ? 0.2047 0.2409 0.2022 -0.0075 -0.0012 -0.0027 379  LYS B NZ  
11796 N N   . ARG B 382  ? 0.2155 0.2450 0.2048 -0.0286 -0.0069 0.0053  380  ARG B N   
11797 C CA  . ARG B 382  ? 0.2281 0.2476 0.2153 -0.0284 -0.0093 0.0045  380  ARG B CA  
11798 C C   . ARG B 382  ? 0.2195 0.2377 0.2074 -0.0301 -0.0103 0.0043  380  ARG B C   
11799 O O   . ARG B 382  ? 0.2197 0.2331 0.2087 -0.0277 -0.0112 0.0026  380  ARG B O   
11800 C CB  . ARG B 382  ? 0.2480 0.2609 0.2296 -0.0313 -0.0112 0.0062  380  ARG B CB  
11801 C CG  . ARG B 382  ? 0.3750 0.3771 0.3540 -0.0303 -0.0139 0.0052  380  ARG B CG  
11802 C CD  . ARG B 382  ? 0.4772 0.4769 0.4578 -0.0255 -0.0139 0.0033  380  ARG B CD  
11803 N NE  . ARG B 382  ? 0.4969 0.4950 0.4810 -0.0222 -0.0140 0.0011  380  ARG B NE  
11804 C CZ  . ARG B 382  ? 0.5357 0.5344 0.5230 -0.0180 -0.0134 -0.0008 380  ARG B CZ  
11805 N NH1 . ARG B 382  ? 0.4703 0.4710 0.4577 -0.0164 -0.0126 -0.0009 380  ARG B NH1 
11806 N NH2 . ARG B 382  ? 0.4436 0.4410 0.4339 -0.0155 -0.0135 -0.0025 380  ARG B NH2 
11807 N N   . ALA B 383  ? 0.1900 0.2127 0.1773 -0.0344 -0.0102 0.0062  381  ALA B N   
11808 C CA  . ALA B 383  ? 0.1814 0.2029 0.1689 -0.0364 -0.0113 0.0060  381  ALA B CA  
11809 C C   . ALA B 383  ? 0.2056 0.2319 0.1981 -0.0328 -0.0098 0.0042  381  ALA B C   
11810 O O   . ALA B 383  ? 0.2088 0.2310 0.2016 -0.0319 -0.0109 0.0029  381  ALA B O   
11811 C CB  . ALA B 383  ? 0.2197 0.2463 0.2059 -0.0420 -0.0113 0.0085  381  ALA B CB  
11812 N N   . GLN B 384  ? 0.1903 0.2248 0.1864 -0.0304 -0.0074 0.0040  382  GLN B N   
11813 C CA  . GLN B 384  ? 0.2049 0.2434 0.2054 -0.0267 -0.0061 0.0024  382  GLN B CA  
11814 C C   . GLN B 384  ? 0.1816 0.2134 0.1827 -0.0227 -0.0066 0.0003  382  GLN B C   
11815 O O   . GLN B 384  ? 0.2075 0.2380 0.2102 -0.0212 -0.0068 -0.0009 382  GLN B O   
11816 C CB  . GLN B 384  ? 0.2084 0.2564 0.2120 -0.0247 -0.0036 0.0027  382  GLN B CB  
11817 C CG  . GLN B 384  ? 0.1895 0.2462 0.1939 -0.0281 -0.0029 0.0045  382  GLN B CG  
11818 C CD  . GLN B 384  ? 0.2073 0.2736 0.2149 -0.0254 -0.0004 0.0045  382  GLN B CD  
11819 O OE1 . GLN B 384  ? 0.2388 0.3043 0.2469 -0.0216 0.0006  0.0033  382  GLN B OE1 
11820 N NE2 . GLN B 384  ? 0.2042 0.2796 0.2138 -0.0272 0.0004  0.0057  382  GLN B NE2 
11821 N N   . LEU B 385  ? 0.1993 0.2275 0.1992 -0.0210 -0.0067 -0.0001 383  LEU B N   
11822 C CA  . LEU B 385  ? 0.1996 0.2221 0.2003 -0.0174 -0.0073 -0.0019 383  LEU B CA  
11823 C C   . LEU B 385  ? 0.2096 0.2249 0.2085 -0.0181 -0.0093 -0.0026 383  LEU B C   
11824 O O   . LEU B 385  ? 0.2228 0.2361 0.2237 -0.0153 -0.0093 -0.0042 383  LEU B O   
11825 C CB  . LEU B 385  ? 0.2327 0.2519 0.2316 -0.0162 -0.0076 -0.0020 383  LEU B CB  
11826 C CG  . LEU B 385  ? 0.2502 0.2750 0.2510 -0.0140 -0.0058 -0.0022 383  LEU B CG  
11827 C CD1 . LEU B 385  ? 0.2359 0.2565 0.2341 -0.0135 -0.0066 -0.0022 383  LEU B CD1 
11828 C CD2 . LEU B 385  ? 0.2605 0.2866 0.2653 -0.0102 -0.0047 -0.0040 383  LEU B CD2 
11829 N N   . ASP B 386  ? 0.2160 0.2272 0.2108 -0.0217 -0.0110 -0.0014 384  ASP B N   
11830 C CA  . ASP B 386  ? 0.2277 0.2308 0.2198 -0.0221 -0.0132 -0.0021 384  ASP B CA  
11831 C C   . ASP B 386  ? 0.2242 0.2282 0.2165 -0.0237 -0.0135 -0.0023 384  ASP B C   
11832 O O   . ASP B 386  ? 0.2501 0.2474 0.2400 -0.0238 -0.0154 -0.0032 384  ASP B O   
11833 C CB  . ASP B 386  ? 0.2459 0.2422 0.2327 -0.0251 -0.0154 -0.0007 384  ASP B CB  
11834 C CG  . ASP B 386  ? 0.3312 0.3244 0.3170 -0.0228 -0.0157 -0.0009 384  ASP B CG  
11835 O OD1 . ASP B 386  ? 0.3101 0.3054 0.2994 -0.0190 -0.0145 -0.0024 384  ASP B OD1 
11836 O OD2 . ASP B 386  ? 0.3219 0.3101 0.3033 -0.0251 -0.0173 0.0004  384  ASP B OD2 
11837 N N   . GLY B 387  ? 0.2151 0.2274 0.2103 -0.0247 -0.0119 -0.0017 385  GLY B N   
11838 C CA  . GLY B 387  ? 0.2136 0.2274 0.2092 -0.0260 -0.0123 -0.0019 385  GLY B CA  
11839 C C   . GLY B 387  ? 0.2568 0.2657 0.2479 -0.0306 -0.0146 -0.0009 385  GLY B C   
11840 O O   . GLY B 387  ? 0.2537 0.2589 0.2433 -0.0310 -0.0159 -0.0018 385  GLY B O   
11841 N N   . LEU B 388  ? 0.2174 0.2259 0.2056 -0.0343 -0.0153 0.0011  386  LEU B N   
11842 C CA  . LEU B 388  ? 0.2482 0.2503 0.2313 -0.0389 -0.0179 0.0021  386  LEU B CA  
11843 C C   . LEU B 388  ? 0.2670 0.2757 0.2508 -0.0432 -0.0178 0.0035  386  LEU B C   
11844 O O   . LEU B 388  ? 0.2359 0.2546 0.2242 -0.0426 -0.0157 0.0039  386  LEU B O   
11845 C CB  . LEU B 388  ? 0.2533 0.2506 0.2325 -0.0410 -0.0190 0.0037  386  LEU B CB  
11846 C CG  . LEU B 388  ? 0.2509 0.2416 0.2295 -0.0365 -0.0194 0.0021  386  LEU B CG  
11847 C CD1 . LEU B 388  ? 0.3297 0.3150 0.3039 -0.0383 -0.0207 0.0037  386  LEU B CD1 
11848 C CD2 . LEU B 388  ? 0.2722 0.2547 0.2492 -0.0340 -0.0211 -0.0001 386  LEU B CD2 
11849 N N   . ALA B 389  ? 0.2545 0.2572 0.2337 -0.0477 -0.0204 0.0044  387  ALA B N   
11850 C CA  . ALA B 389  ? 0.2768 0.2846 0.2565 -0.0517 -0.0209 0.0053  387  ALA B CA  
11851 C C   . ALA B 389  ? 0.2596 0.2788 0.2423 -0.0548 -0.0192 0.0077  387  ALA B C   
11852 O O   . ALA B 389  ? 0.2943 0.3224 0.2804 -0.0557 -0.0182 0.0080  387  ALA B O   
11853 C CB  . ALA B 389  ? 0.3294 0.3276 0.3030 -0.0564 -0.0243 0.0057  387  ALA B CB  
11854 N N   . ASP B 390  ? 0.2797 0.2990 0.2609 -0.0563 -0.0187 0.0093  388  ASP B N   
11855 C CA  . ASP B 390  ? 0.2486 0.2787 0.2320 -0.0593 -0.0170 0.0117  388  ASP B CA  
11856 C C   . ASP B 390  ? 0.2127 0.2410 0.1944 -0.0583 -0.0161 0.0126  388  ASP B C   
11857 O O   . ASP B 390  ? 0.2478 0.2668 0.2269 -0.0555 -0.0171 0.0114  388  ASP B O   
11858 C CB  . ASP B 390  ? 0.2620 0.2931 0.2427 -0.0665 -0.0188 0.0140  388  ASP B CB  
11859 C CG  . ASP B 390  ? 0.3116 0.3572 0.2967 -0.0690 -0.0168 0.0159  388  ASP B CG  
11860 O OD1 . ASP B 390  ? 0.2815 0.3346 0.2691 -0.0672 -0.0143 0.0166  388  ASP B OD1 
11861 O OD2 . ASP B 390  ? 0.3189 0.3686 0.3048 -0.0726 -0.0179 0.0165  388  ASP B OD2 
11862 N N   . PHE B 391  ? 0.2341 0.2714 0.2171 -0.0606 -0.0144 0.0147  389  PHE B N   
11863 C CA  . PHE B 391  ? 0.2317 0.2678 0.2125 -0.0604 -0.0136 0.0158  389  PHE B CA  
11864 C C   . PHE B 391  ? 0.2441 0.2723 0.2185 -0.0662 -0.0161 0.0180  389  PHE B C   
11865 O O   . PHE B 391  ? 0.2544 0.2817 0.2268 -0.0715 -0.0179 0.0194  389  PHE B O   
11866 C CB  . PHE B 391  ? 0.2561 0.3056 0.2406 -0.0603 -0.0106 0.0170  389  PHE B CB  
11867 C CG  . PHE B 391  ? 0.1898 0.2466 0.1801 -0.0546 -0.0083 0.0149  389  PHE B CG  
11868 C CD1 . PHE B 391  ? 0.2167 0.2705 0.2081 -0.0488 -0.0073 0.0128  389  PHE B CD1 
11869 C CD2 . PHE B 391  ? 0.2091 0.2749 0.2035 -0.0552 -0.0075 0.0150  389  PHE B CD2 
11870 C CE1 . PHE B 391  ? 0.1975 0.2568 0.1937 -0.0437 -0.0055 0.0110  389  PHE B CE1 
11871 C CE2 . PHE B 391  ? 0.2019 0.2735 0.2012 -0.0498 -0.0057 0.0131  389  PHE B CE2 
11872 C CZ  . PHE B 391  ? 0.2057 0.2738 0.2057 -0.0442 -0.0046 0.0111  389  PHE B CZ  
11873 N N   . PRO B 392  ? 0.2242 0.2459 0.1949 -0.0653 -0.0166 0.0185  390  PRO B N   
11874 C CA  . PRO B 392  ? 0.2190 0.2336 0.1833 -0.0709 -0.0188 0.0211  390  PRO B CA  
11875 C C   . PRO B 392  ? 0.2518 0.2756 0.2158 -0.0752 -0.0170 0.0242  390  PRO B C   
11876 O O   . PRO B 392  ? 0.2632 0.2820 0.2218 -0.0801 -0.0186 0.0267  390  PRO B O   
11877 C CB  . PRO B 392  ? 0.2548 0.2590 0.2158 -0.0670 -0.0199 0.0199  390  PRO B CB  
11878 C CG  . PRO B 392  ? 0.2319 0.2437 0.1979 -0.0611 -0.0169 0.0182  390  PRO B CG  
11879 C CD  . PRO B 392  ? 0.2077 0.2279 0.1797 -0.0592 -0.0153 0.0166  390  PRO B CD  
11880 N N   . VAL B 393  ? 0.2234 0.2604 0.1930 -0.0731 -0.0138 0.0240  391  VAL B N   
11881 C CA  . VAL B 393  ? 0.2347 0.2828 0.2050 -0.0764 -0.0116 0.0266  391  VAL B CA  
11882 C C   . VAL B 393  ? 0.2220 0.2830 0.1980 -0.0775 -0.0100 0.0268  391  VAL B C   
11883 O O   . VAL B 393  ? 0.2329 0.2946 0.2126 -0.0743 -0.0101 0.0245  391  VAL B O   
11884 C CB  . VAL B 393  ? 0.2212 0.2733 0.1924 -0.0716 -0.0090 0.0259  391  VAL B CB  
11885 C CG1 . VAL B 393  ? 0.2509 0.2905 0.2164 -0.0707 -0.0109 0.0259  391  VAL B CG1 
11886 C CG2 . VAL B 393  ? 0.2228 0.2791 0.1997 -0.0645 -0.0072 0.0227  391  VAL B CG2 
11887 N N   . PHE B 394  ? 0.2157 0.2872 0.1923 -0.0820 -0.0085 0.0296  392  PHE B N   
11888 C CA  . PHE B 394  ? 0.2180 0.3039 0.2006 -0.0826 -0.0067 0.0299  392  PHE B CA  
11889 C C   . PHE B 394  ? 0.2400 0.3341 0.2278 -0.0751 -0.0035 0.0276  392  PHE B C   
11890 O O   . PHE B 394  ? 0.2497 0.3405 0.2363 -0.0707 -0.0024 0.0264  392  PHE B O   
11891 C CB  . PHE B 394  ? 0.2267 0.3224 0.2087 -0.0894 -0.0058 0.0336  392  PHE B CB  
11892 C CG  . PHE B 394  ? 0.2442 0.3314 0.2207 -0.0972 -0.0091 0.0361  392  PHE B CG  
11893 C CD1 . PHE B 394  ? 0.2624 0.3463 0.2394 -0.1002 -0.0116 0.0357  392  PHE B CD1 
11894 C CD2 . PHE B 394  ? 0.2693 0.3504 0.2397 -0.1013 -0.0099 0.0386  392  PHE B CD2 
11895 C CE1 . PHE B 394  ? 0.2786 0.3532 0.2499 -0.1072 -0.0149 0.0378  392  PHE B CE1 
11896 C CE2 . PHE B 394  ? 0.2761 0.3479 0.2408 -0.1085 -0.0132 0.0409  392  PHE B CE2 
11897 C CZ  . PHE B 394  ? 0.2608 0.3291 0.2259 -0.1114 -0.0158 0.0404  392  PHE B CZ  
11898 N N   . THR B 395  ? 0.2299 0.3344 0.2234 -0.0737 -0.0024 0.0269  393  THR B N   
11899 C CA  . THR B 395  ? 0.2367 0.3490 0.2351 -0.0667 0.0004  0.0247  393  THR B CA  
11900 C C   . THR B 395  ? 0.2193 0.3481 0.2216 -0.0671 0.0032  0.0262  393  THR B C   
11901 O O   . THR B 395  ? 0.2494 0.3846 0.2549 -0.0612 0.0056  0.0245  393  THR B O   
11902 C CB  . THR B 395  ? 0.2204 0.3310 0.2223 -0.0630 -0.0004 0.0222  393  THR B CB  
11903 O OG1 . THR B 395  ? 0.2392 0.3562 0.2434 -0.0673 -0.0014 0.0234  393  THR B OG1 
11904 C CG2 . THR B 395  ? 0.2358 0.3308 0.2343 -0.0614 -0.0029 0.0203  393  THR B CG2 
11905 N N   . ARG B 396  ? 0.2330 0.3688 0.2349 -0.0739 0.0030  0.0292  394  ARG B N   
11906 C CA  . ARG B 396  ? 0.2298 0.3819 0.2350 -0.0748 0.0059  0.0310  394  ARG B CA  
11907 C C   . ARG B 396  ? 0.2609 0.4123 0.2613 -0.0791 0.0065  0.0336  394  ARG B C   
11908 O O   . ARG B 396  ? 0.2559 0.3986 0.2514 -0.0852 0.0041  0.0356  394  ARG B O   
11909 C CB  . ARG B 396  ? 0.2167 0.3799 0.2259 -0.0793 0.0055  0.0327  394  ARG B CB  
11910 C CG  . ARG B 396  ? 0.2570 0.4224 0.2711 -0.0749 0.0051  0.0302  394  ARG B CG  
11911 C CD  . ARG B 396  ? 0.2699 0.4484 0.2883 -0.0793 0.0049  0.0321  394  ARG B CD  
11912 N NE  . ARG B 396  ? 0.2800 0.4580 0.3018 -0.0762 0.0036  0.0300  394  ARG B NE  
11913 C CZ  . ARG B 396  ? 0.3554 0.5460 0.3830 -0.0726 0.0051  0.0293  394  ARG B CZ  
11914 N NH1 . ARG B 396  ? 0.4102 0.6160 0.4414 -0.0718 0.0079  0.0306  394  ARG B NH1 
11915 N NH2 . ARG B 396  ? 0.3328 0.5209 0.3627 -0.0696 0.0038  0.0273  394  ARG B NH2 
11916 N N   . LYS B 397  ? 0.2847 0.4449 0.2859 -0.0758 0.0097  0.0337  395  LYS B N   
11917 C CA  . LYS B 397  ? 0.2828 0.4424 0.2791 -0.0792 0.0105  0.0361  395  LYS B CA  
11918 C C   . LYS B 397  ? 0.2585 0.4246 0.2538 -0.0883 0.0099  0.0401  395  LYS B C   
11919 O O   . LYS B 397  ? 0.2967 0.4558 0.2863 -0.0937 0.0087  0.0425  395  LYS B O   
11920 C CB  . LYS B 397  ? 0.2969 0.4661 0.2946 -0.0735 0.0142  0.0351  395  LYS B CB  
11921 C CG  . LYS B 397  ? 0.2854 0.4512 0.2773 -0.0750 0.0150  0.0366  395  LYS B CG  
11922 C CD  . LYS B 397  ? 0.3314 0.5103 0.3231 -0.0808 0.0170  0.0403  395  LYS B CD  
11923 C CE  . LYS B 397  ? 0.3169 0.4929 0.3024 -0.0821 0.0180  0.0419  395  LYS B CE  
11924 N NZ  . LYS B 397  ? 0.2779 0.4672 0.2633 -0.0883 0.0200  0.0458  395  LYS B NZ  
11925 N N   . ILE B 398  ? 0.2696 0.4488 0.2704 -0.0903 0.0107  0.0410  396  ILE B N   
11926 C CA  . ILE B 398  ? 0.3032 0.4896 0.3037 -0.0993 0.0100  0.0449  396  ILE B CA  
11927 C C   . ILE B 398  ? 0.2332 0.4049 0.2288 -0.1058 0.0058  0.0461  396  ILE B C   
11928 O O   . ILE B 398  ? 0.2593 0.4307 0.2514 -0.1139 0.0046  0.0496  396  ILE B O   
11929 C CB  . ILE B 398  ? 0.3316 0.5353 0.3396 -0.0993 0.0114  0.0451  396  ILE B CB  
11930 C CG1 . ILE B 398  ? 0.4005 0.6159 0.4090 -0.1081 0.0118  0.0494  396  ILE B CG1 
11931 C CG2 . ILE B 398  ? 0.3274 0.5259 0.3382 -0.0983 0.0087  0.0431  396  ILE B CG2 
11932 C CD1 . ILE B 398  ? 0.4367 0.6719 0.4528 -0.1071 0.0140  0.0498  396  ILE B CD1 
11933 N N   . HIS B 399  ? 0.2781 0.4368 0.2730 -0.1022 0.0034  0.0432  397  HIS B N   
11934 C CA  . HIS B 399  ? 0.2673 0.4109 0.2569 -0.1075 -0.0007 0.0439  397  HIS B CA  
11935 C C   . HIS B 399  ? 0.2717 0.4031 0.2538 -0.1097 -0.0018 0.0453  397  HIS B C   
11936 O O   . HIS B 399  ? 0.3005 0.4244 0.2775 -0.1170 -0.0044 0.0479  397  HIS B O   
11937 C CB  . HIS B 399  ? 0.2686 0.4022 0.2593 -0.1025 -0.0027 0.0403  397  HIS B CB  
11938 C CG  . HIS B 399  ? 0.2947 0.4383 0.2918 -0.1015 -0.0025 0.0392  397  HIS B CG  
11939 N ND1 . HIS B 399  ? 0.2825 0.4208 0.2819 -0.0961 -0.0034 0.0359  397  HIS B ND1 
11940 C CD2 . HIS B 399  ? 0.3162 0.4750 0.3179 -0.1052 -0.0015 0.0412  397  HIS B CD2 
11941 C CE1 . HIS B 399  ? 0.2510 0.4005 0.2558 -0.0964 -0.0031 0.0359  397  HIS B CE1 
11942 N NE2 . HIS B 399  ? 0.2507 0.4129 0.2572 -0.1018 -0.0020 0.0389  397  HIS B NE2 
11943 N N   . THR B 400  ? 0.2821 0.4108 0.2632 -0.1034 0.0001  0.0436  398  THR B N   
11944 C CA  . THR B 400  ? 0.2792 0.3977 0.2532 -0.1051 -0.0007 0.0450  398  THR B CA  
11945 C C   . THR B 400  ? 0.2374 0.3644 0.2090 -0.1123 0.0005  0.0493  398  THR B C   
11946 O O   . THR B 400  ? 0.2933 0.4108 0.2583 -0.1179 -0.0016 0.0519  398  THR B O   
11947 C CB  . THR B 400  ? 0.2519 0.3682 0.2259 -0.0968 0.0013  0.0423  398  THR B CB  
11948 O OG1 . THR B 400  ? 0.2433 0.3494 0.2184 -0.0912 -0.0004 0.0386  398  THR B OG1 
11949 C CG2 . THR B 400  ? 0.2730 0.3809 0.2399 -0.0985 0.0008  0.0439  398  THR B CG2 
11950 N N   . ASP B 401  ? 0.3101 0.4551 0.2871 -0.1122 0.0039  0.0503  399  ASP B N   
11951 C CA  . ASP B 401  ? 0.3261 0.4810 0.3014 -0.1191 0.0054  0.0545  399  ASP B CA  
11952 C C   . ASP B 401  ? 0.2757 0.4280 0.2489 -0.1290 0.0023  0.0578  399  ASP B C   
11953 O O   . ASP B 401  ? 0.3114 0.4602 0.2789 -0.1359 0.0014  0.0614  399  ASP B O   
11954 C CB  . ASP B 401  ? 0.3485 0.5242 0.3306 -0.1164 0.0096  0.0545  399  ASP B CB  
11955 C CG  . ASP B 401  ? 0.4256 0.6041 0.4082 -0.1078 0.0128  0.0520  399  ASP B CG  
11956 O OD1 . ASP B 401  ? 0.3786 0.5449 0.3555 -0.1058 0.0120  0.0514  399  ASP B OD1 
11957 O OD2 . ASP B 401  ? 0.3430 0.5357 0.3316 -0.1030 0.0158  0.0505  399  ASP B OD2 
11958 N N   . VAL B 402  ? 0.2814 0.4350 0.2587 -0.1298 0.0006  0.0566  400  VAL B N   
11959 C CA  . VAL B 402  ? 0.3097 0.4593 0.2846 -0.1391 -0.0028 0.0594  400  VAL B CA  
11960 C C   . VAL B 402  ? 0.2738 0.4020 0.2401 -0.1416 -0.0067 0.0597  400  VAL B C   
11961 O O   . VAL B 402  ? 0.3358 0.4587 0.2965 -0.1500 -0.0088 0.0633  400  VAL B O   
11962 C CB  . VAL B 402  ? 0.2728 0.4272 0.2537 -0.1385 -0.0040 0.0576  400  VAL B CB  
11963 C CG1 . VAL B 402  ? 0.3716 0.5197 0.3492 -0.1480 -0.0080 0.0600  400  VAL B CG1 
11964 C CG2 . VAL B 402  ? 0.4013 0.5775 0.3905 -0.1363 -0.0003 0.0577  400  VAL B CG2 
11965 N N   . SER B 403  ? 0.2852 0.4008 0.2502 -0.1344 -0.0078 0.0559  401  SER B N   
11966 C CA  . SER B 403  ? 0.3377 0.4330 0.2948 -0.1355 -0.0115 0.0557  401  SER B CA  
11967 C C   . SER B 403  ? 0.3101 0.4014 0.2605 -0.1392 -0.0112 0.0590  401  SER B C   
11968 O O   . SER B 403  ? 0.3303 0.4097 0.2737 -0.1456 -0.0145 0.0615  401  SER B O   
11969 C CB  . SER B 403  ? 0.2864 0.3720 0.2443 -0.1261 -0.0118 0.0512  401  SER B CB  
11970 O OG  . SER B 403  ? 0.3405 0.4077 0.2909 -0.1264 -0.0150 0.0510  401  SER B OG  
11971 N N   . TYR B 404  ? 0.3120 0.4127 0.2642 -0.1352 -0.0075 0.0590  402  TYR B N   
11972 C CA  . TYR B 404  ? 0.3536 0.4518 0.2994 -0.1383 -0.0068 0.0621  402  TYR B CA  
11973 C C   . TYR B 404  ? 0.3405 0.4440 0.2837 -0.1490 -0.0075 0.0672  402  TYR B C   
11974 O O   . TYR B 404  ? 0.3394 0.4315 0.2747 -0.1547 -0.0099 0.0701  402  TYR B O   
11975 C CB  . TYR B 404  ? 0.2819 0.3922 0.2310 -0.1321 -0.0023 0.0610  402  TYR B CB  
11976 C CG  . TYR B 404  ? 0.2922 0.3982 0.2344 -0.1331 -0.0016 0.0633  402  TYR B CG  
11977 C CD1 . TYR B 404  ? 0.3460 0.4591 0.2851 -0.1408 -0.0005 0.0679  402  TYR B CD1 
11978 C CD2 . TYR B 404  ? 0.3232 0.4186 0.2622 -0.1264 -0.0020 0.0607  402  TYR B CD2 
11979 C CE1 . TYR B 404  ? 0.3472 0.4565 0.2797 -0.1417 0.0002  0.0700  402  TYR B CE1 
11980 C CE2 . TYR B 404  ? 0.3294 0.4210 0.2621 -0.1272 -0.0015 0.0627  402  TYR B CE2 
11981 C CZ  . TYR B 404  ? 0.3816 0.4799 0.3108 -0.1348 -0.0004 0.0674  402  TYR B CZ  
11982 O OH  . TYR B 404  ? 0.3958 0.4905 0.3182 -0.1357 0.0001  0.0695  402  TYR B OH  
11983 N N   . ILE B 405  ? 0.3313 0.4519 0.2809 -0.1520 -0.0053 0.0684  403  ILE B N   
11984 C CA  . ILE B 405  ? 0.3372 0.4651 0.2851 -0.1624 -0.0056 0.0733  403  ILE B CA  
11985 C C   . ILE B 405  ? 0.3279 0.4412 0.2707 -0.1698 -0.0107 0.0748  403  ILE B C   
11986 O O   . ILE B 405  ? 0.3787 0.4863 0.3149 -0.1782 -0.0126 0.0790  403  ILE B O   
11987 C CB  . ILE B 405  ? 0.3732 0.5239 0.3301 -0.1631 -0.0022 0.0739  403  ILE B CB  
11988 C CG1 . ILE B 405  ? 0.4188 0.5829 0.3791 -0.1563 0.0029  0.0728  403  ILE B CG1 
11989 C CG2 . ILE B 405  ? 0.3572 0.5154 0.3130 -0.1734 -0.0029 0.0785  403  ILE B CG2 
11990 C CD1 . ILE B 405  ? 0.4595 0.6461 0.4290 -0.1549 0.0065  0.0727  403  ILE B CD1 
11991 N N   . ALA B 406  ? 0.3675 0.4738 0.3126 -0.1667 -0.0132 0.0715  404  ALA B N   
11992 C CA  . ALA B 406  ? 0.3937 0.4845 0.3333 -0.1727 -0.0182 0.0722  404  ALA B CA  
11993 C C   . ALA B 406  ? 0.3674 0.4378 0.2971 -0.1730 -0.0212 0.0728  404  ALA B C   
11994 O O   . ALA B 406  ? 0.4120 0.4718 0.3348 -0.1811 -0.0247 0.0759  404  ALA B O   
11995 C CB  . ALA B 406  ? 0.3711 0.4582 0.3150 -0.1678 -0.0199 0.0679  404  ALA B CB  
11996 N N   . CYS B 407  ? 0.3737 0.4381 0.3027 -0.1644 -0.0201 0.0699  405  CYS B N   
11997 C CA  . CYS B 407  ? 0.3926 0.4383 0.3126 -0.1641 -0.0229 0.0704  405  CYS B CA  
11998 C C   . CYS B 407  ? 0.3512 0.3989 0.2656 -0.1701 -0.0219 0.0751  405  CYS B C   
11999 O O   . CYS B 407  ? 0.4037 0.4361 0.3092 -0.1744 -0.0253 0.0774  405  CYS B O   
12000 C CB  . CYS B 407  ? 0.3628 0.4030 0.2842 -0.1533 -0.0219 0.0659  405  CYS B CB  
12001 S SG  . CYS B 407  ? 0.4332 0.4665 0.3590 -0.1470 -0.0240 0.0607  405  CYS B SG  
12002 N N   . ALA B 408  ? 0.3593 0.4254 0.2784 -0.1704 -0.0174 0.0767  406  ALA B N   
12003 C CA  . ALA B 408  ? 0.3807 0.4509 0.2948 -0.1771 -0.0162 0.0817  406  ALA B CA  
12004 C C   . ALA B 408  ? 0.4245 0.4912 0.3343 -0.1888 -0.0193 0.0861  406  ALA B C   
12005 O O   . ALA B 408  ? 0.4680 0.5250 0.3696 -0.1934 -0.0215 0.0891  406  ALA B O   
12006 C CB  . ALA B 408  ? 0.3984 0.4909 0.3192 -0.1752 -0.0106 0.0823  406  ALA B CB  
12007 N N   . ALA B 409  ? 0.4201 0.4932 0.3352 -0.1913 -0.0203 0.0853  407  ALA B N   
12008 C CA  . ALA B 409  ? 0.4602 0.5291 0.3717 -0.1987 -0.0241 0.0873  407  ALA B CA  
12009 C C   . ALA B 409  ? 0.4472 0.4918 0.3489 -0.2012 -0.0296 0.0875  407  ALA B C   
12010 O O   . ALA B 409  ? 0.4831 0.5198 0.3778 -0.2070 -0.0325 0.0902  407  ALA B O   
12011 C CB  . ALA B 409  ? 0.3919 0.4720 0.3110 -0.1997 -0.0243 0.0859  407  ALA B CB  
12012 N N   . LYS B 410  ? 0.3932 0.4256 0.2942 -0.1967 -0.0310 0.0846  408  LYS B N   
12013 C CA  . LYS B 410  ? 0.4159 0.4247 0.3077 -0.1977 -0.0362 0.0843  408  LYS B CA  
12014 C C   . LYS B 410  ? 0.5174 0.5156 0.4006 -0.1981 -0.0369 0.0867  408  LYS B C   
12015 O O   . LYS B 410  ? 0.5062 0.4893 0.3808 -0.2020 -0.0412 0.0883  408  LYS B O   
12016 C CB  . LYS B 410  ? 0.4642 0.4643 0.3585 -0.1888 -0.0373 0.0789  408  LYS B CB  
12017 C CG  . LYS B 410  ? 0.4423 0.4186 0.3278 -0.1884 -0.0427 0.0777  408  LYS B CG  
12018 C CD  . LYS B 410  ? 0.4779 0.4477 0.3665 -0.1778 -0.0430 0.0719  408  LYS B CD  
12019 C CE  . LYS B 410  ? 0.4748 0.4529 0.3710 -0.1764 -0.0426 0.0690  408  LYS B CE  
12020 N NZ  . LYS B 410  ? 0.5272 0.4954 0.4187 -0.1839 -0.0472 0.0700  408  LYS B NZ  
12021 N N   . LEU B 411  ? 0.4918 0.4976 0.3772 -0.1928 -0.0329 0.0864  409  LEU B N   
12022 C CA  . LEU B 411  ? 0.4630 0.4592 0.3401 -0.1928 -0.0334 0.0888  409  LEU B CA  
12023 C C   . LEU B 411  ? 0.5019 0.5028 0.3752 -0.2003 -0.0336 0.0930  409  LEU B C   
12024 O O   . LEU B 411  ? 0.4977 0.4843 0.3618 -0.2030 -0.0369 0.0950  409  LEU B O   
12025 C CB  . LEU B 411  ? 0.4297 0.4347 0.3111 -0.1836 -0.0292 0.0862  409  LEU B CB  
12026 C CG  . LEU B 411  ? 0.4623 0.4574 0.3453 -0.1731 -0.0303 0.0807  409  LEU B CG  
12027 C CD1 . LEU B 411  ? 0.4391 0.4473 0.3289 -0.1645 -0.0256 0.0779  409  LEU B CD1 
12028 C CD2 . LEU B 411  ? 0.4807 0.4542 0.3539 -0.1722 -0.0346 0.0811  409  LEU B CD2 
12029 N N   . LEU B 412  ? 0.4829 0.5040 0.3633 -0.2027 -0.0303 0.0939  410  LEU B N   
12030 C CA  . LEU B 412  ? 0.5025 0.5299 0.3801 -0.2089 -0.0302 0.0975  410  LEU B CA  
12031 C C   . LEU B 412  ? 0.5626 0.5772 0.4338 -0.2157 -0.0356 0.0990  410  LEU B C   
12032 O O   . LEU B 412  ? 0.5654 0.5802 0.4319 -0.2213 -0.0366 0.1023  410  LEU B O   
12033 C CB  . LEU B 412  ? 0.4672 0.5193 0.3544 -0.2093 -0.0257 0.0978  410  LEU B CB  
12034 C CG  . LEU B 412  ? 0.5393 0.6051 0.4312 -0.2033 -0.0201 0.0970  410  LEU B CG  
12035 C CD1 . LEU B 412  ? 0.5671 0.6563 0.4696 -0.2018 -0.0159 0.0960  410  LEU B CD1 
12036 C CD2 . LEU B 412  ? 0.5960 0.6606 0.4814 -0.2051 -0.0192 0.1000  410  LEU B CD2 
12037 N N   . ALA B 413  ? 0.5342 0.5377 0.4048 -0.2154 -0.0392 0.0968  411  ALA B N   
12038 C CA  . ALA B 413  ? 0.5374 0.5272 0.4011 -0.2212 -0.0445 0.0978  411  ALA B CA  
12039 C C   . ALA B 413  ? 0.6095 0.5752 0.4626 -0.2201 -0.0490 0.0978  411  ALA B C   
12040 O O   . ALA B 413  ? 0.5995 0.5519 0.4455 -0.2246 -0.0537 0.0987  411  ALA B O   
12041 C CB  . ALA B 413  ? 0.5295 0.5205 0.3979 -0.2215 -0.0462 0.0953  411  ALA B CB  
12042 N N   . ALA B 414  ? 0.5216 0.4812 0.3731 -0.2142 -0.0477 0.0967  412  ALA B N   
12043 C CA  . ALA B 414  ? 0.5667 0.5036 0.4084 -0.2121 -0.0519 0.0964  412  ALA B CA  
12044 C C   . ALA B 414  ? 0.5790 0.5140 0.4158 -0.2108 -0.0505 0.0987  412  ALA B C   
12045 O O   . ALA B 414  ? 0.5696 0.4893 0.4005 -0.2064 -0.0525 0.0978  412  ALA B O   
12046 C CB  . ALA B 414  ? 0.5622 0.4893 0.4055 -0.2052 -0.0529 0.0923  412  ALA B CB  
12047 N N   . THR B 415  ? 0.6234 0.5735 0.4622 -0.2146 -0.0472 0.1017  413  THR B N   
12048 C CA  . THR B 415  ? 0.5696 0.5204 0.4045 -0.2131 -0.0452 0.1037  413  THR B CA  
12049 C C   . THR B 415  ? 0.6523 0.5830 0.4756 -0.2150 -0.0499 0.1056  413  THR B C   
12050 O O   . THR B 415  ? 0.5790 0.5064 0.3979 -0.2127 -0.0490 0.1069  413  THR B O   
12051 C CB  . THR B 415  ? 0.5303 0.5018 0.3698 -0.2168 -0.0408 0.1064  413  THR B CB  
12052 O OG1 . THR B 415  ? 0.6073 0.5803 0.4450 -0.2247 -0.0431 0.1087  413  THR B OG1 
12053 C CG2 . THR B 415  ? 0.4991 0.4910 0.3498 -0.2131 -0.0356 0.1043  413  THR B CG2 
12054 N N   . ASP B 416  ? 0.6059 0.5232 0.4237 -0.2192 -0.0550 0.1059  414  ASP B N   
12055 C CA  . ASP B 416  ? 0.5193 0.4160 0.3258 -0.2197 -0.0598 0.1071  414  ASP B CA  
12056 C C   . ASP B 416  ? 0.7251 0.6055 0.5286 -0.2121 -0.0621 0.1040  414  ASP B C   
12057 O O   . ASP B 416  ? 0.7320 0.5976 0.5272 -0.2101 -0.0648 0.1047  414  ASP B O   
12058 C CB  . ASP B 416  ? 0.7329 0.6201 0.5339 -0.2264 -0.0645 0.1083  414  ASP B CB  
12059 N N   . VAL B 417  ? 0.5988 0.4821 0.4090 -0.2075 -0.0609 0.1005  415  VAL B N   
12060 C CA  . VAL B 417  ? 0.5808 0.4496 0.3890 -0.2001 -0.0631 0.0972  415  VAL B CA  
12061 C C   . VAL B 417  ? 0.4803 0.3576 0.2932 -0.1939 -0.0587 0.0963  415  VAL B C   
12062 O O   . VAL B 417  ? 0.6328 0.4978 0.4418 -0.1879 -0.0603 0.0949  415  VAL B O   
12063 C CB  . VAL B 417  ? 0.5864 0.4516 0.3983 -0.1990 -0.0649 0.0938  415  VAL B CB  
12064 N N   . VAL B 418  ? 0.5671 0.4654 0.3884 -0.1949 -0.0533 0.0970  416  VAL B N   
12065 C CA  . VAL B 418  ? 0.4777 0.3854 0.3040 -0.1888 -0.0490 0.0958  416  VAL B CA  
12066 C C   . VAL B 418  ? 0.5623 0.4891 0.3920 -0.1910 -0.0439 0.0983  416  VAL B C   
12067 O O   . VAL B 418  ? 0.5336 0.4708 0.3651 -0.1971 -0.0429 0.1004  416  VAL B O   
12068 C CB  . VAL B 418  ? 0.5212 0.4377 0.3584 -0.1822 -0.0471 0.0903  416  VAL B CB  
12069 C CG1 . VAL B 418  ? 0.4742 0.3729 0.3089 -0.1778 -0.0518 0.0866  416  VAL B CG1 
12070 C CG2 . VAL B 418  ? 0.5406 0.4726 0.3843 -0.1888 -0.0449 0.0917  416  VAL B CG2 
12071 N N   . PHE B 419  ? 0.4969 0.4294 0.3287 -0.1839 -0.0408 0.0967  417  PHE B N   
12072 C CA  . PHE B 419  ? 0.4617 0.4122 0.2964 -0.1849 -0.0356 0.0988  417  PHE B CA  
12073 C C   . PHE B 419  ? 0.4968 0.4649 0.3435 -0.1780 -0.0311 0.0943  417  PHE B C   
12074 O O   . PHE B 419  ? 0.4358 0.4035 0.2858 -0.1685 -0.0301 0.0901  417  PHE B O   
12075 C CB  . PHE B 419  ? 0.4391 0.3831 0.2669 -0.1813 -0.0357 0.0998  417  PHE B CB  
12076 C CG  . PHE B 419  ? 0.5002 0.4619 0.3303 -0.1813 -0.0304 0.1015  417  PHE B CG  
12077 C CD1 . PHE B 419  ? 0.5085 0.4825 0.3395 -0.1884 -0.0283 0.1048  417  PHE B CD1 
12078 C CD2 . PHE B 419  ? 0.4166 0.3831 0.2496 -0.1722 -0.0278 0.0981  417  PHE B CD2 
12079 C CE1 . PHE B 419  ? 0.5146 0.5051 0.3481 -0.1875 -0.0234 0.1058  417  PHE B CE1 
12080 C CE2 . PHE B 419  ? 0.4507 0.4328 0.2851 -0.1719 -0.0231 0.0995  417  PHE B CE2 
12081 C CZ  . PHE B 419  ? 0.4718 0.4658 0.3053 -0.1805 -0.0205 0.1042  417  PHE B CZ  
12082 N N   . PRO B 420  ? 0.4480 0.4319 0.3016 -0.1823 -0.0284 0.0951  418  PRO B N   
12083 C CA  . PRO B 420  ? 0.4542 0.4542 0.3191 -0.1756 -0.0244 0.0908  418  PRO B CA  
12084 C C   . PRO B 420  ? 0.4598 0.4731 0.3271 -0.1708 -0.0196 0.0904  418  PRO B C   
12085 O O   . PRO B 420  ? 0.4217 0.4421 0.2853 -0.1759 -0.0175 0.0946  418  PRO B O   
12086 C CB  . PRO B 420  ? 0.4228 0.4354 0.2929 -0.1830 -0.0232 0.0928  418  PRO B CB  
12087 C CG  . PRO B 420  ? 0.4596 0.4586 0.3216 -0.1922 -0.0278 0.0967  418  PRO B CG  
12088 C CD  . PRO B 420  ? 0.4637 0.4510 0.3160 -0.1924 -0.0294 0.0990  418  PRO B CD  
12089 N N   . GLN B 421  ? 0.3864 0.4027 0.2596 -0.1609 -0.0179 0.0854  419  GLN B N   
12090 C CA  . GLN B 421  ? 0.4332 0.4613 0.3090 -0.1551 -0.0136 0.0841  419  GLN B CA  
12091 C C   . GLN B 421  ? 0.4004 0.4434 0.2872 -0.1496 -0.0102 0.0801  419  GLN B C   
12092 O O   . GLN B 421  ? 0.3637 0.4015 0.2547 -0.1429 -0.0113 0.0756  419  GLN B O   
12093 C CB  . GLN B 421  ? 0.3692 0.3844 0.2402 -0.1481 -0.0153 0.0817  419  GLN B CB  
12094 C CG  . GLN B 421  ? 0.4051 0.4034 0.2651 -0.1529 -0.0194 0.0854  419  GLN B CG  
12095 C CD  . GLN B 421  ? 0.4120 0.3951 0.2681 -0.1457 -0.0223 0.0825  419  GLN B CD  
12096 O OE1 . GLN B 421  ? 0.3862 0.3609 0.2452 -0.1409 -0.0247 0.0788  419  GLN B OE1 
12097 N NE2 . GLN B 421  ? 0.3805 0.3603 0.2298 -0.1450 -0.0222 0.0844  419  GLN B NE2 
12098 N N   . PHE B 422  ? 0.3792 0.4409 0.2706 -0.1523 -0.0060 0.0818  420  PHE B N   
12099 C CA  . PHE B 422  ? 0.3893 0.4655 0.2910 -0.1482 -0.0031 0.0786  420  PHE B CA  
12100 C C   . PHE B 422  ? 0.3608 0.4458 0.2659 -0.1393 0.0007  0.0753  420  PHE B C   
12101 O O   . PHE B 422  ? 0.3585 0.4570 0.2639 -0.1399 0.0045  0.0770  420  PHE B O   
12102 C CB  . PHE B 422  ? 0.3728 0.4646 0.2782 -0.1560 -0.0011 0.0821  420  PHE B CB  
12103 C CG  . PHE B 422  ? 0.4037 0.4864 0.3056 -0.1650 -0.0051 0.0852  420  PHE B CG  
12104 C CD1 . PHE B 422  ? 0.4097 0.4838 0.3144 -0.1639 -0.0083 0.0825  420  PHE B CD1 
12105 C CD2 . PHE B 422  ? 0.3960 0.4784 0.2916 -0.1747 -0.0057 0.0907  420  PHE B CD2 
12106 C CE1 . PHE B 422  ? 0.4138 0.4787 0.3147 -0.1720 -0.0122 0.0851  420  PHE B CE1 
12107 C CE2 . PHE B 422  ? 0.4393 0.5124 0.3312 -0.1832 -0.0097 0.0936  420  PHE B CE2 
12108 C CZ  . PHE B 422  ? 0.4218 0.4860 0.3163 -0.1818 -0.0130 0.0906  420  PHE B CZ  
12109 N N   . ALA B 423  ? 0.3556 0.4329 0.2631 -0.1310 -0.0004 0.0706  421  ALA B N   
12110 C CA  . ALA B 423  ? 0.3169 0.4001 0.2274 -0.1223 0.0025  0.0670  421  ALA B CA  
12111 C C   . ALA B 423  ? 0.3298 0.4284 0.2500 -0.1184 0.0057  0.0643  421  ALA B C   
12112 O O   . ALA B 423  ? 0.3582 0.4539 0.2835 -0.1157 0.0043  0.0615  421  ALA B O   
12113 C CB  . ALA B 423  ? 0.3329 0.4004 0.2414 -0.1156 -0.0004 0.0634  421  ALA B CB  
12114 N N   . THR B 424  ? 0.3781 0.4930 0.3007 -0.1177 0.0100  0.0650  422  THR B N   
12115 C CA  . THR B 424  ? 0.3238 0.4537 0.2553 -0.1133 0.0132  0.0625  422  THR B CA  
12116 C C   . THR B 424  ? 0.3520 0.4970 0.2841 -0.1107 0.0178  0.0628  422  THR B C   
12117 O O   . THR B 424  ? 0.3608 0.5091 0.2875 -0.1155 0.0190  0.0664  422  THR B O   
12118 C CB  . THR B 424  ? 0.3652 0.5030 0.3015 -0.1196 0.0128  0.0645  422  THR B CB  
12119 O OG1 . THR B 424  ? 0.3277 0.4798 0.2726 -0.1146 0.0157  0.0618  422  THR B OG1 
12120 C CG2 . THR B 424  ? 0.3716 0.5173 0.3045 -0.1289 0.0139  0.0700  422  THR B CG2 
12121 N N   . HIS B 425  ? 0.3385 0.4920 0.2766 -0.1029 0.0203  0.0589  423  HIS B N   
12122 C CA  . HIS B 425  ? 0.4023 0.5717 0.3421 -0.0994 0.0250  0.0585  423  HIS B CA  
12123 C C   . HIS B 425  ? 0.4145 0.6020 0.3620 -0.1008 0.0277  0.0591  423  HIS B C   
12124 O O   . HIS B 425  ? 0.4143 0.6165 0.3644 -0.0970 0.0317  0.0584  423  HIS B O   
12125 C CB  . HIS B 425  ? 0.3044 0.4709 0.2450 -0.0894 0.0259  0.0536  423  HIS B CB  
12126 C CG  . HIS B 425  ? 0.3231 0.4737 0.2563 -0.0876 0.0235  0.0529  423  HIS B CG  
12127 N ND1 . HIS B 425  ? 0.4183 0.5582 0.3522 -0.0806 0.0217  0.0487  423  HIS B ND1 
12128 C CD2 . HIS B 425  ? 0.3709 0.5147 0.2960 -0.0920 0.0225  0.0561  423  HIS B CD2 
12129 C CE1 . HIS B 425  ? 0.4441 0.5718 0.3709 -0.0807 0.0197  0.0492  423  HIS B CE1 
12130 N NE2 . HIS B 425  ? 0.3720 0.5015 0.2932 -0.0874 0.0200  0.0536  423  HIS B NE2 
12131 N N   . ASN B 426  ? 0.3752 0.5618 0.3261 -0.1059 0.0255  0.0604  424  ASN B N   
12132 C CA  . ASN B 426  ? 0.3351 0.5379 0.2939 -0.1071 0.0274  0.0608  424  ASN B CA  
12133 C C   . ASN B 426  ? 0.3461 0.5600 0.3036 -0.1165 0.0287  0.0661  424  ASN B C   
12134 O O   . ASN B 426  ? 0.3480 0.5538 0.3020 -0.1247 0.0257  0.0693  424  ASN B O   
12135 C CB  . ASN B 426  ? 0.3276 0.5226 0.2906 -0.1072 0.0241  0.0590  424  ASN B CB  
12136 C CG  . ASN B 426  ? 0.4040 0.6147 0.3755 -0.1070 0.0257  0.0586  424  ASN B CG  
12137 O OD1 . ASN B 426  ? 0.3759 0.6011 0.3495 -0.1125 0.0276  0.0619  424  ASN B OD1 
12138 N ND2 . ASN B 426  ? 0.3894 0.5977 0.3660 -0.1009 0.0248  0.0548  424  ASN B ND2 
12139 N N   . ALA B 427  ? 0.3890 0.6215 0.3493 -0.1153 0.0331  0.0669  425  ALA B N   
12140 C CA  . ALA B 427  ? 0.4053 0.6484 0.3650 -0.1229 0.0341  0.0713  425  ALA B CA  
12141 C C   . ALA B 427  ? 0.3714 0.6174 0.3362 -0.1290 0.0315  0.0728  425  ALA B C   
12142 O O   . ALA B 427  ? 0.3674 0.6119 0.3296 -0.1368 0.0295  0.0762  425  ALA B O   
12143 C CB  . ALA B 427  ? 0.4528 0.7127 0.4160 -0.1173 0.0382  0.0699  425  ALA B CB  
12144 N N   . GLN B 428  ? 0.4063 0.6563 0.3781 -0.1255 0.0313  0.0702  426  GLN B N   
12145 C CA  . GLN B 428  ? 0.4020 0.6534 0.3780 -0.1311 0.0284  0.0713  426  GLN B CA  
12146 C C   . GLN B 428  ? 0.3759 0.6094 0.3459 -0.1386 0.0241  0.0736  426  GLN B C   
12147 O O   . GLN B 428  ? 0.4120 0.6434 0.3803 -0.1464 0.0214  0.0765  426  GLN B O   
12148 C CB  . GLN B 428  ? 0.3798 0.6381 0.3641 -0.1252 0.0290  0.0679  426  GLN B CB  
12149 C CG  . GLN B 428  ? 0.3837 0.6481 0.3734 -0.1298 0.0266  0.0688  426  GLN B CG  
12150 C CD  . GLN B 428  ? 0.4175 0.6670 0.4039 -0.1370 0.0222  0.0703  426  GLN B CD  
12151 O OE1 . GLN B 428  ? 0.4399 0.6761 0.4234 -0.1358 0.0210  0.0691  426  GLN B OE1 
12152 N NE2 . GLN B 428  ? 0.4524 0.7034 0.4387 -0.1445 0.0196  0.0730  426  GLN B NE2 
12153 N N   . THR B 429  ? 0.3946 0.6125 0.3608 -0.1350 0.0226  0.0715  427  THR B N   
12154 C CA  . THR B 429  ? 0.4279 0.6259 0.3875 -0.1402 0.0179  0.0727  427  THR B CA  
12155 C C   . THR B 429  ? 0.3929 0.5876 0.3447 -0.1483 0.0176  0.0776  427  THR B C   
12156 O O   . THR B 429  ? 0.3737 0.5610 0.3221 -0.1565 0.0142  0.0805  427  THR B O   
12157 C CB  . THR B 429  ? 0.3633 0.5441 0.3202 -0.1323 0.0159  0.0685  427  THR B CB  
12158 O OG1 . THR B 429  ? 0.3704 0.5553 0.3345 -0.1245 0.0167  0.0641  427  THR B OG1 
12159 C CG2 . THR B 429  ? 0.4224 0.5834 0.3736 -0.1368 0.0109  0.0693  427  THR B CG2 
12160 N N   . LEU B 430  ? 0.4145 0.6132 0.3628 -0.1454 0.0206  0.0781  428  LEU B N   
12161 C CA  . LEU B 430  ? 0.3594 0.5536 0.3001 -0.1513 0.0198  0.0818  428  LEU B CA  
12162 C C   . LEU B 430  ? 0.3719 0.5753 0.3152 -0.1580 0.0189  0.0845  428  LEU B C   
12163 O O   . LEU B 430  ? 0.3960 0.5896 0.3338 -0.1656 0.0156  0.0876  428  LEU B O   
12164 C CB  . LEU B 430  ? 0.4449 0.6452 0.3831 -0.1458 0.0237  0.0812  428  LEU B CB  
12165 C CG  . LEU B 430  ? 0.3930 0.5873 0.3225 -0.1491 0.0235  0.0842  428  LEU B CG  
12166 C CD1 . LEU B 430  ? 0.3952 0.5958 0.3234 -0.1415 0.0275  0.0821  428  LEU B CD1 
12167 C CD2 . LEU B 430  ? 0.4493 0.6514 0.3789 -0.1560 0.0232  0.0875  428  LEU B CD2 
12168 N N   . ALA B 431  ? 0.4353 0.6572 0.3867 -0.1551 0.0217  0.0833  429  ALA B N   
12169 C CA  . ALA B 431  ? 0.4270 0.6593 0.3809 -0.1612 0.0211  0.0858  429  ALA B CA  
12170 C C   . ALA B 431  ? 0.4361 0.6597 0.3898 -0.1683 0.0165  0.0872  429  ALA B C   
12171 O O   . ALA B 431  ? 0.4645 0.6860 0.4147 -0.1760 0.0142  0.0904  429  ALA B O   
12172 C CB  . ALA B 431  ? 0.4040 0.6571 0.3670 -0.1558 0.0247  0.0838  429  ALA B CB  
12173 N N   . ALA B 432  ? 0.4309 0.6493 0.3879 -0.1657 0.0151  0.0846  430  ALA B N   
12174 C CA  . ALA B 432  ? 0.3609 0.5709 0.3176 -0.1718 0.0106  0.0854  430  ALA B CA  
12175 C C   . ALA B 432  ? 0.4281 0.6189 0.3751 -0.1786 0.0066  0.0882  430  ALA B C   
12176 O O   . ALA B 432  ? 0.4532 0.6401 0.3977 -0.1860 0.0033  0.0905  430  ALA B O   
12177 C CB  . ALA B 432  ? 0.3805 0.5869 0.3418 -0.1671 0.0100  0.0820  430  ALA B CB  
12178 N N   . ILE B 433  ? 0.4330 0.6112 0.3738 -0.1760 0.0068  0.0879  431  ILE B N   
12179 C CA  . ILE B 433  ? 0.4424 0.6013 0.3734 -0.1816 0.0028  0.0903  431  ILE B CA  
12180 C C   . ILE B 433  ? 0.3925 0.5544 0.3188 -0.1868 0.0031  0.0939  431  ILE B C   
12181 O O   . ILE B 433  ? 0.4745 0.6254 0.3946 -0.1939 -0.0007 0.0966  431  ILE B O   
12182 C CB  . ILE B 433  ? 0.4320 0.5766 0.3578 -0.1769 0.0027  0.0889  431  ILE B CB  
12183 C CG1 . ILE B 433  ? 0.4934 0.6357 0.4243 -0.1721 0.0025  0.0855  431  ILE B CG1 
12184 C CG2 . ILE B 433  ? 0.4833 0.6071 0.3988 -0.1820 -0.0017 0.0913  431  ILE B CG2 
12185 C CD1 . ILE B 433  ? 0.4702 0.5976 0.3975 -0.1641 0.0014  0.0820  431  ILE B CD1 
12186 N N   . TYR B 434  ? 0.4484 0.6247 0.3771 -0.1832 0.0075  0.0940  432  TYR B N   
12187 C CA  . TYR B 434  ? 0.4265 0.6070 0.3511 -0.1878 0.0081  0.0973  432  TYR B CA  
12188 C C   . TYR B 434  ? 0.4679 0.6537 0.3940 -0.1957 0.0058  0.0998  432  TYR B C   
12189 O O   . TYR B 434  ? 0.5286 0.7067 0.4481 -0.2026 0.0033  0.1032  432  TYR B O   
12190 C CB  . TYR B 434  ? 0.4613 0.6588 0.3897 -0.1818 0.0135  0.0963  432  TYR B CB  
12191 C CG  . TYR B 434  ? 0.4679 0.6748 0.3945 -0.1861 0.0150  0.0995  432  TYR B CG  
12192 C CD1 . TYR B 434  ? 0.5176 0.7133 0.4350 -0.1903 0.0136  0.1025  432  TYR B CD1 
12193 C CD2 . TYR B 434  ? 0.4893 0.7162 0.4231 -0.1859 0.0177  0.0996  432  TYR B CD2 
12194 C CE1 . TYR B 434  ? 0.6081 0.8128 0.5238 -0.1944 0.0150  0.1055  432  TYR B CE1 
12195 C CE2 . TYR B 434  ? 0.4935 0.7296 0.4257 -0.1899 0.0191  0.1026  432  TYR B CE2 
12196 C CZ  . TYR B 434  ? 0.6081 0.8331 0.5313 -0.1943 0.0178  0.1055  432  TYR B CZ  
12197 O OH  . TYR B 434  ? 0.6001 0.8346 0.5217 -0.1984 0.0194  0.1086  432  TYR B OH  
12198 N N   . HIS B 435  ? 0.4917 0.6895 0.4260 -0.1948 0.0064  0.0983  433  HIS B N   
12199 C CA  . HIS B 435  ? 0.5350 0.7384 0.4709 -0.2021 0.0041  0.1006  433  HIS B CA  
12200 C C   . HIS B 435  ? 0.5067 0.6931 0.4383 -0.2076 -0.0014 0.1011  433  HIS B C   
12201 O O   . HIS B 435  ? 0.4998 0.6826 0.4276 -0.2154 -0.0044 0.1040  433  HIS B O   
12202 C CB  . HIS B 435  ? 0.5378 0.7620 0.4840 -0.1988 0.0069  0.0989  433  HIS B CB  
12203 C CG  . HIS B 435  ? 0.5289 0.7709 0.4784 -0.1956 0.0116  0.0994  433  HIS B CG  
12204 N ND1 . HIS B 435  ? 0.4696 0.7202 0.4178 -0.2014 0.0120  0.1028  433  HIS B ND1 
12205 C CD2 . HIS B 435  ? 0.4683 0.7205 0.4219 -0.1871 0.0161  0.0968  433  HIS B CD2 
12206 C CE1 . HIS B 435  ? 0.5335 0.7992 0.4851 -0.1965 0.0165  0.1022  433  HIS B CE1 
12207 N NE2 . HIS B 435  ? 0.4437 0.7104 0.3985 -0.1877 0.0190  0.0986  433  HIS B NE2 
12208 N N   . MET B 436  ? 0.4655 0.6411 0.3975 -0.2036 -0.0027 0.0982  434  MET B N   
12209 C CA  . MET B 436  ? 0.4755 0.6331 0.4026 -0.2080 -0.0080 0.0984  434  MET B CA  
12210 C C   . MET B 436  ? 0.5424 0.6825 0.4586 -0.2135 -0.0113 0.1013  434  MET B C   
12211 O O   . MET B 436  ? 0.5402 0.6685 0.4516 -0.2196 -0.0159 0.1026  434  MET B O   
12212 C CB  . MET B 436  ? 0.4951 0.6441 0.4241 -0.2018 -0.0083 0.0947  434  MET B CB  
12213 C CG  . MET B 436  ? 0.5129 0.6416 0.4363 -0.2050 -0.0135 0.0943  434  MET B CG  
12214 S SD  . MET B 436  ? 0.5929 0.7135 0.5189 -0.1969 -0.0130 0.0900  434  MET B SD  
12215 C CE  . MET B 436  ? 0.5005 0.6434 0.4391 -0.1926 -0.0095 0.0874  434  MET B CE  
12216 N N   . ALA B 437  ? 0.4878 0.6257 0.3999 -0.2112 -0.0092 0.1022  435  ALA B N   
12217 C CA  . ALA B 437  ? 0.5305 0.6507 0.4320 -0.2156 -0.0124 0.1048  435  ALA B CA  
12218 C C   . ALA B 437  ? 0.5656 0.6890 0.4636 -0.2239 -0.0139 0.1087  435  ALA B C   
12219 O O   . ALA B 437  ? 0.5656 0.6728 0.4548 -0.2290 -0.0180 0.1109  435  ALA B O   
12220 C CB  . ALA B 437  ? 0.5611 0.6785 0.4590 -0.2104 -0.0097 0.1046  435  ALA B CB  
12221 N N   . GLY B 438  ? 0.5396 0.6831 0.4441 -0.2252 -0.0110 0.1096  436  GLY B N   
12222 C CA  . GLY B 438  ? 0.5733 0.7211 0.4749 -0.2333 -0.0122 0.1134  436  GLY B CA  
12223 C C   . GLY B 438  ? 0.6039 0.7557 0.5016 -0.2337 -0.0096 0.1159  436  GLY B C   
12224 O O   . GLY B 438  ? 0.5873 0.7421 0.4858 -0.2272 -0.0060 0.1145  436  GLY B O   
12225 N N   . LYS B 439  ? 0.6325 0.7838 0.5255 -0.2416 -0.0114 0.1197  437  LYS B N   
12226 C CA  . LYS B 439  ? 0.4842 0.6408 0.3737 -0.2431 -0.0089 0.1225  437  LYS B CA  
12227 C C   . LYS B 439  ? 0.6469 0.7829 0.5249 -0.2462 -0.0122 0.1247  437  LYS B C   
12228 O O   . LYS B 439  ? 0.6882 0.8262 0.5626 -0.2458 -0.0100 0.1265  437  LYS B O   
12229 C CB  . LYS B 439  ? 0.5843 0.7566 0.4765 -0.2499 -0.0082 0.1256  437  LYS B CB  
12230 N N   . ASP B 440  ? 0.6229 0.7392 0.4949 -0.2492 -0.0175 0.1246  438  ASP B N   
12231 C CA  . ASP B 440  ? 0.7328 0.8286 0.5937 -0.2518 -0.0210 0.1266  438  ASP B CA  
12232 C C   . ASP B 440  ? 0.7395 0.8262 0.5984 -0.2436 -0.0198 0.1240  438  ASP B C   
12233 O O   . ASP B 440  ? 0.7767 0.8526 0.6359 -0.2398 -0.0218 0.1211  438  ASP B O   
12234 C CB  . ASP B 440  ? 0.7556 0.8336 0.6105 -0.2574 -0.0273 0.1272  438  ASP B CB  
12235 N N   . PHE B 441  ? 0.6254 0.7167 0.4823 -0.2409 -0.0165 0.1250  439  PHE B N   
12236 C CA  . PHE B 441  ? 0.6654 0.7495 0.5204 -0.2331 -0.0150 0.1227  439  PHE B CA  
12237 C C   . PHE B 441  ? 0.7375 0.8106 0.5827 -0.2342 -0.0158 0.1253  439  PHE B C   
12238 O O   . PHE B 441  ? 0.6466 0.7290 0.4905 -0.2375 -0.0137 0.1281  439  PHE B O   
12239 C CB  . PHE B 441  ? 0.5933 0.6966 0.4570 -0.2259 -0.0090 0.1201  439  PHE B CB  
12240 C CG  . PHE B 441  ? 0.6481 0.7439 0.5099 -0.2178 -0.0077 0.1176  439  PHE B CG  
12241 C CD1 . PHE B 441  ? 0.5825 0.6719 0.4473 -0.2129 -0.0087 0.1141  439  PHE B CD1 
12242 C CD2 . PHE B 441  ? 0.5415 0.6363 0.3981 -0.2153 -0.0056 0.1186  439  PHE B CD2 
12243 C CE1 . PHE B 441  ? 0.5754 0.6579 0.4381 -0.2057 -0.0077 0.1119  439  PHE B CE1 
12244 C CE2 . PHE B 441  ? 0.6016 0.6892 0.4559 -0.2079 -0.0047 0.1163  439  PHE B CE2 
12245 C CZ  . PHE B 441  ? 0.6137 0.6951 0.4710 -0.2032 -0.0058 0.1130  439  PHE B CZ  
12246 N N   . HIS B 442  ? 0.6467 0.7002 0.4852 -0.2311 -0.0190 0.1242  440  HIS B N   
12247 C CA  . HIS B 442  ? 0.6355 0.6779 0.4652 -0.2296 -0.0195 0.1257  440  HIS B CA  
12248 C C   . HIS B 442  ? 0.6209 0.6582 0.4511 -0.2206 -0.0182 0.1224  440  HIS B C   
12249 O O   . HIS B 442  ? 0.6226 0.6555 0.4564 -0.2173 -0.0194 0.1195  440  HIS B O   
12250 C CB  . HIS B 442  ? 0.7089 0.7296 0.5282 -0.2350 -0.0256 0.1281  440  HIS B CB  
12251 C CG  . HIS B 442  ? 0.8554 0.8600 0.6735 -0.2341 -0.0303 0.1258  440  HIS B CG  
12252 N ND1 . HIS B 442  ? 0.7995 0.7858 0.6119 -0.2290 -0.0331 0.1241  440  HIS B ND1 
12253 C CD2 . HIS B 442  ? 0.7586 0.7628 0.5803 -0.2373 -0.0326 0.1249  440  HIS B CD2 
12254 C CE1 . HIS B 442  ? 0.8636 0.8389 0.6761 -0.2291 -0.0369 0.1222  440  HIS B CE1 
12255 N NE2 . HIS B 442  ? 0.9342 0.9198 0.7522 -0.2342 -0.0367 0.1226  440  HIS B NE2 
12256 N N   . VAL B 443  ? 0.5905 0.6290 0.4171 -0.2167 -0.0157 0.1228  441  VAL B N   
12257 C CA  . VAL B 443  ? 0.5248 0.5555 0.3499 -0.2086 -0.0154 0.1200  441  VAL B CA  
12258 C C   . VAL B 443  ? 0.6322 0.6394 0.4506 -0.2089 -0.0214 0.1196  441  VAL B C   
12259 O O   . VAL B 443  ? 0.6203 0.6143 0.4309 -0.2140 -0.0254 0.1222  441  VAL B O   
12260 C CB  . VAL B 443  ? 0.5987 0.6321 0.4192 -0.2050 -0.0126 0.1208  441  VAL B CB  
12261 C CG1 . VAL B 443  ? 0.5382 0.5579 0.3542 -0.1978 -0.0141 0.1185  441  VAL B CG1 
12262 C CG2 . VAL B 443  ? 0.6175 0.6743 0.4458 -0.2021 -0.0063 0.1198  441  VAL B CG2 
12263 N N   . GLY B 444  ? 0.5946 0.5969 0.4162 -0.2036 -0.0221 0.1162  442  GLY B N   
12264 C CA  . GLY B 444  ? 0.4879 0.4697 0.3048 -0.2037 -0.0276 0.1153  442  GLY B CA  
12265 C C   . GLY B 444  ? 0.5740 0.5572 0.3967 -0.2064 -0.0291 0.1139  442  GLY B C   
12266 O O   . GLY B 444  ? 0.5706 0.5382 0.3909 -0.2051 -0.0332 0.1122  442  GLY B O   
12267 N N   . LYS B 445  ? 0.5789 0.5803 0.4092 -0.2099 -0.0261 0.1144  443  LYS B N   
12268 C CA  . LYS B 445  ? 0.5554 0.5600 0.3919 -0.2123 -0.0273 0.1129  443  LYS B CA  
12269 C C   . LYS B 445  ? 0.5463 0.5557 0.3900 -0.2054 -0.0251 0.1090  443  LYS B C   
12270 O O   . LYS B 445  ? 0.5555 0.5531 0.3990 -0.2038 -0.0282 0.1069  443  LYS B O   
12271 C CB  . LYS B 445  ? 0.5982 0.6214 0.4404 -0.2179 -0.0249 0.1147  443  LYS B CB  
12272 C CG  . LYS B 445  ? 0.6070 0.6375 0.4569 -0.2197 -0.0253 0.1130  443  LYS B CG  
12273 C CD  . LYS B 445  ? 0.6792 0.7038 0.5255 -0.2281 -0.0295 0.1154  443  LYS B CD  
12274 C CE  . LYS B 445  ? 0.7691 0.8068 0.6239 -0.2302 -0.0288 0.1142  443  LYS B CE  
12275 N NZ  . LYS B 445  ? 0.8523 0.9146 0.7161 -0.2287 -0.0230 0.1143  443  LYS B NZ  
12276 N N   . TYR B 446  ? 0.5160 0.5428 0.3659 -0.2010 -0.0197 0.1079  444  TYR B N   
12277 C CA  . TYR B 446  ? 0.4902 0.5220 0.3462 -0.1938 -0.0171 0.1044  444  TYR B CA  
12278 C C   . TYR B 446  ? 0.5288 0.5738 0.3864 -0.1889 -0.0120 0.1041  444  TYR B C   
12279 O O   . TYR B 446  ? 0.4903 0.5421 0.3456 -0.1914 -0.0103 0.1065  444  TYR B O   
12280 C CB  . TYR B 446  ? 0.4276 0.4713 0.2934 -0.1945 -0.0160 0.1025  444  TYR B CB  
12281 C CG  . TYR B 446  ? 0.5284 0.5949 0.4016 -0.1963 -0.0118 0.1032  444  TYR B CG  
12282 C CD1 . TYR B 446  ? 0.4862 0.5697 0.3662 -0.1904 -0.0065 0.1013  444  TYR B CD1 
12283 C CD2 . TYR B 446  ? 0.5192 0.5901 0.3925 -0.2038 -0.0132 0.1058  444  TYR B CD2 
12284 C CE1 . TYR B 446  ? 0.5499 0.6539 0.4367 -0.1914 -0.0027 0.1018  444  TYR B CE1 
12285 C CE2 . TYR B 446  ? 0.5434 0.6351 0.4234 -0.2053 -0.0095 0.1065  444  TYR B CE2 
12286 C CZ  . TYR B 446  ? 0.5317 0.6399 0.4186 -0.1989 -0.0043 0.1045  444  TYR B CZ  
12287 O OH  . TYR B 446  ? 0.6297 0.7586 0.5234 -0.1998 -0.0008 0.1050  444  TYR B OH  
12288 N N   . GLU B 447  ? 0.4764 0.5248 0.3378 -0.1817 -0.0096 0.1010  445  GLU B N   
12289 C CA  . GLU B 447  ? 0.4622 0.5241 0.3256 -0.1763 -0.0046 0.1001  445  GLU B CA  
12290 C C   . GLU B 447  ? 0.4036 0.4770 0.2774 -0.1687 -0.0018 0.0952  445  GLU B C   
12291 O O   . GLU B 447  ? 0.4255 0.4938 0.3040 -0.1667 -0.0040 0.0922  445  GLU B O   
12292 C CB  . GLU B 447  ? 0.3854 0.4346 0.2406 -0.1718 -0.0059 0.0998  445  GLU B CB  
12293 C CG  . GLU B 447  ? 0.3782 0.4134 0.2350 -0.1631 -0.0090 0.0945  445  GLU B CG  
12294 C CD  . GLU B 447  ? 0.4266 0.4499 0.2762 -0.1582 -0.0106 0.0938  445  GLU B CD  
12295 O OE1 . GLU B 447  ? 0.4409 0.4644 0.2830 -0.1622 -0.0099 0.0977  445  GLU B OE1 
12296 O OE2 . GLU B 447  ? 0.4406 0.4548 0.2919 -0.1504 -0.0125 0.0893  445  GLU B OE2 
12297 N N   . PHE B 448  ? 0.4091 0.4979 0.2867 -0.1640 0.0030  0.0939  446  PHE B N   
12298 C CA  . PHE B 448  ? 0.3807 0.4777 0.2671 -0.1545 0.0054  0.0883  446  PHE B CA  
12299 C C   . PHE B 448  ? 0.3465 0.4341 0.2299 -0.1457 0.0049  0.0847  446  PHE B C   
12300 O O   . PHE B 448  ? 0.3870 0.4653 0.2620 -0.1467 0.0035  0.0867  446  PHE B O   
12301 C CB  . PHE B 448  ? 0.4642 0.5844 0.3571 -0.1541 0.0109  0.0886  446  PHE B CB  
12302 C CG  . PHE B 448  ? 0.4570 0.5885 0.3547 -0.1619 0.0115  0.0915  446  PHE B CG  
12303 C CD1 . PHE B 448  ? 0.4519 0.5878 0.3581 -0.1597 0.0111  0.0886  446  PHE B CD1 
12304 C CD2 . PHE B 448  ? 0.4562 0.5919 0.3520 -0.1682 0.0112  0.0948  446  PHE B CD2 
12305 C CE1 . PHE B 448  ? 0.4023 0.5478 0.3137 -0.1655 0.0109  0.0902  446  PHE B CE1 
12306 C CE2 . PHE B 448  ? 0.4749 0.6198 0.3765 -0.1733 0.0106  0.0958  446  PHE B CE2 
12307 C CZ  . PHE B 448  ? 0.4222 0.5720 0.3316 -0.1719 0.0104  0.0935  446  PHE B CZ  
12308 N N   . GLN B 449  ? 0.3842 0.4742 0.2746 -0.1371 0.0058  0.0794  447  GLN B N   
12309 C CA  . GLN B 449  ? 0.3815 0.4640 0.2702 -0.1284 0.0054  0.0756  447  GLN B CA  
12310 C C   . GLN B 449  ? 0.3764 0.4723 0.2733 -0.1205 0.0092  0.0713  447  GLN B C   
12311 O O   . GLN B 449  ? 0.3658 0.4723 0.2703 -0.1204 0.0109  0.0702  447  GLN B O   
12312 C CB  . GLN B 449  ? 0.3402 0.4037 0.2272 -0.1257 0.0005  0.0733  447  GLN B CB  
12313 C CG  . GLN B 449  ? 0.4136 0.4618 0.2919 -0.1326 -0.0038 0.0772  447  GLN B CG  
12314 C CD  . GLN B 449  ? 0.3451 0.3748 0.2200 -0.1278 -0.0081 0.0746  447  GLN B CD  
12315 O OE1 . GLN B 449  ? 0.4155 0.4441 0.2957 -0.1202 -0.0081 0.0699  447  GLN B OE1 
12316 N NE2 . GLN B 449  ? 0.3807 0.3960 0.2468 -0.1323 -0.0118 0.0777  447  GLN B NE2 
12317 N N   . CYS B 450  ? 0.3422 0.4372 0.2368 -0.1139 0.0105  0.0689  448  CYS B N   
12318 C CA  . CYS B 450  ? 0.3331 0.4390 0.2343 -0.1059 0.0138  0.0646  448  CYS B CA  
12319 C C   . CYS B 450  ? 0.3274 0.4232 0.2257 -0.0984 0.0125  0.0611  448  CYS B C   
12320 O O   . CYS B 450  ? 0.3465 0.4294 0.2375 -0.0996 0.0097  0.0623  448  CYS B O   
12321 C CB  . CYS B 450  ? 0.3506 0.4752 0.2530 -0.1068 0.0188  0.0662  448  CYS B CB  
12322 S SG  . CYS B 450  ? 0.3837 0.5081 0.2765 -0.1066 0.0204  0.0682  448  CYS B SG  
12323 N N   . LEU B 451  ? 0.3407 0.4425 0.2446 -0.0907 0.0145  0.0566  449  LEU B N   
12324 C CA  . LEU B 451  ? 0.3600 0.4542 0.2622 -0.0833 0.0136  0.0529  449  LEU B CA  
12325 C C   . LEU B 451  ? 0.3734 0.4751 0.2711 -0.0812 0.0167  0.0532  449  LEU B C   
12326 O O   . LEU B 451  ? 0.3837 0.5005 0.2836 -0.0814 0.0207  0.0539  449  LEU B O   
12327 C CB  . LEU B 451  ? 0.3759 0.4723 0.2862 -0.0763 0.0141  0.0480  449  LEU B CB  
12328 C CG  . LEU B 451  ? 0.4866 0.5747 0.3964 -0.0686 0.0128  0.0438  449  LEU B CG  
12329 C CD1 . LEU B 451  ? 0.4888 0.5598 0.3944 -0.0696 0.0081  0.0440  449  LEU B CD1 
12330 C CD2 . LEU B 451  ? 0.4682 0.5608 0.3863 -0.0628 0.0139  0.0396  449  LEU B CD2 
12331 N N   . HIS B 452  ? 0.3416 0.4327 0.2326 -0.0790 0.0147  0.0527  450  HIS B N   
12332 C CA  . HIS B 452  ? 0.4555 0.5521 0.3416 -0.0761 0.0173  0.0524  450  HIS B CA  
12333 C C   . HIS B 452  ? 0.3352 0.4434 0.2271 -0.0691 0.0208  0.0483  450  HIS B C   
12334 O O   . HIS B 452  ? 0.3588 0.4642 0.2564 -0.0639 0.0199  0.0443  450  HIS B O   
12335 C CB  . HIS B 452  ? 0.3688 0.4511 0.2483 -0.0732 0.0140  0.0513  450  HIS B CB  
12336 C CG  . HIS B 452  ? 0.4035 0.4902 0.2786 -0.0686 0.0162  0.0496  450  HIS B CG  
12337 N ND1 . HIS B 452  ? 0.4103 0.5009 0.2778 -0.0720 0.0178  0.0530  450  HIS B ND1 
12338 C CD2 . HIS B 452  ? 0.3705 0.4583 0.2476 -0.0609 0.0170  0.0450  450  HIS B CD2 
12339 C CE1 . HIS B 452  ? 0.4360 0.5301 0.3009 -0.0664 0.0196  0.0503  450  HIS B CE1 
12340 N NE2 . HIS B 452  ? 0.4201 0.5124 0.2906 -0.0596 0.0191  0.0454  450  HIS B NE2 
12341 N N   . GLY B 453  ? 0.4142 0.5354 0.3042 -0.0689 0.0249  0.0492  451  GLY B N   
12342 C CA  . GLY B 453  ? 0.4796 0.6114 0.3737 -0.0617 0.0282  0.0453  451  GLY B CA  
12343 C C   . GLY B 453  ? 0.6116 0.7523 0.5152 -0.0602 0.0297  0.0436  451  GLY B C   
12344 O O   . GLY B 453  ? 0.6910 0.8359 0.5988 -0.0532 0.0312  0.0395  451  GLY B O   
12345 N N   . MET B 454  ? 0.4917 0.6346 0.3986 -0.0666 0.0291  0.0467  452  MET B N   
12346 C CA  . MET B 454  ? 0.4247 0.5769 0.3405 -0.0660 0.0304  0.0457  452  MET B CA  
12347 C C   . MET B 454  ? 0.4831 0.6451 0.3998 -0.0742 0.0318  0.0504  452  MET B C   
12348 O O   . MET B 454  ? 0.5036 0.6813 0.4255 -0.0741 0.0351  0.0507  452  MET B O   
12349 C CB  . MET B 454  ? 0.3839 0.5244 0.3041 -0.0643 0.0268  0.0433  452  MET B CB  
12350 C CG  . MET B 454  ? 0.4699 0.6188 0.3987 -0.0645 0.0277  0.0426  452  MET B CG  
12351 S SD  . MET B 454  ? 0.6993 0.8622 0.6338 -0.0559 0.0317  0.0385  452  MET B SD  
12352 C CE  . MET B 454  ? 0.5305 0.6799 0.4619 -0.0479 0.0298  0.0338  452  MET B CE  
12353 N N   . GLY B 455  ? 0.4198 0.5726 0.3314 -0.0815 0.0290  0.0543  453  GLY B N   
12354 C CA  . GLY B 455  ? 0.3546 0.5142 0.2665 -0.0903 0.0295  0.0591  453  GLY B CA  
12355 C C   . GLY B 455  ? 0.4731 0.6427 0.3797 -0.0949 0.0325  0.0631  453  GLY B C   
12356 O O   . GLY B 455  ? 0.4659 0.6442 0.3736 -0.1023 0.0336  0.0672  453  GLY B O   
12357 N N   . GLU B 456  ? 0.5568 0.7256 0.4575 -0.0911 0.0339  0.0622  454  GLU B N   
12358 C CA  . GLU B 456  ? 0.5496 0.7276 0.4444 -0.0955 0.0368  0.0662  454  GLU B CA  
12359 C C   . GLU B 456  ? 0.4386 0.6383 0.3388 -0.0961 0.0418  0.0671  454  GLU B C   
12360 O O   . GLU B 456  ? 0.4973 0.7053 0.3955 -0.1039 0.0433  0.0720  454  GLU B O   
12361 C CB  . GLU B 456  ? 0.5814 0.7543 0.4688 -0.0903 0.0373  0.0645  454  GLU B CB  
12362 C CG  . GLU B 456  ? 0.6678 0.8208 0.5477 -0.0918 0.0326  0.0652  454  GLU B CG  
12363 C CD  . GLU B 456  ? 0.6211 0.7618 0.5038 -0.0846 0.0296  0.0601  454  GLU B CD  
12364 O OE1 . GLU B 456  ? 0.6135 0.7580 0.5044 -0.0811 0.0299  0.0571  454  GLU B OE1 
12365 O OE2 . GLU B 456  ? 0.4630 0.5906 0.3395 -0.0824 0.0269  0.0592  454  GLU B OE2 
12366 N N   . PRO B 457  ? 0.4318 0.6416 0.3387 -0.0885 0.0444  0.0629  455  PRO B N   
12367 C CA  . PRO B 457  ? 0.5037 0.7350 0.4160 -0.0892 0.0490  0.0640  455  PRO B CA  
12368 C C   . PRO B 457  ? 0.4909 0.7275 0.4086 -0.0974 0.0480  0.0677  455  PRO B C   
12369 O O   . PRO B 457  ? 0.5624 0.8101 0.4827 -0.1004 0.0495  0.0697  455  PRO B O   
12370 C CB  . PRO B 457  ? 0.4765 0.7126 0.3956 -0.0793 0.0504  0.0584  455  PRO B CB  
12371 C CG  . PRO B 457  ? 0.5182 0.7390 0.4324 -0.0728 0.0482  0.0546  455  PRO B CG  
12372 C CD  . PRO B 457  ? 0.5134 0.7164 0.4224 -0.0787 0.0436  0.0570  455  PRO B CD  
12373 N N   . LEU B 458  ? 0.5175 0.7442 0.4376 -0.1003 0.0445  0.0678  456  LEU B N   
12374 C CA  . LEU B 458  ? 0.4427 0.6733 0.3670 -0.1085 0.0432  0.0713  456  LEU B CA  
12375 C C   . LEU B 458  ? 0.4329 0.6557 0.3505 -0.1173 0.0409  0.0760  456  LEU B C   
12376 O O   . LEU B 458  ? 0.4421 0.6735 0.3622 -0.1225 0.0412  0.0787  456  LEU B O   
12377 C CB  . LEU B 458  ? 0.4089 0.6297 0.3379 -0.1081 0.0396  0.0693  456  LEU B CB  
12378 C CG  . LEU B 458  ? 0.4581 0.6798 0.3903 -0.1169 0.0375  0.0727  456  LEU B CG  
12379 C CD1 . LEU B 458  ? 0.4360 0.6761 0.3755 -0.1183 0.0398  0.0735  456  LEU B CD1 
12380 C CD2 . LEU B 458  ? 0.4119 0.6232 0.3490 -0.1141 0.0340  0.0694  456  LEU B CD2 
12381 N N   . TYR B 459  ? 0.4244 0.6307 0.3331 -0.1190 0.0383  0.0772  457  TYR B N   
12382 C CA  . TYR B 459  ? 0.4156 0.6122 0.3178 -0.1275 0.0354  0.0817  457  TYR B CA  
12383 C C   . TYR B 459  ? 0.4229 0.6247 0.3203 -0.1286 0.0374  0.0837  457  TYR B C   
12384 O O   . TYR B 459  ? 0.4381 0.6350 0.3313 -0.1360 0.0354  0.0877  457  TYR B O   
12385 C CB  . TYR B 459  ? 0.4184 0.5935 0.3142 -0.1280 0.0308  0.0816  457  TYR B CB  
12386 C CG  . TYR B 459  ? 0.3912 0.5594 0.2926 -0.1295 0.0275  0.0804  457  TYR B CG  
12387 C CD1 . TYR B 459  ? 0.4110 0.5772 0.3116 -0.1392 0.0253  0.0847  457  TYR B CD1 
12388 C CD2 . TYR B 459  ? 0.4275 0.5919 0.3349 -0.1215 0.0266  0.0751  457  TYR B CD2 
12389 C CE1 . TYR B 459  ? 0.4189 0.5791 0.3243 -0.1406 0.0223  0.0836  457  TYR B CE1 
12390 C CE2 . TYR B 459  ? 0.4020 0.5607 0.3145 -0.1230 0.0236  0.0741  457  TYR B CE2 
12391 C CZ  . TYR B 459  ? 0.3614 0.5178 0.2726 -0.1324 0.0215  0.0783  457  TYR B CZ  
12392 O OH  . TYR B 459  ? 0.3642 0.5147 0.2798 -0.1340 0.0185  0.0772  457  TYR B OH  
12393 N N   . GLU B 460  ? 0.4160 0.6276 0.3140 -0.1213 0.0412  0.0810  458  GLU B N   
12394 C CA  . GLU B 460  ? 0.5867 0.8078 0.4825 -0.1222 0.0439  0.0826  458  GLU B CA  
12395 C C   . GLU B 460  ? 0.5813 0.8145 0.4832 -0.1283 0.0444  0.0853  458  GLU B C   
12396 O O   . GLU B 460  ? 0.5503 0.7869 0.4489 -0.1330 0.0450  0.0885  458  GLU B O   
12397 C CB  . GLU B 460  ? 0.5460 0.7781 0.4435 -0.1127 0.0481  0.0786  458  GLU B CB  
12398 C CG  . GLU B 460  ? 0.6268 0.8489 0.5155 -0.1077 0.0481  0.0769  458  GLU B CG  
12399 C CD  . GLU B 460  ? 0.7672 0.9987 0.6584 -0.0977 0.0516  0.0720  458  GLU B CD  
12400 O OE1 . GLU B 460  ? 0.7635 1.0103 0.6626 -0.0949 0.0545  0.0706  458  GLU B OE1 
12401 O OE2 . GLU B 460  ? 0.8805 1.1036 0.7657 -0.0924 0.0513  0.0696  458  GLU B OE2 
12402 N N   . GLU B 461  ? 0.5296 0.7693 0.4402 -0.1283 0.0441  0.0841  459  GLU B N   
12403 C CA  . GLU B 461  ? 0.5313 0.7832 0.4485 -0.1336 0.0443  0.0861  459  GLU B CA  
12404 C C   . GLU B 461  ? 0.5940 0.8355 0.5096 -0.1431 0.0399  0.0897  459  GLU B C   
12405 O O   . GLU B 461  ? 0.5432 0.7934 0.4644 -0.1478 0.0393  0.0912  459  GLU B O   
12406 C CB  . GLU B 461  ? 0.5195 0.7844 0.4469 -0.1279 0.0461  0.0826  459  GLU B CB  
12407 C CG  . GLU B 461  ? 0.4464 0.7194 0.3753 -0.1175 0.0500  0.0784  459  GLU B CG  
12408 C CD  . GLU B 461  ? 0.5841 0.8677 0.5108 -0.1165 0.0532  0.0793  459  GLU B CD  
12409 O OE1 . GLU B 461  ? 0.6133 0.9042 0.5411 -0.1229 0.0532  0.0828  459  GLU B OE1 
12410 O OE2 . GLU B 461  ? 0.5757 0.8602 0.4991 -0.1092 0.0557  0.0766  459  GLU B OE2 
12411 N N   . VAL B 462  ? 0.4490 0.6720 0.3569 -0.1458 0.0365  0.0910  460  VAL B N   
12412 C CA  . VAL B 462  ? 0.5377 0.7482 0.4430 -0.1542 0.0319  0.0940  460  VAL B CA  
12413 C C   . VAL B 462  ? 0.6000 0.7984 0.4951 -0.1593 0.0300  0.0976  460  VAL B C   
12414 O O   . VAL B 462  ? 0.5559 0.7496 0.4485 -0.1674 0.0272  0.1011  460  VAL B O   
12415 C CB  . VAL B 462  ? 0.4398 0.6376 0.3457 -0.1524 0.0291  0.0919  460  VAL B CB  
12416 C CG1 . VAL B 462  ? 0.4759 0.6596 0.3784 -0.1607 0.0241  0.0948  460  VAL B CG1 
12417 C CG2 . VAL B 462  ? 0.4179 0.6280 0.3339 -0.1471 0.0311  0.0883  460  VAL B CG2 
12418 N N   . VAL B 463  ? 0.5096 0.7021 0.3984 -0.1544 0.0311  0.0965  461  VAL B N   
12419 C CA  . VAL B 463  ? 0.4398 0.6205 0.3185 -0.1582 0.0293  0.0997  461  VAL B CA  
12420 C C   . VAL B 463  ? 0.4844 0.6787 0.3626 -0.1592 0.0328  0.1015  461  VAL B C   
12421 O O   . VAL B 463  ? 0.5704 0.7792 0.4528 -0.1531 0.0371  0.0990  461  VAL B O   
12422 C CB  . VAL B 463  ? 0.4387 0.6063 0.3103 -0.1524 0.0285  0.0978  461  VAL B CB  
12423 C CG1 . VAL B 463  ? 0.5175 0.6722 0.3784 -0.1562 0.0263  0.1011  461  VAL B CG1 
12424 C CG2 . VAL B 463  ? 0.4121 0.5674 0.2849 -0.1510 0.0253  0.0958  461  VAL B CG2 
12425 N N   . GLY B 464  ? 0.5714 0.7611 0.4445 -0.1670 0.0308  0.1057  462  GLY B N   
12426 C CA  . GLY B 464  ? 0.5069 0.7081 0.3785 -0.1690 0.0338  0.1080  462  GLY B CA  
12427 C C   . GLY B 464  ? 0.6445 0.8565 0.5214 -0.1763 0.0336  0.1107  462  GLY B C   
12428 O O   . GLY B 464  ? 0.6167 0.8348 0.5014 -0.1768 0.0331  0.1095  462  GLY B O   
12429 N N   . ARG B 465  ? 0.6553 0.8695 0.5276 -0.1820 0.0339  0.1145  463  ARG B N   
12430 C CA  . ARG B 465  ? 0.5792 0.8042 0.4559 -0.1893 0.0337  0.1174  463  ARG B CA  
12431 C C   . ARG B 465  ? 0.6651 0.9125 0.5520 -0.1850 0.0380  0.1151  463  ARG B C   
12432 O O   . ARG B 465  ? 0.7251 0.9818 0.6183 -0.1894 0.0373  0.1161  463  ARG B O   
12433 C CB  . ARG B 465  ? 0.7393 0.9631 0.6088 -0.1957 0.0335  0.1219  463  ARG B CB  
12434 N N   . GLY B 466  ? 0.6005 0.8564 0.4888 -0.1764 0.0421  0.1120  464  GLY B N   
12435 C CA  . GLY B 466  ? 0.6114 0.8874 0.5089 -0.1710 0.0461  0.1093  464  GLY B CA  
12436 C C   . GLY B 466  ? 0.6538 0.9324 0.5596 -0.1671 0.0454  0.1059  464  GLY B C   
12437 O O   . GLY B 466  ? 0.6358 0.9303 0.5493 -0.1617 0.0485  0.1033  464  GLY B O   
12438 N N   . LYS B 467  ? 0.6938 0.9568 0.5979 -0.1695 0.0414  0.1057  465  LYS B N   
12439 C CA  . LYS B 467  ? 0.6895 0.9533 0.6009 -0.1665 0.0403  0.1028  465  LYS B CA  
12440 C C   . LYS B 467  ? 0.6900 0.9444 0.6013 -0.1750 0.0355  0.1053  465  LYS B C   
12441 O O   . LYS B 467  ? 0.6688 0.9253 0.5786 -0.1829 0.0341  0.1090  465  LYS B O   
12442 C CB  . LYS B 467  ? 0.7062 0.9591 0.6155 -0.1590 0.0402  0.0991  465  LYS B CB  
12443 C CG  . LYS B 467  ? 0.6421 0.8971 0.5472 -0.1518 0.0437  0.0972  465  LYS B CG  
12444 C CD  . LYS B 467  ? 0.6688 0.9433 0.5813 -0.1448 0.0482  0.0942  465  LYS B CD  
12445 C CE  . LYS B 467  ? 0.6959 0.9713 0.6037 -0.1372 0.0514  0.0920  465  LYS B CE  
12446 N NZ  . LYS B 467  ? 0.7280 1.0211 0.6426 -0.1296 0.0557  0.0886  465  LYS B NZ  
12447 N N   . LEU B 468  ? 0.6440 0.8879 0.5567 -0.1734 0.0329  0.1032  466  LEU B N   
12448 C CA  . LEU B 468  ? 0.4482 0.6767 0.3572 -0.1809 0.0278  0.1055  466  LEU B CA  
12449 C C   . LEU B 468  ? 0.5266 0.7380 0.4247 -0.1838 0.0257  0.1078  466  LEU B C   
12450 O O   . LEU B 468  ? 0.6047 0.8150 0.4985 -0.1789 0.0280  0.1070  466  LEU B O   
12451 C CB  . LEU B 468  ? 0.5112 0.7323 0.4239 -0.1777 0.0259  0.1024  466  LEU B CB  
12452 C CG  . LEU B 468  ? 0.5806 0.8182 0.5035 -0.1710 0.0290  0.0988  466  LEU B CG  
12453 C CD1 . LEU B 468  ? 0.5821 0.8116 0.5081 -0.1676 0.0272  0.0958  466  LEU B CD1 
12454 C CD2 . LEU B 468  ? 0.5840 0.8379 0.5135 -0.1752 0.0297  0.1003  466  LEU B CD2 
12455 N N   . ASP B 469  ? 0.6020 0.7998 0.4949 -0.1916 0.0212  0.1108  467  ASP B N   
12456 C CA  . ASP B 469  ? 0.6248 0.8065 0.5071 -0.1934 0.0192  0.1129  467  ASP B CA  
12457 C C   . ASP B 469  ? 0.5069 0.6680 0.3847 -0.1929 0.0149  0.1119  467  ASP B C   
12458 O O   . ASP B 469  ? 0.5150 0.6611 0.3866 -0.1992 0.0104  0.1144  467  ASP B O   
12459 C CB  . ASP B 469  ? 0.6557 0.8360 0.5328 -0.2023 0.0175  0.1176  467  ASP B CB  
12460 C CG  . ASP B 469  ? 0.7602 0.9313 0.6276 -0.2023 0.0176  0.1196  467  ASP B CG  
12461 O OD1 . ASP B 469  ? 0.7982 0.9781 0.6658 -0.1964 0.0218  0.1182  467  ASP B OD1 
12462 O OD2 . ASP B 469  ? 0.8573 1.0123 0.7168 -0.2080 0.0135  0.1224  467  ASP B OD2 
12463 N N   . ARG B 470  ? 0.5481 0.7082 0.4287 -0.1853 0.0162  0.1081  468  ARG B N   
12464 C CA  . ARG B 470  ? 0.5776 0.7208 0.4560 -0.1840 0.0125  0.1066  468  ARG B CA  
12465 C C   . ARG B 470  ? 0.4520 0.5865 0.3252 -0.1771 0.0133  0.1047  468  ARG B C   
12466 O O   . ARG B 470  ? 0.4662 0.6122 0.3425 -0.1703 0.0175  0.1023  468  ARG B O   
12467 C CB  . ARG B 470  ? 0.5419 0.6926 0.4297 -0.1817 0.0129  0.1037  468  ARG B CB  
12468 C CG  . ARG B 470  ? 0.4728 0.6321 0.3658 -0.1884 0.0118  0.1054  468  ARG B CG  
12469 C CD  . ARG B 470  ? 0.4725 0.6155 0.3580 -0.1967 0.0066  0.1087  468  ARG B CD  
12470 N NE  . ARG B 470  ? 0.5142 0.6641 0.4036 -0.2036 0.0051  0.1104  468  ARG B NE  
12471 C CZ  . ARG B 470  ? 0.6150 0.7696 0.5020 -0.2102 0.0048  0.1139  468  ARG B CZ  
12472 N NH1 . ARG B 470  ? 0.6333 0.7868 0.5142 -0.2109 0.0060  0.1162  468  ARG B NH1 
12473 N NH2 . ARG B 470  ? 0.5894 0.7499 0.4799 -0.2162 0.0030  0.1153  468  ARG B NH2 
12474 N N   . PRO B 471  ? 0.4842 0.5984 0.3492 -0.1782 0.0092  0.1055  469  PRO B N   
12475 C CA  . PRO B 471  ? 0.4183 0.5236 0.2777 -0.1718 0.0094  0.1039  469  PRO B CA  
12476 C C   . PRO B 471  ? 0.5037 0.6095 0.3681 -0.1651 0.0102  0.0999  469  PRO B C   
12477 O O   . PRO B 471  ? 0.4351 0.5421 0.3055 -0.1661 0.0092  0.0987  469  PRO B O   
12478 C CB  . PRO B 471  ? 0.4831 0.5663 0.3325 -0.1759 0.0040  0.1063  469  PRO B CB  
12479 C CG  . PRO B 471  ? 0.5236 0.6020 0.3757 -0.1820 0.0006  0.1074  469  PRO B CG  
12480 C CD  . PRO B 471  ? 0.5218 0.6200 0.3818 -0.1852 0.0038  0.1080  469  PRO B CD  
12481 N N   . CYS B 472  ? 0.4460 0.5509 0.3076 -0.1581 0.0120  0.0977  470  CYS B N   
12482 C CA  . CYS B 472  ? 0.4069 0.5096 0.2741 -0.1493 0.0119  0.0922  470  CYS B CA  
12483 C C   . CYS B 472  ? 0.4644 0.5506 0.3254 -0.1435 0.0089  0.0899  470  CYS B C   
12484 O O   . CYS B 472  ? 0.4357 0.5219 0.2903 -0.1424 0.0102  0.0912  470  CYS B O   
12485 C CB  . CYS B 472  ? 0.4422 0.5642 0.3172 -0.1430 0.0171  0.0890  470  CYS B CB  
12486 S SG  . CYS B 472  ? 0.4478 0.5665 0.3311 -0.1318 0.0165  0.0816  470  CYS B SG  
12487 N N   . ARG B 473  ? 0.4369 0.5094 0.2998 -0.1397 0.0051  0.0867  471  ARG B N   
12488 C CA  . ARG B 473  ? 0.4200 0.4780 0.2787 -0.1331 0.0023  0.0838  471  ARG B CA  
12489 C C   . ARG B 473  ? 0.4389 0.5032 0.3049 -0.1232 0.0045  0.0779  471  ARG B C   
12490 O O   . ARG B 473  ? 0.4030 0.4721 0.2774 -0.1207 0.0050  0.0750  471  ARG B O   
12491 C CB  . ARG B 473  ? 0.3609 0.3998 0.2169 -0.1345 -0.0033 0.0836  471  ARG B CB  
12492 C CG  . ARG B 473  ? 0.4131 0.4371 0.2642 -0.1282 -0.0065 0.0812  471  ARG B CG  
12493 C CD  . ARG B 473  ? 0.3608 0.3659 0.2075 -0.1304 -0.0121 0.0820  471  ARG B CD  
12494 N NE  . ARG B 473  ? 0.4113 0.4124 0.2518 -0.1403 -0.0136 0.0876  471  ARG B NE  
12495 C CZ  . ARG B 473  ? 0.4335 0.4268 0.2640 -0.1448 -0.0153 0.0919  471  ARG B CZ  
12496 N NH1 . ARG B 473  ? 0.4330 0.4214 0.2583 -0.1403 -0.0157 0.0912  471  ARG B NH1 
12497 N NH2 . ARG B 473  ? 0.4566 0.4468 0.2821 -0.1543 -0.0167 0.0970  471  ARG B NH2 
12498 N N   . ILE B 474  ? 0.4170 0.4811 0.2796 -0.1178 0.0056  0.0763  472  ILE B N   
12499 C CA  . ILE B 474  ? 0.3607 0.4301 0.2291 -0.1085 0.0075  0.0709  472  ILE B CA  
12500 C C   . ILE B 474  ? 0.3938 0.4471 0.2619 -0.1031 0.0033  0.0674  472  ILE B C   
12501 O O   . ILE B 474  ? 0.3950 0.4358 0.2558 -0.1032 0.0003  0.0684  472  ILE B O   
12502 C CB  . ILE B 474  ? 0.3914 0.4693 0.2560 -0.1054 0.0110  0.0707  472  ILE B CB  
12503 C CG1 . ILE B 474  ? 0.4315 0.5266 0.2967 -0.1106 0.0154  0.0742  472  ILE B CG1 
12504 C CG2 . ILE B 474  ? 0.4070 0.4887 0.2768 -0.0959 0.0125  0.0650  472  ILE B CG2 
12505 C CD1 . ILE B 474  ? 0.4010 0.5034 0.2603 -0.1090 0.0186  0.0750  472  ILE B CD1 
12506 N N   . TYR B 475  ? 0.3436 0.3977 0.2199 -0.0985 0.0031  0.0633  473  TYR B N   
12507 C CA  . TYR B 475  ? 0.3317 0.3736 0.2095 -0.0923 -0.0001 0.0594  473  TYR B CA  
12508 C C   . TYR B 475  ? 0.3641 0.4090 0.2416 -0.0850 0.0015  0.0560  473  TYR B C   
12509 O O   . TYR B 475  ? 0.3808 0.4377 0.2638 -0.0810 0.0051  0.0535  473  TYR B O   
12510 C CB  . TYR B 475  ? 0.3430 0.3863 0.2295 -0.0904 -0.0005 0.0566  473  TYR B CB  
12511 C CG  . TYR B 475  ? 0.3558 0.3870 0.2446 -0.0850 -0.0039 0.0528  473  TYR B CG  
12512 C CD1 . TYR B 475  ? 0.3825 0.4000 0.2686 -0.0877 -0.0081 0.0538  473  TYR B CD1 
12513 C CD2 . TYR B 475  ? 0.4786 0.5123 0.3722 -0.0773 -0.0028 0.0482  473  TYR B CD2 
12514 C CE1 . TYR B 475  ? 0.3339 0.3414 0.2226 -0.0826 -0.0110 0.0503  473  TYR B CE1 
12515 C CE2 . TYR B 475  ? 0.5100 0.5338 0.4062 -0.0727 -0.0057 0.0449  473  TYR B CE2 
12516 C CZ  . TYR B 475  ? 0.4820 0.4931 0.3758 -0.0753 -0.0097 0.0460  473  TYR B CZ  
12517 O OH  . TYR B 475  ? 0.4599 0.4619 0.3564 -0.0705 -0.0123 0.0428  473  TYR B OH  
12518 N N   . ALA B 476  ? 0.3333 0.3674 0.2040 -0.0833 -0.0011 0.0561  474  ALA B N   
12519 C CA  . ALA B 476  ? 0.3976 0.4345 0.2656 -0.0780 0.0004  0.0540  474  ALA B CA  
12520 C C   . ALA B 476  ? 0.3711 0.3980 0.2409 -0.0712 -0.0025 0.0497  474  ALA B C   
12521 O O   . ALA B 476  ? 0.3671 0.3810 0.2321 -0.0715 -0.0065 0.0505  474  ALA B O   
12522 C CB  . ALA B 476  ? 0.3825 0.4164 0.2405 -0.0819 0.0000  0.0580  474  ALA B CB  
12523 N N   . PRO B 477  ? 0.3681 0.4006 0.2448 -0.0651 -0.0008 0.0453  475  PRO B N   
12524 C CA  . PRO B 477  ? 0.3523 0.3761 0.2307 -0.0590 -0.0035 0.0414  475  PRO B CA  
12525 C C   . PRO B 477  ? 0.3622 0.3817 0.2335 -0.0565 -0.0045 0.0411  475  PRO B C   
12526 O O   . PRO B 477  ? 0.3932 0.4205 0.2606 -0.0567 -0.0017 0.0420  475  PRO B O   
12527 C CB  . PRO B 477  ? 0.3226 0.3553 0.2092 -0.0538 -0.0008 0.0373  475  PRO B CB  
12528 C CG  . PRO B 477  ? 0.4028 0.4464 0.2934 -0.0577 0.0022  0.0392  475  PRO B CG  
12529 C CD  . PRO B 477  ? 0.3604 0.4070 0.2441 -0.0638 0.0033  0.0438  475  PRO B CD  
12530 N N   . VAL B 478  ? 0.3333 0.3409 0.2029 -0.0539 -0.0085 0.0397  476  VAL B N   
12531 C CA  . VAL B 478  ? 0.3184 0.3206 0.1813 -0.0513 -0.0102 0.0393  476  VAL B CA  
12532 C C   . VAL B 478  ? 0.3560 0.3523 0.2231 -0.0451 -0.0127 0.0349  476  VAL B C   
12533 O O   . VAL B 478  ? 0.4270 0.4156 0.2973 -0.0447 -0.0156 0.0342  476  VAL B O   
12534 C CB  . VAL B 478  ? 0.3529 0.3449 0.2073 -0.0558 -0.0135 0.0434  476  VAL B CB  
12535 C CG1 . VAL B 478  ? 0.4155 0.4026 0.2632 -0.0528 -0.0153 0.0428  476  VAL B CG1 
12536 C CG2 . VAL B 478  ? 0.3766 0.3742 0.2271 -0.0628 -0.0112 0.0481  476  VAL B CG2 
12537 N N   . GLY B 479  ? 0.4005 0.4007 0.2676 -0.0404 -0.0114 0.0318  477  GLY B N   
12538 C CA  . GLY B 479  ? 0.4599 0.4547 0.3307 -0.0349 -0.0138 0.0278  477  GLY B CA  
12539 C C   . GLY B 479  ? 0.4719 0.4730 0.3435 -0.0301 -0.0117 0.0243  477  GLY B C   
12540 O O   . GLY B 479  ? 0.4561 0.4663 0.3258 -0.0304 -0.0080 0.0247  477  GLY B O   
12541 N N   . THR B 480  ? 0.5019 0.4979 0.3763 -0.0255 -0.0141 0.0208  478  THR B N   
12542 C CA  . THR B 480  ? 0.5744 0.5737 0.4492 -0.0206 -0.0130 0.0171  478  THR B CA  
12543 C C   . THR B 480  ? 0.5585 0.5663 0.4406 -0.0185 -0.0097 0.0147  478  THR B C   
12544 O O   . THR B 480  ? 0.5634 0.5741 0.4507 -0.0206 -0.0084 0.0157  478  THR B O   
12545 C CB  . THR B 480  ? 0.5307 0.5215 0.4065 -0.0170 -0.0171 0.0144  478  THR B CB  
12546 O OG1 . THR B 480  ? 0.6543 0.6426 0.5380 -0.0164 -0.0183 0.0132  478  THR B OG1 
12547 C CG2 . THR B 480  ? 0.5328 0.5152 0.4015 -0.0188 -0.0207 0.0168  478  THR B CG2 
12548 N N   . HIS B 481  ? 0.6108 0.6220 0.4929 -0.0141 -0.0083 0.0113  479  HIS B N   
12549 C CA  . HIS B 481  ? 0.5518 0.5702 0.4405 -0.0113 -0.0055 0.0087  479  HIS B CA  
12550 C C   . HIS B 481  ? 0.6289 0.6434 0.5256 -0.0103 -0.0072 0.0072  479  HIS B C   
12551 O O   . HIS B 481  ? 0.5596 0.5792 0.4621 -0.0109 -0.0052 0.0072  479  HIS B O   
12552 C CB  . HIS B 481  ? 0.5081 0.5285 0.3945 -0.0064 -0.0046 0.0051  479  HIS B CB  
12553 C CG  . HIS B 481  ? 0.6337 0.6594 0.5125 -0.0068 -0.0022 0.0063  479  HIS B CG  
12554 N ND1 . HIS B 481  ? 0.7179 0.7453 0.5929 -0.0025 -0.0013 0.0033  479  HIS B ND1 
12555 C CD2 . HIS B 481  ? 0.5730 0.6028 0.4470 -0.0109 -0.0005 0.0101  479  HIS B CD2 
12556 C CE1 . HIS B 481  ? 0.7199 0.7526 0.5881 -0.0038 0.0010  0.0051  479  HIS B CE1 
12557 N NE2 . HIS B 481  ? 0.7088 0.7432 0.5764 -0.0090 0.0016  0.0094  479  HIS B NE2 
12558 N N   . GLU B 482  ? 0.6066 0.6123 0.5036 -0.0089 -0.0110 0.0058  480  GLU B N   
12559 C CA  . GLU B 482  ? 0.5468 0.5491 0.4512 -0.0079 -0.0127 0.0044  480  GLU B CA  
12560 C C   . GLU B 482  ? 0.5300 0.5317 0.4370 -0.0119 -0.0127 0.0073  480  GLU B C   
12561 O O   . GLU B 482  ? 0.6420 0.6466 0.5554 -0.0118 -0.0116 0.0066  480  GLU B O   
12562 C CB  . GLU B 482  ? 0.6410 0.6347 0.5450 -0.0059 -0.0169 0.0027  480  GLU B CB  
12563 N N   . THR B 483  ? 0.6072 0.6050 0.5087 -0.0155 -0.0142 0.0105  481  THR B N   
12564 C CA  . THR B 483  ? 0.6889 0.6851 0.5919 -0.0196 -0.0146 0.0133  481  THR B CA  
12565 C C   . THR B 483  ? 0.6519 0.6574 0.5577 -0.0218 -0.0107 0.0145  481  THR B C   
12566 O O   . THR B 483  ? 0.5997 0.6058 0.5107 -0.0233 -0.0105 0.0149  481  THR B O   
12567 C CB  . THR B 483  ? 0.6729 0.6630 0.5684 -0.0232 -0.0168 0.0168  481  THR B CB  
12568 N N   . LEU B 484  ? 0.6164 0.6297 0.5190 -0.0220 -0.0077 0.0150  482  LEU B N   
12569 C CA  . LEU B 484  ? 0.6276 0.6506 0.5328 -0.0244 -0.0040 0.0165  482  LEU B CA  
12570 C C   . LEU B 484  ? 0.5708 0.5992 0.4838 -0.0209 -0.0022 0.0135  482  LEU B C   
12571 O O   . LEU B 484  ? 0.5430 0.5760 0.4606 -0.0229 -0.0008 0.0144  482  LEU B O   
12572 C CB  . LEU B 484  ? 0.5413 0.5718 0.4408 -0.0255 -0.0011 0.0181  482  LEU B CB  
12573 C CG  . LEU B 484  ? 0.5787 0.6158 0.4776 -0.0207 0.0014  0.0151  482  LEU B CG  
12574 C CD1 . LEU B 484  ? 0.5849 0.6331 0.4894 -0.0196 0.0052  0.0142  482  LEU B CD1 
12575 C CD2 . LEU B 484  ? 0.5902 0.6292 0.4806 -0.0217 0.0024  0.0168  482  LEU B CD2 
12576 N N   . LEU B 485  ? 0.5345 0.5622 0.4488 -0.0159 -0.0024 0.0099  483  LEU B N   
12577 C CA  . LEU B 485  ? 0.6197 0.6520 0.5407 -0.0125 -0.0007 0.0071  483  LEU B CA  
12578 C C   . LEU B 485  ? 0.5817 0.6099 0.5090 -0.0130 -0.0024 0.0067  483  LEU B C   
12579 O O   . LEU B 485  ? 0.5780 0.6109 0.5110 -0.0115 -0.0007 0.0053  483  LEU B O   
12580 C CB  . LEU B 485  ? 0.6433 0.6740 0.5636 -0.0072 -0.0010 0.0034  483  LEU B CB  
12581 C CG  . LEU B 485  ? 0.5917 0.6289 0.5072 -0.0052 0.0017  0.0027  483  LEU B CG  
12582 C CD1 . LEU B 485  ? 0.5718 0.6049 0.4856 -0.0004 0.0004  -0.0009 483  LEU B CD1 
12583 C CD2 . LEU B 485  ? 0.5241 0.5721 0.4433 -0.0046 0.0056  0.0027  483  LEU B CD2 
12584 N N   . ALA B 486  ? 0.5993 0.6188 0.5254 -0.0149 -0.0056 0.0078  484  ALA B N   
12585 C CA  . ALA B 486  ? 0.5435 0.5584 0.4752 -0.0147 -0.0075 0.0070  484  ALA B CA  
12586 C C   . ALA B 486  ? 0.6162 0.6353 0.5517 -0.0177 -0.0060 0.0086  484  ALA B C   
12587 O O   . ALA B 486  ? 0.6453 0.6631 0.5863 -0.0167 -0.0066 0.0074  484  ALA B O   
12588 C CB  . ALA B 486  ? 0.5520 0.5568 0.4808 -0.0157 -0.0114 0.0078  484  ALA B CB  
12589 N N   . TYR B 487  ? 0.5914 0.6157 0.5241 -0.0216 -0.0042 0.0115  485  TYR B N   
12590 C CA  . TYR B 487  ? 0.5478 0.5768 0.4841 -0.0248 -0.0029 0.0131  485  TYR B CA  
12591 C C   . TYR B 487  ? 0.5919 0.6321 0.5275 -0.0265 0.0006  0.0147  485  TYR B C   
12592 O O   . TYR B 487  ? 0.5186 0.5633 0.4558 -0.0304 0.0016  0.0169  485  TYR B O   
12593 C CB  . TYR B 487  ? 0.6220 0.6439 0.5559 -0.0294 -0.0055 0.0159  485  TYR B CB  
12594 N N   . LEU B 488  ? 0.6671 0.7120 0.6002 -0.0236 0.0025  0.0135  486  LEU B N   
12595 C CA  . LEU B 488  ? 0.6083 0.6648 0.5411 -0.0245 0.0062  0.0147  486  LEU B CA  
12596 C C   . LEU B 488  ? 0.5543 0.6188 0.4941 -0.0234 0.0083  0.0137  486  LEU B C   
12597 O O   . LEU B 488  ? 0.4571 0.5312 0.3979 -0.0259 0.0108  0.0156  486  LEU B O   
12598 C CB  . LEU B 488  ? 0.5140 0.5734 0.4430 -0.0206 0.0077  0.0129  486  LEU B CB  
12599 C CG  . LEU B 488  ? 0.6132 0.6851 0.5411 -0.0210 0.0116  0.0140  486  LEU B CG  
12600 C CD1 . LEU B 488  ? 0.6688 0.7433 0.5932 -0.0276 0.0120  0.0185  486  LEU B CD1 
12601 C CD2 . LEU B 488  ? 0.4256 0.4991 0.3490 -0.0167 0.0128  0.0120  486  LEU B CD2 
12602 N N   . VAL B 489  ? 0.5774 0.6383 0.5221 -0.0197 0.0072  0.0108  487  VAL B N   
12603 C CA  . VAL B 489  ? 0.4545 0.5222 0.4056 -0.0185 0.0089  0.0099  487  VAL B CA  
12604 C C   . VAL B 489  ? 0.4512 0.5219 0.4041 -0.0240 0.0089  0.0129  487  VAL B C   
12605 O O   . VAL B 489  ? 0.5687 0.6497 0.5238 -0.0254 0.0114  0.0141  487  VAL B O   
12606 C CB  . VAL B 489  ? 0.4848 0.5464 0.4403 -0.0146 0.0073  0.0068  487  VAL B CB  
12607 C CG1 . VAL B 489  ? 0.5499 0.6174 0.5117 -0.0140 0.0086  0.0064  487  VAL B CG1 
12608 C CG2 . VAL B 489  ? 0.5613 0.6214 0.5153 -0.0092 0.0076  0.0038  487  VAL B CG2 
12609 N N   . ARG B 490  ? 0.5230 0.5846 0.4746 -0.0273 0.0060  0.0142  488  ARG B N   
12610 C CA  . ARG B 490  ? 0.5791 0.6419 0.5317 -0.0327 0.0056  0.0169  488  ARG B CA  
12611 C C   . ARG B 490  ? 0.5383 0.6084 0.4872 -0.0374 0.0074  0.0203  488  ARG B C   
12612 O O   . ARG B 490  ? 0.5190 0.5963 0.4703 -0.0410 0.0086  0.0222  488  ARG B O   
12613 C CB  . ARG B 490  ? 0.5255 0.5760 0.4761 -0.0349 0.0019  0.0176  488  ARG B CB  
12614 C CG  . ARG B 490  ? 0.5045 0.5540 0.4563 -0.0399 0.0008  0.0197  488  ARG B CG  
12615 C CD  . ARG B 490  ? 0.5288 0.5653 0.4776 -0.0415 -0.0029 0.0201  488  ARG B CD  
12616 N NE  . ARG B 490  ? 0.5710 0.6021 0.5128 -0.0435 -0.0042 0.0221  488  ARG B NE  
12617 C CZ  . ARG B 490  ? 0.5803 0.6007 0.5188 -0.0421 -0.0071 0.0215  488  ARG B CZ  
12618 N NH1 . ARG B 490  ? 0.4307 0.4450 0.3725 -0.0386 -0.0089 0.0189  488  ARG B NH1 
12619 N NH2 . ARG B 490  ? 0.5232 0.5394 0.4551 -0.0442 -0.0082 0.0236  488  ARG B NH2 
12620 N N   . ARG B 491  ? 0.4649 0.5339 0.4080 -0.0374 0.0076  0.0211  489  ARG B N   
12621 C CA  . ARG B 491  ? 0.5124 0.5884 0.4515 -0.0419 0.0094  0.0245  489  ARG B CA  
12622 C C   . ARG B 491  ? 0.6725 0.7632 0.6151 -0.0403 0.0134  0.0241  489  ARG B C   
12623 O O   . ARG B 491  ? 0.6462 0.7457 0.5890 -0.0449 0.0151  0.0270  489  ARG B O   
12624 C CB  . ARG B 491  ? 0.5350 0.6059 0.4668 -0.0418 0.0087  0.0252  489  ARG B CB  
12625 N N   . LEU B 492  ? 0.6440 0.7376 0.5893 -0.0339 0.0148  0.0206  490  LEU B N   
12626 C CA  . LEU B 492  ? 0.6175 0.7247 0.5657 -0.0313 0.0185  0.0199  490  LEU B CA  
12627 C C   . LEU B 492  ? 0.6684 0.7827 0.6234 -0.0323 0.0193  0.0201  490  LEU B C   
12628 O O   . LEU B 492  ? 0.5584 0.6854 0.5155 -0.0336 0.0221  0.0215  490  LEU B O   
12629 C CB  . LEU B 492  ? 0.5638 0.6703 0.5120 -0.0239 0.0193  0.0160  490  LEU B CB  
12630 C CG  . LEU B 492  ? 0.6461 0.7479 0.5873 -0.0223 0.0190  0.0154  490  LEU B CG  
12631 C CD1 . LEU B 492  ? 0.5782 0.6753 0.5199 -0.0154 0.0185  0.0112  490  LEU B CD1 
12632 C CD2 . LEU B 492  ? 0.6253 0.7384 0.5632 -0.0235 0.0223  0.0173  490  LEU B CD2 
12633 N N   . LEU B 493  ? 0.6575 0.7644 0.6161 -0.0317 0.0170  0.0188  491  LEU B N   
12634 C CA  . LEU B 493  ? 0.5157 0.6286 0.4804 -0.0329 0.0174  0.0191  491  LEU B CA  
12635 C C   . LEU B 493  ? 0.6628 0.7807 0.6270 -0.0403 0.0175  0.0231  491  LEU B C   
12636 O O   . LEU B 493  ? 0.7657 0.8933 0.7345 -0.0418 0.0189  0.0239  491  LEU B O   
12637 C CB  . LEU B 493  ? 0.5944 0.6974 0.5622 -0.0314 0.0147  0.0172  491  LEU B CB  
12638 C CG  . LEU B 493  ? 0.5944 0.6959 0.5653 -0.0243 0.0151  0.0133  491  LEU B CG  
12639 C CD1 . LEU B 493  ? 0.5326 0.6256 0.5067 -0.0237 0.0126  0.0120  491  LEU B CD1 
12640 C CD2 . LEU B 493  ? 0.5855 0.6998 0.5604 -0.0212 0.0182  0.0125  491  LEU B CD2 
12641 N N   . GLU B 494  ? 0.6885 0.7999 0.6470 -0.0451 0.0160  0.0256  492  GLU B N   
12642 C CA  . GLU B 494  ? 0.6558 0.7697 0.6129 -0.0528 0.0155  0.0296  492  GLU B CA  
12643 C C   . GLU B 494  ? 0.6216 0.7518 0.5805 -0.0549 0.0190  0.0316  492  GLU B C   
12644 O O   . GLU B 494  ? 0.5951 0.7313 0.5567 -0.0600 0.0191  0.0339  492  GLU B O   
12645 C CB  . GLU B 494  ? 0.6059 0.7100 0.5554 -0.0569 0.0135  0.0320  492  GLU B CB  
12646 N N   . ALA B 497  ? 0.6792 0.8367 0.6585 -0.0311 0.0260  0.0203  495  ALA B N   
12647 C CA  . ALA B 497  ? 0.6680 0.8289 0.6536 -0.0295 0.0256  0.0192  495  ALA B CA  
12648 C C   . ALA B 497  ? 0.5702 0.7479 0.5599 -0.0308 0.0283  0.0209  495  ALA B C   
12649 O O   . ALA B 497  ? 0.6999 0.8852 0.6876 -0.0354 0.0297  0.0238  495  ALA B O   
12650 C CB  . ALA B 497  ? 0.4768 0.6280 0.4632 -0.0340 0.0224  0.0202  495  ALA B CB  
12651 N N   . ASN B 498  ? 0.6068 0.7904 0.6022 -0.0270 0.0289  0.0192  496  ASN B N   
12652 C CA  . ASN B 498  ? 0.6162 0.8166 0.6159 -0.0272 0.0314  0.0204  496  ASN B CA  
12653 C C   . ASN B 498  ? 0.6172 0.8232 0.6177 -0.0359 0.0309  0.0244  496  ASN B C   
12654 O O   . ASN B 498  ? 0.5919 0.8115 0.5933 -0.0384 0.0333  0.0266  496  ASN B O   
12655 C CB  . ASN B 498  ? 0.5969 0.8008 0.6024 -0.0220 0.0314  0.0181  496  ASN B CB  
12656 N N   . SER B 499  ? 0.5142 0.7099 0.5143 -0.0406 0.0277  0.0254  497  SER B N   
12657 C CA  . SER B 499  ? 0.4540 0.6531 0.4544 -0.0492 0.0267  0.0290  497  SER B CA  
12658 C C   . SER B 499  ? 0.3919 0.5885 0.3862 -0.0548 0.0268  0.0320  497  SER B C   
12659 O O   . SER B 499  ? 0.4636 0.6638 0.4575 -0.0624 0.0261  0.0354  497  SER B O   
12660 C CB  . SER B 499  ? 0.4389 0.6264 0.4399 -0.0519 0.0231  0.0288  497  SER B CB  
12661 O OG  . SER B 499  ? 0.5278 0.6994 0.5246 -0.0496 0.0212  0.0269  497  SER B OG  
12662 N N   . SER B 500  ? 0.4098 0.5999 0.3991 -0.0516 0.0273  0.0308  498  SER B N   
12663 C CA  . SER B 500  ? 0.4268 0.6125 0.4097 -0.0569 0.0270  0.0336  498  SER B CA  
12664 C C   . SER B 500  ? 0.4527 0.6540 0.4352 -0.0589 0.0305  0.0360  498  SER B C   
12665 O O   . SER B 500  ? 0.5141 0.7265 0.4993 -0.0533 0.0335  0.0343  498  SER B O   
12666 C CB  . SER B 500  ? 0.4786 0.6510 0.4561 -0.0527 0.0260  0.0314  498  SER B CB  
12667 O OG  . SER B 500  ? 0.6325 0.8099 0.6107 -0.0452 0.0284  0.0285  498  SER B OG  
12668 N N   . PHE B 501  ? 0.3923 0.5945 0.3714 -0.0671 0.0300  0.0401  499  PHE B N   
12669 C CA  . PHE B 501  ? 0.4236 0.6410 0.4022 -0.0702 0.0333  0.0430  499  PHE B CA  
12670 C C   . PHE B 501  ? 0.5137 0.7334 0.4883 -0.0646 0.0360  0.0414  499  PHE B C   
12671 O O   . PHE B 501  ? 0.6236 0.8588 0.5999 -0.0630 0.0397  0.0419  499  PHE B O   
12672 C CB  . PHE B 501  ? 0.4094 0.6239 0.3836 -0.0803 0.0318  0.0477  499  PHE B CB  
12673 C CG  . PHE B 501  ? 0.4195 0.6499 0.3930 -0.0848 0.0351  0.0513  499  PHE B CG  
12674 C CD1 . PHE B 501  ? 0.4794 0.7108 0.4470 -0.0837 0.0372  0.0520  499  PHE B CD1 
12675 C CD2 . PHE B 501  ? 0.4161 0.6603 0.3945 -0.0903 0.0360  0.0541  499  PHE B CD2 
12676 C CE1 . PHE B 501  ? 0.4349 0.6814 0.4018 -0.0879 0.0404  0.0554  499  PHE B CE1 
12677 C CE2 . PHE B 501  ? 0.4789 0.7384 0.4569 -0.0948 0.0391  0.0576  499  PHE B CE2 
12678 C CZ  . PHE B 501  ? 0.4851 0.7459 0.4574 -0.0935 0.0414  0.0583  499  PHE B CZ  
12679 N N   . VAL B 502  ? 0.6242 0.8291 0.5936 -0.0616 0.0343  0.0395  500  VAL B N   
12680 C CA  . VAL B 502  ? 0.7345 0.9402 0.6996 -0.0562 0.0364  0.0378  500  VAL B CA  
12681 C C   . VAL B 502  ? 0.7674 0.9828 0.7373 -0.0477 0.0391  0.0342  500  VAL B C   
12682 O O   . VAL B 502  ? 0.8137 1.0419 0.7832 -0.0452 0.0427  0.0342  500  VAL B O   
12683 C CB  . VAL B 502  ? 0.6594 0.8467 0.6188 -0.0543 0.0335  0.0362  500  VAL B CB  
12684 N N   . HIS B 503  ? 0.6422 0.8518 0.6163 -0.0430 0.0374  0.0310  501  HIS B N   
12685 C CA  . HIS B 503  ? 0.6237 0.8412 0.6022 -0.0349 0.0396  0.0276  501  HIS B CA  
12686 C C   . HIS B 503  ? 0.6818 0.9182 0.6660 -0.0359 0.0424  0.0291  501  HIS B C   
12687 O O   . HIS B 503  ? 0.6423 0.8896 0.6281 -0.0300 0.0454  0.0273  501  HIS B O   
12688 C CB  . HIS B 503  ? 0.6953 0.9020 0.6771 -0.0308 0.0369  0.0244  501  HIS B CB  
12689 C CG  . HIS B 503  ? 0.6821 0.8972 0.6694 -0.0239 0.0385  0.0216  501  HIS B CG  
12690 N ND1 . HIS B 503  ? 0.7157 0.9417 0.7095 -0.0252 0.0391  0.0225  501  HIS B ND1 
12691 C CD2 . HIS B 503  ? 0.5843 0.7981 0.5714 -0.0156 0.0395  0.0178  501  HIS B CD2 
12692 C CE1 . HIS B 503  ? 0.6366 0.8676 0.6339 -0.0177 0.0404  0.0195  501  HIS B CE1 
12693 N NE2 . HIS B 503  ? 0.6513 0.8748 0.6445 -0.0118 0.0406  0.0166  501  HIS B NE2 
12694 N N   . ARG B 504  ? 0.5454 0.7859 0.5326 -0.0433 0.0414  0.0324  502  ARG B N   
12695 C CA  . ARG B 504  ? 0.5564 0.8152 0.5498 -0.0445 0.0437  0.0339  502  ARG B CA  
12696 C C   . ARG B 504  ? 0.5660 0.8394 0.5574 -0.0463 0.0474  0.0362  502  ARG B C   
12697 O O   . ARG B 504  ? 0.5715 0.8613 0.5673 -0.0430 0.0504  0.0359  502  ARG B O   
12698 C CB  . ARG B 504  ? 0.4921 0.7504 0.4887 -0.0524 0.0412  0.0367  502  ARG B CB  
12699 C CG  . ARG B 504  ? 0.5606 0.8109 0.5615 -0.0495 0.0385  0.0342  502  ARG B CG  
12700 C CD  . ARG B 504  ? 0.4318 0.6768 0.4338 -0.0575 0.0353  0.0367  502  ARG B CD  
12701 N NE  . ARG B 504  ? 0.4978 0.7583 0.5038 -0.0636 0.0365  0.0401  502  ARG B NE  
12702 C CZ  . ARG B 504  ? 0.4805 0.7542 0.4934 -0.0615 0.0375  0.0396  502  ARG B CZ  
12703 N NH1 . ARG B 504  ? 0.5257 0.7996 0.5422 -0.0532 0.0379  0.0359  502  ARG B NH1 
12704 N NH2 . ARG B 504  ? 0.5157 0.8026 0.5320 -0.0681 0.0381  0.0429  502  ARG B NH2 
12705 N N   . ILE B 505  ? 0.5478 0.8158 0.5325 -0.0514 0.0472  0.0388  503  ILE B N   
12706 C CA  . ILE B 505  ? 0.5504 0.8318 0.5326 -0.0535 0.0508  0.0413  503  ILE B CA  
12707 C C   . ILE B 505  ? 0.5815 0.8695 0.5626 -0.0441 0.0541  0.0378  503  ILE B C   
12708 O O   . ILE B 505  ? 0.5351 0.8371 0.5166 -0.0435 0.0572  0.0388  503  ILE B O   
12709 C CB  . ILE B 505  ? 0.4985 0.7702 0.4728 -0.0605 0.0495  0.0445  503  ILE B CB  
12710 N N   . ASN B 506  ? 0.5530 0.8294 0.5330 -0.0366 0.0527  0.0335  504  ASN B N   
12711 C CA  . ASN B 506  ? 0.6383 0.9186 0.6167 -0.0273 0.0553  0.0298  504  ASN B CA  
12712 C C   . ASN B 506  ? 0.6784 0.9641 0.6634 -0.0198 0.0558  0.0263  504  ASN B C   
12713 O O   . ASN B 506  ? 0.6862 0.9709 0.6697 -0.0113 0.0570  0.0225  504  ASN B O   
12714 C CB  . ASN B 506  ? 0.6376 0.9007 0.6088 -0.0241 0.0535  0.0273  504  ASN B CB  
12715 N N   . ASP B 507  ? 0.6236 0.9142 0.6153 -0.0227 0.0547  0.0275  505  ASP B N   
12716 C CA  . ASP B 507  ? 0.6243 0.9219 0.6224 -0.0159 0.0553  0.0248  505  ASP B CA  
12717 C C   . ASP B 507  ? 0.6717 0.9879 0.6747 -0.0163 0.0576  0.0264  505  ASP B C   
12718 O O   . ASP B 507  ? 0.6253 0.9468 0.6316 -0.0238 0.0565  0.0298  505  ASP B O   
12719 C CB  . ASP B 507  ? 0.5969 0.8857 0.5994 -0.0179 0.0517  0.0245  505  ASP B CB  
12720 N N   . PRO B 508  ? 0.7177 1.0406 0.7209 -0.0085 0.0594  0.0238  506  PRO B N   
12721 C CA  . PRO B 508  ? 0.6999 1.0374 0.7076 -0.0085 0.0603  0.0251  506  PRO B CA  
12722 C C   . PRO B 508  ? 0.7067 1.0505 0.7222 -0.0094 0.0586  0.0256  506  PRO B C   
12723 O O   . PRO B 508  ? 0.6612 1.0171 0.6805 -0.0114 0.0589  0.0275  506  PRO B O   
12724 C CB  . PRO B 508  ? 0.7510 1.0916 0.7569 0.0015  0.0623  0.0214  506  PRO B CB  
12725 C CG  . PRO B 508  ? 0.7332 1.0609 0.7318 0.0046  0.0627  0.0191  506  PRO B CG  
12726 C CD  . PRO B 508  ? 0.6467 0.9636 0.6456 0.0006  0.0606  0.0196  506  PRO B CD  
12727 N N   . LYS B 509  ? 0.6770 1.0129 0.6947 -0.0079 0.0569  0.0241  507  LYS B N   
12728 C CA  . LYS B 509  ? 0.6830 1.0241 0.7077 -0.0087 0.0551  0.0246  507  LYS B CA  
12729 C C   . LYS B 509  ? 0.7571 1.1001 0.7837 -0.0195 0.0534  0.0288  507  LYS B C   
12730 O O   . LYS B 509  ? 0.7768 1.1279 0.8088 -0.0216 0.0522  0.0301  507  LYS B O   
12731 C CB  . LYS B 509  ? 0.5993 0.9310 0.6254 -0.0038 0.0537  0.0216  507  LYS B CB  
12732 N N   . VAL B 510  ? 0.7033 1.0387 0.7251 -0.0264 0.0531  0.0311  508  VAL B N   
12733 C CA  . VAL B 510  ? 0.6870 1.0219 0.7096 -0.0370 0.0511  0.0351  508  VAL B CA  
12734 C C   . VAL B 510  ? 0.6610 1.0058 0.6825 -0.0418 0.0522  0.0382  508  VAL B C   
12735 O O   . VAL B 510  ? 0.7485 1.0938 0.7654 -0.0403 0.0542  0.0381  508  VAL B O   
12736 C CB  . VAL B 510  ? 0.5938 0.9143 0.6111 -0.0421 0.0499  0.0362  508  VAL B CB  
12737 N N   . SER B 511  ? 0.6029 0.9555 0.6287 -0.0477 0.0507  0.0408  509  SER B N   
12738 C CA  . SER B 511  ? 0.6390 1.0020 0.6645 -0.0527 0.0515  0.0438  509  SER B CA  
12739 C C   . SER B 511  ? 0.6346 0.9904 0.6557 -0.0632 0.0500  0.0478  509  SER B C   
12740 O O   . SER B 511  ? 0.6552 0.9992 0.6745 -0.0674 0.0478  0.0484  509  SER B O   
12741 C CB  . SER B 511  ? 0.6745 1.0504 0.7067 -0.0534 0.0506  0.0447  509  SER B CB  
12742 O OG  . SER B 511  ? 0.6250 0.9977 0.6587 -0.0621 0.0476  0.0474  509  SER B OG  
12743 N N   . ILE B 512  ? 0.5677 0.9307 0.5867 -0.0675 0.0511  0.0505  510  ILE B N   
12744 C CA  . ILE B 512  ? 0.5990 0.9561 0.6139 -0.0780 0.0494  0.0546  510  ILE B CA  
12745 C C   . ILE B 512  ? 0.6007 0.9567 0.6192 -0.0849 0.0460  0.0565  510  ILE B C   
12746 O O   . ILE B 512  ? 0.5263 0.8711 0.5413 -0.0923 0.0436  0.0587  510  ILE B O   
12747 C CB  . ILE B 512  ? 0.4898 0.8566 0.5026 -0.0812 0.0512  0.0572  510  ILE B CB  
12748 N N   . ASP B 513  ? 0.5991 0.9664 0.6244 -0.0823 0.0457  0.0556  511  ASP B N   
12749 C CA  . ASP B 513  ? 0.5933 0.9599 0.6220 -0.0882 0.0425  0.0571  511  ASP B CA  
12750 C C   . ASP B 513  ? 0.5686 0.9207 0.5964 -0.0882 0.0404  0.0556  511  ASP B C   
12751 O O   . ASP B 513  ? 0.5347 0.8785 0.5609 -0.0960 0.0374  0.0577  511  ASP B O   
12752 C CB  . ASP B 513  ? 0.5999 0.9809 0.6357 -0.0839 0.0428  0.0559  511  ASP B CB  
12753 C CG  . ASP B 513  ? 0.6586 1.0539 0.6958 -0.0879 0.0436  0.0587  511  ASP B CG  
12754 O OD1 . ASP B 513  ? 0.6970 1.0903 0.7302 -0.0959 0.0430  0.0620  511  ASP B OD1 
12755 O OD2 . ASP B 513  ? 0.7506 1.1593 0.7929 -0.0829 0.0446  0.0576  511  ASP B OD2 
12756 N N   . GLU B 514  ? 0.4948 0.8437 0.5236 -0.0794 0.0417  0.0519  512  GLU B N   
12757 C CA  . GLU B 514  ? 0.5712 0.9067 0.5992 -0.0789 0.0400  0.0503  512  GLU B CA  
12758 C C   . GLU B 514  ? 0.5709 0.8924 0.5918 -0.0849 0.0391  0.0522  512  GLU B C   
12759 O O   . GLU B 514  ? 0.4897 0.8004 0.5094 -0.0896 0.0364  0.0530  512  GLU B O   
12760 C CB  . GLU B 514  ? 0.5084 0.8433 0.5382 -0.0681 0.0419  0.0461  512  GLU B CB  
12761 C CG  . GLU B 514  ? 0.6716 1.0199 0.7074 -0.0612 0.0430  0.0441  512  GLU B CG  
12762 C CD  . GLU B 514  ? 0.7342 1.0811 0.7706 -0.0503 0.0449  0.0399  512  GLU B CD  
12763 O OE1 . GLU B 514  ? 0.7524 1.0881 0.7874 -0.0482 0.0442  0.0381  512  GLU B OE1 
12764 O OE2 . GLU B 514  ? 0.7620 1.1185 0.7999 -0.0438 0.0469  0.0384  512  GLU B OE2 
12765 N N   . LEU B 515  ? 0.4819 0.8032 0.4978 -0.0847 0.0412  0.0531  513  LEU B N   
12766 C CA  . LEU B 515  ? 0.4770 0.7845 0.4854 -0.0896 0.0403  0.0548  513  LEU B CA  
12767 C C   . LEU B 515  ? 0.5158 0.8191 0.5215 -0.1005 0.0375  0.0590  513  LEU B C   
12768 O O   . LEU B 515  ? 0.4788 0.7680 0.4790 -0.1056 0.0355  0.0604  513  LEU B O   
12769 C CB  . LEU B 515  ? 0.4811 0.7895 0.4845 -0.0858 0.0433  0.0543  513  LEU B CB  
12770 C CG  . LEU B 515  ? 0.3915 0.7007 0.3955 -0.0750 0.0459  0.0500  513  LEU B CG  
12771 C CD1 . LEU B 515  ? 0.5366 0.8476 0.5353 -0.0720 0.0486  0.0498  513  LEU B CD1 
12772 C CD2 . LEU B 515  ? 0.5549 0.8497 0.5571 -0.0729 0.0443  0.0479  513  LEU B CD2 
12773 N N   . ILE B 516  ? 0.4030 0.7177 0.4120 -0.1043 0.0372  0.0609  514  ILE B N   
12774 C CA  . ILE B 516  ? 0.4495 0.7608 0.4559 -0.1147 0.0343  0.0649  514  ILE B CA  
12775 C C   . ILE B 516  ? 0.4199 0.7300 0.4304 -0.1184 0.0310  0.0651  514  ILE B C   
12776 O O   . ILE B 516  ? 0.4646 0.7729 0.4736 -0.1268 0.0284  0.0681  514  ILE B O   
12777 C CB  . ILE B 516  ? 0.5301 0.8539 0.5365 -0.1178 0.0357  0.0675  514  ILE B CB  
12778 C CG1 . ILE B 516  ? 0.4644 0.8050 0.4786 -0.1146 0.0365  0.0665  514  ILE B CG1 
12779 C CG2 . ILE B 516  ? 0.4818 0.8070 0.4840 -0.1139 0.0390  0.0671  514  ILE B CG2 
12780 C CD1 . ILE B 516  ? 0.5180 0.8716 0.5328 -0.1189 0.0374  0.0694  514  ILE B CD1 
12781 N N   . ALA B 517  ? 0.4436 0.7547 0.4591 -0.1122 0.0311  0.0618  515  ALA B N   
12782 C CA  . ALA B 517  ? 0.4996 0.8076 0.5184 -0.1153 0.0279  0.0617  515  ALA B CA  
12783 C C   . ALA B 517  ? 0.4690 0.7601 0.4820 -0.1231 0.0245  0.0636  515  ALA B C   
12784 O O   . ALA B 517  ? 0.4765 0.7558 0.4846 -0.1223 0.0247  0.0632  515  ALA B O   
12785 C CB  . ALA B 517  ? 0.4113 0.7202 0.4352 -0.1069 0.0287  0.0578  515  ALA B CB  
12786 N N   . ASP B 518  ? 0.4369 0.7267 0.4499 -0.1307 0.0212  0.0658  516  ASP B N   
12787 C CA  . ASP B 518  ? 0.4319 0.7053 0.4390 -0.1384 0.0175  0.0677  516  ASP B CA  
12788 C C   . ASP B 518  ? 0.4069 0.6705 0.4155 -0.1358 0.0157  0.0650  516  ASP B C   
12789 O O   . ASP B 518  ? 0.4139 0.6825 0.4278 -0.1347 0.0145  0.0637  516  ASP B O   
12790 C CB  . ASP B 518  ? 0.3722 0.6478 0.3785 -0.1471 0.0145  0.0707  516  ASP B CB  
12791 C CG  . ASP B 518  ? 0.5005 0.7581 0.4994 -0.1553 0.0105  0.0729  516  ASP B CG  
12792 O OD1 . ASP B 518  ? 0.4163 0.6595 0.4112 -0.1542 0.0096  0.0718  516  ASP B OD1 
12793 O OD2 . ASP B 518  ? 0.4629 0.7203 0.4597 -0.1629 0.0079  0.0756  516  ASP B OD2 
12794 N N   . PRO B 519  ? 0.3366 0.5866 0.3408 -0.1346 0.0156  0.0642  517  PRO B N   
12795 C CA  . PRO B 519  ? 0.3648 0.6029 0.3699 -0.1307 0.0132  0.0609  517  PRO B CA  
12796 C C   . PRO B 519  ? 0.3487 0.5802 0.3533 -0.1380 0.0089  0.0621  517  PRO B C   
12797 O O   . PRO B 519  ? 0.3767 0.6054 0.3847 -0.1347 0.0072  0.0594  517  PRO B O   
12798 C CB  . PRO B 519  ? 0.3678 0.5875 0.3658 -0.1270 0.0124  0.0593  517  PRO B CB  
12799 C CG  . PRO B 519  ? 0.3819 0.6015 0.3741 -0.1334 0.0131  0.0632  517  PRO B CG  
12800 C CD  . PRO B 519  ? 0.3768 0.6184 0.3738 -0.1359 0.0166  0.0658  517  PRO B CD  
12801 N N   . VAL B 520  ? 0.3348 0.5624 0.3345 -0.1473 0.0068  0.0658  518  VAL B N   
12802 C CA  . VAL B 520  ? 0.3778 0.5968 0.3756 -0.1539 0.0023  0.0667  518  VAL B CA  
12803 C C   . VAL B 520  ? 0.4167 0.6488 0.4215 -0.1531 0.0019  0.0659  518  VAL B C   
12804 O O   . VAL B 520  ? 0.4070 0.6342 0.4134 -0.1537 -0.0008 0.0644  518  VAL B O   
12805 C CB  . VAL B 520  ? 0.3914 0.6026 0.3817 -0.1625 -0.0001 0.0704  518  VAL B CB  
12806 C CG1 . VAL B 520  ? 0.5011 0.7011 0.4883 -0.1691 -0.0051 0.0710  518  VAL B CG1 
12807 C CG2 . VAL B 520  ? 0.3822 0.5811 0.3654 -0.1627 0.0004  0.0714  518  VAL B CG2 
12808 N N   . GLU B 521  ? 0.4158 0.6647 0.4246 -0.1515 0.0045  0.0667  519  GLU B N   
12809 C CA  . GLU B 521  ? 0.3873 0.6493 0.4024 -0.1507 0.0042  0.0662  519  GLU B CA  
12810 C C   . GLU B 521  ? 0.4218 0.6901 0.4437 -0.1419 0.0060  0.0626  519  GLU B C   
12811 O O   . GLU B 521  ? 0.4309 0.7035 0.4569 -0.1414 0.0044  0.0615  519  GLU B O   
12812 C CB  . GLU B 521  ? 0.4002 0.6780 0.4172 -0.1520 0.0062  0.0684  519  GLU B CB  
12813 C CG  . GLU B 521  ? 0.4170 0.6899 0.4279 -0.1612 0.0042  0.0722  519  GLU B CG  
12814 C CD  . GLU B 521  ? 0.5276 0.7905 0.5354 -0.1687 -0.0007 0.0733  519  GLU B CD  
12815 O OE1 . GLU B 521  ? 0.5483 0.8148 0.5605 -0.1674 -0.0020 0.0718  519  GLU B OE1 
12816 O OE2 . GLU B 521  ? 0.5677 0.8188 0.5683 -0.1758 -0.0032 0.0758  519  GLU B OE2 
12817 N N   . VAL B 522  ? 0.3673 0.6361 0.3901 -0.1349 0.0092  0.0607  520  VAL B N   
12818 C CA  . VAL B 522  ? 0.3772 0.6502 0.4057 -0.1265 0.0106  0.0572  520  VAL B CA  
12819 C C   . VAL B 522  ? 0.4353 0.6952 0.4631 -0.1277 0.0075  0.0556  520  VAL B C   
12820 O O   . VAL B 522  ? 0.4181 0.6818 0.4507 -0.1246 0.0066  0.0536  520  VAL B O   
12821 C CB  . VAL B 522  ? 0.3809 0.6563 0.4097 -0.1188 0.0147  0.0555  520  VAL B CB  
12822 C CG1 . VAL B 522  ? 0.3887 0.6649 0.4222 -0.1097 0.0156  0.0515  520  VAL B CG1 
12823 C CG2 . VAL B 522  ? 0.4861 0.7755 0.5160 -0.1168 0.0177  0.0566  520  VAL B CG2 
12824 N N   . VAL B 523  ? 0.3472 0.5885 0.3676 -0.1306 0.0051  0.0558  521  VAL B N   
12825 C CA  . VAL B 523  ? 0.3683 0.5927 0.3858 -0.1300 0.0013  0.0534  521  VAL B CA  
12826 C C   . VAL B 523  ? 0.3560 0.5835 0.3753 -0.1374 -0.0019 0.0550  521  VAL B C   
12827 O O   . VAL B 523  ? 0.3627 0.5871 0.3841 -0.1347 -0.0038 0.0526  521  VAL B O   
12828 C CB  . VAL B 523  ? 0.3689 0.5729 0.3777 -0.1315 -0.0007 0.0534  521  VAL B CB  
12829 C CG1 . VAL B 523  ? 0.3660 0.5536 0.3716 -0.1324 -0.0050 0.0515  521  VAL B CG1 
12830 C CG2 . VAL B 523  ? 0.3574 0.5569 0.3650 -0.1228 0.0019  0.0510  521  VAL B CG2 
12831 N N   . ARG B 524  ? 0.3656 0.5977 0.3830 -0.1460 -0.0028 0.0587  522  ARG B N   
12832 C CA  . ARG B 524  ? 0.4339 0.6652 0.4508 -0.1518 -0.0065 0.0596  522  ARG B CA  
12833 C C   . ARG B 524  ? 0.4547 0.7001 0.4791 -0.1474 -0.0058 0.0580  522  ARG B C   
12834 O O   . ARG B 524  ? 0.4344 0.6769 0.4594 -0.1497 -0.0089 0.0573  522  ARG B O   
12835 C CB  . ARG B 524  ? 0.4331 0.6664 0.4458 -0.1593 -0.0074 0.0633  522  ARG B CB  
12836 C CG  . ARG B 524  ? 0.4299 0.6598 0.4407 -0.1661 -0.0116 0.0645  522  ARG B CG  
12837 C CD  . ARG B 524  ? 0.4731 0.7110 0.4823 -0.1723 -0.0117 0.0681  522  ARG B CD  
12838 N NE  . ARG B 524  ? 0.4607 0.6930 0.4642 -0.1751 -0.0107 0.0703  522  ARG B NE  
12839 C CZ  . ARG B 524  ? 0.5073 0.7225 0.5027 -0.1809 -0.0138 0.0717  522  ARG B CZ  
12840 N NH1 . ARG B 524  ? 0.5402 0.7414 0.5318 -0.1842 -0.0180 0.0709  522  ARG B NH1 
12841 N NH2 . ARG B 524  ? 0.5161 0.7278 0.5067 -0.1830 -0.0126 0.0739  522  ARG B NH2 
12842 N N   . ALA B 525  ? 0.4338 0.6941 0.4638 -0.1408 -0.0019 0.0573  523  ALA B N   
12843 C CA  . ALA B 525  ? 0.4112 0.6854 0.4481 -0.1363 -0.0012 0.0560  523  ALA B CA  
12844 C C   . ALA B 525  ? 0.4496 0.7224 0.4906 -0.1287 -0.0007 0.0524  523  ALA B C   
12845 O O   . ALA B 525  ? 0.4101 0.6928 0.4563 -0.1247 -0.0005 0.0512  523  ALA B O   
12846 C CB  . ALA B 525  ? 0.4387 0.7296 0.4791 -0.1326 0.0025  0.0569  523  ALA B CB  
12847 N N   . MET B 526  ? 0.4348 0.6958 0.4734 -0.1267 -0.0006 0.0509  524  MET B N   
12848 C CA  A MET B 526  ? 0.4106 0.6660 0.4510 -0.1181 -0.0006 0.0470  524  MET B CA  
12849 C CA  B MET B 526  ? 0.4106 0.6659 0.4509 -0.1181 -0.0006 0.0470  524  MET B CA  
12850 C C   . MET B 526  ? 0.4448 0.6958 0.4857 -0.1208 -0.0044 0.0461  524  MET B C   
12851 O O   . MET B 526  ? 0.3849 0.6285 0.4219 -0.1290 -0.0077 0.0478  524  MET B O   
12852 C CB  A MET B 526  ? 0.4299 0.6668 0.4642 -0.1135 -0.0006 0.0447  524  MET B CB  
12853 C CB  B MET B 526  ? 0.4299 0.6667 0.4642 -0.1135 -0.0006 0.0447  524  MET B CB  
12854 C CG  A MET B 526  ? 0.4641 0.7050 0.4980 -0.1094 0.0032  0.0450  524  MET B CG  
12855 C CG  B MET B 526  ? 0.4609 0.7017 0.4968 -0.1048 0.0034  0.0430  524  MET B CG  
12856 S SD  A MET B 526  ? 0.4679 0.7274 0.5097 -0.1002 0.0073  0.0433  524  MET B SD  
12857 S SD  B MET B 526  ? 0.4914 0.7145 0.5195 -0.1034 0.0037  0.0424  524  MET B SD  
12858 C CE  A MET B 526  ? 0.4445 0.6912 0.4862 -0.0910 0.0062  0.0387  524  MET B CE  
12859 C CE  B MET B 526  ? 0.4488 0.6731 0.4795 -0.0912 0.0070  0.0387  524  MET B CE  
12860 N N   . PRO B 527  ? 0.4420 0.6974 0.4875 -0.1140 -0.0042 0.0436  525  PRO B N   
12861 C CA  . PRO B 527  ? 0.5131 0.7645 0.5589 -0.1163 -0.0078 0.0427  525  PRO B CA  
12862 C C   . PRO B 527  ? 0.4761 0.7057 0.5145 -0.1179 -0.0110 0.0411  525  PRO B C   
12863 O O   . PRO B 527  ? 0.4110 0.6353 0.4471 -0.1240 -0.0147 0.0417  525  PRO B O   
12864 C CB  . PRO B 527  ? 0.5517 0.8104 0.6030 -0.1071 -0.0063 0.0400  525  PRO B CB  
12865 C CG  . PRO B 527  ? 0.4963 0.7522 0.5470 -0.0992 -0.0029 0.0383  525  PRO B CG  
12866 C CD  . PRO B 527  ? 0.5602 0.8213 0.6096 -0.1037 -0.0009 0.0411  525  PRO B CD  
12867 N N   . VAL B 528  ? 0.3876 0.6047 0.4222 -0.1126 -0.0098 0.0392  526  VAL B N   
12868 C CA  . VAL B 528  ? 0.3542 0.5508 0.3816 -0.1135 -0.0125 0.0378  526  VAL B CA  
12869 C C   . VAL B 528  ? 0.3657 0.5550 0.3883 -0.1153 -0.0114 0.0391  526  VAL B C   
12870 O O   . VAL B 528  ? 0.4087 0.5971 0.4316 -0.1090 -0.0086 0.0379  526  VAL B O   
12871 C CB  . VAL B 528  ? 0.3613 0.5491 0.3887 -0.1048 -0.0123 0.0340  526  VAL B CB  
12872 C CG1 . VAL B 528  ? 0.3617 0.5292 0.3820 -0.1053 -0.0147 0.0325  526  VAL B CG1 
12873 C CG2 . VAL B 528  ? 0.4018 0.5963 0.4335 -0.1033 -0.0136 0.0328  526  VAL B CG2 
12874 N N   . VAL B 529  ? 0.3217 0.5057 0.3396 -0.1241 -0.0138 0.0417  527  VAL B N   
12875 C CA  . VAL B 529  ? 0.3036 0.4810 0.3166 -0.1265 -0.0129 0.0434  527  VAL B CA  
12876 C C   . VAL B 529  ? 0.3137 0.4733 0.3217 -0.1209 -0.0135 0.0407  527  VAL B C   
12877 O O   . VAL B 529  ? 0.3592 0.5053 0.3635 -0.1209 -0.0165 0.0388  527  VAL B O   
12878 C CB  . VAL B 529  ? 0.3333 0.5073 0.3417 -0.1374 -0.0158 0.0469  527  VAL B CB  
12879 C CG1 . VAL B 529  ? 0.3355 0.4990 0.3374 -0.1395 -0.0156 0.0484  527  VAL B CG1 
12880 C CG2 . VAL B 529  ? 0.3394 0.5332 0.3534 -0.1431 -0.0147 0.0501  527  VAL B CG2 
12881 N N   . GLY B 530  ? 0.2838 0.4435 0.2916 -0.1159 -0.0105 0.0402  528  GLY B N   
12882 C CA  . GLY B 530  ? 0.2957 0.4395 0.2988 -0.1109 -0.0110 0.0378  528  GLY B CA  
12883 C C   . GLY B 530  ? 0.2891 0.4301 0.2952 -0.1022 -0.0102 0.0340  528  GLY B C   
12884 O O   . GLY B 530  ? 0.2817 0.4085 0.2839 -0.0987 -0.0113 0.0319  528  GLY B O   
12885 N N   . ALA B 531  ? 0.2519 0.4058 0.2644 -0.0985 -0.0085 0.0331  529  ALA B N   
12886 C CA  . ALA B 531  ? 0.2535 0.4049 0.2685 -0.0901 -0.0076 0.0298  529  ALA B CA  
12887 C C   . ALA B 531  ? 0.2993 0.4460 0.3132 -0.0839 -0.0053 0.0283  529  ALA B C   
12888 O O   . ALA B 531  ? 0.3199 0.4734 0.3343 -0.0839 -0.0029 0.0297  529  ALA B O   
12889 C CB  . ALA B 531  ? 0.3276 0.4947 0.3497 -0.0871 -0.0060 0.0294  529  ALA B CB  
12890 N N   . LYS B 532  ? 0.2370 0.3718 0.2492 -0.0788 -0.0060 0.0255  530  LYS B N   
12891 C CA  . LYS B 532  ? 0.2352 0.3652 0.2467 -0.0724 -0.0041 0.0237  530  LYS B CA  
12892 C C   . LYS B 532  ? 0.2474 0.3908 0.2641 -0.0673 -0.0008 0.0234  530  LYS B C   
12893 O O   . LYS B 532  ? 0.2598 0.4143 0.2813 -0.0665 -0.0001 0.0235  530  LYS B O   
12894 C CB  . LYS B 532  ? 0.2625 0.3807 0.2730 -0.0677 -0.0054 0.0207  530  LYS B CB  
12895 C CG  . LYS B 532  ? 0.2951 0.4093 0.3061 -0.0604 -0.0036 0.0185  530  LYS B CG  
12896 C CD  . LYS B 532  ? 0.3106 0.4153 0.3213 -0.0563 -0.0048 0.0158  530  LYS B CD  
12897 C CE  . LYS B 532  ? 0.2890 0.4011 0.3043 -0.0535 -0.0043 0.0148  530  LYS B CE  
12898 N NZ  . LYS B 532  ? 0.3077 0.4302 0.3275 -0.0483 -0.0014 0.0143  530  LYS B NZ  
12899 N N   . HIS B 533  ? 0.2459 0.3880 0.2614 -0.0637 0.0012  0.0229  531  HIS B N   
12900 C CA  . HIS B 533  ? 0.2584 0.4110 0.2780 -0.0578 0.0043  0.0220  531  HIS B CA  
12901 C C   . HIS B 533  ? 0.2643 0.4176 0.2877 -0.0521 0.0044  0.0195  531  HIS B C   
12902 O O   . HIS B 533  ? 0.2538 0.3959 0.2756 -0.0499 0.0029  0.0177  531  HIS B O   
12903 C CB  . HIS B 533  ? 0.2498 0.3968 0.2665 -0.0543 0.0058  0.0211  531  HIS B CB  
12904 C CG  . HIS B 533  ? 0.2948 0.4530 0.3144 -0.0495 0.0090  0.0207  531  HIS B CG  
12905 N ND1 . HIS B 533  ? 0.2742 0.4370 0.2978 -0.0430 0.0103  0.0186  531  HIS B ND1 
12906 C CD2 . HIS B 533  ? 0.3537 0.5188 0.3724 -0.0502 0.0111  0.0221  531  HIS B CD2 
12907 C CE1 . HIS B 533  ? 0.3497 0.5216 0.3746 -0.0396 0.0130  0.0186  531  HIS B CE1 
12908 N NE2 . HIS B 533  ? 0.3701 0.5439 0.3920 -0.0438 0.0136  0.0206  531  HIS B NE2 
12909 N N   . ASP B 534  ? 0.2721 0.4389 0.3004 -0.0496 0.0061  0.0197  532  ASP B N   
12910 C CA  . ASP B 534  ? 0.3026 0.4710 0.3344 -0.0443 0.0061  0.0177  532  ASP B CA  
12911 C C   . ASP B 534  ? 0.2898 0.4502 0.3207 -0.0373 0.0071  0.0151  532  ASP B C   
12912 O O   . ASP B 534  ? 0.3157 0.4721 0.3479 -0.0337 0.0064  0.0134  532  ASP B O   
12913 C CB  . ASP B 534  ? 0.2943 0.4792 0.3313 -0.0427 0.0078  0.0185  532  ASP B CB  
12914 C CG  . ASP B 534  ? 0.5432 0.7361 0.5821 -0.0491 0.0063  0.0206  532  ASP B CG  
12915 O OD1 . ASP B 534  ? 0.5763 0.7617 0.6137 -0.0522 0.0037  0.0205  532  ASP B OD1 
12916 O OD2 . ASP B 534  ? 0.6527 0.8595 0.6945 -0.0510 0.0077  0.0225  532  ASP B OD2 
12917 N N   . ARG B 535  ? 0.2584 0.4166 0.2872 -0.0355 0.0086  0.0148  533  ARG B N   
12918 C CA  . ARG B 535  ? 0.2656 0.4179 0.2938 -0.0288 0.0096  0.0125  533  ARG B CA  
12919 C C   . ARG B 535  ? 0.2673 0.4052 0.2913 -0.0293 0.0083  0.0116  533  ARG B C   
12920 O O   . ARG B 535  ? 0.2907 0.4235 0.3135 -0.0248 0.0091  0.0099  533  ARG B O   
12921 C CB  . ARG B 535  ? 0.3948 0.5556 0.4239 -0.0252 0.0124  0.0124  533  ARG B CB  
12922 N N   . ILE B 536  ? 0.2409 0.3722 0.2623 -0.0347 0.0061  0.0126  534  ILE B N   
12923 C CA  . ILE B 536  ? 0.2155 0.3331 0.2328 -0.0352 0.0046  0.0117  534  ILE B CA  
12924 C C   . ILE B 536  ? 0.1998 0.3104 0.2169 -0.0365 0.0023  0.0110  534  ILE B C   
12925 O O   . ILE B 536  ? 0.2369 0.3492 0.2536 -0.0414 0.0008  0.0124  534  ILE B O   
12926 C CB  . ILE B 536  ? 0.2343 0.3489 0.2474 -0.0402 0.0040  0.0137  534  ILE B CB  
12927 C CG1 . ILE B 536  ? 0.2721 0.3940 0.2851 -0.0386 0.0065  0.0143  534  ILE B CG1 
12928 C CG2 . ILE B 536  ? 0.2549 0.3551 0.2638 -0.0403 0.0021  0.0127  534  ILE B CG2 
12929 C CD1 . ILE B 536  ? 0.3036 0.4235 0.3124 -0.0436 0.0061  0.0165  534  ILE B CD1 
12930 N N   . ALA B 537  ? 0.2006 0.3034 0.2176 -0.0322 0.0020  0.0088  535  ALA B N   
12931 C CA  . ALA B 537  ? 0.2083 0.3048 0.2251 -0.0327 0.0001  0.0079  535  ALA B CA  
12932 C C   . ALA B 537  ? 0.2322 0.3180 0.2445 -0.0364 -0.0022 0.0082  535  ALA B C   
12933 O O   . ALA B 537  ? 0.2022 0.2815 0.2119 -0.0357 -0.0022 0.0079  535  ALA B O   
12934 C CB  . ALA B 537  ? 0.2301 0.3227 0.2485 -0.0268 0.0007  0.0056  535  ALA B CB  
12935 N N   . LEU B 538  ? 0.2031 0.2867 0.2142 -0.0403 -0.0042 0.0087  536  LEU B N   
12936 C CA  . LEU B 538  ? 0.2281 0.2997 0.2348 -0.0423 -0.0065 0.0082  536  LEU B CA  
12937 C C   . LEU B 538  ? 0.2238 0.2879 0.2307 -0.0370 -0.0063 0.0058  536  LEU B C   
12938 O O   . LEU B 538  ? 0.2159 0.2835 0.2261 -0.0329 -0.0050 0.0045  536  LEU B O   
12939 C CB  . LEU B 538  ? 0.2253 0.2952 0.2308 -0.0462 -0.0087 0.0085  536  LEU B CB  
12940 C CG  . LEU B 538  ? 0.2873 0.3616 0.2914 -0.0529 -0.0098 0.0110  536  LEU B CG  
12941 C CD1 . LEU B 538  ? 0.2978 0.3708 0.3011 -0.0558 -0.0120 0.0108  536  LEU B CD1 
12942 C CD2 . LEU B 538  ? 0.2472 0.3135 0.2462 -0.0564 -0.0111 0.0122  536  LEU B CD2 
12943 N N   . PRO B 539  ? 0.1903 0.2440 0.1935 -0.0371 -0.0077 0.0052  537  PRO B N   
12944 C CA  . PRO B 539  ? 0.1964 0.2439 0.2002 -0.0323 -0.0075 0.0030  537  PRO B CA  
12945 C C   . PRO B 539  ? 0.2101 0.2577 0.2158 -0.0302 -0.0076 0.0015  537  PRO B C   
12946 O O   . PRO B 539  ? 0.2241 0.2725 0.2325 -0.0257 -0.0063 0.0002  537  PRO B O   
12947 C CB  . PRO B 539  ? 0.2293 0.2660 0.2285 -0.0337 -0.0096 0.0028  537  PRO B CB  
12948 C CG  . PRO B 539  ? 0.1955 0.2340 0.1921 -0.0381 -0.0099 0.0051  537  PRO B CG  
12949 C CD  . PRO B 539  ? 0.2161 0.2640 0.2147 -0.0415 -0.0094 0.0066  537  PRO B CD  
12950 N N   . ALA B 540  ? 0.2132 0.2602 0.2176 -0.0334 -0.0092 0.0019  538  ALA B N   
12951 C CA  . ALA B 540  ? 0.2376 0.2847 0.2434 -0.0316 -0.0094 0.0006  538  ALA B CA  
12952 C C   . ALA B 540  ? 0.2409 0.2977 0.2513 -0.0290 -0.0074 0.0007  538  ALA B C   
12953 O O   . ALA B 540  ? 0.2270 0.2839 0.2389 -0.0261 -0.0070 -0.0005 538  ALA B O   
12954 C CB  . ALA B 540  ? 0.2434 0.2883 0.2463 -0.0360 -0.0117 0.0010  538  ALA B CB  
12955 N N   . GLU B 541  ? 0.2417 0.3069 0.2541 -0.0298 -0.0061 0.0021  539  GLU B N   
12956 C CA  . GLU B 541  ? 0.2300 0.3049 0.2464 -0.0276 -0.0045 0.0024  539  GLU B CA  
12957 C C   . GLU B 541  ? 0.2216 0.2992 0.2404 -0.0230 -0.0024 0.0019  539  GLU B C   
12958 O O   . GLU B 541  ? 0.2449 0.3309 0.2666 -0.0211 -0.0009 0.0023  539  GLU B O   
12959 C CB  . GLU B 541  ? 0.2820 0.3657 0.2992 -0.0319 -0.0048 0.0044  539  GLU B CB  
12960 C CG  . GLU B 541  ? 0.3063 0.3872 0.3212 -0.0364 -0.0073 0.0047  539  GLU B CG  
12961 C CD  . GLU B 541  ? 0.5024 0.5912 0.5178 -0.0417 -0.0080 0.0068  539  GLU B CD  
12962 O OE1 . GLU B 541  ? 0.4196 0.5177 0.4376 -0.0419 -0.0064 0.0081  539  GLU B OE1 
12963 O OE2 . GLU B 541  ? 0.5177 0.6036 0.5308 -0.0459 -0.0103 0.0071  539  GLU B OE2 
12964 N N   . LEU B 542  ? 0.2074 0.2776 0.2247 -0.0210 -0.0022 0.0008  540  LEU B N   
12965 C CA  . LEU B 542  ? 0.2131 0.2847 0.2319 -0.0170 -0.0005 0.0003  540  LEU B CA  
12966 C C   . LEU B 542  ? 0.2655 0.3410 0.2875 -0.0128 0.0008  -0.0005 540  LEU B C   
12967 O O   . LEU B 542  ? 0.2381 0.3179 0.2616 -0.0099 0.0023  -0.0006 540  LEU B O   
12968 C CB  . LEU B 542  ? 0.2512 0.3138 0.2681 -0.0155 -0.0009 -0.0009 540  LEU B CB  
12969 C CG  . LEU B 542  ? 0.3088 0.3675 0.3228 -0.0176 -0.0015 -0.0003 540  LEU B CG  
12970 C CD1 . LEU B 542  ? 0.2378 0.2893 0.2512 -0.0146 -0.0016 -0.0018 540  LEU B CD1 
12971 C CD2 . LEU B 542  ? 0.2850 0.3510 0.2993 -0.0184 -0.0002 0.0010  540  LEU B CD2 
12972 N N   . PHE B 543  ? 0.2115 0.2852 0.2339 -0.0123 0.0001  -0.0011 541  PHE B N   
12973 C CA  . PHE B 543  ? 0.2189 0.2949 0.2437 -0.0084 0.0010  -0.0018 541  PHE B CA  
12974 C C   . PHE B 543  ? 0.2095 0.2934 0.2361 -0.0091 0.0010  -0.0009 541  PHE B C   
12975 O O   . PHE B 543  ? 0.2387 0.3245 0.2669 -0.0061 0.0014  -0.0013 541  PHE B O   
12976 C CB  . PHE B 543  ? 0.1886 0.2570 0.2127 -0.0069 0.0005  -0.0031 541  PHE B CB  
12977 C CG  . PHE B 543  ? 0.2107 0.2719 0.2332 -0.0065 0.0003  -0.0039 541  PHE B CG  
12978 C CD1 . PHE B 543  ? 0.2457 0.3069 0.2689 -0.0042 0.0014  -0.0042 541  PHE B CD1 
12979 C CD2 . PHE B 543  ? 0.1946 0.2491 0.2148 -0.0084 -0.0011 -0.0045 541  PHE B CD2 
12980 C CE1 . PHE B 543  ? 0.2243 0.2793 0.2462 -0.0039 0.0010  -0.0049 541  PHE B CE1 
12981 C CE2 . PHE B 543  ? 0.2286 0.2770 0.2475 -0.0078 -0.0014 -0.0052 541  PHE B CE2 
12982 C CZ  . PHE B 543  ? 0.2542 0.3031 0.2741 -0.0057 -0.0004 -0.0053 541  PHE B CZ  
12983 N N   . GLY B 544  ? 0.2269 0.3156 0.2531 -0.0130 0.0003  0.0003  542  GLY B N   
12984 C CA  . GLY B 544  ? 0.2271 0.3248 0.2555 -0.0138 0.0002  0.0013  542  GLY B CA  
12985 C C   . GLY B 544  ? 0.2447 0.3404 0.2729 -0.0136 -0.0010 0.0008  542  GLY B C   
12986 O O   . GLY B 544  ? 0.2602 0.3486 0.2858 -0.0156 -0.0023 0.0002  542  GLY B O   
12987 N N   . ASP B 545  ? 0.2471 0.3492 0.2777 -0.0110 -0.0005 0.0010  543  ASP B N   
12988 C CA  . ASP B 545  ? 0.3561 0.4575 0.3864 -0.0109 -0.0016 0.0007  543  ASP B CA  
12989 C C   . ASP B 545  ? 0.2885 0.3816 0.3176 -0.0079 -0.0013 -0.0006 543  ASP B C   
12990 O O   . ASP B 545  ? 0.2945 0.3854 0.3225 -0.0082 -0.0022 -0.0010 543  ASP B O   
12991 C CB  . ASP B 545  ? 0.3520 0.4630 0.3853 -0.0088 -0.0012 0.0015  543  ASP B CB  
12992 C CG  . ASP B 545  ? 0.6004 0.7209 0.6352 -0.0123 -0.0017 0.0030  543  ASP B CG  
12993 O OD1 . ASP B 545  ? 0.5586 0.6775 0.5917 -0.0173 -0.0030 0.0035  543  ASP B OD1 
12994 O OD2 . ASP B 545  ? 0.6861 0.8158 0.7240 -0.0100 -0.0009 0.0037  543  ASP B OD2 
12995 N N   . ALA B 546  ? 0.2492 0.3379 0.2783 -0.0053 -0.0001 -0.0013 544  ALA B N   
12996 C CA  . ALA B 546  ? 0.2370 0.3189 0.2654 -0.0025 0.0003  -0.0024 544  ALA B CA  
12997 C C   . ALA B 546  ? 0.2419 0.3165 0.2676 -0.0048 -0.0008 -0.0032 544  ALA B C   
12998 O O   . ALA B 546  ? 0.2556 0.3273 0.2805 -0.0038 -0.0011 -0.0038 544  ALA B O   
12999 C CB  . ALA B 546  ? 0.2300 0.3088 0.2590 0.0003  0.0016  -0.0030 544  ALA B CB  
13000 N N   . ARG B 547  ? 0.1950 0.2665 0.2190 -0.0078 -0.0016 -0.0033 545  ARG B N   
13001 C CA  . ARG B 547  ? 0.2154 0.2795 0.2366 -0.0094 -0.0028 -0.0043 545  ARG B CA  
13002 C C   . ARG B 547  ? 0.2213 0.2833 0.2406 -0.0131 -0.0038 -0.0039 545  ARG B C   
13003 O O   . ARG B 547  ? 0.2274 0.2931 0.2477 -0.0138 -0.0033 -0.0029 545  ARG B O   
13004 C CB  . ARG B 547  ? 0.2428 0.3007 0.2639 -0.0064 -0.0020 -0.0055 545  ARG B CB  
13005 C CG  . ARG B 547  ? 0.2077 0.2641 0.2297 -0.0052 -0.0011 -0.0055 545  ARG B CG  
13006 C CD  . ARG B 547  ? 0.2315 0.2827 0.2539 -0.0024 -0.0004 -0.0066 545  ARG B CD  
13007 N NE  . ARG B 547  ? 0.2507 0.3020 0.2745 -0.0006 0.0006  -0.0066 545  ARG B NE  
13008 C CZ  . ARG B 547  ? 0.2263 0.2733 0.2493 -0.0010 0.0003  -0.0071 545  ARG B CZ  
13009 N NH1 . ARG B 547  ? 0.2226 0.2647 0.2434 -0.0026 -0.0009 -0.0077 545  ARG B NH1 
13010 N NH2 . ARG B 547  ? 0.2394 0.2869 0.2635 0.0007  0.0011  -0.0071 545  ARG B NH2 
13011 N N   . THR B 548  ? 0.2008 0.2565 0.2169 -0.0152 -0.0054 -0.0045 546  THR B N   
13012 C CA  . THR B 548  ? 0.1892 0.2410 0.2026 -0.0187 -0.0068 -0.0042 546  THR B CA  
13013 C C   . THR B 548  ? 0.2026 0.2478 0.2151 -0.0168 -0.0064 -0.0051 546  THR B C   
13014 O O   . THR B 548  ? 0.1926 0.2331 0.2049 -0.0142 -0.0062 -0.0064 546  THR B O   
13015 C CB  . THR B 548  ? 0.2185 0.2659 0.2283 -0.0218 -0.0090 -0.0046 546  THR B CB  
13016 O OG1 . THR B 548  ? 0.2726 0.3267 0.2834 -0.0236 -0.0094 -0.0038 546  THR B OG1 
13017 C CG2 . THR B 548  ? 0.2569 0.2994 0.2634 -0.0256 -0.0106 -0.0041 546  THR B CG2 
13018 N N   . ASN B 549  ? 0.1946 0.2400 0.2069 -0.0181 -0.0063 -0.0042 547  ASN B N   
13019 C CA  . ASN B 549  ? 0.1801 0.2193 0.1913 -0.0166 -0.0063 -0.0049 547  ASN B CA  
13020 C C   . ASN B 549  ? 0.2077 0.2384 0.2152 -0.0179 -0.0083 -0.0059 547  ASN B C   
13021 O O   . ASN B 549  ? 0.2255 0.2545 0.2302 -0.0214 -0.0099 -0.0054 547  ASN B O   
13022 C CB  . ASN B 549  ? 0.1958 0.2374 0.2070 -0.0181 -0.0059 -0.0037 547  ASN B CB  
13023 C CG  . ASN B 549  ? 0.1733 0.2099 0.1839 -0.0161 -0.0058 -0.0043 547  ASN B CG  
13024 O OD1 . ASN B 549  ? 0.1980 0.2311 0.2095 -0.0131 -0.0054 -0.0057 547  ASN B OD1 
13025 N ND2 . ASN B 549  ? 0.1894 0.2260 0.1985 -0.0180 -0.0060 -0.0033 547  ASN B ND2 
13026 N N   . SER B 550  ? 0.2004 0.2257 0.2077 -0.0151 -0.0082 -0.0072 548  SER B N   
13027 C CA  . SER B 550  ? 0.2041 0.2210 0.2076 -0.0157 -0.0101 -0.0082 548  SER B CA  
13028 C C   . SER B 550  ? 0.2230 0.2366 0.2233 -0.0190 -0.0116 -0.0070 548  SER B C   
13029 O O   . SER B 550  ? 0.2259 0.2429 0.2273 -0.0197 -0.0108 -0.0058 548  SER B O   
13030 C CB  . SER B 550  ? 0.1818 0.1948 0.1863 -0.0118 -0.0095 -0.0097 548  SER B CB  
13031 O OG  . SER B 550  ? 0.2167 0.2305 0.2227 -0.0109 -0.0088 -0.0092 548  SER B OG  
13032 N N   . ALA B 551  ? 0.2229 0.2295 0.2189 -0.0210 -0.0138 -0.0074 549  ALA B N   
13033 C CA  . ALA B 551  ? 0.2254 0.2273 0.2175 -0.0244 -0.0156 -0.0062 549  ALA B CA  
13034 C C   . ALA B 551  ? 0.2250 0.2185 0.2147 -0.0222 -0.0168 -0.0073 549  ALA B C   
13035 O O   . ALA B 551  ? 0.2479 0.2373 0.2372 -0.0192 -0.0171 -0.0092 549  ALA B O   
13036 C CB  . ALA B 551  ? 0.2282 0.2275 0.2165 -0.0288 -0.0177 -0.0056 549  ALA B CB  
13037 N N   . GLY B 552  ? 0.2341 0.2252 0.2221 -0.0235 -0.0174 -0.0062 550  GLY B N   
13038 C CA  . GLY B 552  ? 0.2699 0.2529 0.2550 -0.0217 -0.0189 -0.0069 550  GLY B CA  
13039 C C   . GLY B 552  ? 0.2448 0.2194 0.2238 -0.0251 -0.0219 -0.0064 550  GLY B C   
13040 O O   . GLY B 552  ? 0.2849 0.2589 0.2617 -0.0285 -0.0229 -0.0059 550  GLY B O   
13041 N N   . LEU B 553  ? 0.2746 0.2421 0.2506 -0.0243 -0.0234 -0.0064 551  LEU B N   
13042 C CA  . LEU B 553  ? 0.2983 0.2563 0.2677 -0.0272 -0.0265 -0.0057 551  LEU B CA  
13043 C C   . LEU B 553  ? 0.2581 0.2142 0.2256 -0.0285 -0.0270 -0.0039 551  LEU B C   
13044 O O   . LEU B 553  ? 0.3045 0.2629 0.2749 -0.0253 -0.0258 -0.0043 551  LEU B O   
13045 C CB  . LEU B 553  ? 0.2985 0.2475 0.2650 -0.0237 -0.0284 -0.0080 551  LEU B CB  
13046 C CG  . LEU B 553  ? 0.3202 0.2695 0.2871 -0.0225 -0.0282 -0.0100 551  LEU B CG  
13047 C CD1 . LEU B 553  ? 0.3420 0.2839 0.3068 -0.0179 -0.0294 -0.0125 551  LEU B CD1 
13048 C CD2 . LEU B 553  ? 0.3448 0.2915 0.3075 -0.0276 -0.0299 -0.0090 551  LEU B CD2 
13049 N N   . ASP B 554  ? 0.2700 0.2220 0.2326 -0.0335 -0.0289 -0.0019 552  ASP B N   
13050 C CA  . ASP B 554  ? 0.2405 0.1911 0.2007 -0.0356 -0.0294 0.0003  552  ASP B CA  
13051 C C   . ASP B 554  ? 0.2749 0.2134 0.2295 -0.0342 -0.0324 -0.0002 552  ASP B C   
13052 O O   . ASP B 554  ? 0.2873 0.2173 0.2360 -0.0372 -0.0351 0.0005  552  ASP B O   
13053 C CB  . ASP B 554  ? 0.2881 0.2416 0.2461 -0.0421 -0.0296 0.0031  552  ASP B CB  
13054 C CG  . ASP B 554  ? 0.2818 0.2348 0.2372 -0.0445 -0.0298 0.0056  552  ASP B CG  
13055 O OD1 . ASP B 554  ? 0.3243 0.2745 0.2795 -0.0411 -0.0299 0.0050  552  ASP B OD1 
13056 O OD2 . ASP B 554  ? 0.3490 0.3049 0.3026 -0.0500 -0.0299 0.0081  552  ASP B OD2 
13057 N N   . LEU B 555  ? 0.2903 0.2281 0.2466 -0.0296 -0.0320 -0.0012 553  LEU B N   
13058 C CA  . LEU B 555  ? 0.2900 0.2171 0.2416 -0.0274 -0.0349 -0.0018 553  LEU B CA  
13059 C C   . LEU B 555  ? 0.3216 0.2437 0.2679 -0.0310 -0.0366 0.0009  553  LEU B C   
13060 O O   . LEU B 555  ? 0.3086 0.2222 0.2509 -0.0290 -0.0390 0.0007  553  LEU B O   
13061 C CB  . LEU B 555  ? 0.2967 0.2257 0.2526 -0.0212 -0.0339 -0.0039 553  LEU B CB  
13062 C CG  . LEU B 555  ? 0.3138 0.2471 0.2747 -0.0174 -0.0323 -0.0065 553  LEU B CG  
13063 C CD1 . LEU B 555  ? 0.3146 0.2490 0.2791 -0.0118 -0.0318 -0.0083 553  LEU B CD1 
13064 C CD2 . LEU B 555  ? 0.3469 0.2730 0.3038 -0.0176 -0.0343 -0.0078 553  LEU B CD2 
13065 N N   . SER B 556  ? 0.2996 0.2271 0.2456 -0.0361 -0.0355 0.0035  554  SER B N   
13066 C CA  . SER B 556  ? 0.2912 0.2134 0.2312 -0.0406 -0.0373 0.0064  554  SER B CA  
13067 C C   . SER B 556  ? 0.3194 0.2366 0.2543 -0.0464 -0.0393 0.0079  554  SER B C   
13068 O O   . SER B 556  ? 0.3336 0.2456 0.2628 -0.0510 -0.0411 0.0106  554  SER B O   
13069 C CB  . SER B 556  ? 0.3272 0.2589 0.2697 -0.0427 -0.0348 0.0085  554  SER B CB  
13070 O OG  . SER B 556  ? 0.3219 0.2626 0.2672 -0.0466 -0.0328 0.0095  554  SER B OG  
13071 N N   . ASN B 557  ? 0.3051 0.2234 0.2416 -0.0466 -0.0392 0.0064  555  ASN B N   
13072 C CA  . ASN B 557  ? 0.3243 0.2382 0.2563 -0.0522 -0.0412 0.0076  555  ASN B CA  
13073 C C   . ASN B 557  ? 0.3455 0.2450 0.2711 -0.0506 -0.0449 0.0060  555  ASN B C   
13074 O O   . ASN B 557  ? 0.3280 0.2255 0.2553 -0.0453 -0.0449 0.0030  555  ASN B O   
13075 C CB  . ASN B 557  ? 0.3201 0.2436 0.2574 -0.0531 -0.0390 0.0067  555  ASN B CB  
13076 C CG  . ASN B 557  ? 0.3617 0.2818 0.2949 -0.0591 -0.0411 0.0078  555  ASN B CG  
13077 O OD1 . ASN B 557  ? 0.3595 0.2677 0.2865 -0.0598 -0.0444 0.0071  555  ASN B OD1 
13078 N ND2 . ASN B 557  ? 0.3212 0.2518 0.2577 -0.0635 -0.0393 0.0096  555  ASN B ND2 
13079 N N   . GLU B 558  ? 0.3408 0.2301 0.2587 -0.0549 -0.0481 0.0082  556  GLU B N   
13080 C CA  . GLU B 558  ? 0.3820 0.2563 0.2929 -0.0531 -0.0519 0.0067  556  GLU B CA  
13081 C C   . GLU B 558  ? 0.4042 0.2756 0.3143 -0.0530 -0.0530 0.0044  556  GLU B C   
13082 O O   . GLU B 558  ? 0.4066 0.2691 0.3138 -0.0484 -0.0549 0.0018  556  GLU B O   
13083 C CB  . GLU B 558  ? 0.4528 0.3161 0.3550 -0.0584 -0.0553 0.0097  556  GLU B CB  
13084 C CG  . GLU B 558  ? 0.4313 0.2934 0.3320 -0.0576 -0.0554 0.0116  556  GLU B CG  
13085 C CD  . GLU B 558  ? 0.4321 0.2891 0.3332 -0.0497 -0.0562 0.0092  556  GLU B CD  
13086 O OE1 . GLU B 558  ? 0.4067 0.2583 0.3075 -0.0448 -0.0574 0.0060  556  GLU B OE1 
13087 O OE2 . GLU B 558  ? 0.4183 0.2773 0.3199 -0.0486 -0.0556 0.0105  556  GLU B OE2 
13088 N N   . GLU B 559  ? 0.3532 0.2316 0.2653 -0.0580 -0.0519 0.0054  557  GLU B N   
13089 C CA  . GLU B 559  ? 0.3604 0.2367 0.2719 -0.0577 -0.0528 0.0031  557  GLU B CA  
13090 C C   . GLU B 559  ? 0.3598 0.2418 0.2775 -0.0503 -0.0503 -0.0003 557  GLU B C   
13091 O O   . GLU B 559  ? 0.3837 0.2590 0.2992 -0.0465 -0.0517 -0.0032 557  GLU B O   
13092 C CB  . GLU B 559  ? 0.4187 0.3035 0.3324 -0.0641 -0.0518 0.0048  557  GLU B CB  
13093 C CG  . GLU B 559  ? 0.4924 0.3732 0.4005 -0.0723 -0.0541 0.0082  557  GLU B CG  
13094 C CD  . GLU B 559  ? 0.6066 0.4968 0.5177 -0.0779 -0.0531 0.0094  557  GLU B CD  
13095 O OE1 . GLU B 559  ? 0.7081 0.6018 0.6222 -0.0756 -0.0524 0.0069  557  GLU B OE1 
13096 O OE2 . GLU B 559  ? 0.5542 0.4489 0.4648 -0.0846 -0.0530 0.0128  557  GLU B OE2 
13097 N N   . THR B 560  ? 0.3315 0.2260 0.2569 -0.0482 -0.0466 0.0000  558  THR B N   
13098 C CA  . THR B 560  ? 0.3088 0.2093 0.2403 -0.0417 -0.0441 -0.0029 558  THR B CA  
13099 C C   . THR B 560  ? 0.3291 0.2212 0.2585 -0.0356 -0.0455 -0.0050 558  THR B C   
13100 O O   . THR B 560  ? 0.3294 0.2201 0.2598 -0.0308 -0.0454 -0.0079 558  THR B O   
13101 C CB  . THR B 560  ? 0.3004 0.2145 0.2396 -0.0409 -0.0403 -0.0019 558  THR B CB  
13102 O OG1 . THR B 560  ? 0.3316 0.2540 0.2728 -0.0462 -0.0390 0.0000  558  THR B OG1 
13103 C CG2 . THR B 560  ? 0.3089 0.2291 0.2543 -0.0346 -0.0378 -0.0046 558  THR B CG2 
13104 N N   . LEU B 561  ? 0.3135 0.2002 0.2398 -0.0355 -0.0469 -0.0036 559  LEU B N   
13105 C CA  . LEU B 561  ? 0.3198 0.1992 0.2444 -0.0294 -0.0483 -0.0055 559  LEU B CA  
13106 C C   . LEU B 561  ? 0.3356 0.2024 0.2534 -0.0282 -0.0517 -0.0074 559  LEU B C   
13107 O O   . LEU B 561  ? 0.3502 0.2142 0.2685 -0.0221 -0.0520 -0.0103 559  LEU B O   
13108 C CB  . LEU B 561  ? 0.3216 0.1974 0.2437 -0.0298 -0.0495 -0.0034 559  LEU B CB  
13109 C CG  . LEU B 561  ? 0.2892 0.1769 0.2180 -0.0295 -0.0462 -0.0022 559  LEU B CG  
13110 C CD1 . LEU B 561  ? 0.3336 0.2168 0.2585 -0.0310 -0.0477 0.0002  559  LEU B CD1 
13111 C CD2 . LEU B 561  ? 0.3047 0.1988 0.2403 -0.0229 -0.0440 -0.0049 559  LEU B CD2 
13112 N N   . ALA B 562  ? 0.3487 0.2077 0.2597 -0.0339 -0.0544 -0.0059 560  ALA B N   
13113 C CA  . ALA B 562  ? 0.3805 0.2264 0.2841 -0.0330 -0.0579 -0.0078 560  ALA B CA  
13114 C C   . ALA B 562  ? 0.3990 0.2485 0.3054 -0.0301 -0.0566 -0.0109 560  ALA B C   
13115 O O   . ALA B 562  ? 0.3918 0.2344 0.2955 -0.0248 -0.0580 -0.0139 560  ALA B O   
13116 C CB  . ALA B 562  ? 0.3771 0.2145 0.2731 -0.0406 -0.0610 -0.0052 560  ALA B CB  
13117 N N   . SER B 563  ? 0.3437 0.2042 0.2552 -0.0333 -0.0540 -0.0102 561  SER B N   
13118 C CA  . SER B 563  ? 0.3568 0.2208 0.2706 -0.0308 -0.0528 -0.0130 561  SER B CA  
13119 C C   . SER B 563  ? 0.3779 0.2489 0.2983 -0.0234 -0.0500 -0.0154 561  SER B C   
13120 O O   . SER B 563  ? 0.3741 0.2428 0.2939 -0.0190 -0.0500 -0.0184 561  SER B O   
13121 C CB  . SER B 563  ? 0.4047 0.2787 0.3222 -0.0362 -0.0510 -0.0115 561  SER B CB  
13122 O OG  . SER B 563  ? 0.4372 0.3244 0.3626 -0.0362 -0.0474 -0.0100 561  SER B OG  
13123 N N   . LEU B 564  ? 0.3353 0.2147 0.2617 -0.0222 -0.0475 -0.0141 562  LEU B N   
13124 C CA  A LEU B 564  ? 0.3274 0.2132 0.2599 -0.0156 -0.0449 -0.0161 562  LEU B CA  
13125 C CA  B LEU B 564  ? 0.3284 0.2142 0.2610 -0.0156 -0.0449 -0.0161 562  LEU B CA  
13126 C C   . LEU B 564  ? 0.3816 0.2580 0.3105 -0.0100 -0.0471 -0.0183 562  LEU B C   
13127 O O   . LEU B 564  ? 0.3647 0.2429 0.2959 -0.0046 -0.0460 -0.0211 562  LEU B O   
13128 C CB  A LEU B 564  ? 0.3409 0.2364 0.2797 -0.0160 -0.0423 -0.0142 562  LEU B CB  
13129 C CB  B LEU B 564  ? 0.3411 0.2364 0.2799 -0.0159 -0.0424 -0.0142 562  LEU B CB  
13130 C CG  A LEU B 564  ? 0.3185 0.2216 0.2643 -0.0101 -0.0397 -0.0158 562  LEU B CG  
13131 C CG  B LEU B 564  ? 0.3620 0.2705 0.3090 -0.0146 -0.0385 -0.0146 562  LEU B CG  
13132 C CD1 A LEU B 564  ? 0.3639 0.2742 0.3140 -0.0084 -0.0372 -0.0176 562  LEU B CD1 
13133 C CD1 B LEU B 564  ? 0.3408 0.2565 0.2928 -0.0144 -0.0365 -0.0129 562  LEU B CD1 
13134 C CD2 A LEU B 564  ? 0.3331 0.2439 0.2836 -0.0112 -0.0377 -0.0137 562  LEU B CD2 
13135 C CD2 B LEU B 564  ? 0.3601 0.2701 0.3098 -0.0088 -0.0373 -0.0177 562  LEU B CD2 
13136 N N   . THR B 565  ? 0.3614 0.2279 0.2844 -0.0110 -0.0502 -0.0171 563  THR B N   
13137 C CA  . THR B 565  ? 0.3242 0.1807 0.2427 -0.0056 -0.0527 -0.0192 563  THR B CA  
13138 C C   . THR B 565  ? 0.3762 0.2271 0.2912 -0.0026 -0.0538 -0.0223 563  THR B C   
13139 O O   . THR B 565  ? 0.3775 0.2287 0.2942 0.0039  -0.0532 -0.0251 563  THR B O   
13140 C CB  . THR B 565  ? 0.3790 0.2236 0.2898 -0.0085 -0.0565 -0.0171 563  THR B CB  
13141 O OG1 . THR B 565  ? 0.3945 0.2445 0.3084 -0.0105 -0.0554 -0.0144 563  THR B OG1 
13142 C CG2 . THR B 565  ? 0.3960 0.2292 0.3015 -0.0027 -0.0595 -0.0193 563  THR B CG2 
13143 N N   . GLU B 566  ? 0.3726 0.2189 0.2829 -0.0074 -0.0552 -0.0220 564  GLU B N   
13144 C CA  . GLU B 566  ? 0.3679 0.2079 0.2737 -0.0048 -0.0566 -0.0251 564  GLU B CA  
13145 C C   . GLU B 566  ? 0.3680 0.2194 0.2808 -0.0012 -0.0528 -0.0272 564  GLU B C   
13146 O O   . GLU B 566  ? 0.3776 0.2267 0.2894 0.0045  -0.0528 -0.0304 564  GLU B O   
13147 C CB  . GLU B 566  ? 0.4370 0.2694 0.3359 -0.0114 -0.0592 -0.0242 564  GLU B CB  
13148 C CG  . GLU B 566  ? 0.5259 0.3448 0.4164 -0.0149 -0.0634 -0.0222 564  GLU B CG  
13149 C CD  . GLU B 566  ? 0.6798 0.4882 0.5657 -0.0086 -0.0659 -0.0240 564  GLU B CD  
13150 O OE1 . GLU B 566  ? 0.7409 0.5439 0.6240 -0.0031 -0.0668 -0.0275 564  GLU B OE1 
13151 O OE2 . GLU B 566  ? 0.6324 0.4379 0.5175 -0.0089 -0.0669 -0.0219 564  GLU B OE2 
13152 N N   . ALA B 567  ? 0.3509 0.2145 0.2705 -0.0045 -0.0497 -0.0255 565  ALA B N   
13153 C CA  . ALA B 567  ? 0.3431 0.2176 0.2694 -0.0014 -0.0461 -0.0271 565  ALA B CA  
13154 C C   . ALA B 567  ? 0.3528 0.2317 0.2841 0.0054  -0.0443 -0.0287 565  ALA B C   
13155 O O   . ALA B 567  ? 0.3418 0.2246 0.2755 0.0099  -0.0425 -0.0311 565  ALA B O   
13156 C CB  . ALA B 567  ? 0.3398 0.2260 0.2722 -0.0060 -0.0433 -0.0247 565  ALA B CB  
13157 N N   . LEU B 568  ? 0.3035 0.1825 0.2365 0.0060  -0.0446 -0.0272 566  LEU B N   
13158 C CA  . LEU B 568  ? 0.3039 0.1877 0.2420 0.0121  -0.0430 -0.0285 566  LEU B CA  
13159 C C   . LEU B 568  ? 0.3514 0.2265 0.2848 0.0179  -0.0452 -0.0314 566  LEU B C   
13160 O O   . LEU B 568  ? 0.3382 0.2183 0.2754 0.0234  -0.0434 -0.0337 566  LEU B O   
13161 C CB  . LEU B 568  ? 0.3067 0.1922 0.2472 0.0111  -0.0432 -0.0261 566  LEU B CB  
13162 C CG  . LEU B 568  ? 0.3125 0.2082 0.2587 0.0066  -0.0406 -0.0235 566  LEU B CG  
13163 C CD1 . LEU B 568  ? 0.3601 0.2551 0.3066 0.0055  -0.0414 -0.0214 566  LEU B CD1 
13164 C CD2 . LEU B 568  ? 0.3093 0.2170 0.2636 0.0091  -0.0368 -0.0245 566  LEU B CD2 
13165 N N   . ARG B 569  ? 0.3415 0.2035 0.2665 0.0169  -0.0491 -0.0313 567  ARG B N   
13166 C CA  . ARG B 569  ? 0.3623 0.2146 0.2816 0.0225  -0.0515 -0.0343 567  ARG B CA  
13167 C C   . ARG B 569  ? 0.3826 0.2365 0.3013 0.0249  -0.0503 -0.0372 567  ARG B C   
13168 O O   . ARG B 569  ? 0.4089 0.2641 0.3288 0.0315  -0.0495 -0.0400 567  ARG B O   
13169 C CB  . ARG B 569  ? 0.3826 0.2195 0.2920 0.0199  -0.0561 -0.0335 567  ARG B CB  
13170 C CG  . ARG B 569  ? 0.4888 0.3224 0.3977 0.0199  -0.0578 -0.0314 567  ARG B CG  
13171 C CD  . ARG B 569  ? 0.4798 0.2980 0.3786 0.0165  -0.0624 -0.0301 567  ARG B CD  
13172 N NE  . ARG B 569  ? 0.5473 0.3638 0.4460 0.0151  -0.0636 -0.0274 567  ARG B NE  
13173 C CZ  . ARG B 569  ? 0.5559 0.3614 0.4471 0.0107  -0.0670 -0.0251 567  ARG B CZ  
13174 N NH1 . ARG B 569  ? 0.6234 0.4185 0.5067 0.0066  -0.0697 -0.0250 567  ARG B NH1 
13175 N NH2 . ARG B 569  ? 0.6443 0.4494 0.5359 0.0101  -0.0678 -0.0227 567  ARG B NH2 
13176 N N   . GLU B 570  ? 0.3561 0.2107 0.2732 0.0197  -0.0500 -0.0365 568  GLU B N   
13177 C CA  . GLU B 570  ? 0.3706 0.2264 0.2866 0.0216  -0.0489 -0.0392 568  GLU B CA  
13178 C C   . GLU B 570  ? 0.3681 0.2376 0.2929 0.0255  -0.0446 -0.0401 568  GLU B C   
13179 O O   . GLU B 570  ? 0.3977 0.2681 0.3220 0.0303  -0.0436 -0.0430 568  GLU B O   
13180 C CB  . GLU B 570  ? 0.4078 0.2626 0.3209 0.0148  -0.0495 -0.0379 568  GLU B CB  
13181 C CG  . GLU B 570  ? 0.4617 0.3016 0.3649 0.0111  -0.0541 -0.0375 568  GLU B CG  
13182 C CD  . GLU B 570  ? 0.6144 0.4550 0.5162 0.0028  -0.0548 -0.0350 568  GLU B CD  
13183 O OE1 . GLU B 570  ? 0.5926 0.4451 0.5008 0.0005  -0.0517 -0.0339 568  GLU B OE1 
13184 O OE2 . GLU B 570  ? 0.6782 0.5075 0.5724 -0.0013 -0.0585 -0.0341 568  GLU B OE2 
13185 N N   . SER B 571  ? 0.3445 0.2245 0.2770 0.0235  -0.0419 -0.0377 569  SER B N   
13186 C CA  . SER B 571  ? 0.3532 0.2460 0.2940 0.0267  -0.0379 -0.0383 569  SER B CA  
13187 C C   . SER B 571  ? 0.4019 0.2952 0.3444 0.0339  -0.0376 -0.0406 569  SER B C   
13188 O O   . SER B 571  ? 0.3634 0.2638 0.3097 0.0377  -0.0350 -0.0423 569  SER B O   
13189 C CB  . SER B 571  ? 0.3422 0.2446 0.2902 0.0232  -0.0357 -0.0353 569  SER B CB  
13190 O OG  . SER B 571  ? 0.3568 0.2589 0.3070 0.0251  -0.0363 -0.0345 569  SER B OG  
13191 N N   . ALA B 572  ? 0.3500 0.2360 0.2897 0.0358  -0.0403 -0.0405 570  ALA B N   
13192 C CA  . ALA B 572  ? 0.3995 0.2861 0.3407 0.0429  -0.0403 -0.0426 570  ALA B CA  
13193 C C   . ALA B 572  ? 0.4075 0.2874 0.3429 0.0478  -0.0415 -0.0461 570  ALA B C   
13194 O O   . ALA B 572  ? 0.4337 0.3169 0.3714 0.0542  -0.0406 -0.0483 570  ALA B O   
13195 C CB  . ALA B 572  ? 0.4079 0.2883 0.3474 0.0435  -0.0431 -0.0414 570  ALA B CB  
13196 N N   . ALA B 573  ? 0.3623 0.2333 0.2901 0.0450  -0.0435 -0.0468 571  ALA B N   
13197 C CA  . ALA B 573  ? 0.4042 0.2682 0.3257 0.0497  -0.0447 -0.0503 571  ALA B CA  
13198 C C   . ALA B 573  ? 0.4057 0.2780 0.3299 0.0506  -0.0414 -0.0519 571  ALA B C   
13199 O O   . ALA B 573  ? 0.4282 0.2963 0.3476 0.0550  -0.0419 -0.0551 571  ALA B O   
13200 C CB  . ALA B 573  ? 0.4384 0.2869 0.3493 0.0465  -0.0491 -0.0505 571  ALA B CB  
13201 N N   . MET B 574  ? 0.3734 0.2571 0.3045 0.0467  -0.0382 -0.0498 572  MET B N   
13202 C CA  . MET B 574  ? 0.3540 0.2456 0.2876 0.0473  -0.0351 -0.0509 572  MET B CA  
13203 C C   . MET B 574  ? 0.3770 0.2787 0.3169 0.0534  -0.0319 -0.0523 572  MET B C   
13204 O O   . MET B 574  ? 0.3779 0.2846 0.3235 0.0552  -0.0312 -0.0514 572  MET B O   
13205 C CB  . MET B 574  ? 0.3871 0.2868 0.3255 0.0408  -0.0331 -0.0479 572  MET B CB  
13206 C CG  . MET B 574  ? 0.3989 0.2908 0.3317 0.0344  -0.0358 -0.0464 572  MET B CG  
13207 S SD  . MET B 574  ? 0.4327 0.3349 0.3726 0.0276  -0.0335 -0.0424 572  MET B SD  
13208 C CE  . MET B 574  ? 0.3861 0.2781 0.3182 0.0207  -0.0372 -0.0412 572  MET B CE  
13209 N N   . LYS B 575  ? 0.3332 0.2382 0.2722 0.0563  -0.0300 -0.0546 573  LYS B N   
13210 C CA  . LYS B 575  ? 0.3591 0.2753 0.3047 0.0614  -0.0265 -0.0557 573  LYS B CA  
13211 C C   . LYS B 575  ? 0.2910 0.2197 0.2448 0.0575  -0.0229 -0.0530 573  LYS B C   
13212 O O   . LYS B 575  ? 0.3245 0.2561 0.2777 0.0547  -0.0214 -0.0527 573  LYS B O   
13213 C CB  . LYS B 575  ? 0.3426 0.2576 0.2836 0.0663  -0.0257 -0.0592 573  LYS B CB  
13214 C CG  . LYS B 575  ? 0.4023 0.3291 0.3497 0.0717  -0.0220 -0.0603 573  LYS B CG  
13215 C CD  . LYS B 575  ? 0.4966 0.4239 0.4397 0.0756  -0.0207 -0.0634 573  LYS B CD  
13216 C CE  . LYS B 575  ? 0.6584 0.5914 0.6040 0.0834  -0.0189 -0.0659 573  LYS B CE  
13217 N NZ  . LYS B 575  ? 0.6105 0.5570 0.5668 0.0836  -0.0158 -0.0637 573  LYS B NZ  
13218 N N   . TRP B 576  ? 0.3259 0.2617 0.2870 0.0574  -0.0216 -0.0511 574  TRP B N   
13219 C CA  . TRP B 576  ? 0.2944 0.2414 0.2633 0.0540  -0.0184 -0.0486 574  TRP B CA  
13220 C C   . TRP B 576  ? 0.2892 0.2469 0.2638 0.0582  -0.0150 -0.0495 574  TRP B C   
13221 O O   . TRP B 576  ? 0.3065 0.2664 0.2835 0.0630  -0.0149 -0.0507 574  TRP B O   
13222 C CB  . TRP B 576  ? 0.2665 0.2149 0.2399 0.0512  -0.0192 -0.0460 574  TRP B CB  
13223 C CG  . TRP B 576  ? 0.2883 0.2277 0.2568 0.0464  -0.0221 -0.0445 574  TRP B CG  
13224 C CD1 . TRP B 576  ? 0.3227 0.2527 0.2869 0.0466  -0.0255 -0.0445 574  TRP B CD1 
13225 C CD2 . TRP B 576  ? 0.2626 0.2020 0.2301 0.0406  -0.0220 -0.0426 574  TRP B CD2 
13226 N NE1 . TRP B 576  ? 0.3263 0.2506 0.2869 0.0409  -0.0274 -0.0427 574  TRP B NE1 
13227 C CE2 . TRP B 576  ? 0.3399 0.2703 0.3027 0.0373  -0.0252 -0.0415 574  TRP B CE2 
13228 C CE3 . TRP B 576  ? 0.2892 0.2357 0.2594 0.0380  -0.0194 -0.0417 574  TRP B CE3 
13229 C CZ2 . TRP B 576  ? 0.3589 0.2878 0.3198 0.0313  -0.0258 -0.0396 574  TRP B CZ2 
13230 C CZ3 . TRP B 576  ? 0.3456 0.2904 0.3140 0.0324  -0.0202 -0.0399 574  TRP B CZ3 
13231 C CH2 . TRP B 576  ? 0.3773 0.3138 0.3413 0.0291  -0.0233 -0.0388 574  TRP B CH2 
13232 N N   . THR B 577  ? 0.3045 0.2691 0.2812 0.0565  -0.0121 -0.0490 575  THR B N   
13233 C CA  . THR B 577  ? 0.2584 0.2338 0.2405 0.0596  -0.0086 -0.0494 575  THR B CA  
13234 C C   . THR B 577  ? 0.2750 0.2593 0.2633 0.0553  -0.0058 -0.0465 575  THR B C   
13235 O O   . THR B 577  ? 0.2732 0.2554 0.2605 0.0504  -0.0065 -0.0447 575  THR B O   
13236 C CB  . THR B 577  ? 0.3208 0.2954 0.2979 0.0631  -0.0076 -0.0522 575  THR B CB  
13237 O OG1 . THR B 577  ? 0.3451 0.3169 0.3182 0.0590  -0.0077 -0.0515 575  THR B OG1 
13238 C CG2 . THR B 577  ? 0.3244 0.2893 0.2948 0.0678  -0.0105 -0.0553 575  THR B CG2 
13239 N N   . ALA B 578  ? 0.2615 0.2560 0.2561 0.0572  -0.0028 -0.0462 576  ALA B N   
13240 C CA  . ALA B 578  ? 0.2395 0.2425 0.2394 0.0538  0.0000  -0.0437 576  ALA B CA  
13241 C C   . ALA B 578  ? 0.2530 0.2645 0.2553 0.0571  0.0032  -0.0446 576  ALA B C   
13242 O O   . ALA B 578  ? 0.2664 0.2817 0.2713 0.0613  0.0038  -0.0460 576  ALA B O   
13243 C CB  . ALA B 578  ? 0.2426 0.2496 0.2491 0.0515  0.0000  -0.0413 576  ALA B CB  
13244 N N   . LEU B 579  ? 0.2510 0.2654 0.2520 0.0553  0.0052  -0.0441 577  LEU B N   
13245 C CA  . LEU B 579  ? 0.2243 0.2461 0.2262 0.0581  0.0083  -0.0449 577  LEU B CA  
13246 C C   . LEU B 579  ? 0.2158 0.2456 0.2224 0.0544  0.0111  -0.0420 577  LEU B C   
13247 O O   . LEU B 579  ? 0.2252 0.2530 0.2323 0.0500  0.0104  -0.0399 577  LEU B O   
13248 C CB  . LEU B 579  ? 0.2704 0.2869 0.2643 0.0600  0.0079  -0.0474 577  LEU B CB  
13249 C CG  . LEU B 579  ? 0.3122 0.3177 0.2993 0.0624  0.0044  -0.0501 577  LEU B CG  
13250 C CD1 . LEU B 579  ? 0.3102 0.3103 0.2891 0.0633  0.0039  -0.0522 577  LEU B CD1 
13251 C CD2 . LEU B 579  ? 0.3048 0.3116 0.2935 0.0679  0.0042  -0.0521 577  LEU B CD2 
13252 N N   . PRO B 580  ? 0.2194 0.2581 0.2291 0.0562  0.0143  -0.0419 578  PRO B N   
13253 C CA  . PRO B 580  ? 0.1865 0.2314 0.1989 0.0528  0.0169  -0.0393 578  PRO B CA  
13254 C C   . PRO B 580  ? 0.2186 0.2591 0.2244 0.0516  0.0166  -0.0397 578  PRO B C   
13255 O O   . PRO B 580  ? 0.2607 0.3018 0.2623 0.0544  0.0178  -0.0416 578  PRO B O   
13256 C CB  . PRO B 580  ? 0.2164 0.2715 0.2328 0.0556  0.0202  -0.0394 578  PRO B CB  
13257 C CG  . PRO B 580  ? 0.2630 0.3182 0.2810 0.0600  0.0192  -0.0417 578  PRO B CG  
13258 C CD  . PRO B 580  ? 0.2319 0.2757 0.2428 0.0615  0.0158  -0.0440 578  PRO B CD  
13259 N N   . GLN B 581  ? 0.2076 0.2433 0.2121 0.0475  0.0149  -0.0381 579  GLN B N   
13260 C CA  . GLN B 581  ? 0.2340 0.2655 0.2325 0.0458  0.0142  -0.0383 579  GLN B CA  
13261 C C   . GLN B 581  ? 0.2679 0.3056 0.2685 0.0433  0.0167  -0.0357 579  GLN B C   
13262 O O   . GLN B 581  ? 0.2481 0.2863 0.2514 0.0396  0.0165  -0.0332 579  GLN B O   
13263 C CB  . GLN B 581  ? 0.2511 0.2747 0.2472 0.0427  0.0109  -0.0379 579  GLN B CB  
13264 C CG  . GLN B 581  ? 0.2553 0.2717 0.2487 0.0448  0.0082  -0.0401 579  GLN B CG  
13265 C CD  . GLN B 581  ? 0.3498 0.3604 0.3357 0.0476  0.0070  -0.0431 579  GLN B CD  
13266 O OE1 . GLN B 581  ? 0.3262 0.3386 0.3089 0.0480  0.0084  -0.0437 579  GLN B OE1 
13267 N NE2 . GLN B 581  ? 0.3909 0.3938 0.3733 0.0494  0.0043  -0.0451 579  GLN B NE2 
13268 N N   . LEU B 582  ? 0.2355 0.2780 0.2347 0.0455  0.0192  -0.0364 580  LEU B N   
13269 C CA  . LEU B 582  ? 0.2387 0.2866 0.2387 0.0433  0.0216  -0.0340 580  LEU B CA  
13270 C C   . LEU B 582  ? 0.2695 0.3127 0.2630 0.0418  0.0203  -0.0343 580  LEU B C   
13271 O O   . LEU B 582  ? 0.2854 0.3215 0.2737 0.0426  0.0178  -0.0366 580  LEU B O   
13272 C CB  . LEU B 582  ? 0.2592 0.3151 0.2606 0.0460  0.0250  -0.0343 580  LEU B CB  
13273 C CG  . LEU B 582  ? 0.3446 0.4079 0.3539 0.0455  0.0269  -0.0324 580  LEU B CG  
13274 C CD1 . LEU B 582  ? 0.3045 0.3661 0.3170 0.0475  0.0253  -0.0339 580  LEU B CD1 
13275 C CD2 . LEU B 582  ? 0.3577 0.4298 0.3683 0.0473  0.0305  -0.0321 580  LEU B CD2 
13276 N N   . ALA B 583  ? 0.2293 0.2761 0.2230 0.0395  0.0219  -0.0319 581  ALA B N   
13277 C CA  . ALA B 583  ? 0.2648 0.3079 0.2529 0.0379  0.0206  -0.0319 581  ALA B CA  
13278 C C   . ALA B 583  ? 0.3387 0.3792 0.3199 0.0409  0.0204  -0.0350 581  ALA B C   
13279 O O   . ALA B 583  ? 0.3705 0.4050 0.3461 0.0402  0.0180  -0.0362 581  ALA B O   
13280 C CB  . ALA B 583  ? 0.2777 0.3256 0.2671 0.0355  0.0224  -0.0287 581  ALA B CB  
13281 N N   . THR B 584  ? 0.2672 0.3121 0.2486 0.0445  0.0228  -0.0363 582  THR B N   
13282 C CA  . THR B 584  ? 0.2916 0.3346 0.2662 0.0479  0.0230  -0.0394 582  THR B CA  
13283 C C   . THR B 584  ? 0.3015 0.3382 0.2735 0.0512  0.0208  -0.0429 582  THR B C   
13284 O O   . THR B 584  ? 0.3064 0.3409 0.2725 0.0547  0.0209  -0.0460 582  THR B O   
13285 C CB  . THR B 584  ? 0.2808 0.3324 0.2567 0.0504  0.0270  -0.0392 582  THR B CB  
13286 O OG1 . THR B 584  ? 0.3414 0.3986 0.3246 0.0511  0.0286  -0.0382 582  THR B OG1 
13287 C CG2 . THR B 584  ? 0.3768 0.4329 0.3526 0.0474  0.0288  -0.0361 582  THR B CG2 
13288 N N   . GLY B 585  ? 0.2880 0.3215 0.2637 0.0502  0.0189  -0.0426 583  GLY B N   
13289 C CA  . GLY B 585  ? 0.2879 0.3149 0.2610 0.0531  0.0165  -0.0456 583  GLY B CA  
13290 C C   . GLY B 585  ? 0.2874 0.3183 0.2671 0.0550  0.0174  -0.0454 583  GLY B C   
13291 O O   . GLY B 585  ? 0.2924 0.3315 0.2786 0.0541  0.0200  -0.0431 583  GLY B O   
13292 N N   . PRO B 586  ? 0.2693 0.2941 0.2472 0.0576  0.0151  -0.0478 584  PRO B N   
13293 C CA  . PRO B 586  ? 0.2621 0.2905 0.2462 0.0597  0.0156  -0.0478 584  PRO B CA  
13294 C C   . PRO B 586  ? 0.2864 0.3234 0.2728 0.0641  0.0189  -0.0488 584  PRO B C   
13295 O O   . PRO B 586  ? 0.3115 0.3482 0.2927 0.0678  0.0198  -0.0514 584  PRO B O   
13296 C CB  . PRO B 586  ? 0.3190 0.3373 0.2988 0.0616  0.0119  -0.0503 584  PRO B CB  
13297 C CG  . PRO B 586  ? 0.3556 0.3667 0.3264 0.0626  0.0105  -0.0527 584  PRO B CG  
13298 C CD  . PRO B 586  ? 0.3029 0.3169 0.2731 0.0585  0.0117  -0.0505 584  PRO B CD  
13299 N N   . ALA B 587  ? 0.2659 0.3111 0.2603 0.0637  0.0208  -0.0469 585  ALA B N   
13300 C CA  . ALA B 587  ? 0.2637 0.3188 0.2618 0.0672  0.0241  -0.0474 585  ALA B CA  
13301 C C   . ALA B 587  ? 0.2237 0.2785 0.2239 0.0717  0.0230  -0.0496 585  ALA B C   
13302 O O   . ALA B 587  ? 0.2761 0.3251 0.2774 0.0709  0.0200  -0.0495 585  ALA B O   
13303 C CB  . ALA B 587  ? 0.3066 0.3713 0.3123 0.0636  0.0268  -0.0437 585  ALA B CB  
13304 N N   . ALA B 588  ? 0.2840 0.3456 0.2847 0.0767  0.0253  -0.0515 586  ALA B N   
13305 C CA  . ALA B 588  ? 0.2592 0.3228 0.2629 0.0815  0.0247  -0.0534 586  ALA B CA  
13306 C C   . ALA B 588  ? 0.2737 0.3453 0.2870 0.0791  0.0255  -0.0506 586  ALA B C   
13307 O O   . ALA B 588  ? 0.3005 0.3784 0.3184 0.0747  0.0276  -0.0475 586  ALA B O   
13308 C CB  . ALA B 588  ? 0.2879 0.3580 0.2899 0.0875  0.0273  -0.0561 586  ALA B CB  
13309 N N   . GLY B 589  ? 0.2930 0.3638 0.3090 0.0821  0.0237  -0.0519 587  GLY B N   
13310 C CA  . GLY B 589  ? 0.2661 0.3446 0.2911 0.0804  0.0242  -0.0496 587  GLY B CA  
13311 C C   . GLY B 589  ? 0.3454 0.4220 0.3719 0.0849  0.0219  -0.0517 587  GLY B C   
13312 O O   . GLY B 589  ? 0.3431 0.4131 0.3637 0.0898  0.0201  -0.0549 587  GLY B O   
13313 N N   . GLU B 590  ? 0.3227 0.4050 0.3569 0.0832  0.0216  -0.0497 588  GLU B N   
13314 C CA  . GLU B 590  ? 0.3176 0.3989 0.3540 0.0873  0.0192  -0.0513 588  GLU B CA  
13315 C C   . GLU B 590  ? 0.2897 0.3574 0.3214 0.0857  0.0149  -0.0515 588  GLU B C   
13316 O O   . GLU B 590  ? 0.2773 0.3415 0.3099 0.0801  0.0140  -0.0491 588  GLU B O   
13317 C CB  . GLU B 590  ? 0.3473 0.4397 0.3935 0.0857  0.0203  -0.0491 588  GLU B CB  
13318 N N   . THR B 591  ? 0.3274 0.3875 0.3540 0.0908  0.0123  -0.0545 589  THR B N   
13319 C CA  . THR B 591  ? 0.3312 0.3775 0.3520 0.0895  0.0083  -0.0549 589  THR B CA  
13320 C C   . THR B 591  ? 0.3353 0.3800 0.3591 0.0918  0.0055  -0.0552 589  THR B C   
13321 O O   . THR B 591  ? 0.3520 0.4022 0.3783 0.0975  0.0057  -0.0570 589  THR B O   
13322 C CB  . THR B 591  ? 0.3201 0.3561 0.3312 0.0929  0.0068  -0.0580 589  THR B CB  
13323 O OG1 . THR B 591  ? 0.3659 0.4032 0.3741 0.0903  0.0092  -0.0576 589  THR B OG1 
13324 C CG2 . THR B 591  ? 0.3520 0.3738 0.3571 0.0909  0.0025  -0.0581 589  THR B CG2 
13325 N N   . ARG B 592  ? 0.3090 0.3467 0.3324 0.0876  0.0028  -0.0534 590  ARG B N   
13326 C CA  . ARG B 592  ? 0.3506 0.3848 0.3753 0.0895  -0.0004 -0.0535 590  ARG B CA  
13327 C C   . ARG B 592  ? 0.3504 0.3708 0.3687 0.0864  -0.0040 -0.0530 590  ARG B C   
13328 O O   . ARG B 592  ? 0.3208 0.3364 0.3356 0.0817  -0.0038 -0.0518 590  ARG B O   
13329 C CB  . ARG B 592  ? 0.3607 0.4049 0.3948 0.0870  0.0005  -0.0511 590  ARG B CB  
13330 C CG  . ARG B 592  ? 0.3858 0.4292 0.4216 0.0798  0.0009  -0.0480 590  ARG B CG  
13331 C CD  . ARG B 592  ? 0.4250 0.4740 0.4680 0.0775  0.0003  -0.0459 590  ARG B CD  
13332 N NE  . ARG B 592  ? 0.4074 0.4570 0.4525 0.0710  0.0013  -0.0430 590  ARG B NE  
13333 C CZ  . ARG B 592  ? 0.4366 0.4779 0.4787 0.0672  -0.0009 -0.0418 590  ARG B CZ  
13334 N NH1 . ARG B 592  ? 0.3739 0.4053 0.4108 0.0687  -0.0042 -0.0428 590  ARG B NH1 
13335 N NH2 . ARG B 592  ? 0.4294 0.4723 0.4735 0.0618  0.0002  -0.0393 590  ARG B NH2 
13336 N N   . THR B 593  ? 0.3396 0.3541 0.3567 0.0888  -0.0073 -0.0536 591  THR B N   
13337 C CA  . THR B 593  ? 0.3271 0.3288 0.3382 0.0859  -0.0108 -0.0529 591  THR B CA  
13338 C C   . THR B 593  ? 0.3375 0.3412 0.3531 0.0798  -0.0110 -0.0496 591  THR B C   
13339 O O   . THR B 593  ? 0.3277 0.3411 0.3510 0.0791  -0.0096 -0.0483 591  THR B O   
13340 C CB  . THR B 593  ? 0.3586 0.3526 0.3660 0.0909  -0.0145 -0.0547 591  THR B CB  
13341 O OG1 . THR B 593  ? 0.4026 0.4052 0.4174 0.0933  -0.0144 -0.0542 591  THR B OG1 
13342 C CG2 . THR B 593  ? 0.4538 0.4438 0.4553 0.0971  -0.0147 -0.0582 591  THR B CG2 
13343 N N   . VAL B 594  ? 0.2818 0.2761 0.2924 0.0754  -0.0129 -0.0485 592  VAL B N   
13344 C CA  . VAL B 594  ? 0.2747 0.2686 0.2878 0.0700  -0.0136 -0.0456 592  VAL B CA  
13345 C C   . VAL B 594  ? 0.3183 0.3023 0.3271 0.0707  -0.0176 -0.0457 592  VAL B C   
13346 O O   . VAL B 594  ? 0.3070 0.2803 0.3081 0.0714  -0.0199 -0.0468 592  VAL B O   
13347 C CB  . VAL B 594  ? 0.2868 0.2785 0.2975 0.0643  -0.0124 -0.0441 592  VAL B CB  
13348 C CG1 . VAL B 594  ? 0.3031 0.2944 0.3162 0.0591  -0.0131 -0.0413 592  VAL B CG1 
13349 C CG2 . VAL B 594  ? 0.3484 0.3494 0.3628 0.0640  -0.0086 -0.0440 592  VAL B CG2 
13350 N N   . LEU B 595  ? 0.3039 0.2910 0.3173 0.0706  -0.0186 -0.0445 593  LEU B N   
13351 C CA  . LEU B 595  ? 0.3289 0.3076 0.3387 0.0719  -0.0224 -0.0445 593  LEU B CA  
13352 C C   . LEU B 595  ? 0.2773 0.2527 0.2868 0.0661  -0.0235 -0.0417 593  LEU B C   
13353 O O   . LEU B 595  ? 0.3001 0.2826 0.3148 0.0624  -0.0214 -0.0399 593  LEU B O   
13354 C CB  . LEU B 595  ? 0.3048 0.2893 0.3195 0.0769  -0.0231 -0.0453 593  LEU B CB  
13355 C CG  . LEU B 595  ? 0.3350 0.3250 0.3512 0.0832  -0.0217 -0.0480 593  LEU B CG  
13356 C CD1 . LEU B 595  ? 0.4066 0.4038 0.4288 0.0875  -0.0225 -0.0485 593  LEU B CD1 
13357 C CD2 . LEU B 595  ? 0.3184 0.2974 0.3257 0.0868  -0.0236 -0.0504 593  LEU B CD2 
13358 N N   . ASN B 596  ? 0.2676 0.2320 0.2707 0.0656  -0.0269 -0.0415 594  ASN B N   
13359 C CA  . ASN B 596  ? 0.3050 0.2658 0.3071 0.0606  -0.0282 -0.0390 594  ASN B CA  
13360 C C   . ASN B 596  ? 0.2466 0.2143 0.2551 0.0611  -0.0284 -0.0379 594  ASN B C   
13361 O O   . ASN B 596  ? 0.2663 0.2337 0.2754 0.0657  -0.0302 -0.0390 594  ASN B O   
13362 C CB  . ASN B 596  ? 0.2874 0.2348 0.2808 0.0605  -0.0319 -0.0390 594  ASN B CB  
13363 C CG  . ASN B 596  ? 0.2879 0.2310 0.2791 0.0549  -0.0332 -0.0364 594  ASN B CG  
13364 O OD1 . ASN B 596  ? 0.2941 0.2433 0.2903 0.0525  -0.0322 -0.0347 594  ASN B OD1 
13365 N ND2 . ASN B 596  ? 0.2911 0.2232 0.2744 0.0527  -0.0354 -0.0360 594  ASN B ND2 
13366 N N   . PRO B 597  ? 0.2456 0.2197 0.2590 0.0569  -0.0266 -0.0360 595  PRO B N   
13367 C CA  . PRO B 597  ? 0.2491 0.2294 0.2683 0.0572  -0.0270 -0.0352 595  PRO B CA  
13368 C C   . PRO B 597  ? 0.2694 0.2422 0.2848 0.0578  -0.0307 -0.0345 595  PRO B C   
13369 O O   . PRO B 597  ? 0.2720 0.2488 0.2913 0.0600  -0.0318 -0.0345 595  PRO B O   
13370 C CB  . PRO B 597  ? 0.2597 0.2456 0.2828 0.0520  -0.0246 -0.0332 595  PRO B CB  
13371 C CG  . PRO B 597  ? 0.2578 0.2380 0.2757 0.0485  -0.0239 -0.0326 595  PRO B CG  
13372 C CD  . PRO B 597  ? 0.2444 0.2206 0.2582 0.0519  -0.0241 -0.0347 595  PRO B CD  
13373 N N   . GLY B 598  ? 0.2595 0.2218 0.2674 0.0557  -0.0326 -0.0339 596  GLY B N   
13374 C CA  . GLY B 598  ? 0.2636 0.2182 0.2672 0.0560  -0.0362 -0.0331 596  GLY B CA  
13375 C C   . GLY B 598  ? 0.3019 0.2501 0.3015 0.0617  -0.0390 -0.0349 596  GLY B C   
13376 O O   . GLY B 598  ? 0.3267 0.2687 0.3229 0.0628  -0.0422 -0.0343 596  GLY B O   
13377 N N   . ASP B 599  ? 0.2692 0.2188 0.2690 0.0654  -0.0378 -0.0371 597  ASP B N   
13378 C CA  . ASP B 599  ? 0.3178 0.2614 0.3135 0.0714  -0.0404 -0.0392 597  ASP B CA  
13379 C C   . ASP B 599  ? 0.3185 0.2676 0.3166 0.0753  -0.0380 -0.0416 597  ASP B C   
13380 O O   . ASP B 599  ? 0.3013 0.2461 0.2951 0.0742  -0.0371 -0.0424 597  ASP B O   
13381 C CB  . ASP B 599  ? 0.2941 0.2229 0.2798 0.0701  -0.0435 -0.0388 597  ASP B CB  
13382 C CG  . ASP B 599  ? 0.3612 0.2820 0.3417 0.0764  -0.0467 -0.0408 597  ASP B CG  
13383 O OD1 . ASP B 599  ? 0.3498 0.2768 0.3343 0.0822  -0.0460 -0.0430 597  ASP B OD1 
13384 O OD2 . ASP B 599  ? 0.4054 0.3136 0.3778 0.0754  -0.0500 -0.0402 597  ASP B OD2 
13385 N N   . HIS B 600  ? 0.2900 0.2491 0.2949 0.0797  -0.0369 -0.0428 598  HIS B N   
13386 C CA  . HIS B 600  ? 0.3109 0.2772 0.3188 0.0831  -0.0340 -0.0449 598  HIS B CA  
13387 C C   . HIS B 600  ? 0.3013 0.2588 0.3021 0.0882  -0.0356 -0.0475 598  HIS B C   
13388 O O   . HIS B 600  ? 0.3684 0.3303 0.3700 0.0907  -0.0333 -0.0494 598  HIS B O   
13389 C CB  . HIS B 600  ? 0.3079 0.2875 0.3250 0.0864  -0.0326 -0.0454 598  HIS B CB  
13390 C CG  . HIS B 600  ? 0.3277 0.3170 0.3521 0.0812  -0.0302 -0.0432 598  HIS B CG  
13391 N ND1 . HIS B 600  ? 0.3702 0.3719 0.4032 0.0826  -0.0288 -0.0430 598  HIS B ND1 
13392 C CD2 . HIS B 600  ? 0.2724 0.2605 0.2964 0.0748  -0.0290 -0.0410 598  HIS B CD2 
13393 C CE1 . HIS B 600  ? 0.3716 0.3785 0.4090 0.0771  -0.0270 -0.0410 598  HIS B CE1 
13394 N NE2 . HIS B 600  ? 0.3201 0.3190 0.3521 0.0725  -0.0271 -0.0398 598  HIS B NE2 
13395 N N   . ARG B 601  ? 0.3288 0.2738 0.3221 0.0896  -0.0396 -0.0477 599  ARG B N   
13396 C CA  . ARG B 601  ? 0.3198 0.2545 0.3050 0.0939  -0.0415 -0.0501 599  ARG B CA  
13397 C C   . ARG B 601  ? 0.3746 0.3024 0.3538 0.0895  -0.0406 -0.0500 599  ARG B C   
13398 O O   . ARG B 601  ? 0.4005 0.3218 0.3739 0.0927  -0.0413 -0.0524 599  ARG B O   
13399 C CB  . ARG B 601  ? 0.4046 0.3271 0.3832 0.0964  -0.0463 -0.0501 599  ARG B CB  
13400 C CG  . ARG B 601  ? 0.3993 0.3279 0.3832 0.1012  -0.0477 -0.0502 599  ARG B CG  
13401 C CD  . ARG B 601  ? 0.4485 0.3645 0.4255 0.1023  -0.0525 -0.0494 599  ARG B CD  
13402 N NE  . ARG B 601  ? 0.4075 0.3180 0.3818 0.0947  -0.0533 -0.0463 599  ARG B NE  
13403 C CZ  . ARG B 601  ? 0.4605 0.3593 0.4280 0.0936  -0.0572 -0.0448 599  ARG B CZ  
13404 N NH1 . ARG B 601  ? 0.4789 0.3698 0.4417 0.0996  -0.0609 -0.0461 599  ARG B NH1 
13405 N NH2 . ARG B 601  ? 0.4508 0.3460 0.4162 0.0865  -0.0574 -0.0420 599  ARG B NH2 
13406 N N   . ASP B 602  ? 0.3351 0.2643 0.3157 0.0823  -0.0394 -0.0475 600  ASP B N   
13407 C CA  . ASP B 602  ? 0.3352 0.2587 0.3107 0.0774  -0.0387 -0.0470 600  ASP B CA  
13408 C C   . ASP B 602  ? 0.3402 0.2746 0.3211 0.0768  -0.0344 -0.0477 600  ASP B C   
13409 O O   . ASP B 602  ? 0.3329 0.2771 0.3207 0.0733  -0.0317 -0.0459 600  ASP B O   
13410 C CB  . ASP B 602  ? 0.3783 0.2981 0.3525 0.0704  -0.0396 -0.0438 600  ASP B CB  
13411 C CG  . ASP B 602  ? 0.3942 0.3091 0.3637 0.0650  -0.0390 -0.0431 600  ASP B CG  
13412 O OD1 . ASP B 602  ? 0.4088 0.3182 0.3731 0.0669  -0.0394 -0.0452 600  ASP B OD1 
13413 O OD2 . ASP B 602  ? 0.3886 0.3055 0.3597 0.0591  -0.0381 -0.0406 600  ASP B OD2 
13414 N N   . VAL B 603  ? 0.3605 0.2931 0.3380 0.0805  -0.0337 -0.0503 601  VAL B N   
13415 C CA  . VAL B 603  ? 0.3209 0.2630 0.3025 0.0801  -0.0297 -0.0510 601  VAL B CA  
13416 C C   . VAL B 603  ? 0.3395 0.2777 0.3175 0.0737  -0.0291 -0.0496 601  VAL B C   
13417 O O   . VAL B 603  ? 0.3777 0.3048 0.3475 0.0727  -0.0313 -0.0503 601  VAL B O   
13418 C CB  . VAL B 603  ? 0.3401 0.2821 0.3190 0.0868  -0.0292 -0.0545 601  VAL B CB  
13419 C CG1 . VAL B 603  ? 0.3570 0.3085 0.3394 0.0859  -0.0251 -0.0549 601  VAL B CG1 
13420 C CG2 . VAL B 603  ? 0.3579 0.3049 0.3409 0.0936  -0.0298 -0.0559 601  VAL B CG2 
13421 N N   . VAL B 604  ? 0.3298 0.2772 0.3140 0.0692  -0.0262 -0.0475 602  VAL B N   
13422 C CA  . VAL B 604  ? 0.3204 0.2652 0.3020 0.0632  -0.0256 -0.0460 602  VAL B CA  
13423 C C   . VAL B 604  ? 0.2957 0.2428 0.2757 0.0639  -0.0234 -0.0476 602  VAL B C   
13424 O O   . VAL B 604  ? 0.3173 0.2576 0.2913 0.0610  -0.0243 -0.0477 602  VAL B O   
13425 C CB  . VAL B 604  ? 0.2674 0.2200 0.2555 0.0582  -0.0238 -0.0430 602  VAL B CB  
13426 C CG1 . VAL B 604  ? 0.2516 0.2015 0.2370 0.0522  -0.0234 -0.0413 602  VAL B CG1 
13427 C CG2 . VAL B 604  ? 0.2859 0.2364 0.2753 0.0580  -0.0260 -0.0416 602  VAL B CG2 
13428 N N   . GLY B 605  ? 0.2935 0.2501 0.2784 0.0677  -0.0205 -0.0488 603  GLY B N   
13429 C CA  . GLY B 605  ? 0.3265 0.2863 0.3102 0.0682  -0.0181 -0.0502 603  GLY B CA  
13430 C C   . GLY B 605  ? 0.3089 0.2806 0.2990 0.0723  -0.0149 -0.0511 603  GLY B C   
13431 O O   . GLY B 605  ? 0.3199 0.2960 0.3144 0.0759  -0.0150 -0.0515 603  GLY B O   
13432 N N   . SER B 606  ? 0.2934 0.2707 0.2843 0.0716  -0.0120 -0.0514 604  SER B N   
13433 C CA  . SER B 606  ? 0.2904 0.2786 0.2862 0.0755  -0.0087 -0.0525 604  SER B CA  
13434 C C   . SER B 606  ? 0.2939 0.2907 0.2942 0.0711  -0.0053 -0.0503 604  SER B C   
13435 O O   . SER B 606  ? 0.3242 0.3173 0.3209 0.0672  -0.0053 -0.0496 604  SER B O   
13436 C CB  . SER B 606  ? 0.3868 0.3713 0.3765 0.0809  -0.0088 -0.0559 604  SER B CB  
13437 O OG  . SER B 606  ? 0.4599 0.4553 0.4534 0.0832  -0.0050 -0.0566 604  SER B OG  
13438 N N   . VAL B 607  ? 0.2810 0.2894 0.2892 0.0717  -0.0026 -0.0493 605  VAL B N   
13439 C CA  . VAL B 607  ? 0.2326 0.2493 0.2451 0.0679  0.0006  -0.0472 605  VAL B CA  
13440 C C   . VAL B 607  ? 0.2503 0.2766 0.2655 0.0716  0.0039  -0.0484 605  VAL B C   
13441 O O   . VAL B 607  ? 0.2668 0.2983 0.2854 0.0760  0.0043  -0.0496 605  VAL B O   
13442 C CB  . VAL B 607  ? 0.2527 0.2745 0.2721 0.0638  0.0010  -0.0442 605  VAL B CB  
13443 C CG1 . VAL B 607  ? 0.2596 0.2870 0.2848 0.0669  0.0007  -0.0445 605  VAL B CG1 
13444 C CG2 . VAL B 607  ? 0.2326 0.2622 0.2557 0.0602  0.0042  -0.0421 605  VAL B CG2 
13445 N N   . THR B 608  ? 0.2290 0.2579 0.2426 0.0699  0.0063  -0.0480 606  THR B N   
13446 C CA  . THR B 608  ? 0.2529 0.2920 0.2694 0.0722  0.0099  -0.0485 606  THR B CA  
13447 C C   . THR B 608  ? 0.2363 0.2837 0.2591 0.0674  0.0124  -0.0452 606  THR B C   
13448 O O   . THR B 608  ? 0.2485 0.2929 0.2697 0.0628  0.0123  -0.0434 606  THR B O   
13449 C CB  . THR B 608  ? 0.2873 0.3227 0.2965 0.0739  0.0106  -0.0505 606  THR B CB  
13450 O OG1 . THR B 608  ? 0.2989 0.3260 0.3020 0.0787  0.0081  -0.0537 606  THR B OG1 
13451 C CG2 . THR B 608  ? 0.2648 0.3112 0.2768 0.0759  0.0147  -0.0507 606  THR B CG2 
13452 N N   . GLU B 609  ? 0.2481 0.3058 0.2781 0.0684  0.0144  -0.0443 607  GLU B N   
13453 C CA  . GLU B 609  ? 0.2786 0.3428 0.3146 0.0635  0.0161  -0.0411 607  GLU B CA  
13454 C C   . GLU B 609  ? 0.2415 0.3138 0.2785 0.0628  0.0199  -0.0402 607  GLU B C   
13455 O O   . GLU B 609  ? 0.2670 0.3427 0.3020 0.0668  0.0216  -0.0421 607  GLU B O   
13456 C CB  . GLU B 609  ? 0.2836 0.3535 0.3269 0.0637  0.0156  -0.0402 607  GLU B CB  
13457 C CG  . GLU B 609  ? 0.3259 0.3871 0.3678 0.0625  0.0119  -0.0401 607  GLU B CG  
13458 C CD  . GLU B 609  ? 0.3848 0.4503 0.4331 0.0629  0.0108  -0.0394 607  GLU B CD  
13459 O OE1 . GLU B 609  ? 0.4242 0.4991 0.4776 0.0657  0.0124  -0.0399 607  GLU B OE1 
13460 O OE2 . GLU B 609  ? 0.3708 0.4307 0.4190 0.0605  0.0084  -0.0384 607  GLU B OE2 
13461 N N   . THR B 610  ? 0.2623 0.3371 0.3020 0.0578  0.0210  -0.0372 608  THR B N   
13462 C CA  . THR B 610  ? 0.2419 0.3219 0.2811 0.0560  0.0241  -0.0358 608  THR B CA  
13463 C C   . THR B 610  ? 0.2283 0.3204 0.2742 0.0563  0.0272  -0.0346 608  THR B C   
13464 O O   . THR B 610  ? 0.2515 0.3477 0.3036 0.0544  0.0269  -0.0330 608  THR B O   
13465 C CB  . THR B 610  ? 0.2383 0.3148 0.2771 0.0505  0.0238  -0.0331 608  THR B CB  
13466 O OG1 . THR B 610  ? 0.2273 0.2934 0.2610 0.0497  0.0208  -0.0339 608  THR B OG1 
13467 C CG2 . THR B 610  ? 0.2328 0.3129 0.2695 0.0490  0.0265  -0.0318 608  THR B CG2 
13468 N N   . SER B 611  ? 0.2247 0.3227 0.2691 0.0585  0.0300  -0.0354 609  SER B N   
13469 C CA  . SER B 611  ? 0.2516 0.3617 0.3022 0.0579  0.0332  -0.0336 609  SER B CA  
13470 C C   . SER B 611  ? 0.2815 0.3932 0.3343 0.0518  0.0344  -0.0299 609  SER B C   
13471 O O   . SER B 611  ? 0.2406 0.3454 0.2890 0.0492  0.0336  -0.0290 609  SER B O   
13472 C CB  . SER B 611  ? 0.2619 0.3780 0.3098 0.0617  0.0362  -0.0352 609  SER B CB  
13473 O OG  . SER B 611  ? 0.2724 0.3855 0.3149 0.0596  0.0374  -0.0344 609  SER B OG  
13474 N N   . GLU B 612  ? 0.2698 0.3908 0.3296 0.0497  0.0361  -0.0277 610  GLU B N   
13475 C CA  . GLU B 612  ? 0.2703 0.3925 0.3319 0.0440  0.0371  -0.0241 610  GLU B CA  
13476 C C   . GLU B 612  ? 0.2240 0.3469 0.2807 0.0432  0.0396  -0.0232 610  GLU B C   
13477 O O   . GLU B 612  ? 0.2638 0.3822 0.3183 0.0394  0.0393  -0.0210 610  GLU B O   
13478 C CB  . GLU B 612  ? 0.3147 0.4468 0.3843 0.0417  0.0385  -0.0219 610  GLU B CB  
13479 C CG  . GLU B 612  ? 0.3949 0.5253 0.4691 0.0413  0.0356  -0.0222 610  GLU B CG  
13480 C CD  . GLU B 612  ? 0.5087 0.6488 0.5908 0.0386  0.0367  -0.0200 610  GLU B CD  
13481 O OE1 . GLU B 612  ? 0.6221 0.7666 0.7058 0.0346  0.0388  -0.0172 610  GLU B OE1 
13482 O OE2 . GLU B 612  ? 0.5154 0.6587 0.6021 0.0404  0.0353  -0.0211 610  GLU B OE2 
13483 N N   . GLU B 613  ? 0.2916 0.4199 0.3464 0.0470  0.0420  -0.0249 611  GLU B N   
13484 C CA  . GLU B 613  ? 0.2510 0.3794 0.3003 0.0468  0.0441  -0.0244 611  GLU B CA  
13485 C C   . GLU B 613  ? 0.2726 0.3895 0.3146 0.0465  0.0418  -0.0254 611  GLU B C   
13486 O O   . GLU B 613  ? 0.2704 0.3848 0.3091 0.0436  0.0423  -0.0235 611  GLU B O   
13487 C CB  . GLU B 613  ? 0.3303 0.4660 0.3781 0.0517  0.0468  -0.0267 611  GLU B CB  
13488 N N   . ASP B 614  ? 0.2580 0.3677 0.2974 0.0495  0.0390  -0.0283 612  ASP B N   
13489 C CA  . ASP B 614  ? 0.2642 0.3634 0.2969 0.0490  0.0366  -0.0293 612  ASP B CA  
13490 C C   . ASP B 614  ? 0.2377 0.3317 0.2720 0.0443  0.0346  -0.0268 612  ASP B C   
13491 O O   . ASP B 614  ? 0.2377 0.3256 0.2673 0.0424  0.0336  -0.0262 612  ASP B O   
13492 C CB  . ASP B 614  ? 0.2545 0.3472 0.2836 0.0533  0.0341  -0.0330 612  ASP B CB  
13493 C CG  . ASP B 614  ? 0.3151 0.4098 0.3395 0.0581  0.0357  -0.0358 612  ASP B CG  
13494 O OD1 . ASP B 614  ? 0.3337 0.4320 0.3554 0.0576  0.0381  -0.0351 612  ASP B OD1 
13495 O OD2 . ASP B 614  ? 0.3286 0.4211 0.3517 0.0626  0.0344  -0.0389 612  ASP B OD2 
13496 N N   . ALA B 615  ? 0.2236 0.3200 0.2642 0.0424  0.0340  -0.0253 613  ALA B N   
13497 C CA  . ALA B 615  ? 0.2060 0.2981 0.2480 0.0380  0.0325  -0.0229 613  ALA B CA  
13498 C C   . ALA B 615  ? 0.2399 0.3343 0.2810 0.0346  0.0344  -0.0199 613  ALA B C   
13499 O O   . ALA B 615  ? 0.2143 0.3029 0.2522 0.0323  0.0333  -0.0188 613  ALA B O   
13500 C CB  . ALA B 615  ? 0.2447 0.3395 0.2934 0.0367  0.0316  -0.0220 613  ALA B CB  
13501 N N   . ARG B 616  ? 0.2446 0.3475 0.2883 0.0344  0.0374  -0.0186 614  ARG B N   
13502 C CA  . ARG B 616  ? 0.2283 0.3332 0.2707 0.0312  0.0394  -0.0157 614  ARG B CA  
13503 C C   . ARG B 616  ? 0.2356 0.3366 0.2707 0.0324  0.0396  -0.0165 614  ARG B C   
13504 O O   . ARG B 616  ? 0.2468 0.3443 0.2792 0.0297  0.0393  -0.0145 614  ARG B O   
13505 C CB  . ARG B 616  ? 0.2554 0.3708 0.3019 0.0307  0.0427  -0.0141 614  ARG B CB  
13506 C CG  . ARG B 616  ? 0.3047 0.4235 0.3584 0.0275  0.0423  -0.0120 614  ARG B CG  
13507 C CD  . ARG B 616  ? 0.3781 0.5073 0.4357 0.0259  0.0455  -0.0098 614  ARG B CD  
13508 N NE  . ARG B 616  ? 0.4458 0.5828 0.5057 0.0300  0.0471  -0.0122 614  ARG B NE  
13509 C CZ  . ARG B 616  ? 0.4560 0.5964 0.5213 0.0315  0.0461  -0.0135 614  ARG B CZ  
13510 N NH1 . ARG B 616  ? 0.4298 0.5669 0.4989 0.0289  0.0437  -0.0126 614  ARG B NH1 
13511 N NH2 . ARG B 616  ? 0.3871 0.5343 0.4539 0.0359  0.0475  -0.0159 614  ARG B NH2 
13512 N N   . ARG B 617  ? 0.2379 0.3392 0.2695 0.0366  0.0400  -0.0196 615  ARG B N   
13513 C CA  . ARG B 617  ? 0.2664 0.3634 0.2906 0.0377  0.0398  -0.0208 615  ARG B CA  
13514 C C   . ARG B 617  ? 0.2536 0.3412 0.2746 0.0361  0.0366  -0.0209 615  ARG B C   
13515 O O   . ARG B 617  ? 0.2393 0.3240 0.2560 0.0346  0.0364  -0.0198 615  ARG B O   
13516 C CB  . ARG B 617  ? 0.2809 0.3787 0.3017 0.0428  0.0403  -0.0245 615  ARG B CB  
13517 C CG  . ARG B 617  ? 0.2876 0.3809 0.3002 0.0441  0.0401  -0.0259 615  ARG B CG  
13518 C CD  . ARG B 617  ? 0.3975 0.4936 0.4066 0.0490  0.0415  -0.0292 615  ARG B CD  
13519 N NE  . ARG B 617  ? 0.4484 0.5401 0.4571 0.0526  0.0393  -0.0326 615  ARG B NE  
13520 C CZ  . ARG B 617  ? 0.5361 0.6191 0.5387 0.0543  0.0366  -0.0353 615  ARG B CZ  
13521 N NH1 . ARG B 617  ? 0.5087 0.5866 0.5053 0.0527  0.0357  -0.0350 615  ARG B NH1 
13522 N NH2 . ARG B 617  ? 0.5480 0.6270 0.5501 0.0577  0.0347  -0.0382 615  ARG B NH2 
13523 N N   . ALA B 618  ? 0.2268 0.3100 0.2500 0.0364  0.0340  -0.0220 616  ALA B N   
13524 C CA  . ALA B 618  ? 0.2194 0.2946 0.2402 0.0346  0.0311  -0.0220 616  ALA B CA  
13525 C C   . ALA B 618  ? 0.2062 0.2811 0.2282 0.0306  0.0312  -0.0186 616  ALA B C   
13526 O O   . ALA B 618  ? 0.2236 0.2939 0.2417 0.0293  0.0299  -0.0181 616  ALA B O   
13527 C CB  . ALA B 618  ? 0.2148 0.2863 0.2383 0.0352  0.0286  -0.0234 616  ALA B CB  
13528 N N   . VAL B 619  ? 0.2270 0.3066 0.2543 0.0286  0.0326  -0.0162 617  VAL B N   
13529 C CA  . VAL B 619  ? 0.2111 0.2895 0.2392 0.0251  0.0324  -0.0131 617  VAL B CA  
13530 C C   . VAL B 619  ? 0.2338 0.3134 0.2575 0.0245  0.0340  -0.0117 617  VAL B C   
13531 O O   . VAL B 619  ? 0.2483 0.3241 0.2694 0.0228  0.0330  -0.0102 617  VAL B O   
13532 C CB  . VAL B 619  ? 0.2120 0.2945 0.2463 0.0229  0.0333  -0.0110 617  VAL B CB  
13533 C CG1 . VAL B 619  ? 0.2493 0.3296 0.2837 0.0195  0.0330  -0.0078 617  VAL B CG1 
13534 C CG2 . VAL B 619  ? 0.2541 0.3349 0.2923 0.0235  0.0314  -0.0124 617  VAL B CG2 
13535 N N   . ARG B 620  ? 0.2486 0.3337 0.2711 0.0261  0.0366  -0.0122 618  ARG B N   
13536 C CA  . ARG B 620  ? 0.2526 0.3386 0.2701 0.0257  0.0381  -0.0109 618  ARG B CA  
13537 C C   . ARG B 620  ? 0.2351 0.3151 0.2465 0.0270  0.0360  -0.0127 618  ARG B C   
13538 O O   . ARG B 620  ? 0.2712 0.3491 0.2791 0.0255  0.0357  -0.0111 618  ARG B O   
13539 C CB  . ARG B 620  ? 0.2806 0.3739 0.2977 0.0276  0.0413  -0.0113 618  ARG B CB  
13540 C CG  . ARG B 620  ? 0.3573 0.4577 0.3803 0.0257  0.0435  -0.0090 618  ARG B CG  
13541 C CD  . ARG B 620  ? 0.4380 0.5463 0.4598 0.0269  0.0471  -0.0087 618  ARG B CD  
13542 N NE  . ARG B 620  ? 0.5107 0.6203 0.5298 0.0315  0.0476  -0.0125 618  ARG B NE  
13543 C CZ  . ARG B 620  ? 0.4697 0.5839 0.4927 0.0341  0.0482  -0.0146 618  ARG B CZ  
13544 N NH1 . ARG B 620  ? 0.3832 0.5015 0.4132 0.0325  0.0484  -0.0133 618  ARG B NH1 
13545 N NH2 . ARG B 620  ? 0.5322 0.6467 0.5518 0.0386  0.0485  -0.0181 618  ARG B NH2 
13546 N N   . LEU B 621  ? 0.2281 0.3052 0.2380 0.0296  0.0345  -0.0161 619  LEU B N   
13547 C CA  . LEU B 621  ? 0.2408 0.3118 0.2449 0.0303  0.0323  -0.0178 619  LEU B CA  
13548 C C   . LEU B 621  ? 0.2899 0.3561 0.2946 0.0276  0.0298  -0.0163 619  LEU B C   
13549 O O   . LEU B 621  ? 0.2693 0.3324 0.2697 0.0269  0.0285  -0.0160 619  LEU B O   
13550 C CB  . LEU B 621  ? 0.2775 0.3456 0.2800 0.0334  0.0309  -0.0216 619  LEU B CB  
13551 C CG  . LEU B 621  ? 0.2696 0.3414 0.2698 0.0370  0.0330  -0.0239 619  LEU B CG  
13552 C CD1 . LEU B 621  ? 0.2882 0.3564 0.2877 0.0401  0.0312  -0.0274 619  LEU B CD1 
13553 C CD2 . LEU B 621  ? 0.3581 0.4294 0.3514 0.0377  0.0336  -0.0243 619  LEU B CD2 
13554 N N   . ALA B 622  ? 0.2550 0.3206 0.2650 0.0263  0.0290  -0.0154 620  ALA B N   
13555 C CA  . ALA B 622  ? 0.2406 0.3024 0.2515 0.0239  0.0269  -0.0139 620  ALA B CA  
13556 C C   . ALA B 622  ? 0.2460 0.3091 0.2561 0.0219  0.0278  -0.0108 620  ALA B C   
13557 O O   . ALA B 622  ? 0.2350 0.2950 0.2426 0.0209  0.0262  -0.0100 620  ALA B O   
13558 C CB  . ALA B 622  ? 0.2405 0.3017 0.2569 0.0231  0.0260  -0.0136 620  ALA B CB  
13559 N N   . ALA B 623  ? 0.2280 0.2957 0.2400 0.0213  0.0303  -0.0089 621  ALA B N   
13560 C CA  . ALA B 623  ? 0.2584 0.3269 0.2693 0.0194  0.0312  -0.0057 621  ALA B CA  
13561 C C   . ALA B 623  ? 0.2533 0.3210 0.2580 0.0201  0.0312  -0.0058 621  ALA B C   
13562 O O   . ALA B 623  ? 0.2734 0.3389 0.2760 0.0189  0.0301  -0.0040 621  ALA B O   
13563 C CB  . ALA B 623  ? 0.2626 0.3362 0.2765 0.0183  0.0339  -0.0037 621  ALA B CB  
13564 N N   . ASP B 624  ? 0.2748 0.3444 0.2763 0.0222  0.0322  -0.0080 622  ASP B N   
13565 C CA  . ASP B 624  ? 0.2827 0.3515 0.2779 0.0230  0.0321  -0.0084 622  ASP B CA  
13566 C C   . ASP B 624  ? 0.2825 0.3461 0.2751 0.0226  0.0289  -0.0093 622  ASP B C   
13567 O O   . ASP B 624  ? 0.3841 0.4467 0.3729 0.0220  0.0282  -0.0081 622  ASP B O   
13568 C CB  . ASP B 624  ? 0.3451 0.4161 0.3371 0.0257  0.0335  -0.0112 622  ASP B CB  
13569 C CG  . ASP B 624  ? 0.4288 0.5063 0.4228 0.0262  0.0370  -0.0102 622  ASP B CG  
13570 O OD1 . ASP B 624  ? 0.5361 0.6163 0.5320 0.0240  0.0384  -0.0068 622  ASP B OD1 
13571 O OD2 . ASP B 624  ? 0.4824 0.5624 0.4760 0.0288  0.0382  -0.0127 622  ASP B OD2 
13572 N N   . ALA B 625  ? 0.3295 0.3901 0.3242 0.0230  0.0270  -0.0113 623  ALA B N   
13573 C CA  . ALA B 625  ? 0.3566 0.4127 0.3491 0.0224  0.0240  -0.0122 623  ALA B CA  
13574 C C   . ALA B 625  ? 0.3026 0.3574 0.2984 0.0204  0.0226  -0.0100 623  ALA B C   
13575 O O   . ALA B 625  ? 0.3383 0.3905 0.3329 0.0197  0.0203  -0.0104 623  ALA B O   
13576 C CB  . ALA B 625  ? 0.4504 0.5035 0.4428 0.0236  0.0225  -0.0154 623  ALA B CB  
13577 N N   . ALA B 626  ? 0.2601 0.3168 0.2599 0.0194  0.0240  -0.0077 624  ALA B N   
13578 C CA  . ALA B 626  ? 0.2585 0.3135 0.2612 0.0179  0.0226  -0.0059 624  ALA B CA  
13579 C C   . ALA B 626  ? 0.2471 0.3009 0.2466 0.0174  0.0212  -0.0045 624  ALA B C   
13580 O O   . ALA B 626  ? 0.2827 0.3346 0.2831 0.0168  0.0191  -0.0047 624  ALA B O   
13581 C CB  . ALA B 626  ? 0.2292 0.2859 0.2360 0.0169  0.0243  -0.0037 624  ALA B CB  
13582 N N   . PRO B 627  ? 0.2606 0.3159 0.2565 0.0175  0.0221  -0.0032 625  PRO B N   
13583 C CA  . PRO B 627  ? 0.2801 0.3343 0.2731 0.0171  0.0204  -0.0018 625  PRO B CA  
13584 C C   . PRO B 627  ? 0.2792 0.3321 0.2698 0.0173  0.0180  -0.0040 625  PRO B C   
13585 O O   . PRO B 627  ? 0.2916 0.3439 0.2824 0.0168  0.0161  -0.0032 625  PRO B O   
13586 C CB  . PRO B 627  ? 0.3155 0.3716 0.3045 0.0174  0.0220  -0.0002 625  PRO B CB  
13587 C CG  . PRO B 627  ? 0.3220 0.3801 0.3131 0.0172  0.0247  0.0005  625  PRO B CG  
13588 C CD  . PRO B 627  ? 0.3291 0.3872 0.3234 0.0178  0.0247  -0.0023 625  PRO B CD  
13589 N N   . ASP B 628  ? 0.2731 0.3255 0.2614 0.0181  0.0180  -0.0067 626  ASP B N   
13590 C CA  . ASP B 628  ? 0.3376 0.3881 0.3231 0.0179  0.0155  -0.0087 626  ASP B CA  
13591 C C   . ASP B 628  ? 0.2860 0.3347 0.2750 0.0169  0.0137  -0.0093 626  ASP B C   
13592 O O   . ASP B 628  ? 0.3008 0.3489 0.2889 0.0159  0.0114  -0.0096 626  ASP B O   
13593 C CB  . ASP B 628  ? 0.3115 0.3609 0.2932 0.0191  0.0159  -0.0116 626  ASP B CB  
13594 C CG  . ASP B 628  ? 0.4116 0.4628 0.3885 0.0201  0.0174  -0.0113 626  ASP B CG  
13595 O OD1 . ASP B 628  ? 0.4110 0.4636 0.3864 0.0196  0.0173  -0.0090 626  ASP B OD1 
13596 O OD2 . ASP B 628  ? 0.5249 0.5760 0.4994 0.0216  0.0186  -0.0133 626  ASP B OD2 
13597 N N   . TRP B 629  ? 0.2576 0.3060 0.2510 0.0170  0.0146  -0.0096 627  TRP B N   
13598 C CA  . TRP B 629  ? 0.2131 0.2598 0.2096 0.0161  0.0130  -0.0100 627  TRP B CA  
13599 C C   . TRP B 629  ? 0.2381 0.2859 0.2373 0.0153  0.0125  -0.0076 627  TRP B C   
13600 O O   . TRP B 629  ? 0.2455 0.2929 0.2455 0.0145  0.0106  -0.0077 627  TRP B O   
13601 C CB  . TRP B 629  ? 0.2324 0.2782 0.2322 0.0167  0.0140  -0.0112 627  TRP B CB  
13602 C CG  . TRP B 629  ? 0.2373 0.2813 0.2400 0.0157  0.0124  -0.0116 627  TRP B CG  
13603 C CD1 . TRP B 629  ? 0.2286 0.2728 0.2358 0.0154  0.0129  -0.0106 627  TRP B CD1 
13604 C CD2 . TRP B 629  ? 0.2198 0.2615 0.2209 0.0147  0.0101  -0.0130 627  TRP B CD2 
13605 N NE1 . TRP B 629  ? 0.1953 0.2377 0.2037 0.0146  0.0111  -0.0114 627  TRP B NE1 
13606 C CE2 . TRP B 629  ? 0.1875 0.2284 0.1923 0.0140  0.0094  -0.0127 627  TRP B CE2 
13607 C CE3 . TRP B 629  ? 0.2076 0.2478 0.2044 0.0142  0.0084  -0.0144 627  TRP B CE3 
13608 C CZ2 . TRP B 629  ? 0.2146 0.2536 0.2190 0.0126  0.0073  -0.0136 627  TRP B CZ2 
13609 C CZ3 . TRP B 629  ? 0.2451 0.2831 0.2415 0.0126  0.0061  -0.0153 627  TRP B CZ3 
13610 C CH2 . TRP B 629  ? 0.2539 0.2914 0.2541 0.0118  0.0057  -0.0148 627  TRP B CH2 
13611 N N   . ALA B 630  ? 0.2350 0.2842 0.2353 0.0157  0.0141  -0.0055 628  ALA B N   
13612 C CA  . ALA B 630  ? 0.2408 0.2904 0.2428 0.0154  0.0135  -0.0032 628  ALA B CA  
13613 C C   . ALA B 630  ? 0.2656 0.3163 0.2650 0.0153  0.0117  -0.0028 628  ALA B C   
13614 O O   . ALA B 630  ? 0.2968 0.3480 0.2978 0.0152  0.0104  -0.0018 628  ALA B O   
13615 C CB  . ALA B 630  ? 0.3112 0.3613 0.3139 0.0157  0.0154  -0.0009 628  ALA B CB  
13616 N N   . ALA B 631  ? 0.2552 0.3064 0.2503 0.0154  0.0115  -0.0035 629  ALA B N   
13617 C CA  . ALA B 631  ? 0.2654 0.3179 0.2576 0.0152  0.0096  -0.0030 629  ALA B CA  
13618 C C   . ALA B 631  ? 0.2956 0.3480 0.2878 0.0141  0.0073  -0.0048 629  ALA B C   
13619 O O   . ALA B 631  ? 0.2683 0.3226 0.2591 0.0136  0.0055  -0.0043 629  ALA B O   
13620 C CB  . ALA B 631  ? 0.2707 0.3236 0.2578 0.0157  0.0102  -0.0032 629  ALA B CB  
13621 N N   . VAL B 632  ? 0.2560 0.3065 0.2499 0.0135  0.0072  -0.0066 630  VAL B N   
13622 C CA  . VAL B 632  ? 0.2322 0.2823 0.2263 0.0119  0.0050  -0.0079 630  VAL B CA  
13623 C C   . VAL B 632  ? 0.2563 0.3085 0.2544 0.0117  0.0044  -0.0063 630  VAL B C   
13624 O O   . VAL B 632  ? 0.2634 0.3150 0.2648 0.0123  0.0057  -0.0056 630  VAL B O   
13625 C CB  . VAL B 632  ? 0.2743 0.3211 0.2686 0.0115  0.0050  -0.0102 630  VAL B CB  
13626 C CG1 . VAL B 632  ? 0.2341 0.2802 0.2287 0.0095  0.0027  -0.0110 630  VAL B CG1 
13627 C CG2 . VAL B 632  ? 0.2627 0.3074 0.2526 0.0123  0.0055  -0.0120 630  VAL B CG2 
13628 N N   . PRO B 633  ? 0.2411 0.2960 0.2390 0.0108  0.0025  -0.0057 631  PRO B N   
13629 C CA  . PRO B 633  ? 0.1984 0.2561 0.2000 0.0110  0.0021  -0.0042 631  PRO B CA  
13630 C C   . PRO B 633  ? 0.2246 0.2808 0.2295 0.0105  0.0025  -0.0049 631  PRO B C   
13631 O O   . PRO B 633  ? 0.2478 0.3017 0.2521 0.0091  0.0019  -0.0066 631  PRO B O   
13632 C CB  . PRO B 633  ? 0.2519 0.3131 0.2524 0.0097  -0.0002 -0.0041 631  PRO B CB  
13633 C CG  . PRO B 633  ? 0.3309 0.3915 0.3268 0.0095  -0.0008 -0.0047 631  PRO B CG  
13634 C CD  . PRO B 633  ? 0.2382 0.2943 0.2324 0.0097  0.0006  -0.0064 631  PRO B CD  
13635 N N   . PRO B 634  ? 0.2359 0.2930 0.2441 0.0116  0.0033  -0.0037 632  PRO B N   
13636 C CA  . PRO B 634  ? 0.2602 0.3159 0.2713 0.0111  0.0035  -0.0043 632  PRO B CA  
13637 C C   . PRO B 634  ? 0.2066 0.2633 0.2179 0.0090  0.0019  -0.0053 632  PRO B C   
13638 O O   . PRO B 634  ? 0.2221 0.2760 0.2339 0.0080  0.0019  -0.0065 632  PRO B O   
13639 C CB  . PRO B 634  ? 0.2529 0.3101 0.2666 0.0128  0.0041  -0.0027 632  PRO B CB  
13640 C CG  . PRO B 634  ? 0.3088 0.3660 0.3208 0.0143  0.0048  -0.0013 632  PRO B CG  
13641 C CD  . PRO B 634  ? 0.2410 0.2995 0.2497 0.0135  0.0039  -0.0017 632  PRO B CD  
13642 N N   . SER B 635  ? 0.2268 0.2875 0.2376 0.0081  0.0004  -0.0047 633  SER B N   
13643 C CA  . SER B 635  ? 0.2605 0.3224 0.2714 0.0056  -0.0012 -0.0054 633  SER B CA  
13644 C C   . SER B 635  ? 0.2365 0.2943 0.2441 0.0037  -0.0021 -0.0072 633  SER B C   
13645 O O   . SER B 635  ? 0.2215 0.2774 0.2291 0.0017  -0.0029 -0.0081 633  SER B O   
13646 C CB  . SER B 635  ? 0.3245 0.3923 0.3357 0.0048  -0.0027 -0.0044 633  SER B CB  
13647 O OG  . SER B 635  ? 0.3734 0.4416 0.3814 0.0047  -0.0036 -0.0045 633  SER B OG  
13648 N N   . GLU B 636  ? 0.2318 0.2877 0.2363 0.0044  -0.0019 -0.0078 634  GLU B N   
13649 C CA  . GLU B 636  ? 0.2287 0.2802 0.2296 0.0032  -0.0027 -0.0098 634  GLU B CA  
13650 C C   . GLU B 636  ? 0.2349 0.2819 0.2364 0.0043  -0.0012 -0.0109 634  GLU B C   
13651 O O   . GLU B 636  ? 0.2397 0.2827 0.2394 0.0031  -0.0022 -0.0124 634  GLU B O   
13652 C CB  . GLU B 636  ? 0.2440 0.2953 0.2409 0.0039  -0.0029 -0.0101 634  GLU B CB  
13653 C CG  . GLU B 636  ? 0.3833 0.4294 0.3758 0.0032  -0.0036 -0.0124 634  GLU B CG  
13654 C CD  . GLU B 636  ? 0.4867 0.5306 0.4778 0.0002  -0.0060 -0.0135 634  GLU B CD  
13655 O OE1 . GLU B 636  ? 0.4643 0.5118 0.4560 -0.0020 -0.0077 -0.0126 634  GLU B OE1 
13656 O OE2 . GLU B 636  ? 0.4003 0.4390 0.3897 0.0000  -0.0062 -0.0153 634  GLU B OE2 
13657 N N   . ARG B 637  ? 0.1963 0.2437 0.2002 0.0065  0.0008  -0.0100 635  ARG B N   
13658 C CA  . ARG B 637  ? 0.1886 0.2327 0.1939 0.0073  0.0021  -0.0109 635  ARG B CA  
13659 C C   . ARG B 637  ? 0.1966 0.2397 0.2040 0.0060  0.0012  -0.0111 635  ARG B C   
13660 O O   . ARG B 637  ? 0.2085 0.2479 0.2152 0.0056  0.0009  -0.0125 635  ARG B O   
13661 C CB  . ARG B 637  ? 0.1896 0.2346 0.1973 0.0094  0.0042  -0.0097 635  ARG B CB  
13662 C CG  . ARG B 637  ? 0.2029 0.2489 0.2083 0.0106  0.0052  -0.0092 635  ARG B CG  
13663 C CD  . ARG B 637  ? 0.1949 0.2410 0.2024 0.0121  0.0074  -0.0082 635  ARG B CD  
13664 N NE  . ARG B 637  ? 0.2079 0.2552 0.2186 0.0124  0.0077  -0.0065 635  ARG B NE  
13665 C CZ  . ARG B 637  ? 0.2753 0.3241 0.2861 0.0133  0.0083  -0.0046 635  ARG B CZ  
13666 N NH1 . ARG B 637  ? 0.2919 0.3417 0.2999 0.0138  0.0085  -0.0039 635  ARG B NH1 
13667 N NH2 . ARG B 637  ? 0.2386 0.2876 0.2522 0.0139  0.0085  -0.0034 635  ARG B NH2 
13668 N N   . ALA B 638  ? 0.1877 0.2344 0.1975 0.0054  0.0008  -0.0097 636  ALA B N   
13669 C CA  . ALA B 638  ? 0.1726 0.2191 0.1841 0.0039  0.0001  -0.0097 636  ALA B CA  
13670 C C   . ALA B 638  ? 0.1903 0.2347 0.1990 0.0013  -0.0019 -0.0108 636  ALA B C   
13671 O O   . ALA B 638  ? 0.2048 0.2463 0.2135 0.0002  -0.0025 -0.0114 636  ALA B O   
13672 C CB  . ALA B 638  ? 0.1999 0.2514 0.2141 0.0041  0.0001  -0.0081 636  ALA B CB  
13673 N N   . ALA B 639  ? 0.2006 0.2460 0.2065 0.0001  -0.0032 -0.0110 637  ALA B N   
13674 C CA  . ALA B 639  ? 0.2288 0.2715 0.2315 -0.0028 -0.0054 -0.0120 637  ALA B CA  
13675 C C   . ALA B 639  ? 0.1950 0.2309 0.1949 -0.0023 -0.0056 -0.0139 637  ALA B C   
13676 O O   . ALA B 639  ? 0.1946 0.2266 0.1925 -0.0044 -0.0072 -0.0147 637  ALA B O   
13677 C CB  . ALA B 639  ? 0.1972 0.2423 0.1973 -0.0042 -0.0069 -0.0119 637  ALA B CB  
13678 N N   . CYS B 640  ? 0.1988 0.2331 0.1982 0.0005  -0.0040 -0.0147 638  CYS B N   
13679 C CA  . CYS B 640  ? 0.2084 0.2371 0.2059 0.0017  -0.0038 -0.0165 638  CYS B CA  
13680 C C   . CYS B 640  ? 0.1709 0.1976 0.1709 0.0017  -0.0037 -0.0165 638  CYS B C   
13681 O O   . CYS B 640  ? 0.2006 0.2223 0.1984 0.0010  -0.0050 -0.0177 638  CYS B O   
13682 C CB  . CYS B 640  ? 0.1977 0.2269 0.1954 0.0048  -0.0017 -0.0170 638  CYS B CB  
13683 S SG  . CYS B 640  ? 0.2364 0.2665 0.2299 0.0053  -0.0019 -0.0175 638  CYS B SG  
13684 N N   . LEU B 641  ? 0.1994 0.2298 0.2038 0.0025  -0.0022 -0.0150 639  LEU B N   
13685 C CA  . LEU B 641  ? 0.1841 0.2128 0.1907 0.0024  -0.0021 -0.0149 639  LEU B CA  
13686 C C   . LEU B 641  ? 0.1653 0.1927 0.1705 -0.0006 -0.0041 -0.0147 639  LEU B C   
13687 O O   . LEU B 641  ? 0.1961 0.2190 0.2002 -0.0011 -0.0050 -0.0154 639  LEU B O   
13688 C CB  . LEU B 641  ? 0.1881 0.2208 0.1990 0.0036  -0.0005 -0.0134 639  LEU B CB  
13689 C CG  . LEU B 641  ? 0.2022 0.2349 0.2153 0.0062  0.0015  -0.0136 639  LEU B CG  
13690 C CD1 . LEU B 641  ? 0.2334 0.2668 0.2449 0.0076  0.0024  -0.0139 639  LEU B CD1 
13691 C CD2 . LEU B 641  ? 0.1899 0.2257 0.2066 0.0069  0.0026  -0.0120 639  LEU B CD2 
13692 N N   . ASP B 642  ? 0.1794 0.2106 0.1845 -0.0027 -0.0049 -0.0136 640  ASP B N   
13693 C CA  . ASP B 642  ? 0.1971 0.2279 0.2011 -0.0060 -0.0067 -0.0131 640  ASP B CA  
13694 C C   . ASP B 642  ? 0.2007 0.2250 0.1998 -0.0078 -0.0089 -0.0145 640  ASP B C   
13695 O O   . ASP B 642  ? 0.2164 0.2371 0.2140 -0.0098 -0.0102 -0.0146 640  ASP B O   
13696 C CB  . ASP B 642  ? 0.1889 0.2262 0.1940 -0.0079 -0.0072 -0.0116 640  ASP B CB  
13697 C CG  . ASP B 642  ? 0.2301 0.2731 0.2396 -0.0068 -0.0056 -0.0100 640  ASP B CG  
13698 O OD1 . ASP B 642  ? 0.2258 0.2673 0.2371 -0.0056 -0.0047 -0.0100 640  ASP B OD1 
13699 O OD2 . ASP B 642  ? 0.2279 0.2768 0.2389 -0.0070 -0.0056 -0.0089 640  ASP B OD2 
13700 N N   . ARG B 643  ? 0.2056 0.2280 0.2018 -0.0069 -0.0092 -0.0158 641  ARG B N   
13701 C CA  . ARG B 643  ? 0.2129 0.2283 0.2039 -0.0080 -0.0113 -0.0175 641  ARG B CA  
13702 C C   . ARG B 643  ? 0.2238 0.2332 0.2141 -0.0059 -0.0111 -0.0188 641  ARG B C   
13703 O O   . ARG B 643  ? 0.2192 0.2225 0.2061 -0.0075 -0.0130 -0.0196 641  ARG B O   
13704 C CB  . ARG B 643  ? 0.2081 0.2227 0.1958 -0.0070 -0.0115 -0.0188 641  ARG B CB  
13705 C CG  . ARG B 643  ? 0.2460 0.2645 0.2326 -0.0099 -0.0130 -0.0179 641  ARG B CG  
13706 C CD  . ARG B 643  ? 0.2863 0.3024 0.2683 -0.0093 -0.0138 -0.0195 641  ARG B CD  
13707 N NE  . ARG B 643  ? 0.2550 0.2741 0.2385 -0.0056 -0.0114 -0.0196 641  ARG B NE  
13708 C CZ  . ARG B 643  ? 0.2892 0.3147 0.2749 -0.0051 -0.0104 -0.0183 641  ARG B CZ  
13709 N NH1 . ARG B 643  ? 0.2883 0.3185 0.2752 -0.0078 -0.0116 -0.0168 641  ARG B NH1 
13710 N NH2 . ARG B 643  ? 0.3185 0.3457 0.3050 -0.0019 -0.0082 -0.0183 641  ARG B NH2 
13711 N N   . ALA B 644  ? 0.1942 0.2053 0.1875 -0.0025 -0.0088 -0.0190 642  ALA B N   
13712 C CA  . ALA B 644  ? 0.1861 0.1927 0.1795 -0.0004 -0.0086 -0.0202 642  ALA B CA  
13713 C C   . ALA B 644  ? 0.2227 0.2278 0.2171 -0.0023 -0.0095 -0.0192 642  ALA B C   
13714 O O   . ALA B 644  ? 0.2140 0.2131 0.2061 -0.0021 -0.0108 -0.0201 642  ALA B O   
13715 C CB  . ALA B 644  ? 0.1954 0.2054 0.1927 0.0031  -0.0060 -0.0202 642  ALA B CB  
13716 N N   . ALA B 645  ? 0.1990 0.2095 0.1968 -0.0038 -0.0088 -0.0173 643  ALA B N   
13717 C CA  . ALA B 645  ? 0.1986 0.2083 0.1973 -0.0057 -0.0095 -0.0162 643  ALA B CA  
13718 C C   . ALA B 645  ? 0.2139 0.2186 0.2079 -0.0092 -0.0122 -0.0162 643  ALA B C   
13719 O O   . ALA B 645  ? 0.2307 0.2306 0.2232 -0.0100 -0.0133 -0.0163 643  ALA B O   
13720 C CB  . ALA B 645  ? 0.2141 0.2310 0.2168 -0.0065 -0.0082 -0.0143 643  ALA B CB  
13721 N N   . GLU B 646  ? 0.2137 0.2193 0.2054 -0.0115 -0.0133 -0.0162 644  GLU B N   
13722 C CA  . GLU B 646  ? 0.2385 0.2391 0.2256 -0.0153 -0.0161 -0.0162 644  GLU B CA  
13723 C C   . GLU B 646  ? 0.2363 0.2274 0.2187 -0.0140 -0.0177 -0.0182 644  GLU B C   
13724 O O   . GLU B 646  ? 0.2527 0.2377 0.2317 -0.0163 -0.0198 -0.0181 644  GLU B O   
13725 C CB  . GLU B 646  ? 0.2493 0.2526 0.2346 -0.0178 -0.0171 -0.0160 644  GLU B CB  
13726 C CG  . GLU B 646  ? 0.3229 0.3355 0.3123 -0.0196 -0.0162 -0.0140 644  GLU B CG  
13727 C CD  . GLU B 646  ? 0.4112 0.4255 0.4016 -0.0230 -0.0168 -0.0122 644  GLU B CD  
13728 O OE1 . GLU B 646  ? 0.4942 0.5026 0.4805 -0.0263 -0.0191 -0.0122 644  GLU B OE1 
13729 O OE2 . GLU B 646  ? 0.4744 0.4956 0.4693 -0.0224 -0.0151 -0.0107 644  GLU B OE2 
13730 N N   . LEU B 647  ? 0.2303 0.2198 0.2121 -0.0102 -0.0167 -0.0201 645  LEU B N   
13731 C CA  . LEU B 647  ? 0.2622 0.2431 0.2396 -0.0081 -0.0181 -0.0222 645  LEU B CA  
13732 C C   . LEU B 647  ? 0.2623 0.2404 0.2411 -0.0064 -0.0179 -0.0222 645  LEU B C   
13733 O O   . LEU B 647  ? 0.2584 0.2286 0.2331 -0.0067 -0.0200 -0.0230 645  LEU B O   
13734 C CB  . LEU B 647  ? 0.2446 0.2260 0.2216 -0.0042 -0.0167 -0.0242 645  LEU B CB  
13735 C CG  . LEU B 647  ? 0.2570 0.2399 0.2314 -0.0055 -0.0173 -0.0247 645  LEU B CG  
13736 C CD1 . LEU B 647  ? 0.2495 0.2332 0.2234 -0.0013 -0.0156 -0.0265 645  LEU B CD1 
13737 C CD2 . LEU B 647  ? 0.3059 0.2813 0.2738 -0.0088 -0.0207 -0.0254 645  LEU B CD2 
13738 N N   . MET B 648  ? 0.2233 0.2074 0.2077 -0.0046 -0.0155 -0.0212 646  MET B N   
13739 C CA  . MET B 648  ? 0.1989 0.1807 0.1848 -0.0031 -0.0155 -0.0211 646  MET B CA  
13740 C C   . MET B 648  ? 0.2306 0.2098 0.2148 -0.0069 -0.0173 -0.0195 646  MET B C   
13741 O O   . MET B 648  ? 0.2371 0.2104 0.2192 -0.0064 -0.0186 -0.0198 646  MET B O   
13742 C CB  . MET B 648  ? 0.2333 0.2221 0.2253 -0.0008 -0.0128 -0.0203 646  MET B CB  
13743 C CG  . MET B 648  ? 0.2459 0.2369 0.2397 0.0030  -0.0109 -0.0217 646  MET B CG  
13744 S SD  . MET B 648  ? 0.2346 0.2313 0.2350 0.0053  -0.0085 -0.0208 646  MET B SD  
13745 C CE  . MET B 648  ? 0.2714 0.2709 0.2733 0.0089  -0.0065 -0.0222 646  MET B CE  
13746 N N   . GLN B 649  ? 0.2237 0.2075 0.2087 -0.0106 -0.0172 -0.0177 647  GLN B N   
13747 C CA  . GLN B 649  ? 0.2321 0.2140 0.2153 -0.0146 -0.0188 -0.0160 647  GLN B CA  
13748 C C   . GLN B 649  ? 0.2474 0.2198 0.2240 -0.0167 -0.0219 -0.0168 647  GLN B C   
13749 O O   . GLN B 649  ? 0.2682 0.2348 0.2421 -0.0178 -0.0235 -0.0163 647  GLN B O   
13750 C CB  . GLN B 649  ? 0.2347 0.2245 0.2203 -0.0180 -0.0181 -0.0141 647  GLN B CB  
13751 C CG  . GLN B 649  ? 0.2664 0.2560 0.2508 -0.0222 -0.0192 -0.0121 647  GLN B CG  
13752 C CD  . GLN B 649  ? 0.2399 0.2319 0.2276 -0.0207 -0.0178 -0.0112 647  GLN B CD  
13753 O OE1 . GLN B 649  ? 0.2638 0.2636 0.2561 -0.0197 -0.0156 -0.0103 647  GLN B OE1 
13754 N NE2 . GLN B 649  ? 0.2457 0.2306 0.2306 -0.0203 -0.0191 -0.0114 647  GLN B NE2 
13755 N N   . ALA B 650  ? 0.2434 0.2135 0.2168 -0.0173 -0.0230 -0.0180 648  ALA B N   
13756 C CA  . ALA B 650  ? 0.2674 0.2279 0.2339 -0.0196 -0.0263 -0.0188 648  ALA B CA  
13757 C C   . ALA B 650  ? 0.3040 0.2556 0.2672 -0.0158 -0.0273 -0.0208 648  ALA B C   
13758 O O   . ALA B 650  ? 0.3342 0.2768 0.2919 -0.0175 -0.0301 -0.0209 648  ALA B O   
13759 C CB  . ALA B 650  ? 0.2948 0.2553 0.2587 -0.0207 -0.0271 -0.0200 648  ALA B CB  
13760 N N   . ARG B 651  ? 0.2855 0.2397 0.2519 -0.0107 -0.0252 -0.0223 649  ARG B N   
13761 C CA  . ARG B 651  ? 0.2607 0.2082 0.2249 -0.0064 -0.0260 -0.0243 649  ARG B CA  
13762 C C   . ARG B 651  ? 0.2606 0.2091 0.2281 -0.0045 -0.0252 -0.0235 649  ARG B C   
13763 O O   . ARG B 651  ? 0.2872 0.2318 0.2541 -0.0004 -0.0254 -0.0250 649  ARG B O   
13764 C CB  . ARG B 651  ? 0.2679 0.2179 0.2333 -0.0019 -0.0242 -0.0265 649  ARG B CB  
13765 C CG  . ARG B 651  ? 0.2913 0.2391 0.2523 -0.0037 -0.0254 -0.0275 649  ARG B CG  
13766 C CD  . ARG B 651  ? 0.2925 0.2437 0.2545 0.0003  -0.0235 -0.0295 649  ARG B CD  
13767 N NE  . ARG B 651  ? 0.3182 0.2683 0.2763 -0.0021 -0.0246 -0.0301 649  ARG B NE  
13768 C CZ  . ARG B 651  ? 0.3158 0.2692 0.2738 0.0002  -0.0232 -0.0314 649  ARG B CZ  
13769 N NH1 . ARG B 651  ? 0.2857 0.2435 0.2473 0.0048  -0.0205 -0.0323 649  ARG B NH1 
13770 N NH2 . ARG B 651  ? 0.2998 0.2524 0.2542 -0.0025 -0.0246 -0.0317 649  ARG B NH2 
13771 N N   . MET B 652  ? 0.2384 0.1921 0.2093 -0.0074 -0.0243 -0.0211 650  MET B N   
13772 C CA  . MET B 652  ? 0.2541 0.2088 0.2280 -0.0057 -0.0236 -0.0203 650  MET B CA  
13773 C C   . MET B 652  ? 0.2780 0.2232 0.2475 -0.0042 -0.0261 -0.0211 650  MET B C   
13774 O O   . MET B 652  ? 0.2906 0.2363 0.2626 -0.0002 -0.0254 -0.0220 650  MET B O   
13775 C CB  . MET B 652  ? 0.2611 0.2210 0.2374 -0.0096 -0.0230 -0.0177 650  MET B CB  
13776 C CG  . MET B 652  ? 0.2647 0.2253 0.2434 -0.0082 -0.0225 -0.0168 650  MET B CG  
13777 S SD  . MET B 652  ? 0.2916 0.2589 0.2728 -0.0124 -0.0214 -0.0139 650  MET B SD  
13778 C CE  . MET B 652  ? 0.2794 0.2576 0.2672 -0.0107 -0.0181 -0.0140 650  MET B CE  
13779 N N   . PRO B 653  ? 0.2606 0.1970 0.2236 -0.0069 -0.0291 -0.0210 651  PRO B N   
13780 C CA  . PRO B 653  ? 0.2962 0.2231 0.2548 -0.0050 -0.0316 -0.0217 651  PRO B CA  
13781 C C   . PRO B 653  ? 0.2937 0.2179 0.2520 0.0010  -0.0315 -0.0245 651  PRO B C   
13782 O O   . PRO B 653  ? 0.3091 0.2311 0.2681 0.0044  -0.0319 -0.0250 651  PRO B O   
13783 C CB  . PRO B 653  ? 0.3218 0.2396 0.2729 -0.0094 -0.0348 -0.0211 651  PRO B CB  
13784 C CG  . PRO B 653  ? 0.3409 0.2656 0.2941 -0.0148 -0.0338 -0.0188 651  PRO B CG  
13785 C CD  . PRO B 653  ? 0.2884 0.2230 0.2476 -0.0124 -0.0306 -0.0197 651  PRO B CD  
13786 N N   . THR B 654  ? 0.2815 0.2063 0.2390 0.0025  -0.0309 -0.0264 652  THR B N   
13787 C CA  . THR B 654  ? 0.3000 0.2234 0.2575 0.0084  -0.0304 -0.0292 652  THR B CA  
13788 C C   . THR B 654  ? 0.3381 0.2712 0.3034 0.0119  -0.0273 -0.0292 652  THR B C   
13789 O O   . THR B 654  ? 0.3137 0.2459 0.2801 0.0163  -0.0273 -0.0305 652  THR B O   
13790 C CB  . THR B 654  ? 0.3302 0.2525 0.2846 0.0088  -0.0304 -0.0311 652  THR B CB  
13791 O OG1 . THR B 654  ? 0.3599 0.2724 0.3067 0.0053  -0.0337 -0.0311 652  THR B OG1 
13792 C CG2 . THR B 654  ? 0.3427 0.2638 0.2967 0.0151  -0.0298 -0.0340 652  THR B CG2 
13793 N N   . LEU B 655  ? 0.2875 0.2298 0.2580 0.0098  -0.0247 -0.0277 653  LEU B N   
13794 C CA  . LEU B 655  ? 0.2655 0.2165 0.2432 0.0124  -0.0219 -0.0275 653  LEU B CA  
13795 C C   . LEU B 655  ? 0.2981 0.2482 0.2775 0.0132  -0.0226 -0.0266 653  LEU B C   
13796 O O   . LEU B 655  ? 0.2749 0.2284 0.2583 0.0169  -0.0215 -0.0273 653  LEU B O   
13797 C CB  . LEU B 655  ? 0.2582 0.2178 0.2402 0.0096  -0.0195 -0.0258 653  LEU B CB  
13798 C CG  . LEU B 655  ? 0.2765 0.2381 0.2572 0.0087  -0.0187 -0.0264 653  LEU B CG  
13799 C CD1 . LEU B 655  ? 0.2742 0.2442 0.2594 0.0062  -0.0166 -0.0246 653  LEU B CD1 
13800 C CD2 . LEU B 655  ? 0.3609 0.3235 0.3422 0.0133  -0.0175 -0.0287 653  LEU B CD2 
13801 N N   . LEU B 656  ? 0.3005 0.2465 0.2772 0.0095  -0.0244 -0.0248 654  LEU B N   
13802 C CA  . LEU B 656  ? 0.3074 0.2516 0.2847 0.0102  -0.0254 -0.0239 654  LEU B CA  
13803 C C   . LEU B 656  ? 0.3004 0.2387 0.2756 0.0148  -0.0271 -0.0258 654  LEU B C   
13804 O O   . LEU B 656  ? 0.3457 0.2867 0.3245 0.0177  -0.0266 -0.0260 654  LEU B O   
13805 C CB  . LEU B 656  ? 0.3370 0.2761 0.3100 0.0055  -0.0274 -0.0218 654  LEU B CB  
13806 C CG  . LEU B 656  ? 0.3677 0.3122 0.3421 0.0006  -0.0262 -0.0197 654  LEU B CG  
13807 C CD1 . LEU B 656  ? 0.3690 0.3086 0.3392 -0.0036 -0.0283 -0.0176 654  LEU B CD1 
13808 C CD2 . LEU B 656  ? 0.3353 0.2895 0.3167 0.0016  -0.0233 -0.0191 654  LEU B CD2 
13809 N N   . GLY B 657  ? 0.3186 0.2487 0.2877 0.0155  -0.0292 -0.0273 655  GLY B N   
13810 C CA  . GLY B 657  ? 0.3202 0.2439 0.2865 0.0203  -0.0311 -0.0292 655  GLY B CA  
13811 C C   . GLY B 657  ? 0.3125 0.2435 0.2846 0.0254  -0.0288 -0.0310 655  GLY B C   
13812 O O   . GLY B 657  ? 0.3230 0.2537 0.2966 0.0292  -0.0294 -0.0317 655  GLY B O   
13813 N N   . LEU B 658  ? 0.2817 0.2196 0.2570 0.0255  -0.0261 -0.0315 656  LEU B N   
13814 C CA  . LEU B 658  ? 0.2930 0.2382 0.2736 0.0299  -0.0238 -0.0330 656  LEU B CA  
13815 C C   . LEU B 658  ? 0.3181 0.2711 0.3056 0.0298  -0.0221 -0.0315 656  LEU B C   
13816 O O   . LEU B 658  ? 0.3108 0.2670 0.3019 0.0337  -0.0217 -0.0324 656  LEU B O   
13817 C CB  . LEU B 658  ? 0.2638 0.2136 0.2451 0.0297  -0.0215 -0.0338 656  LEU B CB  
13818 C CG  . LEU B 658  ? 0.2863 0.2440 0.2727 0.0339  -0.0188 -0.0352 656  LEU B CG  
13819 C CD1 . LEU B 658  ? 0.2747 0.2286 0.2591 0.0394  -0.0201 -0.0376 656  LEU B CD1 
13820 C CD2 . LEU B 658  ? 0.2777 0.2389 0.2636 0.0330  -0.0168 -0.0357 656  LEU B CD2 
13821 N N   . ILE B 659  ? 0.2437 0.1999 0.2332 0.0255  -0.0213 -0.0293 657  ILE B N   
13822 C CA  . ILE B 659  ? 0.2174 0.1806 0.2130 0.0252  -0.0198 -0.0280 657  ILE B CA  
13823 C C   . ILE B 659  ? 0.2522 0.2116 0.2472 0.0267  -0.0220 -0.0278 657  ILE B C   
13824 O O   . ILE B 659  ? 0.2760 0.2402 0.2758 0.0289  -0.0214 -0.0279 657  ILE B O   
13825 C CB  . ILE B 659  ? 0.2663 0.2331 0.2633 0.0206  -0.0186 -0.0258 657  ILE B CB  
13826 C CG1 . ILE B 659  ? 0.2335 0.2052 0.2320 0.0198  -0.0163 -0.0260 657  ILE B CG1 
13827 C CG2 . ILE B 659  ? 0.2747 0.2467 0.2767 0.0202  -0.0177 -0.0245 657  ILE B CG2 
13828 C CD1 . ILE B 659  ? 0.2605 0.2343 0.2589 0.0154  -0.0157 -0.0241 657  ILE B CD1 
13829 N N   . ILE B 660  ? 0.2449 0.1955 0.2338 0.0252  -0.0248 -0.0273 658  ILE B N   
13830 C CA  . ILE B 660  ? 0.2507 0.1968 0.2381 0.0266  -0.0272 -0.0270 658  ILE B CA  
13831 C C   . ILE B 660  ? 0.2847 0.2310 0.2737 0.0323  -0.0277 -0.0291 658  ILE B C   
13832 O O   . ILE B 660  ? 0.3105 0.2597 0.3030 0.0344  -0.0281 -0.0290 658  ILE B O   
13833 C CB  . ILE B 660  ? 0.2747 0.2103 0.2544 0.0240  -0.0302 -0.0262 658  ILE B CB  
13834 C CG1 . ILE B 660  ? 0.2671 0.2042 0.2463 0.0183  -0.0296 -0.0237 658  ILE B CG1 
13835 C CG2 . ILE B 660  ? 0.3024 0.2315 0.2793 0.0266  -0.0331 -0.0264 658  ILE B CG2 
13836 C CD1 . ILE B 660  ? 0.3123 0.2399 0.2839 0.0147  -0.0323 -0.0226 658  ILE B CD1 
13837 N N   . ARG B 661  ? 0.2766 0.2202 0.2630 0.0350  -0.0278 -0.0312 659  ARG B N   
13838 C CA  . ARG B 661  ? 0.2826 0.2255 0.2695 0.0409  -0.0287 -0.0334 659  ARG B CA  
13839 C C   . ARG B 661  ? 0.2861 0.2401 0.2805 0.0436  -0.0256 -0.0342 659  ARG B C   
13840 O O   . ARG B 661  ? 0.2867 0.2437 0.2842 0.0476  -0.0259 -0.0352 659  ARG B O   
13841 C CB  . ARG B 661  ? 0.3015 0.2358 0.2815 0.0431  -0.0304 -0.0354 659  ARG B CB  
13842 C CG  . ARG B 661  ? 0.3545 0.2768 0.3268 0.0413  -0.0341 -0.0346 659  ARG B CG  
13843 C CD  . ARG B 661  ? 0.3740 0.2868 0.3388 0.0429  -0.0360 -0.0367 659  ARG B CD  
13844 N NE  . ARG B 661  ? 0.3690 0.2817 0.3339 0.0497  -0.0362 -0.0395 659  ARG B NE  
13845 C CZ  . ARG B 661  ? 0.3986 0.3129 0.3628 0.0523  -0.0348 -0.0418 659  ARG B CZ  
13846 N NH1 . ARG B 661  ? 0.4180 0.3336 0.3812 0.0487  -0.0333 -0.0415 659  ARG B NH1 
13847 N NH2 . ARG B 661  ? 0.3847 0.2990 0.3488 0.0588  -0.0351 -0.0444 659  ARG B NH2 
13848 N N   . GLU B 662  ? 0.2856 0.2458 0.2828 0.0413  -0.0228 -0.0338 660  GLU B N   
13849 C CA  . GLU B 662  ? 0.2649 0.2352 0.2689 0.0436  -0.0199 -0.0344 660  GLU B CA  
13850 C C   . GLU B 662  ? 0.2799 0.2572 0.2902 0.0419  -0.0188 -0.0327 660  GLU B C   
13851 O O   . GLU B 662  ? 0.2792 0.2632 0.2949 0.0445  -0.0178 -0.0332 660  GLU B O   
13852 C CB  . GLU B 662  ? 0.2940 0.2680 0.2982 0.0420  -0.0173 -0.0346 660  GLU B CB  
13853 C CG  . GLU B 662  ? 0.2452 0.2298 0.2562 0.0439  -0.0141 -0.0350 660  GLU B CG  
13854 C CD  . GLU B 662  ? 0.2830 0.2709 0.2937 0.0427  -0.0116 -0.0351 660  GLU B CD  
13855 O OE1 . GLU B 662  ? 0.2782 0.2636 0.2863 0.0389  -0.0117 -0.0340 660  GLU B OE1 
13856 O OE2 . GLU B 662  ? 0.3037 0.2972 0.3169 0.0456  -0.0097 -0.0363 660  GLU B OE2 
13857 N N   . ALA B 663  ? 0.2488 0.2248 0.2585 0.0375  -0.0191 -0.0307 661  ALA B N   
13858 C CA  . ALA B 663  ? 0.2661 0.2487 0.2815 0.0357  -0.0178 -0.0292 661  ALA B CA  
13859 C C   . ALA B 663  ? 0.2676 0.2471 0.2823 0.0350  -0.0201 -0.0282 661  ALA B C   
13860 O O   . ALA B 663  ? 0.3543 0.3383 0.3729 0.0333  -0.0194 -0.0270 661  ALA B O   
13861 C CB  . ALA B 663  ? 0.2520 0.2376 0.2683 0.0316  -0.0158 -0.0278 661  ALA B CB  
13862 N N   . GLY B 664  ? 0.2906 0.2620 0.3001 0.0363  -0.0230 -0.0287 662  GLY B N   
13863 C CA  . GLY B 664  ? 0.3321 0.3003 0.3405 0.0357  -0.0253 -0.0276 662  GLY B CA  
13864 C C   . GLY B 664  ? 0.3643 0.3303 0.3704 0.0309  -0.0254 -0.0255 662  GLY B C   
13865 O O   . GLY B 664  ? 0.3460 0.3119 0.3526 0.0300  -0.0265 -0.0244 662  GLY B O   
13866 N N   . LYS B 665  ? 0.2760 0.2405 0.2795 0.0278  -0.0244 -0.0249 663  LYS B N   
13867 C CA  A LYS B 665  ? 0.2693 0.2333 0.2712 0.0233  -0.0242 -0.0229 663  LYS B CA  
13868 C CA  B LYS B 665  ? 0.2693 0.2332 0.2711 0.0233  -0.0241 -0.0229 663  LYS B CA  
13869 C C   . LYS B 665  ? 0.2371 0.1920 0.2320 0.0215  -0.0268 -0.0221 663  LYS B C   
13870 O O   . LYS B 665  ? 0.2729 0.2213 0.2633 0.0228  -0.0285 -0.0230 663  LYS B O   
13871 C CB  A LYS B 665  ? 0.2713 0.2392 0.2743 0.0207  -0.0217 -0.0225 663  LYS B CB  
13872 C CB  B LYS B 665  ? 0.2713 0.2392 0.2742 0.0208  -0.0217 -0.0225 663  LYS B CB  
13873 C CG  A LYS B 665  ? 0.3028 0.2791 0.3120 0.0220  -0.0190 -0.0230 663  LYS B CG  
13874 C CG  B LYS B 665  ? 0.3029 0.2790 0.3120 0.0221  -0.0190 -0.0231 663  LYS B CG  
13875 C CD  A LYS B 665  ? 0.2418 0.2229 0.2554 0.0218  -0.0184 -0.0223 663  LYS B CD  
13876 C CD  B LYS B 665  ? 0.3258 0.3071 0.3380 0.0194  -0.0174 -0.0216 663  LYS B CD  
13877 C CE  A LYS B 665  ? 0.2788 0.2677 0.2982 0.0224  -0.0157 -0.0225 663  LYS B CE  
13878 C CE  B LYS B 665  ? 0.2969 0.2854 0.3145 0.0205  -0.0148 -0.0221 663  LYS B CE  
13879 N NZ  A LYS B 665  ? 0.2699 0.2631 0.2936 0.0223  -0.0154 -0.0220 663  LYS B NZ  
13880 N NZ  B LYS B 665  ? 0.3012 0.2934 0.3201 0.0176  -0.0130 -0.0208 663  LYS B NZ  
13881 N N   . SER B 666  ? 0.2904 0.2449 0.2841 0.0183  -0.0272 -0.0202 664  SER B N   
13882 C CA  . SER B 666  ? 0.3081 0.2549 0.2952 0.0154  -0.0294 -0.0188 664  SER B CA  
13883 C C   . SER B 666  ? 0.3428 0.2894 0.3278 0.0120  -0.0284 -0.0183 664  SER B C   
13884 O O   . SER B 666  ? 0.2882 0.2412 0.2770 0.0116  -0.0259 -0.0186 664  SER B O   
13885 C CB  . SER B 666  ? 0.3226 0.2700 0.3092 0.0130  -0.0298 -0.0169 664  SER B CB  
13886 O OG  . SER B 666  ? 0.3492 0.3033 0.3387 0.0101  -0.0272 -0.0159 664  SER B OG  
13887 N N   . ALA B 667  ? 0.3173 0.2562 0.2959 0.0093  -0.0305 -0.0173 665  ALA B N   
13888 C CA  . ALA B 667  ? 0.2960 0.2347 0.2723 0.0055  -0.0298 -0.0166 665  ALA B CA  
13889 C C   . ALA B 667  ? 0.2871 0.2341 0.2672 0.0023  -0.0273 -0.0151 665  ALA B C   
13890 O O   . ALA B 667  ? 0.2766 0.2283 0.2587 0.0012  -0.0255 -0.0153 665  ALA B O   
13891 C CB  . ALA B 667  ? 0.3344 0.2635 0.3032 0.0025  -0.0328 -0.0155 665  ALA B CB  
13892 N N   . LEU B 668  ? 0.2903 0.2391 0.2709 0.0011  -0.0272 -0.0136 666  LEU B N   
13893 C CA  A LEU B 668  ? 0.3054 0.2619 0.2892 -0.0014 -0.0249 -0.0122 666  LEU B CA  
13894 C CA  B LEU B 668  ? 0.3054 0.2619 0.2893 -0.0014 -0.0249 -0.0122 666  LEU B CA  
13895 C C   . LEU B 668  ? 0.2729 0.2370 0.2631 0.0011  -0.0223 -0.0135 666  LEU B C   
13896 O O   . LEU B 668  ? 0.2747 0.2443 0.2671 -0.0005 -0.0203 -0.0131 666  LEU B O   
13897 C CB  A LEU B 668  ? 0.3573 0.3142 0.3405 -0.0024 -0.0252 -0.0108 666  LEU B CB  
13898 C CB  B LEU B 668  ? 0.3575 0.3142 0.3406 -0.0024 -0.0253 -0.0108 666  LEU B CB  
13899 C CG  A LEU B 668  ? 0.3928 0.3451 0.3703 -0.0065 -0.0268 -0.0086 666  LEU B CG  
13900 C CG  B LEU B 668  ? 0.3642 0.3252 0.3468 -0.0064 -0.0240 -0.0087 666  LEU B CG  
13901 C CD1 A LEU B 668  ? 0.3506 0.3033 0.3276 -0.0064 -0.0272 -0.0075 666  LEU B CD1 
13902 C CD1 B LEU B 668  ? 0.4097 0.3679 0.3882 -0.0105 -0.0248 -0.0075 666  LEU B CD1 
13903 C CD2 A LEU B 668  ? 0.4144 0.3713 0.3919 -0.0107 -0.0253 -0.0072 666  LEU B CD2 
13904 C CD2 B LEU B 668  ? 0.4437 0.4031 0.4241 -0.0070 -0.0250 -0.0074 666  LEU B CD2 
13905 N N   . ASN B 669  ? 0.2648 0.2295 0.2579 0.0049  -0.0223 -0.0149 667  ASN B N   
13906 C CA  . ASN B 669  ? 0.2462 0.2179 0.2451 0.0070  -0.0199 -0.0159 667  ASN B CA  
13907 C C   . ASN B 669  ? 0.2786 0.2511 0.2779 0.0074  -0.0190 -0.0170 667  ASN B C   
13908 O O   . ASN B 669  ? 0.2849 0.2634 0.2876 0.0072  -0.0168 -0.0170 667  ASN B O   
13909 C CB  . ASN B 669  ? 0.3221 0.2945 0.3241 0.0106  -0.0204 -0.0171 667  ASN B CB  
13910 C CG  . ASN B 669  ? 0.3545 0.3272 0.3567 0.0102  -0.0211 -0.0162 667  ASN B CG  
13911 O OD1 . ASN B 669  ? 0.4204 0.3957 0.4226 0.0078  -0.0201 -0.0149 667  ASN B OD1 
13912 N ND2 . ASN B 669  ? 0.3741 0.3443 0.3765 0.0128  -0.0228 -0.0169 667  ASN B ND2 
13913 N N   . ALA B 670  ? 0.2424 0.2087 0.2377 0.0082  -0.0208 -0.0179 668  ALA B N   
13914 C CA  . ALA B 670  ? 0.2521 0.2187 0.2470 0.0087  -0.0200 -0.0190 668  ALA B CA  
13915 C C   . ALA B 670  ? 0.2163 0.1848 0.2099 0.0048  -0.0192 -0.0178 668  ALA B C   
13916 O O   . ALA B 670  ? 0.2334 0.2061 0.2291 0.0049  -0.0176 -0.0183 668  ALA B O   
13917 C CB  . ALA B 670  ? 0.2324 0.1910 0.2226 0.0106  -0.0223 -0.0205 668  ALA B CB  
13918 N N   . ILE B 671  ? 0.2296 0.1955 0.2199 0.0012  -0.0205 -0.0161 669  ILE B N   
13919 C CA  . ILE B 671  ? 0.2289 0.1980 0.2186 -0.0026 -0.0196 -0.0148 669  ILE B CA  
13920 C C   . ILE B 671  ? 0.2411 0.2191 0.2363 -0.0023 -0.0169 -0.0143 669  ILE B C   
13921 O O   . ILE B 671  ? 0.2383 0.2206 0.2350 -0.0031 -0.0155 -0.0143 669  ILE B O   
13922 C CB  . ILE B 671  ? 0.2556 0.2214 0.2413 -0.0066 -0.0212 -0.0128 669  ILE B CB  
13923 C CG1 . ILE B 671  ? 0.2832 0.2393 0.2625 -0.0076 -0.0242 -0.0131 669  ILE B CG1 
13924 C CG2 . ILE B 671  ? 0.2792 0.2509 0.2658 -0.0104 -0.0199 -0.0112 669  ILE B CG2 
13925 C CD1 . ILE B 671  ? 0.3055 0.2569 0.2804 -0.0111 -0.0261 -0.0111 669  ILE B CD1 
13926 N N   . ALA B 672  ? 0.2225 0.2032 0.2205 -0.0012 -0.0161 -0.0139 670  ALA B N   
13927 C CA  . ALA B 672  ? 0.2643 0.2525 0.2669 -0.0007 -0.0137 -0.0135 670  ALA B CA  
13928 C C   . ALA B 672  ? 0.2462 0.2375 0.2523 0.0019  -0.0122 -0.0148 670  ALA B C   
13929 O O   . ALA B 672  ? 0.2387 0.2355 0.2475 0.0017  -0.0104 -0.0145 670  ALA B O   
13930 C CB  . ALA B 672  ? 0.2847 0.2738 0.2889 0.0003  -0.0137 -0.0131 670  ALA B CB  
13931 N N   . GLU B 673  ? 0.2169 0.2051 0.2230 0.0046  -0.0130 -0.0163 671  GLU B N   
13932 C CA  . GLU B 673  ? 0.2197 0.2109 0.2287 0.0070  -0.0115 -0.0175 671  GLU B CA  
13933 C C   . GLU B 673  ? 0.2293 0.2214 0.2368 0.0058  -0.0109 -0.0176 671  GLU B C   
13934 O O   . GLU B 673  ? 0.2184 0.2156 0.2287 0.0061  -0.0090 -0.0175 671  GLU B O   
13935 C CB  . GLU B 673  ? 0.2275 0.2151 0.2361 0.0101  -0.0125 -0.0191 671  GLU B CB  
13936 C CG  . GLU B 673  ? 0.2472 0.2382 0.2586 0.0127  -0.0109 -0.0204 671  GLU B CG  
13937 C CD  . GLU B 673  ? 0.3270 0.3233 0.3437 0.0142  -0.0094 -0.0203 671  GLU B CD  
13938 O OE1 . GLU B 673  ? 0.3668 0.3637 0.3849 0.0137  -0.0098 -0.0195 671  GLU B OE1 
13939 O OE2 . GLU B 673  ? 0.2467 0.2466 0.2661 0.0158  -0.0078 -0.0209 671  GLU B OE2 
13940 N N   . VAL B 674  ? 0.2062 0.1931 0.2090 0.0042  -0.0127 -0.0178 672  VAL B N   
13941 C CA  . VAL B 674  ? 0.1977 0.1851 0.1987 0.0027  -0.0125 -0.0179 672  VAL B CA  
13942 C C   . VAL B 674  ? 0.1901 0.1829 0.1926 -0.0001 -0.0114 -0.0162 672  VAL B C   
13943 O O   . VAL B 674  ? 0.1985 0.1955 0.2024 -0.0001 -0.0102 -0.0162 672  VAL B O   
13944 C CB  . VAL B 674  ? 0.2129 0.1927 0.2080 0.0013  -0.0151 -0.0185 672  VAL B CB  
13945 C CG1 . VAL B 674  ? 0.2163 0.1966 0.2093 -0.0004 -0.0151 -0.0187 672  VAL B CG1 
13946 C CG2 . VAL B 674  ? 0.2380 0.2125 0.2315 0.0049  -0.0162 -0.0204 672  VAL B CG2 
13947 N N   . ARG B 675  ? 0.1888 0.1822 0.1911 -0.0022 -0.0118 -0.0148 673  ARG B N   
13948 C CA  . ARG B 675  ? 0.2019 0.2013 0.2060 -0.0043 -0.0106 -0.0133 673  ARG B CA  
13949 C C   . ARG B 675  ? 0.1915 0.1968 0.2001 -0.0020 -0.0083 -0.0134 673  ARG B C   
13950 O O   . ARG B 675  ? 0.1861 0.1962 0.1961 -0.0027 -0.0072 -0.0128 673  ARG B O   
13951 C CB  . ARG B 675  ? 0.1994 0.1990 0.2027 -0.0063 -0.0111 -0.0118 673  ARG B CB  
13952 C CG  . ARG B 675  ? 0.2096 0.2042 0.2081 -0.0097 -0.0133 -0.0110 673  ARG B CG  
13953 C CD  . ARG B 675  ? 0.2044 0.2011 0.2026 -0.0119 -0.0131 -0.0093 673  ARG B CD  
13954 N NE  . ARG B 675  ? 0.2115 0.2161 0.2123 -0.0132 -0.0114 -0.0082 673  ARG B NE  
13955 C CZ  . ARG B 675  ? 0.2215 0.2305 0.2233 -0.0142 -0.0105 -0.0069 673  ARG B CZ  
13956 N NH1 . ARG B 675  ? 0.2424 0.2488 0.2431 -0.0140 -0.0110 -0.0065 673  ARG B NH1 
13957 N NH2 . ARG B 675  ? 0.2112 0.2276 0.2154 -0.0150 -0.0090 -0.0060 673  ARG B NH2 
13958 N N   . GLU B 676  ? 0.1819 0.1870 0.1930 0.0006  -0.0077 -0.0140 674  GLU B N   
13959 C CA  . GLU B 676  ? 0.2016 0.2117 0.2168 0.0024  -0.0057 -0.0140 674  GLU B CA  
13960 C C   . GLU B 676  ? 0.1780 0.1897 0.1938 0.0035  -0.0048 -0.0147 674  GLU B C   
13961 O O   . GLU B 676  ? 0.1735 0.1896 0.1914 0.0037  -0.0034 -0.0141 674  GLU B O   
13962 C CB  . GLU B 676  ? 0.2011 0.2104 0.2186 0.0046  -0.0056 -0.0146 674  GLU B CB  
13963 C CG  . GLU B 676  ? 0.2227 0.2364 0.2442 0.0060  -0.0038 -0.0143 674  GLU B CG  
13964 C CD  . GLU B 676  ? 0.3892 0.4049 0.4113 0.0053  -0.0035 -0.0134 674  GLU B CD  
13965 O OE1 . GLU B 676  ? 0.4268 0.4428 0.4468 0.0033  -0.0039 -0.0125 674  GLU B OE1 
13966 O OE2 . GLU B 676  ? 0.3467 0.3637 0.3714 0.0066  -0.0028 -0.0135 674  GLU B OE2 
13967 N N   . ALA B 677  ? 0.1728 0.1807 0.1865 0.0043  -0.0057 -0.0159 675  ALA B N   
13968 C CA  . ALA B 677  ? 0.1785 0.1879 0.1922 0.0053  -0.0048 -0.0166 675  ALA B CA  
13969 C C   . ALA B 677  ? 0.1769 0.1884 0.1890 0.0030  -0.0049 -0.0158 675  ALA B C   
13970 O O   . ALA B 677  ? 0.1796 0.1951 0.1932 0.0035  -0.0036 -0.0154 675  ALA B O   
13971 C CB  . ALA B 677  ? 0.1886 0.1931 0.1996 0.0067  -0.0059 -0.0183 675  ALA B CB  
13972 N N   . ILE B 678  ? 0.1781 0.1872 0.1872 0.0003  -0.0065 -0.0153 676  ILE B N   
13973 C CA  . ILE B 678  ? 0.1603 0.1721 0.1682 -0.0023 -0.0068 -0.0143 676  ILE B CA  
13974 C C   . ILE B 678  ? 0.1828 0.2013 0.1942 -0.0023 -0.0052 -0.0130 676  ILE B C   
13975 O O   . ILE B 678  ? 0.1826 0.2052 0.1947 -0.0026 -0.0046 -0.0125 676  ILE B O   
13976 C CB  . ILE B 678  ? 0.1855 0.1936 0.1897 -0.0056 -0.0090 -0.0138 676  ILE B CB  
13977 C CG1 . ILE B 678  ? 0.2104 0.2113 0.2103 -0.0055 -0.0108 -0.0153 676  ILE B CG1 
13978 C CG2 . ILE B 678  ? 0.1942 0.2069 0.1982 -0.0088 -0.0092 -0.0124 676  ILE B CG2 
13979 C CD1 . ILE B 678  ? 0.1932 0.1886 0.1894 -0.0082 -0.0130 -0.0148 676  ILE B CD1 
13980 N N   . ASP B 679  ? 0.1740 0.1934 0.1874 -0.0018 -0.0047 -0.0124 677  ASP B N   
13981 C CA  . ASP B 679  ? 0.1754 0.2005 0.1916 -0.0015 -0.0033 -0.0112 677  ASP B CA  
13982 C C   . ASP B 679  ? 0.1725 0.2000 0.1913 0.0011  -0.0017 -0.0115 677  ASP B C   
13983 O O   . ASP B 679  ? 0.1781 0.2102 0.1983 0.0013  -0.0008 -0.0107 677  ASP B O   
13984 C CB  . ASP B 679  ? 0.1775 0.2023 0.1945 -0.0015 -0.0033 -0.0108 677  ASP B CB  
13985 C CG  . ASP B 679  ? 0.2039 0.2276 0.2183 -0.0046 -0.0046 -0.0100 677  ASP B CG  
13986 O OD1 . ASP B 679  ? 0.2389 0.2648 0.2520 -0.0069 -0.0051 -0.0092 677  ASP B OD1 
13987 O OD2 . ASP B 679  ? 0.2411 0.2619 0.2547 -0.0047 -0.0052 -0.0099 677  ASP B OD2 
13988 N N   . PHE B 680  ? 0.1604 0.1854 0.1802 0.0031  -0.0013 -0.0125 678  PHE B N   
13989 C CA  . PHE B 680  ? 0.1781 0.2052 0.1999 0.0051  0.0002  -0.0125 678  PHE B CA  
13990 C C   . PHE B 680  ? 0.1898 0.2188 0.2103 0.0046  0.0003  -0.0124 678  PHE B C   
13991 O O   . PHE B 680  ? 0.1753 0.2078 0.1972 0.0053  0.0014  -0.0116 678  PHE B O   
13992 C CB  . PHE B 680  ? 0.1787 0.2032 0.2014 0.0068  0.0005  -0.0137 678  PHE B CB  
13993 C CG  . PHE B 680  ? 0.1571 0.1813 0.1823 0.0079  0.0008  -0.0136 678  PHE B CG  
13994 C CD1 . PHE B 680  ? 0.1944 0.2212 0.2218 0.0083  0.0018  -0.0127 678  PHE B CD1 
13995 C CD2 . PHE B 680  ? 0.1672 0.1881 0.1923 0.0085  0.0000  -0.0146 678  PHE B CD2 
13996 C CE1 . PHE B 680  ? 0.2147 0.2407 0.2441 0.0091  0.0019  -0.0128 678  PHE B CE1 
13997 C CE2 . PHE B 680  ? 0.2250 0.2459 0.2525 0.0093  0.0001  -0.0146 678  PHE B CE2 
13998 C CZ  . PHE B 680  ? 0.2045 0.2277 0.2339 0.0094  0.0010  -0.0137 678  PHE B CZ  
13999 N N   . LEU B 681  ? 0.1678 0.1940 0.1853 0.0036  -0.0008 -0.0132 679  LEU B N   
14000 C CA  . LEU B 681  ? 0.1620 0.1897 0.1778 0.0031  -0.0010 -0.0133 679  LEU B CA  
14001 C C   . LEU B 681  ? 0.1783 0.2106 0.1946 0.0016  -0.0010 -0.0119 679  LEU B C   
14002 O O   . LEU B 681  ? 0.1758 0.2115 0.1928 0.0024  -0.0002 -0.0113 679  LEU B O   
14003 C CB  . LEU B 681  ? 0.1756 0.1987 0.1874 0.0019  -0.0026 -0.0145 679  LEU B CB  
14004 C CG  . LEU B 681  ? 0.1556 0.1748 0.1666 0.0041  -0.0025 -0.0161 679  LEU B CG  
14005 C CD1 . LEU B 681  ? 0.1791 0.1924 0.1859 0.0030  -0.0045 -0.0173 679  LEU B CD1 
14006 C CD2 . LEU B 681  ? 0.1820 0.2031 0.1931 0.0059  -0.0011 -0.0166 679  LEU B CD2 
14007 N N   . ARG B 682  ? 0.1671 0.1998 0.1830 -0.0005 -0.0020 -0.0113 680  ARG B N   
14008 C CA  . ARG B 682  ? 0.1605 0.1985 0.1770 -0.0020 -0.0021 -0.0100 680  ARG B CA  
14009 C C   . ARG B 682  ? 0.1767 0.2190 0.1965 0.0000  -0.0006 -0.0090 680  ARG B C   
14010 O O   . ARG B 682  ? 0.1821 0.2292 0.2028 0.0002  -0.0003 -0.0082 680  ARG B O   
14011 C CB  . ARG B 682  ? 0.1579 0.1956 0.1730 -0.0050 -0.0035 -0.0094 680  ARG B CB  
14012 C CG  . ARG B 682  ? 0.1782 0.2116 0.1895 -0.0074 -0.0054 -0.0102 680  ARG B CG  
14013 C CD  . ARG B 682  ? 0.1742 0.2070 0.1841 -0.0108 -0.0067 -0.0094 680  ARG B CD  
14014 N NE  . ARG B 682  ? 0.1936 0.2219 0.1993 -0.0135 -0.0089 -0.0099 680  ARG B NE  
14015 C CZ  . ARG B 682  ? 0.1999 0.2243 0.2029 -0.0165 -0.0105 -0.0096 680  ARG B CZ  
14016 N NH1 . ARG B 682  ? 0.2215 0.2465 0.2255 -0.0171 -0.0102 -0.0086 680  ARG B NH1 
14017 N NH2 . ARG B 682  ? 0.2355 0.2548 0.2343 -0.0188 -0.0126 -0.0102 680  ARG B NH2 
14018 N N   . TYR B 683  ? 0.1777 0.2182 0.1991 0.0016  0.0002  -0.0093 681  TYR B N   
14019 C CA  . TYR B 683  ? 0.1901 0.2336 0.2139 0.0036  0.0015  -0.0086 681  TYR B CA  
14020 C C   . TYR B 683  ? 0.1893 0.2336 0.2139 0.0055  0.0024  -0.0084 681  TYR B C   
14021 O O   . TYR B 683  ? 0.1733 0.2213 0.1988 0.0066  0.0029  -0.0075 681  TYR B O   
14022 C CB  . TYR B 683  ? 0.1534 0.1941 0.1783 0.0045  0.0018  -0.0090 681  TYR B CB  
14023 C CG  . TYR B 683  ? 0.1643 0.2069 0.1912 0.0066  0.0029  -0.0085 681  TYR B CG  
14024 C CD1 . TYR B 683  ? 0.1832 0.2294 0.2106 0.0068  0.0031  -0.0078 681  TYR B CD1 
14025 C CD2 . TYR B 683  ? 0.1554 0.1961 0.1835 0.0085  0.0037  -0.0087 681  TYR B CD2 
14026 C CE1 . TYR B 683  ? 0.1571 0.2043 0.1858 0.0091  0.0039  -0.0075 681  TYR B CE1 
14027 C CE2 . TYR B 683  ? 0.1802 0.2216 0.2096 0.0103  0.0044  -0.0082 681  TYR B CE2 
14028 C CZ  . TYR B 683  ? 0.1728 0.2172 0.2023 0.0107  0.0045  -0.0078 681  TYR B CZ  
14029 O OH  . TYR B 683  ? 0.1912 0.2357 0.2215 0.0128  0.0051  -0.0075 681  TYR B OH  
14030 N N   . TYR B 684  ? 0.1628 0.2039 0.1869 0.0062  0.0027  -0.0092 682  TYR B N   
14031 C CA  . TYR B 684  ? 0.1660 0.2079 0.1905 0.0078  0.0037  -0.0088 682  TYR B CA  
14032 C C   . TYR B 684  ? 0.1725 0.2172 0.1954 0.0072  0.0033  -0.0084 682  TYR B C   
14033 O O   . TYR B 684  ? 0.1785 0.2254 0.2019 0.0085  0.0039  -0.0075 682  TYR B O   
14034 C CB  . TYR B 684  ? 0.1732 0.2120 0.1978 0.0086  0.0043  -0.0097 682  TYR B CB  
14035 C CG  . TYR B 684  ? 0.1595 0.1962 0.1861 0.0093  0.0047  -0.0100 682  TYR B CG  
14036 C CD1 . TYR B 684  ? 0.1703 0.2079 0.1986 0.0101  0.0052  -0.0092 682  TYR B CD1 
14037 C CD2 . TYR B 684  ? 0.1678 0.2016 0.1942 0.0094  0.0045  -0.0112 682  TYR B CD2 
14038 C CE1 . TYR B 684  ? 0.1694 0.2049 0.1993 0.0106  0.0053  -0.0096 682  TYR B CE1 
14039 C CE2 . TYR B 684  ? 0.1705 0.2028 0.1989 0.0100  0.0046  -0.0114 682  TYR B CE2 
14040 C CZ  . TYR B 684  ? 0.1869 0.2201 0.2171 0.0104  0.0050  -0.0106 682  TYR B CZ  
14041 O OH  . TYR B 684  ? 0.1894 0.2209 0.2213 0.0108  0.0049  -0.0110 682  TYR B OH  
14042 N N   . ALA B 685  ? 0.1710 0.2155 0.1920 0.0051  0.0020  -0.0088 683  ALA B N   
14043 C CA  . ALA B 685  ? 0.1699 0.2174 0.1893 0.0042  0.0012  -0.0084 683  ALA B CA  
14044 C C   . ALA B 685  ? 0.1506 0.2035 0.1718 0.0045  0.0013  -0.0070 683  ALA B C   
14045 O O   . ALA B 685  ? 0.1713 0.2273 0.1926 0.0056  0.0015  -0.0062 683  ALA B O   
14046 C CB  . ALA B 685  ? 0.1673 0.2131 0.1841 0.0015  -0.0005 -0.0092 683  ALA B CB  
14047 N N   . GLU B 686  ? 0.1525 0.2068 0.1751 0.0039  0.0012  -0.0067 684  GLU B N   
14048 C CA  . GLU B 686  ? 0.1836 0.2435 0.2079 0.0046  0.0014  -0.0056 684  GLU B CA  
14049 C C   . GLU B 686  ? 0.1891 0.2492 0.2148 0.0078  0.0026  -0.0051 684  GLU B C   
14050 O O   . GLU B 686  ? 0.1884 0.2524 0.2147 0.0092  0.0027  -0.0042 684  GLU B O   
14051 C CB  . GLU B 686  ? 0.1823 0.2438 0.2075 0.0033  0.0012  -0.0054 684  GLU B CB  
14052 C CG  . GLU B 686  ? 0.2006 0.2683 0.2278 0.0047  0.0017  -0.0044 684  GLU B CG  
14053 C CD  . GLU B 686  ? 0.2782 0.3522 0.3055 0.0039  0.0009  -0.0035 684  GLU B CD  
14054 O OE1 . GLU B 686  ? 0.2561 0.3298 0.2818 0.0017  -0.0003 -0.0037 684  GLU B OE1 
14055 O OE2 . GLU B 686  ? 0.2832 0.3628 0.3123 0.0056  0.0013  -0.0027 684  GLU B OE2 
14056 N N   . GLN B 687  ? 0.1711 0.2269 0.1974 0.0090  0.0035  -0.0056 685  GLN B N   
14057 C CA  . GLN B 687  ? 0.1873 0.2425 0.2147 0.0116  0.0044  -0.0050 685  GLN B CA  
14058 C C   . GLN B 687  ? 0.1711 0.2267 0.1974 0.0125  0.0046  -0.0044 685  GLN B C   
14059 O O   . GLN B 687  ? 0.2016 0.2589 0.2283 0.0145  0.0049  -0.0034 685  GLN B O   
14060 C CB  . GLN B 687  ? 0.2031 0.2535 0.2311 0.0122  0.0051  -0.0056 685  GLN B CB  
14061 C CG  . GLN B 687  ? 0.1853 0.2354 0.2141 0.0118  0.0049  -0.0061 685  GLN B CG  
14062 C CD  . GLN B 687  ? 0.2100 0.2635 0.2395 0.0134  0.0051  -0.0055 685  GLN B CD  
14063 O OE1 . GLN B 687  ? 0.2070 0.2600 0.2369 0.0157  0.0056  -0.0050 685  GLN B OE1 
14064 N NE2 . GLN B 687  ? 0.2744 0.3314 0.3040 0.0123  0.0047  -0.0054 685  GLN B NE2 
14065 N N   . THR B 688  ? 0.1488 0.2029 0.1736 0.0112  0.0044  -0.0049 686  THR B N   
14066 C CA  . THR B 688  ? 0.1739 0.2287 0.1972 0.0119  0.0045  -0.0043 686  THR B CA  
14067 C C   . THR B 688  ? 0.1674 0.2272 0.1904 0.0120  0.0036  -0.0034 686  THR B C   
14068 O O   . THR B 688  ? 0.2058 0.2670 0.2285 0.0138  0.0038  -0.0023 686  THR B O   
14069 C CB  . THR B 688  ? 0.1707 0.2230 0.1920 0.0105  0.0043  -0.0054 686  THR B CB  
14070 O OG1 . THR B 688  ? 0.1855 0.2340 0.2074 0.0109  0.0053  -0.0060 686  THR B OG1 
14071 C CG2 . THR B 688  ? 0.2099 0.2634 0.2292 0.0110  0.0044  -0.0048 686  THR B CG2 
14072 N N   . ARG B 689  ? 0.1544 0.2170 0.1774 0.0101  0.0025  -0.0038 687  ARG B N   
14073 C CA  . ARG B 689  ? 0.1672 0.2355 0.1902 0.0099  0.0015  -0.0029 687  ARG B CA  
14074 C C   . ARG B 689  ? 0.2056 0.2774 0.2307 0.0125  0.0020  -0.0018 687  ARG B C   
14075 O O   . ARG B 689  ? 0.2173 0.2936 0.2425 0.0137  0.0014  -0.0009 687  ARG B O   
14076 C CB  . ARG B 689  ? 0.1939 0.2648 0.2168 0.0069  0.0003  -0.0033 687  ARG B CB  
14077 C CG  . ARG B 689  ? 0.1893 0.2574 0.2095 0.0044  -0.0008 -0.0043 687  ARG B CG  
14078 C CD  . ARG B 689  ? 0.2118 0.2825 0.2316 0.0011  -0.0024 -0.0044 687  ARG B CD  
14079 N NE  . ARG B 689  ? 0.2189 0.2882 0.2398 -0.0001 -0.0021 -0.0046 687  ARG B NE  
14080 C CZ  . ARG B 689  ? 0.2294 0.2934 0.2486 -0.0018 -0.0025 -0.0057 687  ARG B CZ  
14081 N NH1 . ARG B 689  ? 0.2277 0.2870 0.2441 -0.0024 -0.0031 -0.0068 687  ARG B NH1 
14082 N NH2 . ARG B 689  ? 0.2104 0.2736 0.2305 -0.0028 -0.0023 -0.0056 687  ARG B NH2 
14083 N N   . ARG B 690  ? 0.1704 0.2400 0.1968 0.0137  0.0029  -0.0021 688  ARG B N   
14084 C CA  . ARG B 690  ? 0.1751 0.2470 0.2029 0.0165  0.0033  -0.0014 688  ARG B CA  
14085 C C   . ARG B 690  ? 0.1890 0.2576 0.2161 0.0193  0.0039  -0.0007 688  ARG B C   
14086 O O   . ARG B 690  ? 0.1917 0.2621 0.2192 0.0220  0.0039  0.0000  688  ARG B O   
14087 C CB  . ARG B 690  ? 0.1751 0.2456 0.2042 0.0166  0.0039  -0.0021 688  ARG B CB  
14088 C CG  . ARG B 690  ? 0.1905 0.2646 0.2202 0.0141  0.0034  -0.0024 688  ARG B CG  
14089 C CD  . ARG B 690  ? 0.2456 0.3277 0.2767 0.0149  0.0030  -0.0016 688  ARG B CD  
14090 N NE  . ARG B 690  ? 0.2698 0.3529 0.3019 0.0185  0.0038  -0.0014 688  ARG B NE  
14091 C CZ  . ARG B 690  ? 0.3193 0.4048 0.3516 0.0217  0.0037  -0.0007 688  ARG B CZ  
14092 N NH1 . ARG B 690  ? 0.2798 0.3679 0.3117 0.0216  0.0029  0.0000  688  ARG B NH1 
14093 N NH2 . ARG B 690  ? 0.2336 0.3189 0.2662 0.0251  0.0043  -0.0008 688  ARG B NH2 
14094 N N   . THR B 691  ? 0.1871 0.2509 0.2128 0.0187  0.0043  -0.0008 689  THR B N   
14095 C CA  . THR B 691  ? 0.2049 0.2648 0.2300 0.0208  0.0050  0.0000  689  THR B CA  
14096 C C   . THR B 691  ? 0.2327 0.2912 0.2558 0.0208  0.0051  0.0008  689  THR B C   
14097 O O   . THR B 691  ? 0.2586 0.3161 0.2807 0.0228  0.0051  0.0020  689  THR B O   
14098 C CB  . THR B 691  ? 0.1935 0.2483 0.2193 0.0205  0.0058  -0.0007 689  THR B CB  
14099 O OG1 . THR B 691  ? 0.1951 0.2481 0.2208 0.0181  0.0061  -0.0017 689  THR B OG1 
14100 C CG2 . THR B 691  ? 0.2309 0.2865 0.2582 0.0212  0.0058  -0.0013 689  THR B CG2 
14101 N N   . LEU B 692  ? 0.1800 0.2376 0.2021 0.0186  0.0053  0.0001  690  LEU B N   
14102 C CA  . LEU B 692  ? 0.1914 0.2466 0.2116 0.0187  0.0059  0.0008  690  LEU B CA  
14103 C C   . LEU B 692  ? 0.2342 0.2923 0.2523 0.0194  0.0051  0.0018  690  LEU B C   
14104 O O   . LEU B 692  ? 0.2400 0.3017 0.2577 0.0183  0.0041  0.0014  690  LEU B O   
14105 C CB  . LEU B 692  ? 0.1994 0.2525 0.2191 0.0167  0.0065  -0.0005 690  LEU B CB  
14106 C CG  . LEU B 692  ? 0.2039 0.2538 0.2254 0.0163  0.0073  -0.0013 690  LEU B CG  
14107 C CD1 . LEU B 692  ? 0.2335 0.2815 0.2545 0.0149  0.0079  -0.0024 690  LEU B CD1 
14108 C CD2 . LEU B 692  ? 0.2306 0.2777 0.2528 0.0177  0.0080  -0.0001 690  LEU B CD2 
14109 N N   . GLY B 693  ? 0.2486 0.3049 0.2653 0.0210  0.0055  0.0033  691  GLY B N   
14110 C CA  . GLY B 693  ? 0.2238 0.2822 0.2381 0.0219  0.0048  0.0046  691  GLY B CA  
14111 C C   . GLY B 693  ? 0.2369 0.2920 0.2487 0.0218  0.0058  0.0055  691  GLY B C   
14112 O O   . GLY B 693  ? 0.2632 0.3150 0.2754 0.0208  0.0071  0.0052  691  GLY B O   
14113 N N   . PRO B 694  ? 0.2820 0.3383 0.2911 0.0228  0.0052  0.0069  692  PRO B N   
14114 C CA  . PRO B 694  ? 0.3165 0.3703 0.3226 0.0223  0.0062  0.0079  692  PRO B CA  
14115 C C   . PRO B 694  ? 0.3065 0.3557 0.3128 0.0225  0.0075  0.0092  692  PRO B C   
14116 O O   . PRO B 694  ? 0.3496 0.3970 0.3546 0.0213  0.0089  0.0094  692  PRO B O   
14117 C CB  . PRO B 694  ? 0.3333 0.3894 0.3366 0.0237  0.0049  0.0094  692  PRO B CB  
14118 C CG  . PRO B 694  ? 0.3635 0.4244 0.3685 0.0242  0.0031  0.0086  692  PRO B CG  
14119 C CD  . PRO B 694  ? 0.2872 0.3477 0.2959 0.0242  0.0035  0.0076  692  PRO B CD  
14120 N N   . GLY B 695  ? 0.2880 0.3352 0.2955 0.0241  0.0071  0.0099  693  GLY B N   
14121 C CA  . GLY B 695  ? 0.3120 0.3541 0.3194 0.0241  0.0080  0.0111  693  GLY B CA  
14122 C C   . GLY B 695  ? 0.3377 0.3779 0.3478 0.0225  0.0091  0.0099  693  GLY B C   
14123 O O   . GLY B 695  ? 0.3054 0.3416 0.3157 0.0221  0.0098  0.0108  693  GLY B O   
14124 N N   . HIS B 696  ? 0.3095 0.3524 0.3218 0.0214  0.0092  0.0077  694  HIS B N   
14125 C CA  . HIS B 696  ? 0.2255 0.2668 0.2404 0.0200  0.0100  0.0064  694  HIS B CA  
14126 C C   . HIS B 696  ? 0.2936 0.3358 0.3080 0.0183  0.0113  0.0058  694  HIS B C   
14127 O O   . HIS B 696  ? 0.3103 0.3546 0.3254 0.0175  0.0112  0.0040  694  HIS B O   
14128 C CB  . HIS B 696  ? 0.2428 0.2859 0.2602 0.0202  0.0092  0.0047  694  HIS B CB  
14129 C CG  . HIS B 696  ? 0.2373 0.2807 0.2548 0.0222  0.0081  0.0052  694  HIS B CG  
14130 N ND1 . HIS B 696  ? 0.2379 0.2856 0.2556 0.0231  0.0070  0.0047  694  HIS B ND1 
14131 C CD2 . HIS B 696  ? 0.2770 0.3171 0.2945 0.0238  0.0078  0.0061  694  HIS B CD2 
14132 C CE1 . HIS B 696  ? 0.2566 0.3043 0.2747 0.0253  0.0063  0.0053  694  HIS B CE1 
14133 N NE2 . HIS B 696  ? 0.2612 0.3039 0.2789 0.0260  0.0067  0.0060  694  HIS B NE2 
14134 N N   . GLY B 697  ? 0.2943 0.3349 0.3074 0.0177  0.0124  0.0073  695  GLY B N   
14135 C CA  . GLY B 697  ? 0.2892 0.3312 0.3014 0.0165  0.0138  0.0068  695  GLY B CA  
14136 C C   . GLY B 697  ? 0.2811 0.3231 0.2963 0.0154  0.0147  0.0052  695  GLY B C   
14137 O O   . GLY B 697  ? 0.2787 0.3187 0.2964 0.0151  0.0147  0.0052  695  GLY B O   
14138 N N   . PRO B 698  ? 0.2629 0.3069 0.2776 0.0149  0.0154  0.0037  696  PRO B N   
14139 C CA  . PRO B 698  ? 0.2321 0.2764 0.2496 0.0142  0.0162  0.0021  696  PRO B CA  
14140 C C   . PRO B 698  ? 0.2369 0.2809 0.2558 0.0133  0.0178  0.0034  696  PRO B C   
14141 O O   . PRO B 698  ? 0.2661 0.3100 0.2831 0.0129  0.0187  0.0055  696  PRO B O   
14142 C CB  . PRO B 698  ? 0.3140 0.3601 0.3297 0.0144  0.0164  0.0003  696  PRO B CB  
14143 C CG  . PRO B 698  ? 0.4017 0.4489 0.4136 0.0148  0.0166  0.0015  696  PRO B CG  
14144 C CD  . PRO B 698  ? 0.3371 0.3832 0.3485 0.0153  0.0154  0.0032  696  PRO B CD  
14145 N N   . LEU B 699  ? 0.2239 0.2679 0.2461 0.0127  0.0182  0.0023  697  LEU B N   
14146 C CA  . LEU B 699  ? 0.2368 0.2816 0.2609 0.0115  0.0197  0.0033  697  LEU B CA  
14147 C C   . LEU B 699  ? 0.2312 0.2794 0.2540 0.0116  0.0215  0.0030  697  LEU B C   
14148 O O   . LEU B 699  ? 0.2469 0.2965 0.2694 0.0106  0.0231  0.0048  697  LEU B O   
14149 C CB  . LEU B 699  ? 0.2201 0.2644 0.2481 0.0110  0.0193  0.0021  697  LEU B CB  
14150 C CG  . LEU B 699  ? 0.2484 0.2894 0.2776 0.0110  0.0177  0.0022  697  LEU B CG  
14151 C CD1 . LEU B 699  ? 0.2533 0.2944 0.2861 0.0106  0.0173  0.0007  697  LEU B CD1 
14152 C CD2 . LEU B 699  ? 0.2976 0.3359 0.3261 0.0102  0.0177  0.0047  697  LEU B CD2 
14153 N N   . GLY B 700  ? 0.2168 0.2664 0.2387 0.0127  0.0213  0.0007  698  GLY B N   
14154 C CA  . GLY B 700  ? 0.2051 0.2579 0.2261 0.0133  0.0229  -0.0002 698  GLY B CA  
14155 C C   . GLY B 700  ? 0.2140 0.2675 0.2375 0.0140  0.0226  -0.0028 698  GLY B C   
14156 O O   . GLY B 700  ? 0.2129 0.2640 0.2377 0.0142  0.0210  -0.0039 698  GLY B O   
14157 N N   . PRO B 701  ? 0.2108 0.2675 0.2347 0.0147  0.0243  -0.0037 699  PRO B N   
14158 C CA  . PRO B 701  ? 0.1779 0.2352 0.2040 0.0159  0.0240  -0.0062 699  PRO B CA  
14159 C C   . PRO B 701  ? 0.2185 0.2748 0.2491 0.0150  0.0230  -0.0060 699  PRO B C   
14160 O O   . PRO B 701  ? 0.2246 0.2822 0.2580 0.0136  0.0238  -0.0043 699  PRO B O   
14161 C CB  . PRO B 701  ? 0.2245 0.2866 0.2510 0.0167  0.0263  -0.0064 699  PRO B CB  
14162 C CG  . PRO B 701  ? 0.2266 0.2898 0.2492 0.0164  0.0276  -0.0049 699  PRO B CG  
14163 C CD  . PRO B 701  ? 0.2242 0.2846 0.2467 0.0146  0.0266  -0.0024 699  PRO B CD  
14164 N N   . ILE B 702  ? 0.2013 0.2549 0.2322 0.0157  0.0212  -0.0079 700  ILE B N   
14165 C CA  A ILE B 702  ? 0.1858 0.2381 0.2203 0.0151  0.0201  -0.0080 700  ILE B CA  
14166 C CA  B ILE B 702  ? 0.1861 0.2383 0.2206 0.0151  0.0200  -0.0080 700  ILE B CA  
14167 C C   . ILE B 702  ? 0.2166 0.2698 0.2527 0.0166  0.0198  -0.0103 700  ILE B C   
14168 O O   . ILE B 702  ? 0.1872 0.2390 0.2206 0.0181  0.0192  -0.0122 700  ILE B O   
14169 C CB  A ILE B 702  ? 0.1827 0.2309 0.2162 0.0146  0.0181  -0.0080 700  ILE B CB  
14170 C CB  B ILE B 702  ? 0.1832 0.2313 0.2165 0.0147  0.0180  -0.0081 700  ILE B CB  
14171 C CG1 A ILE B 702  ? 0.2184 0.2658 0.2513 0.0134  0.0182  -0.0056 700  ILE B CG1 
14172 C CG1 B ILE B 702  ? 0.2164 0.2636 0.2480 0.0137  0.0181  -0.0060 700  ILE B CG1 
14173 C CG2 A ILE B 702  ? 0.2181 0.2647 0.2546 0.0144  0.0167  -0.0089 700  ILE B CG2 
14174 C CG2 B ILE B 702  ? 0.2164 0.2630 0.2530 0.0142  0.0168  -0.0085 700  ILE B CG2 
14175 C CD1 A ILE B 702  ? 0.1774 0.2218 0.2094 0.0132  0.0165  -0.0055 700  ILE B CD1 
14176 C CD1 B ILE B 702  ? 0.2252 0.2728 0.2591 0.0124  0.0189  -0.0039 700  ILE B CD1 
14177 N N   . VAL B 703  ? 0.1981 0.2536 0.2384 0.0162  0.0202  -0.0100 701  VAL B N   
14178 C CA  . VAL B 703  ? 0.1638 0.2205 0.2062 0.0178  0.0198  -0.0120 701  VAL B CA  
14179 C C   . VAL B 703  ? 0.1960 0.2486 0.2393 0.0174  0.0175  -0.0126 701  VAL B C   
14180 O O   . VAL B 703  ? 0.1995 0.2513 0.2450 0.0158  0.0170  -0.0113 701  VAL B O   
14181 C CB  . VAL B 703  ? 0.1811 0.2433 0.2279 0.0174  0.0214  -0.0112 701  VAL B CB  
14182 C CG1 . VAL B 703  ? 0.1855 0.2489 0.2350 0.0192  0.0206  -0.0131 701  VAL B CG1 
14183 C CG2 . VAL B 703  ? 0.1863 0.2528 0.2318 0.0180  0.0238  -0.0107 701  VAL B CG2 
14184 N N   . CYS B 704  ? 0.1642 0.2140 0.2055 0.0190  0.0161  -0.0146 702  CYS B N   
14185 C CA  . CYS B 704  ? 0.1599 0.2059 0.2015 0.0186  0.0139  -0.0152 702  CYS B CA  
14186 C C   . CYS B 704  ? 0.1839 0.2307 0.2276 0.0203  0.0133  -0.0168 702  CYS B C   
14187 O O   . CYS B 704  ? 0.1789 0.2255 0.2209 0.0224  0.0132  -0.0185 702  CYS B O   
14188 C CB  . CYS B 704  ? 0.1708 0.2125 0.2080 0.0186  0.0126  -0.0160 702  CYS B CB  
14189 S SG  . CYS B 704  ? 0.1878 0.2291 0.2226 0.0170  0.0130  -0.0142 702  CYS B SG  
14190 N N   . ILE B 705  ? 0.1649 0.2124 0.2123 0.0194  0.0127  -0.0162 703  ILE B N   
14191 C CA  . ILE B 705  ? 0.1643 0.2132 0.2144 0.0210  0.0119  -0.0175 703  ILE B CA  
14192 C C   . ILE B 705  ? 0.1780 0.2223 0.2275 0.0205  0.0095  -0.0179 703  ILE B C   
14193 O O   . ILE B 705  ? 0.1862 0.2291 0.2365 0.0186  0.0090  -0.0167 703  ILE B O   
14194 C CB  . ILE B 705  ? 0.1606 0.2151 0.2158 0.0202  0.0131  -0.0164 703  ILE B CB  
14195 C CG1 . ILE B 705  ? 0.1963 0.2558 0.2518 0.0207  0.0156  -0.0161 703  ILE B CG1 
14196 C CG2 . ILE B 705  ? 0.2013 0.2573 0.2595 0.0216  0.0119  -0.0177 703  ILE B CG2 
14197 C CD1 . ILE B 705  ? 0.2263 0.2914 0.2864 0.0190  0.0170  -0.0144 703  ILE B CD1 
14198 N N   . SER B 706  ? 0.1880 0.2296 0.2356 0.0224  0.0081  -0.0196 704  SER B N   
14199 C CA  . SER B 706  ? 0.2134 0.2499 0.2591 0.0219  0.0058  -0.0199 704  SER B CA  
14200 C C   . SER B 706  ? 0.1975 0.2337 0.2451 0.0235  0.0043  -0.0210 704  SER B C   
14201 O O   . SER B 706  ? 0.2043 0.2436 0.2537 0.0257  0.0048  -0.0220 704  SER B O   
14202 C CB  . SER B 706  ? 0.2316 0.2635 0.2722 0.0221  0.0050  -0.0207 704  SER B CB  
14203 O OG  . SER B 706  ? 0.2086 0.2405 0.2475 0.0245  0.0052  -0.0223 704  SER B OG  
14204 N N   . PRO B 707  ? 0.2092 0.2421 0.2564 0.0225  0.0025  -0.0208 705  PRO B N   
14205 C CA  . PRO B 707  ? 0.2284 0.2608 0.2772 0.0240  0.0008  -0.0216 705  PRO B CA  
14206 C C   . PRO B 707  ? 0.2406 0.2681 0.2853 0.0259  -0.0010 -0.0231 705  PRO B C   
14207 O O   . PRO B 707  ? 0.2646 0.2884 0.3051 0.0255  -0.0011 -0.0233 705  PRO B O   
14208 C CB  . PRO B 707  ? 0.2217 0.2523 0.2710 0.0218  -0.0004 -0.0206 705  PRO B CB  
14209 C CG  . PRO B 707  ? 0.2247 0.2522 0.2705 0.0200  -0.0001 -0.0198 705  PRO B CG  
14210 C CD  . PRO B 707  ? 0.2586 0.2888 0.3041 0.0201  0.0020  -0.0196 705  PRO B CD  
14211 N N   . TRP B 708  ? 0.2085 0.2358 0.2545 0.0279  -0.0025 -0.0240 706  TRP B N   
14212 C CA  . TRP B 708  ? 0.2098 0.2314 0.2515 0.0298  -0.0045 -0.0253 706  TRP B CA  
14213 C C   . TRP B 708  ? 0.2417 0.2573 0.2799 0.0279  -0.0065 -0.0246 706  TRP B C   
14214 O O   . TRP B 708  ? 0.2810 0.2908 0.3146 0.0286  -0.0081 -0.0253 706  TRP B O   
14215 C CB  . TRP B 708  ? 0.2063 0.2296 0.2502 0.0332  -0.0056 -0.0266 706  TRP B CB  
14216 C CG  . TRP B 708  ? 0.2723 0.2989 0.3206 0.0326  -0.0063 -0.0259 706  TRP B CG  
14217 C CD1 . TRP B 708  ? 0.3932 0.4270 0.4472 0.0324  -0.0048 -0.0254 706  TRP B CD1 
14218 C CD2 . TRP B 708  ? 0.2951 0.3180 0.3425 0.0319  -0.0087 -0.0255 706  TRP B CD2 
14219 N NE1 . TRP B 708  ? 0.3584 0.3931 0.4151 0.0315  -0.0063 -0.0249 706  TRP B NE1 
14220 C CE2 . TRP B 708  ? 0.2382 0.2662 0.2908 0.0313  -0.0086 -0.0250 706  TRP B CE2 
14221 C CE3 . TRP B 708  ? 0.2999 0.3155 0.3424 0.0315  -0.0108 -0.0255 706  TRP B CE3 
14222 C CZ2 . TRP B 708  ? 0.3733 0.3994 0.4262 0.0306  -0.0108 -0.0246 706  TRP B CZ2 
14223 C CZ3 . TRP B 708  ? 0.2694 0.2833 0.3121 0.0308  -0.0128 -0.0249 706  TRP B CZ3 
14224 C CH2 . TRP B 708  ? 0.3880 0.4070 0.4358 0.0305  -0.0128 -0.0246 706  TRP B CH2 
14225 N N   . ASN B 709  ? 0.1882 0.2047 0.2282 0.0256  -0.0066 -0.0233 707  ASN B N   
14226 C CA  . ASN B 709  ? 0.2069 0.2183 0.2438 0.0244  -0.0087 -0.0228 707  ASN B CA  
14227 C C   . ASN B 709  ? 0.2332 0.2409 0.2658 0.0220  -0.0085 -0.0221 707  ASN B C   
14228 O O   . ASN B 709  ? 0.2605 0.2634 0.2894 0.0211  -0.0103 -0.0218 707  ASN B O   
14229 C CB  . ASN B 709  ? 0.1815 0.1950 0.2215 0.0232  -0.0091 -0.0220 707  ASN B CB  
14230 C CG  . ASN B 709  ? 0.2203 0.2365 0.2618 0.0208  -0.0073 -0.0208 707  ASN B CG  
14231 O OD1 . ASN B 709  ? 0.3085 0.3284 0.3521 0.0207  -0.0054 -0.0207 707  ASN B OD1 
14232 N ND2 . ASN B 709  ? 0.2750 0.2891 0.3149 0.0190  -0.0080 -0.0200 707  ASN B ND2 
14233 N N   . PHE B 710  ? 0.2053 0.2156 0.2383 0.0208  -0.0066 -0.0216 708  PHE B N   
14234 C CA  . PHE B 710  ? 0.2302 0.2380 0.2594 0.0189  -0.0064 -0.0210 708  PHE B CA  
14235 C C   . PHE B 710  ? 0.2169 0.2256 0.2452 0.0200  -0.0053 -0.0219 708  PHE B C   
14236 O O   . PHE B 710  ? 0.2033 0.2154 0.2327 0.0191  -0.0035 -0.0213 708  PHE B O   
14237 C CB  . PHE B 710  ? 0.1973 0.2075 0.2276 0.0165  -0.0053 -0.0196 708  PHE B CB  
14238 C CG  . PHE B 710  ? 0.2753 0.2847 0.3061 0.0156  -0.0063 -0.0189 708  PHE B CG  
14239 C CD1 . PHE B 710  ? 0.3612 0.3663 0.3891 0.0153  -0.0084 -0.0189 708  PHE B CD1 
14240 C CD2 . PHE B 710  ? 0.3241 0.3368 0.3580 0.0150  -0.0053 -0.0182 708  PHE B CD2 
14241 C CE1 . PHE B 710  ? 0.2856 0.2901 0.3136 0.0145  -0.0092 -0.0183 708  PHE B CE1 
14242 C CE2 . PHE B 710  ? 0.2913 0.3031 0.3253 0.0143  -0.0063 -0.0177 708  PHE B CE2 
14243 C CZ  . PHE B 710  ? 0.3038 0.3117 0.3348 0.0141  -0.0082 -0.0178 708  PHE B CZ  
14244 N N   . PRO B 711  ? 0.2153 0.2209 0.2413 0.0221  -0.0064 -0.0233 709  PRO B N   
14245 C CA  . PRO B 711  ? 0.1979 0.2051 0.2236 0.0241  -0.0052 -0.0245 709  PRO B CA  
14246 C C   . PRO B 711  ? 0.1923 0.1977 0.2143 0.0225  -0.0048 -0.0244 709  PRO B C   
14247 O O   . PRO B 711  ? 0.2209 0.2282 0.2426 0.0239  -0.0035 -0.0252 709  PRO B O   
14248 C CB  . PRO B 711  ? 0.2404 0.2439 0.2643 0.0271  -0.0069 -0.0262 709  PRO B CB  
14249 C CG  . PRO B 711  ? 0.2347 0.2319 0.2551 0.0256  -0.0094 -0.0257 709  PRO B CG  
14250 C CD  . PRO B 711  ? 0.2161 0.2162 0.2394 0.0231  -0.0089 -0.0239 709  PRO B CD  
14251 N N   . LEU B 712  ? 0.1934 0.1957 0.2126 0.0198  -0.0058 -0.0234 710  LEU B N   
14252 C CA  . LEU B 712  ? 0.1945 0.1964 0.2109 0.0178  -0.0054 -0.0230 710  LEU B CA  
14253 C C   . LEU B 712  ? 0.1965 0.2025 0.2152 0.0154  -0.0041 -0.0212 710  LEU B C   
14254 O O   . LEU B 712  ? 0.2072 0.2161 0.2260 0.0148  -0.0028 -0.0208 710  LEU B O   
14255 C CB  . LEU B 712  ? 0.2212 0.2165 0.2322 0.0162  -0.0077 -0.0233 710  LEU B CB  
14256 C CG  . LEU B 712  ? 0.1774 0.1724 0.1854 0.0141  -0.0076 -0.0230 710  LEU B CG  
14257 C CD1 . LEU B 712  ? 0.2019 0.1978 0.2089 0.0161  -0.0066 -0.0244 710  LEU B CD1 
14258 C CD2 . LEU B 712  ? 0.2444 0.2329 0.2471 0.0117  -0.0101 -0.0228 710  LEU B CD2 
14259 N N   . ALA B 713  ? 0.2100 0.2162 0.2301 0.0142  -0.0046 -0.0202 711  ALA B N   
14260 C CA  . ALA B 713  ? 0.2029 0.2122 0.2243 0.0121  -0.0037 -0.0186 711  ALA B CA  
14261 C C   . ALA B 713  ? 0.1858 0.2002 0.2112 0.0130  -0.0016 -0.0182 711  ALA B C   
14262 O O   . ALA B 713  ? 0.2088 0.2257 0.2341 0.0122  -0.0005 -0.0175 711  ALA B O   
14263 C CB  . ALA B 713  ? 0.2094 0.2175 0.2309 0.0109  -0.0047 -0.0178 711  ALA B CB  
14264 N N   . ILE B 714  ? 0.2005 0.2164 0.2291 0.0145  -0.0012 -0.0185 712  ILE B N   
14265 C CA  . ILE B 714  ? 0.2049 0.2251 0.2369 0.0148  0.0007  -0.0178 712  ILE B CA  
14266 C C   . ILE B 714  ? 0.2091 0.2313 0.2410 0.0159  0.0020  -0.0183 712  ILE B C   
14267 O O   . ILE B 714  ? 0.1933 0.2184 0.2261 0.0154  0.0035  -0.0174 712  ILE B O   
14268 C CB  . ILE B 714  ? 0.2024 0.2240 0.2381 0.0156  0.0006  -0.0179 712  ILE B CB  
14269 C CG1 . ILE B 714  ? 0.2170 0.2368 0.2523 0.0143  -0.0004 -0.0172 712  ILE B CG1 
14270 C CG2 . ILE B 714  ? 0.2239 0.2496 0.2630 0.0158  0.0024  -0.0172 712  ILE B CG2 
14271 C CD1 . ILE B 714  ? 0.3489 0.3702 0.3875 0.0145  -0.0005 -0.0169 712  ILE B CD1 
14272 N N   . PHE B 715  ? 0.2024 0.2228 0.2328 0.0175  0.0015  -0.0197 713  PHE B N   
14273 C CA  . PHE B 715  ? 0.1827 0.2044 0.2118 0.0187  0.0026  -0.0205 713  PHE B CA  
14274 C C   . PHE B 715  ? 0.1865 0.2081 0.2130 0.0171  0.0029  -0.0198 713  PHE B C   
14275 O O   . PHE B 715  ? 0.1859 0.2108 0.2132 0.0171  0.0046  -0.0191 713  PHE B O   
14276 C CB  . PHE B 715  ? 0.1800 0.1982 0.2065 0.0207  0.0013  -0.0224 713  PHE B CB  
14277 C CG  . PHE B 715  ? 0.1737 0.1926 0.1980 0.0222  0.0023  -0.0235 713  PHE B CG  
14278 C CD1 . PHE B 715  ? 0.1853 0.2088 0.2125 0.0242  0.0041  -0.0238 713  PHE B CD1 
14279 C CD2 . PHE B 715  ? 0.1915 0.2068 0.2110 0.0215  0.0014  -0.0240 713  PHE B CD2 
14280 C CE1 . PHE B 715  ? 0.2138 0.2384 0.2388 0.0257  0.0052  -0.0249 713  PHE B CE1 
14281 C CE2 . PHE B 715  ? 0.2234 0.2392 0.2405 0.0230  0.0022  -0.0252 713  PHE B CE2 
14282 C CZ  . PHE B 715  ? 0.2203 0.2407 0.2401 0.0253  0.0042  -0.0257 713  PHE B CZ  
14283 N N   . THR B 716  ? 0.1868 0.2050 0.2102 0.0155  0.0013  -0.0197 714  THR B N   
14284 C CA  . THR B 716  ? 0.1611 0.1795 0.1819 0.0139  0.0013  -0.0191 714  THR B CA  
14285 C C   . THR B 716  ? 0.1910 0.2132 0.2141 0.0127  0.0025  -0.0174 714  THR B C   
14286 O O   . THR B 716  ? 0.1899 0.2144 0.2125 0.0124  0.0034  -0.0168 714  THR B O   
14287 C CB  . THR B 716  ? 0.1867 0.2008 0.2038 0.0121  -0.0008 -0.0193 714  THR B CB  
14288 O OG1 . THR B 716  ? 0.2130 0.2226 0.2271 0.0134  -0.0021 -0.0210 714  THR B OG1 
14289 C CG2 . THR B 716  ? 0.2123 0.2276 0.2273 0.0101  -0.0009 -0.0185 714  THR B CG2 
14290 N N   . GLY B 717  ? 0.1842 0.2069 0.2098 0.0122  0.0024  -0.0166 715  GLY B N   
14291 C CA  . GLY B 717  ? 0.1760 0.2015 0.2034 0.0115  0.0033  -0.0151 715  GLY B CA  
14292 C C   . GLY B 717  ? 0.1611 0.1897 0.1905 0.0124  0.0050  -0.0145 715  GLY B C   
14293 O O   . GLY B 717  ? 0.1859 0.2163 0.2147 0.0120  0.0057  -0.0135 715  GLY B O   
14294 N N   . GLN B 718  ? 0.1643 0.1934 0.1958 0.0136  0.0057  -0.0150 716  GLN B N   
14295 C CA  . GLN B 718  ? 0.1751 0.2073 0.2085 0.0141  0.0075  -0.0142 716  GLN B CA  
14296 C C   . GLN B 718  ? 0.1780 0.2112 0.2089 0.0144  0.0083  -0.0142 716  GLN B C   
14297 O O   . GLN B 718  ? 0.1775 0.2125 0.2082 0.0140  0.0092  -0.0130 716  GLN B O   
14298 C CB  . GLN B 718  ? 0.1699 0.2033 0.2062 0.0150  0.0081  -0.0147 716  GLN B CB  
14299 C CG  . GLN B 718  ? 0.1776 0.2102 0.2165 0.0146  0.0073  -0.0145 716  GLN B CG  
14300 C CD  . GLN B 718  ? 0.2004 0.2351 0.2427 0.0153  0.0077  -0.0148 716  GLN B CD  
14301 O OE1 . GLN B 718  ? 0.2393 0.2747 0.2842 0.0146  0.0077  -0.0140 716  GLN B OE1 
14302 N NE2 . GLN B 718  ? 0.1977 0.2336 0.2400 0.0168  0.0081  -0.0160 716  GLN B NE2 
14303 N N   . ILE B 719  ? 0.1570 0.1887 0.1856 0.0151  0.0077  -0.0157 717  ILE B N   
14304 C CA  . ILE B 719  ? 0.1647 0.1971 0.1904 0.0156  0.0083  -0.0161 717  ILE B CA  
14305 C C   . ILE B 719  ? 0.1864 0.2187 0.2098 0.0142  0.0077  -0.0153 717  ILE B C   
14306 O O   . ILE B 719  ? 0.1814 0.2156 0.2037 0.0142  0.0087  -0.0145 717  ILE B O   
14307 C CB  . ILE B 719  ? 0.1928 0.2225 0.2160 0.0169  0.0075  -0.0182 717  ILE B CB  
14308 C CG1 . ILE B 719  ? 0.1753 0.2067 0.2012 0.0188  0.0085  -0.0190 717  ILE B CG1 
14309 C CG2 . ILE B 719  ? 0.2627 0.2922 0.2820 0.0172  0.0077  -0.0188 717  ILE B CG2 
14310 C CD1 . ILE B 719  ? 0.2665 0.2945 0.2901 0.0204  0.0072  -0.0211 717  ILE B CD1 
14311 N N   . ALA B 720  ? 0.1744 0.2047 0.1970 0.0129  0.0061  -0.0153 718  ALA B N   
14312 C CA  . ALA B 720  ? 0.1665 0.1974 0.1871 0.0115  0.0054  -0.0145 718  ALA B CA  
14313 C C   . ALA B 720  ? 0.1859 0.2200 0.2084 0.0115  0.0065  -0.0127 718  ALA B C   
14314 O O   . ALA B 720  ? 0.1880 0.2239 0.2090 0.0112  0.0066  -0.0120 718  ALA B O   
14315 C CB  . ALA B 720  ? 0.1817 0.2107 0.2016 0.0099  0.0037  -0.0146 718  ALA B CB  
14316 N N   . ALA B 721  ? 0.1650 0.1995 0.1906 0.0118  0.0071  -0.0120 719  ALA B N   
14317 C CA  . ALA B 721  ? 0.1745 0.2110 0.2015 0.0120  0.0079  -0.0104 719  ALA B CA  
14318 C C   . ALA B 721  ? 0.1806 0.2185 0.2072 0.0127  0.0093  -0.0097 719  ALA B C   
14319 O O   . ALA B 721  ? 0.1887 0.2281 0.2143 0.0127  0.0096  -0.0085 719  ALA B O   
14320 C CB  . ALA B 721  ? 0.1918 0.2275 0.2216 0.0121  0.0080  -0.0101 719  ALA B CB  
14321 N N   . ALA B 722  ? 0.1701 0.2080 0.1975 0.0133  0.0102  -0.0104 720  ALA B N   
14322 C CA  . ALA B 722  ? 0.1857 0.2255 0.2127 0.0138  0.0118  -0.0096 720  ALA B CA  
14323 C C   . ALA B 722  ? 0.2039 0.2443 0.2273 0.0139  0.0116  -0.0098 720  ALA B C   
14324 O O   . ALA B 722  ? 0.1838 0.2256 0.2060 0.0139  0.0123  -0.0084 720  ALA B O   
14325 C CB  . ALA B 722  ? 0.1642 0.2047 0.1929 0.0145  0.0129  -0.0105 720  ALA B CB  
14326 N N   . LEU B 723  ? 0.1762 0.2151 0.1974 0.0138  0.0105  -0.0115 721  LEU B N   
14327 C CA  . LEU B 723  ? 0.1739 0.2130 0.1913 0.0137  0.0101  -0.0119 721  LEU B CA  
14328 C C   . LEU B 723  ? 0.1811 0.2214 0.1977 0.0128  0.0092  -0.0106 721  LEU B C   
14329 O O   . LEU B 723  ? 0.2017 0.2436 0.2163 0.0130  0.0096  -0.0098 721  LEU B O   
14330 C CB  . LEU B 723  ? 0.1792 0.2155 0.1942 0.0136  0.0086  -0.0140 721  LEU B CB  
14331 C CG  . LEU B 723  ? 0.1750 0.2100 0.1895 0.0151  0.0092  -0.0157 721  LEU B CG  
14332 C CD1 . LEU B 723  ? 0.1907 0.2218 0.2028 0.0148  0.0073  -0.0175 721  LEU B CD1 
14333 C CD2 . LEU B 723  ? 0.2163 0.2530 0.2285 0.0162  0.0106  -0.0159 721  LEU B CD2 
14334 N N   . VAL B 724  ? 0.1804 0.2204 0.1984 0.0120  0.0081  -0.0103 722  VAL B N   
14335 C CA  . VAL B 724  ? 0.1730 0.2149 0.1902 0.0113  0.0072  -0.0092 722  VAL B CA  
14336 C C   . VAL B 724  ? 0.1836 0.2274 0.2021 0.0122  0.0082  -0.0073 722  VAL B C   
14337 O O   . VAL B 724  ? 0.2019 0.2477 0.2191 0.0123  0.0077  -0.0063 722  VAL B O   
14338 C CB  . VAL B 724  ? 0.1725 0.2141 0.1908 0.0101  0.0058  -0.0094 722  VAL B CB  
14339 C CG1 . VAL B 724  ? 0.1932 0.2350 0.2147 0.0107  0.0064  -0.0086 722  VAL B CG1 
14340 C CG2 . VAL B 724  ? 0.1893 0.2334 0.2061 0.0090  0.0045  -0.0089 722  VAL B CG2 
14341 N N   . ALA B 725  ? 0.1762 0.2191 0.1968 0.0129  0.0094  -0.0068 723  ALA B N   
14342 C CA  . ALA B 725  ? 0.1834 0.2271 0.2045 0.0136  0.0103  -0.0050 723  ALA B CA  
14343 C C   . ALA B 725  ? 0.2443 0.2889 0.2631 0.0140  0.0113  -0.0043 723  ALA B C   
14344 O O   . ALA B 725  ? 0.2524 0.2972 0.2709 0.0145  0.0120  -0.0026 723  ALA B O   
14345 C CB  . ALA B 725  ? 0.1834 0.2256 0.2074 0.0138  0.0111  -0.0045 723  ALA B CB  
14346 N N   . GLY B 726  ? 0.1978 0.2425 0.2146 0.0138  0.0114  -0.0057 724  GLY B N   
14347 C CA  . GLY B 726  ? 0.1993 0.2451 0.2132 0.0142  0.0123  -0.0053 724  GLY B CA  
14348 C C   . GLY B 726  ? 0.2180 0.2640 0.2324 0.0146  0.0141  -0.0056 724  GLY B C   
14349 O O   . GLY B 726  ? 0.2514 0.2986 0.2637 0.0150  0.0153  -0.0047 724  GLY B O   
14350 N N   . ASN B 727  ? 0.2068 0.2520 0.2239 0.0147  0.0145  -0.0067 725  ASN B N   
14351 C CA  . ASN B 727  ? 0.2062 0.2524 0.2245 0.0151  0.0162  -0.0069 725  ASN B CA  
14352 C C   . ASN B 727  ? 0.2050 0.2509 0.2220 0.0160  0.0162  -0.0093 725  ASN B C   
14353 O O   . ASN B 727  ? 0.2106 0.2544 0.2279 0.0159  0.0147  -0.0108 725  ASN B O   
14354 C CB  . ASN B 727  ? 0.1845 0.2303 0.2071 0.0146  0.0165  -0.0063 725  ASN B CB  
14355 C CG  . ASN B 727  ? 0.2264 0.2714 0.2499 0.0139  0.0163  -0.0042 725  ASN B CG  
14356 O OD1 . ASN B 727  ? 0.2066 0.2523 0.2297 0.0137  0.0174  -0.0024 725  ASN B OD1 
14357 N ND2 . ASN B 727  ? 0.2100 0.2534 0.2347 0.0138  0.0148  -0.0044 725  ASN B ND2 
14358 N N   . PRO B 728  ? 0.1935 0.2412 0.2089 0.0169  0.0177  -0.0098 726  PRO B N   
14359 C CA  . PRO B 728  ? 0.1886 0.2359 0.2033 0.0183  0.0177  -0.0123 726  PRO B CA  
14360 C C   . PRO B 728  ? 0.2036 0.2515 0.2227 0.0185  0.0181  -0.0127 726  PRO B C   
14361 O O   . PRO B 728  ? 0.2125 0.2621 0.2349 0.0177  0.0191  -0.0109 726  PRO B O   
14362 C CB  . PRO B 728  ? 0.2241 0.2740 0.2361 0.0194  0.0197  -0.0124 726  PRO B CB  
14363 C CG  . PRO B 728  ? 0.2442 0.2967 0.2578 0.0182  0.0212  -0.0095 726  PRO B CG  
14364 C CD  . PRO B 728  ? 0.1934 0.2438 0.2082 0.0168  0.0197  -0.0079 726  PRO B CD  
14365 N N   . VAL B 729  ? 0.1776 0.2236 0.1965 0.0197  0.0171  -0.0149 727  VAL B N   
14366 C CA  . VAL B 729  ? 0.1871 0.2330 0.2099 0.0200  0.0169  -0.0155 727  VAL B CA  
14367 C C   . VAL B 729  ? 0.2107 0.2583 0.2338 0.0223  0.0178  -0.0174 727  VAL B C   
14368 O O   . VAL B 729  ? 0.1958 0.2417 0.2151 0.0238  0.0174  -0.0193 727  VAL B O   
14369 C CB  . VAL B 729  ? 0.1714 0.2131 0.1939 0.0193  0.0144  -0.0163 727  VAL B CB  
14370 C CG1 . VAL B 729  ? 0.1890 0.2301 0.2147 0.0201  0.0139  -0.0173 727  VAL B CG1 
14371 C CG2 . VAL B 729  ? 0.1786 0.2199 0.2021 0.0174  0.0139  -0.0143 727  VAL B CG2 
14372 N N   . LEU B 730  ? 0.1909 0.2416 0.2184 0.0225  0.0189  -0.0168 728  LEU B N   
14373 C CA  . LEU B 730  ? 0.1791 0.2318 0.2082 0.0247  0.0194  -0.0186 728  LEU B CA  
14374 C C   . LEU B 730  ? 0.1803 0.2304 0.2120 0.0247  0.0174  -0.0193 728  LEU B C   
14375 O O   . LEU B 730  ? 0.2022 0.2534 0.2378 0.0231  0.0174  -0.0178 728  LEU B O   
14376 C CB  . LEU B 730  ? 0.1788 0.2380 0.2116 0.0248  0.0220  -0.0174 728  LEU B CB  
14377 C CG  . LEU B 730  ? 0.1937 0.2564 0.2243 0.0247  0.0242  -0.0164 728  LEU B CG  
14378 C CD1 . LEU B 730  ? 0.2095 0.2701 0.2345 0.0269  0.0240  -0.0185 728  LEU B CD1 
14379 C CD2 . LEU B 730  ? 0.1846 0.2465 0.2148 0.0219  0.0244  -0.0137 728  LEU B CD2 
14380 N N   . ALA B 731  ? 0.1763 0.2224 0.2055 0.0263  0.0157  -0.0214 729  ALA B N   
14381 C CA  . ALA B 731  ? 0.1463 0.1889 0.1768 0.0262  0.0136  -0.0220 729  ALA B CA  
14382 C C   . ALA B 731  ? 0.1904 0.2353 0.2236 0.0287  0.0138  -0.0235 729  ALA B C   
14383 O O   . ALA B 731  ? 0.1856 0.2299 0.2164 0.0315  0.0138  -0.0255 729  ALA B O   
14384 C CB  . ALA B 731  ? 0.1911 0.2275 0.2169 0.0259  0.0113  -0.0232 729  ALA B CB  
14385 N N   . LYS B 732  ? 0.1762 0.2238 0.2144 0.0280  0.0138  -0.0225 730  LYS B N   
14386 C CA  . LYS B 732  ? 0.1866 0.2372 0.2281 0.0303  0.0138  -0.0236 730  LYS B CA  
14387 C C   . LYS B 732  ? 0.1888 0.2351 0.2309 0.0301  0.0112  -0.0240 730  LYS B C   
14388 O O   . LYS B 732  ? 0.2175 0.2644 0.2628 0.0280  0.0108  -0.0226 730  LYS B O   
14389 C CB  . LYS B 732  ? 0.1896 0.2474 0.2365 0.0293  0.0159  -0.0220 730  LYS B CB  
14390 C CG  . LYS B 732  ? 0.1947 0.2585 0.2445 0.0322  0.0171  -0.0232 730  LYS B CG  
14391 C CD  . LYS B 732  ? 0.2380 0.3004 0.2893 0.0345  0.0150  -0.0249 730  LYS B CD  
14392 C CE  . LYS B 732  ? 0.1981 0.2608 0.2537 0.0322  0.0137  -0.0235 730  LYS B CE  
14393 N NZ  . LYS B 732  ? 0.2373 0.2990 0.2942 0.0348  0.0117  -0.0251 730  LYS B NZ  
14394 N N   . PRO B 733  ? 0.2054 0.2468 0.2441 0.0321  0.0094  -0.0259 731  PRO B N   
14395 C CA  . PRO B 733  ? 0.2026 0.2394 0.2413 0.0319  0.0069  -0.0262 731  PRO B CA  
14396 C C   . PRO B 733  ? 0.1897 0.2304 0.2330 0.0338  0.0066  -0.0267 731  PRO B C   
14397 O O   . PRO B 733  ? 0.1900 0.2363 0.2358 0.0360  0.0082  -0.0274 731  PRO B O   
14398 C CB  . PRO B 733  ? 0.2075 0.2376 0.2403 0.0336  0.0051  -0.0281 731  PRO B CB  
14399 C CG  . PRO B 733  ? 0.2391 0.2720 0.2707 0.0365  0.0066  -0.0296 731  PRO B CG  
14400 C CD  . PRO B 733  ? 0.2298 0.2688 0.2638 0.0347  0.0094  -0.0280 731  PRO B CD  
14401 N N   . ALA B 734  ? 0.2062 0.2441 0.2504 0.0329  0.0046  -0.0263 732  ALA B N   
14402 C CA  . ALA B 734  ? 0.1886 0.2294 0.2369 0.0348  0.0038  -0.0269 732  ALA B CA  
14403 C C   . ALA B 734  ? 0.2208 0.2614 0.2676 0.0391  0.0033  -0.0291 732  ALA B C   
14404 O O   . ALA B 734  ? 0.2358 0.2705 0.2772 0.0405  0.0023  -0.0305 732  ALA B O   
14405 C CB  . ALA B 734  ? 0.2076 0.2438 0.2555 0.0335  0.0013  -0.0264 732  ALA B CB  
14406 N N   . GLU B 735  ? 0.2042 0.2513 0.2558 0.0413  0.0039  -0.0296 733  GLU B N   
14407 C CA  . GLU B 735  ? 0.1830 0.2308 0.2336 0.0460  0.0036  -0.0319 733  GLU B CA  
14408 C C   . GLU B 735  ? 0.2186 0.2583 0.2652 0.0480  0.0004  -0.0332 733  GLU B C   
14409 O O   . GLU B 735  ? 0.2228 0.2591 0.2655 0.0517  -0.0003 -0.0352 733  GLU B O   
14410 C CB  . GLU B 735  ? 0.2547 0.3122 0.3120 0.0478  0.0049  -0.0319 733  GLU B CB  
14411 C CG  . GLU B 735  ? 0.3415 0.4010 0.4036 0.0461  0.0034  -0.0307 733  GLU B CG  
14412 C CD  . GLU B 735  ? 0.4415 0.5056 0.5077 0.0415  0.0049  -0.0283 733  GLU B CD  
14413 O OE1 . GLU B 735  ? 0.3238 0.3855 0.3875 0.0387  0.0061  -0.0271 733  GLU B OE1 
14414 O OE2 . GLU B 735  ? 0.3879 0.4578 0.4597 0.0408  0.0048  -0.0275 733  GLU B OE2 
14415 N N   . GLU B 736  ? 0.2300 0.2658 0.2767 0.0456  -0.0016 -0.0320 734  GLU B N   
14416 C CA  . GLU B 736  ? 0.2206 0.2486 0.2634 0.0471  -0.0048 -0.0329 734  GLU B CA  
14417 C C   . GLU B 736  ? 0.2502 0.2692 0.2857 0.0462  -0.0059 -0.0334 734  GLU B C   
14418 O O   . GLU B 736  ? 0.2532 0.2652 0.2842 0.0484  -0.0083 -0.0346 734  GLU B O   
14419 C CB  . GLU B 736  ? 0.2288 0.2560 0.2738 0.0446  -0.0064 -0.0314 734  GLU B CB  
14420 C CG  . GLU B 736  ? 0.2539 0.2891 0.3058 0.0455  -0.0062 -0.0311 734  GLU B CG  
14421 C CD  . GLU B 736  ? 0.3004 0.3424 0.3572 0.0421  -0.0039 -0.0294 734  GLU B CD  
14422 O OE1 . GLU B 736  ? 0.2464 0.2883 0.3018 0.0398  -0.0019 -0.0286 734  GLU B OE1 
14423 O OE2 . GLU B 736  ? 0.3653 0.4126 0.4274 0.0417  -0.0041 -0.0288 734  GLU B OE2 
14424 N N   . THR B 737  ? 0.2493 0.2680 0.2833 0.0430  -0.0044 -0.0323 735  THR B N   
14425 C CA  . THR B 737  ? 0.2167 0.2273 0.2444 0.0410  -0.0058 -0.0323 735  THR B CA  
14426 C C   . THR B 737  ? 0.2390 0.2503 0.2642 0.0405  -0.0039 -0.0326 735  THR B C   
14427 O O   . THR B 737  ? 0.2350 0.2450 0.2586 0.0370  -0.0035 -0.0314 735  THR B O   
14428 C CB  . THR B 737  ? 0.2449 0.2534 0.2726 0.0368  -0.0066 -0.0302 735  THR B CB  
14429 O OG1 . THR B 737  ? 0.2273 0.2425 0.2598 0.0345  -0.0043 -0.0287 735  THR B OG1 
14430 C CG2 . THR B 737  ? 0.2417 0.2476 0.2701 0.0373  -0.0089 -0.0300 735  THR B CG2 
14431 N N   . PRO B 738  ? 0.2242 0.2376 0.2487 0.0440  -0.0028 -0.0344 736  PRO B N   
14432 C CA  . PRO B 738  ? 0.2042 0.2184 0.2261 0.0436  -0.0010 -0.0348 736  PRO B CA  
14433 C C   . PRO B 738  ? 0.2539 0.2592 0.2684 0.0428  -0.0030 -0.0357 736  PRO B C   
14434 O O   . PRO B 738  ? 0.2362 0.2416 0.2483 0.0411  -0.0019 -0.0355 736  PRO B O   
14435 C CB  . PRO B 738  ? 0.2189 0.2384 0.2424 0.0481  0.0006  -0.0366 736  PRO B CB  
14436 C CG  . PRO B 738  ? 0.2478 0.2637 0.2706 0.0516  -0.0017 -0.0382 736  PRO B CG  
14437 C CD  . PRO B 738  ? 0.2198 0.2350 0.2456 0.0489  -0.0032 -0.0363 736  PRO B CD  
14438 N N   . LEU B 739  ? 0.2178 0.2154 0.2283 0.0440  -0.0059 -0.0367 737  LEU B N   
14439 C CA  . LEU B 739  ? 0.2141 0.2029 0.2172 0.0435  -0.0079 -0.0379 737  LEU B CA  
14440 C C   . LEU B 739  ? 0.2263 0.2127 0.2276 0.0382  -0.0084 -0.0359 737  LEU B C   
14441 O O   . LEU B 739  ? 0.2396 0.2237 0.2370 0.0367  -0.0083 -0.0362 737  LEU B O   
14442 C CB  . LEU B 739  ? 0.2096 0.1901 0.2086 0.0459  -0.0110 -0.0393 737  LEU B CB  
14443 C CG  . LEU B 739  ? 0.2142 0.1969 0.2145 0.0517  -0.0108 -0.0415 737  LEU B CG  
14444 C CD1 . LEU B 739  ? 0.2512 0.2247 0.2472 0.0538  -0.0144 -0.0425 737  LEU B CD1 
14445 C CD2 . LEU B 739  ? 0.2310 0.2149 0.2286 0.0549  -0.0093 -0.0437 737  LEU B CD2 
14446 N N   . ILE B 740  ? 0.2242 0.2113 0.2283 0.0354  -0.0089 -0.0339 738  ILE B N   
14447 C CA  . ILE B 740  ? 0.2168 0.2026 0.2197 0.0307  -0.0092 -0.0320 738  ILE B CA  
14448 C C   . ILE B 740  ? 0.2161 0.2088 0.2219 0.0292  -0.0065 -0.0311 738  ILE B C   
14449 O O   . ILE B 740  ? 0.2296 0.2213 0.2330 0.0264  -0.0065 -0.0303 738  ILE B O   
14450 C CB  . ILE B 740  ? 0.2722 0.2573 0.2771 0.0284  -0.0103 -0.0303 738  ILE B CB  
14451 C CG1 . ILE B 740  ? 0.2404 0.2240 0.2434 0.0238  -0.0108 -0.0285 738  ILE B CG1 
14452 C CG2 . ILE B 740  ? 0.2585 0.2513 0.2702 0.0291  -0.0084 -0.0293 738  ILE B CG2 
14453 C CD1 . ILE B 740  ? 0.2918 0.2676 0.2880 0.0223  -0.0131 -0.0291 738  ILE B CD1 
14454 N N   . ALA B 741  ? 0.2173 0.2171 0.2281 0.0312  -0.0041 -0.0310 739  ALA B N   
14455 C CA  . ALA B 741  ? 0.2388 0.2447 0.2519 0.0300  -0.0016 -0.0300 739  ALA B CA  
14456 C C   . ALA B 741  ? 0.2047 0.2090 0.2133 0.0309  -0.0012 -0.0314 739  ALA B C   
14457 O O   . ALA B 741  ? 0.2265 0.2317 0.2337 0.0285  -0.0006 -0.0305 739  ALA B O   
14458 C CB  . ALA B 741  ? 0.2294 0.2428 0.2484 0.0317  0.0007  -0.0297 739  ALA B CB  
14459 N N   . ALA B 742  ? 0.2177 0.2195 0.2236 0.0345  -0.0017 -0.0337 740  ALA B N   
14460 C CA  . ALA B 742  ? 0.2179 0.2172 0.2186 0.0356  -0.0016 -0.0354 740  ALA B CA  
14461 C C   . ALA B 742  ? 0.2289 0.2215 0.2242 0.0323  -0.0039 -0.0351 740  ALA B C   
14462 O O   . ALA B 742  ? 0.2343 0.2272 0.2269 0.0310  -0.0034 -0.0352 740  ALA B O   
14463 C CB  . ALA B 742  ? 0.2429 0.2393 0.2409 0.0404  -0.0023 -0.0382 740  ALA B CB  
14464 N N   . GLU B 743  ? 0.2350 0.2220 0.2289 0.0308  -0.0064 -0.0347 741  GLU B N   
14465 C CA  . GLU B 743  ? 0.2198 0.2008 0.2089 0.0272  -0.0086 -0.0342 741  GLU B CA  
14466 C C   . GLU B 743  ? 0.2143 0.2003 0.2060 0.0233  -0.0074 -0.0318 741  GLU B C   
14467 O O   . GLU B 743  ? 0.2336 0.2182 0.2220 0.0210  -0.0081 -0.0317 741  GLU B O   
14468 C CB  . GLU B 743  ? 0.2499 0.2241 0.2369 0.0263  -0.0114 -0.0340 741  GLU B CB  
14469 C CG  . GLU B 743  ? 0.2675 0.2355 0.2495 0.0222  -0.0138 -0.0333 741  GLU B CG  
14470 C CD  . GLU B 743  ? 0.3271 0.2887 0.3022 0.0226  -0.0154 -0.0353 741  GLU B CD  
14471 O OE1 . GLU B 743  ? 0.2849 0.2455 0.2582 0.0267  -0.0150 -0.0376 741  GLU B OE1 
14472 O OE2 . GLU B 743  ? 0.3432 0.3010 0.3146 0.0186  -0.0173 -0.0345 741  GLU B OE2 
14473 N N   . GLY B 744  ? 0.2296 0.2216 0.2273 0.0227  -0.0058 -0.0301 742  GLY B N   
14474 C CA  . GLY B 744  ? 0.2234 0.2204 0.2236 0.0198  -0.0045 -0.0280 742  GLY B CA  
14475 C C   . GLY B 744  ? 0.2100 0.2105 0.2094 0.0202  -0.0028 -0.0282 742  GLY B C   
14476 O O   . GLY B 744  ? 0.2161 0.2176 0.2142 0.0176  -0.0030 -0.0272 742  GLY B O   
14477 N N   . VAL B 745  ? 0.2092 0.2123 0.2095 0.0235  -0.0011 -0.0295 743  VAL B N   
14478 C CA  . VAL B 745  ? 0.2079 0.2144 0.2070 0.0240  0.0006  -0.0297 743  VAL B CA  
14479 C C   . VAL B 745  ? 0.2206 0.2216 0.2130 0.0236  -0.0012 -0.0312 743  VAL B C   
14480 O O   . VAL B 745  ? 0.2291 0.2318 0.2199 0.0219  -0.0009 -0.0306 743  VAL B O   
14481 C CB  . VAL B 745  ? 0.2166 0.2275 0.2182 0.0276  0.0029  -0.0306 743  VAL B CB  
14482 C CG1 . VAL B 745  ? 0.2075 0.2208 0.2063 0.0285  0.0044  -0.0312 743  VAL B CG1 
14483 C CG2 . VAL B 745  ? 0.2452 0.2622 0.2534 0.0270  0.0048  -0.0286 743  VAL B CG2 
14484 N N   . ARG B 746  ? 0.2199 0.2140 0.2082 0.0248  -0.0034 -0.0332 744  ARG B N   
14485 C CA  . ARG B 746  ? 0.2407 0.2286 0.2222 0.0239  -0.0056 -0.0347 744  ARG B CA  
14486 C C   . ARG B 746  ? 0.2133 0.2007 0.1940 0.0192  -0.0070 -0.0328 744  ARG B C   
14487 O O   . ARG B 746  ? 0.2317 0.2185 0.2088 0.0178  -0.0076 -0.0331 744  ARG B O   
14488 C CB  . ARG B 746  ? 0.2397 0.2189 0.2167 0.0255  -0.0082 -0.0367 744  ARG B CB  
14489 C CG  . ARG B 746  ? 0.2585 0.2371 0.2349 0.0306  -0.0074 -0.0391 744  ARG B CG  
14490 C CD  . ARG B 746  ? 0.2629 0.2316 0.2340 0.0320  -0.0106 -0.0410 744  ARG B CD  
14491 N NE  . ARG B 746  ? 0.2932 0.2621 0.2647 0.0374  -0.0098 -0.0431 744  ARG B NE  
14492 C CZ  . ARG B 746  ? 0.2387 0.2089 0.2141 0.0395  -0.0097 -0.0429 744  ARG B CZ  
14493 N NH1 . ARG B 746  ? 0.2783 0.2477 0.2564 0.0367  -0.0108 -0.0409 744  ARG B NH1 
14494 N NH2 . ARG B 746  ? 0.2950 0.2678 0.2716 0.0446  -0.0084 -0.0448 744  ARG B NH2 
14495 N N   . ILE B 747  ? 0.2126 0.2005 0.1964 0.0169  -0.0076 -0.0310 745  ILE B N   
14496 C CA  . ILE B 747  ? 0.2050 0.1930 0.1883 0.0125  -0.0089 -0.0293 745  ILE B CA  
14497 C C   . ILE B 747  ? 0.2249 0.2203 0.2112 0.0114  -0.0069 -0.0276 745  ILE B C   
14498 O O   . ILE B 747  ? 0.2205 0.2164 0.2046 0.0089  -0.0078 -0.0271 745  ILE B O   
14499 C CB  . ILE B 747  ? 0.2262 0.2132 0.2119 0.0107  -0.0098 -0.0278 745  ILE B CB  
14500 C CG1 . ILE B 747  ? 0.2354 0.2136 0.2165 0.0109  -0.0125 -0.0292 745  ILE B CG1 
14501 C CG2 . ILE B 747  ? 0.2316 0.2218 0.2186 0.0065  -0.0102 -0.0256 745  ILE B CG2 
14502 C CD1 . ILE B 747  ? 0.2470 0.2233 0.2297 0.0095  -0.0135 -0.0279 745  ILE B CD1 
14503 N N   . LEU B 748  ? 0.2050 0.2061 0.1963 0.0133  -0.0043 -0.0268 746  LEU B N   
14504 C CA  . LEU B 748  ? 0.2014 0.2089 0.1952 0.0125  -0.0025 -0.0251 746  LEU B CA  
14505 C C   . LEU B 748  ? 0.1964 0.2042 0.1865 0.0134  -0.0022 -0.0262 746  LEU B C   
14506 O O   . LEU B 748  ? 0.2038 0.2142 0.1932 0.0116  -0.0023 -0.0251 746  LEU B O   
14507 C CB  . LEU B 748  ? 0.1846 0.1973 0.1840 0.0142  0.0000  -0.0240 746  LEU B CB  
14508 C CG  . LEU B 748  ? 0.2629 0.2770 0.2663 0.0126  -0.0002 -0.0222 746  LEU B CG  
14509 C CD1 . LEU B 748  ? 0.2592 0.2762 0.2672 0.0146  0.0017  -0.0219 746  LEU B CD1 
14510 C CD2 . LEU B 748  ? 0.2853 0.3032 0.2898 0.0104  0.0000  -0.0203 746  LEU B CD2 
14511 N N   . ARG B 749  ? 0.1981 0.2033 0.1855 0.0163  -0.0019 -0.0284 747  ARG B N   
14512 C CA  . ARG B 749  ? 0.2404 0.2454 0.2234 0.0172  -0.0017 -0.0296 747  ARG B CA  
14513 C C   . ARG B 749  ? 0.2050 0.2049 0.1825 0.0146  -0.0046 -0.0303 747  ARG B C   
14514 O O   . ARG B 749  ? 0.2179 0.2196 0.1932 0.0133  -0.0048 -0.0300 747  ARG B O   
14515 C CB  . ARG B 749  ? 0.2375 0.2407 0.2185 0.0212  -0.0007 -0.0320 747  ARG B CB  
14516 C CG  . ARG B 749  ? 0.2363 0.2460 0.2222 0.0236  0.0025  -0.0312 747  ARG B CG  
14517 C CD  . ARG B 749  ? 0.2532 0.2625 0.2368 0.0276  0.0036  -0.0336 747  ARG B CD  
14518 N NE  . ARG B 749  ? 0.2469 0.2632 0.2351 0.0295  0.0068  -0.0327 747  ARG B NE  
14519 C CZ  . ARG B 749  ? 0.3226 0.3409 0.3096 0.0329  0.0085  -0.0343 747  ARG B CZ  
14520 N NH1 . ARG B 749  ? 0.3419 0.3554 0.3230 0.0352  0.0074  -0.0371 747  ARG B NH1 
14521 N NH2 . ARG B 749  ? 0.3065 0.3317 0.2982 0.0341  0.0114  -0.0332 747  ARG B NH2 
14522 N N   . GLU B 750  ? 0.2131 0.2068 0.1884 0.0134  -0.0070 -0.0311 748  GLU B N   
14523 C CA  . GLU B 750  ? 0.2255 0.2141 0.1956 0.0103  -0.0101 -0.0317 748  GLU B CA  
14524 C C   . GLU B 750  ? 0.2093 0.2028 0.1817 0.0064  -0.0104 -0.0292 748  GLU B C   
14525 O O   . GLU B 750  ? 0.2453 0.2380 0.2142 0.0041  -0.0121 -0.0294 748  GLU B O   
14526 C CB  . GLU B 750  ? 0.2249 0.2060 0.1927 0.0094  -0.0125 -0.0325 748  GLU B CB  
14527 C CG  . GLU B 750  ? 0.2772 0.2522 0.2392 0.0058  -0.0159 -0.0330 748  GLU B CG  
14528 C CD  . GLU B 750  ? 0.2721 0.2385 0.2308 0.0050  -0.0185 -0.0338 748  GLU B CD  
14529 O OE1 . GLU B 750  ? 0.2944 0.2592 0.2547 0.0081  -0.0177 -0.0345 748  GLU B OE1 
14530 O OE2 . GLU B 750  ? 0.3175 0.2790 0.2721 0.0012  -0.0214 -0.0336 748  GLU B OE2 
14531 N N   . ALA B 751  ? 0.2126 0.2114 0.1910 0.0059  -0.0089 -0.0270 749  ALA B N   
14532 C CA  . ALA B 751  ? 0.2141 0.2182 0.1953 0.0030  -0.0089 -0.0247 749  ALA B CA  
14533 C C   . ALA B 751  ? 0.2442 0.2542 0.2264 0.0037  -0.0074 -0.0239 749  ALA B C   
14534 O O   . ALA B 751  ? 0.2441 0.2586 0.2283 0.0016  -0.0076 -0.0220 749  ALA B O   
14535 C CB  . ALA B 751  ? 0.2223 0.2296 0.2092 0.0028  -0.0078 -0.0229 749  ALA B CB  
14536 N N   . GLY B 752  ? 0.2316 0.2418 0.2126 0.0067  -0.0058 -0.0250 750  GLY B N   
14537 C CA  . GLY B 752  ? 0.2105 0.2256 0.1915 0.0073  -0.0045 -0.0242 750  GLY B CA  
14538 C C   . GLY B 752  ? 0.2229 0.2421 0.2073 0.0101  -0.0014 -0.0234 750  GLY B C   
14539 O O   . GLY B 752  ? 0.2399 0.2626 0.2238 0.0109  -0.0002 -0.0227 750  GLY B O   
14540 N N   . ILE B 753  ? 0.2098 0.2288 0.1977 0.0116  -0.0001 -0.0235 751  ILE B N   
14541 C CA  . ILE B 753  ? 0.2200 0.2432 0.2113 0.0139  0.0028  -0.0226 751  ILE B CA  
14542 C C   . ILE B 753  ? 0.2222 0.2445 0.2099 0.0165  0.0038  -0.0245 751  ILE B C   
14543 O O   . ILE B 753  ? 0.2507 0.2689 0.2361 0.0180  0.0032  -0.0267 751  ILE B O   
14544 C CB  . ILE B 753  ? 0.1825 0.2059 0.1784 0.0147  0.0037  -0.0222 751  ILE B CB  
14545 C CG1 . ILE B 753  ? 0.2191 0.2430 0.2180 0.0123  0.0026  -0.0206 751  ILE B CG1 
14546 C CG2 . ILE B 753  ? 0.2050 0.2329 0.2044 0.0164  0.0064  -0.0212 751  ILE B CG2 
14547 C CD1 . ILE B 753  ? 0.2116 0.2404 0.2129 0.0113  0.0034  -0.0183 751  ILE B CD1 
14548 N N   . PRO B 754  ? 0.2121 0.2382 0.1992 0.0173  0.0055  -0.0236 752  PRO B N   
14549 C CA  . PRO B 754  ? 0.2260 0.2519 0.2094 0.0198  0.0068  -0.0254 752  PRO B CA  
14550 C C   . PRO B 754  ? 0.2253 0.2519 0.2113 0.0224  0.0086  -0.0263 752  PRO B C   
14551 O O   . PRO B 754  ? 0.2229 0.2521 0.2142 0.0223  0.0098  -0.0249 752  PRO B O   
14552 C CB  . PRO B 754  ? 0.2691 0.2999 0.2524 0.0197  0.0085  -0.0235 752  PRO B CB  
14553 C CG  . PRO B 754  ? 0.2965 0.3285 0.2815 0.0170  0.0071  -0.0214 752  PRO B CG  
14554 C CD  . PRO B 754  ? 0.2143 0.2447 0.2032 0.0159  0.0061  -0.0211 752  PRO B CD  
14555 N N   . ALA B 755  ? 0.2803 0.3050 0.2624 0.0250  0.0089  -0.0288 753  ALA B N   
14556 C CA  . ALA B 755  ? 0.2956 0.3216 0.2801 0.0279  0.0106  -0.0300 753  ALA B CA  
14557 C C   . ALA B 755  ? 0.2401 0.2731 0.2294 0.0284  0.0138  -0.0278 753  ALA B C   
14558 O O   . ALA B 755  ? 0.2758 0.3112 0.2699 0.0292  0.0149  -0.0274 753  ALA B O   
14559 C CB  . ALA B 755  ? 0.3526 0.3758 0.3315 0.0311  0.0106  -0.0331 753  ALA B CB  
14560 N N   . SER B 756  ? 0.2440 0.2803 0.2320 0.0275  0.0151  -0.0263 754  SER B N   
14561 C CA  . SER B 756  ? 0.2319 0.2742 0.2240 0.0275  0.0179  -0.0239 754  SER B CA  
14562 C C   . SER B 756  ? 0.2538 0.2972 0.2514 0.0251  0.0176  -0.0214 754  SER B C   
14563 O O   . SER B 756  ? 0.2487 0.2962 0.2505 0.0249  0.0196  -0.0196 754  SER B O   
14564 C CB  . SER B 756  ? 0.2742 0.3191 0.2628 0.0272  0.0191  -0.0228 754  SER B CB  
14565 O OG  . SER B 756  ? 0.3342 0.3770 0.3211 0.0249  0.0171  -0.0217 754  SER B OG  
14566 N N   . ALA B 757  ? 0.2105 0.2504 0.2079 0.0232  0.0152  -0.0212 755  ALA B N   
14567 C CA  . ALA B 757  ? 0.2007 0.2413 0.2028 0.0213  0.0148  -0.0191 755  ALA B CA  
14568 C C   . ALA B 757  ? 0.2119 0.2510 0.2176 0.0217  0.0142  -0.0198 755  ALA B C   
14569 O O   . ALA B 757  ? 0.2199 0.2601 0.2298 0.0205  0.0143  -0.0182 755  ALA B O   
14570 C CB  . ALA B 757  ? 0.2254 0.2641 0.2260 0.0192  0.0127  -0.0182 755  ALA B CB  
14571 N N   . LEU B 758  ? 0.2025 0.2389 0.2065 0.0234  0.0135  -0.0223 756  LEU B N   
14572 C CA  . LEU B 758  ? 0.2024 0.2369 0.2094 0.0238  0.0126  -0.0231 756  LEU B CA  
14573 C C   . LEU B 758  ? 0.2196 0.2539 0.2256 0.0270  0.0132  -0.0254 756  LEU B C   
14574 O O   . LEU B 758  ? 0.2367 0.2668 0.2379 0.0282  0.0118  -0.0277 756  LEU B O   
14575 C CB  . LEU B 758  ? 0.1895 0.2190 0.1949 0.0221  0.0098  -0.0235 756  LEU B CB  
14576 C CG  . LEU B 758  ? 0.2031 0.2300 0.2107 0.0226  0.0086  -0.0243 756  LEU B CG  
14577 C CD1 . LEU B 758  ? 0.2223 0.2530 0.2358 0.0222  0.0099  -0.0226 756  LEU B CD1 
14578 C CD2 . LEU B 758  ? 0.2282 0.2501 0.2335 0.0205  0.0059  -0.0244 756  LEU B CD2 
14579 N N   . GLN B 759  ? 0.1927 0.2316 0.2030 0.0282  0.0151  -0.0250 757  GLN B N   
14580 C CA  . GLN B 759  ? 0.1905 0.2306 0.2008 0.0315  0.0160  -0.0271 757  GLN B CA  
14581 C C   . GLN B 759  ? 0.2236 0.2634 0.2383 0.0320  0.0151  -0.0272 757  GLN B C   
14582 O O   . GLN B 759  ? 0.2254 0.2670 0.2444 0.0299  0.0153  -0.0253 757  GLN B O   
14583 C CB  . GLN B 759  ? 0.1958 0.2427 0.2077 0.0326  0.0191  -0.0263 757  GLN B CB  
14584 C CG  . GLN B 759  ? 0.2051 0.2521 0.2119 0.0325  0.0199  -0.0263 757  GLN B CG  
14585 C CD  . GLN B 759  ? 0.1844 0.2383 0.1928 0.0329  0.0231  -0.0250 757  GLN B CD  
14586 O OE1 . GLN B 759  ? 0.2433 0.3000 0.2501 0.0357  0.0247  -0.0265 757  GLN B OE1 
14587 N NE2 . GLN B 759  ? 0.1891 0.2457 0.2003 0.0302  0.0240  -0.0220 757  GLN B NE2 
14588 N N   . LEU B 760  ? 0.1961 0.2331 0.2092 0.0348  0.0140  -0.0297 758  LEU B N   
14589 C CA  . LEU B 760  ? 0.1819 0.2182 0.1985 0.0357  0.0130  -0.0301 758  LEU B CA  
14590 C C   . LEU B 760  ? 0.2003 0.2427 0.2203 0.0389  0.0150  -0.0310 758  LEU B C   
14591 O O   . LEU B 760  ? 0.2125 0.2555 0.2295 0.0420  0.0157  -0.0330 758  LEU B O   
14592 C CB  . LEU B 760  ? 0.2081 0.2364 0.2204 0.0368  0.0100  -0.0321 758  LEU B CB  
14593 C CG  . LEU B 760  ? 0.2296 0.2565 0.2448 0.0379  0.0085  -0.0326 758  LEU B CG  
14594 C CD1 . LEU B 760  ? 0.2183 0.2438 0.2361 0.0343  0.0073  -0.0305 758  LEU B CD1 
14595 C CD2 . LEU B 760  ? 0.2605 0.2801 0.2706 0.0405  0.0061  -0.0352 758  LEU B CD2 
14596 N N   . LEU B 761  ? 0.1979 0.2449 0.2240 0.0382  0.0157  -0.0296 759  LEU B N   
14597 C CA  . LEU B 761  ? 0.1988 0.2529 0.2291 0.0407  0.0176  -0.0300 759  LEU B CA  
14598 C C   . LEU B 761  ? 0.2142 0.2678 0.2482 0.0418  0.0159  -0.0306 759  LEU B C   
14599 O O   . LEU B 761  ? 0.2222 0.2789 0.2612 0.0397  0.0160  -0.0288 759  LEU B O   
14600 C CB  . LEU B 761  ? 0.2059 0.2676 0.2405 0.0385  0.0204  -0.0275 759  LEU B CB  
14601 C CG  . LEU B 761  ? 0.2120 0.2754 0.2436 0.0373  0.0223  -0.0264 759  LEU B CG  
14602 C CD1 . LEU B 761  ? 0.2386 0.3012 0.2649 0.0406  0.0229  -0.0289 759  LEU B CD1 
14603 C CD2 . LEU B 761  ? 0.2437 0.3020 0.2730 0.0338  0.0210  -0.0248 759  LEU B CD2 
14604 N N   . PRO B 762  ? 0.1952 0.2443 0.2263 0.0451  0.0141  -0.0331 760  PRO B N   
14605 C CA  . PRO B 762  ? 0.2125 0.2611 0.2468 0.0465  0.0123  -0.0336 760  PRO B CA  
14606 C C   . PRO B 762  ? 0.2165 0.2745 0.2570 0.0482  0.0143  -0.0333 760  PRO B C   
14607 O O   . PRO B 762  ? 0.2184 0.2826 0.2597 0.0498  0.0168  -0.0337 760  PRO B O   
14608 C CB  . PRO B 762  ? 0.2123 0.2538 0.2410 0.0502  0.0101  -0.0364 760  PRO B CB  
14609 C CG  . PRO B 762  ? 0.2247 0.2613 0.2470 0.0492  0.0101  -0.0370 760  PRO B CG  
14610 C CD  . PRO B 762  ? 0.2026 0.2464 0.2270 0.0477  0.0133  -0.0355 760  PRO B CD  
14611 N N   . GLY B 763  ? 0.1966 0.2560 0.2417 0.0476  0.0130  -0.0326 761  GLY B N   
14612 C CA  . GLY B 763  ? 0.2303 0.2986 0.2817 0.0493  0.0143  -0.0326 761  GLY B CA  
14613 C C   . GLY B 763  ? 0.2076 0.2779 0.2644 0.0461  0.0134  -0.0306 761  GLY B C   
14614 O O   . GLY B 763  ? 0.2403 0.3045 0.2955 0.0433  0.0116  -0.0296 761  GLY B O   
14615 N N   . ASP B 764  ? 0.2794 0.3586 0.3424 0.0466  0.0147  -0.0300 762  ASP B N   
14616 C CA  . ASP B 764  ? 0.2696 0.3508 0.3377 0.0439  0.0135  -0.0284 762  ASP B CA  
14617 C C   . ASP B 764  ? 0.3361 0.4209 0.4069 0.0392  0.0153  -0.0257 762  ASP B C   
14618 O O   . ASP B 764  ? 0.2435 0.3271 0.3112 0.0378  0.0170  -0.0249 762  ASP B O   
14619 C CB  . ASP B 764  ? 0.2830 0.3714 0.3565 0.0470  0.0132  -0.0294 762  ASP B CB  
14620 C CG  . ASP B 764  ? 0.3430 0.4424 0.4206 0.0480  0.0164  -0.0291 762  ASP B CG  
14621 O OD1 . ASP B 764  ? 0.3030 0.4051 0.3805 0.0453  0.0188  -0.0275 762  ASP B OD1 
14622 O OD2 . ASP B 764  ? 0.5091 0.6148 0.5902 0.0517  0.0164  -0.0305 762  ASP B OD2 
14623 N N   . GLY B 765  ? 0.3013 0.3901 0.3774 0.0368  0.0149  -0.0242 763  GLY B N   
14624 C CA  . GLY B 765  ? 0.2553 0.3458 0.3333 0.0322  0.0162  -0.0216 763  GLY B CA  
14625 C C   . GLY B 765  ? 0.2306 0.3287 0.3103 0.0315  0.0195  -0.0205 763  GLY B C   
14626 O O   . GLY B 765  ? 0.2795 0.3771 0.3586 0.0280  0.0207  -0.0184 763  GLY B O   
14627 N N   . ARG B 766  ? 0.2650 0.3700 0.3465 0.0349  0.0210  -0.0218 764  ARG B N   
14628 C CA  . ARG B 766  ? 0.2537 0.3663 0.3363 0.0345  0.0244  -0.0208 764  ARG B CA  
14629 C C   . ARG B 766  ? 0.2516 0.3589 0.3277 0.0344  0.0255  -0.0208 764  ARG B C   
14630 O O   . ARG B 766  ? 0.2494 0.3599 0.3253 0.0320  0.0279  -0.0189 764  ARG B O   
14631 C CB  . ARG B 766  ? 0.3289 0.4500 0.4143 0.0388  0.0257  -0.0226 764  ARG B CB  
14632 C CG  . ARG B 766  ? 0.3567 0.4861 0.4497 0.0384  0.0252  -0.0221 764  ARG B CG  
14633 C CD  . ARG B 766  ? 0.4244 0.5606 0.5194 0.0440  0.0258  -0.0245 764  ARG B CD  
14634 N NE  . ARG B 766  ? 0.5054 0.6330 0.5944 0.0485  0.0240  -0.0273 764  ARG B NE  
14635 C CZ  . ARG B 766  ? 0.6194 0.7495 0.7081 0.0542  0.0238  -0.0300 764  ARG B CZ  
14636 N NH1 . ARG B 766  ? 0.6142 0.7559 0.7085 0.0565  0.0255  -0.0303 764  ARG B NH1 
14637 N NH2 . ARG B 766  ? 0.6389 0.7596 0.7214 0.0577  0.0219  -0.0324 764  ARG B NH2 
14638 N N   . VAL B 767  ? 0.2514 0.3508 0.3221 0.0369  0.0238  -0.0229 765  VAL B N   
14639 C CA  . VAL B 767  ? 0.2412 0.3351 0.3056 0.0366  0.0245  -0.0229 765  VAL B CA  
14640 C C   . VAL B 767  ? 0.2223 0.3118 0.2859 0.0320  0.0239  -0.0205 765  VAL B C   
14641 O O   . VAL B 767  ? 0.2403 0.3301 0.3017 0.0302  0.0256  -0.0190 765  VAL B O   
14642 C CB  . VAL B 767  ? 0.2018 0.2880 0.2607 0.0400  0.0224  -0.0257 765  VAL B CB  
14643 C CG1 . VAL B 767  ? 0.2175 0.2984 0.2701 0.0392  0.0228  -0.0256 765  VAL B CG1 
14644 C CG2 . VAL B 767  ? 0.2324 0.3225 0.2916 0.0450  0.0229  -0.0282 765  VAL B CG2 
14645 N N   . GLY B 768  ? 0.2072 0.2926 0.2724 0.0303  0.0215  -0.0201 766  GLY B N   
14646 C CA  . GLY B 768  ? 0.2027 0.2842 0.2674 0.0264  0.0210  -0.0179 766  GLY B CA  
14647 C C   . GLY B 768  ? 0.1912 0.2786 0.2592 0.0233  0.0231  -0.0153 766  GLY B C   
14648 O O   . GLY B 768  ? 0.2162 0.3015 0.2818 0.0210  0.0240  -0.0136 766  GLY B O   
14649 N N   . ALA B 769  ? 0.2237 0.3184 0.2971 0.0232  0.0239  -0.0150 767  ALA B N   
14650 C CA  . ALA B 769  ? 0.2208 0.3212 0.2976 0.0198  0.0258  -0.0123 767  ALA B CA  
14651 C C   . ALA B 769  ? 0.2666 0.3702 0.3407 0.0199  0.0287  -0.0115 767  ALA B C   
14652 O O   . ALA B 769  ? 0.2489 0.3522 0.3223 0.0167  0.0298  -0.0090 767  ALA B O   
14653 C CB  . ALA B 769  ? 0.2327 0.3414 0.3161 0.0197  0.0260  -0.0123 767  ALA B CB  
14654 N N   . ALA B 770  ? 0.2130 0.3192 0.2852 0.0238  0.0299  -0.0136 768  ALA B N   
14655 C CA  . ALA B 770  ? 0.1967 0.3058 0.2658 0.0242  0.0326  -0.0130 768  ALA B CA  
14656 C C   . ALA B 770  ? 0.2317 0.3330 0.2949 0.0228  0.0321  -0.0122 768  ALA B C   
14657 O O   . ALA B 770  ? 0.2353 0.3381 0.2967 0.0210  0.0339  -0.0102 768  ALA B O   
14658 C CB  . ALA B 770  ? 0.2398 0.3521 0.3072 0.0291  0.0336  -0.0159 768  ALA B CB  
14659 N N   . LEU B 771  ? 0.2027 0.2961 0.2630 0.0236  0.0295  -0.0136 769  LEU B N   
14660 C CA  . LEU B 771  ? 0.1980 0.2848 0.2533 0.0223  0.0288  -0.0128 769  LEU B CA  
14661 C C   . LEU B 771  ? 0.2248 0.3103 0.2815 0.0182  0.0287  -0.0098 769  LEU B C   
14662 O O   . LEU B 771  ? 0.2132 0.2974 0.2669 0.0167  0.0297  -0.0081 769  LEU B O   
14663 C CB  . LEU B 771  ? 0.1890 0.2683 0.2413 0.0237  0.0261  -0.0148 769  LEU B CB  
14664 C CG  . LEU B 771  ? 0.1830 0.2613 0.2321 0.0276  0.0258  -0.0177 769  LEU B CG  
14665 C CD1 . LEU B 771  ? 0.2212 0.2921 0.2679 0.0284  0.0229  -0.0193 769  LEU B CD1 
14666 C CD2 . LEU B 771  ? 0.2125 0.2906 0.2565 0.0283  0.0273  -0.0178 769  LEU B CD2 
14667 N N   . VAL B 772  ? 0.1806 0.2657 0.2414 0.0166  0.0273  -0.0092 770  VAL B N   
14668 C CA  . VAL B 772  ? 0.2006 0.2835 0.2625 0.0129  0.0268  -0.0067 770  VAL B CA  
14669 C C   . VAL B 772  ? 0.2391 0.3271 0.3021 0.0105  0.0293  -0.0041 770  VAL B C   
14670 O O   . VAL B 772  ? 0.2516 0.3365 0.3125 0.0081  0.0294  -0.0018 770  VAL B O   
14671 C CB  . VAL B 772  ? 0.2143 0.2966 0.2805 0.0119  0.0249  -0.0069 770  VAL B CB  
14672 C CG1 . VAL B 772  ? 0.2170 0.2982 0.2849 0.0080  0.0246  -0.0042 770  VAL B CG1 
14673 C CG2 . VAL B 772  ? 0.2198 0.2956 0.2839 0.0135  0.0223  -0.0088 770  VAL B CG2 
14674 N N   . ALA B 773  ? 0.2205 0.3164 0.2866 0.0113  0.0312  -0.0043 771  ALA B N   
14675 C CA  . ALA B 773  ? 0.2273 0.3292 0.2951 0.0087  0.0337  -0.0017 771  ALA B CA  
14676 C C   . ALA B 773  ? 0.3017 0.4043 0.3646 0.0094  0.0358  -0.0010 771  ALA B C   
14677 O O   . ALA B 773  ? 0.2996 0.4057 0.3626 0.0068  0.0378  0.0016  771  ALA B O   
14678 C CB  . ALA B 773  ? 0.2484 0.3597 0.3218 0.0092  0.0350  -0.0021 771  ALA B CB  
14679 N N   . ALA B 774  ? 0.2418 0.3410 0.3003 0.0126  0.0354  -0.0032 772  ALA B N   
14680 C CA  . ALA B 774  ? 0.2457 0.3457 0.2993 0.0136  0.0373  -0.0029 772  ALA B CA  
14681 C C   . ALA B 774  ? 0.2500 0.3460 0.3005 0.0105  0.0374  0.0001  772  ALA B C   
14682 O O   . ALA B 774  ? 0.2813 0.3710 0.3314 0.0090  0.0352  0.0009  772  ALA B O   
14683 C CB  . ALA B 774  ? 0.2640 0.3599 0.3131 0.0173  0.0363  -0.0059 772  ALA B CB  
14684 N N   . ALA B 775  ? 0.3135 0.4132 0.3616 0.0098  0.0398  0.0018  773  ALA B N   
14685 C CA  . ALA B 775  ? 0.3435 0.4401 0.3890 0.0067  0.0401  0.0051  773  ALA B CA  
14686 C C   . ALA B 775  ? 0.2821 0.3706 0.3227 0.0074  0.0379  0.0048  773  ALA B C   
14687 O O   . ALA B 775  ? 0.3264 0.4101 0.3661 0.0051  0.0368  0.0070  773  ALA B O   
14688 C CB  . ALA B 775  ? 0.3531 0.4555 0.3964 0.0061  0.0432  0.0069  773  ALA B CB  
14689 N N   . GLU B 776  ? 0.2495 0.3362 0.2869 0.0106  0.0373  0.0021  774  GLU B N   
14690 C CA  . GLU B 776  ? 0.2133 0.2934 0.2462 0.0111  0.0354  0.0019  774  GLU B CA  
14691 C C   . GLU B 776  ? 0.2330 0.3078 0.2676 0.0114  0.0326  0.0006  774  GLU B C   
14692 O O   . GLU B 776  ? 0.2439 0.3137 0.2753 0.0117  0.0309  0.0005  774  GLU B O   
14693 C CB  . GLU B 776  ? 0.2557 0.3361 0.2838 0.0139  0.0359  -0.0001 774  GLU B CB  
14694 C CG  . GLU B 776  ? 0.3338 0.4196 0.3595 0.0140  0.0388  0.0010  774  GLU B CG  
14695 C CD  . GLU B 776  ? 0.4263 0.5191 0.4548 0.0157  0.0409  -0.0006 774  GLU B CD  
14696 O OE1 . GLU B 776  ? 0.3160 0.4097 0.3487 0.0168  0.0401  -0.0025 774  GLU B OE1 
14697 O OE2 . GLU B 776  ? 0.4454 0.5434 0.4720 0.0161  0.0435  0.0000  774  GLU B OE2 
14698 N N   . THR B 777  ? 0.2155 0.2914 0.2548 0.0112  0.0320  -0.0003 775  THR B N   
14699 C CA  . THR B 777  ? 0.1978 0.2688 0.2383 0.0113  0.0294  -0.0014 775  THR B CA  
14700 C C   . THR B 777  ? 0.2250 0.2915 0.2650 0.0091  0.0282  0.0009  775  THR B C   
14701 O O   . THR B 777  ? 0.2430 0.3104 0.2849 0.0067  0.0289  0.0032  775  THR B O   
14702 C CB  . THR B 777  ? 0.1997 0.2732 0.2453 0.0115  0.0290  -0.0027 775  THR B CB  
14703 O OG1 . THR B 777  ? 0.2423 0.3192 0.2878 0.0144  0.0297  -0.0052 775  THR B OG1 
14704 C CG2 . THR B 777  ? 0.2120 0.2803 0.2587 0.0114  0.0264  -0.0035 775  THR B CG2 
14705 N N   . ALA B 778  ? 0.1962 0.2577 0.2335 0.0098  0.0264  0.0003  776  ALA B N   
14706 C CA  . ALA B 778  ? 0.2030 0.2601 0.2390 0.0085  0.0252  0.0022  776  ALA B CA  
14707 C C   . ALA B 778  ? 0.2197 0.2730 0.2577 0.0083  0.0231  0.0015  776  ALA B C   
14708 O O   . ALA B 778  ? 0.2320 0.2815 0.2691 0.0075  0.0220  0.0029  776  ALA B O   
14709 C CB  . ALA B 778  ? 0.2322 0.2873 0.2633 0.0096  0.0248  0.0025  776  ALA B CB  
14710 N N   . GLY B 779  ? 0.1923 0.2464 0.2327 0.0093  0.0224  -0.0007 777  GLY B N   
14711 C CA  . GLY B 779  ? 0.2112 0.2620 0.2533 0.0091  0.0205  -0.0015 777  GLY B CA  
14712 C C   . GLY B 779  ? 0.2131 0.2655 0.2575 0.0103  0.0200  -0.0039 777  GLY B C   
14713 O O   . GLY B 779  ? 0.2066 0.2616 0.2503 0.0118  0.0208  -0.0052 777  GLY B O   
14714 N N   . VAL B 780  ? 0.1815 0.2323 0.2285 0.0098  0.0186  -0.0043 778  VAL B N   
14715 C CA  . VAL B 780  ? 0.1795 0.2314 0.2287 0.0110  0.0179  -0.0064 778  VAL B CA  
14716 C C   . VAL B 780  ? 0.2045 0.2521 0.2532 0.0112  0.0157  -0.0073 778  VAL B C   
14717 O O   . VAL B 780  ? 0.1974 0.2424 0.2464 0.0100  0.0149  -0.0063 778  VAL B O   
14718 C CB  . VAL B 780  ? 0.1778 0.2337 0.2315 0.0100  0.0185  -0.0061 778  VAL B CB  
14719 C CG1 . VAL B 780  ? 0.1987 0.2554 0.2544 0.0116  0.0174  -0.0083 778  VAL B CG1 
14720 C CG2 . VAL B 780  ? 0.2014 0.2624 0.2556 0.0098  0.0209  -0.0051 778  VAL B CG2 
14721 N N   . MET B 781  ? 0.1634 0.2100 0.2109 0.0127  0.0148  -0.0092 779  MET B N   
14722 C CA  . MET B 781  ? 0.1939 0.2371 0.2410 0.0128  0.0129  -0.0101 779  MET B CA  
14723 C C   . MET B 781  ? 0.2170 0.2611 0.2665 0.0137  0.0121  -0.0116 779  MET B C   
14724 O O   . MET B 781  ? 0.2081 0.2536 0.2570 0.0153  0.0124  -0.0129 779  MET B O   
14725 C CB  . MET B 781  ? 0.1760 0.2168 0.2194 0.0135  0.0122  -0.0107 779  MET B CB  
14726 C CG  . MET B 781  ? 0.1775 0.2180 0.2186 0.0130  0.0129  -0.0092 779  MET B CG  
14727 S SD  . MET B 781  ? 0.2057 0.2446 0.2428 0.0135  0.0120  -0.0100 779  MET B SD  
14728 C CE  . MET B 781  ? 0.1937 0.2299 0.2310 0.0130  0.0103  -0.0101 779  MET B CE  
14729 N N   . PHE B 782  ? 0.1978 0.2413 0.2498 0.0129  0.0111  -0.0114 780  PHE B N   
14730 C CA  . PHE B 782  ? 0.1851 0.2301 0.2399 0.0137  0.0103  -0.0126 780  PHE B CA  
14731 C C   . PHE B 782  ? 0.2190 0.2602 0.2732 0.0135  0.0082  -0.0132 780  PHE B C   
14732 O O   . PHE B 782  ? 0.2360 0.2750 0.2899 0.0123  0.0077  -0.0124 780  PHE B O   
14733 C CB  . PHE B 782  ? 0.1932 0.2421 0.2522 0.0125  0.0110  -0.0117 780  PHE B CB  
14734 C CG  . PHE B 782  ? 0.1838 0.2345 0.2459 0.0132  0.0099  -0.0128 780  PHE B CG  
14735 C CD1 . PHE B 782  ? 0.2041 0.2582 0.2674 0.0153  0.0103  -0.0141 780  PHE B CD1 
14736 C CD2 . PHE B 782  ? 0.2147 0.2636 0.2784 0.0120  0.0082  -0.0127 780  PHE B CD2 
14737 C CE1 . PHE B 782  ? 0.2463 0.3023 0.3125 0.0163  0.0091  -0.0151 780  PHE B CE1 
14738 C CE2 . PHE B 782  ? 0.2085 0.2593 0.2751 0.0128  0.0069  -0.0137 780  PHE B CE2 
14739 C CZ  . PHE B 782  ? 0.2432 0.2977 0.3113 0.0150  0.0074  -0.0148 780  PHE B CZ  
14740 N N   . THR B 783  ? 0.1826 0.2229 0.2364 0.0150  0.0071  -0.0147 781  THR B N   
14741 C CA  . THR B 783  ? 0.2181 0.2553 0.2715 0.0150  0.0050  -0.0153 781  THR B CA  
14742 C C   . THR B 783  ? 0.2289 0.2681 0.2850 0.0163  0.0042  -0.0164 781  THR B C   
14743 O O   . THR B 783  ? 0.2193 0.2596 0.2749 0.0182  0.0045  -0.0175 781  THR B O   
14744 C CB  . THR B 783  ? 0.1879 0.2211 0.2371 0.0153  0.0041  -0.0158 781  THR B CB  
14745 O OG1 . THR B 783  ? 0.2225 0.2549 0.2698 0.0142  0.0049  -0.0148 781  THR B OG1 
14746 C CG2 . THR B 783  ? 0.2499 0.2801 0.2986 0.0151  0.0022  -0.0162 781  THR B CG2 
14747 N N   . GLY B 784  ? 0.1995 0.2392 0.2582 0.0155  0.0031  -0.0163 782  GLY B N   
14748 C CA  . GLY B 784  ? 0.2161 0.2588 0.2781 0.0168  0.0023  -0.0171 782  GLY B CA  
14749 C C   . GLY B 784  ? 0.2393 0.2832 0.3045 0.0151  0.0013  -0.0165 782  GLY B C   
14750 O O   . GLY B 784  ? 0.2436 0.2844 0.3076 0.0135  0.0007  -0.0158 782  GLY B O   
14751 N N   . SER B 785  ? 0.2519 0.3006 0.3213 0.0156  0.0011  -0.0168 783  SER B N   
14752 C CA  . SER B 785  ? 0.2838 0.3339 0.3565 0.0139  -0.0002 -0.0164 783  SER B CA  
14753 C C   . SER B 785  ? 0.3078 0.3591 0.3819 0.0111  0.0010  -0.0148 783  SER B C   
14754 O O   . SER B 785  ? 0.2516 0.3054 0.3260 0.0106  0.0032  -0.0139 783  SER B O   
14755 C CB  . SER B 785  ? 0.2535 0.3092 0.3307 0.0153  -0.0008 -0.0171 783  SER B CB  
14756 O OG  . SER B 785  ? 0.2707 0.3327 0.3510 0.0155  0.0013  -0.0167 783  SER B OG  
14757 N N   . THR B 786  ? 0.2990 0.3482 0.3738 0.0091  -0.0005 -0.0143 784  THR B N   
14758 C CA  . THR B 786  ? 0.2901 0.3396 0.3661 0.0062  0.0001  -0.0128 784  THR B CA  
14759 C C   . THR B 786  ? 0.2347 0.2913 0.3154 0.0051  0.0015  -0.0120 784  THR B C   
14760 O O   . THR B 786  ? 0.2777 0.3355 0.3587 0.0033  0.0032  -0.0105 784  THR B O   
14761 C CB  . THR B 786  ? 0.2958 0.3416 0.3715 0.0045  -0.0022 -0.0129 784  THR B CB  
14762 O OG1 . THR B 786  ? 0.3558 0.3956 0.4268 0.0055  -0.0031 -0.0136 784  THR B OG1 
14763 C CG2 . THR B 786  ? 0.4270 0.4720 0.5033 0.0014  -0.0018 -0.0113 784  THR B CG2 
14764 N N   . GLU B 787  ? 0.2585 0.3203 0.3431 0.0061  0.0007  -0.0128 785  GLU B N   
14765 C CA  . GLU B 787  ? 0.2630 0.3328 0.3527 0.0051  0.0021  -0.0120 785  GLU B CA  
14766 C C   . GLU B 787  ? 0.2704 0.3432 0.3594 0.0062  0.0050  -0.0115 785  GLU B C   
14767 O O   . GLU B 787  ? 0.2430 0.3199 0.3341 0.0040  0.0067  -0.0099 785  GLU B O   
14768 C CB  . GLU B 787  ? 0.3600 0.4352 0.4538 0.0070  0.0007  -0.0132 785  GLU B CB  
14769 N N   . VAL B 788  ? 0.2442 0.3148 0.3299 0.0093  0.0055  -0.0128 786  VAL B N   
14770 C CA  . VAL B 788  ? 0.2427 0.3158 0.3271 0.0106  0.0081  -0.0125 786  VAL B CA  
14771 C C   . VAL B 788  ? 0.1991 0.2685 0.2803 0.0084  0.0094  -0.0109 786  VAL B C   
14772 O O   . VAL B 788  ? 0.2321 0.3049 0.3137 0.0075  0.0116  -0.0097 786  VAL B O   
14773 C CB  . VAL B 788  ? 0.2556 0.3267 0.3370 0.0144  0.0079  -0.0145 786  VAL B CB  
14774 C CG1 . VAL B 788  ? 0.2367 0.3088 0.3156 0.0154  0.0104  -0.0143 786  VAL B CG1 
14775 C CG2 . VAL B 788  ? 0.2633 0.3387 0.3479 0.0170  0.0069  -0.0160 786  VAL B CG2 
14776 N N   . ALA B 789  ? 0.2078 0.2701 0.2856 0.0077  0.0079  -0.0109 787  ALA B N   
14777 C CA  . ALA B 789  ? 0.1759 0.2344 0.2506 0.0060  0.0088  -0.0094 787  ALA B CA  
14778 C C   . ALA B 789  ? 0.1743 0.2354 0.2516 0.0027  0.0096  -0.0074 787  ALA B C   
14779 O O   . ALA B 789  ? 0.2090 0.2699 0.2846 0.0017  0.0113  -0.0059 787  ALA B O   
14780 C CB  . ALA B 789  ? 0.1838 0.2353 0.2551 0.0058  0.0070  -0.0098 787  ALA B CB  
14781 N N   . ARG B 790  ? 0.1909 0.2540 0.2719 0.0010  0.0082  -0.0072 788  ARG B N   
14782 C CA  . ARG B 790  ? 0.2098 0.2752 0.2933 -0.0026 0.0087  -0.0052 788  ARG B CA  
14783 C C   . ARG B 790  ? 0.2326 0.3055 0.3186 -0.0029 0.0114  -0.0041 788  ARG B C   
14784 O O   . ARG B 790  ? 0.2610 0.3345 0.3467 -0.0056 0.0127  -0.0020 788  ARG B O   
14785 C CB  . ARG B 790  ? 0.2795 0.3467 0.3670 -0.0045 0.0066  -0.0054 788  ARG B CB  
14786 C CG  . ARG B 790  ? 0.3085 0.3684 0.3934 -0.0053 0.0041  -0.0058 788  ARG B CG  
14787 C CD  . ARG B 790  ? 0.3370 0.3989 0.4258 -0.0079 0.0021  -0.0057 788  ARG B CD  
14788 N NE  . ARG B 790  ? 0.4968 0.5518 0.5828 -0.0076 -0.0005 -0.0069 788  ARG B NE  
14789 C CZ  . ARG B 790  ? 0.5832 0.6308 0.6652 -0.0088 -0.0014 -0.0064 788  ARG B CZ  
14790 N NH1 . ARG B 790  ? 0.4790 0.5246 0.5594 -0.0109 -0.0002 -0.0046 788  ARG B NH1 
14791 N NH2 . ARG B 790  ? 0.5570 0.5990 0.6362 -0.0078 -0.0035 -0.0078 788  ARG B NH2 
14792 N N   . LEU B 791  ? 0.2405 0.3192 0.3288 -0.0002 0.0122  -0.0055 789  LEU B N   
14793 C CA  . LEU B 791  ? 0.2293 0.3157 0.3198 0.0000  0.0149  -0.0047 789  LEU B CA  
14794 C C   . LEU B 791  ? 0.2510 0.3349 0.3368 0.0007  0.0169  -0.0040 789  LEU B C   
14795 O O   . LEU B 791  ? 0.2403 0.3279 0.3266 -0.0011 0.0190  -0.0022 789  LEU B O   
14796 C CB  . LEU B 791  ? 0.2739 0.3662 0.3671 0.0036  0.0151  -0.0068 789  LEU B CB  
14797 C CG  . LEU B 791  ? 0.3481 0.4438 0.4461 0.0034  0.0130  -0.0076 789  LEU B CG  
14798 C CD1 . LEU B 791  ? 0.2883 0.3889 0.3880 0.0077  0.0131  -0.0098 789  LEU B CD1 
14799 C CD2 . LEU B 791  ? 0.3128 0.4148 0.4157 -0.0007 0.0135  -0.0055 789  LEU B CD2 
14800 N N   . ILE B 792  ? 0.2380 0.3158 0.3194 0.0031  0.0162  -0.0053 790  ILE B N   
14801 C CA  . ILE B 792  ? 0.1827 0.2577 0.2595 0.0037  0.0177  -0.0047 790  ILE B CA  
14802 C C   . ILE B 792  ? 0.2133 0.2847 0.2884 0.0005  0.0179  -0.0023 790  ILE B C   
14803 O O   . ILE B 792  ? 0.2364 0.3092 0.3099 -0.0004 0.0198  -0.0007 790  ILE B O   
14804 C CB  . ILE B 792  ? 0.1774 0.2466 0.2501 0.0064  0.0165  -0.0066 790  ILE B CB  
14805 C CG1 . ILE B 792  ? 0.1610 0.2334 0.2346 0.0097  0.0164  -0.0089 790  ILE B CG1 
14806 C CG2 . ILE B 792  ? 0.2138 0.2794 0.2817 0.0066  0.0175  -0.0058 790  ILE B CG2 
14807 C CD1 . ILE B 792  ? 0.1960 0.2627 0.2658 0.0120  0.0150  -0.0106 790  ILE B CD1 
14808 N N   . GLN B 793  ? 0.2138 0.2800 0.2887 -0.0011 0.0158  -0.0020 791  GLN B N   
14809 C CA  . GLN B 793  ? 0.2130 0.2747 0.2859 -0.0040 0.0155  0.0001  791  GLN B CA  
14810 C C   . GLN B 793  ? 0.2097 0.2762 0.2852 -0.0072 0.0170  0.0024  791  GLN B C   
14811 O O   . GLN B 793  ? 0.2463 0.3110 0.3192 -0.0087 0.0181  0.0045  791  GLN B O   
14812 C CB  . GLN B 793  ? 0.2525 0.3085 0.3252 -0.0049 0.0128  -0.0004 791  GLN B CB  
14813 C CG  . GLN B 793  ? 0.2680 0.3179 0.3381 -0.0074 0.0120  0.0014  791  GLN B CG  
14814 C CD  . GLN B 793  ? 0.3649 0.4113 0.4362 -0.0091 0.0095  0.0010  791  GLN B CD  
14815 O OE1 . GLN B 793  ? 0.3571 0.4077 0.4325 -0.0099 0.0087  0.0003  791  GLN B OE1 
14816 N NE2 . GLN B 793  ? 0.3529 0.3916 0.4204 -0.0093 0.0081  0.0012  791  GLN B NE2 
14817 N N   . ALA B 794  ? 0.2302 0.3033 0.3109 -0.0082 0.0171  0.0022  792  ALA B N   
14818 C CA  . ALA B 794  ? 0.2792 0.3582 0.3629 -0.0116 0.0186  0.0046  792  ALA B CA  
14819 C C   . ALA B 794  ? 0.3020 0.3858 0.3844 -0.0105 0.0217  0.0054  792  ALA B C   
14820 O O   . ALA B 794  ? 0.2808 0.3653 0.3623 -0.0134 0.0231  0.0080  792  ALA B O   
14821 C CB  . ALA B 794  ? 0.2843 0.3705 0.3742 -0.0125 0.0181  0.0040  792  ALA B CB  
14822 N N   . GLN B 795  ? 0.2338 0.3208 0.3160 -0.0066 0.0227  0.0033  793  GLN B N   
14823 C CA  A GLN B 795  ? 0.2518 0.3430 0.3322 -0.0053 0.0255  0.0038  793  GLN B CA  
14824 C CA  B GLN B 795  ? 0.2521 0.3431 0.3323 -0.0051 0.0255  0.0037  793  GLN B CA  
14825 C C   . GLN B 795  ? 0.2442 0.3290 0.3189 -0.0059 0.0259  0.0053  793  GLN B C   
14826 O O   . GLN B 795  ? 0.2492 0.3366 0.3227 -0.0076 0.0280  0.0075  793  GLN B O   
14827 C CB  A GLN B 795  ? 0.2991 0.3931 0.3792 -0.0007 0.0260  0.0009  793  GLN B CB  
14828 C CB  B GLN B 795  ? 0.3008 0.3935 0.3802 -0.0004 0.0258  0.0007  793  GLN B CB  
14829 C CG  A GLN B 795  ? 0.2932 0.3914 0.3710 0.0010  0.0289  0.0011  793  GLN B CG  
14830 C CG  B GLN B 795  ? 0.2608 0.3610 0.3451 0.0016  0.0259  -0.0011 793  GLN B CG  
14831 C CD  A GLN B 795  ? 0.2983 0.4056 0.3796 -0.0012 0.0314  0.0030  793  GLN B CD  
14832 C CD  B GLN B 795  ? 0.3343 0.4340 0.4163 0.0064  0.0259  -0.0040 793  GLN B CD  
14833 O OE1 A GLN B 795  ? 0.3412 0.4487 0.4206 -0.0037 0.0330  0.0056  793  GLN B OE1 
14834 O OE1 B GLN B 795  ? 0.3603 0.4544 0.4409 0.0082  0.0237  -0.0058 793  GLN B OE1 
14835 N NE2 A GLN B 795  ? 0.2651 0.3801 0.3516 -0.0002 0.0318  0.0020  793  GLN B NE2 
14836 N NE2 B GLN B 795  ? 0.2308 0.3360 0.3122 0.0085  0.0284  -0.0045 793  GLN B NE2 
14837 N N   . LEU B 796  ? 0.2063 0.2831 0.2775 -0.0047 0.0240  0.0044  794  LEU B N   
14838 C CA  . LEU B 796  ? 0.1969 0.2680 0.2628 -0.0047 0.0242  0.0056  794  LEU B CA  
14839 C C   . LEU B 796  ? 0.2648 0.3329 0.3298 -0.0085 0.0241  0.0087  794  LEU B C   
14840 O O   . LEU B 796  ? 0.2937 0.3601 0.3550 -0.0090 0.0252  0.0105  794  LEU B O   
14841 C CB  . LEU B 796  ? 0.1998 0.2639 0.2628 -0.0025 0.0221  0.0039  794  LEU B CB  
14842 C CG  . LEU B 796  ? 0.2396 0.3050 0.3019 0.0012  0.0220  0.0011  794  LEU B CG  
14843 C CD1 . LEU B 796  ? 0.2177 0.2763 0.2771 0.0026  0.0199  -0.0001 794  LEU B CD1 
14844 C CD2 . LEU B 796  ? 0.2143 0.2825 0.2738 0.0026  0.0242  0.0013  794  LEU B CD2 
14845 N N   . ALA B 797  ? 0.2691 0.3361 0.3370 -0.0112 0.0226  0.0093  795  ALA B N   
14846 C CA  . ALA B 797  ? 0.3116 0.3743 0.3781 -0.0150 0.0220  0.0122  795  ALA B CA  
14847 C C   . ALA B 797  ? 0.3398 0.4082 0.4073 -0.0179 0.0244  0.0149  795  ALA B C   
14848 O O   . ALA B 797  ? 0.3727 0.4372 0.4379 -0.0210 0.0243  0.0176  795  ALA B O   
14849 C CB  . ALA B 797  ? 0.2980 0.3580 0.3672 -0.0173 0.0196  0.0119  795  ALA B CB  
14850 N N   . ASP B 798  ? 0.2865 0.3641 0.3572 -0.0169 0.0266  0.0142  796  ASP B N   
14851 C CA  . ASP B 798  ? 0.3329 0.4168 0.4041 -0.0192 0.0293  0.0168  796  ASP B CA  
14852 C C   . ASP B 798  ? 0.3609 0.4420 0.4264 -0.0180 0.0308  0.0179  796  ASP B C   
14853 O O   . ASP B 798  ? 0.3966 0.4803 0.4609 -0.0206 0.0327  0.0208  796  ASP B O   
14854 C CB  . ASP B 798  ? 0.2944 0.3892 0.3704 -0.0178 0.0314  0.0154  796  ASP B CB  
14855 N N   . ARG B 799  ? 0.3461 0.4223 0.4079 -0.0143 0.0299  0.0160  797  ARG B N   
14856 C CA  . ARG B 799  ? 0.3928 0.4675 0.4494 -0.0125 0.0312  0.0165  797  ARG B CA  
14857 C C   . ARG B 799  ? 0.3692 0.4343 0.4211 -0.0122 0.0292  0.0173  797  ARG B C   
14858 O O   . ARG B 799  ? 0.3094 0.3688 0.3617 -0.0124 0.0268  0.0165  797  ARG B O   
14859 C CB  . ARG B 799  ? 0.3739 0.4521 0.4301 -0.0081 0.0320  0.0134  797  ARG B CB  
14860 C CG  . ARG B 799  ? 0.4907 0.5776 0.5518 -0.0071 0.0334  0.0117  797  ARG B CG  
14861 C CD  . ARG B 799  ? 0.4587 0.5488 0.5180 -0.0029 0.0346  0.0091  797  ARG B CD  
14862 N NE  . ARG B 799  ? 0.4943 0.5798 0.5527 0.0002  0.0325  0.0061  797  ARG B NE  
14863 C CZ  . ARG B 799  ? 0.5097 0.5896 0.5635 0.0021  0.0316  0.0053  797  ARG B CZ  
14864 N NH1 . ARG B 799  ? 0.4042 0.4821 0.4535 0.0015  0.0324  0.0071  797  ARG B NH1 
14865 N NH2 . ARG B 799  ? 0.4491 0.5256 0.5025 0.0044  0.0296  0.0028  797  ARG B NH2 
14866 N N   . LEU B 800  ? 0.2987 0.3620 0.3458 -0.0116 0.0302  0.0187  798  LEU B N   
14867 C CA  . LEU B 800  ? 0.3259 0.3812 0.3681 -0.0104 0.0285  0.0192  798  LEU B CA  
14868 C C   . LEU B 800  ? 0.3310 0.3876 0.3698 -0.0071 0.0293  0.0179  798  LEU B C   
14869 O O   . LEU B 800  ? 0.3567 0.4195 0.3957 -0.0064 0.0315  0.0175  798  LEU B O   
14870 C CB  . LEU B 800  ? 0.4235 0.4741 0.4625 -0.0134 0.0283  0.0229  798  LEU B CB  
14871 C CG  . LEU B 800  ? 0.3986 0.4453 0.4395 -0.0170 0.0268  0.0245  798  LEU B CG  
14872 C CD1 . LEU B 800  ? 0.4448 0.4865 0.4813 -0.0198 0.0268  0.0282  798  LEU B CD1 
14873 C CD2 . LEU B 800  ? 0.3214 0.3617 0.3625 -0.0154 0.0240  0.0224  798  LEU B CD2 
14874 N N   . SER B 801  ? 0.3377 0.3886 0.3735 -0.0049 0.0275  0.0170  799  SER B N   
14875 C CA  . SER B 801  ? 0.4367 0.4881 0.4688 -0.0021 0.0279  0.0161  799  SER B CA  
14876 C C   . SER B 801  ? 0.5168 0.5690 0.5450 -0.0032 0.0295  0.0189  799  SER B C   
14877 O O   . SER B 801  ? 0.4193 0.4704 0.4473 -0.0062 0.0300  0.0217  799  SER B O   
14878 C CB  . SER B 801  ? 0.4063 0.4518 0.4361 0.0000  0.0255  0.0151  799  SER B CB  
14879 O OG  . SER B 801  ? 0.4536 0.4935 0.4805 -0.0011 0.0245  0.0176  799  SER B OG  
14880 N N   . PRO B 802  ? 0.6055 0.6595 0.6303 -0.0011 0.0303  0.0182  800  PRO B N   
14881 C CA  . PRO B 802  ? 0.6146 0.6683 0.6348 -0.0020 0.0314  0.0211  800  PRO B CA  
14882 C C   . PRO B 802  ? 0.5583 0.6049 0.5756 -0.0030 0.0297  0.0237  800  PRO B C   
14883 O O   . PRO B 802  ? 0.5963 0.6419 0.6109 -0.0052 0.0306  0.0269  800  PRO B O   
14884 C CB  . PRO B 802  ? 0.6902 0.7454 0.7070 0.0010  0.0315  0.0192  800  PRO B CB  
14885 C CG  . PRO B 802  ? 0.7019 0.7607 0.7222 0.0028  0.0316  0.0157  800  PRO B CG  
14886 C CD  . PRO B 802  ? 0.5599 0.6162 0.5845 0.0019  0.0301  0.0150  800  PRO B CD  
14887 N N   . ALA B 803  ? 0.5328 0.5742 0.5502 -0.0015 0.0272  0.0225  801  ALA B N   
14888 C CA  . ALA B 803  ? 0.4836 0.5178 0.4983 -0.0018 0.0254  0.0246  801  ALA B CA  
14889 C C   . ALA B 803  ? 0.5511 0.5819 0.5679 -0.0049 0.0248  0.0261  801  ALA B C   
14890 O O   . ALA B 803  ? 0.5838 0.6077 0.5983 -0.0050 0.0230  0.0276  801  ALA B O   
14891 C CB  . ALA B 803  ? 0.4809 0.5118 0.4950 0.0013  0.0231  0.0225  801  ALA B CB  
14892 N N   . GLY B 804  ? 0.4428 0.4782 0.4640 -0.0071 0.0261  0.0257  802  GLY B N   
14893 C CA  . GLY B 804  ? 0.4320 0.4646 0.4553 -0.0104 0.0255  0.0273  802  GLY B CA  
14894 C C   . GLY B 804  ? 0.4357 0.4639 0.4613 -0.0097 0.0232  0.0253  802  GLY B C   
14895 O O   . GLY B 804  ? 0.3954 0.4179 0.4206 -0.0118 0.0217  0.0267  802  GLY B O   
14896 N N   . ARG B 805  ? 0.3869 0.4175 0.4147 -0.0069 0.0227  0.0220  803  ARG B N   
14897 C CA  . ARG B 805  ? 0.3377 0.3645 0.3673 -0.0058 0.0206  0.0200  803  ARG B CA  
14898 C C   . ARG B 805  ? 0.2965 0.3287 0.3311 -0.0058 0.0211  0.0175  803  ARG B C   
14899 O O   . ARG B 805  ? 0.3151 0.3538 0.3514 -0.0054 0.0229  0.0167  803  ARG B O   
14900 C CB  . ARG B 805  ? 0.3802 0.4037 0.4069 -0.0022 0.0192  0.0186  803  ARG B CB  
14901 C CG  . ARG B 805  ? 0.4477 0.4654 0.4694 -0.0016 0.0182  0.0210  803  ARG B CG  
14902 C CD  . ARG B 805  ? 0.5358 0.5463 0.5566 -0.0034 0.0166  0.0225  803  ARG B CD  
14903 N NE  . ARG B 805  ? 0.5878 0.5920 0.6034 -0.0025 0.0155  0.0247  803  ARG B NE  
14904 C CZ  . ARG B 805  ? 0.5391 0.5407 0.5517 -0.0048 0.0160  0.0279  803  ARG B CZ  
14905 N NH1 . ARG B 805  ? 0.5295 0.5350 0.5440 -0.0085 0.0177  0.0295  803  ARG B NH1 
14906 N NH2 . ARG B 805  ? 0.5923 0.5877 0.5999 -0.0034 0.0147  0.0298  803  ARG B NH2 
14907 N N   . PRO B 806  ? 0.2878 0.3173 0.3247 -0.0061 0.0194  0.0162  804  PRO B N   
14908 C CA  . PRO B 806  ? 0.2723 0.3068 0.3140 -0.0059 0.0196  0.0138  804  PRO B CA  
14909 C C   . PRO B 806  ? 0.2655 0.3032 0.3070 -0.0027 0.0201  0.0113  804  PRO B C   
14910 O O   . PRO B 806  ? 0.2768 0.3117 0.3153 -0.0004 0.0193  0.0107  804  PRO B O   
14911 C CB  . PRO B 806  ? 0.2821 0.3115 0.3248 -0.0063 0.0173  0.0129  804  PRO B CB  
14912 C CG  . PRO B 806  ? 0.3296 0.3525 0.3692 -0.0083 0.0163  0.0154  804  PRO B CG  
14913 C CD  . PRO B 806  ? 0.2986 0.3204 0.3339 -0.0067 0.0171  0.0168  804  PRO B CD  
14914 N N   . ILE B 807  ? 0.2491 0.2931 0.2940 -0.0025 0.0213  0.0100  805  ILE B N   
14915 C CA  . ILE B 807  ? 0.2367 0.2833 0.2816 0.0003  0.0214  0.0074  805  ILE B CA  
14916 C C   . ILE B 807  ? 0.2436 0.2870 0.2896 0.0015  0.0193  0.0053  805  ILE B C   
14917 O O   . ILE B 807  ? 0.2380 0.2815 0.2872 0.0004  0.0186  0.0048  805  ILE B O   
14918 C CB  . ILE B 807  ? 0.2216 0.2752 0.2695 0.0004  0.0232  0.0065  805  ILE B CB  
14919 C CG1 . ILE B 807  ? 0.3083 0.3657 0.3553 -0.0011 0.0255  0.0086  805  ILE B CG1 
14920 C CG2 . ILE B 807  ? 0.2292 0.2842 0.2764 0.0034  0.0230  0.0037  805  ILE B CG2 
14921 C CD1 . ILE B 807  ? 0.4013 0.4580 0.4437 0.0005  0.0263  0.0091  805  ILE B CD1 
14922 N N   . PRO B 808  ? 0.2343 0.2752 0.2776 0.0037  0.0184  0.0042  806  PRO B N   
14923 C CA  . PRO B 808  ? 0.2291 0.2671 0.2732 0.0047  0.0165  0.0024  806  PRO B CA  
14924 C C   . PRO B 808  ? 0.2544 0.2955 0.3015 0.0053  0.0164  0.0003  806  PRO B C   
14925 O O   . PRO B 808  ? 0.2226 0.2675 0.2700 0.0062  0.0175  -0.0006 806  PRO B O   
14926 C CB  . PRO B 808  ? 0.2356 0.2718 0.2763 0.0068  0.0160  0.0019  806  PRO B CB  
14927 C CG  . PRO B 808  ? 0.3415 0.3776 0.3794 0.0065  0.0170  0.0039  806  PRO B CG  
14928 C CD  . PRO B 808  ? 0.2451 0.2854 0.2846 0.0051  0.0188  0.0047  806  PRO B CD  
14929 N N   . LEU B 809  ? 0.2007 0.2398 0.2497 0.0048  0.0149  -0.0005 807  LEU B N   
14930 C CA  . LEU B 809  ? 0.2058 0.2470 0.2574 0.0056  0.0143  -0.0025 807  LEU B CA  
14931 C C   . LEU B 809  ? 0.1986 0.2358 0.2490 0.0066  0.0125  -0.0037 807  LEU B C   
14932 O O   . LEU B 809  ? 0.2312 0.2649 0.2812 0.0058  0.0114  -0.0032 807  LEU B O   
14933 C CB  . LEU B 809  ? 0.2045 0.2481 0.2602 0.0038  0.0143  -0.0022 807  LEU B CB  
14934 C CG  . LEU B 809  ? 0.2261 0.2712 0.2845 0.0045  0.0131  -0.0041 807  LEU B CG  
14935 C CD1 . LEU B 809  ? 0.2162 0.2648 0.2747 0.0067  0.0140  -0.0056 807  LEU B CD1 
14936 C CD2 . LEU B 809  ? 0.2583 0.3060 0.3208 0.0024  0.0129  -0.0035 807  LEU B CD2 
14937 N N   . ILE B 810  ? 0.1803 0.2181 0.2298 0.0082  0.0121  -0.0054 808  ILE B N   
14938 C CA  . ILE B 810  ? 0.1842 0.2191 0.2330 0.0089  0.0104  -0.0066 808  ILE B CA  
14939 C C   . ILE B 810  ? 0.2405 0.2771 0.2920 0.0091  0.0098  -0.0080 808  ILE B C   
14940 O O   . ILE B 810  ? 0.2253 0.2645 0.2773 0.0101  0.0103  -0.0089 808  ILE B O   
14941 C CB  . ILE B 810  ? 0.1827 0.2169 0.2286 0.0103  0.0102  -0.0073 808  ILE B CB  
14942 C CG1 . ILE B 810  ? 0.2027 0.2361 0.2461 0.0104  0.0108  -0.0059 808  ILE B CG1 
14943 C CG2 . ILE B 810  ? 0.2409 0.2727 0.2862 0.0107  0.0086  -0.0083 808  ILE B CG2 
14944 C CD1 . ILE B 810  ? 0.2609 0.2938 0.3016 0.0115  0.0103  -0.0065 808  ILE B CD1 
14945 N N   . ALA B 811  ? 0.2196 0.2547 0.2728 0.0083  0.0085  -0.0082 809  ALA B N   
14946 C CA  . ALA B 811  ? 0.2075 0.2444 0.2636 0.0084  0.0077  -0.0093 809  ALA B CA  
14947 C C   . ALA B 811  ? 0.2660 0.2995 0.3210 0.0088  0.0058  -0.0103 809  ALA B C   
14948 O O   . ALA B 811  ? 0.2673 0.2981 0.3220 0.0079  0.0049  -0.0099 809  ALA B O   
14949 C CB  . ALA B 811  ? 0.2461 0.2855 0.3057 0.0067  0.0080  -0.0084 809  ALA B CB  
14950 N N   . GLU B 812  ? 0.2305 0.2637 0.2844 0.0101  0.0052  -0.0116 810  GLU B N   
14951 C CA  . GLU B 812  ? 0.2361 0.2664 0.2887 0.0105  0.0035  -0.0125 810  GLU B CA  
14952 C C   . GLU B 812  ? 0.2465 0.2782 0.3015 0.0109  0.0023  -0.0135 810  GLU B C   
14953 O O   . GLU B 812  ? 0.2559 0.2896 0.3116 0.0121  0.0027  -0.0142 810  GLU B O   
14954 C CB  . GLU B 812  ? 0.2847 0.3133 0.3338 0.0113  0.0034  -0.0128 810  GLU B CB  
14955 C CG  . GLU B 812  ? 0.3133 0.3417 0.3606 0.0111  0.0046  -0.0117 810  GLU B CG  
14956 C CD  . GLU B 812  ? 0.3494 0.3754 0.3960 0.0106  0.0041  -0.0111 810  GLU B CD  
14957 O OE1 . GLU B 812  ? 0.3473 0.3714 0.3921 0.0110  0.0033  -0.0116 810  GLU B OE1 
14958 O OE2 . GLU B 812  ? 0.2858 0.3117 0.3334 0.0099  0.0047  -0.0102 810  GLU B OE2 
14959 N N   . THR B 813  ? 0.2411 0.2718 0.2975 0.0101  0.0010  -0.0136 811  THR B N   
14960 C CA  . THR B 813  ? 0.2155 0.2484 0.2751 0.0102  -0.0001 -0.0143 811  THR B CA  
14961 C C   . THR B 813  ? 0.2633 0.2932 0.3214 0.0106  -0.0022 -0.0152 811  THR B C   
14962 O O   . THR B 813  ? 0.2698 0.2966 0.3245 0.0112  -0.0026 -0.0155 811  THR B O   
14963 C CB  . THR B 813  ? 0.2395 0.2751 0.3026 0.0084  0.0003  -0.0133 811  THR B CB  
14964 O OG1 . THR B 813  ? 0.2340 0.2659 0.2954 0.0070  0.0000  -0.0126 811  THR B OG1 
14965 C CG2 . THR B 813  ? 0.2618 0.3012 0.3263 0.0083  0.0026  -0.0125 811  THR B CG2 
14966 N N   . GLY B 814  ? 0.2754 0.3065 0.3363 0.0102  -0.0036 -0.0156 812  GLY B N   
14967 C CA  . GLY B 814  ? 0.2758 0.3047 0.3354 0.0110  -0.0057 -0.0165 812  GLY B CA  
14968 C C   . GLY B 814  ? 0.2750 0.2995 0.3314 0.0103  -0.0068 -0.0165 812  GLY B C   
14969 O O   . GLY B 814  ? 0.2805 0.3033 0.3355 0.0094  -0.0060 -0.0159 812  GLY B O   
14970 N N   . GLY B 815  ? 0.2369 0.2594 0.2919 0.0109  -0.0087 -0.0173 813  GLY B N   
14971 C CA  . GLY B 815  ? 0.2252 0.2441 0.2773 0.0103  -0.0099 -0.0175 813  GLY B CA  
14972 C C   . GLY B 815  ? 0.2219 0.2405 0.2750 0.0103  -0.0123 -0.0182 813  GLY B C   
14973 O O   . GLY B 815  ? 0.2904 0.3115 0.3460 0.0111  -0.0131 -0.0185 813  GLY B O   
14974 N N   . GLN B 816  ? 0.2022 0.2177 0.2530 0.0096  -0.0135 -0.0185 814  GLN B N   
14975 C CA  . GLN B 816  ? 0.2078 0.2222 0.2583 0.0097  -0.0160 -0.0192 814  GLN B CA  
14976 C C   . GLN B 816  ? 0.1760 0.1862 0.2212 0.0100  -0.0165 -0.0195 814  GLN B C   
14977 O O   . GLN B 816  ? 0.2226 0.2303 0.2660 0.0094  -0.0173 -0.0199 814  GLN B O   
14978 C CB  . GLN B 816  ? 0.2284 0.2438 0.2820 0.0081  -0.0173 -0.0194 814  GLN B CB  
14979 C CG  . GLN B 816  ? 0.2316 0.2470 0.2857 0.0082  -0.0201 -0.0202 814  GLN B CG  
14980 C CD  . GLN B 816  ? 0.2629 0.2821 0.3200 0.0096  -0.0207 -0.0203 814  GLN B CD  
14981 O OE1 . GLN B 816  ? 0.2550 0.2729 0.3097 0.0112  -0.0206 -0.0204 814  GLN B OE1 
14982 N NE2 . GLN B 816  ? 0.2455 0.2693 0.3078 0.0089  -0.0213 -0.0202 814  GLN B NE2 
14983 N N   . ASN B 817  ? 0.1838 0.1932 0.2263 0.0110  -0.0159 -0.0193 815  ASN B N   
14984 C CA  . ASN B 817  ? 0.1920 0.1989 0.2299 0.0111  -0.0152 -0.0192 815  ASN B CA  
14985 C C   . ASN B 817  ? 0.1933 0.1975 0.2277 0.0113  -0.0171 -0.0197 815  ASN B C   
14986 O O   . ASN B 817  ? 0.2107 0.2146 0.2451 0.0117  -0.0187 -0.0198 815  ASN B O   
14987 C CB  . ASN B 817  ? 0.1976 0.2050 0.2340 0.0116  -0.0137 -0.0185 815  ASN B CB  
14988 C CG  . ASN B 817  ? 0.2013 0.2114 0.2409 0.0116  -0.0120 -0.0181 815  ASN B CG  
14989 O OD1 . ASN B 817  ? 0.1926 0.2035 0.2335 0.0111  -0.0108 -0.0179 815  ASN B OD1 
14990 N ND2 . ASN B 817  ? 0.1659 0.1770 0.2064 0.0122  -0.0120 -0.0181 815  ASN B ND2 
14991 N N   . ALA B 818  ? 0.2003 0.2024 0.2317 0.0112  -0.0170 -0.0200 816  ALA B N   
14992 C CA  . ALA B 818  ? 0.1916 0.1911 0.2192 0.0114  -0.0188 -0.0206 816  ALA B CA  
14993 C C   . ALA B 818  ? 0.1953 0.1940 0.2183 0.0118  -0.0176 -0.0201 816  ALA B C   
14994 O O   . ALA B 818  ? 0.2087 0.2087 0.2313 0.0119  -0.0155 -0.0196 816  ALA B O   
14995 C CB  . ALA B 818  ? 0.2009 0.1985 0.2280 0.0111  -0.0198 -0.0215 816  ALA B CB  
14996 N N   . MET B 819  ? 0.1959 0.1929 0.2154 0.0119  -0.0190 -0.0203 817  MET B N   
14997 C CA  . MET B 819  ? 0.2065 0.2028 0.2210 0.0121  -0.0181 -0.0199 817  MET B CA  
14998 C C   . MET B 819  ? 0.2074 0.2012 0.2185 0.0125  -0.0197 -0.0209 817  MET B C   
14999 O O   . MET B 819  ? 0.2127 0.2051 0.2239 0.0123  -0.0221 -0.0213 817  MET B O   
15000 C CB  . MET B 819  ? 0.2058 0.2022 0.2184 0.0116  -0.0181 -0.0188 817  MET B CB  
15001 C CG  . MET B 819  ? 0.2183 0.2145 0.2257 0.0114  -0.0173 -0.0182 817  MET B CG  
15002 S SD  . MET B 819  ? 0.2479 0.2430 0.2524 0.0102  -0.0180 -0.0166 817  MET B SD  
15003 C CE  . MET B 819  ? 0.2536 0.2511 0.2613 0.0096  -0.0160 -0.0158 817  MET B CE  
15004 N N   . ILE B 820  ? 0.2077 0.2013 0.2158 0.0131  -0.0185 -0.0214 818  ILE B N   
15005 C CA  . ILE B 820  ? 0.2038 0.1948 0.2077 0.0137  -0.0198 -0.0225 818  ILE B CA  
15006 C C   . ILE B 820  ? 0.2166 0.2083 0.2156 0.0139  -0.0190 -0.0218 818  ILE B C   
15007 O O   . ILE B 820  ? 0.2236 0.2178 0.2218 0.0140  -0.0167 -0.0210 818  ILE B O   
15008 C CB  . ILE B 820  ? 0.2220 0.2119 0.2254 0.0147  -0.0192 -0.0237 818  ILE B CB  
15009 C CG1 . ILE B 820  ? 0.2586 0.2476 0.2667 0.0140  -0.0203 -0.0242 818  ILE B CG1 
15010 C CG2 . ILE B 820  ? 0.2458 0.2328 0.2439 0.0157  -0.0205 -0.0250 818  ILE B CG2 
15011 C CD1 . ILE B 820  ? 0.2751 0.2618 0.2825 0.0147  -0.0200 -0.0253 818  ILE B CD1 
15012 N N   . VAL B 821  ? 0.2186 0.2082 0.2141 0.0137  -0.0210 -0.0220 819  VAL B N   
15013 C CA  . VAL B 821  ? 0.2115 0.2014 0.2018 0.0135  -0.0205 -0.0211 819  VAL B CA  
15014 C C   . VAL B 821  ? 0.2262 0.2139 0.2117 0.0145  -0.0215 -0.0225 819  VAL B C   
15015 O O   . VAL B 821  ? 0.2514 0.2364 0.2369 0.0146  -0.0241 -0.0235 819  VAL B O   
15016 C CB  . VAL B 821  ? 0.2127 0.2016 0.2026 0.0123  -0.0221 -0.0198 819  VAL B CB  
15017 C CG1 . VAL B 821  ? 0.2376 0.2266 0.2217 0.0117  -0.0216 -0.0186 819  VAL B CG1 
15018 C CG2 . VAL B 821  ? 0.2387 0.2292 0.2332 0.0116  -0.0212 -0.0187 819  VAL B CG2 
15019 N N   . ASP B 822  ? 0.2332 0.2225 0.2148 0.0154  -0.0196 -0.0226 820  ASP B N   
15020 C CA  . ASP B 822  ? 0.2521 0.2392 0.2283 0.0166  -0.0205 -0.0240 820  ASP B CA  
15021 C C   . ASP B 822  ? 0.2763 0.2639 0.2473 0.0159  -0.0206 -0.0228 820  ASP B C   
15022 O O   . ASP B 822  ? 0.2728 0.2618 0.2443 0.0143  -0.0202 -0.0208 820  ASP B O   
15023 C CB  . ASP B 822  ? 0.2582 0.2460 0.2330 0.0187  -0.0187 -0.0255 820  ASP B CB  
15024 C CG  . ASP B 822  ? 0.2727 0.2652 0.2455 0.0193  -0.0155 -0.0245 820  ASP B CG  
15025 O OD1 . ASP B 822  ? 0.2585 0.2536 0.2301 0.0179  -0.0147 -0.0227 820  ASP B OD1 
15026 O OD2 . ASP B 822  ? 0.3065 0.3001 0.2789 0.0214  -0.0139 -0.0256 820  ASP B OD2 
15027 N N   . SER B 823  ? 0.2491 0.2350 0.2145 0.0170  -0.0213 -0.0240 821  SER B N   
15028 C CA  . SER B 823  ? 0.2876 0.2736 0.2475 0.0162  -0.0217 -0.0228 821  SER B CA  
15029 C C   . SER B 823  ? 0.3078 0.2985 0.2654 0.0159  -0.0185 -0.0212 821  SER B C   
15030 O O   . SER B 823  ? 0.3215 0.3127 0.2746 0.0147  -0.0185 -0.0197 821  SER B O   
15031 C CB  . SER B 823  ? 0.2822 0.2650 0.2366 0.0176  -0.0235 -0.0246 821  SER B CB  
15032 O OG  . SER B 823  ? 0.3332 0.3169 0.2854 0.0198  -0.0217 -0.0264 821  SER B OG  
15033 N N   . SER B 824  ? 0.2705 0.2649 0.2309 0.0167  -0.0159 -0.0214 822  SER B N   
15034 C CA  . SER B 824  ? 0.2750 0.2749 0.2338 0.0161  -0.0129 -0.0197 822  SER B CA  
15035 C C   . SER B 824  ? 0.2832 0.2849 0.2456 0.0135  -0.0124 -0.0173 822  SER B C   
15036 O O   . SER B 824  ? 0.3112 0.3172 0.2720 0.0120  -0.0104 -0.0155 822  SER B O   
15037 C CB  . SER B 824  ? 0.2954 0.2990 0.2551 0.0186  -0.0103 -0.0210 822  SER B CB  
15038 O OG  . SER B 824  ? 0.2573 0.2615 0.2232 0.0186  -0.0098 -0.0211 822  SER B OG  
15039 N N   . ALA B 825  ? 0.2431 0.2420 0.2101 0.0127  -0.0140 -0.0173 823  ALA B N   
15040 C CA  . ALA B 825  ? 0.2612 0.2613 0.2314 0.0105  -0.0136 -0.0154 823  ALA B CA  
15041 C C   . ALA B 825  ? 0.2879 0.2865 0.2542 0.0082  -0.0147 -0.0133 823  ALA B C   
15042 O O   . ALA B 825  ? 0.3244 0.3196 0.2869 0.0083  -0.0167 -0.0135 823  ALA B O   
15043 C CB  . ALA B 825  ? 0.2509 0.2483 0.2266 0.0107  -0.0152 -0.0160 823  ALA B CB  
15044 N N   . LEU B 826  ? 0.2894 0.2900 0.2565 0.0060  -0.0136 -0.0112 824  LEU B N   
15045 C CA  . LEU B 826  ? 0.2933 0.2916 0.2566 0.0034  -0.0148 -0.0090 824  LEU B CA  
15046 C C   . LEU B 826  ? 0.3035 0.2965 0.2690 0.0031  -0.0177 -0.0090 824  LEU B C   
15047 O O   . LEU B 826  ? 0.3027 0.2958 0.2730 0.0030  -0.0175 -0.0091 824  LEU B O   
15048 C CB  . LEU B 826  ? 0.3591 0.3616 0.3222 0.0008  -0.0127 -0.0068 824  LEU B CB  
15049 C CG  . LEU B 826  ? 0.3607 0.3608 0.3192 -0.0025 -0.0137 -0.0041 824  LEU B CG  
15050 C CD1 . LEU B 826  ? 0.4191 0.4179 0.3714 -0.0024 -0.0144 -0.0037 824  LEU B CD1 
15051 C CD2 . LEU B 826  ? 0.4323 0.4374 0.3910 -0.0052 -0.0114 -0.0021 824  LEU B CD2 
15052 N N   . ALA B 827  ? 0.3000 0.2885 0.2620 0.0032  -0.0203 -0.0088 825  ALA B N   
15053 C CA  . ALA B 827  ? 0.2719 0.2557 0.2362 0.0037  -0.0232 -0.0092 825  ALA B CA  
15054 C C   . ALA B 827  ? 0.2998 0.2822 0.2656 0.0020  -0.0233 -0.0076 825  ALA B C   
15055 O O   . ALA B 827  ? 0.2798 0.2610 0.2502 0.0029  -0.0242 -0.0084 825  ALA B O   
15056 C CB  . ALA B 827  ? 0.3214 0.3009 0.2808 0.0039  -0.0260 -0.0089 825  ALA B CB  
15057 N N   . GLU B 828  ? 0.2912 0.2737 0.2530 -0.0006 -0.0226 -0.0053 826  GLU B N   
15058 C CA  . GLU B 828  ? 0.3144 0.2946 0.2768 -0.0025 -0.0231 -0.0038 826  GLU B CA  
15059 C C   . GLU B 828  ? 0.3175 0.3011 0.2857 -0.0022 -0.0212 -0.0047 826  GLU B C   
15060 O O   . GLU B 828  ? 0.2846 0.2656 0.2554 -0.0020 -0.0223 -0.0048 826  GLU B O   
15061 C CB  . GLU B 828  ? 0.3055 0.2859 0.2625 -0.0059 -0.0223 -0.0011 826  GLU B CB  
15062 C CG  . GLU B 828  ? 0.4142 0.3892 0.3649 -0.0068 -0.0248 0.0004  826  GLU B CG  
15063 C CD  . GLU B 828  ? 0.4433 0.4199 0.3905 -0.0057 -0.0245 -0.0001 826  GLU B CD  
15064 O OE1 . GLU B 828  ? 0.3823 0.3642 0.3317 -0.0042 -0.0223 -0.0018 826  GLU B OE1 
15065 O OE2 . GLU B 828  ? 0.4536 0.4259 0.3954 -0.0063 -0.0266 0.0010  826  GLU B OE2 
15066 N N   . GLN B 829  ? 0.2751 0.2645 0.2452 -0.0018 -0.0185 -0.0053 827  GLN B N   
15067 C CA  . GLN B 829  ? 0.2925 0.2855 0.2680 -0.0013 -0.0167 -0.0061 827  GLN B CA  
15068 C C   . GLN B 829  ? 0.2755 0.2669 0.2558 0.0013  -0.0178 -0.0082 827  GLN B C   
15069 O O   . GLN B 829  ? 0.2642 0.2553 0.2482 0.0015  -0.0178 -0.0085 827  GLN B O   
15070 C CB  . GLN B 829  ? 0.3392 0.3386 0.3153 -0.0009 -0.0138 -0.0064 827  GLN B CB  
15071 C CG  . GLN B 829  ? 0.4759 0.4791 0.4490 -0.0036 -0.0120 -0.0044 827  GLN B CG  
15072 C CD  . GLN B 829  ? 0.5646 0.5749 0.5397 -0.0024 -0.0091 -0.0051 827  GLN B CD  
15073 O OE1 . GLN B 829  ? 0.4514 0.4625 0.4283 0.0005  -0.0086 -0.0071 827  GLN B OE1 
15074 N NE2 . GLN B 829  ? 0.5627 0.5780 0.5375 -0.0047 -0.0073 -0.0034 827  GLN B NE2 
15075 N N   . VAL B 830  ? 0.2550 0.2457 0.2351 0.0032  -0.0187 -0.0096 828  VAL B N   
15076 C CA  . VAL B 830  ? 0.2363 0.2257 0.2209 0.0053  -0.0199 -0.0114 828  VAL B CA  
15077 C C   . VAL B 830  ? 0.2733 0.2589 0.2590 0.0052  -0.0221 -0.0111 828  VAL B C   
15078 O O   . VAL B 830  ? 0.2471 0.2332 0.2375 0.0061  -0.0221 -0.0118 828  VAL B O   
15079 C CB  . VAL B 830  ? 0.2358 0.2242 0.2190 0.0068  -0.0212 -0.0128 828  VAL B CB  
15080 C CG1 . VAL B 830  ? 0.2498 0.2368 0.2375 0.0084  -0.0229 -0.0144 828  VAL B CG1 
15081 C CG2 . VAL B 830  ? 0.2758 0.2676 0.2580 0.0075  -0.0190 -0.0136 828  VAL B CG2 
15082 N N   . VAL B 831  ? 0.2481 0.2298 0.2294 0.0045  -0.0242 -0.0099 829  VAL B N   
15083 C CA  . VAL B 831  ? 0.2262 0.2038 0.2083 0.0051  -0.0266 -0.0098 829  VAL B CA  
15084 C C   . VAL B 831  ? 0.2496 0.2270 0.2335 0.0042  -0.0258 -0.0092 829  VAL B C   
15085 O O   . VAL B 831  ? 0.2603 0.2369 0.2479 0.0056  -0.0265 -0.0101 829  VAL B O   
15086 C CB  . VAL B 831  ? 0.2358 0.2086 0.2120 0.0044  -0.0291 -0.0085 829  VAL B CB  
15087 C CG1 . VAL B 831  ? 0.2858 0.2538 0.2619 0.0050  -0.0315 -0.0081 829  VAL B CG1 
15088 C CG2 . VAL B 831  ? 0.2802 0.2528 0.2556 0.0059  -0.0306 -0.0096 829  VAL B CG2 
15089 N N   . GLY B 832  ? 0.2337 0.2121 0.2150 0.0018  -0.0241 -0.0077 830  GLY B N   
15090 C CA  . GLY B 832  ? 0.2388 0.2169 0.2215 0.0007  -0.0234 -0.0072 830  GLY B CA  
15091 C C   . GLY B 832  ? 0.2758 0.2578 0.2645 0.0022  -0.0217 -0.0088 830  GLY B C   
15092 O O   . GLY B 832  ? 0.2611 0.2419 0.2523 0.0029  -0.0222 -0.0092 830  GLY B O   
15093 N N   . ASP B 833  ? 0.2524 0.2390 0.2432 0.0029  -0.0199 -0.0096 831  ASP B N   
15094 C CA  . ASP B 833  ? 0.2254 0.2155 0.2216 0.0041  -0.0183 -0.0108 831  ASP B CA  
15095 C C   . ASP B 833  ? 0.2334 0.2223 0.2333 0.0064  -0.0198 -0.0123 831  ASP B C   
15096 O O   . ASP B 833  ? 0.2385 0.2291 0.2426 0.0072  -0.0190 -0.0131 831  ASP B O   
15097 C CB  . ASP B 833  ? 0.2102 0.2048 0.2071 0.0043  -0.0161 -0.0112 831  ASP B CB  
15098 C CG  . ASP B 833  ? 0.2720 0.2694 0.2665 0.0023  -0.0143 -0.0097 831  ASP B CG  
15099 O OD1 . ASP B 833  ? 0.2871 0.2832 0.2803 0.0004  -0.0146 -0.0085 831  ASP B OD1 
15100 O OD2 . ASP B 833  ? 0.2664 0.2675 0.2602 0.0025  -0.0127 -0.0098 831  ASP B OD2 
15101 N N   . VAL B 834  ? 0.2208 0.2074 0.2193 0.0072  -0.0218 -0.0127 832  VAL B N   
15102 C CA  . VAL B 834  ? 0.2135 0.1997 0.2159 0.0091  -0.0234 -0.0140 832  VAL B CA  
15103 C C   . VAL B 834  ? 0.2375 0.2211 0.2405 0.0098  -0.0247 -0.0138 832  VAL B C   
15104 O O   . VAL B 834  ? 0.2404 0.2254 0.2478 0.0112  -0.0247 -0.0148 832  VAL B O   
15105 C CB  . VAL B 834  ? 0.2289 0.2136 0.2295 0.0099  -0.0254 -0.0145 832  VAL B CB  
15106 C CG1 . VAL B 834  ? 0.2462 0.2304 0.2505 0.0116  -0.0275 -0.0155 832  VAL B CG1 
15107 C CG2 . VAL B 834  ? 0.2387 0.2258 0.2393 0.0098  -0.0241 -0.0152 832  VAL B CG2 
15108 N N   . ILE B 835  ? 0.2271 0.2066 0.2254 0.0089  -0.0261 -0.0126 833  ILE B N   
15109 C CA  . ILE B 835  ? 0.2529 0.2288 0.2509 0.0098  -0.0277 -0.0126 833  ILE B CA  
15110 C C   . ILE B 835  ? 0.2738 0.2514 0.2746 0.0097  -0.0259 -0.0129 833  ILE B C   
15111 O O   . ILE B 835  ? 0.2986 0.2761 0.3024 0.0116  -0.0265 -0.0139 833  ILE B O   
15112 C CB  . ILE B 835  ? 0.2850 0.2553 0.2766 0.0083  -0.0294 -0.0109 833  ILE B CB  
15113 C CG1 . ILE B 835  ? 0.3603 0.3285 0.3488 0.0088  -0.0316 -0.0106 833  ILE B CG1 
15114 C CG2 . ILE B 835  ? 0.3338 0.2996 0.3244 0.0093  -0.0310 -0.0110 833  ILE B CG2 
15115 C CD1 . ILE B 835  ? 0.4402 0.4043 0.4282 0.0110  -0.0347 -0.0110 833  ILE B CD1 
15116 N N   . THR B 836  ? 0.2540 0.2337 0.2540 0.0076  -0.0237 -0.0122 834  THR B N   
15117 C CA  A THR B 836  ? 0.2502 0.2320 0.2527 0.0074  -0.0220 -0.0125 834  THR B CA  
15118 C CA  B THR B 836  ? 0.2505 0.2321 0.2530 0.0075  -0.0221 -0.0125 834  THR B CA  
15119 C C   . THR B 836  ? 0.2532 0.2394 0.2615 0.0092  -0.0208 -0.0139 834  THR B C   
15120 O O   . THR B 836  ? 0.2810 0.2676 0.2922 0.0106  -0.0207 -0.0147 834  THR B O   
15121 C CB  A THR B 836  ? 0.2699 0.2537 0.2703 0.0048  -0.0201 -0.0113 834  THR B CB  
15122 C CB  B THR B 836  ? 0.2725 0.2560 0.2730 0.0049  -0.0202 -0.0113 834  THR B CB  
15123 O OG1 A THR B 836  ? 0.3148 0.2945 0.3098 0.0027  -0.0213 -0.0097 834  THR B OG1 
15124 O OG1 B THR B 836  ? 0.2488 0.2362 0.2499 0.0045  -0.0187 -0.0112 834  THR B OG1 
15125 C CG2 A THR B 836  ? 0.2405 0.2268 0.2435 0.0045  -0.0184 -0.0116 834  THR B CG2 
15126 C CG2 B THR B 836  ? 0.3077 0.2867 0.3025 0.0026  -0.0215 -0.0097 834  THR B CG2 
15127 N N   . SER B 837  ? 0.2273 0.2166 0.2372 0.0091  -0.0197 -0.0141 835  SER B N   
15128 C CA  . SER B 837  ? 0.2129 0.2062 0.2278 0.0103  -0.0184 -0.0152 835  SER B CA  
15129 C C   . SER B 837  ? 0.1926 0.1859 0.2110 0.0122  -0.0198 -0.0162 835  SER B C   
15130 O O   . SER B 837  ? 0.2146 0.2106 0.2371 0.0130  -0.0188 -0.0169 835  SER B O   
15131 C CB  . SER B 837  ? 0.1972 0.1927 0.2124 0.0099  -0.0174 -0.0153 835  SER B CB  
15132 O OG  . SER B 837  ? 0.2111 0.2076 0.2236 0.0085  -0.0159 -0.0144 835  SER B OG  
15133 N N   . ALA B 838  ? 0.2050 0.1958 0.2219 0.0129  -0.0222 -0.0163 836  ALA B N   
15134 C CA  . ALA B 838  ? 0.2166 0.2085 0.2372 0.0148  -0.0236 -0.0173 836  ALA B CA  
15135 C C   . ALA B 838  ? 0.2074 0.1975 0.2283 0.0165  -0.0246 -0.0176 836  ALA B C   
15136 O O   . ALA B 838  ? 0.2230 0.2159 0.2483 0.0182  -0.0247 -0.0185 836  ALA B O   
15137 C CB  . ALA B 838  ? 0.2166 0.2070 0.2358 0.0152  -0.0259 -0.0175 836  ALA B CB  
15138 N N   . PHE B 839  ? 0.2216 0.2072 0.2378 0.0160  -0.0255 -0.0169 837  PHE B N   
15139 C CA  . PHE B 839  ? 0.2385 0.2210 0.2539 0.0180  -0.0272 -0.0173 837  PHE B CA  
15140 C C   . PHE B 839  ? 0.2590 0.2391 0.2722 0.0175  -0.0263 -0.0171 837  PHE B C   
15141 O O   . PHE B 839  ? 0.2484 0.2262 0.2614 0.0196  -0.0274 -0.0178 837  PHE B O   
15142 C CB  . PHE B 839  ? 0.2449 0.2224 0.2559 0.0184  -0.0301 -0.0167 837  PHE B CB  
15143 C CG  . PHE B 839  ? 0.2398 0.2193 0.2525 0.0190  -0.0314 -0.0170 837  PHE B CG  
15144 C CD1 . PHE B 839  ? 0.2356 0.2195 0.2540 0.0209  -0.0318 -0.0182 837  PHE B CD1 
15145 C CD2 . PHE B 839  ? 0.2708 0.2482 0.2795 0.0174  -0.0322 -0.0160 837  PHE B CD2 
15146 C CE1 . PHE B 839  ? 0.2307 0.2163 0.2505 0.0211  -0.0333 -0.0185 837  PHE B CE1 
15147 C CE2 . PHE B 839  ? 0.2796 0.2585 0.2894 0.0178  -0.0336 -0.0165 837  PHE B CE2 
15148 C CZ  . PHE B 839  ? 0.2888 0.2717 0.3042 0.0196  -0.0342 -0.0177 837  PHE B CZ  
15149 N N   . ASP B 840  ? 0.2263 0.2069 0.2377 0.0150  -0.0245 -0.0162 838  ASP B N   
15150 C CA  . ASP B 840  ? 0.2384 0.2178 0.2486 0.0143  -0.0234 -0.0162 838  ASP B CA  
15151 C C   . ASP B 840  ? 0.2547 0.2373 0.2695 0.0166  -0.0225 -0.0176 838  ASP B C   
15152 O O   . ASP B 840  ? 0.2404 0.2282 0.2600 0.0173  -0.0212 -0.0181 838  ASP B O   
15153 C CB  . ASP B 840  ? 0.2665 0.2483 0.2760 0.0115  -0.0212 -0.0152 838  ASP B CB  
15154 C CG  . ASP B 840  ? 0.2900 0.2711 0.2983 0.0106  -0.0203 -0.0151 838  ASP B CG  
15155 O OD1 . ASP B 840  ? 0.3159 0.2999 0.3277 0.0119  -0.0190 -0.0161 838  ASP B OD1 
15156 O OD2 . ASP B 840  ? 0.3674 0.3451 0.3713 0.0083  -0.0208 -0.0140 838  ASP B OD2 
15157 N N   . SER B 841  ? 0.2551 0.2345 0.2681 0.0178  -0.0231 -0.0182 839  SER B N   
15158 C CA  . SER B 841  ? 0.2904 0.2726 0.3070 0.0203  -0.0222 -0.0196 839  SER B CA  
15159 C C   . SER B 841  ? 0.2447 0.2305 0.2658 0.0230  -0.0229 -0.0205 839  SER B C   
15160 O O   . SER B 841  ? 0.2404 0.2315 0.2664 0.0243  -0.0214 -0.0213 839  SER B O   
15161 C CB  . SER B 841  ? 0.2934 0.2805 0.3128 0.0190  -0.0194 -0.0195 839  SER B CB  
15162 O OG  . SER B 841  ? 0.2854 0.2700 0.3009 0.0164  -0.0189 -0.0186 839  SER B OG  
15163 N N   . ALA B 842  ? 0.2315 0.2144 0.2510 0.0237  -0.0253 -0.0202 840  ALA B N   
15164 C CA  . ALA B 842  ? 0.2257 0.2120 0.2493 0.0259  -0.0264 -0.0210 840  ALA B CA  
15165 C C   . ALA B 842  ? 0.2294 0.2226 0.2585 0.0249  -0.0245 -0.0210 840  ALA B C   
15166 O O   . ALA B 842  ? 0.2218 0.2199 0.2559 0.0266  -0.0243 -0.0218 840  ALA B O   
15167 C CB  . ALA B 842  ? 0.2736 0.2601 0.2987 0.0297  -0.0273 -0.0224 840  ALA B CB  
15168 N N   . GLY B 843  ? 0.2073 0.2008 0.2353 0.0220  -0.0231 -0.0200 841  GLY B N   
15169 C CA  . GLY B 843  ? 0.2175 0.2161 0.2496 0.0208  -0.0215 -0.0200 841  GLY B CA  
15170 C C   . GLY B 843  ? 0.2184 0.2218 0.2547 0.0213  -0.0192 -0.0205 841  GLY B C   
15171 O O   . GLY B 843  ? 0.2182 0.2259 0.2586 0.0207  -0.0182 -0.0205 841  GLY B O   
15172 N N   . GLN B 844  ? 0.1926 0.1949 0.2278 0.0223  -0.0185 -0.0209 842  GLN B N   
15173 C CA  . GLN B 844  ? 0.2207 0.2274 0.2592 0.0228  -0.0162 -0.0213 842  GLN B CA  
15174 C C   . GLN B 844  ? 0.2274 0.2342 0.2645 0.0205  -0.0141 -0.0205 842  GLN B C   
15175 O O   . GLN B 844  ? 0.2756 0.2822 0.3115 0.0207  -0.0130 -0.0207 842  GLN B O   
15176 C CB  . GLN B 844  ? 0.1892 0.1950 0.2272 0.0255  -0.0166 -0.0224 842  GLN B CB  
15177 C CG  . GLN B 844  ? 0.2079 0.2144 0.2479 0.0282  -0.0187 -0.0232 842  GLN B CG  
15178 C CD  . GLN B 844  ? 0.2900 0.2945 0.3285 0.0314  -0.0196 -0.0244 842  GLN B CD  
15179 O OE1 . GLN B 844  ? 0.2110 0.2201 0.2533 0.0340  -0.0193 -0.0254 842  GLN B OE1 
15180 N NE2 . GLN B 844  ? 0.3341 0.3315 0.3667 0.0314  -0.0210 -0.0243 842  GLN B NE2 
15181 N N   . ARG B 845  ? 0.1963 0.2034 0.2331 0.0185  -0.0138 -0.0197 843  ARG B N   
15182 C CA  . ARG B 845  ? 0.1953 0.2035 0.2316 0.0167  -0.0119 -0.0189 843  ARG B CA  
15183 C C   . ARG B 845  ? 0.2089 0.2208 0.2490 0.0161  -0.0109 -0.0187 843  ARG B C   
15184 O O   . ARG B 845  ? 0.2032 0.2152 0.2445 0.0161  -0.0122 -0.0189 843  ARG B O   
15185 C CB  . ARG B 845  ? 0.1854 0.1904 0.2174 0.0150  -0.0124 -0.0181 843  ARG B CB  
15186 C CG  . ARG B 845  ? 0.2124 0.2131 0.2401 0.0148  -0.0134 -0.0180 843  ARG B CG  
15187 C CD  . ARG B 845  ? 0.2612 0.2602 0.2852 0.0126  -0.0134 -0.0168 843  ARG B CD  
15188 N NE  . ARG B 845  ? 0.3256 0.3204 0.3452 0.0117  -0.0144 -0.0164 843  ARG B NE  
15189 C CZ  . ARG B 845  ? 0.2970 0.2917 0.3146 0.0101  -0.0135 -0.0159 843  ARG B CZ  
15190 N NH1 . ARG B 845  ? 0.3136 0.3124 0.3334 0.0095  -0.0115 -0.0157 843  ARG B NH1 
15191 N NH2 . ARG B 845  ? 0.3351 0.3253 0.3484 0.0090  -0.0149 -0.0155 843  ARG B NH2 
15192 N N   . CYS B 846  ? 0.2118 0.2265 0.2537 0.0155  -0.0089 -0.0184 844  CYS B N   
15193 C CA  . CYS B 846  ? 0.2262 0.2433 0.2709 0.0146  -0.0082 -0.0180 844  CYS B CA  
15194 C C   . CYS B 846  ? 0.1802 0.1950 0.2225 0.0136  -0.0089 -0.0177 844  CYS B C   
15195 O O   . CYS B 846  ? 0.2216 0.2369 0.2656 0.0131  -0.0094 -0.0177 844  CYS B O   
15196 C CB  . CYS B 846  ? 0.2460 0.2655 0.2919 0.0141  -0.0060 -0.0175 844  CYS B CB  
15197 S SG  . CYS B 846  ? 0.2985 0.3163 0.3404 0.0135  -0.0049 -0.0169 844  CYS B SG  
15198 N N   . SER B 847  ? 0.1939 0.2063 0.2323 0.0131  -0.0089 -0.0173 845  SER B N   
15199 C CA  . SER B 847  ? 0.1913 0.2019 0.2269 0.0122  -0.0093 -0.0170 845  SER B CA  
15200 C C   . SER B 847  ? 0.1876 0.1958 0.2216 0.0124  -0.0114 -0.0173 845  SER B C   
15201 O O   . SER B 847  ? 0.1827 0.1896 0.2141 0.0119  -0.0118 -0.0171 845  SER B O   
15202 C CB  . SER B 847  ? 0.2060 0.2161 0.2384 0.0115  -0.0084 -0.0163 845  SER B CB  
15203 O OG  . SER B 847  ? 0.2122 0.2204 0.2429 0.0116  -0.0093 -0.0164 845  SER B OG  
15204 N N   . ALA B 848  ? 0.2050 0.2127 0.2401 0.0134  -0.0129 -0.0178 846  ALA B N   
15205 C CA  . ALA B 848  ? 0.1874 0.1922 0.2202 0.0138  -0.0151 -0.0179 846  ALA B CA  
15206 C C   . ALA B 848  ? 0.1988 0.2036 0.2319 0.0134  -0.0161 -0.0182 846  ALA B C   
15207 O O   . ALA B 848  ? 0.1928 0.1997 0.2291 0.0133  -0.0157 -0.0185 846  ALA B O   
15208 C CB  . ALA B 848  ? 0.1884 0.1931 0.2229 0.0154  -0.0166 -0.0186 846  ALA B CB  
15209 N N   . LEU B 849  ? 0.2092 0.2110 0.2384 0.0131  -0.0175 -0.0180 847  LEU B N   
15210 C CA  . LEU B 849  ? 0.1963 0.1975 0.2249 0.0129  -0.0188 -0.0183 847  LEU B CA  
15211 C C   . LEU B 849  ? 0.1897 0.1917 0.2215 0.0138  -0.0208 -0.0191 847  LEU B C   
15212 O O   . LEU B 849  ? 0.2130 0.2139 0.2444 0.0149  -0.0224 -0.0191 847  LEU B O   
15213 C CB  . LEU B 849  ? 0.2195 0.2176 0.2428 0.0124  -0.0197 -0.0178 847  LEU B CB  
15214 C CG  . LEU B 849  ? 0.1916 0.1884 0.2133 0.0124  -0.0214 -0.0183 847  LEU B CG  
15215 C CD1 . LEU B 849  ? 0.2192 0.2174 0.2420 0.0121  -0.0202 -0.0189 847  LEU B CD1 
15216 C CD2 . LEU B 849  ? 0.2132 0.2072 0.2292 0.0118  -0.0220 -0.0175 847  LEU B CD2 
15217 N N   . ARG B 850  ? 0.1803 0.1843 0.2153 0.0135  -0.0208 -0.0196 848  ARG B N   
15218 C CA  . ARG B 850  ? 0.1896 0.1955 0.2283 0.0140  -0.0227 -0.0202 848  ARG B CA  
15219 C C   . ARG B 850  ? 0.2011 0.2053 0.2381 0.0135  -0.0249 -0.0207 848  ARG B C   
15220 O O   . ARG B 850  ? 0.2230 0.2279 0.2616 0.0142  -0.0273 -0.0211 848  ARG B O   
15221 C CB  . ARG B 850  ? 0.2005 0.2104 0.2444 0.0134  -0.0215 -0.0203 848  ARG B CB  
15222 C CG  . ARG B 850  ? 0.1965 0.2083 0.2419 0.0138  -0.0191 -0.0199 848  ARG B CG  
15223 C CD  . ARG B 850  ? 0.2004 0.2122 0.2457 0.0155  -0.0198 -0.0200 848  ARG B CD  
15224 N NE  . ARG B 850  ? 0.2166 0.2304 0.2634 0.0160  -0.0177 -0.0198 848  ARG B NE  
15225 C CZ  . ARG B 850  ? 0.2259 0.2392 0.2721 0.0176  -0.0178 -0.0201 848  ARG B CZ  
15226 N NH1 . ARG B 850  ? 0.2125 0.2230 0.2564 0.0188  -0.0199 -0.0203 848  ARG B NH1 
15227 N NH2 . ARG B 850  ? 0.2081 0.2233 0.2555 0.0180  -0.0159 -0.0200 848  ARG B NH2 
15228 N N   . VAL B 851  ? 0.2113 0.2134 0.2453 0.0126  -0.0244 -0.0207 849  VAL B N   
15229 C CA  . VAL B 851  ? 0.2233 0.2235 0.2552 0.0122  -0.0264 -0.0214 849  VAL B CA  
15230 C C   . VAL B 851  ? 0.2377 0.2347 0.2636 0.0122  -0.0259 -0.0212 849  VAL B C   
15231 O O   . VAL B 851  ? 0.2286 0.2254 0.2530 0.0119  -0.0239 -0.0211 849  VAL B O   
15232 C CB  . VAL B 851  ? 0.2407 0.2418 0.2753 0.0110  -0.0263 -0.0220 849  VAL B CB  
15233 C CG1 . VAL B 851  ? 0.2643 0.2630 0.2966 0.0106  -0.0289 -0.0229 849  VAL B CG1 
15234 C CG2 . VAL B 851  ? 0.2869 0.2921 0.3277 0.0106  -0.0262 -0.0219 849  VAL B CG2 
15235 N N   . LEU B 852  ? 0.2195 0.2144 0.2419 0.0126  -0.0278 -0.0211 850  LEU B N   
15236 C CA  . LEU B 852  ? 0.2388 0.2310 0.2552 0.0124  -0.0275 -0.0208 850  LEU B CA  
15237 C C   . LEU B 852  ? 0.2141 0.2046 0.2284 0.0123  -0.0291 -0.0219 850  LEU B C   
15238 O O   . LEU B 852  ? 0.2238 0.2138 0.2389 0.0124  -0.0318 -0.0224 850  LEU B O   
15239 C CB  . LEU B 852  ? 0.2057 0.1960 0.2188 0.0128  -0.0287 -0.0199 850  LEU B CB  
15240 C CG  . LEU B 852  ? 0.2212 0.2091 0.2278 0.0123  -0.0285 -0.0194 850  LEU B CG  
15241 C CD1 . LEU B 852  ? 0.2271 0.2163 0.2322 0.0117  -0.0255 -0.0188 850  LEU B CD1 
15242 C CD2 . LEU B 852  ? 0.2560 0.2415 0.2596 0.0124  -0.0301 -0.0183 850  LEU B CD2 
15243 N N   . CYS B 853  ? 0.2213 0.2109 0.2328 0.0122  -0.0277 -0.0223 851  CYS B N   
15244 C CA  . CYS B 853  ? 0.2262 0.2136 0.2350 0.0122  -0.0291 -0.0236 851  CYS B CA  
15245 C C   . CYS B 853  ? 0.2243 0.2098 0.2265 0.0127  -0.0289 -0.0235 851  CYS B C   
15246 O O   . CYS B 853  ? 0.2281 0.2143 0.2280 0.0130  -0.0265 -0.0231 851  CYS B O   
15247 C CB  . CYS B 853  ? 0.2319 0.2192 0.2421 0.0121  -0.0277 -0.0244 851  CYS B CB  
15248 S SG  . CYS B 853  ? 0.2641 0.2543 0.2818 0.0113  -0.0272 -0.0241 851  CYS B SG  
15249 N N   . LEU B 854  ? 0.2224 0.2059 0.2217 0.0128  -0.0315 -0.0238 852  LEU B N   
15250 C CA  . LEU B 854  ? 0.2306 0.2124 0.2233 0.0131  -0.0315 -0.0234 852  LEU B CA  
15251 C C   . LEU B 854  ? 0.2423 0.2217 0.2310 0.0135  -0.0328 -0.0250 852  LEU B C   
15252 O O   . LEU B 854  ? 0.2610 0.2390 0.2508 0.0134  -0.0355 -0.0261 852  LEU B O   
15253 C CB  . LEU B 854  ? 0.2279 0.2087 0.2194 0.0129  -0.0336 -0.0224 852  LEU B CB  
15254 C CG  . LEU B 854  ? 0.2220 0.2042 0.2165 0.0126  -0.0328 -0.0209 852  LEU B CG  
15255 C CD1 . LEU B 854  ? 0.2387 0.2188 0.2311 0.0128  -0.0355 -0.0201 852  LEU B CD1 
15256 C CD2 . LEU B 854  ? 0.2399 0.2232 0.2323 0.0121  -0.0298 -0.0198 852  LEU B CD2 
15257 N N   . GLN B 855  ? 0.2456 0.2247 0.2294 0.0142  -0.0309 -0.0253 853  GLN B N   
15258 C CA  . GLN B 855  ? 0.2337 0.2100 0.2124 0.0150  -0.0322 -0.0269 853  GLN B CA  
15259 C C   . GLN B 855  ? 0.2886 0.2629 0.2643 0.0147  -0.0353 -0.0268 853  GLN B C   
15260 O O   . GLN B 855  ? 0.2693 0.2441 0.2435 0.0143  -0.0355 -0.0252 853  GLN B O   
15261 C CB  . GLN B 855  ? 0.2390 0.2162 0.2126 0.0161  -0.0295 -0.0270 853  GLN B CB  
15262 C CG  . GLN B 855  ? 0.2823 0.2565 0.2512 0.0175  -0.0304 -0.0292 853  GLN B CG  
15263 C CD  . GLN B 855  ? 0.3272 0.3028 0.2909 0.0191  -0.0277 -0.0295 853  GLN B CD  
15264 O OE1 . GLN B 855  ? 0.3331 0.3119 0.2984 0.0195  -0.0248 -0.0286 853  GLN B OE1 
15265 N NE2 . GLN B 855  ? 0.3706 0.3438 0.3277 0.0201  -0.0288 -0.0307 853  GLN B NE2 
15266 N N   . GLU B 856  ? 0.2691 0.2407 0.2437 0.0148  -0.0379 -0.0285 854  GLU B N   
15267 C CA  . GLU B 856  ? 0.2945 0.2645 0.2674 0.0145  -0.0415 -0.0286 854  GLU B CA  
15268 C C   . GLU B 856  ? 0.2993 0.2684 0.2655 0.0148  -0.0414 -0.0275 854  GLU B C   
15269 O O   . GLU B 856  ? 0.3158 0.2845 0.2816 0.0144  -0.0433 -0.0263 854  GLU B O   
15270 C CB  . GLU B 856  ? 0.3397 0.3068 0.3112 0.0145  -0.0442 -0.0308 854  GLU B CB  
15271 C CG  . GLU B 856  ? 0.4645 0.4295 0.4324 0.0143  -0.0479 -0.0311 854  GLU B CG  
15272 C CD  . GLU B 856  ? 0.5393 0.5062 0.5126 0.0136  -0.0501 -0.0300 854  GLU B CD  
15273 O OE1 . GLU B 856  ? 0.5222 0.4917 0.5024 0.0131  -0.0493 -0.0295 854  GLU B OE1 
15274 O OE2 . GLU B 856  ? 0.5895 0.5553 0.5598 0.0138  -0.0527 -0.0295 854  GLU B OE2 
15275 N N   . ASP B 857  ? 0.3113 0.2804 0.2723 0.0156  -0.0390 -0.0277 855  ASP B N   
15276 C CA  . ASP B 857  ? 0.3489 0.3174 0.3029 0.0157  -0.0388 -0.0267 855  ASP B CA  
15277 C C   . ASP B 857  ? 0.3416 0.3119 0.2962 0.0147  -0.0376 -0.0240 855  ASP B C   
15278 O O   . ASP B 857  ? 0.3692 0.3382 0.3186 0.0142  -0.0386 -0.0228 855  ASP B O   
15279 C CB  . ASP B 857  ? 0.4018 0.3709 0.3505 0.0170  -0.0362 -0.0277 855  ASP B CB  
15280 N N   . VAL B 858  ? 0.2707 0.2434 0.2308 0.0141  -0.0357 -0.0231 856  VAL B N   
15281 C CA  . VAL B 858  ? 0.2572 0.2310 0.2177 0.0130  -0.0347 -0.0207 856  VAL B CA  
15282 C C   . VAL B 858  ? 0.2386 0.2119 0.2047 0.0126  -0.0366 -0.0201 856  VAL B C   
15283 O O   . VAL B 858  ? 0.2772 0.2505 0.2436 0.0118  -0.0361 -0.0182 856  VAL B O   
15284 C CB  . VAL B 858  ? 0.2742 0.2515 0.2356 0.0126  -0.0308 -0.0198 856  VAL B CB  
15285 C CG1 . VAL B 858  ? 0.3217 0.3002 0.2769 0.0131  -0.0288 -0.0200 856  VAL B CG1 
15286 C CG2 . VAL B 858  ? 0.2939 0.2730 0.2615 0.0132  -0.0295 -0.0211 856  VAL B CG2 
15287 N N   . ALA B 859  ? 0.2828 0.2557 0.2533 0.0132  -0.0387 -0.0216 857  ALA B N   
15288 C CA  . ALA B 859  ? 0.2665 0.2403 0.2433 0.0131  -0.0398 -0.0212 857  ALA B CA  
15289 C C   . ALA B 859  ? 0.2422 0.2139 0.2170 0.0132  -0.0422 -0.0197 857  ALA B C   
15290 O O   . ALA B 859  ? 0.2847 0.2567 0.2620 0.0130  -0.0418 -0.0185 857  ALA B O   
15291 C CB  . ALA B 859  ? 0.2586 0.2330 0.2401 0.0135  -0.0417 -0.0230 857  ALA B CB  
15292 N N   . ASP B 860  ? 0.3025 0.2716 0.2723 0.0134  -0.0448 -0.0198 858  ASP B N   
15293 C CA  . ASP B 860  ? 0.3093 0.2759 0.2770 0.0137  -0.0475 -0.0184 858  ASP B CA  
15294 C C   . ASP B 860  ? 0.3087 0.2740 0.2728 0.0127  -0.0457 -0.0161 858  ASP B C   
15295 O O   . ASP B 860  ? 0.3000 0.2637 0.2652 0.0129  -0.0468 -0.0149 858  ASP B O   
15296 C CB  . ASP B 860  ? 0.2986 0.2626 0.2610 0.0141  -0.0505 -0.0188 858  ASP B CB  
15297 C CG  . ASP B 860  ? 0.3816 0.3466 0.3478 0.0148  -0.0532 -0.0208 858  ASP B CG  
15298 O OD1 . ASP B 860  ? 0.3999 0.3674 0.3733 0.0151  -0.0535 -0.0213 858  ASP B OD1 
15299 O OD2 . ASP B 860  ? 0.4659 0.4293 0.4280 0.0149  -0.0549 -0.0219 858  ASP B OD2 
15300 N N   . ARG B 861  ? 0.2812 0.2469 0.2406 0.0117  -0.0432 -0.0156 859  ARG B N   
15301 C CA  . ARG B 861  ? 0.2665 0.2313 0.2221 0.0103  -0.0416 -0.0132 859  ARG B CA  
15302 C C   . ARG B 861  ? 0.2811 0.2475 0.2419 0.0098  -0.0396 -0.0127 859  ARG B C   
15303 O O   . ARG B 861  ? 0.2896 0.2538 0.2494 0.0090  -0.0402 -0.0109 859  ARG B O   
15304 C CB  . ARG B 861  ? 0.3329 0.2991 0.2830 0.0093  -0.0391 -0.0127 859  ARG B CB  
15305 C CG  . ARG B 861  ? 0.4899 0.4562 0.4369 0.0072  -0.0370 -0.0102 859  ARG B CG  
15306 C CD  . ARG B 861  ? 0.6043 0.5710 0.5438 0.0061  -0.0358 -0.0091 859  ARG B CD  
15307 N NE  . ARG B 861  ? 0.6935 0.6607 0.6306 0.0036  -0.0339 -0.0064 859  ARG B NE  
15308 C CZ  . ARG B 861  ? 0.6293 0.6010 0.5685 0.0026  -0.0305 -0.0061 859  ARG B CZ  
15309 N NH1 . ARG B 861  ? 0.5263 0.5020 0.4696 0.0040  -0.0285 -0.0082 859  ARG B NH1 
15310 N NH2 . ARG B 861  ? 0.5876 0.5594 0.5248 0.0000  -0.0294 -0.0036 859  ARG B NH2 
15311 N N   . ILE B 862  ? 0.2669 0.2369 0.2329 0.0102  -0.0375 -0.0141 860  ILE B N   
15312 C CA  . ILE B 862  ? 0.2327 0.2045 0.2037 0.0098  -0.0357 -0.0137 860  ILE B CA  
15313 C C   . ILE B 862  ? 0.2354 0.2056 0.2104 0.0109  -0.0381 -0.0138 860  ILE B C   
15314 O O   . ILE B 862  ? 0.2721 0.2413 0.2481 0.0105  -0.0378 -0.0127 860  ILE B O   
15315 C CB  . ILE B 862  ? 0.2413 0.2169 0.2166 0.0102  -0.0332 -0.0152 860  ILE B CB  
15316 C CG1 . ILE B 862  ? 0.2915 0.2691 0.2628 0.0094  -0.0305 -0.0148 860  ILE B CG1 
15317 C CG2 . ILE B 862  ? 0.2612 0.2387 0.2421 0.0101  -0.0317 -0.0150 860  ILE B CG2 
15318 C CD1 . ILE B 862  ? 0.3222 0.3030 0.2965 0.0102  -0.0283 -0.0164 860  ILE B CD1 
15319 N N   . LEU B 863  ? 0.2508 0.2208 0.2281 0.0123  -0.0407 -0.0152 861  LEU B N   
15320 C CA  . LEU B 863  ? 0.2848 0.2543 0.2663 0.0136  -0.0429 -0.0153 861  LEU B CA  
15321 C C   . LEU B 863  ? 0.3104 0.2754 0.2875 0.0138  -0.0450 -0.0137 861  LEU B C   
15322 O O   . LEU B 863  ? 0.2693 0.2332 0.2486 0.0146  -0.0456 -0.0132 861  LEU B O   
15323 C CB  . LEU B 863  ? 0.2747 0.2458 0.2598 0.0148  -0.0453 -0.0170 861  LEU B CB  
15324 C CG  . LEU B 863  ? 0.3116 0.2867 0.3025 0.0147  -0.0435 -0.0186 861  LEU B CG  
15325 C CD1 . LEU B 863  ? 0.3303 0.3063 0.3232 0.0152  -0.0462 -0.0201 861  LEU B CD1 
15326 C CD2 . LEU B 863  ? 0.3424 0.3199 0.3393 0.0152  -0.0422 -0.0186 861  LEU B CD2 
15327 N N   . THR B 864  ? 0.2671 0.2291 0.2375 0.0132  -0.0464 -0.0127 862  THR B N   
15328 C CA  . THR B 864  ? 0.2690 0.2260 0.2343 0.0131  -0.0485 -0.0108 862  THR B CA  
15329 C C   . THR B 864  ? 0.2987 0.2542 0.2625 0.0115  -0.0464 -0.0092 862  THR B C   
15330 O O   . THR B 864  ? 0.3102 0.2621 0.2735 0.0121  -0.0478 -0.0083 862  THR B O   
15331 C CB  . THR B 864  ? 0.3452 0.2995 0.3030 0.0124  -0.0499 -0.0099 862  THR B CB  
15332 O OG1 . THR B 864  ? 0.3758 0.3310 0.3350 0.0140  -0.0524 -0.0115 862  THR B OG1 
15333 C CG2 . THR B 864  ? 0.3920 0.3405 0.3438 0.0120  -0.0520 -0.0076 862  THR B CG2 
15334 N N   . MET B 865  ? 0.2680 0.2262 0.2310 0.0096  -0.0430 -0.0089 863  MET B N   
15335 C CA  . MET B 865  ? 0.2706 0.2280 0.2323 0.0076  -0.0410 -0.0073 863  MET B CA  
15336 C C   . MET B 865  ? 0.2599 0.2184 0.2278 0.0087  -0.0404 -0.0082 863  MET B C   
15337 O O   . MET B 865  ? 0.2666 0.2219 0.2332 0.0081  -0.0408 -0.0070 863  MET B O   
15338 C CB  . MET B 865  ? 0.2734 0.2348 0.2337 0.0057  -0.0376 -0.0069 863  MET B CB  
15339 C CG  . MET B 865  ? 0.3170 0.2782 0.2755 0.0032  -0.0356 -0.0051 863  MET B CG  
15340 S SD  . MET B 865  ? 0.3550 0.3222 0.3124 0.0013  -0.0316 -0.0048 863  MET B SD  
15341 C CE  . MET B 865  ? 0.3831 0.3495 0.3344 0.0017  -0.0327 -0.0047 863  MET B CE  
15342 N N   . LEU B 866  ? 0.2581 0.2210 0.2322 0.0101  -0.0395 -0.0102 864  LEU B N   
15343 C CA  . LEU B 866  ? 0.2589 0.2235 0.2389 0.0112  -0.0388 -0.0110 864  LEU B CA  
15344 C C   . LEU B 866  ? 0.2634 0.2243 0.2438 0.0131  -0.0418 -0.0110 864  LEU B C   
15345 O O   . LEU B 866  ? 0.2714 0.2307 0.2527 0.0134  -0.0415 -0.0107 864  LEU B O   
15346 C CB  . LEU B 866  ? 0.2863 0.2560 0.2725 0.0122  -0.0376 -0.0130 864  LEU B CB  
15347 C CG  . LEU B 866  ? 0.2647 0.2368 0.2573 0.0135  -0.0369 -0.0140 864  LEU B CG  
15348 C CD1 . LEU B 866  ? 0.3004 0.2728 0.2928 0.0121  -0.0344 -0.0132 864  LEU B CD1 
15349 C CD2 . LEU B 866  ? 0.3079 0.2847 0.3059 0.0140  -0.0361 -0.0156 864  LEU B CD2 
15350 N N   . LYS B 867  ? 0.2729 0.2326 0.2526 0.0147  -0.0447 -0.0114 865  LYS B N   
15351 C CA  . LYS B 867  ? 0.2711 0.2276 0.2512 0.0171  -0.0477 -0.0115 865  LYS B CA  
15352 C C   . LYS B 867  ? 0.3002 0.2500 0.2738 0.0163  -0.0489 -0.0095 865  LYS B C   
15353 O O   . LYS B 867  ? 0.2785 0.2254 0.2526 0.0178  -0.0500 -0.0095 865  LYS B O   
15354 C CB  . LYS B 867  ? 0.2880 0.2449 0.2684 0.0188  -0.0508 -0.0122 865  LYS B CB  
15355 C CG  . LYS B 867  ? 0.3064 0.2697 0.2942 0.0197  -0.0501 -0.0142 865  LYS B CG  
15356 C CD  . LYS B 867  ? 0.3691 0.3332 0.3567 0.0205  -0.0529 -0.0149 865  LYS B CD  
15357 C CE  . LYS B 867  ? 0.4622 0.4324 0.4566 0.0206  -0.0520 -0.0167 865  LYS B CE  
15358 N NZ  . LYS B 867  ? 0.4892 0.4601 0.4833 0.0211  -0.0550 -0.0175 865  LYS B NZ  
15359 N N   . GLY B 868  ? 0.2783 0.2255 0.2454 0.0138  -0.0486 -0.0078 866  GLY B N   
15360 C CA  . GLY B 868  ? 0.2921 0.2326 0.2527 0.0123  -0.0496 -0.0056 866  GLY B CA  
15361 C C   . GLY B 868  ? 0.2956 0.2357 0.2572 0.0109  -0.0475 -0.0052 866  GLY B C   
15362 O O   . GLY B 868  ? 0.3078 0.2422 0.2667 0.0111  -0.0490 -0.0044 866  GLY B O   
15363 N N   . ALA B 869  ? 0.2910 0.2369 0.2564 0.0095  -0.0440 -0.0059 867  ALA B N   
15364 C CA  . ALA B 869  ? 0.2908 0.2372 0.2578 0.0082  -0.0419 -0.0058 867  ALA B CA  
15365 C C   . ALA B 869  ? 0.2805 0.2264 0.2521 0.0111  -0.0428 -0.0074 867  ALA B C   
15366 O O   . ALA B 869  ? 0.3061 0.2485 0.2765 0.0108  -0.0430 -0.0069 867  ALA B O   
15367 C CB  . ALA B 869  ? 0.2640 0.2172 0.2345 0.0066  -0.0383 -0.0063 867  ALA B CB  
15368 N N   . LEU B 870  ? 0.2508 0.2006 0.2279 0.0139  -0.0434 -0.0092 868  LEU B N   
15369 C CA  . LEU B 870  ? 0.2960 0.2465 0.2779 0.0169  -0.0440 -0.0107 868  LEU B CA  
15370 C C   . LEU B 870  ? 0.3002 0.2436 0.2781 0.0189  -0.0472 -0.0102 868  LEU B C   
15371 O O   . LEU B 870  ? 0.3097 0.2517 0.2891 0.0206  -0.0474 -0.0110 868  LEU B O   
15372 C CB  . LEU B 870  ? 0.2837 0.2400 0.2719 0.0192  -0.0443 -0.0125 868  LEU B CB  
15373 C CG  . LEU B 870  ? 0.3919 0.3550 0.3857 0.0183  -0.0411 -0.0135 868  LEU B CG  
15374 C CD1 . LEU B 870  ? 0.4056 0.3736 0.4048 0.0200  -0.0418 -0.0150 868  LEU B CD1 
15375 C CD2 . LEU B 870  ? 0.3619 0.3259 0.3585 0.0187  -0.0393 -0.0141 868  LEU B CD2 
15376 N N   . HIS B 871  ? 0.2858 0.2246 0.2584 0.0188  -0.0499 -0.0090 869  HIS B N   
15377 C CA  . HIS B 871  ? 0.2993 0.2308 0.2679 0.0209  -0.0533 -0.0084 869  HIS B CA  
15378 C C   . HIS B 871  ? 0.3215 0.2461 0.2844 0.0188  -0.0532 -0.0070 869  HIS B C   
15379 O O   . HIS B 871  ? 0.3672 0.2849 0.3266 0.0208  -0.0559 -0.0067 869  HIS B O   
15380 C CB  . HIS B 871  ? 0.3933 0.3216 0.3575 0.0215  -0.0563 -0.0074 869  HIS B CB  
15381 C CG  . HIS B 871  ? 0.6166 0.5499 0.5862 0.0247  -0.0578 -0.0091 869  HIS B CG  
15382 N ND1 . HIS B 871  ? 0.5729 0.5107 0.5437 0.0237  -0.0575 -0.0093 869  HIS B ND1 
15383 C CD2 . HIS B 871  ? 0.6227 0.5578 0.5970 0.0288  -0.0594 -0.0107 869  HIS B CD2 
15384 C CE1 . HIS B 871  ? 0.6792 0.6210 0.6553 0.0267  -0.0591 -0.0109 869  HIS B CE1 
15385 N NE2 . HIS B 871  ? 0.7277 0.6685 0.7062 0.0298  -0.0602 -0.0117 869  HIS B NE2 
15386 N N   . GLU B 872  ? 0.2923 0.2186 0.2542 0.0150  -0.0504 -0.0060 870  GLU B N   
15387 C CA  . GLU B 872  ? 0.3114 0.2319 0.2685 0.0124  -0.0502 -0.0046 870  GLU B CA  
15388 C C   . GLU B 872  ? 0.2980 0.2205 0.2592 0.0132  -0.0485 -0.0062 870  GLU B C   
15389 O O   . GLU B 872  ? 0.3128 0.2308 0.2704 0.0110  -0.0483 -0.0053 870  GLU B O   
15390 C CB  . GLU B 872  ? 0.3011 0.2228 0.2545 0.0075  -0.0483 -0.0025 870  GLU B CB  
15391 C CG  . GLU B 872  ? 0.2921 0.2119 0.2406 0.0065  -0.0498 -0.0009 870  GLU B CG  
15392 C CD  . GLU B 872  ? 0.3384 0.2482 0.2797 0.0069  -0.0536 0.0007  870  GLU B CD  
15393 O OE1 . GLU B 872  ? 0.4004 0.3040 0.3389 0.0064  -0.0546 0.0012  870  GLU B OE1 
15394 O OE2 . GLU B 872  ? 0.3690 0.2767 0.3072 0.0078  -0.0558 0.0014  870  GLU B OE2 
15395 N N   . LEU B 873  ? 0.2915 0.2207 0.2601 0.0160  -0.0472 -0.0084 871  LEU B N   
15396 C CA  . LEU B 873  ? 0.2945 0.2260 0.2670 0.0169  -0.0454 -0.0099 871  LEU B CA  
15397 C C   . LEU B 873  ? 0.3254 0.2510 0.2965 0.0205  -0.0478 -0.0109 871  LEU B C   
15398 O O   . LEU B 873  ? 0.3384 0.2619 0.3092 0.0238  -0.0505 -0.0114 871  LEU B O   
15399 C CB  . LEU B 873  ? 0.2654 0.2062 0.2459 0.0184  -0.0429 -0.0116 871  LEU B CB  
15400 C CG  . LEU B 873  ? 0.3722 0.3190 0.3547 0.0154  -0.0401 -0.0110 871  LEU B CG  
15401 C CD1 . LEU B 873  ? 0.3400 0.2947 0.3301 0.0168  -0.0379 -0.0128 871  LEU B CD1 
15402 C CD2 . LEU B 873  ? 0.3236 0.2691 0.3025 0.0114  -0.0384 -0.0095 871  LEU B CD2 
15403 N N   . HIS B 874  ? 0.3074 0.2308 0.2777 0.0201  -0.0470 -0.0114 872  HIS B N   
15404 C CA  . HIS B 874  ? 0.3459 0.2639 0.3148 0.0237  -0.0490 -0.0128 872  HIS B CA  
15405 C C   . HIS B 874  ? 0.2771 0.2022 0.2531 0.0265  -0.0467 -0.0151 872  HIS B C   
15406 O O   . HIS B 874  ? 0.2765 0.2056 0.2547 0.0242  -0.0439 -0.0153 872  HIS B O   
15407 C CB  . HIS B 874  ? 0.3036 0.2125 0.2652 0.0210  -0.0501 -0.0116 872  HIS B CB  
15408 C CG  . HIS B 874  ? 0.3325 0.2345 0.2915 0.0248  -0.0523 -0.0131 872  HIS B CG  
15409 N ND1 . HIS B 874  ? 0.4364 0.3293 0.3887 0.0229  -0.0537 -0.0124 872  HIS B ND1 
15410 C CD2 . HIS B 874  ? 0.3839 0.2868 0.3460 0.0304  -0.0534 -0.0153 872  HIS B CD2 
15411 C CE1 . HIS B 874  ? 0.4277 0.3156 0.3787 0.0274  -0.0556 -0.0143 872  HIS B CE1 
15412 N NE2 . HIS B 874  ? 0.4264 0.3206 0.3834 0.0322  -0.0553 -0.0161 872  HIS B NE2 
15413 N N   . ILE B 875  ? 0.3003 0.2277 0.2800 0.0312  -0.0479 -0.0168 873  ILE B N   
15414 C CA  . ILE B 875  ? 0.2906 0.2254 0.2773 0.0341  -0.0459 -0.0189 873  ILE B CA  
15415 C C   . ILE B 875  ? 0.3076 0.2369 0.2918 0.0380  -0.0475 -0.0204 873  ILE B C   
15416 O O   . ILE B 875  ? 0.3305 0.2537 0.3111 0.0410  -0.0507 -0.0206 873  ILE B O   
15417 C CB  . ILE B 875  ? 0.3581 0.3008 0.3514 0.0365  -0.0458 -0.0197 873  ILE B CB  
15418 C CG1 . ILE B 875  ? 0.4372 0.3863 0.4338 0.0329  -0.0436 -0.0188 873  ILE B CG1 
15419 C CG2 . ILE B 875  ? 0.3208 0.2700 0.3205 0.0401  -0.0443 -0.0219 873  ILE B CG2 
15420 C CD1 . ILE B 875  ? 0.5144 0.4593 0.5058 0.0297  -0.0448 -0.0168 873  ILE B CD1 
15421 N N   . GLY B 876  ? 0.2657 0.1967 0.2513 0.0380  -0.0454 -0.0216 874  GLY B N   
15422 C CA  . GLY B 876  ? 0.3001 0.2260 0.2832 0.0421  -0.0467 -0.0234 874  GLY B CA  
15423 C C   . GLY B 876  ? 0.2816 0.2096 0.2658 0.0414  -0.0441 -0.0245 874  GLY B C   
15424 O O   . GLY B 876  ? 0.2740 0.2085 0.2619 0.0383  -0.0411 -0.0240 874  GLY B O   
15425 N N   . ARG B 877  ? 0.3160 0.2380 0.2965 0.0446  -0.0455 -0.0261 875  ARG B N   
15426 C CA  . ARG B 877  ? 0.3020 0.2245 0.2822 0.0443  -0.0435 -0.0273 875  ARG B CA  
15427 C C   . ARG B 877  ? 0.3101 0.2290 0.2862 0.0382  -0.0428 -0.0255 875  ARG B C   
15428 O O   . ARG B 877  ? 0.3482 0.2587 0.3180 0.0356  -0.0451 -0.0239 875  ARG B O   
15429 C CB  . ARG B 877  ? 0.3026 0.2174 0.2781 0.0489  -0.0457 -0.0294 875  ARG B CB  
15430 C CG  . ARG B 877  ? 0.3474 0.2651 0.3241 0.0503  -0.0434 -0.0314 875  ARG B CG  
15431 C CD  . ARG B 877  ? 0.4468 0.3571 0.4188 0.0557  -0.0456 -0.0338 875  ARG B CD  
15432 N NE  . ARG B 877  ? 0.4053 0.3031 0.3681 0.0536  -0.0480 -0.0335 875  ARG B NE  
15433 C CZ  . ARG B 877  ? 0.5412 0.4306 0.4984 0.0575  -0.0500 -0.0356 875  ARG B CZ  
15434 N NH1 . ARG B 877  ? 0.4377 0.3300 0.3973 0.0643  -0.0501 -0.0381 875  ARG B NH1 
15435 N NH2 . ARG B 877  ? 0.4990 0.3769 0.4477 0.0547  -0.0521 -0.0352 875  ARG B NH2 
15436 N N   . THR B 878  ? 0.2700 0.1954 0.2496 0.0359  -0.0396 -0.0257 876  THR B N   
15437 C CA  . THR B 878  ? 0.2847 0.2103 0.2628 0.0300  -0.0383 -0.0237 876  THR B CA  
15438 C C   . THR B 878  ? 0.3099 0.2274 0.2813 0.0275  -0.0394 -0.0235 876  THR B C   
15439 O O   . THR B 878  ? 0.3206 0.2392 0.2910 0.0226  -0.0382 -0.0220 876  THR B O   
15440 C CB  . THR B 878  ? 0.2796 0.2161 0.2647 0.0287  -0.0345 -0.0237 876  THR B CB  
15441 O OG1 . THR B 878  ? 0.3246 0.2642 0.3121 0.0319  -0.0331 -0.0259 876  THR B OG1 
15442 C CG2 . THR B 878  ? 0.2841 0.2276 0.2750 0.0296  -0.0338 -0.0233 876  THR B CG2 
15443 N N   . ASP B 879  ? 0.3227 0.2318 0.2889 0.0305  -0.0418 -0.0250 877  ASP B N   
15444 C CA  . ASP B 879  ? 0.3320 0.2322 0.2911 0.0278  -0.0433 -0.0249 877  ASP B CA  
15445 C C   . ASP B 879  ? 0.3309 0.2213 0.2829 0.0245  -0.0465 -0.0227 877  ASP B C   
15446 O O   . ASP B 879  ? 0.3385 0.2184 0.2831 0.0235  -0.0490 -0.0229 877  ASP B O   
15447 C CB  . ASP B 879  ? 0.3412 0.2366 0.2976 0.0324  -0.0443 -0.0277 877  ASP B CB  
15448 C CG  . ASP B 879  ? 0.3944 0.2837 0.3483 0.0379  -0.0472 -0.0290 877  ASP B CG  
15449 O OD1 . ASP B 879  ? 0.4501 0.3432 0.4077 0.0397  -0.0474 -0.0284 877  ASP B OD1 
15450 O OD2 . ASP B 879  ? 0.4081 0.2885 0.3561 0.0406  -0.0494 -0.0307 877  ASP B OD2 
15451 N N   . ARG B 880  ? 0.3625 0.2558 0.3163 0.0226  -0.0464 -0.0207 878  ARG B N   
15452 C CA  . ARG B 880  ? 0.3286 0.2143 0.2761 0.0186  -0.0488 -0.0181 878  ARG B CA  
15453 C C   . ARG B 880  ? 0.3029 0.1965 0.2538 0.0136  -0.0463 -0.0158 878  ARG B C   
15454 O O   . ARG B 880  ? 0.3275 0.2304 0.2851 0.0150  -0.0441 -0.0160 878  ARG B O   
15455 C CB  . ARG B 880  ? 0.3630 0.2436 0.3083 0.0220  -0.0516 -0.0179 878  ARG B CB  
15456 C CG  . ARG B 880  ? 0.4034 0.2735 0.3431 0.0265  -0.0550 -0.0196 878  ARG B CG  
15457 C CD  . ARG B 880  ? 0.4699 0.3355 0.4075 0.0295  -0.0579 -0.0189 878  ARG B CD  
15458 N NE  . ARG B 880  ? 0.7522 0.6043 0.6816 0.0320  -0.0620 -0.0195 878  ARG B NE  
15459 C CZ  . ARG B 880  ? 0.7776 0.6269 0.7068 0.0386  -0.0634 -0.0222 878  ARG B CZ  
15460 N NH1 . ARG B 880  ? 0.7893 0.6488 0.7264 0.0431  -0.0610 -0.0245 878  ARG B NH1 
15461 N NH2 . ARG B 880  ? 0.8235 0.6593 0.7443 0.0407  -0.0673 -0.0225 878  ARG B NH2 
15462 N N   . LEU B 881  ? 0.3115 0.2015 0.2578 0.0080  -0.0468 -0.0137 879  LEU B N   
15463 C CA  . LEU B 881  ? 0.3146 0.2120 0.2636 0.0033  -0.0445 -0.0115 879  LEU B CA  
15464 C C   . LEU B 881  ? 0.3046 0.2046 0.2550 0.0040  -0.0446 -0.0102 879  LEU B C   
15465 O O   . LEU B 881  ? 0.3223 0.2312 0.2775 0.0025  -0.0421 -0.0095 879  LEU B O   
15466 C CB  . LEU B 881  ? 0.3192 0.2114 0.2621 -0.0028 -0.0455 -0.0092 879  LEU B CB  
15467 C CG  . LEU B 881  ? 0.3519 0.2517 0.2969 -0.0080 -0.0431 -0.0068 879  LEU B CG  
15468 C CD1 . LEU B 881  ? 0.3442 0.2545 0.2959 -0.0079 -0.0397 -0.0079 879  LEU B CD1 
15469 C CD2 . LEU B 881  ? 0.3283 0.2218 0.2664 -0.0140 -0.0449 -0.0043 879  LEU B CD2 
15470 N N   . SER B 882  ? 0.3074 0.1996 0.2537 0.0065  -0.0477 -0.0101 880  SER B N   
15471 C CA  . SER B 882  ? 0.2827 0.1765 0.2296 0.0071  -0.0483 -0.0089 880  SER B CA  
15472 C C   . SER B 882  ? 0.2965 0.1990 0.2511 0.0115  -0.0467 -0.0107 880  SER B C   
15473 O O   . SER B 882  ? 0.3299 0.2347 0.2856 0.0120  -0.0470 -0.0099 880  SER B O   
15474 C CB  . SER B 882  ? 0.3374 0.2198 0.2773 0.0087  -0.0524 -0.0083 880  SER B CB  
15475 O OG  . SER B 882  ? 0.3683 0.2479 0.3092 0.0146  -0.0539 -0.0109 880  SER B OG  
15476 N N   . VAL B 883  ? 0.2870 0.1943 0.2467 0.0146  -0.0450 -0.0131 881  VAL B N   
15477 C CA  . VAL B 883  ? 0.2865 0.2021 0.2535 0.0184  -0.0436 -0.0147 881  VAL B CA  
15478 C C   . VAL B 883  ? 0.2639 0.1893 0.2363 0.0158  -0.0402 -0.0141 881  VAL B C   
15479 O O   . VAL B 883  ? 0.3227 0.2511 0.2961 0.0132  -0.0380 -0.0139 881  VAL B O   
15480 C CB  . VAL B 883  ? 0.3001 0.2168 0.2701 0.0230  -0.0433 -0.0173 881  VAL B CB  
15481 C CG1 . VAL B 883  ? 0.3182 0.2451 0.2965 0.0260  -0.0412 -0.0187 881  VAL B CG1 
15482 C CG2 . VAL B 883  ? 0.3166 0.2240 0.2816 0.0267  -0.0468 -0.0181 881  VAL B CG2 
15483 N N   . ASP B 884  ? 0.2814 0.2116 0.2571 0.0166  -0.0399 -0.0138 882  ASP B N   
15484 C CA  . ASP B 884  ? 0.2843 0.2231 0.2648 0.0146  -0.0370 -0.0133 882  ASP B CA  
15485 C C   . ASP B 884  ? 0.3127 0.2593 0.3006 0.0174  -0.0350 -0.0152 882  ASP B C   
15486 O O   . ASP B 884  ? 0.3526 0.3054 0.3442 0.0159  -0.0322 -0.0153 882  ASP B O   
15487 C CB  . ASP B 884  ? 0.2924 0.2314 0.2716 0.0135  -0.0379 -0.0119 882  ASP B CB  
15488 C CG  . ASP B 884  ? 0.3090 0.2407 0.2807 0.0103  -0.0397 -0.0097 882  ASP B CG  
15489 O OD1 . ASP B 884  ? 0.3199 0.2515 0.2894 0.0065  -0.0384 -0.0086 882  ASP B OD1 
15490 O OD2 . ASP B 884  ? 0.3219 0.2482 0.2898 0.0114  -0.0425 -0.0091 882  ASP B OD2 
15491 N N   . VAL B 885  ? 0.2793 0.2260 0.2696 0.0216  -0.0364 -0.0166 883  VAL B N   
15492 C CA  . VAL B 885  ? 0.2558 0.2104 0.2533 0.0242  -0.0348 -0.0182 883  VAL B CA  
15493 C C   . VAL B 885  ? 0.2578 0.2110 0.2562 0.0283  -0.0356 -0.0200 883  VAL B C   
15494 O O   . VAL B 885  ? 0.2701 0.2176 0.2653 0.0309  -0.0384 -0.0204 883  VAL B O   
15495 C CB  . VAL B 885  ? 0.3058 0.2639 0.3063 0.0252  -0.0356 -0.0181 883  VAL B CB  
15496 C CG1 . VAL B 885  ? 0.3265 0.2928 0.3346 0.0276  -0.0341 -0.0196 883  VAL B CG1 
15497 C CG2 . VAL B 885  ? 0.3414 0.3008 0.3406 0.0215  -0.0347 -0.0165 883  VAL B CG2 
15498 N N   . GLY B 886  ? 0.2547 0.2126 0.2569 0.0289  -0.0332 -0.0212 884  GLY B N   
15499 C CA  . GLY B 886  ? 0.2633 0.2208 0.2664 0.0329  -0.0335 -0.0230 884  GLY B CA  
15500 C C   . GLY B 886  ? 0.2457 0.2109 0.2557 0.0362  -0.0329 -0.0243 884  GLY B C   
15501 O O   . GLY B 886  ? 0.2289 0.1982 0.2422 0.0358  -0.0331 -0.0237 884  GLY B O   
15502 N N   . PRO B 887  ? 0.2355 0.2029 0.2475 0.0396  -0.0322 -0.0260 885  PRO B N   
15503 C CA  . PRO B 887  ? 0.2221 0.1975 0.2409 0.0429  -0.0316 -0.0272 885  PRO B CA  
15504 C C   . PRO B 887  ? 0.2203 0.2047 0.2453 0.0408  -0.0284 -0.0269 885  PRO B C   
15505 O O   . PRO B 887  ? 0.2305 0.2153 0.2548 0.0376  -0.0264 -0.0261 885  PRO B O   
15506 C CB  . PRO B 887  ? 0.2253 0.1991 0.2429 0.0472  -0.0318 -0.0291 885  PRO B CB  
15507 C CG  . PRO B 887  ? 0.2380 0.2071 0.2510 0.0446  -0.0306 -0.0289 885  PRO B CG  
15508 C CD  . PRO B 887  ? 0.2500 0.2126 0.2580 0.0405  -0.0320 -0.0270 885  PRO B CD  
15509 N N   . VAL B 888  ? 0.2117 0.2035 0.2429 0.0427  -0.0281 -0.0274 886  VAL B N   
15510 C CA  . VAL B 888  ? 0.2157 0.2161 0.2529 0.0415  -0.0251 -0.0274 886  VAL B CA  
15511 C C   . VAL B 888  ? 0.2129 0.2160 0.2512 0.0442  -0.0234 -0.0289 886  VAL B C   
15512 O O   . VAL B 888  ? 0.2294 0.2288 0.2650 0.0478  -0.0248 -0.0302 886  VAL B O   
15513 C CB  . VAL B 888  ? 0.2673 0.2748 0.3108 0.0417  -0.0255 -0.0272 886  VAL B CB  
15514 C CG1 . VAL B 888  ? 0.2605 0.2648 0.3019 0.0388  -0.0271 -0.0259 886  VAL B CG1 
15515 C CG2 . VAL B 888  ? 0.2921 0.3023 0.3380 0.0462  -0.0272 -0.0285 886  VAL B CG2 
15516 N N   . ILE B 889  ? 0.2108 0.2199 0.2527 0.0425  -0.0204 -0.0286 887  ILE B N   
15517 C CA  . ILE B 889  ? 0.2104 0.2202 0.2514 0.0442  -0.0185 -0.0297 887  ILE B CA  
15518 C C   . ILE B 889  ? 0.2221 0.2367 0.2663 0.0490  -0.0185 -0.0315 887  ILE B C   
15519 O O   . ILE B 889  ? 0.2155 0.2275 0.2566 0.0518  -0.0183 -0.0329 887  ILE B O   
15520 C CB  . ILE B 889  ? 0.2139 0.2285 0.2574 0.0410  -0.0154 -0.0288 887  ILE B CB  
15521 C CG1 . ILE B 889  ? 0.2119 0.2266 0.2535 0.0424  -0.0135 -0.0299 887  ILE B CG1 
15522 C CG2 . ILE B 889  ? 0.2348 0.2583 0.2854 0.0403  -0.0140 -0.0283 887  ILE B CG2 
15523 C CD1 . ILE B 889  ? 0.2319 0.2375 0.2663 0.0424  -0.0149 -0.0304 887  ILE B CD1 
15524 N N   . THR B 890  ? 0.1947 0.2165 0.2449 0.0501  -0.0187 -0.0314 888  THR B N   
15525 C CA  . THR B 890  ? 0.2316 0.2601 0.2859 0.0546  -0.0184 -0.0329 888  THR B CA  
15526 C C   . THR B 890  ? 0.1983 0.2302 0.2565 0.0562  -0.0207 -0.0329 888  THR B C   
15527 O O   . THR B 890  ? 0.2080 0.2389 0.2669 0.0532  -0.0219 -0.0316 888  THR B O   
15528 C CB  . THR B 890  ? 0.2128 0.2511 0.2728 0.0537  -0.0149 -0.0327 888  THR B CB  
15529 O OG1 . THR B 890  ? 0.2395 0.2825 0.3040 0.0496  -0.0142 -0.0310 888  THR B OG1 
15530 C CG2 . THR B 890  ? 0.2297 0.2655 0.2861 0.0525  -0.0125 -0.0329 888  THR B CG2 
15531 N N   . SER B 891  ? 0.2092 0.2459 0.2702 0.0610  -0.0211 -0.0344 889  SER B N   
15532 C CA  A SER B 891  ? 0.1883 0.2306 0.2544 0.0628  -0.0231 -0.0344 889  SER B CA  
15533 C CA  B SER B 891  ? 0.1876 0.2298 0.2536 0.0628  -0.0231 -0.0344 889  SER B CA  
15534 C C   . SER B 891  ? 0.2340 0.2856 0.3072 0.0591  -0.0215 -0.0330 889  SER B C   
15535 O O   . SER B 891  ? 0.2409 0.2944 0.3168 0.0579  -0.0235 -0.0323 889  SER B O   
15536 C CB  A SER B 891  ? 0.2545 0.3015 0.3227 0.0691  -0.0235 -0.0364 889  SER B CB  
15537 C CB  B SER B 891  ? 0.2546 0.3013 0.3226 0.0691  -0.0236 -0.0364 889  SER B CB  
15538 O OG  A SER B 891  ? 0.2918 0.3291 0.3529 0.0729  -0.0255 -0.0377 889  SER B OG  
15539 O OG  B SER B 891  ? 0.2909 0.3466 0.3634 0.0699  -0.0202 -0.0369 889  SER B OG  
15540 N N   . GLU B 892  ? 0.2139 0.2712 0.2899 0.0572  -0.0181 -0.0327 890  GLU B N   
15541 C CA  . GLU B 892  ? 0.2471 0.3125 0.3293 0.0532  -0.0165 -0.0312 890  GLU B CA  
15542 C C   . GLU B 892  ? 0.2310 0.2907 0.3109 0.0484  -0.0176 -0.0297 890  GLU B C   
15543 O O   . GLU B 892  ? 0.2491 0.3125 0.3330 0.0462  -0.0187 -0.0288 890  GLU B O   
15544 C CB  . GLU B 892  ? 0.2995 0.3704 0.3838 0.0518  -0.0127 -0.0309 890  GLU B CB  
15545 C CG  . GLU B 892  ? 0.3705 0.4481 0.4601 0.0471  -0.0111 -0.0291 890  GLU B CG  
15546 C CD  . GLU B 892  ? 0.6667 0.7469 0.7565 0.0449  -0.0075 -0.0284 890  GLU B CD  
15547 O OE1 . GLU B 892  ? 0.7055 0.7795 0.7898 0.0453  -0.0065 -0.0288 890  GLU B OE1 
15548 O OE2 . GLU B 892  ? 0.6657 0.7542 0.7610 0.0425  -0.0057 -0.0273 890  GLU B OE2 
15549 N N   . ALA B 893  ? 0.2233 0.2741 0.2968 0.0468  -0.0174 -0.0294 891  ALA B N   
15550 C CA  . ALA B 893  ? 0.1888 0.2343 0.2598 0.0428  -0.0183 -0.0280 891  ALA B CA  
15551 C C   . ALA B 893  ? 0.2132 0.2556 0.2832 0.0437  -0.0218 -0.0281 891  ALA B C   
15552 O O   . ALA B 893  ? 0.2348 0.2780 0.3065 0.0409  -0.0228 -0.0271 891  ALA B O   
15553 C CB  . ALA B 893  ? 0.2462 0.2835 0.3105 0.0414  -0.0176 -0.0277 891  ALA B CB  
15554 N N   . LYS B 894  ? 0.2211 0.2593 0.2879 0.0476  -0.0239 -0.0292 892  LYS B N   
15555 C CA  . LYS B 894  ? 0.2258 0.2607 0.2912 0.0489  -0.0274 -0.0292 892  LYS B CA  
15556 C C   . LYS B 894  ? 0.2421 0.2857 0.3145 0.0490  -0.0284 -0.0291 892  LYS B C   
15557 O O   . LYS B 894  ? 0.2340 0.2764 0.3065 0.0470  -0.0304 -0.0283 892  LYS B O   
15558 C CB  . LYS B 894  ? 0.2447 0.2741 0.3058 0.0536  -0.0294 -0.0304 892  LYS B CB  
15559 C CG  . LYS B 894  ? 0.2415 0.2678 0.3012 0.0555  -0.0332 -0.0304 892  LYS B CG  
15560 C CD  . LYS B 894  ? 0.2431 0.2628 0.2978 0.0603  -0.0353 -0.0316 892  LYS B CD  
15561 C CE  . LYS B 894  ? 0.3148 0.3312 0.3680 0.0623  -0.0393 -0.0314 892  LYS B CE  
15562 N NZ  . LYS B 894  ? 0.4640 0.4716 0.5107 0.0665  -0.0417 -0.0323 892  LYS B NZ  
15563 N N   . ASP B 895  ? 0.2158 0.2686 0.2942 0.0511  -0.0269 -0.0298 893  ASP B N   
15564 C CA  . ASP B 895  ? 0.2187 0.2809 0.3044 0.0509  -0.0278 -0.0296 893  ASP B CA  
15565 C C   . ASP B 895  ? 0.2500 0.3142 0.3381 0.0454  -0.0269 -0.0281 893  ASP B C   
15566 O O   . ASP B 895  ? 0.2686 0.3356 0.3597 0.0440  -0.0291 -0.0277 893  ASP B O   
15567 C CB  . ASP B 895  ? 0.2529 0.3254 0.3446 0.0538  -0.0258 -0.0305 893  ASP B CB  
15568 C CG  . ASP B 895  ? 0.2870 0.3585 0.3771 0.0600  -0.0271 -0.0322 893  ASP B CG  
15569 O OD1 . ASP B 895  ? 0.3506 0.4145 0.4360 0.0621  -0.0302 -0.0326 893  ASP B OD1 
15570 O OD2 . ASP B 895  ? 0.3045 0.3829 0.3979 0.0629  -0.0251 -0.0332 893  ASP B OD2 
15571 N N   . ASN B 896  ? 0.2217 0.2848 0.3086 0.0423  -0.0240 -0.0274 894  ASN B N   
15572 C CA  . ASN B 896  ? 0.2186 0.2828 0.3072 0.0373  -0.0231 -0.0261 894  ASN B CA  
15573 C C   . ASN B 896  ? 0.2581 0.3147 0.3422 0.0353  -0.0255 -0.0256 894  ASN B C   
15574 O O   . ASN B 896  ? 0.2545 0.3131 0.3410 0.0328  -0.0269 -0.0251 894  ASN B O   
15575 C CB  . ASN B 896  ? 0.2662 0.3293 0.3531 0.0354  -0.0196 -0.0256 894  ASN B CB  
15576 C CG  . ASN B 896  ? 0.3485 0.4119 0.4365 0.0305  -0.0185 -0.0242 894  ASN B CG  
15577 O OD1 . ASN B 896  ? 0.3842 0.4423 0.4693 0.0283  -0.0200 -0.0237 894  ASN B OD1 
15578 N ND2 . ASN B 896  ? 0.4532 0.5225 0.5449 0.0290  -0.0158 -0.0236 894  ASN B ND2 
15579 N N   . ILE B 897  ? 0.2319 0.2799 0.3094 0.0364  -0.0262 -0.0258 895  ILE B N   
15580 C CA  . ILE B 897  ? 0.2300 0.2708 0.3025 0.0347  -0.0283 -0.0253 895  ILE B CA  
15581 C C   . ILE B 897  ? 0.2456 0.2878 0.3198 0.0363  -0.0318 -0.0256 895  ILE B C   
15582 O O   . ILE B 897  ? 0.2597 0.3012 0.3338 0.0339  -0.0334 -0.0251 895  ILE B O   
15583 C CB  . ILE B 897  ? 0.2053 0.2373 0.2706 0.0357  -0.0284 -0.0253 895  ILE B CB  
15584 C CG1 . ILE B 897  ? 0.1932 0.2241 0.2570 0.0337  -0.0251 -0.0249 895  ILE B CG1 
15585 C CG2 . ILE B 897  ? 0.2279 0.2531 0.2881 0.0342  -0.0307 -0.0247 895  ILE B CG2 
15586 C CD1 . ILE B 897  ? 0.2147 0.2391 0.2727 0.0352  -0.0249 -0.0252 895  ILE B CD1 
15587 N N   . GLU B 898  ? 0.2466 0.2907 0.3220 0.0405  -0.0332 -0.0266 896  GLU B N   
15588 C CA  . GLU B 898  ? 0.2411 0.2864 0.3177 0.0425  -0.0367 -0.0269 896  GLU B CA  
15589 C C   . GLU B 898  ? 0.2538 0.3083 0.3377 0.0407  -0.0372 -0.0267 896  GLU B C   
15590 O O   . GLU B 898  ? 0.2627 0.3170 0.3469 0.0401  -0.0401 -0.0265 896  GLU B O   
15591 C CB  . GLU B 898  ? 0.2677 0.3130 0.3439 0.0479  -0.0380 -0.0280 896  GLU B CB  
15592 C CG  . GLU B 898  ? 0.2631 0.2974 0.3308 0.0492  -0.0386 -0.0280 896  GLU B CG  
15593 C CD  . GLU B 898  ? 0.4121 0.4445 0.4782 0.0546  -0.0403 -0.0291 896  GLU B CD  
15594 O OE1 . GLU B 898  ? 0.3854 0.4257 0.4570 0.0578  -0.0399 -0.0302 896  GLU B OE1 
15595 O OE2 . GLU B 898  ? 0.4769 0.4996 0.5358 0.0557  -0.0419 -0.0290 896  GLU B OE2 
15596 N N   . LYS B 899  ? 0.2230 0.2851 0.3125 0.0395  -0.0345 -0.0266 897  LYS B N   
15597 C CA  . LYS B 899  ? 0.2421 0.3128 0.3384 0.0370  -0.0349 -0.0262 897  LYS B CA  
15598 C C   . LYS B 899  ? 0.2828 0.3491 0.3768 0.0324  -0.0358 -0.0254 897  LYS B C   
15599 O O   . LYS B 899  ? 0.2850 0.3544 0.3819 0.0309  -0.0382 -0.0252 897  LYS B O   
15600 C CB  . LYS B 899  ? 0.2746 0.3536 0.3766 0.0359  -0.0315 -0.0259 897  LYS B CB  
15601 C CG  . LYS B 899  ? 0.3118 0.3996 0.4208 0.0328  -0.0320 -0.0253 897  LYS B CG  
15602 C CD  . LYS B 899  ? 0.4220 0.5188 0.5368 0.0319  -0.0287 -0.0248 897  LYS B CD  
15603 C CE  . LYS B 899  ? 0.3919 0.4848 0.5041 0.0279  -0.0258 -0.0238 897  LYS B CE  
15604 N NZ  . LYS B 899  ? 0.3821 0.4843 0.5004 0.0257  -0.0231 -0.0229 897  LYS B NZ  
15605 N N   . HIS B 900  ? 0.2243 0.2837 0.3132 0.0303  -0.0340 -0.0249 898  HIS B N   
15606 C CA  . HIS B 900  ? 0.2282 0.2826 0.3140 0.0265  -0.0348 -0.0243 898  HIS B CA  
15607 C C   . HIS B 900  ? 0.2597 0.3087 0.3412 0.0276  -0.0382 -0.0245 898  HIS B C   
15608 O O   . HIS B 900  ? 0.2873 0.3363 0.3692 0.0255  -0.0404 -0.0245 898  HIS B O   
15609 C CB  . HIS B 900  ? 0.2422 0.2907 0.3233 0.0248  -0.0320 -0.0237 898  HIS B CB  
15610 C CG  . HIS B 900  ? 0.2570 0.2993 0.3335 0.0220  -0.0329 -0.0234 898  HIS B CG  
15611 N ND1 . HIS B 900  ? 0.2891 0.3328 0.3676 0.0187  -0.0332 -0.0231 898  HIS B ND1 
15612 C CD2 . HIS B 900  ? 0.2555 0.2900 0.3253 0.0222  -0.0337 -0.0233 898  HIS B CD2 
15613 C CE1 . HIS B 900  ? 0.2568 0.2940 0.3300 0.0172  -0.0340 -0.0230 898  HIS B CE1 
15614 N NE2 . HIS B 900  ? 0.2529 0.2849 0.3209 0.0193  -0.0342 -0.0231 898  HIS B NE2 
15615 N N   . ILE B 901  ? 0.2462 0.2902 0.3232 0.0307  -0.0390 -0.0248 899  ILE B N   
15616 C CA  . ILE B 901  ? 0.2286 0.2667 0.3007 0.0317  -0.0422 -0.0249 899  ILE B CA  
15617 C C   . ILE B 901  ? 0.3008 0.3444 0.3773 0.0327  -0.0454 -0.0253 899  ILE B C   
15618 O O   . ILE B 901  ? 0.3008 0.3424 0.3756 0.0312  -0.0479 -0.0252 899  ILE B O   
15619 C CB  . ILE B 901  ? 0.2593 0.2911 0.3259 0.0349  -0.0425 -0.0250 899  ILE B CB  
15620 C CG1 . ILE B 901  ? 0.2437 0.2695 0.3052 0.0331  -0.0398 -0.0244 899  ILE B CG1 
15621 C CG2 . ILE B 901  ? 0.2805 0.3071 0.3425 0.0362  -0.0462 -0.0249 899  ILE B CG2 
15622 C CD1 . ILE B 901  ? 0.2767 0.2968 0.3333 0.0358  -0.0397 -0.0245 899  ILE B CD1 
15623 N N   . GLU B 902  ? 0.2574 0.3088 0.3400 0.0353  -0.0453 -0.0258 900  GLU B N   
15624 C CA  . GLU B 902  ? 0.2738 0.3315 0.3612 0.0366  -0.0485 -0.0262 900  GLU B CA  
15625 C C   . GLU B 902  ? 0.2942 0.3575 0.3865 0.0324  -0.0488 -0.0259 900  GLU B C   
15626 O O   . GLU B 902  ? 0.3273 0.3933 0.4216 0.0321  -0.0521 -0.0260 900  GLU B O   
15627 C CB  . GLU B 902  ? 0.3422 0.4074 0.4350 0.0409  -0.0482 -0.0269 900  GLU B CB  
15628 C CG  . GLU B 902  ? 0.3929 0.4520 0.4805 0.0456  -0.0490 -0.0274 900  GLU B CG  
15629 C CD  . GLU B 902  ? 0.4679 0.5193 0.5495 0.0465  -0.0528 -0.0272 900  GLU B CD  
15630 O OE1 . GLU B 902  ? 0.4202 0.4753 0.5045 0.0463  -0.0558 -0.0272 900  GLU B OE1 
15631 O OE2 . GLU B 902  ? 0.4505 0.4925 0.5247 0.0472  -0.0528 -0.0269 900  GLU B OE2 
15632 N N   . ARG B 903  ? 0.3105 0.3754 0.4045 0.0290  -0.0457 -0.0254 901  ARG B N   
15633 C CA  . ARG B 903  ? 0.2842 0.3527 0.3818 0.0247  -0.0463 -0.0250 901  ARG B CA  
15634 C C   . ARG B 903  ? 0.3525 0.4131 0.4442 0.0223  -0.0483 -0.0249 901  ARG B C   
15635 O O   . ARG B 903  ? 0.3624 0.4248 0.4558 0.0201  -0.0509 -0.0251 901  ARG B O   
15636 C CB  . ARG B 903  ? 0.3504 0.4216 0.4506 0.0218  -0.0425 -0.0243 901  ARG B CB  
15637 C CG  . ARG B 903  ? 0.4374 0.5112 0.5407 0.0170  -0.0431 -0.0238 901  ARG B CG  
15638 C CD  . ARG B 903  ? 0.4929 0.5692 0.5986 0.0142  -0.0395 -0.0230 901  ARG B CD  
15639 N NE  . ARG B 903  ? 0.6068 0.6852 0.7153 0.0095  -0.0404 -0.0224 901  ARG B NE  
15640 C CZ  . ARG B 903  ? 0.5773 0.6484 0.6813 0.0064  -0.0407 -0.0223 901  ARG B CZ  
15641 N NH1 . ARG B 903  ? 0.4839 0.5460 0.5807 0.0074  -0.0399 -0.0225 901  ARG B NH1 
15642 N NH2 . ARG B 903  ? 0.6010 0.6739 0.7075 0.0022  -0.0420 -0.0218 901  ARG B NH2 
15643 N N   . MET B 904  ? 0.2828 0.3346 0.3673 0.0226  -0.0470 -0.0248 902  MET B N   
15644 C CA  . MET B 904  ? 0.3056 0.3499 0.3838 0.0209  -0.0488 -0.0248 902  MET B CA  
15645 C C   . MET B 904  ? 0.3685 0.4120 0.4452 0.0230  -0.0529 -0.0252 902  MET B C   
15646 O O   . MET B 904  ? 0.3450 0.3870 0.4203 0.0211  -0.0555 -0.0255 902  MET B O   
15647 C CB  . MET B 904  ? 0.3709 0.4071 0.4421 0.0212  -0.0466 -0.0245 902  MET B CB  
15648 C CG  . MET B 904  ? 0.3047 0.3413 0.3768 0.0192  -0.0428 -0.0241 902  MET B CG  
15649 S SD  . MET B 904  ? 0.4022 0.4382 0.4748 0.0147  -0.0429 -0.0241 902  MET B SD  
15650 C CE  . MET B 904  ? 0.4468 0.4926 0.5286 0.0132  -0.0417 -0.0237 902  MET B CE  
15651 N N   . ARG B 905  ? 0.3308 0.3750 0.4076 0.0270  -0.0537 -0.0254 903  ARG B N   
15652 C CA  . ARG B 905  ? 0.3999 0.4436 0.4755 0.0293  -0.0577 -0.0256 903  ARG B CA  
15653 C C   . ARG B 905  ? 0.3717 0.4237 0.4540 0.0283  -0.0603 -0.0260 903  ARG B C   
15654 O O   . ARG B 905  ? 0.3776 0.4282 0.4581 0.0274  -0.0637 -0.0262 903  ARG B O   
15655 C CB  . ARG B 905  ? 0.4310 0.4742 0.5058 0.0341  -0.0580 -0.0257 903  ARG B CB  
15656 C CG  . ARG B 905  ? 0.4940 0.5311 0.5629 0.0366  -0.0615 -0.0256 903  ARG B CG  
15657 C CD  . ARG B 905  ? 0.4292 0.4667 0.4985 0.0416  -0.0623 -0.0258 903  ARG B CD  
15658 N NE  . ARG B 905  ? 0.4793 0.5126 0.5457 0.0425  -0.0591 -0.0257 903  ARG B NE  
15659 C CZ  . ARG B 905  ? 0.4039 0.4277 0.4624 0.0428  -0.0589 -0.0251 903  ARG B CZ  
15660 N NH1 . ARG B 905  ? 0.4489 0.4663 0.5013 0.0420  -0.0613 -0.0245 903  ARG B NH1 
15661 N NH2 . ARG B 905  ? 0.4900 0.5109 0.5466 0.0437  -0.0562 -0.0251 903  ARG B NH2 
15662 N N   . GLY B 906  ? 0.3458 0.4068 0.4359 0.0281  -0.0587 -0.0260 904  GLY B N   
15663 C CA  . GLY B 906  ? 0.3601 0.4302 0.4574 0.0269  -0.0611 -0.0262 904  GLY B CA  
15664 C C   . GLY B 906  ? 0.4322 0.5011 0.5291 0.0219  -0.0622 -0.0261 904  GLY B C   
15665 O O   . GLY B 906  ? 0.4399 0.5132 0.5401 0.0206  -0.0655 -0.0264 904  GLY B O   
15666 N N   . LEU B 907  ? 0.4114 0.4740 0.5041 0.0190  -0.0597 -0.0259 905  LEU B N   
15667 C CA  . LEU B 907  ? 0.4242 0.4836 0.5149 0.0146  -0.0607 -0.0260 905  LEU B CA  
15668 C C   . LEU B 907  ? 0.4643 0.5154 0.5473 0.0149  -0.0635 -0.0264 905  LEU B C   
15669 O O   . LEU B 907  ? 0.4372 0.4843 0.5172 0.0117  -0.0644 -0.0268 905  LEU B O   
15670 C CB  . LEU B 907  ? 0.3995 0.4555 0.4886 0.0119  -0.0568 -0.0255 905  LEU B CB  
15671 N N   . GLY B 908  ? 0.3673 0.4155 0.4467 0.0187  -0.0649 -0.0265 906  GLY B N   
15672 C CA  . GLY B 908  ? 0.3821 0.4231 0.4541 0.0191  -0.0676 -0.0267 906  GLY B CA  
15673 C C   . GLY B 908  ? 0.4833 0.5150 0.5470 0.0189  -0.0654 -0.0265 906  GLY B C   
15674 O O   . GLY B 908  ? 0.4369 0.4625 0.4939 0.0191  -0.0674 -0.0266 906  GLY B O   
15675 N N   . ARG B 909  ? 0.3631 0.3938 0.4269 0.0184  -0.0613 -0.0261 907  ARG B N   
15676 C CA  . ARG B 909  ? 0.3633 0.3861 0.4197 0.0183  -0.0591 -0.0258 907  ARG B CA  
15677 C C   . ARG B 909  ? 0.3756 0.3943 0.4273 0.0216  -0.0599 -0.0252 907  ARG B C   
15678 O O   . ARG B 909  ? 0.4208 0.4427 0.4755 0.0244  -0.0607 -0.0251 907  ARG B O   
15679 C CB  . ARG B 909  ? 0.3233 0.3467 0.3814 0.0173  -0.0548 -0.0254 907  ARG B CB  
15680 C CG  . ARG B 909  ? 0.4391 0.4663 0.5019 0.0142  -0.0537 -0.0256 907  ARG B CG  
15681 C CD  . ARG B 909  ? 0.5420 0.5637 0.6000 0.0115  -0.0539 -0.0260 907  ARG B CD  
15682 N NE  . ARG B 909  ? 0.6575 0.6816 0.7194 0.0086  -0.0523 -0.0260 907  ARG B NE  
15683 C CZ  . ARG B 909  ? 0.6431 0.6716 0.7098 0.0063  -0.0543 -0.0263 907  ARG B CZ  
15684 N NH1 . ARG B 909  ? 0.7352 0.7662 0.8034 0.0065  -0.0580 -0.0267 907  ARG B NH1 
15685 N NH2 . ARG B 909  ? 0.7290 0.7594 0.7990 0.0035  -0.0526 -0.0260 907  ARG B NH2 
15686 N N   . LYS B 910  ? 0.3173 0.3287 0.3611 0.0212  -0.0598 -0.0249 908  LYS B N   
15687 C CA  . LYS B 910  ? 0.3209 0.3274 0.3593 0.0236  -0.0604 -0.0242 908  LYS B CA  
15688 C C   . LYS B 910  ? 0.3857 0.3916 0.4245 0.0246  -0.0570 -0.0236 908  LYS B C   
15689 O O   . LYS B 910  ? 0.3680 0.3726 0.4058 0.0228  -0.0538 -0.0235 908  LYS B O   
15690 C CB  . LYS B 910  ? 0.4076 0.4072 0.4376 0.0225  -0.0609 -0.0239 908  LYS B CB  
15691 C CG  . LYS B 910  ? 0.4667 0.4607 0.4903 0.0244  -0.0617 -0.0228 908  LYS B CG  
15692 C CD  . LYS B 910  ? 0.5770 0.5652 0.5925 0.0230  -0.0624 -0.0224 908  LYS B CD  
15693 C CE  . LYS B 910  ? 0.6468 0.6293 0.6557 0.0246  -0.0637 -0.0210 908  LYS B CE  
15694 N NZ  . LYS B 910  ? 0.6444 0.6217 0.6451 0.0230  -0.0633 -0.0204 908  LYS B NZ  
15695 N N   . VAL B 911  ? 0.2977 0.3044 0.3379 0.0277  -0.0579 -0.0234 909  VAL B N   
15696 C CA  . VAL B 911  ? 0.3364 0.3423 0.3768 0.0291  -0.0553 -0.0230 909  VAL B CA  
15697 C C   . VAL B 911  ? 0.3204 0.3197 0.3543 0.0312  -0.0568 -0.0223 909  VAL B C   
15698 O O   . VAL B 911  ? 0.3461 0.3450 0.3796 0.0336  -0.0602 -0.0223 909  VAL B O   
15699 C CB  . VAL B 911  ? 0.3287 0.3420 0.3770 0.0310  -0.0547 -0.0237 909  VAL B CB  
15700 C CG1 . VAL B 911  ? 0.3270 0.3387 0.3746 0.0328  -0.0523 -0.0235 909  VAL B CG1 
15701 C CG2 . VAL B 911  ? 0.3702 0.3900 0.4247 0.0283  -0.0532 -0.0242 909  VAL B CG2 
15702 N N   . GLU B 912  ? 0.2932 0.2874 0.3223 0.0303  -0.0545 -0.0215 910  GLU B N   
15703 C CA  . GLU B 912  ? 0.3420 0.3291 0.3645 0.0318  -0.0557 -0.0205 910  GLU B CA  
15704 C C   . GLU B 912  ? 0.4099 0.3954 0.4322 0.0325  -0.0533 -0.0203 910  GLU B C   
15705 O O   . GLU B 912  ? 0.3486 0.3358 0.3724 0.0305  -0.0500 -0.0204 910  GLU B O   
15706 C CB  . GLU B 912  ? 0.3690 0.3504 0.3840 0.0293  -0.0558 -0.0194 910  GLU B CB  
15707 C CG  . GLU B 912  ? 0.5118 0.4938 0.5258 0.0289  -0.0586 -0.0197 910  GLU B CG  
15708 C CD  . GLU B 912  ? 0.5396 0.5166 0.5463 0.0265  -0.0584 -0.0188 910  GLU B CD  
15709 O OE1 . GLU B 912  ? 0.6659 0.6370 0.6661 0.0269  -0.0596 -0.0175 910  GLU B OE1 
15710 O OE2 . GLU B 912  ? 0.7119 0.6908 0.7191 0.0244  -0.0570 -0.0193 910  GLU B OE2 
15711 N N   . GLN B 913  ? 0.3235 0.3055 0.3437 0.0354  -0.0550 -0.0201 911  GLN B N   
15712 C CA  . GLN B 913  ? 0.3488 0.3284 0.3681 0.0363  -0.0531 -0.0201 911  GLN B CA  
15713 C C   . GLN B 913  ? 0.4511 0.4217 0.4626 0.0373  -0.0551 -0.0190 911  GLN B C   
15714 O O   . GLN B 913  ? 0.4465 0.4139 0.4550 0.0390  -0.0585 -0.0186 911  GLN B O   
15715 C CB  . GLN B 913  ? 0.3548 0.3399 0.3805 0.0397  -0.0530 -0.0215 911  GLN B CB  
15716 C CG  . GLN B 913  ? 0.3830 0.3773 0.4167 0.0388  -0.0512 -0.0224 911  GLN B CG  
15717 C CD  . GLN B 913  ? 0.4177 0.4178 0.4574 0.0422  -0.0509 -0.0236 911  GLN B CD  
15718 O OE1 . GLN B 913  ? 0.5150 0.5164 0.5561 0.0456  -0.0537 -0.0241 911  GLN B OE1 
15719 N NE2 . GLN B 913  ? 0.3362 0.3401 0.3794 0.0414  -0.0476 -0.0240 911  GLN B NE2 
15720 N N   . ILE B 914  ? 0.4143 0.3807 0.4224 0.0361  -0.0531 -0.0184 912  ILE B N   
15721 C CA  . ILE B 914  ? 0.5626 0.5201 0.5634 0.0367  -0.0548 -0.0174 912  ILE B CA  
15722 C C   . ILE B 914  ? 0.6773 0.6335 0.6794 0.0412  -0.0565 -0.0184 912  ILE B C   
15723 O O   . ILE B 914  ? 0.5677 0.5307 0.5766 0.0436  -0.0556 -0.0200 912  ILE B O   
15724 C CB  . ILE B 914  ? 0.5684 0.5223 0.5652 0.0332  -0.0521 -0.0164 912  ILE B CB  
15725 C CG1 . ILE B 914  ? 0.5376 0.4936 0.5379 0.0343  -0.0499 -0.0175 912  ILE B CG1 
15726 C CG2 . ILE B 914  ? 0.6994 0.6570 0.6970 0.0294  -0.0497 -0.0158 912  ILE B CG2 
15727 C CD1 . ILE B 914  ? 0.6052 0.5529 0.5995 0.0349  -0.0508 -0.0170 912  ILE B CD1 
15728 N N   . GLY B 915  ? 0.6743 0.6218 0.6697 0.0426  -0.0591 -0.0176 913  GLY B N   
15729 C CA  . GLY B 915  ? 0.6463 0.5913 0.6417 0.0475  -0.0612 -0.0187 913  GLY B CA  
15730 C C   . GLY B 915  ? 0.6202 0.5620 0.6143 0.0479  -0.0594 -0.0193 913  GLY B C   
15731 O O   . GLY B 915  ? 0.6582 0.5950 0.6475 0.0443  -0.0580 -0.0182 913  GLY B O   
15732 N N   . LEU B 916  ? 0.5743 0.5193 0.5725 0.0523  -0.0595 -0.0212 914  LEU B N   
15733 C CA  . LEU B 916  ? 0.5352 0.4776 0.5324 0.0534  -0.0579 -0.0222 914  LEU B CA  
15734 C C   . LEU B 916  ? 0.5375 0.4707 0.5288 0.0576  -0.0613 -0.0226 914  LEU B C   
15735 O O   . LEU B 916  ? 0.5345 0.4683 0.5270 0.0620  -0.0641 -0.0232 914  LEU B O   
15736 C CB  . LEU B 916  ? 0.5001 0.4529 0.5058 0.0555  -0.0553 -0.0241 914  LEU B CB  
15737 C CG  . LEU B 916  ? 0.4693 0.4305 0.4806 0.0516  -0.0517 -0.0239 914  LEU B CG  
15738 C CD1 . LEU B 916  ? 0.5195 0.4892 0.5379 0.0537  -0.0491 -0.0257 914  LEU B CD1 
15739 C CD2 . LEU B 916  ? 0.4635 0.4200 0.4702 0.0465  -0.0498 -0.0225 914  LEU B CD2 
15740 N N   . ALA B 917  ? 0.4839 0.4083 0.4686 0.0562  -0.0612 -0.0221 915  ALA B N   
15741 C CA  . ALA B 917  ? 0.4733 0.3876 0.4516 0.0601  -0.0644 -0.0226 915  ALA B CA  
15742 C C   . ALA B 917  ? 0.5718 0.4905 0.5547 0.0661  -0.0642 -0.0253 915  ALA B C   
15743 O O   . ALA B 917  ? 0.5044 0.4325 0.4943 0.0662  -0.0609 -0.0267 915  ALA B O   
15744 C CB  . ALA B 917  ? 0.5828 0.4870 0.5532 0.0565  -0.0643 -0.0215 915  ALA B CB  
15745 N N   . SER B 918  ? 0.5404 0.4520 0.5191 0.0713  -0.0677 -0.0261 916  SER B N   
15746 C CA  . SER B 918  ? 0.5380 0.4540 0.5209 0.0778  -0.0678 -0.0288 916  SER B CA  
15747 C C   . SER B 918  ? 0.5284 0.4445 0.5113 0.0778  -0.0649 -0.0304 916  SER B C   
15748 O O   . SER B 918  ? 0.5169 0.4410 0.5057 0.0818  -0.0632 -0.0326 916  SER B O   
15749 C CB  . SER B 918  ? 0.5547 0.4614 0.5317 0.0835  -0.0724 -0.0293 916  SER B CB  
15750 O OG  . SER B 918  ? 0.6285 0.5210 0.5955 0.0822  -0.0741 -0.0286 916  SER B OG  
15751 N N   . GLU B 919  ? 0.4982 0.4059 0.4747 0.0732  -0.0643 -0.0293 917  GLU B N   
15752 C CA  . GLU B 919  ? 0.5852 0.4923 0.5610 0.0729  -0.0618 -0.0307 917  GLU B CA  
15753 C C   . GLU B 919  ? 0.5865 0.5069 0.5712 0.0710  -0.0573 -0.0314 917  GLU B C   
15754 O O   . GLU B 919  ? 0.5062 0.4288 0.4922 0.0722  -0.0551 -0.0331 917  GLU B O   
15755 C CB  . GLU B 919  ? 0.5329 0.4292 0.5004 0.0675  -0.0621 -0.0291 917  GLU B CB  
15756 N N   . THR B 920  ? 0.5059 0.4348 0.4964 0.0682  -0.0560 -0.0301 918  THR B N   
15757 C CA  . THR B 920  ? 0.4204 0.3614 0.4191 0.0662  -0.0519 -0.0305 918  THR B CA  
15758 C C   . THR B 920  ? 0.4062 0.3567 0.4120 0.0716  -0.0509 -0.0328 918  THR B C   
15759 O O   . THR B 920  ? 0.3989 0.3585 0.4106 0.0705  -0.0474 -0.0333 918  THR B O   
15760 C CB  . THR B 920  ? 0.4545 0.4009 0.4567 0.0618  -0.0511 -0.0286 918  THR B CB  
15761 O OG1 . THR B 920  ? 0.4231 0.3717 0.4275 0.0645  -0.0538 -0.0285 918  THR B OG1 
15762 C CG2 . THR B 920  ? 0.4195 0.3581 0.4152 0.0563  -0.0515 -0.0264 918  THR B CG2 
15763 N N   . GLY B 921  ? 0.3877 0.3367 0.3930 0.0774  -0.0538 -0.0339 919  GLY B N   
15764 C CA  . GLY B 921  ? 0.4130 0.3724 0.4257 0.0826  -0.0529 -0.0359 919  GLY B CA  
15765 C C   . GLY B 921  ? 0.4259 0.3879 0.4395 0.0849  -0.0501 -0.0380 919  GLY B C   
15766 O O   . GLY B 921  ? 0.4252 0.3986 0.4463 0.0874  -0.0479 -0.0392 919  GLY B O   
15767 N N   . VAL B 922  ? 0.3387 0.2905 0.3448 0.0840  -0.0503 -0.0383 920  VAL B N   
15768 C CA  . VAL B 922  ? 0.3029 0.2565 0.3091 0.0859  -0.0477 -0.0403 920  VAL B CA  
15769 C C   . VAL B 922  ? 0.3141 0.2753 0.3247 0.0807  -0.0435 -0.0395 920  VAL B C   
15770 O O   . VAL B 922  ? 0.3217 0.2871 0.3340 0.0821  -0.0408 -0.0410 920  VAL B O   
15771 C CB  . VAL B 922  ? 0.3498 0.2891 0.3458 0.0868  -0.0497 -0.0410 920  VAL B CB  
15772 C CG1 . VAL B 922  ? 0.3853 0.3173 0.3769 0.0933  -0.0537 -0.0423 920  VAL B CG1 
15773 C CG2 . VAL B 922  ? 0.3613 0.2918 0.3515 0.0800  -0.0505 -0.0385 920  VAL B CG2 
15774 N N   . GLY B 923  ? 0.3087 0.2719 0.3212 0.0751  -0.0428 -0.0372 921  GLY B N   
15775 C CA  . GLY B 923  ? 0.2822 0.2526 0.2991 0.0704  -0.0390 -0.0364 921  GLY B CA  
15776 C C   . GLY B 923  ? 0.2817 0.2626 0.3065 0.0686  -0.0379 -0.0353 921  GLY B C   
15777 O O   . GLY B 923  ? 0.3095 0.2938 0.3375 0.0716  -0.0398 -0.0356 921  GLY B O   
15778 N N   . THR B 924  ? 0.2424 0.2284 0.2705 0.0638  -0.0350 -0.0341 922  THR B N   
15779 C CA  . THR B 924  ? 0.2482 0.2435 0.2834 0.0616  -0.0340 -0.0331 922  THR B CA  
15780 C C   . THR B 924  ? 0.2706 0.2618 0.3033 0.0563  -0.0345 -0.0310 922  THR B C   
15781 O O   . THR B 924  ? 0.2632 0.2542 0.2951 0.0523  -0.0322 -0.0301 922  THR B O   
15782 C CB  . THR B 924  ? 0.2214 0.2267 0.2629 0.0608  -0.0302 -0.0335 922  THR B CB  
15783 O OG1 . THR B 924  ? 0.2429 0.2447 0.2809 0.0580  -0.0280 -0.0332 922  THR B OG1 
15784 C CG2 . THR B 924  ? 0.2732 0.2846 0.3183 0.0663  -0.0297 -0.0354 922  THR B CG2 
15785 N N   . PHE B 925  ? 0.2577 0.2459 0.2890 0.0565  -0.0374 -0.0303 923  PHE B N   
15786 C CA  . PHE B 925  ? 0.2330 0.2172 0.2613 0.0520  -0.0381 -0.0284 923  PHE B CA  
15787 C C   . PHE B 925  ? 0.2526 0.2432 0.2861 0.0509  -0.0386 -0.0277 923  PHE B C   
15788 O O   . PHE B 925  ? 0.2716 0.2664 0.3087 0.0542  -0.0403 -0.0285 923  PHE B O   
15789 C CB  . PHE B 925  ? 0.2632 0.2362 0.2834 0.0524  -0.0413 -0.0277 923  PHE B CB  
15790 C CG  . PHE B 925  ? 0.2725 0.2375 0.2864 0.0522  -0.0411 -0.0280 923  PHE B CG  
15791 C CD1 . PHE B 925  ? 0.2532 0.2157 0.2656 0.0568  -0.0419 -0.0298 923  PHE B CD1 
15792 C CD2 . PHE B 925  ? 0.2815 0.2415 0.2908 0.0475  -0.0403 -0.0265 923  PHE B CD2 
15793 C CE1 . PHE B 925  ? 0.2754 0.2299 0.2815 0.0565  -0.0420 -0.0302 923  PHE B CE1 
15794 C CE2 . PHE B 925  ? 0.2444 0.1971 0.2479 0.0469  -0.0404 -0.0267 923  PHE B CE2 
15795 C CZ  . PHE B 925  ? 0.2563 0.2058 0.2580 0.0513  -0.0413 -0.0286 923  PHE B CZ  
15796 N N   . VAL B 926  ? 0.2400 0.2312 0.2735 0.0463  -0.0374 -0.0264 924  VAL B N   
15797 C CA  . VAL B 926  ? 0.2407 0.2353 0.2769 0.0446  -0.0384 -0.0256 924  VAL B CA  
15798 C C   . VAL B 926  ? 0.2565 0.2434 0.2861 0.0416  -0.0397 -0.0242 924  VAL B C   
15799 O O   . VAL B 926  ? 0.2564 0.2401 0.2827 0.0387  -0.0379 -0.0234 924  VAL B O   
15800 C CB  . VAL B 926  ? 0.2235 0.2263 0.2658 0.0419  -0.0357 -0.0255 924  VAL B CB  
15801 C CG1 . VAL B 926  ? 0.2430 0.2480 0.2872 0.0400  -0.0371 -0.0248 924  VAL B CG1 
15802 C CG2 . VAL B 926  ? 0.2461 0.2571 0.2949 0.0446  -0.0343 -0.0267 924  VAL B CG2 
15803 N N   . PRO B 927  ? 0.2842 0.2683 0.3116 0.0422  -0.0427 -0.0236 925  PRO B N   
15804 C CA  . PRO B 927  ? 0.2695 0.2467 0.2904 0.0393  -0.0437 -0.0221 925  PRO B CA  
15805 C C   . PRO B 927  ? 0.2726 0.2535 0.2953 0.0353  -0.0417 -0.0214 925  PRO B C   
15806 O O   . PRO B 927  ? 0.2688 0.2568 0.2975 0.0351  -0.0409 -0.0220 925  PRO B O   
15807 C CB  . PRO B 927  ? 0.3394 0.3138 0.3583 0.0415  -0.0476 -0.0219 925  PRO B CB  
15808 C CG  . PRO B 927  ? 0.3051 0.2879 0.3316 0.0441  -0.0480 -0.0231 925  PRO B CG  
15809 C CD  . PRO B 927  ? 0.2996 0.2871 0.3304 0.0456  -0.0454 -0.0244 925  PRO B CD  
15810 N N   . PRO B 928  ? 0.2895 0.2658 0.3070 0.0321  -0.0410 -0.0201 926  PRO B N   
15811 C CA  . PRO B 928  ? 0.2998 0.2788 0.3180 0.0289  -0.0397 -0.0195 926  PRO B CA  
15812 C C   . PRO B 928  ? 0.3005 0.2824 0.3211 0.0295  -0.0417 -0.0198 926  PRO B C   
15813 O O   . PRO B 928  ? 0.3331 0.3118 0.3512 0.0312  -0.0448 -0.0196 926  PRO B O   
15814 C CB  . PRO B 928  ? 0.3398 0.3123 0.3508 0.0263  -0.0398 -0.0180 926  PRO B CB  
15815 C CG  . PRO B 928  ? 0.3695 0.3377 0.3777 0.0270  -0.0395 -0.0179 926  PRO B CG  
15816 C CD  . PRO B 928  ? 0.3423 0.3111 0.3532 0.0312  -0.0412 -0.0192 926  PRO B CD  
15817 N N   . THR B 929  ? 0.2768 0.2646 0.3023 0.0282  -0.0402 -0.0203 927  THR B N   
15818 C CA  . THR B 929  ? 0.2547 0.2463 0.2837 0.0286  -0.0421 -0.0208 927  THR B CA  
15819 C C   . THR B 929  ? 0.2780 0.2705 0.3063 0.0255  -0.0410 -0.0205 927  THR B C   
15820 O O   . THR B 929  ? 0.2933 0.2871 0.3224 0.0237  -0.0381 -0.0204 927  THR B O   
15821 C CB  . THR B 929  ? 0.2822 0.2810 0.3187 0.0304  -0.0416 -0.0219 927  THR B CB  
15822 O OG1 . THR B 929  ? 0.2557 0.2536 0.2924 0.0338  -0.0426 -0.0224 927  THR B OG1 
15823 C CG2 . THR B 929  ? 0.2658 0.2691 0.3063 0.0304  -0.0437 -0.0224 927  THR B CG2 
15824 N N   . ILE B 930  ? 0.3048 0.2964 0.3315 0.0252  -0.0434 -0.0205 928  ILE B N   
15825 C CA  . ILE B 930  ? 0.3017 0.2936 0.3272 0.0228  -0.0429 -0.0205 928  ILE B CA  
15826 C C   . ILE B 930  ? 0.3320 0.3282 0.3622 0.0230  -0.0449 -0.0214 928  ILE B C   
15827 O O   . ILE B 930  ? 0.3072 0.3034 0.3375 0.0247  -0.0480 -0.0216 928  ILE B O   
15828 C CB  . ILE B 930  ? 0.3048 0.2910 0.3228 0.0218  -0.0440 -0.0196 928  ILE B CB  
15829 C CG1 . ILE B 930  ? 0.3134 0.2956 0.3270 0.0211  -0.0421 -0.0185 928  ILE B CG1 
15830 C CG2 . ILE B 930  ? 0.3100 0.2967 0.3267 0.0197  -0.0434 -0.0199 928  ILE B CG2 
15831 C CD1 . ILE B 930  ? 0.4353 0.4124 0.4415 0.0199  -0.0430 -0.0173 928  ILE B CD1 
15832 N N   . ILE B 931  ? 0.3132 0.3131 0.3472 0.0212  -0.0434 -0.0219 929  ILE B N   
15833 C CA  . ILE B 931  ? 0.2830 0.2872 0.3216 0.0208  -0.0452 -0.0227 929  ILE B CA  
15834 C C   . ILE B 931  ? 0.3132 0.3154 0.3490 0.0183  -0.0451 -0.0230 929  ILE B C   
15835 O O   . ILE B 931  ? 0.2804 0.2818 0.3153 0.0169  -0.0424 -0.0229 929  ILE B O   
15836 C CB  . ILE B 931  ? 0.2745 0.2852 0.3206 0.0208  -0.0436 -0.0231 929  ILE B CB  
15837 C CG1 . ILE B 931  ? 0.2783 0.2907 0.3265 0.0236  -0.0434 -0.0231 929  ILE B CG1 
15838 C CG2 . ILE B 931  ? 0.2725 0.2880 0.3236 0.0197  -0.0456 -0.0238 929  ILE B CG2 
15839 C CD1 . ILE B 931  ? 0.3117 0.3311 0.3671 0.0239  -0.0417 -0.0234 929  ILE B CD1 
15840 N N   . GLU B 932  ? 0.2899 0.2913 0.3242 0.0181  -0.0481 -0.0235 930  GLU B N   
15841 C CA  . GLU B 932  ? 0.2802 0.2793 0.3114 0.0161  -0.0483 -0.0240 930  GLU B CA  
15842 C C   . GLU B 932  ? 0.3350 0.3382 0.3719 0.0144  -0.0486 -0.0248 930  GLU B C   
15843 O O   . GLU B 932  ? 0.3520 0.3595 0.3938 0.0147  -0.0507 -0.0251 930  GLU B O   
15844 C CB  . GLU B 932  ? 0.3565 0.3521 0.3825 0.0165  -0.0515 -0.0242 930  GLU B CB  
15845 C CG  . GLU B 932  ? 0.3709 0.3615 0.3900 0.0174  -0.0511 -0.0231 930  GLU B CG  
15846 C CD  . GLU B 932  ? 0.6103 0.5972 0.6234 0.0174  -0.0538 -0.0232 930  GLU B CD  
15847 O OE1 . GLU B 932  ? 0.5930 0.5813 0.6075 0.0170  -0.0565 -0.0242 930  GLU B OE1 
15848 O OE2 . GLU B 932  ? 0.5129 0.4957 0.5197 0.0177  -0.0534 -0.0223 930  GLU B OE2 
15849 N N   . LEU B 933  ? 0.2665 0.2686 0.3027 0.0126  -0.0464 -0.0251 931  LEU B N   
15850 C CA  . LEU B 933  ? 0.2947 0.2997 0.3355 0.0106  -0.0467 -0.0256 931  LEU B CA  
15851 C C   . LEU B 933  ? 0.3440 0.3449 0.3805 0.0091  -0.0484 -0.0266 931  LEU B C   
15852 O O   . LEU B 933  ? 0.4101 0.4062 0.4401 0.0096  -0.0481 -0.0268 931  LEU B O   
15853 C CB  . LEU B 933  ? 0.3214 0.3277 0.3648 0.0097  -0.0431 -0.0252 931  LEU B CB  
15854 C CG  . LEU B 933  ? 0.3542 0.3641 0.4014 0.0111  -0.0409 -0.0244 931  LEU B CG  
15855 C CD1 . LEU B 933  ? 0.3883 0.3988 0.4370 0.0099  -0.0376 -0.0240 931  LEU B CD1 
15856 C CD2 . LEU B 933  ? 0.4258 0.4418 0.4794 0.0117  -0.0425 -0.0244 931  LEU B CD2 
15857 N N   . GLU B 934  ? 0.4339 0.4370 0.4741 0.0072  -0.0503 -0.0272 932  GLU B N   
15858 C CA  . GLU B 934  ? 0.4189 0.4177 0.4551 0.0055  -0.0518 -0.0283 932  GLU B CA  
15859 C C   . GLU B 934  ? 0.5017 0.4978 0.5368 0.0042  -0.0492 -0.0285 932  GLU B C   
15860 O O   . GLU B 934  ? 0.4775 0.4684 0.5069 0.0040  -0.0493 -0.0294 932  GLU B O   
15861 C CB  . GLU B 934  ? 0.4385 0.4400 0.4786 0.0036  -0.0554 -0.0290 932  GLU B CB  
15862 N N   . LYS B 935  ? 0.4146 0.4143 0.4549 0.0036  -0.0468 -0.0276 933  LYS B N   
15863 C CA  . LYS B 935  ? 0.4486 0.4461 0.4882 0.0025  -0.0444 -0.0276 933  LYS B CA  
15864 C C   . LYS B 935  ? 0.4304 0.4316 0.4739 0.0032  -0.0411 -0.0263 933  LYS B C   
15865 O O   . LYS B 935  ? 0.3554 0.3619 0.4039 0.0037  -0.0411 -0.0257 933  LYS B O   
15866 C CB  . LYS B 935  ? 0.4629 0.4600 0.5050 -0.0005 -0.0461 -0.0280 933  LYS B CB  
15867 N N   . LEU B 936  ? 0.3801 0.3787 0.4212 0.0034  -0.0383 -0.0260 934  LEU B N   
15868 C CA  . LEU B 936  ? 0.4174 0.4193 0.4618 0.0040  -0.0352 -0.0249 934  LEU B CA  
15869 C C   . LEU B 936  ? 0.4149 0.4218 0.4660 0.0022  -0.0351 -0.0242 934  LEU B C   
15870 O O   . LEU B 936  ? 0.3844 0.3959 0.4395 0.0030  -0.0335 -0.0234 934  LEU B O   
15871 C CB  . LEU B 936  ? 0.4116 0.4099 0.4522 0.0044  -0.0326 -0.0247 934  LEU B CB  
15872 C CG  . LEU B 936  ? 0.4248 0.4243 0.4645 0.0062  -0.0298 -0.0239 934  LEU B CG  
15873 C CD1 . LEU B 936  ? 0.4413 0.4368 0.4756 0.0071  -0.0281 -0.0241 934  LEU B CD1 
15874 C CD2 . LEU B 936  ? 0.4788 0.4826 0.5238 0.0057  -0.0278 -0.0229 934  LEU B CD2 
15875 N N   . SER B 937  ? 0.4159 0.4222 0.4685 -0.0003 -0.0369 -0.0246 935  SER B N   
15876 C CA  . SER B 937  ? 0.3867 0.3983 0.4459 -0.0026 -0.0370 -0.0238 935  SER B CA  
15877 C C   . SER B 937  ? 0.3960 0.4144 0.4604 -0.0019 -0.0383 -0.0236 935  SER B C   
15878 O O   . SER B 937  ? 0.3935 0.4179 0.4640 -0.0032 -0.0376 -0.0228 935  SER B O   
15879 C CB  . SER B 937  ? 0.3896 0.3983 0.4484 -0.0058 -0.0392 -0.0242 935  SER B CB  
15880 O OG  . SER B 937  ? 0.4652 0.4718 0.5218 -0.0059 -0.0427 -0.0254 935  SER B OG  
15881 N N   . ASP B 938  ? 0.3890 0.4068 0.4513 0.0002  -0.0400 -0.0243 936  ASP B N   
15882 C CA  . ASP B 938  ? 0.3947 0.4187 0.4615 0.0017  -0.0411 -0.0241 936  ASP B CA  
15883 C C   . ASP B 938  ? 0.4356 0.4633 0.5051 0.0036  -0.0381 -0.0233 936  ASP B C   
15884 O O   . ASP B 938  ? 0.4188 0.4527 0.4932 0.0048  -0.0384 -0.0231 936  ASP B O   
15885 C CB  . ASP B 938  ? 0.3952 0.4164 0.4580 0.0039  -0.0435 -0.0249 936  ASP B CB  
15886 C CG  . ASP B 938  ? 0.5579 0.5759 0.6179 0.0023  -0.0469 -0.0258 936  ASP B CG  
15887 O OD1 . ASP B 938  ? 0.4803 0.4989 0.5425 -0.0006 -0.0479 -0.0260 936  ASP B OD1 
15888 O OD2 . ASP B 938  ? 0.5887 0.6033 0.6440 0.0039  -0.0487 -0.0264 936  ASP B OD2 
15889 N N   . LEU B 939  ? 0.3735 0.3978 0.4398 0.0042  -0.0352 -0.0229 937  LEU B N   
15890 C CA  . LEU B 939  ? 0.3849 0.4118 0.4526 0.0060  -0.0324 -0.0223 937  LEU B CA  
15891 C C   . LEU B 939  ? 0.3278 0.3575 0.3991 0.0040  -0.0300 -0.0214 937  LEU B C   
15892 O O   . LEU B 939  ? 0.4481 0.4737 0.5165 0.0025  -0.0289 -0.0212 937  LEU B O   
15893 C CB  . LEU B 939  ? 0.3706 0.3920 0.4322 0.0077  -0.0310 -0.0223 937  LEU B CB  
15894 C CG  . LEU B 939  ? 0.3657 0.3884 0.4275 0.0096  -0.0285 -0.0218 937  LEU B CG  
15895 C CD1 . LEU B 939  ? 0.4167 0.4435 0.4817 0.0118  -0.0296 -0.0220 937  LEU B CD1 
15896 C CD2 . LEU B 939  ? 0.3913 0.4086 0.4468 0.0106  -0.0276 -0.0218 937  LEU B CD2 
15897 N N   . GLN B 940  ? 0.3728 0.4094 0.4499 0.0042  -0.0292 -0.0210 938  GLN B N   
15898 C CA  . GLN B 940  ? 0.4515 0.4918 0.5325 0.0018  -0.0273 -0.0200 938  GLN B CA  
15899 C C   . GLN B 940  ? 0.4308 0.4732 0.5125 0.0032  -0.0239 -0.0193 938  GLN B C   
15900 O O   . GLN B 940  ? 0.4124 0.4571 0.4964 0.0013  -0.0220 -0.0183 938  GLN B O   
15901 C CB  . GLN B 940  ? 0.5217 0.5695 0.6094 0.0003  -0.0288 -0.0197 938  GLN B CB  
15902 N N   . ARG B 941  ? 0.3236 0.3650 0.4030 0.0063  -0.0232 -0.0198 939  ARG B N   
15903 C CA  . ARG B 941  ? 0.3711 0.4146 0.4511 0.0077  -0.0203 -0.0193 939  ARG B CA  
15904 C C   . ARG B 941  ? 0.3082 0.3469 0.3831 0.0102  -0.0199 -0.0198 939  ARG B C   
15905 O O   . ARG B 941  ? 0.3167 0.3521 0.3888 0.0114  -0.0220 -0.0205 939  ARG B O   
15906 C CB  . ARG B 941  ? 0.3847 0.4363 0.4705 0.0090  -0.0198 -0.0193 939  ARG B CB  
15907 C CG  . ARG B 941  ? 0.3498 0.4029 0.4364 0.0118  -0.0221 -0.0203 939  ARG B CG  
15908 C CD  . ARG B 941  ? 0.3823 0.4443 0.4751 0.0132  -0.0216 -0.0204 939  ARG B CD  
15909 N NE  . ARG B 941  ? 0.3983 0.4617 0.4917 0.0167  -0.0236 -0.0214 939  ARG B NE  
15910 C CZ  . ARG B 941  ? 0.4555 0.5178 0.5469 0.0202  -0.0229 -0.0221 939  ARG B CZ  
15911 N NH1 . ARG B 941  ? 0.3823 0.4420 0.4708 0.0206  -0.0202 -0.0219 939  ARG B NH1 
15912 N NH2 . ARG B 941  ? 0.3685 0.4319 0.4604 0.0234  -0.0250 -0.0230 939  ARG B NH2 
15913 N N   . GLU B 942  ? 0.3202 0.3581 0.3935 0.0108  -0.0173 -0.0194 940  GLU B N   
15914 C CA  . GLU B 942  ? 0.3172 0.3512 0.3860 0.0129  -0.0169 -0.0198 940  GLU B CA  
15915 C C   . GLU B 942  ? 0.3141 0.3505 0.3843 0.0156  -0.0179 -0.0205 940  GLU B C   
15916 O O   . GLU B 942  ? 0.3572 0.3990 0.4314 0.0166  -0.0168 -0.0205 940  GLU B O   
15917 C CB  . GLU B 942  ? 0.2780 0.3113 0.3452 0.0127  -0.0140 -0.0191 940  GLU B CB  
15918 C CG  . GLU B 942  ? 0.3137 0.3433 0.3764 0.0144  -0.0135 -0.0194 940  GLU B CG  
15919 C CD  . GLU B 942  ? 0.3459 0.3761 0.4080 0.0144  -0.0108 -0.0189 940  GLU B CD  
15920 O OE1 . GLU B 942  ? 0.3501 0.3849 0.4157 0.0144  -0.0094 -0.0186 940  GLU B OE1 
15921 O OE2 . GLU B 942  ? 0.3294 0.3560 0.3874 0.0143  -0.0102 -0.0187 940  GLU B OE2 
15922 N N   . VAL B 943  ? 0.2458 0.2783 0.3127 0.0170  -0.0199 -0.0210 941  VAL B N   
15923 C CA  . VAL B 943  ? 0.2472 0.2803 0.3142 0.0199  -0.0212 -0.0217 941  VAL B CA  
15924 C C   . VAL B 943  ? 0.2337 0.2619 0.2956 0.0211  -0.0203 -0.0217 941  VAL B C   
15925 O O   . VAL B 943  ? 0.2410 0.2638 0.2981 0.0205  -0.0211 -0.0215 941  VAL B O   
15926 C CB  . VAL B 943  ? 0.2537 0.2856 0.3202 0.0205  -0.0245 -0.0221 941  VAL B CB  
15927 C CG1 . VAL B 943  ? 0.2720 0.3041 0.3384 0.0239  -0.0260 -0.0228 941  VAL B CG1 
15928 C CG2 . VAL B 943  ? 0.3034 0.3402 0.3750 0.0188  -0.0255 -0.0221 941  VAL B CG2 
15929 N N   . PHE B 944  ? 0.2191 0.2493 0.2820 0.0227  -0.0187 -0.0220 942  PHE B N   
15930 C CA  . PHE B 944  ? 0.2159 0.2419 0.2743 0.0231  -0.0174 -0.0219 942  PHE B CA  
15931 C C   . PHE B 944  ? 0.2449 0.2669 0.2999 0.0257  -0.0194 -0.0226 942  PHE B C   
15932 O O   . PHE B 944  ? 0.2378 0.2603 0.2929 0.0281  -0.0191 -0.0233 942  PHE B O   
15933 C CB  . PHE B 944  ? 0.2459 0.2756 0.3064 0.0234  -0.0147 -0.0219 942  PHE B CB  
15934 C CG  . PHE B 944  ? 0.2495 0.2755 0.3059 0.0226  -0.0131 -0.0215 942  PHE B CG  
15935 C CD1 . PHE B 944  ? 0.2908 0.3153 0.3457 0.0201  -0.0121 -0.0206 942  PHE B CD1 
15936 C CD2 . PHE B 944  ? 0.2556 0.2798 0.3096 0.0245  -0.0128 -0.0221 942  PHE B CD2 
15937 C CE1 . PHE B 944  ? 0.2423 0.2642 0.2937 0.0194  -0.0107 -0.0202 942  PHE B CE1 
15938 C CE2 . PHE B 944  ? 0.2907 0.3117 0.3408 0.0235  -0.0115 -0.0218 942  PHE B CE2 
15939 C CZ  . PHE B 944  ? 0.2821 0.3025 0.3313 0.0209  -0.0104 -0.0207 942  PHE B CZ  
15940 N N   . GLY B 945  ? 0.2251 0.2426 0.2767 0.0252  -0.0215 -0.0223 943  GLY B N   
15941 C CA  . GLY B 945  ? 0.2130 0.2261 0.2612 0.0273  -0.0238 -0.0227 943  GLY B CA  
15942 C C   . GLY B 945  ? 0.2606 0.2683 0.3040 0.0258  -0.0254 -0.0220 943  GLY B C   
15943 O O   . GLY B 945  ? 0.2274 0.2349 0.2700 0.0233  -0.0246 -0.0213 943  GLY B O   
15944 N N   . PRO B 946  ? 0.2397 0.2428 0.2794 0.0274  -0.0279 -0.0220 944  PRO B N   
15945 C CA  . PRO B 946  ? 0.2277 0.2253 0.2619 0.0258  -0.0293 -0.0211 944  PRO B CA  
15946 C C   . PRO B 946  ? 0.2286 0.2276 0.2642 0.0256  -0.0313 -0.0212 944  PRO B C   
15947 O O   . PRO B 946  ? 0.2549 0.2508 0.2881 0.0268  -0.0340 -0.0211 944  PRO B O   
15948 C CB  . PRO B 946  ? 0.2349 0.2266 0.2644 0.0276  -0.0311 -0.0211 944  PRO B CB  
15949 C CG  . PRO B 946  ? 0.2624 0.2573 0.2960 0.0312  -0.0320 -0.0223 944  PRO B CG  
15950 C CD  . PRO B 946  ? 0.2078 0.2097 0.2473 0.0308  -0.0292 -0.0229 944  PRO B CD  
15951 N N   . VAL B 947  ? 0.2416 0.2450 0.2810 0.0240  -0.0301 -0.0213 945  VAL B N   
15952 C CA  . VAL B 947  ? 0.2072 0.2125 0.2485 0.0236  -0.0320 -0.0215 945  VAL B CA  
15953 C C   . VAL B 947  ? 0.2631 0.2672 0.3023 0.0208  -0.0310 -0.0210 945  VAL B C   
15954 O O   . VAL B 947  ? 0.2520 0.2588 0.2938 0.0194  -0.0289 -0.0211 945  VAL B O   
15955 C CB  . VAL B 947  ? 0.2453 0.2574 0.2936 0.0244  -0.0320 -0.0222 945  VAL B CB  
15956 C CG1 . VAL B 947  ? 0.2875 0.3012 0.3375 0.0237  -0.0344 -0.0224 945  VAL B CG1 
15957 C CG2 . VAL B 947  ? 0.2591 0.2731 0.3096 0.0276  -0.0326 -0.0228 945  VAL B CG2 
15958 N N   . LEU B 948  ? 0.2383 0.2381 0.2726 0.0202  -0.0326 -0.0206 946  LEU B N   
15959 C CA  . LEU B 948  ? 0.2265 0.2249 0.2581 0.0181  -0.0319 -0.0204 946  LEU B CA  
15960 C C   . LEU B 948  ? 0.2663 0.2660 0.2993 0.0177  -0.0340 -0.0210 946  LEU B C   
15961 O O   . LEU B 948  ? 0.2692 0.2680 0.3015 0.0189  -0.0367 -0.0212 946  LEU B O   
15962 C CB  . LEU B 948  ? 0.2318 0.2251 0.2566 0.0175  -0.0321 -0.0195 946  LEU B CB  
15963 C CG  . LEU B 948  ? 0.2064 0.1985 0.2279 0.0158  -0.0314 -0.0193 946  LEU B CG  
15964 C CD1 . LEU B 948  ? 0.2190 0.2133 0.2420 0.0147  -0.0283 -0.0193 946  LEU B CD1 
15965 C CD2 . LEU B 948  ? 0.2896 0.2773 0.3045 0.0153  -0.0320 -0.0183 946  LEU B CD2 
15966 N N   . HIS B 949  ? 0.2285 0.2300 0.2635 0.0162  -0.0328 -0.0214 947  HIS B N   
15967 C CA  . HIS B 949  ? 0.1901 0.1922 0.2260 0.0154  -0.0349 -0.0221 947  HIS B CA  
15968 C C   . HIS B 949  ? 0.2596 0.2576 0.2895 0.0144  -0.0349 -0.0220 947  HIS B C   
15969 O O   . HIS B 949  ? 0.2778 0.2744 0.3051 0.0139  -0.0326 -0.0216 947  HIS B O   
15970 C CB  . HIS B 949  ? 0.2382 0.2444 0.2795 0.0142  -0.0339 -0.0225 947  HIS B CB  
15971 C CG  . HIS B 949  ? 0.2491 0.2602 0.2963 0.0152  -0.0334 -0.0224 947  HIS B CG  
15972 N ND1 . HIS B 949  ? 0.2481 0.2604 0.2964 0.0157  -0.0308 -0.0220 947  HIS B ND1 
15973 C CD2 . HIS B 949  ? 0.2654 0.2806 0.3172 0.0160  -0.0353 -0.0228 947  HIS B CD2 
15974 C CE1 . HIS B 949  ? 0.2280 0.2448 0.2812 0.0169  -0.0309 -0.0221 947  HIS B CE1 
15975 N NE2 . HIS B 949  ? 0.2328 0.2519 0.2885 0.0172  -0.0336 -0.0226 947  HIS B NE2 
15976 N N   . VAL B 950  ? 0.2560 0.2524 0.2838 0.0144  -0.0376 -0.0225 948  VAL B N   
15977 C CA  . VAL B 950  ? 0.2876 0.2801 0.3092 0.0138  -0.0377 -0.0226 948  VAL B CA  
15978 C C   . VAL B 950  ? 0.3029 0.2953 0.3249 0.0128  -0.0392 -0.0238 948  VAL B C   
15979 O O   . VAL B 950  ? 0.2987 0.2926 0.3235 0.0127  -0.0418 -0.0243 948  VAL B O   
15980 C CB  . VAL B 950  ? 0.3045 0.2938 0.3209 0.0146  -0.0396 -0.0220 948  VAL B CB  
15981 C CG1 . VAL B 950  ? 0.3263 0.3123 0.3363 0.0140  -0.0397 -0.0222 948  VAL B CG1 
15982 C CG2 . VAL B 950  ? 0.2970 0.2853 0.3120 0.0153  -0.0382 -0.0208 948  VAL B CG2 
15983 N N   . ILE B 951  ? 0.2383 0.2288 0.2573 0.0120  -0.0377 -0.0242 949  ILE B N   
15984 C CA  . ILE B 951  ? 0.2466 0.2354 0.2644 0.0111  -0.0390 -0.0254 949  ILE B CA  
15985 C C   . ILE B 951  ? 0.2564 0.2414 0.2669 0.0116  -0.0389 -0.0257 949  ILE B C   
15986 O O   . ILE B 951  ? 0.2791 0.2636 0.2865 0.0121  -0.0366 -0.0250 949  ILE B O   
15987 C CB  . ILE B 951  ? 0.3533 0.3431 0.3742 0.0101  -0.0370 -0.0257 949  ILE B CB  
15988 C CG1 . ILE B 951  ? 0.4400 0.4339 0.4681 0.0093  -0.0374 -0.0255 949  ILE B CG1 
15989 C CG2 . ILE B 951  ? 0.4410 0.4273 0.4585 0.0094  -0.0379 -0.0270 949  ILE B CG2 
15990 C CD1 . ILE B 951  ? 0.5159 0.5105 0.5466 0.0082  -0.0354 -0.0255 949  ILE B CD1 
15991 N N   . ARG B 952  ? 0.2488 0.2315 0.2563 0.0113  -0.0415 -0.0268 950  ARG B N   
15992 C CA  . ARG B 952  ? 0.2705 0.2497 0.2708 0.0118  -0.0415 -0.0274 950  ARG B CA  
15993 C C   . ARG B 952  ? 0.2926 0.2697 0.2918 0.0114  -0.0412 -0.0289 950  ARG B C   
15994 O O   . ARG B 952  ? 0.3329 0.3103 0.3359 0.0103  -0.0428 -0.0297 950  ARG B O   
15995 C CB  . ARG B 952  ? 0.2886 0.2660 0.2852 0.0121  -0.0448 -0.0276 950  ARG B CB  
15996 C CG  . ARG B 952  ? 0.3323 0.3112 0.3304 0.0127  -0.0457 -0.0262 950  ARG B CG  
15997 C CD  . ARG B 952  ? 0.3952 0.3729 0.3917 0.0129  -0.0497 -0.0266 950  ARG B CD  
15998 N NE  . ARG B 952  ? 0.4912 0.4654 0.4797 0.0133  -0.0503 -0.0266 950  ARG B NE  
15999 C CZ  . ARG B 952  ? 0.4759 0.4486 0.4604 0.0139  -0.0510 -0.0252 950  ARG B CZ  
16000 N NH1 . ARG B 952  ? 0.4034 0.3774 0.3909 0.0145  -0.0513 -0.0239 950  ARG B NH1 
16001 N NH2 . ARG B 952  ? 0.4728 0.4426 0.4498 0.0141  -0.0514 -0.0252 950  ARG B NH2 
16002 N N   . TYR B 953  ? 0.2679 0.2430 0.2619 0.0123  -0.0392 -0.0293 951  TYR B N   
16003 C CA  . TYR B 953  ? 0.2870 0.2594 0.2793 0.0124  -0.0391 -0.0309 951  TYR B CA  
16004 C C   . TYR B 953  ? 0.2755 0.2447 0.2600 0.0137  -0.0391 -0.0320 951  TYR B C   
16005 O O   . TYR B 953  ? 0.2819 0.2520 0.2626 0.0146  -0.0377 -0.0312 951  TYR B O   
16006 C CB  . TYR B 953  ? 0.2923 0.2659 0.2876 0.0125  -0.0360 -0.0305 951  TYR B CB  
16007 C CG  . TYR B 953  ? 0.2586 0.2336 0.2509 0.0139  -0.0328 -0.0297 951  TYR B CG  
16008 C CD1 . TYR B 953  ? 0.2555 0.2338 0.2497 0.0138  -0.0312 -0.0280 951  TYR B CD1 
16009 C CD2 . TYR B 953  ? 0.2642 0.2371 0.2516 0.0154  -0.0315 -0.0308 951  TYR B CD2 
16010 C CE1 . TYR B 953  ? 0.2402 0.2200 0.2318 0.0147  -0.0285 -0.0272 951  TYR B CE1 
16011 C CE2 . TYR B 953  ? 0.2877 0.2628 0.2728 0.0167  -0.0285 -0.0300 951  TYR B CE2 
16012 C CZ  . TYR B 953  ? 0.2722 0.2509 0.2595 0.0161  -0.0270 -0.0281 951  TYR B CZ  
16013 O OH  . TYR B 953  ? 0.2596 0.2409 0.2446 0.0169  -0.0242 -0.0273 951  TYR B OH  
16014 N N   . ARG B 954  ? 0.3264 0.2917 0.3080 0.0138  -0.0407 -0.0339 952  ARG B N   
16015 C CA  . ARG B 954  ? 0.3732 0.3353 0.3472 0.0155  -0.0404 -0.0354 952  ARG B CA  
16016 C C   . ARG B 954  ? 0.3249 0.2872 0.2980 0.0171  -0.0370 -0.0356 952  ARG B C   
16017 O O   . ARG B 954  ? 0.2926 0.2550 0.2700 0.0166  -0.0361 -0.0355 952  ARG B O   
16018 C CB  . ARG B 954  ? 0.3864 0.3436 0.3576 0.0150  -0.0438 -0.0376 952  ARG B CB  
16019 N N   . ARG B 955  ? 0.3710 0.3338 0.3385 0.0190  -0.0350 -0.0357 953  ARG B N   
16020 C CA  . ARG B 955  ? 0.3978 0.3620 0.3648 0.0208  -0.0316 -0.0357 953  ARG B CA  
16021 C C   . ARG B 955  ? 0.3559 0.3157 0.3221 0.0217  -0.0322 -0.0376 953  ARG B C   
16022 O O   . ARG B 955  ? 0.3754 0.3362 0.3442 0.0224  -0.0301 -0.0373 953  ARG B O   
16023 C CB  . ARG B 955  ? 0.4492 0.4150 0.4099 0.0227  -0.0296 -0.0357 953  ARG B CB  
16024 C CG  . ARG B 955  ? 0.5435 0.5119 0.5036 0.0249  -0.0261 -0.0357 953  ARG B CG  
16025 C CD  . ARG B 955  ? 0.5237 0.4959 0.4906 0.0238  -0.0241 -0.0338 953  ARG B CD  
16026 N NE  . ARG B 955  ? 0.5177 0.4927 0.4841 0.0259  -0.0209 -0.0338 953  ARG B NE  
16027 C CZ  . ARG B 955  ? 0.5983 0.5707 0.5644 0.0278  -0.0206 -0.0352 953  ARG B CZ  
16028 N NH1 . ARG B 955  ? 0.5245 0.4911 0.4904 0.0275  -0.0231 -0.0368 953  ARG B NH1 
16029 N NH2 . ARG B 955  ? 0.5510 0.5267 0.5168 0.0299  -0.0177 -0.0350 953  ARG B NH2 
16030 N N   . ASP B 956  ? 0.3617 0.3163 0.3243 0.0216  -0.0352 -0.0396 954  ASP B N   
16031 C CA  . ASP B 956  ? 0.3861 0.3354 0.3476 0.0221  -0.0362 -0.0415 954  ASP B CA  
16032 C C   . ASP B 956  ? 0.3912 0.3407 0.3598 0.0198  -0.0366 -0.0405 954  ASP B C   
16033 O O   . ASP B 956  ? 0.4249 0.3705 0.3932 0.0202  -0.0367 -0.0413 954  ASP B O   
16034 C CB  . ASP B 956  ? 0.4277 0.3710 0.3840 0.0218  -0.0399 -0.0438 954  ASP B CB  
16035 C CG  . ASP B 956  ? 0.6602 0.6023 0.6083 0.0245  -0.0395 -0.0453 954  ASP B CG  
16036 O OD1 . ASP B 956  ? 0.5942 0.5391 0.5402 0.0270  -0.0361 -0.0450 954  ASP B OD1 
16037 O OD2 . ASP B 956  ? 0.7247 0.6634 0.6686 0.0241  -0.0425 -0.0467 954  ASP B OD2 
16038 N N   . ASP B 957  ? 0.3216 0.2753 0.2962 0.0175  -0.0370 -0.0386 955  ASP B N   
16039 C CA  . ASP B 957  ? 0.3427 0.2975 0.3243 0.0151  -0.0374 -0.0375 955  ASP B CA  
16040 C C   . ASP B 957  ? 0.2809 0.2405 0.2669 0.0155  -0.0340 -0.0356 955  ASP B C   
16041 O O   . ASP B 957  ? 0.3227 0.2845 0.3148 0.0136  -0.0339 -0.0344 955  ASP B O   
16042 C CB  . ASP B 957  ? 0.3485 0.3054 0.3342 0.0126  -0.0401 -0.0369 955  ASP B CB  
16043 C CG  . ASP B 957  ? 0.4783 0.4306 0.4612 0.0114  -0.0440 -0.0387 955  ASP B CG  
16044 O OD1 . ASP B 957  ? 0.4854 0.4322 0.4650 0.0116  -0.0449 -0.0403 955  ASP B OD1 
16045 O OD2 . ASP B 957  ? 0.4517 0.4056 0.4356 0.0103  -0.0463 -0.0385 955  ASP B OD2 
16046 N N   . LEU B 958  ? 0.2884 0.2500 0.2715 0.0178  -0.0312 -0.0353 956  LEU B N   
16047 C CA  . LEU B 958  ? 0.2749 0.2412 0.2620 0.0180  -0.0282 -0.0335 956  LEU B CA  
16048 C C   . LEU B 958  ? 0.2994 0.2646 0.2901 0.0175  -0.0275 -0.0332 956  LEU B C   
16049 O O   . LEU B 958  ? 0.2685 0.2373 0.2648 0.0162  -0.0264 -0.0316 956  LEU B O   
16050 C CB  . LEU B 958  ? 0.3007 0.2692 0.2837 0.0206  -0.0255 -0.0334 956  LEU B CB  
16051 C CG  . LEU B 958  ? 0.3013 0.2748 0.2878 0.0208  -0.0224 -0.0316 956  LEU B CG  
16052 C CD1 . LEU B 958  ? 0.2701 0.2473 0.2611 0.0187  -0.0225 -0.0298 956  LEU B CD1 
16053 C CD2 . LEU B 958  ? 0.2970 0.2730 0.2791 0.0232  -0.0200 -0.0317 956  LEU B CD2 
16054 N N   . ASP B 959  ? 0.2653 0.2254 0.2527 0.0187  -0.0281 -0.0347 957  ASP B N   
16055 C CA  . ASP B 959  ? 0.2966 0.2550 0.2868 0.0182  -0.0274 -0.0342 957  ASP B CA  
16056 C C   . ASP B 959  ? 0.2785 0.2372 0.2743 0.0147  -0.0293 -0.0333 957  ASP B C   
16057 O O   . ASP B 959  ? 0.2883 0.2495 0.2889 0.0136  -0.0279 -0.0318 957  ASP B O   
16058 C CB  . ASP B 959  ? 0.2950 0.2468 0.2797 0.0202  -0.0282 -0.0361 957  ASP B CB  
16059 C CG  . ASP B 959  ? 0.3173 0.2678 0.3036 0.0208  -0.0267 -0.0354 957  ASP B CG  
16060 O OD1 . ASP B 959  ? 0.3070 0.2626 0.2961 0.0216  -0.0240 -0.0339 957  ASP B OD1 
16061 O OD2 . ASP B 959  ? 0.3353 0.2794 0.3198 0.0204  -0.0284 -0.0363 957  ASP B OD2 
16062 N N   . ARG B 960  ? 0.2769 0.2334 0.2721 0.0130  -0.0323 -0.0342 958  ARG B N   
16063 C CA  . ARG B 960  ? 0.2838 0.2419 0.2848 0.0097  -0.0341 -0.0334 958  ARG B CA  
16064 C C   . ARG B 960  ? 0.2693 0.2345 0.2760 0.0090  -0.0327 -0.0315 958  ARG B C   
16065 O O   . ARG B 960  ? 0.2892 0.2572 0.3015 0.0070  -0.0325 -0.0303 958  ARG B O   
16066 C CB  . ARG B 960  ? 0.3331 0.2880 0.3321 0.0082  -0.0379 -0.0348 958  ARG B CB  
16067 N N   . LEU B 961  ? 0.2393 0.2072 0.2441 0.0106  -0.0317 -0.0313 959  LEU B N   
16068 C CA  . LEU B 961  ? 0.2449 0.2185 0.2542 0.0102  -0.0304 -0.0297 959  LEU B CA  
16069 C C   . LEU B 961  ? 0.2532 0.2294 0.2657 0.0105  -0.0275 -0.0283 959  LEU B C   
16070 O O   . LEU B 961  ? 0.2492 0.2292 0.2670 0.0092  -0.0269 -0.0271 959  LEU B O   
16071 C CB  . LEU B 961  ? 0.2343 0.2093 0.2402 0.0117  -0.0300 -0.0296 959  LEU B CB  
16072 C CG  . LEU B 961  ? 0.2627 0.2426 0.2721 0.0115  -0.0286 -0.0280 959  LEU B CG  
16073 C CD1 . LEU B 961  ? 0.2866 0.2686 0.3006 0.0100  -0.0308 -0.0276 959  LEU B CD1 
16074 C CD2 . LEU B 961  ? 0.2536 0.2340 0.2584 0.0129  -0.0278 -0.0277 959  LEU B CD2 
16075 N N   . VAL B 962  ? 0.2274 0.2019 0.2367 0.0123  -0.0256 -0.0286 960  VAL B N   
16076 C CA  . VAL B 962  ? 0.2256 0.2023 0.2375 0.0126  -0.0230 -0.0274 960  VAL B CA  
16077 C C   . VAL B 962  ? 0.2893 0.2652 0.3054 0.0105  -0.0237 -0.0268 960  VAL B C   
16078 O O   . VAL B 962  ? 0.2659 0.2456 0.2865 0.0096  -0.0222 -0.0254 960  VAL B O   
16079 C CB  . VAL B 962  ? 0.2416 0.2166 0.2492 0.0151  -0.0212 -0.0279 960  VAL B CB  
16080 C CG1 . VAL B 962  ? 0.2816 0.2584 0.2919 0.0154  -0.0190 -0.0266 960  VAL B CG1 
16081 C CG2 . VAL B 962  ? 0.2517 0.2292 0.2560 0.0168  -0.0201 -0.0280 960  VAL B CG2 
16082 N N   . ASP B 963  ? 0.2466 0.2178 0.2612 0.0094  -0.0260 -0.0279 961  ASP B N   
16083 C CA  . ASP B 963  ? 0.2686 0.2392 0.2872 0.0067  -0.0269 -0.0272 961  ASP B CA  
16084 C C   . ASP B 963  ? 0.2771 0.2532 0.3016 0.0047  -0.0274 -0.0261 961  ASP B C   
16085 O O   . ASP B 963  ? 0.2927 0.2719 0.3219 0.0032  -0.0263 -0.0248 961  ASP B O   
16086 C CB  . ASP B 963  ? 0.3055 0.2698 0.3211 0.0054  -0.0298 -0.0286 961  ASP B CB  
16087 C CG  . ASP B 963  ? 0.3591 0.3170 0.3691 0.0073  -0.0296 -0.0296 961  ASP B CG  
16088 O OD1 . ASP B 963  ? 0.3466 0.3053 0.3561 0.0092  -0.0270 -0.0289 961  ASP B OD1 
16089 O OD2 . ASP B 963  ? 0.3880 0.3400 0.3940 0.0070  -0.0321 -0.0312 961  ASP B OD2 
16090 N N   . ASP B 964  ? 0.2668 0.2444 0.2911 0.0048  -0.0290 -0.0268 962  ASP B N   
16091 C CA  . ASP B 964  ? 0.2791 0.2621 0.3089 0.0034  -0.0297 -0.0260 962  ASP B CA  
16092 C C   . ASP B 964  ? 0.2886 0.2765 0.3216 0.0043  -0.0269 -0.0246 962  ASP B C   
16093 O O   . ASP B 964  ? 0.2735 0.2656 0.3117 0.0031  -0.0266 -0.0236 962  ASP B O   
16094 C CB  . ASP B 964  ? 0.2808 0.2639 0.3087 0.0040  -0.0319 -0.0269 962  ASP B CB  
16095 C CG  . ASP B 964  ? 0.3691 0.3482 0.3950 0.0025  -0.0352 -0.0282 962  ASP B CG  
16096 O OD1 . ASP B 964  ? 0.3664 0.3431 0.3933 0.0006  -0.0360 -0.0283 962  ASP B OD1 
16097 O OD2 . ASP B 964  ? 0.4199 0.3980 0.4429 0.0032  -0.0371 -0.0292 962  ASP B OD2 
16098 N N   . VAL B 965  ? 0.2536 0.2411 0.2832 0.0065  -0.0250 -0.0245 963  VAL B N   
16099 C CA  . VAL B 965  ? 0.1970 0.1886 0.2291 0.0072  -0.0225 -0.0233 963  VAL B CA  
16100 C C   . VAL B 965  ? 0.2236 0.2162 0.2585 0.0064  -0.0208 -0.0223 963  VAL B C   
16101 O O   . VAL B 965  ? 0.2549 0.2516 0.2941 0.0058  -0.0197 -0.0213 963  VAL B O   
16102 C CB  . VAL B 965  ? 0.2433 0.2345 0.2711 0.0093  -0.0209 -0.0233 963  VAL B CB  
16103 C CG1 . VAL B 965  ? 0.2168 0.2117 0.2470 0.0097  -0.0185 -0.0221 963  VAL B CG1 
16104 C CG2 . VAL B 965  ? 0.2491 0.2398 0.2742 0.0099  -0.0225 -0.0239 963  VAL B CG2 
16105 N N   . ASN B 966  ? 0.2445 0.2330 0.2767 0.0065  -0.0206 -0.0226 964  ASN B N   
16106 C CA  . ASN B 966  ? 0.2417 0.2304 0.2760 0.0057  -0.0191 -0.0215 964  ASN B CA  
16107 C C   . ASN B 966  ? 0.2814 0.2717 0.3203 0.0029  -0.0202 -0.0209 964  ASN B C   
16108 O O   . ASN B 966  ? 0.2826 0.2753 0.3246 0.0019  -0.0187 -0.0196 964  ASN B O   
16109 C CB  . ASN B 966  ? 0.2534 0.2364 0.2832 0.0066  -0.0191 -0.0220 964  ASN B CB  
16110 C CG  . ASN B 966  ? 0.2595 0.2422 0.2853 0.0095  -0.0174 -0.0224 964  ASN B CG  
16111 O OD1 . ASN B 966  ? 0.2668 0.2537 0.2937 0.0103  -0.0157 -0.0217 964  ASN B OD1 
16112 N ND2 . ASN B 966  ? 0.2553 0.2332 0.2764 0.0110  -0.0179 -0.0235 964  ASN B ND2 
16113 N N   . ALA B 967  ? 0.2441 0.2336 0.2836 0.0014  -0.0229 -0.0217 965  ALA B N   
16114 C CA  . ALA B 967  ? 0.2831 0.2740 0.3269 -0.0016 -0.0242 -0.0211 965  ALA B CA  
16115 C C   . ALA B 967  ? 0.2783 0.2766 0.3282 -0.0023 -0.0232 -0.0200 965  ALA B C   
16116 O O   . ALA B 967  ? 0.3016 0.3025 0.3556 -0.0049 -0.0237 -0.0191 965  ALA B O   
16117 C CB  . ALA B 967  ? 0.2879 0.2764 0.3306 -0.0029 -0.0276 -0.0224 965  ALA B CB  
16118 N N   . THR B 968  ? 0.2435 0.2451 0.2938 -0.0001 -0.0220 -0.0200 966  THR B N   
16119 C CA  . THR B 968  ? 0.2229 0.2311 0.2784 -0.0002 -0.0208 -0.0191 966  THR B CA  
16120 C C   . THR B 968  ? 0.2338 0.2439 0.2914 -0.0010 -0.0184 -0.0177 966  THR B C   
16121 O O   . THR B 968  ? 0.2896 0.3052 0.3519 -0.0017 -0.0175 -0.0169 966  THR B O   
16122 C CB  . THR B 968  ? 0.2461 0.2561 0.3006 0.0023  -0.0200 -0.0195 966  THR B CB  
16123 O OG1 . THR B 968  ? 0.2452 0.2537 0.2969 0.0037  -0.0176 -0.0190 966  THR B OG1 
16124 C CG2 . THR B 968  ? 0.3170 0.3243 0.3683 0.0033  -0.0222 -0.0207 966  THR B CG2 
16125 N N   . GLY B 969  ? 0.2539 0.2597 0.3079 -0.0007 -0.0172 -0.0174 967  GLY B N   
16126 C CA  . GLY B 969  ? 0.2725 0.2795 0.3276 -0.0011 -0.0149 -0.0160 967  GLY B CA  
16127 C C   . GLY B 969  ? 0.2504 0.2596 0.3047 0.0012  -0.0126 -0.0158 967  GLY B C   
16128 O O   . GLY B 969  ? 0.2520 0.2615 0.3061 0.0012  -0.0107 -0.0147 967  GLY B O   
16129 N N   . TYR B 970  ? 0.2141 0.2246 0.2677 0.0030  -0.0128 -0.0166 968  TYR B N   
16130 C CA  . TYR B 970  ? 0.2041 0.2159 0.2564 0.0049  -0.0110 -0.0165 968  TYR B CA  
16131 C C   . TYR B 970  ? 0.2517 0.2595 0.2990 0.0063  -0.0106 -0.0168 968  TYR B C   
16132 O O   . TYR B 970  ? 0.2601 0.2639 0.3047 0.0062  -0.0119 -0.0175 968  TYR B O   
16133 C CB  . TYR B 970  ? 0.2240 0.2385 0.2774 0.0060  -0.0116 -0.0171 968  TYR B CB  
16134 C CG  . TYR B 970  ? 0.2567 0.2763 0.3150 0.0055  -0.0115 -0.0168 968  TYR B CG  
16135 C CD1 . TYR B 970  ? 0.2719 0.2947 0.3317 0.0061  -0.0094 -0.0161 968  TYR B CD1 
16136 C CD2 . TYR B 970  ? 0.2661 0.2875 0.3273 0.0046  -0.0134 -0.0172 968  TYR B CD2 
16137 C CE1 . TYR B 970  ? 0.3391 0.3670 0.4033 0.0061  -0.0091 -0.0160 968  TYR B CE1 
16138 C CE2 . TYR B 970  ? 0.3169 0.3440 0.3830 0.0045  -0.0132 -0.0169 968  TYR B CE2 
16139 C CZ  . TYR B 970  ? 0.3615 0.3919 0.4290 0.0053  -0.0109 -0.0163 968  TYR B CZ  
16140 O OH  . TYR B 970  ? 0.5004 0.5368 0.5726 0.0055  -0.0104 -0.0162 968  TYR B OH  
16141 N N   . GLY B 971  ? 0.2067 0.2156 0.2527 0.0076  -0.0089 -0.0165 969  GLY B N   
16142 C CA  . GLY B 971  ? 0.2123 0.2187 0.2541 0.0090  -0.0084 -0.0167 969  GLY B CA  
16143 C C   . GLY B 971  ? 0.2015 0.2104 0.2427 0.0100  -0.0068 -0.0163 969  GLY B C   
16144 O O   . GLY B 971  ? 0.2263 0.2352 0.2662 0.0106  -0.0054 -0.0157 969  GLY B O   
16145 N N   . LEU B 972  ? 0.1917 0.2023 0.2334 0.0102  -0.0072 -0.0166 970  LEU B N   
16146 C CA  . LEU B 972  ? 0.1705 0.1829 0.2115 0.0108  -0.0059 -0.0161 970  LEU B CA  
16147 C C   . LEU B 972  ? 0.1754 0.1865 0.2125 0.0114  -0.0062 -0.0164 970  LEU B C   
16148 O O   . LEU B 972  ? 0.2072 0.2182 0.2423 0.0120  -0.0052 -0.0161 970  LEU B O   
16149 C CB  . LEU B 972  ? 0.1858 0.2004 0.2292 0.0108  -0.0062 -0.0162 970  LEU B CB  
16150 C CG  . LEU B 972  ? 0.1987 0.2147 0.2413 0.0112  -0.0050 -0.0159 970  LEU B CG  
16151 C CD1 . LEU B 972  ? 0.2407 0.2579 0.2834 0.0112  -0.0031 -0.0151 970  LEU B CD1 
16152 C CD2 . LEU B 972  ? 0.2278 0.2456 0.2728 0.0116  -0.0053 -0.0162 970  LEU B CD2 
16153 N N   . THR B 973  ? 0.1890 0.1995 0.2252 0.0114  -0.0075 -0.0168 971  THR B N   
16154 C CA  . THR B 973  ? 0.1844 0.1939 0.2169 0.0117  -0.0077 -0.0169 971  THR B CA  
16155 C C   . THR B 973  ? 0.1660 0.1731 0.1967 0.0118  -0.0093 -0.0176 971  THR B C   
16156 O O   . THR B 973  ? 0.1913 0.1975 0.2238 0.0115  -0.0107 -0.0182 971  THR B O   
16157 C CB  . THR B 973  ? 0.1721 0.1819 0.2035 0.0114  -0.0080 -0.0166 971  THR B CB  
16158 O OG1 . THR B 973  ? 0.1921 0.2010 0.2249 0.0115  -0.0097 -0.0171 971  THR B OG1 
16159 C CG2 . THR B 973  ? 0.2185 0.2303 0.2511 0.0113  -0.0065 -0.0160 971  THR B CG2 
16160 N N   . PHE B 974  ? 0.1851 0.1915 0.2120 0.0122  -0.0090 -0.0177 972  PHE B N   
16161 C CA  . PHE B 974  ? 0.1740 0.1781 0.1983 0.0125  -0.0104 -0.0185 972  PHE B CA  
16162 C C   . PHE B 974  ? 0.1978 0.2023 0.2181 0.0127  -0.0099 -0.0181 972  PHE B C   
16163 O O   . PHE B 974  ? 0.1987 0.2055 0.2182 0.0129  -0.0082 -0.0175 972  PHE B O   
16164 C CB  . PHE B 974  ? 0.1647 0.1672 0.1885 0.0133  -0.0102 -0.0191 972  PHE B CB  
16165 C CG  . PHE B 974  ? 0.1842 0.1842 0.2044 0.0139  -0.0114 -0.0201 972  PHE B CG  
16166 C CD1 . PHE B 974  ? 0.1955 0.1932 0.2161 0.0133  -0.0136 -0.0209 972  PHE B CD1 
16167 C CD2 . PHE B 974  ? 0.2046 0.2048 0.2210 0.0151  -0.0104 -0.0203 972  PHE B CD2 
16168 C CE1 . PHE B 974  ? 0.2163 0.2114 0.2331 0.0138  -0.0149 -0.0219 972  PHE B CE1 
16169 C CE2 . PHE B 974  ? 0.2106 0.2085 0.2233 0.0158  -0.0115 -0.0214 972  PHE B CE2 
16170 C CZ  . PHE B 974  ? 0.2183 0.2133 0.2309 0.0152  -0.0138 -0.0222 972  PHE B CZ  
16171 N N   . GLY B 975  ? 0.1796 0.1824 0.1976 0.0125  -0.0115 -0.0184 973  GLY B N   
16172 C CA  . GLY B 975  ? 0.1802 0.1834 0.1940 0.0123  -0.0112 -0.0180 973  GLY B CA  
16173 C C   . GLY B 975  ? 0.1773 0.1787 0.1876 0.0132  -0.0119 -0.0189 973  GLY B C   
16174 O O   . GLY B 975  ? 0.1985 0.1973 0.2091 0.0134  -0.0136 -0.0199 973  GLY B O   
16175 N N   . LEU B 976  ? 0.1963 0.1992 0.2031 0.0136  -0.0107 -0.0186 974  LEU B N   
16176 C CA  . LEU B 976  ? 0.2078 0.2093 0.2104 0.0145  -0.0112 -0.0195 974  LEU B CA  
16177 C C   . LEU B 976  ? 0.2190 0.2224 0.2179 0.0138  -0.0105 -0.0184 974  LEU B C   
16178 O O   . LEU B 976  ? 0.2131 0.2202 0.2122 0.0133  -0.0087 -0.0174 974  LEU B O   
16179 C CB  . LEU B 976  ? 0.2148 0.2168 0.2168 0.0165  -0.0099 -0.0205 974  LEU B CB  
16180 C CG  . LEU B 976  ? 0.2319 0.2328 0.2289 0.0180  -0.0101 -0.0216 974  LEU B CG  
16181 C CD1 . LEU B 976  ? 0.2430 0.2393 0.2386 0.0179  -0.0127 -0.0229 974  LEU B CD1 
16182 C CD2 . LEU B 976  ? 0.2497 0.2515 0.2461 0.0203  -0.0086 -0.0225 974  LEU B CD2 
16183 N N   . HIS B 977  ? 0.2075 0.2086 0.2031 0.0134  -0.0122 -0.0186 975  HIS B N   
16184 C CA  . HIS B 977  ? 0.2233 0.2258 0.2146 0.0125  -0.0117 -0.0175 975  HIS B CA  
16185 C C   . HIS B 977  ? 0.2131 0.2150 0.1999 0.0141  -0.0116 -0.0186 975  HIS B C   
16186 O O   . HIS B 977  ? 0.2228 0.2211 0.2081 0.0146  -0.0137 -0.0198 975  HIS B O   
16187 C CB  . HIS B 977  ? 0.2130 0.2129 0.2033 0.0108  -0.0136 -0.0164 975  HIS B CB  
16188 C CG  . HIS B 977  ? 0.2454 0.2464 0.2375 0.0091  -0.0131 -0.0148 975  HIS B CG  
16189 N ND1 . HIS B 977  ? 0.3389 0.3410 0.3279 0.0072  -0.0125 -0.0131 975  HIS B ND1 
16190 C CD2 . HIS B 977  ? 0.3105 0.3117 0.3070 0.0088  -0.0130 -0.0147 975  HIS B CD2 
16191 C CE1 . HIS B 977  ? 0.2705 0.2729 0.2618 0.0059  -0.0124 -0.0121 975  HIS B CE1 
16192 N NE2 . HIS B 977  ? 0.3362 0.3381 0.3320 0.0070  -0.0126 -0.0131 975  HIS B NE2 
16193 N N   . THR B 978  ? 0.2096 0.2155 0.1946 0.0149  -0.0094 -0.0185 976  THR B N   
16194 C CA  . THR B 978  ? 0.2222 0.2283 0.2026 0.0168  -0.0089 -0.0197 976  THR B CA  
16195 C C   . THR B 978  ? 0.2552 0.2674 0.2340 0.0170  -0.0061 -0.0187 976  THR B C   
16196 O O   . THR B 978  ? 0.2430 0.2590 0.2251 0.0165  -0.0045 -0.0177 976  THR B O   
16197 C CB  . THR B 978  ? 0.2253 0.2288 0.2063 0.0193  -0.0093 -0.0219 976  THR B CB  
16198 O OG1 . THR B 978  ? 0.2415 0.2450 0.2174 0.0214  -0.0088 -0.0232 976  THR B OG1 
16199 C CG2 . THR B 978  ? 0.2493 0.2554 0.2341 0.0204  -0.0075 -0.0219 976  THR B CG2 
16200 N N   . ARG B 979  ? 0.2449 0.2585 0.2187 0.0178  -0.0055 -0.0189 977  ARG B N   
16201 C CA  . ARG B 979  ? 0.2330 0.2533 0.2053 0.0184  -0.0027 -0.0182 977  ARG B CA  
16202 C C   . ARG B 979  ? 0.2593 0.2809 0.2305 0.0223  -0.0014 -0.0203 977  ARG B C   
16203 O O   . ARG B 979  ? 0.2741 0.3019 0.2443 0.0235  0.0010  -0.0199 977  ARG B O   
16204 C CB  . ARG B 979  ? 0.3056 0.3277 0.2728 0.0168  -0.0023 -0.0168 977  ARG B CB  
16205 C CG  . ARG B 979  ? 0.3913 0.4122 0.3590 0.0130  -0.0035 -0.0144 977  ARG B CG  
16206 C CD  . ARG B 979  ? 0.4296 0.4510 0.3916 0.0114  -0.0035 -0.0132 977  ARG B CD  
16207 N NE  . ARG B 979  ? 0.4807 0.5014 0.4426 0.0076  -0.0043 -0.0105 977  ARG B NE  
16208 C CZ  . ARG B 979  ? 0.5251 0.5463 0.4821 0.0054  -0.0043 -0.0087 977  ARG B CZ  
16209 N NH1 . ARG B 979  ? 0.4269 0.4499 0.3789 0.0066  -0.0035 -0.0091 977  ARG B NH1 
16210 N NH2 . ARG B 979  ? 0.5045 0.5240 0.4614 0.0018  -0.0053 -0.0063 977  ARG B NH2 
16211 N N   . LEU B 980  ? 0.2278 0.2438 0.1993 0.0242  -0.0030 -0.0224 978  LEU B N   
16212 C CA  . LEU B 980  ? 0.2146 0.2299 0.1834 0.0281  -0.0025 -0.0247 978  LEU B CA  
16213 C C   . LEU B 980  ? 0.2291 0.2443 0.2019 0.0299  -0.0018 -0.0254 978  LEU B C   
16214 O O   . LEU B 980  ? 0.2379 0.2487 0.2141 0.0290  -0.0034 -0.0256 978  LEU B O   
16215 C CB  . LEU B 980  ? 0.2502 0.2584 0.2154 0.0290  -0.0050 -0.0267 978  LEU B CB  
16216 C CG  . LEU B 980  ? 0.2756 0.2829 0.2369 0.0270  -0.0062 -0.0259 978  LEU B CG  
16217 C CD1 . LEU B 980  ? 0.2724 0.2725 0.2306 0.0277  -0.0091 -0.0280 978  LEU B CD1 
16218 C CD2 . LEU B 980  ? 0.2782 0.2912 0.2349 0.0279  -0.0038 -0.0254 978  LEU B CD2 
16219 N N   . ASP B 981  ? 0.2333 0.2536 0.2054 0.0327  0.0005  -0.0257 979  ASP B N   
16220 C CA  . ASP B 981  ? 0.2328 0.2535 0.2084 0.0346  0.0012  -0.0261 979  ASP B CA  
16221 C C   . ASP B 981  ? 0.2456 0.2583 0.2205 0.0364  -0.0009 -0.0283 979  ASP B C   
16222 O O   . ASP B 981  ? 0.2437 0.2543 0.2224 0.0363  -0.0013 -0.0281 979  ASP B O   
16223 C CB  . ASP B 981  ? 0.2520 0.2796 0.2265 0.0378  0.0038  -0.0264 979  ASP B CB  
16224 C CG  . ASP B 981  ? 0.2945 0.3308 0.2715 0.0355  0.0059  -0.0239 979  ASP B CG  
16225 O OD1 . ASP B 981  ? 0.2920 0.3282 0.2722 0.0317  0.0052  -0.0220 979  ASP B OD1 
16226 O OD2 . ASP B 981  ? 0.3096 0.3529 0.2853 0.0377  0.0081  -0.0239 979  ASP B OD2 
16227 N N   . GLU B 982  ? 0.2529 0.2610 0.2228 0.0382  -0.0021 -0.0303 980  GLU B N   
16228 C CA  . GLU B 982  ? 0.2637 0.2637 0.2325 0.0396  -0.0043 -0.0323 980  GLU B CA  
16229 C C   . GLU B 982  ? 0.2578 0.2534 0.2306 0.0360  -0.0065 -0.0315 980  GLU B C   
16230 O O   . GLU B 982  ? 0.2593 0.2507 0.2344 0.0360  -0.0077 -0.0320 980  GLU B O   
16231 C CB  . GLU B 982  ? 0.2813 0.2769 0.2435 0.0417  -0.0055 -0.0347 980  GLU B CB  
16232 C CG  . GLU B 982  ? 0.3280 0.3144 0.2892 0.0421  -0.0084 -0.0366 980  GLU B CG  
16233 C CD  . GLU B 982  ? 0.4240 0.4049 0.3788 0.0433  -0.0103 -0.0389 980  GLU B CD  
16234 O OE1 . GLU B 982  ? 0.4542 0.4360 0.4075 0.0412  -0.0110 -0.0384 980  GLU B OE1 
16235 O OE2 . GLU B 982  ? 0.3691 0.3445 0.3202 0.0463  -0.0112 -0.0413 980  GLU B OE2 
16236 N N   . THR B 983  ? 0.2220 0.2189 0.1956 0.0329  -0.0072 -0.0302 981  THR B N   
16237 C CA  . THR B 983  ? 0.2268 0.2205 0.2044 0.0298  -0.0093 -0.0294 981  THR B CA  
16238 C C   . THR B 983  ? 0.2279 0.2245 0.2113 0.0286  -0.0081 -0.0278 981  THR B C   
16239 O O   . THR B 983  ? 0.2550 0.2484 0.2418 0.0275  -0.0093 -0.0278 981  THR B O   
16240 C CB  . THR B 983  ? 0.2517 0.2459 0.2282 0.0273  -0.0103 -0.0285 981  THR B CB  
16241 O OG1 . THR B 983  ? 0.2785 0.2694 0.2495 0.0286  -0.0117 -0.0302 981  THR B OG1 
16242 C CG2 . THR B 983  ? 0.2895 0.2813 0.2704 0.0246  -0.0123 -0.0277 981  THR B CG2 
16243 N N   . ILE B 984  ? 0.2140 0.2169 0.1984 0.0286  -0.0057 -0.0263 982  ILE B N   
16244 C CA  . ILE B 984  ? 0.2336 0.2395 0.2230 0.0277  -0.0046 -0.0249 982  ILE B CA  
16245 C C   . ILE B 984  ? 0.2157 0.2190 0.2063 0.0298  -0.0046 -0.0258 982  ILE B C   
16246 O O   . ILE B 984  ? 0.2369 0.2384 0.2313 0.0286  -0.0052 -0.0253 982  ILE B O   
16247 C CB  . ILE B 984  ? 0.2234 0.2367 0.2132 0.0274  -0.0022 -0.0233 982  ILE B CB  
16248 C CG1 . ILE B 984  ? 0.2687 0.2835 0.2577 0.0245  -0.0026 -0.0219 982  ILE B CG1 
16249 C CG2 . ILE B 984  ? 0.2735 0.2897 0.2679 0.0269  -0.0011 -0.0221 982  ILE B CG2 
16250 C CD1 . ILE B 984  ? 0.2655 0.2873 0.2537 0.0239  -0.0004 -0.0204 982  ILE B CD1 
16251 N N   . ALA B 985  ? 0.2379 0.2408 0.2249 0.0332  -0.0039 -0.0273 983  ALA B N   
16252 C CA  . ALA B 985  ? 0.2179 0.2176 0.2052 0.0356  -0.0040 -0.0282 983  ALA B CA  
16253 C C   . ALA B 985  ? 0.2590 0.2509 0.2466 0.0344  -0.0065 -0.0291 983  ALA B C   
16254 O O   . ALA B 985  ? 0.2475 0.2370 0.2379 0.0338  -0.0069 -0.0286 983  ALA B O   
16255 C CB  . ALA B 985  ? 0.2378 0.2380 0.2206 0.0399  -0.0030 -0.0298 983  ALA B CB  
16256 N N   . HIS B 986  ? 0.2396 0.2277 0.2241 0.0338  -0.0083 -0.0303 984  HIS B N   
16257 C CA  . HIS B 986  ? 0.2598 0.2409 0.2446 0.0324  -0.0110 -0.0312 984  HIS B CA  
16258 C C   . HIS B 986  ? 0.2550 0.2370 0.2455 0.0289  -0.0115 -0.0295 984  HIS B C   
16259 O O   . HIS B 986  ? 0.2571 0.2363 0.2502 0.0281  -0.0122 -0.0292 984  HIS B O   
16260 C CB  . HIS B 986  ? 0.2707 0.2484 0.2511 0.0321  -0.0129 -0.0327 984  HIS B CB  
16261 C CG  . HIS B 986  ? 0.3008 0.2721 0.2817 0.0302  -0.0159 -0.0336 984  HIS B CG  
16262 N ND1 . HIS B 986  ? 0.3607 0.3281 0.3376 0.0300  -0.0181 -0.0352 984  HIS B ND1 
16263 C CD2 . HIS B 986  ? 0.3234 0.2921 0.3083 0.0280  -0.0171 -0.0330 984  HIS B CD2 
16264 C CE1 . HIS B 986  ? 0.3915 0.3541 0.3701 0.0278  -0.0207 -0.0356 984  HIS B CE1 
16265 N NE2 . HIS B 986  ? 0.3394 0.3029 0.3230 0.0265  -0.0200 -0.0342 984  HIS B NE2 
16266 N N   . VAL B 987  ? 0.2243 0.2103 0.2168 0.0268  -0.0113 -0.0283 985  VAL B N   
16267 C CA  . VAL B 987  ? 0.2225 0.2091 0.2200 0.0239  -0.0120 -0.0270 985  VAL B CA  
16268 C C   . VAL B 987  ? 0.2336 0.2230 0.2351 0.0237  -0.0103 -0.0256 985  VAL B C   
16269 O O   . VAL B 987  ? 0.2569 0.2447 0.2619 0.0221  -0.0110 -0.0251 985  VAL B O   
16270 C CB  . VAL B 987  ? 0.2344 0.2241 0.2324 0.0221  -0.0122 -0.0261 985  VAL B CB  
16271 C CG1 . VAL B 987  ? 0.2622 0.2532 0.2654 0.0197  -0.0126 -0.0248 985  VAL B CG1 
16272 C CG2 . VAL B 987  ? 0.2475 0.2337 0.2418 0.0220  -0.0144 -0.0274 985  VAL B CG2 
16273 N N   . THR B 988  ? 0.2398 0.2337 0.2409 0.0251  -0.0081 -0.0249 986  THR B N   
16274 C CA  . THR B 988  ? 0.2498 0.2463 0.2545 0.0248  -0.0067 -0.0236 986  THR B CA  
16275 C C   . THR B 988  ? 0.2555 0.2482 0.2601 0.0263  -0.0070 -0.0241 986  THR B C   
16276 O O   . THR B 988  ? 0.3425 0.3356 0.3504 0.0254  -0.0065 -0.0230 986  THR B O   
16277 C CB  . THR B 988  ? 0.2871 0.2898 0.2918 0.0257  -0.0045 -0.0226 986  THR B CB  
16278 O OG1 . THR B 988  ? 0.2930 0.2963 0.2940 0.0287  -0.0036 -0.0236 986  THR B OG1 
16279 C CG2 . THR B 988  ? 0.3176 0.3235 0.3224 0.0236  -0.0044 -0.0217 986  THR B CG2 
16280 N N   . SER B 989  ? 0.2655 0.2540 0.2659 0.0286  -0.0077 -0.0258 987  SER B N   
16281 C CA  . SER B 989  ? 0.2900 0.2734 0.2896 0.0299  -0.0084 -0.0263 987  SER B CA  
16282 C C   . SER B 989  ? 0.3325 0.3108 0.3339 0.0272  -0.0105 -0.0263 987  SER B C   
16283 O O   . SER B 989  ? 0.3813 0.3562 0.3834 0.0272  -0.0108 -0.0259 987  SER B O   
16284 C CB  . SER B 989  ? 0.3224 0.3024 0.3164 0.0335  -0.0086 -0.0282 987  SER B CB  
16285 O OG  . SER B 989  ? 0.4124 0.3876 0.4033 0.0331  -0.0107 -0.0298 987  SER B OG  
16286 N N   . ARG B 990  ? 0.2603 0.2383 0.2627 0.0249  -0.0119 -0.0265 988  ARG B N   
16287 C CA  . ARG B 990  ? 0.2892 0.2630 0.2933 0.0223  -0.0141 -0.0266 988  ARG B CA  
16288 C C   . ARG B 990  ? 0.2836 0.2612 0.2933 0.0193  -0.0140 -0.0251 988  ARG B C   
16289 O O   . ARG B 990  ? 0.2807 0.2563 0.2930 0.0171  -0.0151 -0.0246 988  ARG B O   
16290 C CB  . ARG B 990  ? 0.2906 0.2605 0.2913 0.0221  -0.0164 -0.0284 988  ARG B CB  
16291 C CG  . ARG B 990  ? 0.4256 0.3919 0.4202 0.0253  -0.0166 -0.0303 988  ARG B CG  
16292 C CD  . ARG B 990  ? 0.3772 0.3362 0.3694 0.0260  -0.0179 -0.0311 988  ARG B CD  
16293 N NE  . ARG B 990  ? 0.3278 0.2812 0.3185 0.0241  -0.0210 -0.0324 988  ARG B NE  
16294 C CZ  . ARG B 990  ? 0.3049 0.2509 0.2932 0.0238  -0.0229 -0.0332 988  ARG B CZ  
16295 N NH1 . ARG B 990  ? 0.3815 0.3245 0.3687 0.0254  -0.0221 -0.0329 988  ARG B NH1 
16296 N NH2 . ARG B 990  ? 0.3168 0.2579 0.3034 0.0218  -0.0258 -0.0344 988  ARG B NH2 
16297 N N   . ILE B 991  ? 0.2381 0.2211 0.2495 0.0191  -0.0127 -0.0243 989  ILE B N   
16298 C CA  . ILE B 991  ? 0.2446 0.2310 0.2609 0.0167  -0.0126 -0.0230 989  ILE B CA  
16299 C C   . ILE B 991  ? 0.2466 0.2344 0.2658 0.0165  -0.0111 -0.0217 989  ILE B C   
16300 O O   . ILE B 991  ? 0.2772 0.2651 0.2947 0.0183  -0.0097 -0.0214 989  ILE B O   
16301 C CB  . ILE B 991  ? 0.2262 0.2170 0.2427 0.0167  -0.0117 -0.0225 989  ILE B CB  
16302 C CG1 . ILE B 991  ? 0.2728 0.2659 0.2935 0.0146  -0.0123 -0.0217 989  ILE B CG1 
16303 C CG2 . ILE B 991  ? 0.2872 0.2815 0.3030 0.0182  -0.0094 -0.0217 989  ILE B CG2 
16304 C CD1 . ILE B 991  ? 0.3050 0.2958 0.3258 0.0135  -0.0148 -0.0226 989  ILE B CD1 
16305 N N   . LYS B 992  ? 0.2201 0.2092 0.2434 0.0143  -0.0114 -0.0208 990  LYS B N   
16306 C CA  . LYS B 992  ? 0.2283 0.2187 0.2543 0.0137  -0.0100 -0.0195 990  LYS B CA  
16307 C C   . LYS B 992  ? 0.2349 0.2304 0.2645 0.0127  -0.0090 -0.0185 990  LYS B C   
16308 O O   . LYS B 992  ? 0.2862 0.2831 0.3194 0.0109  -0.0095 -0.0180 990  LYS B O   
16309 C CB  . LYS B 992  ? 0.2333 0.2200 0.2605 0.0119  -0.0113 -0.0193 990  LYS B CB  
16310 C CG  . LYS B 992  ? 0.2859 0.2665 0.3088 0.0131  -0.0125 -0.0203 990  LYS B CG  
16311 C CD  . LYS B 992  ? 0.4210 0.3975 0.4449 0.0107  -0.0141 -0.0200 990  LYS B CD  
16312 C CE  . LYS B 992  ? 0.4842 0.4623 0.5112 0.0093  -0.0129 -0.0182 990  LYS B CE  
16313 N NZ  . LYS B 992  ? 0.5738 0.5486 0.6022 0.0063  -0.0145 -0.0176 990  LYS B NZ  
16314 N N   . ALA B 993  ? 0.2483 0.2468 0.2770 0.0139  -0.0076 -0.0182 991  ALA B N   
16315 C CA  . ALA B 993  ? 0.2188 0.2214 0.2502 0.0132  -0.0068 -0.0174 991  ALA B CA  
16316 C C   . ALA B 993  ? 0.1894 0.1945 0.2200 0.0142  -0.0049 -0.0166 991  ALA B C   
16317 O O   . ALA B 993  ? 0.2252 0.2299 0.2531 0.0157  -0.0043 -0.0169 991  ALA B O   
16318 C CB  . ALA B 993  ? 0.2356 0.2390 0.2663 0.0129  -0.0077 -0.0180 991  ALA B CB  
16319 N N   . GLY B 994  ? 0.2031 0.2112 0.2362 0.0134  -0.0039 -0.0158 992  GLY B N   
16320 C CA  . GLY B 994  ? 0.2020 0.2126 0.2346 0.0141  -0.0023 -0.0150 992  GLY B CA  
16321 C C   . GLY B 994  ? 0.1769 0.1898 0.2078 0.0145  -0.0019 -0.0150 992  GLY B C   
16322 O O   . GLY B 994  ? 0.1826 0.1976 0.2124 0.0152  -0.0008 -0.0145 992  GLY B O   
16323 N N   . ASN B 995  ? 0.1868 0.1994 0.2172 0.0138  -0.0029 -0.0154 993  ASN B N   
16324 C CA  . ASN B 995  ? 0.1767 0.1911 0.2052 0.0135  -0.0027 -0.0152 993  ASN B CA  
16325 C C   . ASN B 995  ? 0.1657 0.1783 0.1918 0.0136  -0.0038 -0.0159 993  ASN B C   
16326 O O   . ASN B 995  ? 0.1900 0.2008 0.2166 0.0130  -0.0052 -0.0164 993  ASN B O   
16327 C CB  . ASN B 995  ? 0.1630 0.1784 0.1928 0.0124  -0.0028 -0.0148 993  ASN B CB  
16328 C CG  . ASN B 995  ? 0.1745 0.1923 0.2055 0.0123  -0.0014 -0.0141 993  ASN B CG  
16329 O OD1 . ASN B 995  ? 0.1748 0.1927 0.2080 0.0124  -0.0010 -0.0139 993  ASN B OD1 
16330 N ND2 . ASN B 995  ? 0.1834 0.2033 0.2128 0.0120  -0.0008 -0.0135 993  ASN B ND2 
16331 N N   . LEU B 996  ? 0.1872 0.2006 0.2106 0.0146  -0.0032 -0.0160 994  LEU B N   
16332 C CA  . LEU B 996  ? 0.1720 0.1841 0.1924 0.0149  -0.0040 -0.0166 994  LEU B CA  
16333 C C   . LEU B 996  ? 0.2050 0.2195 0.2235 0.0139  -0.0037 -0.0159 994  LEU B C   
16334 O O   . LEU B 996  ? 0.1886 0.2065 0.2074 0.0136  -0.0024 -0.0150 994  LEU B O   
16335 C CB  . LEU B 996  ? 0.1834 0.1949 0.2018 0.0169  -0.0036 -0.0174 994  LEU B CB  
16336 C CG  . LEU B 996  ? 0.1885 0.1972 0.2084 0.0177  -0.0039 -0.0179 994  LEU B CG  
16337 C CD1 . LEU B 996  ? 0.2456 0.2530 0.2624 0.0200  -0.0036 -0.0188 994  LEU B CD1 
16338 C CD2 . LEU B 996  ? 0.2093 0.2147 0.2308 0.0164  -0.0056 -0.0184 994  LEU B CD2 
16339 N N   . TYR B 997  ? 0.1812 0.1940 0.1976 0.0133  -0.0049 -0.0161 995  TYR B N   
16340 C CA  . TYR B 997  ? 0.2078 0.2222 0.2218 0.0120  -0.0048 -0.0152 995  TYR B CA  
16341 C C   . TYR B 997  ? 0.1997 0.2132 0.2101 0.0124  -0.0053 -0.0156 995  TYR B C   
16342 O O   . TYR B 997  ? 0.2212 0.2312 0.2309 0.0128  -0.0068 -0.0165 995  TYR B O   
16343 C CB  . TYR B 997  ? 0.1885 0.2009 0.2033 0.0104  -0.0060 -0.0147 995  TYR B CB  
16344 C CG  . TYR B 997  ? 0.1596 0.1730 0.1776 0.0100  -0.0054 -0.0144 995  TYR B CG  
16345 C CD1 . TYR B 997  ? 0.2321 0.2483 0.2499 0.0090  -0.0044 -0.0134 995  TYR B CD1 
16346 C CD2 . TYR B 997  ? 0.1707 0.1827 0.1918 0.0107  -0.0059 -0.0150 995  TYR B CD2 
16347 C CE1 . TYR B 997  ? 0.2094 0.2263 0.2295 0.0087  -0.0039 -0.0132 995  TYR B CE1 
16348 C CE2 . TYR B 997  ? 0.1869 0.2002 0.2106 0.0104  -0.0052 -0.0147 995  TYR B CE2 
16349 C CZ  . TYR B 997  ? 0.2000 0.2154 0.2229 0.0096  -0.0043 -0.0139 995  TYR B CZ  
16350 O OH  . TYR B 997  ? 0.2497 0.2662 0.2746 0.0093  -0.0036 -0.0136 995  TYR B OH  
16351 N N   . ILE B 998  ? 0.1822 0.1990 0.1901 0.0124  -0.0040 -0.0150 996  ILE B N   
16352 C CA  . ILE B 998  ? 0.1808 0.1975 0.1848 0.0131  -0.0041 -0.0155 996  ILE B CA  
16353 C C   . ILE B 998  ? 0.1780 0.1958 0.1794 0.0109  -0.0042 -0.0140 996  ILE B C   
16354 O O   . ILE B 998  ? 0.1958 0.2177 0.1973 0.0096  -0.0029 -0.0128 996  ILE B O   
16355 C CB  . ILE B 998  ? 0.2044 0.2245 0.2074 0.0153  -0.0023 -0.0160 996  ILE B CB  
16356 C CG1 . ILE B 998  ? 0.2820 0.3001 0.2872 0.0174  -0.0024 -0.0172 996  ILE B CG1 
16357 C CG2 . ILE B 998  ? 0.2248 0.2446 0.2234 0.0163  -0.0024 -0.0167 996  ILE B CG2 
16358 C CD1 . ILE B 998  ? 0.3332 0.3458 0.3384 0.0177  -0.0043 -0.0185 996  ILE B CD1 
16359 N N   . ASN B 999  ? 0.2109 0.2251 0.2097 0.0103  -0.0059 -0.0142 997  ASN B N   
16360 C CA  . ASN B 999  ? 0.2120 0.2264 0.2074 0.0082  -0.0063 -0.0127 997  ASN B CA  
16361 C C   . ASN B 999  ? 0.2121 0.2264 0.2088 0.0058  -0.0066 -0.0113 997  ASN B C   
16362 O O   . ASN B 999  ? 0.2148 0.2308 0.2092 0.0036  -0.0061 -0.0097 997  ASN B O   
16363 C CB  . ASN B 999  ? 0.2249 0.2440 0.2172 0.0083  -0.0044 -0.0122 997  ASN B CB  
16364 C CG  . ASN B 999  ? 0.2005 0.2186 0.1901 0.0107  -0.0046 -0.0138 997  ASN B CG  
16365 O OD1 . ASN B 999  ? 0.2267 0.2400 0.2153 0.0111  -0.0065 -0.0147 997  ASN B OD1 
16366 N ND2 . ASN B 999  ? 0.2268 0.2493 0.2150 0.0123  -0.0026 -0.0142 997  ASN B ND2 
16367 N N   . ARG B 1000 ? 0.1814 0.1932 0.1815 0.0061  -0.0075 -0.0118 998  ARG B N   
16368 C CA  . ARG B 1000 ? 0.1750 0.1855 0.1760 0.0043  -0.0082 -0.0108 998  ARG B CA  
16369 C C   . ARG B 1000 ? 0.2001 0.2068 0.2038 0.0053  -0.0098 -0.0119 998  ARG B C   
16370 O O   . ARG B 1000 ? 0.2374 0.2429 0.2424 0.0070  -0.0104 -0.0131 998  ARG B O   
16371 C CB  . ARG B 1000 ? 0.2156 0.2303 0.2187 0.0035  -0.0064 -0.0102 998  ARG B CB  
16372 C CG  . ARG B 1000 ? 0.1838 0.2010 0.1902 0.0057  -0.0051 -0.0113 998  ARG B CG  
16373 C CD  . ARG B 1000 ? 0.1882 0.2077 0.1973 0.0050  -0.0042 -0.0108 998  ARG B CD  
16374 N NE  . ARG B 1000 ? 0.1935 0.2093 0.2040 0.0046  -0.0055 -0.0110 998  ARG B NE  
16375 C CZ  . ARG B 1000 ? 0.1990 0.2156 0.2114 0.0040  -0.0051 -0.0108 998  ARG B CZ  
16376 N NH1 . ARG B 1000 ? 0.1999 0.2209 0.2134 0.0038  -0.0036 -0.0103 998  ARG B NH1 
16377 N NH2 . ARG B 1000 ? 0.2182 0.2314 0.2315 0.0039  -0.0063 -0.0111 998  ARG B NH2 
16378 N N   . ASN B 1001 ? 0.1966 0.2014 0.2011 0.0043  -0.0105 -0.0114 999  ASN B N   
16379 C CA  . ASN B 1001 ? 0.1960 0.1983 0.2035 0.0055  -0.0118 -0.0124 999  ASN B CA  
16380 C C   . ASN B 1001 ? 0.1792 0.1843 0.1909 0.0067  -0.0103 -0.0132 999  ASN B C   
16381 O O   . ASN B 1001 ? 0.2113 0.2197 0.2234 0.0067  -0.0085 -0.0129 999  ASN B O   
16382 C CB  . ASN B 1001 ? 0.1910 0.1901 0.1975 0.0045  -0.0131 -0.0118 999  ASN B CB  
16383 C CG  . ASN B 1001 ? 0.2349 0.2357 0.2421 0.0034  -0.0119 -0.0112 999  ASN B CG  
16384 O OD1 . ASN B 1001 ? 0.2387 0.2426 0.2491 0.0041  -0.0104 -0.0117 999  ASN B OD1 
16385 N ND2 . ASN B 1001 ? 0.3029 0.3012 0.3070 0.0014  -0.0128 -0.0101 999  ASN B ND2 
16386 N N   . ILE B 1002 ? 0.1873 0.1911 0.2021 0.0079  -0.0111 -0.0141 1000 ILE B N   
16387 C CA  . ILE B 1002 ? 0.1643 0.1704 0.1828 0.0089  -0.0099 -0.0147 1000 ILE B CA  
16388 C C   . ILE B 1002 ? 0.1929 0.1994 0.2139 0.0089  -0.0095 -0.0147 1000 ILE B C   
16389 O O   . ILE B 1002 ? 0.2010 0.2090 0.2253 0.0097  -0.0088 -0.0152 1000 ILE B O   
16390 C CB  . ILE B 1002 ? 0.1895 0.1947 0.2099 0.0101  -0.0108 -0.0158 1000 ILE B CB  
16391 C CG1 . ILE B 1002 ? 0.1744 0.1777 0.1965 0.0105  -0.0127 -0.0163 1000 ILE B CG1 
16392 C CG2 . ILE B 1002 ? 0.2060 0.2104 0.2234 0.0102  -0.0112 -0.0160 1000 ILE B CG2 
16393 C CD1 . ILE B 1002 ? 0.1817 0.1850 0.2065 0.0112  -0.0135 -0.0172 1000 ILE B CD1 
16394 N N   . ILE B 1003 ? 0.1938 0.1989 0.2129 0.0079  -0.0100 -0.0141 1001 ILE B N   
16395 C CA  . ILE B 1003 ? 0.1894 0.1943 0.2101 0.0082  -0.0099 -0.0143 1001 ILE B CA  
16396 C C   . ILE B 1003 ? 0.2302 0.2362 0.2492 0.0067  -0.0089 -0.0135 1001 ILE B C   
16397 O O   . ILE B 1003 ? 0.2337 0.2410 0.2505 0.0054  -0.0084 -0.0126 1001 ILE B O   
16398 C CB  . ILE B 1003 ? 0.2144 0.2157 0.2343 0.0087  -0.0119 -0.0147 1001 ILE B CB  
16399 C CG1 . ILE B 1003 ? 0.2455 0.2434 0.2607 0.0073  -0.0132 -0.0138 1001 ILE B CG1 
16400 C CG2 . ILE B 1003 ? 0.2036 0.2048 0.2259 0.0102  -0.0130 -0.0156 1001 ILE B CG2 
16401 C CD1 . ILE B 1003 ? 0.2772 0.2707 0.2910 0.0080  -0.0153 -0.0142 1001 ILE B CD1 
16402 N N   . GLY B 1004 ? 0.2555 0.2615 0.2757 0.0069  -0.0086 -0.0138 1002 GLY B N   
16403 C CA  . GLY B 1004 ? 0.2112 0.2179 0.2298 0.0054  -0.0080 -0.0131 1002 GLY B CA  
16404 C C   . GLY B 1004 ? 0.2290 0.2402 0.2487 0.0050  -0.0062 -0.0126 1002 GLY B C   
16405 O O   . GLY B 1004 ? 0.2432 0.2560 0.2611 0.0033  -0.0058 -0.0116 1002 GLY B O   
16406 N N   . ALA B 1005 ? 0.2260 0.2394 0.2489 0.0066  -0.0051 -0.0131 1003 ALA B N   
16407 C CA  . ALA B 1005 ? 0.2128 0.2300 0.2367 0.0067  -0.0035 -0.0126 1003 ALA B CA  
16408 C C   . ALA B 1005 ? 0.2516 0.2703 0.2747 0.0055  -0.0030 -0.0121 1003 ALA B C   
16409 O O   . ALA B 1005 ? 0.2829 0.2998 0.3060 0.0055  -0.0035 -0.0125 1003 ALA B O   
16410 C CB  . ALA B 1005 ? 0.2249 0.2431 0.2519 0.0083  -0.0026 -0.0131 1003 ALA B CB  
16411 N N   . VAL B 1006 ? 0.1819 0.2040 0.2044 0.0047  -0.0022 -0.0113 1004 VAL B N   
16412 C CA  . VAL B 1006 ? 0.2023 0.2263 0.2239 0.0031  -0.0020 -0.0106 1004 VAL B CA  
16413 C C   . VAL B 1006 ? 0.2045 0.2321 0.2282 0.0043  -0.0006 -0.0105 1004 VAL B C   
16414 O O   . VAL B 1006 ? 0.1903 0.2206 0.2150 0.0055  0.0003  -0.0103 1004 VAL B O   
16415 C CB  . VAL B 1006 ? 0.2362 0.2623 0.2555 0.0010  -0.0022 -0.0095 1004 VAL B CB  
16416 C CG1 . VAL B 1006 ? 0.2280 0.2571 0.2468 -0.0008 -0.0020 -0.0088 1004 VAL B CG1 
16417 C CG2 . VAL B 1006 ? 0.2411 0.2628 0.2577 -0.0004 -0.0037 -0.0094 1004 VAL B CG2 
16418 N N   . VAL B 1007 ? 0.1827 0.2100 0.2064 0.0040  -0.0007 -0.0107 1005 VAL B N   
16419 C CA  . VAL B 1007 ? 0.1810 0.2114 0.2063 0.0050  0.0005  -0.0105 1005 VAL B CA  
16420 C C   . VAL B 1007 ? 0.1812 0.2163 0.2066 0.0049  0.0012  -0.0095 1005 VAL B C   
16421 O O   . VAL B 1007 ? 0.1866 0.2237 0.2106 0.0030  0.0008  -0.0089 1005 VAL B O   
16422 C CB  . VAL B 1007 ? 0.1816 0.2111 0.2058 0.0042  0.0001  -0.0107 1005 VAL B CB  
16423 C CG1 . VAL B 1007 ? 0.1829 0.2158 0.2083 0.0051  0.0011  -0.0103 1005 VAL B CG1 
16424 C CG2 . VAL B 1007 ? 0.2199 0.2454 0.2442 0.0050  -0.0004 -0.0118 1005 VAL B CG2 
16425 N N   . GLY B 1008 ? 0.1750 0.2120 0.2021 0.0069  0.0022  -0.0094 1006 GLY B N   
16426 C CA  . GLY B 1008 ? 0.1725 0.2142 0.1998 0.0075  0.0029  -0.0087 1006 GLY B CA  
16427 C C   . GLY B 1008 ? 0.1597 0.2032 0.1864 0.0075  0.0030  -0.0085 1006 GLY B C   
16428 O O   . GLY B 1008 ? 0.2376 0.2857 0.2646 0.0083  0.0037  -0.0079 1006 GLY B O   
16429 N N   . VAL B 1009 ? 0.1742 0.2146 0.1999 0.0066  0.0024  -0.0089 1007 VAL B N   
16430 C CA  . VAL B 1009 ? 0.1785 0.2201 0.2030 0.0066  0.0025  -0.0087 1007 VAL B CA  
16431 C C   . VAL B 1009 ? 0.1646 0.2025 0.1892 0.0084  0.0024  -0.0096 1007 VAL B C   
16432 O O   . VAL B 1009 ? 0.1856 0.2250 0.2100 0.0101  0.0030  -0.0098 1007 VAL B O   
16433 C CB  . VAL B 1009 ? 0.2047 0.2455 0.2271 0.0037  0.0015  -0.0082 1007 VAL B CB  
16434 C CG1 . VAL B 1009 ? 0.1945 0.2374 0.2155 0.0036  0.0019  -0.0079 1007 VAL B CG1 
16435 C CG2 . VAL B 1009 ? 0.2208 0.2649 0.2429 0.0014  0.0014  -0.0073 1007 VAL B CG2 
16436 N N   . GLN B 1010 ? 0.1667 0.2001 0.1918 0.0082  0.0015  -0.0103 1008 GLN B N   
16437 C CA  . GLN B 1010 ? 0.1692 0.1994 0.1952 0.0098  0.0013  -0.0111 1008 GLN B CA  
16438 C C   . GLN B 1010 ? 0.1788 0.2076 0.2068 0.0103  0.0015  -0.0113 1008 GLN B C   
16439 O O   . GLN B 1010 ? 0.1988 0.2249 0.2273 0.0097  0.0008  -0.0118 1008 GLN B O   
16440 C CB  . GLN B 1010 ? 0.2010 0.2276 0.2259 0.0092  0.0001  -0.0117 1008 GLN B CB  
16441 C CG  . GLN B 1010 ? 0.1870 0.2147 0.2094 0.0084  -0.0001 -0.0113 1008 GLN B CG  
16442 C CD  . GLN B 1010 ? 0.2037 0.2313 0.2243 0.0060  -0.0007 -0.0106 1008 GLN B CD  
16443 O OE1 . GLN B 1010 ? 0.2207 0.2456 0.2415 0.0051  -0.0016 -0.0107 1008 GLN B OE1 
16444 N NE2 . GLN B 1010 ? 0.2015 0.2322 0.2203 0.0048  -0.0003 -0.0097 1008 GLN B NE2 
16445 N N   . PRO B 1011 ? 0.1908 0.2215 0.2198 0.0114  0.0024  -0.0110 1009 PRO B N   
16446 C CA  . PRO B 1011 ? 0.1990 0.2283 0.2298 0.0120  0.0027  -0.0111 1009 PRO B CA  
16447 C C   . PRO B 1011 ? 0.1790 0.2049 0.2107 0.0122  0.0020  -0.0118 1009 PRO B C   
16448 O O   . PRO B 1011 ? 0.1716 0.1960 0.2029 0.0128  0.0016  -0.0122 1009 PRO B O   
16449 C CB  . PRO B 1011 ? 0.1768 0.2076 0.2077 0.0136  0.0036  -0.0106 1009 PRO B CB  
16450 C CG  . PRO B 1011 ? 0.2026 0.2373 0.2324 0.0137  0.0039  -0.0101 1009 PRO B CG  
16451 C CD  . PRO B 1011 ? 0.1993 0.2334 0.2278 0.0127  0.0032  -0.0105 1009 PRO B CD  
16452 N N   . PHE B 1012 ? 0.1609 0.1858 0.1940 0.0117  0.0019  -0.0120 1010 PHE B N   
16453 C CA  . PHE B 1012 ? 0.1782 0.2006 0.2124 0.0116  0.0010  -0.0128 1010 PHE B CA  
16454 C C   . PHE B 1012 ? 0.1830 0.2050 0.2195 0.0119  0.0014  -0.0127 1010 PHE B C   
16455 O O   . PHE B 1012 ? 0.1795 0.2029 0.2170 0.0119  0.0022  -0.0123 1010 PHE B O   
16456 C CB  . PHE B 1012 ? 0.1976 0.2193 0.2314 0.0108  0.0002  -0.0132 1010 PHE B CB  
16457 C CG  . PHE B 1012 ? 0.1713 0.1909 0.2061 0.0110  -0.0010 -0.0139 1010 PHE B CG  
16458 C CD1 . PHE B 1012 ? 0.2070 0.2250 0.2405 0.0108  -0.0021 -0.0142 1010 PHE B CD1 
16459 C CD2 . PHE B 1012 ? 0.1978 0.2177 0.2351 0.0114  -0.0009 -0.0143 1010 PHE B CD2 
16460 C CE1 . PHE B 1012 ? 0.1840 0.2002 0.2184 0.0110  -0.0034 -0.0149 1010 PHE B CE1 
16461 C CE2 . PHE B 1012 ? 0.2449 0.2637 0.2836 0.0116  -0.0021 -0.0150 1010 PHE B CE2 
16462 C CZ  . PHE B 1012 ? 0.2093 0.2261 0.2466 0.0115  -0.0034 -0.0153 1010 PHE B CZ  
16463 N N   . GLY B 1013 ? 0.1763 0.1965 0.2136 0.0121  0.0007  -0.0131 1011 GLY B N   
16464 C CA  . GLY B 1013 ? 0.1769 0.1968 0.2167 0.0119  0.0008  -0.0130 1011 GLY B CA  
16465 C C   . GLY B 1013 ? 0.1986 0.2161 0.2381 0.0120  0.0000  -0.0132 1011 GLY B C   
16466 O O   . GLY B 1013 ? 0.1917 0.2081 0.2290 0.0127  -0.0001 -0.0133 1011 GLY B O   
16467 N N   . GLY B 1014 ? 0.2177 0.2345 0.2595 0.0112  -0.0005 -0.0133 1012 GLY B N   
16468 C CA  . GLY B 1014 ? 0.2225 0.2365 0.2639 0.0110  -0.0016 -0.0136 1012 GLY B CA  
16469 C C   . GLY B 1014 ? 0.2666 0.2797 0.3095 0.0102  -0.0013 -0.0128 1012 GLY B C   
16470 O O   . GLY B 1014 ? 0.3208 0.3353 0.3644 0.0100  0.0000  -0.0118 1012 GLY B O   
16471 N N   . ARG B 1015 ? 0.2393 0.2496 0.2823 0.0094  -0.0027 -0.0132 1013 ARG B N   
16472 C CA  . ARG B 1015 ? 0.2868 0.2949 0.3303 0.0083  -0.0029 -0.0125 1013 ARG B CA  
16473 C C   . ARG B 1015 ? 0.2551 0.2638 0.3017 0.0064  -0.0041 -0.0127 1013 ARG B C   
16474 O O   . ARG B 1015 ? 0.2167 0.2275 0.2649 0.0064  -0.0048 -0.0135 1013 ARG B O   
16475 C CB  . ARG B 1015 ? 0.2696 0.2729 0.3095 0.0093  -0.0036 -0.0129 1013 ARG B CB  
16476 C CG  . ARG B 1015 ? 0.2944 0.2957 0.3325 0.0099  -0.0052 -0.0144 1013 ARG B CG  
16477 C CD  . ARG B 1015 ? 0.3965 0.3923 0.4319 0.0101  -0.0066 -0.0150 1013 ARG B CD  
16478 N NE  . ARG B 1015 ? 0.3872 0.3814 0.4247 0.0076  -0.0079 -0.0147 1013 ARG B NE  
16479 C CZ  . ARG B 1015 ? 0.3538 0.3484 0.3930 0.0062  -0.0095 -0.0154 1013 ARG B CZ  
16480 N NH1 . ARG B 1015 ? 0.3321 0.3283 0.3709 0.0072  -0.0100 -0.0165 1013 ARG B NH1 
16481 N NH2 . ARG B 1015 ? 0.4155 0.4091 0.4568 0.0037  -0.0107 -0.0150 1013 ARG B NH2 
16482 N N   . GLY B 1016 ? 0.2379 0.2446 0.2852 0.0047  -0.0046 -0.0119 1014 GLY B N   
16483 C CA  . GLY B 1016 ? 0.2316 0.2395 0.2822 0.0025  -0.0059 -0.0120 1014 GLY B CA  
16484 C C   . GLY B 1016 ? 0.2287 0.2428 0.2835 0.0020  -0.0048 -0.0116 1014 GLY B C   
16485 O O   . GLY B 1016 ? 0.2555 0.2722 0.3110 0.0023  -0.0029 -0.0106 1014 GLY B O   
16486 N N   . LEU B 1017 ? 0.2325 0.2489 0.2898 0.0016  -0.0061 -0.0124 1015 LEU B N   
16487 C CA  . LEU B 1017 ? 0.2294 0.2518 0.2907 0.0017  -0.0053 -0.0124 1015 LEU B CA  
16488 C C   . LEU B 1017 ? 0.2235 0.2472 0.2833 0.0041  -0.0042 -0.0129 1015 LEU B C   
16489 O O   . LEU B 1017 ? 0.2234 0.2514 0.2857 0.0048  -0.0034 -0.0130 1015 LEU B O   
16490 C CB  . LEU B 1017 ? 0.2247 0.2490 0.2888 0.0011  -0.0074 -0.0133 1015 LEU B CB  
16491 C CG  . LEU B 1017 ? 0.2684 0.2923 0.3346 -0.0018 -0.0088 -0.0128 1015 LEU B CG  
16492 C CD1 . LEU B 1017 ? 0.2738 0.2997 0.3425 -0.0020 -0.0111 -0.0138 1015 LEU B CD1 
16493 C CD2 . LEU B 1017 ? 0.2832 0.3114 0.3530 -0.0037 -0.0073 -0.0112 1015 LEU B CD2 
16494 N N   . SER B 1018 ? 0.1943 0.2145 0.2502 0.0055  -0.0041 -0.0133 1016 SER B N   
16495 C CA  . SER B 1018 ? 0.1986 0.2198 0.2529 0.0073  -0.0033 -0.0137 1016 SER B CA  
16496 C C   . SER B 1018 ? 0.1908 0.2132 0.2442 0.0077  -0.0012 -0.0128 1016 SER B C   
16497 O O   . SER B 1018 ? 0.2229 0.2464 0.2753 0.0088  -0.0005 -0.0131 1016 SER B O   
16498 C CB  . SER B 1018 ? 0.2289 0.2465 0.2793 0.0083  -0.0042 -0.0145 1016 SER B CB  
16499 O OG  . SER B 1018 ? 0.2271 0.2440 0.2781 0.0081  -0.0062 -0.0154 1016 SER B OG  
16500 N N   . GLY B 1019 ? 0.2217 0.2434 0.2751 0.0067  -0.0004 -0.0117 1017 GLY B N   
16501 C CA  . GLY B 1019 ? 0.3103 0.3332 0.3627 0.0073  0.0014  -0.0109 1017 GLY B CA  
16502 C C   . GLY B 1019 ? 0.2242 0.2453 0.2756 0.0065  0.0021  -0.0095 1017 GLY B C   
16503 O O   . GLY B 1019 ? 0.2326 0.2500 0.2829 0.0058  0.0010  -0.0094 1017 GLY B O   
16504 N N   . THR B 1020 ? 0.2181 0.2411 0.2692 0.0066  0.0038  -0.0085 1018 THR B N   
16505 C CA  . THR B 1020 ? 0.2241 0.2450 0.2734 0.0063  0.0044  -0.0071 1018 THR B CA  
16506 C C   . THR B 1020 ? 0.2411 0.2600 0.2869 0.0082  0.0045  -0.0073 1018 THR B C   
16507 O O   . THR B 1020 ? 0.2440 0.2598 0.2877 0.0085  0.0044  -0.0064 1018 THR B O   
16508 C CB  . THR B 1020 ? 0.2200 0.2443 0.2704 0.0057  0.0062  -0.0059 1018 THR B CB  
16509 O OG1 . THR B 1020 ? 0.2020 0.2291 0.2518 0.0072  0.0070  -0.0066 1018 THR B OG1 
16510 C CG2 . THR B 1020 ? 0.2116 0.2390 0.2657 0.0039  0.0064  -0.0055 1018 THR B CG2 
16511 N N   . GLY B 1021 ? 0.2336 0.2541 0.2788 0.0094  0.0045  -0.0083 1019 GLY B N   
16512 C CA  . GLY B 1021 ? 0.2320 0.2525 0.2745 0.0108  0.0049  -0.0082 1019 GLY B CA  
16513 C C   . GLY B 1021 ? 0.2329 0.2553 0.2751 0.0108  0.0063  -0.0070 1019 GLY B C   
16514 O O   . GLY B 1021 ? 0.2149 0.2387 0.2587 0.0097  0.0071  -0.0062 1019 GLY B O   
16515 N N   . PRO B 1022 ? 0.1912 0.2142 0.2312 0.0120  0.0067  -0.0067 1020 PRO B N   
16516 C CA  . PRO B 1022 ? 0.2015 0.2242 0.2397 0.0133  0.0060  -0.0074 1020 PRO B CA  
16517 C C   . PRO B 1022 ? 0.2169 0.2412 0.2555 0.0130  0.0057  -0.0086 1020 PRO B C   
16518 O O   . PRO B 1022 ? 0.2128 0.2387 0.2528 0.0123  0.0059  -0.0090 1020 PRO B O   
16519 C CB  . PRO B 1022 ? 0.2215 0.2455 0.2579 0.0143  0.0067  -0.0065 1020 PRO B CB  
16520 C CG  . PRO B 1022 ? 0.2334 0.2595 0.2706 0.0134  0.0077  -0.0059 1020 PRO B CG  
16521 C CD  . PRO B 1022 ? 0.2513 0.2763 0.2906 0.0122  0.0079  -0.0057 1020 PRO B CD  
16522 N N   . LYS B 1023 ? 0.1976 0.2217 0.2349 0.0136  0.0050  -0.0092 1021 LYS B N   
16523 C CA  . LYS B 1023 ? 0.1943 0.2194 0.2315 0.0132  0.0044  -0.0102 1021 LYS B CA  
16524 C C   . LYS B 1023 ? 0.1919 0.2193 0.2285 0.0128  0.0049  -0.0101 1021 LYS B C   
16525 O O   . LYS B 1023 ? 0.1933 0.2223 0.2287 0.0132  0.0054  -0.0094 1021 LYS B O   
16526 C CB  . LYS B 1023 ? 0.1737 0.1985 0.2092 0.0138  0.0039  -0.0105 1021 LYS B CB  
16527 C CG  . LYS B 1023 ? 0.1817 0.2037 0.2171 0.0141  0.0030  -0.0111 1021 LYS B CG  
16528 C CD  . LYS B 1023 ? 0.1787 0.2013 0.2120 0.0151  0.0028  -0.0114 1021 LYS B CD  
16529 C CE  . LYS B 1023 ? 0.1908 0.2106 0.2232 0.0155  0.0019  -0.0123 1021 LYS B CE  
16530 N NZ  . LYS B 1023 ? 0.1828 0.2020 0.2156 0.0142  0.0010  -0.0129 1021 LYS B NZ  
16531 N N   . ALA B 1024 ? 0.2120 0.2392 0.2491 0.0122  0.0045  -0.0108 1022 ALA B N   
16532 C CA  . ALA B 1024 ? 0.2055 0.2339 0.2414 0.0118  0.0045  -0.0111 1022 ALA B CA  
16533 C C   . ALA B 1024 ? 0.1903 0.2192 0.2242 0.0113  0.0039  -0.0110 1022 ALA B C   
16534 O O   . ALA B 1024 ? 0.2113 0.2394 0.2449 0.0113  0.0033  -0.0112 1022 ALA B O   
16535 C CB  . ALA B 1024 ? 0.2043 0.2315 0.2407 0.0116  0.0039  -0.0120 1022 ALA B CB  
16536 N N   . GLY B 1025 ? 0.1452 0.1758 0.1776 0.0108  0.0040  -0.0107 1023 GLY B N   
16537 C CA  . GLY B 1025 ? 0.1522 0.1843 0.1831 0.0101  0.0035  -0.0104 1023 GLY B CA  
16538 C C   . GLY B 1025 ? 0.1625 0.1965 0.1936 0.0110  0.0040  -0.0098 1023 GLY B C   
16539 O O   . GLY B 1025 ? 0.1779 0.2134 0.2081 0.0106  0.0037  -0.0097 1023 GLY B O   
16540 N N   . GLY B 1026 ? 0.1756 0.2098 0.2077 0.0123  0.0047  -0.0093 1024 GLY B N   
16541 C CA  . GLY B 1026 ? 0.1693 0.2047 0.2012 0.0138  0.0050  -0.0088 1024 GLY B CA  
16542 C C   . GLY B 1026 ? 0.1658 0.2028 0.1976 0.0147  0.0057  -0.0079 1024 GLY B C   
16543 O O   . GLY B 1026 ? 0.1712 0.2082 0.2032 0.0141  0.0059  -0.0077 1024 GLY B O   
16544 N N   . PRO B 1027 ? 0.1682 0.2066 0.1996 0.0164  0.0059  -0.0074 1025 PRO B N   
16545 C CA  . PRO B 1027 ? 0.1491 0.1898 0.1802 0.0174  0.0062  -0.0064 1025 PRO B CA  
16546 C C   . PRO B 1027 ? 0.1812 0.2189 0.2123 0.0182  0.0066  -0.0058 1025 PRO B C   
16547 O O   . PRO B 1027 ? 0.1784 0.2176 0.2089 0.0190  0.0068  -0.0049 1025 PRO B O   
16548 C CB  . PRO B 1027 ? 0.2035 0.2469 0.2341 0.0193  0.0062  -0.0063 1025 PRO B CB  
16549 C CG  . PRO B 1027 ? 0.2017 0.2422 0.2321 0.0198  0.0060  -0.0071 1025 PRO B CG  
16550 C CD  . PRO B 1027 ? 0.1895 0.2281 0.2205 0.0175  0.0057  -0.0078 1025 PRO B CD  
16551 N N   . LEU B 1028 ? 0.1955 0.2293 0.2272 0.0180  0.0066  -0.0061 1026 LEU B N   
16552 C CA  . LEU B 1028 ? 0.1763 0.2074 0.2080 0.0182  0.0069  -0.0053 1026 LEU B CA  
16553 C C   . LEU B 1028 ? 0.1889 0.2203 0.2214 0.0166  0.0075  -0.0052 1026 LEU B C   
16554 O O   . LEU B 1028 ? 0.2183 0.2483 0.2508 0.0164  0.0080  -0.0043 1026 LEU B O   
16555 C CB  . LEU B 1028 ? 0.1739 0.2008 0.2058 0.0185  0.0066  -0.0056 1026 LEU B CB  
16556 C CG  . LEU B 1028 ? 0.2059 0.2318 0.2365 0.0206  0.0060  -0.0058 1026 LEU B CG  
16557 C CD1 . LEU B 1028 ? 0.2093 0.2302 0.2397 0.0206  0.0054  -0.0062 1026 LEU B CD1 
16558 C CD2 . LEU B 1028 ? 0.2577 0.2844 0.2868 0.0226  0.0062  -0.0048 1026 LEU B CD2 
16559 N N   . TYR B 1029 ? 0.1631 0.1960 0.1961 0.0154  0.0074  -0.0061 1027 TYR B N   
16560 C CA  . TYR B 1029 ? 0.1667 0.1994 0.2006 0.0143  0.0078  -0.0064 1027 TYR B CA  
16561 C C   . TYR B 1029 ? 0.1670 0.2012 0.2000 0.0143  0.0086  -0.0056 1027 TYR B C   
16562 O O   . TYR B 1029 ? 0.1755 0.2091 0.2091 0.0139  0.0093  -0.0051 1027 TYR B O   
16563 C CB  . TYR B 1029 ? 0.1898 0.2232 0.2238 0.0134  0.0072  -0.0077 1027 TYR B CB  
16564 C CG  . TYR B 1029 ? 0.1970 0.2296 0.2320 0.0127  0.0073  -0.0085 1027 TYR B CG  
16565 C CD1 . TYR B 1029 ? 0.1766 0.2075 0.2135 0.0126  0.0071  -0.0089 1027 TYR B CD1 
16566 C CD2 . TYR B 1029 ? 0.2004 0.2339 0.2344 0.0124  0.0074  -0.0090 1027 TYR B CD2 
16567 C CE1 . TYR B 1029 ? 0.1704 0.2013 0.2086 0.0122  0.0071  -0.0097 1027 TYR B CE1 
16568 C CE2 . TYR B 1029 ? 0.1844 0.2173 0.2194 0.0122  0.0075  -0.0100 1027 TYR B CE2 
16569 C CZ  . TYR B 1029 ? 0.2022 0.2341 0.2394 0.0123  0.0074  -0.0103 1027 TYR B CZ  
16570 O OH  . TYR B 1029 ? 0.2233 0.2552 0.2615 0.0125  0.0073  -0.0113 1027 TYR B OH  
16571 N N   . LEU B 1030 ? 0.1804 0.2169 0.2119 0.0145  0.0084  -0.0054 1028 LEU B N   
16572 C CA  . LEU B 1030 ? 0.1748 0.2127 0.2050 0.0145  0.0089  -0.0047 1028 LEU B CA  
16573 C C   . LEU B 1030 ? 0.1971 0.2340 0.2269 0.0152  0.0096  -0.0032 1028 LEU B C   
16574 O O   . LEU B 1030 ? 0.1927 0.2299 0.2218 0.0149  0.0104  -0.0025 1028 LEU B O   
16575 C CB  . LEU B 1030 ? 0.2082 0.2489 0.2368 0.0145  0.0083  -0.0047 1028 LEU B CB  
16576 C CG  . LEU B 1030 ? 0.2174 0.2588 0.2457 0.0133  0.0075  -0.0060 1028 LEU B CG  
16577 C CD1 . LEU B 1030 ? 0.2354 0.2799 0.2621 0.0129  0.0068  -0.0057 1028 LEU B CD1 
16578 C CD2 . LEU B 1030 ? 0.2104 0.2503 0.2385 0.0126  0.0078  -0.0070 1028 LEU B CD2 
16579 N N   . GLY B 1031 ? 0.2017 0.2370 0.2315 0.0163  0.0092  -0.0025 1029 GLY B N   
16580 C CA  . GLY B 1031 ? 0.2195 0.2528 0.2483 0.0170  0.0095  -0.0010 1029 GLY B CA  
16581 C C   . GLY B 1031 ? 0.2140 0.2452 0.2438 0.0157  0.0103  -0.0004 1029 GLY B C   
16582 O O   . GLY B 1031 ? 0.2221 0.2519 0.2507 0.0157  0.0108  0.0012  1029 GLY B O   
16583 N N   . ARG B 1032 ? 0.1763 0.2073 0.2082 0.0146  0.0104  -0.0016 1030 ARG B N   
16584 C CA  . ARG B 1032 ? 0.1843 0.2146 0.2177 0.0132  0.0112  -0.0011 1030 ARG B CA  
16585 C C   . ARG B 1032 ? 0.1928 0.2259 0.2258 0.0127  0.0125  -0.0009 1030 ARG B C   
16586 O O   . ARG B 1032 ? 0.2150 0.2484 0.2489 0.0116  0.0134  -0.0001 1030 ARG B O   
16587 C CB  . ARG B 1032 ? 0.2242 0.2540 0.2600 0.0125  0.0108  -0.0025 1030 ARG B CB  
16588 C CG  . ARG B 1032 ? 0.2342 0.2633 0.2720 0.0110  0.0113  -0.0020 1030 ARG B CG  
16589 C CD  . ARG B 1032 ? 0.2592 0.2846 0.2964 0.0107  0.0108  -0.0006 1030 ARG B CD  
16590 N NE  . ARG B 1032 ? 0.2533 0.2782 0.2928 0.0088  0.0110  -0.0002 1030 ARG B NE  
16591 C CZ  . ARG B 1032 ? 0.2677 0.2917 0.3070 0.0073  0.0116  0.0016  1030 ARG B CZ  
16592 N NH1 . ARG B 1032 ? 0.2962 0.3190 0.3328 0.0077  0.0121  0.0033  1030 ARG B NH1 
16593 N NH2 . ARG B 1032 ? 0.2790 0.3035 0.3210 0.0052  0.0117  0.0019  1030 ARG B NH2 
16594 N N   . LEU B 1033 ? 0.1986 0.2338 0.2301 0.0133  0.0124  -0.0016 1031 LEU B N   
16595 C CA  . LEU B 1033 ? 0.1978 0.2354 0.2286 0.0130  0.0133  -0.0019 1031 LEU B CA  
16596 C C   . LEU B 1033 ? 0.2042 0.2428 0.2322 0.0135  0.0138  -0.0006 1031 LEU B C   
16597 O O   . LEU B 1033 ? 0.2124 0.2529 0.2388 0.0135  0.0143  -0.0010 1031 LEU B O   
16598 C CB  . LEU B 1033 ? 0.1836 0.2223 0.2143 0.0132  0.0127  -0.0039 1031 LEU B CB  
16599 C CG  . LEU B 1033 ? 0.1898 0.2272 0.2228 0.0129  0.0120  -0.0051 1031 LEU B CG  
16600 C CD1 . LEU B 1033 ? 0.2214 0.2591 0.2537 0.0130  0.0111  -0.0068 1031 LEU B CD1 
16601 C CD2 . LEU B 1033 ? 0.2281 0.2660 0.2636 0.0123  0.0129  -0.0052 1031 LEU B CD2 
16602 N N   . VAL B 1034 ? 0.1907 0.2276 0.2176 0.0140  0.0134  0.0010  1032 VAL B N   
16603 C CA  . VAL B 1034 ? 0.2272 0.2645 0.2513 0.0145  0.0136  0.0027  1032 VAL B CA  
16604 C C   . VAL B 1034 ? 0.2570 0.2912 0.2808 0.0142  0.0140  0.0047  1032 VAL B C   
16605 O O   . VAL B 1034 ? 0.2620 0.2938 0.2876 0.0137  0.0136  0.0047  1032 VAL B O   
16606 C CB  . VAL B 1034 ? 0.2005 0.2387 0.2231 0.0159  0.0123  0.0026  1032 VAL B CB  
16607 C CG1 . VAL B 1034 ? 0.2424 0.2834 0.2646 0.0156  0.0119  0.0008  1032 VAL B CG1 
16608 C CG2 . VAL B 1034 ? 0.2228 0.2592 0.2466 0.0167  0.0113  0.0024  1032 VAL B CG2 
16609 N N   . THR B 1035 ? 0.2503 0.2845 0.2716 0.0142  0.0145  0.0066  1033 THR B N   
16610 C CA  . THR B 1035 ? 0.2777 0.3085 0.2982 0.0135  0.0148  0.0087  1033 THR B CA  
16611 C C   . THR B 1035 ? 0.2842 0.3112 0.3034 0.0150  0.0133  0.0096  1033 THR B C   
16612 O O   . THR B 1035 ? 0.3498 0.3727 0.3687 0.0144  0.0130  0.0109  1033 THR B O   
16613 C CB  . THR B 1035 ? 0.3037 0.3354 0.3216 0.0128  0.0160  0.0107  1033 THR B CB  
16614 O OG1 . THR B 1035 ? 0.3912 0.4249 0.4064 0.0142  0.0156  0.0106  1033 THR B OG1 
16615 C CG2 . THR B 1035 ? 0.3936 0.4285 0.4132 0.0111  0.0178  0.0102  1033 THR B CG2 
16616 N N   . THR B 1036 ? 0.2439 0.2723 0.2623 0.0170  0.0122  0.0088  1034 THR B N   
16617 C CA  . THR B 1036 ? 0.2544 0.2802 0.2719 0.0191  0.0108  0.0091  1034 THR B CA  
16618 C C   . THR B 1036 ? 0.2514 0.2796 0.2709 0.0200  0.0101  0.0069  1034 THR B C   
16619 O O   . THR B 1036 ? 0.2386 0.2710 0.2582 0.0202  0.0100  0.0060  1034 THR B O   
16620 C CB  . THR B 1036 ? 0.3128 0.3388 0.3271 0.0208  0.0102  0.0107  1034 THR B CB  
16621 O OG1 . THR B 1036 ? 0.4235 0.4474 0.4355 0.0196  0.0110  0.0129  1034 THR B OG1 
16622 C CG2 . THR B 1036 ? 0.3632 0.3861 0.3764 0.0235  0.0087  0.0111  1034 THR B CG2 
16623 N N   . ALA B 1037 ? 0.2399 0.2655 0.2607 0.0204  0.0095  0.0061  1035 ALA B N   
16624 C CA  . ALA B 1037 ? 0.2545 0.2826 0.2773 0.0209  0.0090  0.0042  1035 ALA B CA  
16625 C C   . ALA B 1037 ? 0.2327 0.2631 0.2543 0.0234  0.0081  0.0042  1035 ALA B C   
16626 O O   . ALA B 1037 ? 0.2501 0.2780 0.2698 0.0255  0.0074  0.0054  1035 ALA B O   
16627 C CB  . ALA B 1037 ? 0.2617 0.2863 0.2858 0.0207  0.0086  0.0033  1035 ALA B CB  
16628 N N   . PRO B 1038 ? 0.2026 0.2376 0.2253 0.0233  0.0079  0.0030  1036 PRO B N   
16629 C CA  . PRO B 1038 ? 0.2299 0.2681 0.2522 0.0255  0.0070  0.0029  1036 PRO B CA  
16630 C C   . PRO B 1038 ? 0.2131 0.2501 0.2363 0.0270  0.0066  0.0020  1036 PRO B C   
16631 O O   . PRO B 1038 ? 0.2111 0.2450 0.2353 0.0260  0.0068  0.0012  1036 PRO B O   
16632 C CB  . PRO B 1038 ? 0.2135 0.2570 0.2368 0.0241  0.0070  0.0020  1036 PRO B CB  
16633 C CG  . PRO B 1038 ? 0.2330 0.2748 0.2577 0.0217  0.0076  0.0008  1036 PRO B CG  
16634 C CD  . PRO B 1038 ? 0.2182 0.2556 0.2424 0.0212  0.0084  0.0017  1036 PRO B CD  
16635 N N   . VAL B 1039 ? 0.2272 0.2674 0.2502 0.0294  0.0059  0.0020  1037 VAL B N   
16636 C CA  . VAL B 1039 ? 0.2014 0.2419 0.2251 0.0311  0.0057  0.0010  1037 VAL B CA  
16637 C C   . VAL B 1039 ? 0.2079 0.2532 0.2336 0.0292  0.0059  -0.0003 1037 VAL B C   
16638 O O   . VAL B 1039 ? 0.2017 0.2525 0.2279 0.0289  0.0057  -0.0001 1037 VAL B O   
16639 C CB  . VAL B 1039 ? 0.2306 0.2731 0.2532 0.0349  0.0050  0.0015  1037 VAL B CB  
16640 C CG1 . VAL B 1039 ? 0.2525 0.2953 0.2755 0.0369  0.0049  0.0002  1037 VAL B CG1 
16641 C CG2 . VAL B 1039 ? 0.2471 0.2841 0.2670 0.0367  0.0045  0.0029  1037 VAL B CG2 
16642 N N   . PRO B 1040 ? 0.1959 0.2390 0.2225 0.0278  0.0062  -0.0014 1038 PRO B N   
16643 C CA  . PRO B 1040 ? 0.2166 0.2635 0.2446 0.0258  0.0063  -0.0024 1038 PRO B CA  
16644 C C   . PRO B 1040 ? 0.1787 0.2310 0.2071 0.0274  0.0060  -0.0027 1038 PRO B C   
16645 O O   . PRO B 1040 ? 0.2026 0.2550 0.2304 0.0304  0.0059  -0.0025 1038 PRO B O   
16646 C CB  . PRO B 1040 ? 0.2071 0.2497 0.2356 0.0246  0.0064  -0.0035 1038 PRO B CB  
16647 C CG  . PRO B 1040 ? 0.2179 0.2551 0.2458 0.0248  0.0065  -0.0029 1038 PRO B CG  
16648 C CD  . PRO B 1040 ? 0.2120 0.2490 0.2383 0.0276  0.0063  -0.0018 1038 PRO B CD  
16649 N N   . PRO B 1041 ? 0.1812 0.2382 0.2106 0.0253  0.0060  -0.0030 1039 PRO B N   
16650 C CA  . PRO B 1041 ? 0.1792 0.2420 0.2093 0.0262  0.0059  -0.0032 1039 PRO B CA  
16651 C C   . PRO B 1041 ? 0.1928 0.2535 0.2227 0.0281  0.0062  -0.0041 1039 PRO B C   
16652 O O   . PRO B 1041 ? 0.2092 0.2648 0.2388 0.0271  0.0063  -0.0048 1039 PRO B O   
16653 C CB  . PRO B 1041 ? 0.2116 0.2774 0.2425 0.0226  0.0058  -0.0035 1039 PRO B CB  
16654 C CG  . PRO B 1041 ? 0.2154 0.2781 0.2457 0.0206  0.0055  -0.0033 1039 PRO B CG  
16655 C CD  . PRO B 1041 ? 0.2166 0.2731 0.2464 0.0220  0.0059  -0.0034 1039 PRO B CD  
16656 N N   . GLN B 1042 ? 0.1970 0.2615 0.2269 0.0311  0.0063  -0.0040 1040 GLN B N   
16657 C CA  . GLN B 1042 ? 0.2297 0.2933 0.2589 0.0333  0.0067  -0.0050 1040 GLN B CA  
16658 C C   . GLN B 1042 ? 0.2349 0.2901 0.2624 0.0350  0.0064  -0.0055 1040 GLN B C   
16659 O O   . GLN B 1042 ? 0.2099 0.2628 0.2363 0.0364  0.0065  -0.0066 1040 GLN B O   
16660 C CB  . GLN B 1042 ? 0.2752 0.3403 0.3050 0.0307  0.0070  -0.0057 1040 GLN B CB  
16661 C CG  . GLN B 1042 ? 0.3075 0.3805 0.3387 0.0285  0.0071  -0.0051 1040 GLN B CG  
16662 C CD  . GLN B 1042 ? 0.3482 0.4224 0.3794 0.0261  0.0074  -0.0056 1040 GLN B CD  
16663 O OE1 . GLN B 1042 ? 0.5091 0.5893 0.5406 0.0267  0.0079  -0.0056 1040 GLN B OE1 
16664 N NE2 . GLN B 1042 ? 0.4135 0.4823 0.4441 0.0234  0.0071  -0.0060 1040 GLN B NE2 
16665 N N   . HIS B 1043 ? 0.1926 0.2432 0.2194 0.0348  0.0061  -0.0048 1041 HIS B N   
16666 C CA  . HIS B 1043 ? 0.1904 0.2330 0.2158 0.0353  0.0057  -0.0050 1041 HIS B CA  
16667 C C   . HIS B 1043 ? 0.2245 0.2644 0.2478 0.0394  0.0053  -0.0048 1041 HIS B C   
16668 O O   . HIS B 1043 ? 0.2297 0.2679 0.2521 0.0404  0.0049  -0.0037 1041 HIS B O   
16669 C CB  . HIS B 1043 ? 0.1912 0.2305 0.2170 0.0326  0.0057  -0.0042 1041 HIS B CB  
16670 C CG  . HIS B 1043 ? 0.1915 0.2231 0.2161 0.0323  0.0054  -0.0042 1041 HIS B CG  
16671 N ND1 . HIS B 1043 ? 0.2015 0.2298 0.2267 0.0303  0.0054  -0.0051 1041 HIS B ND1 
16672 C CD2 . HIS B 1043 ? 0.2249 0.2515 0.2478 0.0336  0.0050  -0.0033 1041 HIS B CD2 
16673 C CE1 . HIS B 1043 ? 0.2134 0.2356 0.2377 0.0301  0.0049  -0.0048 1041 HIS B CE1 
16674 N NE2 . HIS B 1043 ? 0.2269 0.2476 0.2496 0.0320  0.0047  -0.0036 1041 HIS B NE2 
16675 N N   . SER B 1044 ? 0.1784 0.2176 0.2005 0.0420  0.0052  -0.0060 1042 SER B N   
16676 C CA  . SER B 1044 ? 0.2072 0.2431 0.2268 0.0464  0.0046  -0.0062 1042 SER B CA  
16677 C C   . SER B 1044 ? 0.2033 0.2369 0.2214 0.0482  0.0045  -0.0079 1042 SER B C   
16678 O O   . SER B 1044 ? 0.2178 0.2540 0.2369 0.0463  0.0051  -0.0088 1042 SER B O   
16679 C CB  . SER B 1044 ? 0.2034 0.2463 0.2234 0.0495  0.0047  -0.0055 1042 SER B CB  
16680 O OG  . SER B 1044 ? 0.2092 0.2596 0.2305 0.0505  0.0054  -0.0064 1042 SER B OG  
16681 N N   . SER B 1045 ? 0.2068 0.2351 0.2218 0.0521  0.0038  -0.0084 1043 SER B N   
16682 C CA  . SER B 1045 ? 0.1877 0.2133 0.2005 0.0544  0.0036  -0.0103 1043 SER B CA  
16683 C C   . SER B 1045 ? 0.2199 0.2435 0.2297 0.0601  0.0030  -0.0107 1043 SER B C   
16684 O O   . SER B 1045 ? 0.2244 0.2434 0.2327 0.0614  0.0021  -0.0096 1043 SER B O   
16685 C CB  . SER B 1045 ? 0.2180 0.2346 0.2294 0.0519  0.0028  -0.0109 1043 SER B CB  
16686 O OG  . SER B 1045 ? 0.2430 0.2560 0.2515 0.0546  0.0023  -0.0128 1043 SER B OG  
16687 N N   . VAL B 1046 ? 0.2098 0.2367 0.2184 0.0637  0.0034  -0.0123 1044 VAL B N   
16688 C CA  . VAL B 1046 ? 0.2268 0.2514 0.2322 0.0697  0.0027  -0.0131 1044 VAL B CA  
16689 C C   . VAL B 1046 ? 0.2252 0.2380 0.2259 0.0712  0.0013  -0.0144 1044 VAL B C   
16690 O O   . VAL B 1046 ? 0.2752 0.2834 0.2723 0.0763  0.0004  -0.0151 1044 VAL B O   
16691 C CB  . VAL B 1046 ? 0.2533 0.2872 0.2591 0.0737  0.0039  -0.0143 1044 VAL B CB  
16692 C CG1 . VAL B 1046 ? 0.2984 0.3442 0.3088 0.0721  0.0050  -0.0128 1044 VAL B CG1 
16693 C CG2 . VAL B 1046 ? 0.2548 0.2888 0.2598 0.0728  0.0045  -0.0160 1044 VAL B CG2 
16694 N N   . HIS B 1047 ? 0.2481 0.2554 0.2488 0.0670  0.0010  -0.0147 1045 HIS B N   
16695 C CA  A HIS B 1047 ? 0.2450 0.2413 0.2414 0.0677  -0.0005 -0.0161 1045 HIS B CA  
16696 C CA  B HIS B 1047 ? 0.2454 0.2416 0.2419 0.0674  -0.0005 -0.0160 1045 HIS B CA  
16697 C C   . HIS B 1047 ? 0.2297 0.2168 0.2245 0.0662  -0.0020 -0.0146 1045 HIS B C   
16698 O O   . HIS B 1047 ? 0.2662 0.2550 0.2639 0.0623  -0.0017 -0.0126 1045 HIS B O   
16699 C CB  A HIS B 1047 ? 0.2702 0.2658 0.2674 0.0640  -0.0003 -0.0172 1045 HIS B CB  
16700 C CB  B HIS B 1047 ? 0.2615 0.2568 0.2591 0.0631  -0.0003 -0.0169 1045 HIS B CB  
16701 C CG  A HIS B 1047 ? 0.2834 0.2883 0.2820 0.0650  0.0012  -0.0183 1045 HIS B CG  
16702 C CG  B HIS B 1047 ? 0.2748 0.2588 0.2693 0.0616  -0.0021 -0.0177 1045 HIS B CG  
16703 N ND1 A HIS B 1047 ? 0.3138 0.3203 0.3096 0.0701  0.0015  -0.0201 1045 HIS B ND1 
16704 N ND1 B HIS B 1047 ? 0.2813 0.2585 0.2709 0.0651  -0.0033 -0.0198 1045 HIS B ND1 
16705 C CD2 A HIS B 1047 ? 0.2829 0.2962 0.2854 0.0616  0.0026  -0.0176 1045 HIS B CD2 
16706 C CD2 B HIS B 1047 ? 0.2668 0.2452 0.2622 0.0570  -0.0030 -0.0167 1045 HIS B CD2 
16707 C CE1 A HIS B 1047 ? 0.3252 0.3412 0.3233 0.0695  0.0031  -0.0204 1045 HIS B CE1 
16708 C CE1 B HIS B 1047 ? 0.3221 0.2898 0.3098 0.0624  -0.0050 -0.0200 1045 HIS B CE1 
16709 N NE2 A HIS B 1047 ? 0.2610 0.2809 0.2630 0.0643  0.0037  -0.0189 1045 HIS B NE2 
16710 N NE2 B HIS B 1047 ? 0.3103 0.2789 0.3016 0.0574  -0.0048 -0.0180 1045 HIS B NE2 
16711 N N   . THR B 1048 ? 0.2479 0.2253 0.2378 0.0693  -0.0037 -0.0155 1046 THR B N   
16712 C CA  . THR B 1048 ? 0.2404 0.2078 0.2279 0.0677  -0.0053 -0.0140 1046 THR B CA  
16713 C C   . THR B 1048 ? 0.2474 0.2049 0.2319 0.0657  -0.0069 -0.0153 1046 THR B C   
16714 O O   . THR B 1048 ? 0.2915 0.2453 0.2723 0.0690  -0.0076 -0.0176 1046 THR B O   
16715 C CB  . THR B 1048 ? 0.2996 0.2627 0.2832 0.0731  -0.0065 -0.0136 1046 THR B CB  
16716 O OG1 . THR B 1048 ? 0.2951 0.2686 0.2815 0.0756  -0.0051 -0.0127 1046 THR B OG1 
16717 C CG2 . THR B 1048 ? 0.3347 0.2883 0.3162 0.0707  -0.0080 -0.0115 1046 THR B CG2 
16718 N N   . ASP B 1049 ? 0.2516 0.2052 0.2376 0.0602  -0.0074 -0.0139 1047 ASP B N   
16719 C CA  . ASP B 1049 ? 0.2706 0.2152 0.2541 0.0577  -0.0090 -0.0149 1047 ASP B CA  
16720 C C   . ASP B 1049 ? 0.2788 0.2119 0.2557 0.0614  -0.0113 -0.0158 1047 ASP B C   
16721 O O   . ASP B 1049 ? 0.3049 0.2337 0.2797 0.0630  -0.0120 -0.0142 1047 ASP B O   
16722 C CB  . ASP B 1049 ? 0.2661 0.2092 0.2526 0.0514  -0.0091 -0.0129 1047 ASP B CB  
16723 C CG  . ASP B 1049 ? 0.2874 0.2226 0.2722 0.0482  -0.0109 -0.0138 1047 ASP B CG  
16724 O OD1 . ASP B 1049 ? 0.2932 0.2179 0.2736 0.0484  -0.0129 -0.0136 1047 ASP B OD1 
16725 O OD2 . ASP B 1049 ? 0.3011 0.2403 0.2888 0.0455  -0.0104 -0.0148 1047 ASP B OD2 
16726 N N   . PRO B 1050 ? 0.2777 0.2053 0.2509 0.0632  -0.0125 -0.0183 1048 PRO B N   
16727 C CA  . PRO B 1050 ? 0.3304 0.2464 0.2966 0.0674  -0.0148 -0.0195 1048 PRO B CA  
16728 C C   . PRO B 1050 ? 0.3341 0.2384 0.2976 0.0635  -0.0171 -0.0179 1048 PRO B C   
16729 O O   . PRO B 1050 ? 0.3492 0.2440 0.3072 0.0665  -0.0189 -0.0177 1048 PRO B O   
16730 C CB  . PRO B 1050 ? 0.3473 0.2615 0.3105 0.0697  -0.0153 -0.0228 1048 PRO B CB  
16731 C CG  . PRO B 1050 ? 0.3456 0.2660 0.3137 0.0643  -0.0142 -0.0228 1048 PRO B CG  
16732 C CD  . PRO B 1050 ? 0.2976 0.2291 0.2722 0.0619  -0.0119 -0.0204 1048 PRO B CD  
16733 N N   . VAL B 1051 ? 0.3286 0.2335 0.2957 0.0570  -0.0170 -0.0167 1049 VAL B N   
16734 C CA  . VAL B 1051 ? 0.3057 0.2007 0.2709 0.0526  -0.0190 -0.0149 1049 VAL B CA  
16735 C C   . VAL B 1051 ? 0.3030 0.1993 0.2695 0.0518  -0.0183 -0.0117 1049 VAL B C   
16736 O O   . VAL B 1051 ? 0.3322 0.2185 0.2944 0.0515  -0.0202 -0.0103 1049 VAL B O   
16737 C CB  . VAL B 1051 ? 0.3225 0.2187 0.2913 0.0460  -0.0192 -0.0148 1049 VAL B CB  
16738 C CG1 . VAL B 1051 ? 0.3602 0.2472 0.3275 0.0411  -0.0211 -0.0126 1049 VAL B CG1 
16739 C CG2 . VAL B 1051 ? 0.3702 0.2643 0.3369 0.0471  -0.0202 -0.0180 1049 VAL B CG2 
16740 N N   . LEU B 1052 ? 0.2909 0.1989 0.2627 0.0516  -0.0158 -0.0106 1050 LEU B N   
16741 C CA  . LEU B 1052 ? 0.2806 0.1906 0.2530 0.0522  -0.0151 -0.0079 1050 LEU B CA  
16742 C C   . LEU B 1052 ? 0.3531 0.2564 0.3196 0.0584  -0.0165 -0.0082 1050 LEU B C   
16743 O O   . LEU B 1052 ? 0.3138 0.2102 0.2773 0.0581  -0.0177 -0.0060 1050 LEU B O   
16744 C CB  . LEU B 1052 ? 0.2790 0.2028 0.2575 0.0521  -0.0123 -0.0074 1050 LEU B CB  
16745 C CG  . LEU B 1052 ? 0.2694 0.1974 0.2493 0.0524  -0.0113 -0.0047 1050 LEU B CG  
16746 C CD1 . LEU B 1052 ? 0.3108 0.2387 0.2874 0.0590  -0.0117 -0.0050 1050 LEU B CD1 
16747 C CD2 . LEU B 1052 ? 0.2914 0.2123 0.2700 0.0480  -0.0123 -0.0020 1050 LEU B CD2 
16748 N N   . LEU B 1053 ? 0.3122 0.2176 0.2769 0.0641  -0.0164 -0.0108 1051 LEU B N   
16749 C CA  . LEU B 1053 ? 0.3312 0.2309 0.2905 0.0707  -0.0177 -0.0113 1051 LEU B CA  
16750 C C   . LEU B 1053 ? 0.3245 0.2081 0.2767 0.0705  -0.0208 -0.0113 1051 LEU B C   
16751 O O   . LEU B 1053 ? 0.3839 0.2605 0.3320 0.0730  -0.0223 -0.0097 1051 LEU B O   
16752 C CB  . LEU B 1053 ? 0.3667 0.2717 0.3252 0.0768  -0.0170 -0.0144 1051 LEU B CB  
16753 C CG  . LEU B 1053 ? 0.4053 0.3259 0.3698 0.0781  -0.0141 -0.0143 1051 LEU B CG  
16754 C CD1 . LEU B 1053 ? 0.3613 0.2871 0.3253 0.0827  -0.0133 -0.0174 1051 LEU B CD1 
16755 C CD2 . LEU B 1053 ? 0.3851 0.3089 0.3497 0.0815  -0.0139 -0.0123 1051 LEU B CD2 
16756 N N   . ASP B 1054 ? 0.3544 0.2318 0.3050 0.0676  -0.0221 -0.0129 1052 ASP B N   
16757 C CA  . ASP B 1054 ? 0.4297 0.2912 0.3734 0.0668  -0.0253 -0.0129 1052 ASP B CA  
16758 C C   . ASP B 1054 ? 0.3804 0.2370 0.3243 0.0614  -0.0260 -0.0091 1052 ASP B C   
16759 O O   . ASP B 1054 ? 0.3955 0.2401 0.3333 0.0623  -0.0284 -0.0080 1052 ASP B O   
16760 C CB  . ASP B 1054 ? 0.3884 0.2454 0.3311 0.0638  -0.0265 -0.0152 1052 ASP B CB  
16761 C CG  . ASP B 1054 ? 0.4636 0.3216 0.4035 0.0698  -0.0265 -0.0190 1052 ASP B CG  
16762 O OD1 . ASP B 1054 ? 0.4394 0.2996 0.3773 0.0766  -0.0260 -0.0199 1052 ASP B OD1 
16763 O OD2 . ASP B 1054 ? 0.5164 0.3732 0.4561 0.0678  -0.0271 -0.0212 1052 ASP B OD2 
16764 N N   . PHE B 1055 ? 0.3556 0.2214 0.3063 0.0557  -0.0240 -0.0072 1053 PHE B N   
16765 C CA  . PHE B 1055 ? 0.3372 0.2002 0.2886 0.0505  -0.0242 -0.0035 1053 PHE B CA  
16766 C C   . PHE B 1055 ? 0.3985 0.2612 0.3478 0.0542  -0.0240 -0.0013 1053 PHE B C   
16767 O O   . PHE B 1055 ? 0.3774 0.2305 0.3225 0.0527  -0.0258 0.0011  1053 PHE B O   
16768 C CB  . PHE B 1055 ? 0.3290 0.2032 0.2883 0.0445  -0.0217 -0.0023 1053 PHE B CB  
16769 C CG  . PHE B 1055 ? 0.3333 0.2062 0.2939 0.0389  -0.0216 0.0014  1053 PHE B CG  
16770 C CD1 . PHE B 1055 ? 0.3752 0.2365 0.3319 0.0347  -0.0239 0.0028  1053 PHE B CD1 
16771 C CD2 . PHE B 1055 ? 0.3293 0.2125 0.2948 0.0375  -0.0191 0.0034  1053 PHE B CD2 
16772 C CE1 . PHE B 1055 ? 0.4021 0.2629 0.3600 0.0293  -0.0236 0.0063  1053 PHE B CE1 
16773 C CE2 . PHE B 1055 ? 0.3355 0.2178 0.3018 0.0325  -0.0187 0.0068  1053 PHE B CE2 
16774 C CZ  . PHE B 1055 ? 0.3493 0.2207 0.3120 0.0283  -0.0209 0.0083  1053 PHE B CZ  
16775 N N   . ALA B 1056 ? 0.3568 0.2297 0.3088 0.0590  -0.0221 -0.0021 1054 ALA B N   
16776 C CA  . ALA B 1056 ? 0.3658 0.2390 0.3158 0.0630  -0.0222 -0.0003 1054 ALA B CA  
16777 C C   . ALA B 1056 ? 0.3828 0.2423 0.3244 0.0681  -0.0252 -0.0007 1054 ALA B C   
16778 O O   . ALA B 1056 ? 0.4164 0.2694 0.3543 0.0687  -0.0264 0.0019  1054 ALA B O   
16779 C CB  . ALA B 1056 ? 0.3404 0.2273 0.2948 0.0675  -0.0199 -0.0014 1054 ALA B CB  
16780 N N   . LYS B 1057 ? 0.3887 0.2431 0.3268 0.0720  -0.0265 -0.0040 1055 LYS B N   
16781 C CA  . LYS B 1057 ? 0.4141 0.2547 0.3436 0.0773  -0.0295 -0.0048 1055 LYS B CA  
16782 C C   . LYS B 1057 ? 0.4725 0.2981 0.3968 0.0722  -0.0322 -0.0027 1055 LYS B C   
16783 O O   . LYS B 1057 ? 0.4862 0.3011 0.4043 0.0746  -0.0344 -0.0011 1055 LYS B O   
16784 C CB  . LYS B 1057 ? 0.4522 0.2905 0.3788 0.0823  -0.0302 -0.0091 1055 LYS B CB  
16785 C CG  . LYS B 1057 ? 0.5380 0.3874 0.4667 0.0896  -0.0284 -0.0110 1055 LYS B CG  
16786 C CD  . LYS B 1057 ? 0.4527 0.2987 0.3776 0.0945  -0.0292 -0.0152 1055 LYS B CD  
16787 C CE  . LYS B 1057 ? 0.4602 0.3081 0.3880 0.0889  -0.0286 -0.0167 1055 LYS B CE  
16788 N NZ  . LYS B 1057 ? 0.5191 0.3671 0.4441 0.0941  -0.0287 -0.0208 1055 LYS B NZ  
16789 N N   . TRP B 1058 ? 0.4531 0.2780 0.3800 0.0651  -0.0321 -0.0026 1056 TRP B N   
16790 C CA  . TRP B 1058 ? 0.4860 0.2986 0.4092 0.0590  -0.0345 -0.0002 1056 TRP B CA  
16791 C C   . TRP B 1058 ? 0.4753 0.2883 0.3991 0.0561  -0.0340 0.0041  1056 TRP B C   
16792 O O   . TRP B 1058 ? 0.4724 0.2724 0.3898 0.0552  -0.0365 0.0063  1056 TRP B O   
16793 C CB  . TRP B 1058 ? 0.4499 0.2655 0.3777 0.0518  -0.0339 -0.0008 1056 TRP B CB  
16794 C CG  . TRP B 1058 ? 0.5235 0.3285 0.4487 0.0446  -0.0361 0.0016  1056 TRP B CG  
16795 C CD1 . TRP B 1058 ? 0.5542 0.3435 0.4720 0.0437  -0.0397 0.0008  1056 TRP B CD1 
16796 C CD2 . TRP B 1058 ? 0.4648 0.2742 0.3946 0.0370  -0.0348 0.0052  1056 TRP B CD2 
16797 N NE1 . TRP B 1058 ? 0.5617 0.3457 0.4796 0.0357  -0.0408 0.0039  1056 TRP B NE1 
16798 C CE2 . TRP B 1058 ? 0.5848 0.3814 0.5101 0.0315  -0.0377 0.0066  1056 TRP B CE2 
16799 C CE3 . TRP B 1058 ? 0.4566 0.2797 0.3937 0.0343  -0.0315 0.0073  1056 TRP B CE3 
16800 C CZ2 . TRP B 1058 ? 0.5280 0.3259 0.4564 0.0235  -0.0372 0.0102  1056 TRP B CZ2 
16801 C CZ3 . TRP B 1058 ? 0.4888 0.3128 0.4286 0.0267  -0.0310 0.0106  1056 TRP B CZ3 
16802 C CH2 . TRP B 1058 ? 0.4940 0.3059 0.4296 0.0214  -0.0337 0.0121  1056 TRP B CH2 
16803 N N   . LEU B 1059 ? 0.4284 0.2557 0.3593 0.0547  -0.0308 0.0055  1057 LEU B N   
16804 C CA  . LEU B 1059 ? 0.4931 0.3217 0.4244 0.0525  -0.0301 0.0095  1057 LEU B CA  
16805 C C   . LEU B 1059 ? 0.5379 0.3600 0.4630 0.0593  -0.0317 0.0103  1057 LEU B C   
16806 O O   . LEU B 1059 ? 0.5110 0.3243 0.4315 0.0576  -0.0333 0.0135  1057 LEU B O   
16807 C CB  . LEU B 1059 ? 0.3945 0.2400 0.3343 0.0506  -0.0265 0.0103  1057 LEU B CB  
16808 C CG  . LEU B 1059 ? 0.4222 0.2747 0.3684 0.0435  -0.0247 0.0102  1057 LEU B CG  
16809 C CD1 . LEU B 1059 ? 0.3823 0.2508 0.3360 0.0432  -0.0214 0.0102  1057 LEU B CD1 
16810 C CD2 . LEU B 1059 ? 0.4537 0.2994 0.3986 0.0363  -0.0256 0.0136  1057 LEU B CD2 
16811 N N   . ASP B 1060 ? 0.4876 0.3141 0.4124 0.0670  -0.0315 0.0075  1058 ASP B N   
16812 C CA  . ASP B 1060 ? 0.5238 0.3440 0.4425 0.0745  -0.0333 0.0077  1058 ASP B CA  
16813 C C   . ASP B 1060 ? 0.5699 0.3708 0.4792 0.0747  -0.0371 0.0084  1058 ASP B C   
16814 O O   . ASP B 1060 ? 0.6050 0.3978 0.5091 0.0762  -0.0389 0.0111  1058 ASP B O   
16815 C CB  . ASP B 1060 ? 0.5977 0.4243 0.5171 0.0826  -0.0327 0.0039  1058 ASP B CB  
16816 C CG  . ASP B 1060 ? 0.5895 0.4342 0.5167 0.0840  -0.0294 0.0037  1058 ASP B CG  
16817 O OD1 . ASP B 1060 ? 0.5372 0.3878 0.4671 0.0819  -0.0282 0.0067  1058 ASP B OD1 
16818 O OD2 . ASP B 1060 ? 0.5767 0.4297 0.5070 0.0873  -0.0280 0.0005  1058 ASP B OD2 
16819 N N   . GLY B 1061 ? 0.5210 0.3139 0.4277 0.0734  -0.0387 0.0058  1059 GLY B N   
16820 C CA  . GLY B 1061 ? 0.5916 0.3654 0.4889 0.0736  -0.0427 0.0061  1059 GLY B CA  
16821 C C   . GLY B 1061 ? 0.6581 0.4235 0.5532 0.0661  -0.0439 0.0105  1059 GLY B C   
16822 O O   . GLY B 1061 ? 0.6361 0.3860 0.5228 0.0669  -0.0471 0.0121  1059 GLY B O   
16823 N N   . LYS B 1062 ? 0.6006 0.3762 0.5029 0.0587  -0.0413 0.0127  1060 LYS B N   
16824 C CA  . LYS B 1062 ? 0.6255 0.3958 0.5267 0.0511  -0.0418 0.0172  1060 LYS B CA  
16825 C C   . LYS B 1062 ? 0.6371 0.4104 0.5378 0.0527  -0.0409 0.0207  1060 LYS B C   
16826 O O   . LYS B 1062 ? 0.7055 0.4744 0.6046 0.0468  -0.0413 0.0247  1060 LYS B O   
16827 C CB  . LYS B 1062 ? 0.5920 0.3726 0.5013 0.0428  -0.0393 0.0178  1060 LYS B CB  
16828 C CG  . LYS B 1062 ? 0.6632 0.4391 0.5725 0.0394  -0.0406 0.0153  1060 LYS B CG  
16829 C CD  . LYS B 1062 ? 0.6203 0.4097 0.5388 0.0329  -0.0377 0.0155  1060 LYS B CD  
16830 C CE  . LYS B 1062 ? 0.6181 0.4116 0.5395 0.0265  -0.0361 0.0200  1060 LYS B CE  
16831 N NZ  . LYS B 1062 ? 0.6013 0.3836 0.5191 0.0191  -0.0384 0.0226  1060 LYS B NZ  
16832 N N   . GLY B 1063 ? 0.6366 0.4181 0.5387 0.0600  -0.0398 0.0195  1061 GLY B N   
16833 C CA  . GLY B 1063 ? 0.5879 0.3739 0.4903 0.0612  -0.0388 0.0227  1061 GLY B CA  
16834 C C   . GLY B 1063 ? 0.6583 0.4595 0.5691 0.0557  -0.0352 0.0246  1061 GLY B C   
16835 O O   . GLY B 1063 ? 0.6409 0.4457 0.5517 0.0556  -0.0344 0.0276  1061 GLY B O   
16836 N N   . ALA B 1064 ? 0.5537 0.3638 0.4713 0.0514  -0.0330 0.0228  1062 ALA B N   
16837 C CA  . ALA B 1064 ? 0.5523 0.3770 0.4778 0.0467  -0.0296 0.0241  1062 ALA B CA  
16838 C C   . ALA B 1064 ? 0.5958 0.4342 0.5260 0.0524  -0.0274 0.0222  1062 ALA B C   
16839 O O   . ALA B 1064 ? 0.4816 0.3307 0.4180 0.0526  -0.0254 0.0195  1062 ALA B O   
16840 C CB  . ALA B 1064 ? 0.5864 0.4150 0.5172 0.0403  -0.0284 0.0228  1062 ALA B CB  
16841 N N   . ARG B 1065 ? 0.5452 0.3831 0.4723 0.0570  -0.0280 0.0239  1063 ARG B N   
16842 C CA  . ARG B 1065 ? 0.5370 0.3858 0.4672 0.0635  -0.0268 0.0221  1063 ARG B CA  
16843 C C   . ARG B 1065 ? 0.5167 0.3817 0.4551 0.0604  -0.0234 0.0221  1063 ARG B C   
16844 O O   . ARG B 1065 ? 0.4707 0.3462 0.4140 0.0633  -0.0219 0.0193  1063 ARG B O   
16845 C CB  . ARG B 1065 ? 0.5705 0.4145 0.4951 0.0689  -0.0286 0.0242  1063 ARG B CB  
16846 N N   . ALA B 1066 ? 0.4451 0.3125 0.3851 0.0546  -0.0221 0.0253  1064 ALA B N   
16847 C CA  . ALA B 1066 ? 0.4182 0.3001 0.3655 0.0516  -0.0190 0.0252  1064 ALA B CA  
16848 C C   . ALA B 1066 ? 0.4365 0.3240 0.3894 0.0487  -0.0175 0.0223  1064 ALA B C   
16849 O O   . ALA B 1066 ? 0.4264 0.3258 0.3850 0.0496  -0.0155 0.0204  1064 ALA B O   
16850 C CB  . ALA B 1066 ? 0.5204 0.4028 0.4677 0.0458  -0.0179 0.0290  1064 ALA B CB  
16851 N N   . GLU B 1067 ? 0.4243 0.3032 0.3756 0.0449  -0.0186 0.0221  1065 GLU B N   
16852 C CA  . GLU B 1067 ? 0.3946 0.2784 0.3509 0.0419  -0.0174 0.0195  1065 GLU B CA  
16853 C C   . GLU B 1067 ? 0.3895 0.2755 0.3464 0.0475  -0.0178 0.0157  1065 GLU B C   
16854 O O   . GLU B 1067 ? 0.3835 0.2791 0.3459 0.0469  -0.0160 0.0135  1065 GLU B O   
16855 C CB  . GLU B 1067 ? 0.4607 0.3347 0.4149 0.0364  -0.0188 0.0204  1065 GLU B CB  
16856 C CG  . GLU B 1067 ? 0.3938 0.2689 0.3493 0.0296  -0.0177 0.0240  1065 GLU B CG  
16857 C CD  . GLU B 1067 ? 0.4694 0.3357 0.4187 0.0298  -0.0192 0.0275  1065 GLU B CD  
16858 O OE1 . GLU B 1067 ? 0.4777 0.3357 0.4211 0.0352  -0.0214 0.0272  1065 GLU B OE1 
16859 O OE2 . GLU B 1067 ? 0.4654 0.3331 0.4152 0.0246  -0.0181 0.0307  1065 GLU B OE2 
16860 N N   . ALA B 1068 ? 0.4128 0.2898 0.3637 0.0530  -0.0201 0.0149  1066 ALA B N   
16861 C CA  . ALA B 1068 ? 0.4285 0.3079 0.3795 0.0590  -0.0204 0.0112  1066 ALA B CA  
16862 C C   . ALA B 1068 ? 0.4090 0.3027 0.3650 0.0623  -0.0182 0.0104  1066 ALA B C   
16863 O O   . ALA B 1068 ? 0.3595 0.2609 0.3193 0.0640  -0.0170 0.0076  1066 ALA B O   
16864 C CB  . ALA B 1068 ? 0.4246 0.2918 0.3679 0.0648  -0.0233 0.0107  1066 ALA B CB  
16865 N N   . GLU B 1069 ? 0.3999 0.2972 0.3559 0.0632  -0.0178 0.0129  1067 GLU B N   
16866 C CA  . GLU B 1069 ? 0.4277 0.3387 0.3886 0.0655  -0.0158 0.0124  1067 GLU B CA  
16867 C C   . GLU B 1069 ? 0.4169 0.3382 0.3846 0.0602  -0.0133 0.0119  1067 GLU B C   
16868 O O   . GLU B 1069 ? 0.3747 0.3060 0.3468 0.0618  -0.0118 0.0098  1067 GLU B O   
16869 C CB  . GLU B 1069 ? 0.4705 0.3821 0.4294 0.0670  -0.0162 0.0154  1067 GLU B CB  
16870 C CG  . GLU B 1069 ? 0.4742 0.4000 0.4380 0.0685  -0.0144 0.0152  1067 GLU B CG  
16871 C CD  . GLU B 1069 ? 0.5924 0.5237 0.5568 0.0755  -0.0148 0.0129  1067 GLU B CD  
16872 O OE1 . GLU B 1069 ? 0.6375 0.5619 0.5984 0.0796  -0.0163 0.0111  1067 GLU B OE1 
16873 O OE2 . GLU B 1069 ? 0.6643 0.6070 0.6325 0.0769  -0.0136 0.0128  1067 GLU B OE2 
16874 N N   . ALA B 1070 ? 0.3721 0.2913 0.3408 0.0539  -0.0127 0.0138  1068 ALA B N   
16875 C CA  . ALA B 1070 ? 0.3976 0.3258 0.3725 0.0491  -0.0104 0.0132  1068 ALA B CA  
16876 C C   . ALA B 1070 ? 0.3171 0.2463 0.2941 0.0492  -0.0102 0.0100  1068 ALA B C   
16877 O O   . ALA B 1070 ? 0.3488 0.2877 0.3308 0.0483  -0.0085 0.0085  1068 ALA B O   
16878 C CB  . ALA B 1070 ? 0.4579 0.3830 0.4330 0.0427  -0.0099 0.0157  1068 ALA B CB  
16879 N N   . ALA B 1071 ? 0.3204 0.2393 0.2932 0.0503  -0.0122 0.0090  1069 ALA B N   
16880 C CA  . ALA B 1071 ? 0.2971 0.2165 0.2714 0.0505  -0.0122 0.0059  1069 ALA B CA  
16881 C C   . ALA B 1071 ? 0.3473 0.2746 0.3231 0.0560  -0.0115 0.0035  1069 ALA B C   
16882 O O   . ALA B 1071 ? 0.3268 0.2619 0.3069 0.0550  -0.0100 0.0017  1069 ALA B O   
16883 C CB  . ALA B 1071 ? 0.2985 0.2046 0.2673 0.0508  -0.0148 0.0053  1069 ALA B CB  
16884 N N   . ARG B 1072 ? 0.3166 0.2421 0.2889 0.0618  -0.0125 0.0036  1070 ARG B N   
16885 C CA  A ARG B 1072 ? 0.3189 0.2530 0.2930 0.0671  -0.0117 0.0015  1070 ARG B CA  
16886 C CA  B ARG B 1072 ? 0.3191 0.2532 0.2932 0.0671  -0.0116 0.0015  1070 ARG B CA  
16887 C C   . ARG B 1072 ? 0.3426 0.2902 0.3228 0.0651  -0.0093 0.0020  1070 ARG B C   
16888 O O   . ARG B 1072 ? 0.3103 0.2662 0.2939 0.0661  -0.0080 0.0000  1070 ARG B O   
16889 C CB  A ARG B 1072 ? 0.3187 0.2491 0.2882 0.0737  -0.0132 0.0018  1070 ARG B CB  
16890 C CB  B ARG B 1072 ? 0.3189 0.2495 0.2885 0.0737  -0.0132 0.0019  1070 ARG B CB  
16891 C CG  A ARG B 1072 ? 0.3592 0.2768 0.3222 0.0773  -0.0156 0.0005  1070 ARG B CG  
16892 C CG  B ARG B 1072 ? 0.3609 0.2782 0.3240 0.0766  -0.0156 0.0008  1070 ARG B CG  
16893 C CD  A ARG B 1072 ? 0.3941 0.3084 0.3525 0.0844  -0.0172 0.0008  1070 ARG B CD  
16894 C CD  B ARG B 1072 ? 0.3947 0.3090 0.3532 0.0842  -0.0171 0.0006  1070 ARG B CD  
16895 N NE  A ARG B 1072 ? 0.4236 0.3350 0.3803 0.0834  -0.0179 0.0041  1070 ARG B NE  
16896 N NE  B ARG B 1072 ? 0.4016 0.3051 0.3545 0.0877  -0.0190 -0.0017 1070 ARG B NE  
16897 C CZ  A ARG B 1072 ? 0.4174 0.3156 0.3680 0.0833  -0.0202 0.0059  1070 ARG B CZ  
16898 C CZ  B ARG B 1072 ? 0.3899 0.2788 0.3368 0.0866  -0.0215 -0.0009 1070 ARG B CZ  
16899 N NH1 A ARG B 1072 ? 0.3892 0.2751 0.3344 0.0845  -0.0222 0.0045  1070 ARG B NH1 
16900 N NH1 B ARG B 1072 ? 0.4607 0.3439 0.4060 0.0829  -0.0223 0.0024  1070 ARG B NH1 
16901 N NH2 A ARG B 1072 ? 0.3420 0.2388 0.2913 0.0819  -0.0205 0.0091  1070 ARG B NH2 
16902 N NH2 B ARG B 1072 ? 0.4265 0.3060 0.3686 0.0892  -0.0232 -0.0034 1070 ARG B NH2 
16903 N N   . ASN B 1073 ? 0.3080 0.2576 0.2894 0.0622  -0.0088 0.0046  1071 ASN B N   
16904 C CA  . ASN B 1073 ? 0.2896 0.2512 0.2764 0.0601  -0.0068 0.0050  1071 ASN B CA  
16905 C C   . ASN B 1073 ? 0.2917 0.2573 0.2827 0.0553  -0.0053 0.0038  1071 ASN B C   
16906 O O   . ASN B 1073 ? 0.3145 0.2896 0.3095 0.0551  -0.0039 0.0027  1071 ASN B O   
16907 C CB  . ASN B 1073 ? 0.3642 0.3260 0.3505 0.0580  -0.0066 0.0079  1071 ASN B CB  
16908 C CG  . ASN B 1073 ? 0.4151 0.3754 0.3979 0.0631  -0.0079 0.0091  1071 ASN B CG  
16909 O OD1 . ASN B 1073 ? 0.4543 0.4167 0.4363 0.0685  -0.0086 0.0076  1071 ASN B OD1 
16910 N ND2 . ASN B 1073 ? 0.4582 0.4153 0.4388 0.0616  -0.0084 0.0119  1071 ASN B ND2 
16911 N N   . ALA B 1074 ? 0.2984 0.2567 0.2885 0.0514  -0.0058 0.0040  1072 ALA B N   
16912 C CA  . ALA B 1074 ? 0.3216 0.2832 0.3155 0.0474  -0.0047 0.0027  1072 ALA B CA  
16913 C C   . ALA B 1074 ? 0.2487 0.2125 0.2431 0.0501  -0.0048 -0.0001 1072 ALA B C   
16914 O O   . ALA B 1074 ? 0.2554 0.2266 0.2536 0.0486  -0.0034 -0.0013 1072 ALA B O   
16915 C CB  . ALA B 1074 ? 0.3070 0.2604 0.2997 0.0430  -0.0055 0.0036  1072 ALA B CB  
16916 N N   . GLY B 1075 ? 0.2577 0.2145 0.2478 0.0541  -0.0063 -0.0012 1073 GLY B N   
16917 C CA  . GLY B 1075 ? 0.3044 0.2634 0.2943 0.0571  -0.0062 -0.0040 1073 GLY B CA  
16918 C C   . GLY B 1075 ? 0.3128 0.2836 0.3061 0.0594  -0.0047 -0.0047 1073 GLY B C   
16919 O O   . GLY B 1075 ? 0.3154 0.2919 0.3112 0.0590  -0.0037 -0.0064 1073 GLY B O   
16920 N N   . SER B 1076 ? 0.3093 0.2841 0.3028 0.0616  -0.0045 -0.0032 1074 SER B N   
16921 C CA  . SER B 1076 ? 0.2748 0.2611 0.2715 0.0637  -0.0032 -0.0036 1074 SER B CA  
16922 C C   . SER B 1076 ? 0.3157 0.3100 0.3174 0.0588  -0.0016 -0.0030 1074 SER B C   
16923 O O   . SER B 1076 ? 0.3308 0.3332 0.3354 0.0586  -0.0005 -0.0042 1074 SER B O   
16924 C CB  . SER B 1076 ? 0.3087 0.2967 0.3039 0.0679  -0.0038 -0.0023 1074 SER B CB  
16925 O OG  . SER B 1076 ? 0.3568 0.3392 0.3477 0.0735  -0.0051 -0.0034 1074 SER B OG  
16926 N N   . SER B 1077 ? 0.2801 0.2723 0.2825 0.0548  -0.0015 -0.0012 1075 SER B N   
16927 C CA  . SER B 1077 ? 0.2882 0.2880 0.2948 0.0509  0.0000  -0.0007 1075 SER B CA  
16928 C C   . SER B 1077 ? 0.2745 0.2742 0.2833 0.0471  0.0006  -0.0019 1075 SER B C   
16929 O O   . SER B 1077 ? 0.3011 0.3074 0.3132 0.0446  0.0017  -0.0021 1075 SER B O   
16930 C CB  . SER B 1077 ? 0.3803 0.3789 0.3867 0.0485  0.0000  0.0017  1075 SER B CB  
16931 O OG  . SER B 1077 ? 0.3485 0.3398 0.3540 0.0451  -0.0003 0.0024  1075 SER B OG  
16932 N N   . SER B 1078 ? 0.2427 0.2347 0.2494 0.0468  -0.0003 -0.0028 1076 SER B N   
16933 C CA  . SER B 1078 ? 0.2333 0.2254 0.2420 0.0437  0.0001  -0.0041 1076 SER B CA  
16934 C C   . SER B 1078 ? 0.2005 0.2003 0.2111 0.0449  0.0010  -0.0057 1076 SER B C   
16935 O O   . SER B 1078 ? 0.2309 0.2332 0.2403 0.0489  0.0009  -0.0065 1076 SER B O   
16936 C CB  . SER B 1078 ? 0.2359 0.2187 0.2413 0.0442  -0.0014 -0.0052 1076 SER B CB  
16937 O OG  . SER B 1078 ? 0.2264 0.2098 0.2335 0.0420  -0.0012 -0.0067 1076 SER B OG  
16938 N N   . ALA B 1079 ? 0.2018 0.2056 0.2156 0.0414  0.0018  -0.0061 1077 ALA B N   
16939 C CA  . ALA B 1079 ? 0.1954 0.2057 0.2108 0.0417  0.0026  -0.0074 1077 ALA B CA  
16940 C C   . ALA B 1079 ? 0.2044 0.2113 0.2190 0.0411  0.0021  -0.0091 1077 ALA B C   
16941 O O   . ALA B 1079 ? 0.2085 0.2202 0.2245 0.0404  0.0027  -0.0100 1077 ALA B O   
16942 C CB  . ALA B 1079 ? 0.2099 0.2269 0.2286 0.0386  0.0036  -0.0067 1077 ALA B CB  
16943 N N   . LEU B 1080 ? 0.2051 0.2038 0.2174 0.0410  0.0009  -0.0094 1078 LEU B N   
16944 C CA  . LEU B 1080 ? 0.2072 0.2021 0.2182 0.0409  0.0002  -0.0112 1078 LEU B CA  
16945 C C   . LEU B 1080 ? 0.1866 0.1851 0.1961 0.0445  0.0006  -0.0127 1078 LEU B C   
16946 O O   . LEU B 1080 ? 0.2008 0.1992 0.2081 0.0486  0.0005  -0.0129 1078 LEU B O   
16947 C CB  . LEU B 1080 ? 0.2178 0.2027 0.2255 0.0411  -0.0014 -0.0113 1078 LEU B CB  
16948 C CG  . LEU B 1080 ? 0.2328 0.2127 0.2380 0.0417  -0.0026 -0.0133 1078 LEU B CG  
16949 C CD1 . LEU B 1080 ? 0.2258 0.2067 0.2338 0.0374  -0.0026 -0.0136 1078 LEU B CD1 
16950 C CD2 . LEU B 1080 ? 0.2441 0.2137 0.2450 0.0431  -0.0044 -0.0135 1078 LEU B CD2 
16951 N N   . GLY B 1081 ? 0.1956 0.1972 0.2061 0.0432  0.0010  -0.0139 1079 GLY B N   
16952 C CA  . GLY B 1081 ? 0.2064 0.2122 0.2155 0.0462  0.0016  -0.0152 1079 GLY B CA  
16953 C C   . GLY B 1081 ? 0.2066 0.2224 0.2186 0.0457  0.0031  -0.0146 1079 GLY B C   
16954 O O   . GLY B 1081 ? 0.2353 0.2559 0.2465 0.0477  0.0039  -0.0155 1079 GLY B O   
16955 N N   . LEU B 1082 ? 0.2082 0.2271 0.2231 0.0430  0.0036  -0.0130 1080 LEU B N   
16956 C CA  A LEU B 1082 ? 0.2055 0.2331 0.2230 0.0416  0.0047  -0.0123 1080 LEU B CA  
16957 C CA  B LEU B 1082 ? 0.2054 0.2330 0.2229 0.0416  0.0047  -0.0123 1080 LEU B CA  
16958 C C   . LEU B 1082 ? 0.2095 0.2390 0.2273 0.0396  0.0050  -0.0132 1080 LEU B C   
16959 O O   . LEU B 1082 ? 0.2199 0.2446 0.2374 0.0375  0.0043  -0.0138 1080 LEU B O   
16960 C CB  A LEU B 1082 ? 0.2040 0.2327 0.2241 0.0384  0.0049  -0.0108 1080 LEU B CB  
16961 C CB  B LEU B 1082 ? 0.2040 0.2327 0.2241 0.0384  0.0049  -0.0108 1080 LEU B CB  
16962 C CG  A LEU B 1082 ? 0.1998 0.2363 0.2224 0.0363  0.0057  -0.0100 1080 LEU B CG  
16963 C CG  B LEU B 1082 ? 0.2000 0.2363 0.2225 0.0362  0.0057  -0.0100 1080 LEU B CG  
16964 C CD1 A LEU B 1082 ? 0.2163 0.2597 0.2389 0.0392  0.0063  -0.0098 1080 LEU B CD1 
16965 C CD1 B LEU B 1082 ? 0.2054 0.2423 0.2293 0.0350  0.0057  -0.0086 1080 LEU B CD1 
16966 C CD2 A LEU B 1082 ? 0.2157 0.2521 0.2400 0.0339  0.0057  -0.0087 1080 LEU B CD2 
16967 C CD2 B LEU B 1082 ? 0.1830 0.2194 0.2066 0.0327  0.0057  -0.0105 1080 LEU B CD2 
16968 N N   . ASP B 1083 ? 0.2053 0.2422 0.2235 0.0403  0.0060  -0.0133 1081 ASP B N   
16969 C CA  . ASP B 1083 ? 0.2334 0.2721 0.2512 0.0388  0.0063  -0.0141 1081 ASP B CA  
16970 C C   . ASP B 1083 ? 0.2482 0.2960 0.2678 0.0375  0.0074  -0.0131 1081 ASP B C   
16971 O O   . ASP B 1083 ? 0.3171 0.3707 0.3363 0.0401  0.0082  -0.0132 1081 ASP B O   
16972 C CB  . ASP B 1083 ? 0.2732 0.3095 0.2876 0.0423  0.0062  -0.0157 1081 ASP B CB  
16973 C CG  . ASP B 1083 ? 0.4416 0.4794 0.4549 0.0409  0.0064  -0.0165 1081 ASP B CG  
16974 O OD1 . ASP B 1083 ? 0.4689 0.5066 0.4836 0.0371  0.0062  -0.0160 1081 ASP B OD1 
16975 O OD2 . ASP B 1083 ? 0.5150 0.5539 0.5258 0.0439  0.0068  -0.0177 1081 ASP B OD2 
16976 N N   . LEU B 1084 ? 0.2228 0.2717 0.2444 0.0335  0.0073  -0.0122 1082 LEU B N   
16977 C CA  . LEU B 1084 ? 0.2241 0.2806 0.2474 0.0315  0.0079  -0.0110 1082 LEU B CA  
16978 C C   . LEU B 1084 ? 0.2089 0.2665 0.2319 0.0283  0.0080  -0.0110 1082 LEU B C   
16979 O O   . LEU B 1084 ? 0.2322 0.2841 0.2544 0.0268  0.0072  -0.0116 1082 LEU B O   
16980 C CB  . LEU B 1084 ? 0.2519 0.3084 0.2773 0.0295  0.0076  -0.0099 1082 LEU B CB  
16981 C CG  . LEU B 1084 ? 0.2957 0.3517 0.3215 0.0320  0.0075  -0.0095 1082 LEU B CG  
16982 C CD1 . LEU B 1084 ? 0.3223 0.3783 0.3497 0.0295  0.0072  -0.0084 1082 LEU B CD1 
16983 C CD2 . LEU B 1084 ? 0.3918 0.4548 0.4177 0.0352  0.0081  -0.0092 1082 LEU B CD2 
16984 N N   . GLU B 1085 ? 0.2206 0.2856 0.2442 0.0272  0.0087  -0.0102 1083 GLU B N   
16985 C CA  . GLU B 1085 ? 0.2135 0.2796 0.2368 0.0233  0.0086  -0.0096 1083 GLU B CA  
16986 C C   . GLU B 1085 ? 0.2232 0.2913 0.2484 0.0202  0.0082  -0.0084 1083 GLU B C   
16987 O O   . GLU B 1085 ? 0.2415 0.3155 0.2682 0.0206  0.0086  -0.0076 1083 GLU B O   
16988 C CB  . GLU B 1085 ? 0.2175 0.2901 0.2398 0.0233  0.0096  -0.0094 1083 GLU B CB  
16989 C CG  . GLU B 1085 ? 0.2473 0.3196 0.2688 0.0189  0.0091  -0.0086 1083 GLU B CG  
16990 C CD  . GLU B 1085 ? 0.3410 0.4184 0.3609 0.0184  0.0101  -0.0083 1083 GLU B CD  
16991 O OE1 . GLU B 1085 ? 0.3461 0.4268 0.3651 0.0219  0.0111  -0.0090 1083 GLU B OE1 
16992 O OE2 . GLU B 1085 ? 0.3461 0.4238 0.3651 0.0146  0.0097  -0.0073 1083 GLU B OE2 
16993 N N   . LEU B 1086 ? 0.1919 0.2552 0.2169 0.0173  0.0073  -0.0083 1084 LEU B N   
16994 C CA  . LEU B 1086 ? 0.1960 0.2598 0.2222 0.0144  0.0067  -0.0075 1084 LEU B CA  
16995 C C   . LEU B 1086 ? 0.2696 0.3371 0.2952 0.0109  0.0065  -0.0065 1084 LEU B C   
16996 O O   . LEU B 1086 ? 0.2360 0.3023 0.2599 0.0098  0.0065  -0.0066 1084 LEU B O   
16997 C CB  . LEU B 1086 ? 0.2341 0.2906 0.2603 0.0135  0.0058  -0.0080 1084 LEU B CB  
16998 C CG  . LEU B 1086 ? 0.2388 0.2911 0.2656 0.0161  0.0058  -0.0087 1084 LEU B CG  
16999 C CD1 . LEU B 1086 ? 0.2209 0.2675 0.2481 0.0147  0.0050  -0.0091 1084 LEU B CD1 
17000 C CD2 . LEU B 1086 ? 0.2585 0.3145 0.2865 0.0177  0.0063  -0.0082 1084 LEU B CD2 
17001 N N   . PRO B 1087 ? 0.2183 0.2897 0.2448 0.0088  0.0063  -0.0055 1085 PRO B N   
17002 C CA  . PRO B 1087 ? 0.2373 0.3117 0.2629 0.0048  0.0059  -0.0044 1085 PRO B CA  
17003 C C   . PRO B 1087 ? 0.2031 0.2704 0.2269 0.0023  0.0047  -0.0046 1085 PRO B C   
17004 O O   . PRO B 1087 ? 0.2582 0.3196 0.2821 0.0026  0.0040  -0.0054 1085 PRO B O   
17005 C CB  . PRO B 1087 ? 0.2719 0.3507 0.2990 0.0034  0.0055  -0.0036 1085 PRO B CB  
17006 C CG  . PRO B 1087 ? 0.3248 0.4057 0.3536 0.0073  0.0062  -0.0040 1085 PRO B CG  
17007 C CD  . PRO B 1087 ? 0.2595 0.3334 0.2878 0.0100  0.0064  -0.0053 1085 PRO B CD  
17008 N N   . GLY B 1088 ? 0.2125 0.2805 0.2345 -0.0003 0.0045  -0.0039 1086 GLY B N   
17009 C CA  . GLY B 1088 ? 0.2089 0.2700 0.2285 -0.0025 0.0032  -0.0040 1086 GLY B CA  
17010 C C   . GLY B 1088 ? 0.1789 0.2422 0.1963 -0.0058 0.0031  -0.0027 1086 GLY B C   
17011 O O   . GLY B 1088 ? 0.2231 0.2938 0.2411 -0.0070 0.0039  -0.0016 1086 GLY B O   
17012 N N   . PRO B 1089 ? 0.2119 0.2690 0.2267 -0.0072 0.0020  -0.0028 1087 PRO B N   
17013 C CA  . PRO B 1089 ? 0.2219 0.2801 0.2340 -0.0107 0.0016  -0.0013 1087 PRO B CA  
17014 C C   . PRO B 1089 ? 0.2055 0.2693 0.2173 -0.0095 0.0032  -0.0009 1087 PRO B C   
17015 O O   . PRO B 1089 ? 0.2486 0.3126 0.2612 -0.0057 0.0041  -0.0022 1087 PRO B O   
17016 C CB  . PRO B 1089 ? 0.2355 0.2846 0.2449 -0.0115 -0.0001 -0.0017 1087 PRO B CB  
17017 C CG  . PRO B 1089 ? 0.2828 0.3282 0.2939 -0.0074 0.0001  -0.0036 1087 PRO B CG  
17018 C CD  . PRO B 1089 ? 0.2469 0.2961 0.2612 -0.0055 0.0010  -0.0041 1087 PRO B CD  
17019 N N   . VAL B 1090 ? 0.1982 0.2663 0.2083 -0.0129 0.0034  0.0008  1088 VAL B N   
17020 C CA  . VAL B 1090 ? 0.1897 0.2626 0.1985 -0.0121 0.0049  0.0012  1088 VAL B CA  
17021 C C   . VAL B 1090 ? 0.2073 0.2730 0.2133 -0.0107 0.0042  0.0004  1088 VAL B C   
17022 O O   . VAL B 1090 ? 0.2157 0.2732 0.2202 -0.0116 0.0024  0.0000  1088 VAL B O   
17023 C CB  . VAL B 1090 ? 0.2299 0.3090 0.2374 -0.0166 0.0053  0.0036  1088 VAL B CB  
17024 C CG1 . VAL B 1090 ? 0.2256 0.3121 0.2362 -0.0181 0.0057  0.0044  1088 VAL B CG1 
17025 C CG2 . VAL B 1090 ? 0.2539 0.3256 0.2576 -0.0209 0.0033  0.0048  1088 VAL B CG2 
17026 N N   . GLY B 1091 ? 0.2220 0.2909 0.2270 -0.0084 0.0056  -0.0001 1089 GLY B N   
17027 C CA  . GLY B 1091 ? 0.2192 0.2818 0.2213 -0.0072 0.0049  -0.0009 1089 GLY B CA  
17028 C C   . GLY B 1091 ? 0.2118 0.2683 0.2153 -0.0036 0.0041  -0.0030 1089 GLY B C   
17029 O O   . GLY B 1091 ? 0.2105 0.2609 0.2118 -0.0029 0.0030  -0.0037 1089 GLY B O   
17030 N N   . GLU B 1092 ? 0.2092 0.2673 0.2161 -0.0014 0.0046  -0.0039 1090 GLU B N   
17031 C CA  . GLU B 1092 ? 0.2027 0.2555 0.2111 0.0018  0.0040  -0.0058 1090 GLU B CA  
17032 C C   . GLU B 1092 ? 0.2044 0.2619 0.2155 0.0049  0.0054  -0.0065 1090 GLU B C   
17033 O O   . GLU B 1092 ? 0.2312 0.2949 0.2439 0.0042  0.0063  -0.0056 1090 GLU B O   
17034 C CB  . GLU B 1092 ? 0.2393 0.2864 0.2487 0.0002  0.0024  -0.0058 1090 GLU B CB  
17035 C CG  . GLU B 1092 ? 0.3229 0.3631 0.3326 0.0020  0.0012  -0.0072 1090 GLU B CG  
17036 C CD  . GLU B 1092 ? 0.3223 0.3579 0.3327 0.0004  -0.0002 -0.0071 1090 GLU B CD  
17037 O OE1 . GLU B 1092 ? 0.2587 0.2958 0.2714 0.0004  0.0001  -0.0071 1090 GLU B OE1 
17038 O OE2 . GLU B 1092 ? 0.3358 0.3663 0.3442 -0.0008 -0.0017 -0.0071 1090 GLU B OE2 
17039 N N   . ARG B 1093 ? 0.1943 0.2490 0.2056 0.0084  0.0055  -0.0081 1091 ARG B N   
17040 C CA  . ARG B 1093 ? 0.1819 0.2390 0.1953 0.0117  0.0064  -0.0090 1091 ARG B CA  
17041 C C   . ARG B 1093 ? 0.2023 0.2530 0.2174 0.0126  0.0053  -0.0099 1091 ARG B C   
17042 O O   . ARG B 1093 ? 0.2021 0.2470 0.2162 0.0131  0.0043  -0.0109 1091 ARG B O   
17043 C CB  . ARG B 1093 ? 0.2421 0.3010 0.2539 0.0153  0.0075  -0.0101 1091 ARG B CB  
17044 C CG  . ARG B 1093 ? 0.3506 0.4178 0.3614 0.0152  0.0091  -0.0092 1091 ARG B CG  
17045 C CD  . ARG B 1093 ? 0.4213 0.4898 0.4302 0.0195  0.0101  -0.0107 1091 ARG B CD  
17046 N NE  . ARG B 1093 ? 0.5852 0.6536 0.5958 0.0233  0.0104  -0.0118 1091 ARG B NE  
17047 C CZ  . ARG B 1093 ? 0.6466 0.7085 0.6560 0.0263  0.0096  -0.0135 1091 ARG B CZ  
17048 N NH1 . ARG B 1093 ? 0.6688 0.7244 0.6757 0.0259  0.0086  -0.0145 1091 ARG B NH1 
17049 N NH2 . ARG B 1093 ? 0.6396 0.7013 0.6502 0.0296  0.0099  -0.0142 1091 ARG B NH2 
17050 N N   . ASN B 1094 ? 0.1743 0.2265 0.1919 0.0126  0.0055  -0.0095 1092 ASN B N   
17051 C CA  . ASN B 1094 ? 0.1815 0.2285 0.2007 0.0129  0.0046  -0.0101 1092 ASN B CA  
17052 C C   . ASN B 1094 ? 0.2001 0.2481 0.2208 0.0161  0.0053  -0.0106 1092 ASN B C   
17053 O O   . ASN B 1094 ? 0.2093 0.2624 0.2311 0.0166  0.0062  -0.0100 1092 ASN B O   
17054 C CB  . ASN B 1094 ? 0.1829 0.2298 0.2032 0.0100  0.0041  -0.0092 1092 ASN B CB  
17055 C CG  . ASN B 1094 ? 0.1776 0.2210 0.1961 0.0074  0.0029  -0.0089 1092 ASN B CG  
17056 O OD1 . ASN B 1094 ? 0.1977 0.2359 0.2159 0.0078  0.0019  -0.0097 1092 ASN B OD1 
17057 N ND2 . ASN B 1094 ? 0.2201 0.2665 0.2373 0.0047  0.0029  -0.0077 1092 ASN B ND2 
17058 N N   . LEU B 1095 ? 0.1842 0.2273 0.2044 0.0181  0.0049  -0.0118 1093 LEU B N   
17059 C CA  . LEU B 1095 ? 0.1788 0.2214 0.1992 0.0213  0.0053  -0.0124 1093 LEU B CA  
17060 C C   . LEU B 1095 ? 0.1759 0.2139 0.1980 0.0213  0.0047  -0.0125 1093 LEU B C   
17061 O O   . LEU B 1095 ? 0.1948 0.2289 0.2175 0.0196  0.0038  -0.0127 1093 LEU B O   
17062 C CB  . LEU B 1095 ? 0.1873 0.2275 0.2052 0.0237  0.0052  -0.0137 1093 LEU B CB  
17063 C CG  . LEU B 1095 ? 0.2380 0.2827 0.2539 0.0236  0.0060  -0.0136 1093 LEU B CG  
17064 C CD1 . LEU B 1095 ? 0.3303 0.3722 0.3433 0.0263  0.0058  -0.0151 1093 LEU B CD1 
17065 C CD2 . LEU B 1095 ? 0.2616 0.3143 0.2785 0.0242  0.0073  -0.0127 1093 LEU B CD2 
17066 N N   . TYR B 1096 ? 0.1644 0.2033 0.1872 0.0234  0.0052  -0.0123 1094 TYR B N   
17067 C CA  . TYR B 1096 ? 0.1875 0.2227 0.2117 0.0233  0.0048  -0.0121 1094 TYR B CA  
17068 C C   . TYR B 1096 ? 0.1861 0.2190 0.2092 0.0265  0.0048  -0.0125 1094 TYR B C   
17069 O O   . TYR B 1096 ? 0.1977 0.2343 0.2202 0.0288  0.0055  -0.0124 1094 TYR B O   
17070 C CB  . TYR B 1096 ? 0.1758 0.2144 0.2019 0.0219  0.0052  -0.0109 1094 TYR B CB  
17071 C CG  . TYR B 1096 ? 0.1692 0.2050 0.1964 0.0220  0.0050  -0.0105 1094 TYR B CG  
17072 C CD1 . TYR B 1096 ? 0.2077 0.2403 0.2360 0.0200  0.0046  -0.0105 1094 TYR B CD1 
17073 C CD2 . TYR B 1096 ? 0.2024 0.2391 0.2294 0.0242  0.0054  -0.0100 1094 TYR B CD2 
17074 C CE1 . TYR B 1096 ? 0.2002 0.2309 0.2296 0.0200  0.0047  -0.0100 1094 TYR B CE1 
17075 C CE2 . TYR B 1096 ? 0.2124 0.2466 0.2402 0.0241  0.0053  -0.0094 1094 TYR B CE2 
17076 C CZ  . TYR B 1096 ? 0.2119 0.2433 0.2409 0.0219  0.0051  -0.0094 1094 TYR B CZ  
17077 O OH  . TYR B 1096 ? 0.2074 0.2368 0.2370 0.0216  0.0052  -0.0086 1094 TYR B OH  
17078 N N   . THR B 1097 ? 0.1817 0.2085 0.2044 0.0267  0.0040  -0.0131 1095 THR B N   
17079 C CA  . THR B 1097 ? 0.1812 0.2042 0.2020 0.0296  0.0036  -0.0137 1095 THR B CA  
17080 C C   . THR B 1097 ? 0.1755 0.1933 0.1971 0.0287  0.0029  -0.0133 1095 THR B C   
17081 O O   . THR B 1097 ? 0.2028 0.2192 0.2263 0.0260  0.0026  -0.0130 1095 THR B O   
17082 C CB  . THR B 1097 ? 0.2278 0.2477 0.2460 0.0308  0.0030  -0.0153 1095 THR B CB  
17083 O OG1 . THR B 1097 ? 0.2878 0.3040 0.3066 0.0282  0.0020  -0.0157 1095 THR B OG1 
17084 C CG2 . THR B 1097 ? 0.2527 0.2781 0.2699 0.0316  0.0038  -0.0156 1095 THR B CG2 
17085 N N   . LEU B 1098 ? 0.2000 0.2152 0.2203 0.0311  0.0028  -0.0131 1096 LEU B N   
17086 C CA  . LEU B 1098 ? 0.2059 0.2160 0.2265 0.0302  0.0022  -0.0124 1096 LEU B CA  
17087 C C   . LEU B 1098 ? 0.2033 0.2064 0.2210 0.0316  0.0009  -0.0134 1096 LEU B C   
17088 O O   . LEU B 1098 ? 0.1980 0.1999 0.2130 0.0350  0.0008  -0.0140 1096 LEU B O   
17089 C CB  . LEU B 1098 ? 0.1820 0.1938 0.2029 0.0312  0.0028  -0.0110 1096 LEU B CB  
17090 C CG  . LEU B 1098 ? 0.1773 0.1953 0.2007 0.0296  0.0037  -0.0100 1096 LEU B CG  
17091 C CD1 . LEU B 1098 ? 0.1896 0.2086 0.2128 0.0310  0.0041  -0.0086 1096 LEU B CD1 
17092 C CD2 . LEU B 1098 ? 0.1951 0.2126 0.2207 0.0261  0.0037  -0.0097 1096 LEU B CD2 
17093 N N   . HIS B 1099 ? 0.2020 0.2007 0.2204 0.0292  0.0000  -0.0135 1097 HIS B N   
17094 C CA  . HIS B 1099 ? 0.2085 0.2000 0.2243 0.0295  -0.0016 -0.0145 1097 HIS B CA  
17095 C C   . HIS B 1099 ? 0.1928 0.1796 0.2091 0.0278  -0.0022 -0.0132 1097 HIS B C   
17096 O O   . HIS B 1099 ? 0.2209 0.2105 0.2397 0.0262  -0.0014 -0.0117 1097 HIS B O   
17097 C CB  . HIS B 1099 ? 0.2498 0.2406 0.2663 0.0276  -0.0024 -0.0157 1097 HIS B CB  
17098 C CG  . HIS B 1099 ? 0.2788 0.2739 0.2945 0.0288  -0.0018 -0.0167 1097 HIS B CG  
17099 N ND1 . HIS B 1099 ? 0.3149 0.3076 0.3271 0.0310  -0.0025 -0.0183 1097 HIS B ND1 
17100 C CD2 . HIS B 1099 ? 0.2975 0.2990 0.3151 0.0280  -0.0006 -0.0162 1097 HIS B CD2 
17101 C CE1 . HIS B 1099 ? 0.3425 0.3405 0.3547 0.0314  -0.0016 -0.0187 1097 HIS B CE1 
17102 N NE2 . HIS B 1099 ? 0.3189 0.3221 0.3344 0.0295  -0.0005 -0.0174 1097 HIS B NE2 
17103 N N   . ALA B 1100 ? 0.2530 0.2324 0.2666 0.0280  -0.0038 -0.0138 1098 ALA B N   
17104 C CA  . ALA B 1100 ? 0.2464 0.2212 0.2606 0.0255  -0.0046 -0.0125 1098 ALA B CA  
17105 C C   . ALA B 1100 ? 0.2708 0.2485 0.2891 0.0214  -0.0045 -0.0120 1098 ALA B C   
17106 O O   . ALA B 1100 ? 0.2935 0.2738 0.3131 0.0207  -0.0046 -0.0132 1098 ALA B O   
17107 C CB  . ALA B 1100 ? 0.2858 0.2516 0.2959 0.0260  -0.0067 -0.0134 1098 ALA B CB  
17108 N N   . ARG B 1101 ? 0.2665 0.2442 0.2868 0.0190  -0.0041 -0.0102 1099 ARG B N   
17109 C CA  . ARG B 1101 ? 0.2367 0.2173 0.2610 0.0154  -0.0040 -0.0098 1099 ARG B CA  
17110 C C   . ARG B 1101 ? 0.2604 0.2362 0.2844 0.0133  -0.0060 -0.0106 1099 ARG B C   
17111 O O   . ARG B 1101 ? 0.2854 0.2641 0.3122 0.0114  -0.0064 -0.0112 1099 ARG B O   
17112 C CB  . ARG B 1101 ? 0.2845 0.2669 0.3108 0.0134  -0.0029 -0.0076 1099 ARG B CB  
17113 C CG  . ARG B 1101 ? 0.3019 0.2910 0.3301 0.0143  -0.0010 -0.0070 1099 ARG B CG  
17114 C CD  . ARG B 1101 ? 0.3279 0.3224 0.3603 0.0118  -0.0002 -0.0069 1099 ARG B CD  
17115 N NE  . ARG B 1101 ? 0.3291 0.3292 0.3627 0.0127  0.0014  -0.0065 1099 ARG B NE  
17116 C CZ  . ARG B 1101 ? 0.2953 0.2999 0.3319 0.0111  0.0024  -0.0062 1099 ARG B CZ  
17117 N NH1 . ARG B 1101 ? 0.3109 0.3161 0.3501 0.0088  0.0020  -0.0062 1099 ARG B NH1 
17118 N NH2 . ARG B 1101 ? 0.4005 0.4091 0.4372 0.0120  0.0036  -0.0059 1099 ARG B NH2 
17119 N N   . GLY B 1102 ? 0.2593 0.2278 0.2798 0.0135  -0.0075 -0.0105 1100 GLY B N   
17120 C CA  . GLY B 1102 ? 0.2677 0.2310 0.2877 0.0110  -0.0096 -0.0111 1100 GLY B CA  
17121 C C   . GLY B 1102 ? 0.2635 0.2204 0.2817 0.0092  -0.0106 -0.0095 1100 GLY B C   
17122 O O   . GLY B 1102 ? 0.2609 0.2127 0.2749 0.0116  -0.0108 -0.0092 1100 GLY B O   
17123 N N   . ARG B 1103 ? 0.2491 0.2061 0.2701 0.0049  -0.0112 -0.0084 1101 ARG B N   
17124 C CA  . ARG B 1103 ? 0.2619 0.2130 0.2812 0.0024  -0.0122 -0.0065 1101 ARG B CA  
17125 C C   . ARG B 1103 ? 0.2708 0.2275 0.2937 0.0004  -0.0101 -0.0040 1101 ARG B C   
17126 O O   . ARG B 1103 ? 0.2808 0.2448 0.3086 -0.0017 -0.0090 -0.0037 1101 ARG B O   
17127 C CB  . ARG B 1103 ? 0.2902 0.2369 0.3098 -0.0015 -0.0146 -0.0068 1101 ARG B CB  
17128 C CG  . ARG B 1103 ? 0.3020 0.2408 0.3186 -0.0042 -0.0159 -0.0048 1101 ARG B CG  
17129 C CD  . ARG B 1103 ? 0.3628 0.2956 0.3785 -0.0080 -0.0189 -0.0053 1101 ARG B CD  
17130 N NE  . ARG B 1103 ? 0.3859 0.3127 0.3974 -0.0054 -0.0210 -0.0081 1101 ARG B NE  
17131 C CZ  . ARG B 1103 ? 0.5563 0.4727 0.5613 -0.0035 -0.0230 -0.0090 1101 ARG B CZ  
17132 N NH1 . ARG B 1103 ? 0.4182 0.3279 0.4197 -0.0039 -0.0234 -0.0071 1101 ARG B NH1 
17133 N NH2 . ARG B 1103 ? 0.4302 0.3424 0.4316 -0.0011 -0.0247 -0.0118 1101 ARG B NH2 
17134 N N   . ILE B 1104 ? 0.2376 0.1909 0.2576 0.0013  -0.0095 -0.0023 1102 ILE B N   
17135 C CA  . ILE B 1104 ? 0.2454 0.2036 0.2678 -0.0001 -0.0075 0.0001  1102 ILE B CA  
17136 C C   . ILE B 1104 ? 0.2597 0.2139 0.2819 -0.0046 -0.0083 0.0024  1102 ILE B C   
17137 O O   . ILE B 1104 ? 0.2559 0.2009 0.2736 -0.0050 -0.0103 0.0028  1102 ILE B O   
17138 C CB  . ILE B 1104 ? 0.2438 0.2015 0.2632 0.0037  -0.0063 0.0006  1102 ILE B CB  
17139 C CG1 . ILE B 1104 ? 0.2522 0.2137 0.2715 0.0079  -0.0057 -0.0017 1102 ILE B CG1 
17140 C CG2 . ILE B 1104 ? 0.2402 0.2032 0.2617 0.0022  -0.0042 0.0030  1102 ILE B CG2 
17141 C CD1 . ILE B 1104 ? 0.2659 0.2364 0.2900 0.0073  -0.0042 -0.0024 1102 ILE B CD1 
17142 N N   . LEU B 1105 ? 0.2343 0.1952 0.2612 -0.0080 -0.0069 0.0039  1103 LEU B N   
17143 C CA  . LEU B 1105 ? 0.2620 0.2207 0.2891 -0.0125 -0.0072 0.0065  1103 LEU B CA  
17144 C C   . LEU B 1105 ? 0.2548 0.2110 0.2786 -0.0117 -0.0061 0.0089  1103 LEU B C   
17145 O O   . LEU B 1105 ? 0.2517 0.2140 0.2769 -0.0098 -0.0039 0.0094  1103 LEU B O   
17146 C CB  . LEU B 1105 ? 0.2412 0.2093 0.2747 -0.0160 -0.0058 0.0072  1103 LEU B CB  
17147 C CG  . LEU B 1105 ? 0.2652 0.2338 0.3000 -0.0211 -0.0055 0.0103  1103 LEU B CG  
17148 C CD1 . LEU B 1105 ? 0.2719 0.2323 0.3046 -0.0247 -0.0084 0.0107  1103 LEU B CD1 
17149 C CD2 . LEU B 1105 ? 0.2718 0.2515 0.3131 -0.0232 -0.0035 0.0107  1103 LEU B CD2 
17150 N N   . LEU B 1106 ? 0.2524 0.1991 0.2716 -0.0130 -0.0079 0.0104  1104 LEU B N   
17151 C CA  . LEU B 1106 ? 0.2473 0.1903 0.2626 -0.0124 -0.0073 0.0128  1104 LEU B CA  
17152 C C   . LEU B 1106 ? 0.2557 0.1989 0.2722 -0.0181 -0.0070 0.0160  1104 LEU B C   
17153 O O   . LEU B 1106 ? 0.2887 0.2270 0.3048 -0.0220 -0.0090 0.0166  1104 LEU B O   
17154 C CB  . LEU B 1106 ? 0.2884 0.2200 0.2970 -0.0094 -0.0096 0.0124  1104 LEU B CB  
17155 C CG  . LEU B 1106 ? 0.3826 0.3144 0.3888 -0.0031 -0.0091 0.0106  1104 LEU B CG  
17156 C CD1 . LEU B 1106 ? 0.3273 0.2677 0.3378 -0.0009 -0.0079 0.0079  1104 LEU B CD1 
17157 C CD2 . LEU B 1106 ? 0.2822 0.2026 0.2820 -0.0002 -0.0118 0.0095  1104 LEU B CD2 
17158 N N   . VAL B 1107 ? 0.2600 0.2093 0.2781 -0.0186 -0.0045 0.0182  1105 VAL B N   
17159 C CA  . VAL B 1107 ? 0.2684 0.2186 0.2873 -0.0239 -0.0038 0.0215  1105 VAL B CA  
17160 C C   . VAL B 1107 ? 0.2730 0.2181 0.2865 -0.0228 -0.0034 0.0241  1105 VAL B C   
17161 O O   . VAL B 1107 ? 0.2814 0.2330 0.2960 -0.0220 -0.0010 0.0253  1105 VAL B O   
17162 C CB  . VAL B 1107 ? 0.2380 0.2008 0.2635 -0.0260 -0.0011 0.0218  1105 VAL B CB  
17163 C CG1 . VAL B 1107 ? 0.2630 0.2272 0.2898 -0.0320 -0.0005 0.0252  1105 VAL B CG1 
17164 C CG2 . VAL B 1107 ? 0.2484 0.2165 0.2788 -0.0255 -0.0015 0.0188  1105 VAL B CG2 
17165 N N   . PRO B 1108 ? 0.2727 0.2061 0.2802 -0.0224 -0.0059 0.0249  1106 PRO B N   
17166 C CA  . PRO B 1108 ? 0.3047 0.2326 0.3068 -0.0211 -0.0058 0.0275  1106 PRO B CA  
17167 C C   . PRO B 1108 ? 0.3268 0.2539 0.3282 -0.0268 -0.0053 0.0315  1106 PRO B C   
17168 O O   . PRO B 1108 ? 0.3458 0.2741 0.3500 -0.0322 -0.0056 0.0325  1106 PRO B O   
17169 C CB  . PRO B 1108 ? 0.3170 0.2319 0.3126 -0.0183 -0.0091 0.0264  1106 PRO B CB  
17170 C CG  . PRO B 1108 ? 0.3289 0.2406 0.3261 -0.0219 -0.0111 0.0252  1106 PRO B CG  
17171 C CD  . PRO B 1108 ? 0.3034 0.2274 0.3082 -0.0226 -0.0091 0.0232  1106 PRO B CD  
17172 N N   . ALA B 1109 ? 0.3089 0.2336 0.3062 -0.0257 -0.0045 0.0340  1107 ALA B N   
17173 C CA  . ALA B 1109 ? 0.3514 0.2730 0.3462 -0.0307 -0.0043 0.0383  1107 ALA B CA  
17174 C C   . ALA B 1109 ? 0.4047 0.3119 0.3911 -0.0298 -0.0071 0.0401  1107 ALA B C   
17175 O O   . ALA B 1109 ? 0.3958 0.2960 0.3793 -0.0349 -0.0085 0.0431  1107 ALA B O   
17176 C CB  . ALA B 1109 ? 0.3366 0.2675 0.3329 -0.0306 -0.0010 0.0402  1107 ALA B CB  
17177 N N   . THR B 1110 ? 0.3417 0.2444 0.3243 -0.0235 -0.0081 0.0384  1108 THR B N   
17178 C CA  . THR B 1110 ? 0.3524 0.2417 0.3268 -0.0215 -0.0107 0.0400  1108 THR B CA  
17179 C C   . THR B 1110 ? 0.3583 0.2403 0.3301 -0.0163 -0.0133 0.0365  1108 THR B C   
17180 O O   . THR B 1110 ? 0.3341 0.2227 0.3100 -0.0132 -0.0125 0.0329  1108 THR B O   
17181 C CB  . THR B 1110 ? 0.4066 0.2974 0.3779 -0.0179 -0.0094 0.0419  1108 THR B CB  
17182 O OG1 . THR B 1110 ? 0.3984 0.2972 0.3726 -0.0121 -0.0081 0.0387  1108 THR B OG1 
17183 C CG2 . THR B 1110 ? 0.3792 0.2771 0.3523 -0.0228 -0.0068 0.0455  1108 THR B CG2 
17184 N N   . GLU B 1111 ? 0.3776 0.2456 0.3419 -0.0152 -0.0163 0.0375  1109 GLU B N   
17185 C CA  . GLU B 1111 ? 0.3783 0.2385 0.3390 -0.0098 -0.0188 0.0342  1109 GLU B CA  
17186 C C   . GLU B 1111 ? 0.3706 0.2378 0.3327 -0.0025 -0.0174 0.0317  1109 GLU B C   
17187 O O   . GLU B 1111 ? 0.3581 0.2283 0.3225 0.0010  -0.0175 0.0280  1109 GLU B O   
17188 C CB  . GLU B 1111 ? 0.4052 0.2489 0.3568 -0.0092 -0.0223 0.0360  1109 GLU B CB  
17189 C CG  . GLU B 1111 ? 0.4275 0.2630 0.3747 -0.0026 -0.0248 0.0326  1109 GLU B CG  
17190 C CD  . GLU B 1111 ? 0.4797 0.2981 0.4176 -0.0020 -0.0284 0.0342  1109 GLU B CD  
17191 O OE1 . GLU B 1111 ? 0.4779 0.2870 0.4132 -0.0065 -0.0308 0.0345  1109 GLU B OE1 
17192 O OE2 . GLU B 1111 ? 0.5000 0.3140 0.4330 0.0029  -0.0290 0.0352  1109 GLU B OE2 
17193 N N   . SER B 1112 ? 0.3565 0.2263 0.3170 -0.0003 -0.0162 0.0338  1110 SER B N   
17194 C CA  . SER B 1112 ? 0.3780 0.2549 0.3399 0.0063  -0.0149 0.0317  1110 SER B CA  
17195 C C   . SER B 1112 ? 0.3761 0.2669 0.3460 0.0058  -0.0122 0.0293  1110 SER B C   
17196 O O   . SER B 1112 ? 0.3522 0.2475 0.3241 0.0105  -0.0119 0.0262  1110 SER B O   
17197 C CB  . SER B 1112 ? 0.4527 0.3306 0.4117 0.0080  -0.0142 0.0346  1110 SER B CB  
17198 O OG  . SER B 1112 ? 0.4229 0.3080 0.3835 0.0141  -0.0132 0.0326  1110 SER B OG  
17199 N N   . GLY B 1113 ? 0.3359 0.2337 0.3104 0.0002  -0.0102 0.0308  1111 GLY B N   
17200 C CA  . GLY B 1113 ? 0.3290 0.2391 0.3108 -0.0004 -0.0078 0.0285  1111 GLY B CA  
17201 C C   . GLY B 1113 ? 0.3170 0.2261 0.3009 0.0003  -0.0091 0.0251  1111 GLY B C   
17202 O O   . GLY B 1113 ? 0.3178 0.2340 0.3052 0.0034  -0.0080 0.0223  1111 GLY B O   
17203 N N   . LEU B 1114 ? 0.3010 0.2007 0.2822 -0.0026 -0.0114 0.0254  1112 LEU B N   
17204 C CA  . LEU B 1114 ? 0.3061 0.2037 0.2885 -0.0019 -0.0129 0.0221  1112 LEU B CA  
17205 C C   . LEU B 1114 ? 0.3323 0.2271 0.3117 0.0050  -0.0139 0.0193  1112 LEU B C   
17206 O O   . LEU B 1114 ? 0.3094 0.2091 0.2918 0.0072  -0.0135 0.0162  1112 LEU B O   
17207 C CB  . LEU B 1114 ? 0.3356 0.2225 0.3147 -0.0064 -0.0155 0.0232  1112 LEU B CB  
17208 C CG  . LEU B 1114 ? 0.3448 0.2265 0.3231 -0.0055 -0.0178 0.0199  1112 LEU B CG  
17209 C CD1 . LEU B 1114 ? 0.3095 0.2023 0.2950 -0.0063 -0.0162 0.0174  1112 LEU B CD1 
17210 C CD2 . LEU B 1114 ? 0.4112 0.2815 0.3857 -0.0105 -0.0207 0.0213  1112 LEU B CD2 
17211 N N   . TYR B 1115 ? 0.3363 0.2234 0.3097 0.0087  -0.0152 0.0204  1113 TYR B N   
17212 C CA  . TYR B 1115 ? 0.3173 0.2024 0.2879 0.0157  -0.0161 0.0177  1113 TYR B CA  
17213 C C   . TYR B 1115 ? 0.2984 0.1964 0.2740 0.0189  -0.0135 0.0162  1113 TYR B C   
17214 O O   . TYR B 1115 ? 0.3198 0.2208 0.2966 0.0227  -0.0135 0.0132  1113 TYR B O   
17215 C CB  . TYR B 1115 ? 0.3191 0.1941 0.2824 0.0193  -0.0180 0.0193  1113 TYR B CB  
17216 C CG  . TYR B 1115 ? 0.3134 0.1734 0.2703 0.0172  -0.0212 0.0204  1113 TYR B CG  
17217 C CD1 . TYR B 1115 ? 0.3348 0.1904 0.2922 0.0133  -0.0226 0.0192  1113 TYR B CD1 
17218 C CD2 . TYR B 1115 ? 0.3938 0.2439 0.3439 0.0192  -0.0230 0.0227  1113 TYR B CD2 
17219 C CE1 . TYR B 1115 ? 0.4001 0.2414 0.3512 0.0111  -0.0257 0.0202  1113 TYR B CE1 
17220 C CE2 . TYR B 1115 ? 0.4237 0.2591 0.3673 0.0172  -0.0261 0.0238  1113 TYR B CE2 
17221 C CZ  . TYR B 1115 ? 0.4656 0.2966 0.4097 0.0130  -0.0275 0.0225  1113 TYR B CZ  
17222 O OH  . TYR B 1115 ? 0.5101 0.3260 0.4474 0.0106  -0.0308 0.0236  1113 TYR B OH  
17223 N N   . HIS B 1116 ? 0.2970 0.2025 0.2753 0.0173  -0.0114 0.0184  1114 HIS B N   
17224 C CA  . HIS B 1116 ? 0.3002 0.2177 0.2831 0.0197  -0.0090 0.0170  1114 HIS B CA  
17225 C C   . HIS B 1116 ? 0.3046 0.2295 0.2934 0.0175  -0.0078 0.0147  1114 HIS B C   
17226 O O   . HIS B 1116 ? 0.3028 0.2340 0.2941 0.0207  -0.0070 0.0123  1114 HIS B O   
17227 C CB  . HIS B 1116 ? 0.2965 0.2199 0.2807 0.0182  -0.0072 0.0197  1114 HIS B CB  
17228 C CG  . HIS B 1116 ? 0.3618 0.2816 0.3412 0.0220  -0.0079 0.0214  1114 HIS B CG  
17229 N ND1 . HIS B 1116 ? 0.3787 0.2883 0.3524 0.0211  -0.0096 0.0242  1114 HIS B ND1 
17230 C CD2 . HIS B 1116 ? 0.3394 0.2644 0.3188 0.0268  -0.0074 0.0208  1114 HIS B CD2 
17231 C CE1 . HIS B 1116 ? 0.3842 0.2929 0.3546 0.0254  -0.0101 0.0252  1114 HIS B CE1 
17232 N NE2 . HIS B 1116 ? 0.4015 0.3197 0.3753 0.0289  -0.0088 0.0231  1114 HIS B NE2 
17233 N N   . GLN B 1117 ? 0.2701 0.1947 0.2612 0.0120  -0.0077 0.0156  1115 GLN B N   
17234 C CA  . GLN B 1117 ? 0.2496 0.1808 0.2460 0.0101  -0.0068 0.0134  1115 GLN B CA  
17235 C C   . GLN B 1117 ? 0.2817 0.2088 0.2767 0.0129  -0.0085 0.0103  1115 GLN B C   
17236 O O   . GLN B 1117 ? 0.2613 0.1950 0.2596 0.0145  -0.0077 0.0079  1115 GLN B O   
17237 C CB  . GLN B 1117 ? 0.2757 0.2069 0.2747 0.0039  -0.0067 0.0149  1115 GLN B CB  
17238 C CG  . GLN B 1117 ? 0.2768 0.2144 0.2782 0.0009  -0.0045 0.0176  1115 GLN B CG  
17239 C CD  . GLN B 1117 ? 0.2562 0.1944 0.2603 -0.0052 -0.0044 0.0191  1115 GLN B CD  
17240 O OE1 . GLN B 1117 ? 0.2865 0.2187 0.2897 -0.0075 -0.0063 0.0187  1115 GLN B OE1 
17241 N NE2 . GLN B 1117 ? 0.2466 0.1928 0.2541 -0.0078 -0.0020 0.0208  1115 GLN B NE2 
17242 N N   . LEU B 1118 ? 0.2812 0.1972 0.2710 0.0134  -0.0110 0.0104  1116 LEU B N   
17243 C CA  . LEU B 1118 ? 0.2904 0.2016 0.2779 0.0165  -0.0128 0.0074  1116 LEU B CA  
17244 C C   . LEU B 1118 ? 0.3045 0.2200 0.2915 0.0227  -0.0120 0.0055  1116 LEU B C   
17245 O O   . LEU B 1118 ? 0.3088 0.2278 0.2973 0.0247  -0.0118 0.0028  1116 LEU B O   
17246 C CB  . LEU B 1118 ? 0.3205 0.2179 0.3014 0.0165  -0.0157 0.0079  1116 LEU B CB  
17247 C CG  . LEU B 1118 ? 0.4643 0.3561 0.4452 0.0109  -0.0174 0.0082  1116 LEU B CG  
17248 C CD1 . LEU B 1118 ? 0.4429 0.3203 0.4165 0.0109  -0.0204 0.0093  1116 LEU B CD1 
17249 C CD2 . LEU B 1118 ? 0.4442 0.3384 0.4274 0.0112  -0.0179 0.0049  1116 LEU B CD2 
17250 N N   . ALA B 1119 ? 0.2920 0.2075 0.2767 0.0257  -0.0116 0.0070  1117 ALA B N   
17251 C CA  . ALA B 1119 ? 0.3013 0.2218 0.2859 0.0315  -0.0109 0.0054  1117 ALA B CA  
17252 C C   . ALA B 1119 ? 0.2792 0.2118 0.2698 0.0310  -0.0086 0.0041  1117 ALA B C   
17253 O O   . ALA B 1119 ? 0.2990 0.2353 0.2903 0.0341  -0.0083 0.0016  1117 ALA B O   
17254 C CB  . ALA B 1119 ? 0.2948 0.2147 0.2767 0.0343  -0.0108 0.0075  1117 ALA B CB  
17255 N N   . ALA B 1120 ? 0.2699 0.2087 0.2646 0.0270  -0.0069 0.0057  1118 ALA B N   
17256 C CA  . ALA B 1120 ? 0.2321 0.1817 0.2320 0.0263  -0.0049 0.0045  1118 ALA B CA  
17257 C C   . ALA B 1120 ? 0.2689 0.2193 0.2709 0.0253  -0.0053 0.0021  1118 ALA B C   
17258 O O   . ALA B 1120 ? 0.2514 0.2077 0.2554 0.0273  -0.0045 0.0002  1118 ALA B O   
17259 C CB  . ALA B 1120 ? 0.2707 0.2255 0.2740 0.0222  -0.0033 0.0066  1118 ALA B CB  
17260 N N   . ALA B 1121 ? 0.2450 0.1895 0.2465 0.0218  -0.0065 0.0023  1119 ALA B N   
17261 C CA  . ALA B 1121 ? 0.2409 0.1863 0.2444 0.0204  -0.0070 0.0001  1119 ALA B CA  
17262 C C   . ALA B 1121 ? 0.2261 0.1674 0.2262 0.0246  -0.0084 -0.0024 1119 ALA B C   
17263 O O   . ALA B 1121 ? 0.2334 0.1792 0.2354 0.0256  -0.0079 -0.0045 1119 ALA B O   
17264 C CB  . ALA B 1121 ? 0.2817 0.2220 0.2856 0.0155  -0.0083 0.0011  1119 ALA B CB  
17265 N N   . LEU B 1122 ? 0.2371 0.1697 0.2318 0.0272  -0.0100 -0.0022 1120 LEU B N   
17266 C CA  . LEU B 1122 ? 0.2460 0.1743 0.2369 0.0316  -0.0113 -0.0048 1120 LEU B CA  
17267 C C   . LEU B 1122 ? 0.2651 0.2014 0.2570 0.0363  -0.0097 -0.0059 1120 LEU B C   
17268 O O   . LEU B 1122 ? 0.2555 0.1938 0.2472 0.0387  -0.0097 -0.0083 1120 LEU B O   
17269 C CB  . LEU B 1122 ? 0.2577 0.1744 0.2422 0.0337  -0.0135 -0.0043 1120 LEU B CB  
17270 C CG  . LEU B 1122 ? 0.2965 0.2037 0.2789 0.0292  -0.0156 -0.0033 1120 LEU B CG  
17271 C CD1 . LEU B 1122 ? 0.3243 0.2196 0.2997 0.0317  -0.0178 -0.0027 1120 LEU B CD1 
17272 C CD2 . LEU B 1122 ? 0.3084 0.2140 0.2912 0.0274  -0.0167 -0.0057 1120 LEU B CD2 
17273 N N   . ALA B 1123 ? 0.2393 0.1804 0.2325 0.0373  -0.0084 -0.0041 1121 ALA B N   
17274 C CA  . ALA B 1123 ? 0.2478 0.1971 0.2423 0.0413  -0.0070 -0.0049 1121 ALA B CA  
17275 C C   . ALA B 1123 ? 0.2710 0.2292 0.2700 0.0398  -0.0055 -0.0062 1121 ALA B C   
17276 O O   . ALA B 1123 ? 0.2607 0.2247 0.2602 0.0430  -0.0046 -0.0076 1121 ALA B O   
17277 C CB  . ALA B 1123 ? 0.2765 0.2294 0.2717 0.0418  -0.0060 -0.0026 1121 ALA B CB  
17278 N N   . THR B 1124 ? 0.2263 0.1859 0.2286 0.0350  -0.0051 -0.0058 1122 THR B N   
17279 C CA  . THR B 1124 ? 0.2139 0.1809 0.2202 0.0333  -0.0039 -0.0069 1122 THR B CA  
17280 C C   . THR B 1124 ? 0.2191 0.1827 0.2248 0.0323  -0.0051 -0.0089 1122 THR B C   
17281 O O   . THR B 1124 ? 0.2455 0.2137 0.2544 0.0300  -0.0045 -0.0096 1122 THR B O   
17282 C CB  . THR B 1124 ? 0.2265 0.1985 0.2370 0.0293  -0.0027 -0.0053 1122 THR B CB  
17283 O OG1 . THR B 1124 ? 0.2149 0.1811 0.2248 0.0262  -0.0035 -0.0037 1122 THR B OG1 
17284 C CG2 . THR B 1124 ? 0.2255 0.2034 0.2369 0.0308  -0.0013 -0.0039 1122 THR B CG2 
17285 N N   . GLY B 1125 ? 0.2125 0.1676 0.2138 0.0340  -0.0068 -0.0098 1123 GLY B N   
17286 C CA  . GLY B 1125 ? 0.2165 0.1681 0.2162 0.0340  -0.0081 -0.0120 1123 GLY B CA  
17287 C C   . GLY B 1125 ? 0.2535 0.2008 0.2543 0.0292  -0.0094 -0.0117 1123 GLY B C   
17288 O O   . GLY B 1125 ? 0.2605 0.2056 0.2605 0.0287  -0.0106 -0.0135 1123 GLY B O   
17289 N N   . ASN B 1126 ? 0.2328 0.1795 0.2355 0.0258  -0.0093 -0.0095 1124 ASN B N   
17290 C CA  . ASN B 1126 ? 0.2318 0.1769 0.2368 0.0208  -0.0101 -0.0089 1124 ASN B CA  
17291 C C   . ASN B 1126 ? 0.2288 0.1632 0.2297 0.0196  -0.0126 -0.0087 1124 ASN B C   
17292 O O   . ASN B 1126 ? 0.2616 0.1893 0.2579 0.0220  -0.0135 -0.0083 1124 ASN B O   
17293 C CB  . ASN B 1126 ? 0.2273 0.1779 0.2367 0.0175  -0.0085 -0.0065 1124 ASN B CB  
17294 C CG  . ASN B 1126 ? 0.2129 0.1733 0.2260 0.0185  -0.0064 -0.0067 1124 ASN B CG  
17295 O OD1 . ASN B 1126 ? 0.2289 0.1936 0.2447 0.0176  -0.0061 -0.0080 1124 ASN B OD1 
17296 N ND2 . ASN B 1126 ? 0.2232 0.1867 0.2362 0.0202  -0.0050 -0.0055 1124 ASN B ND2 
17297 N N   . SER B 1127 ? 0.2748 0.2073 0.2771 0.0156  -0.0139 -0.0091 1125 SER B N   
17298 C CA  . SER B 1127 ? 0.2484 0.1722 0.2483 0.0125  -0.0161 -0.0081 1125 SER B CA  
17299 C C   . SER B 1127 ? 0.2725 0.1997 0.2763 0.0080  -0.0151 -0.0052 1125 SER B C   
17300 O O   . SER B 1127 ? 0.2520 0.1882 0.2603 0.0075  -0.0128 -0.0044 1125 SER B O   
17301 C CB  . SER B 1127 ? 0.2816 0.2019 0.2811 0.0102  -0.0183 -0.0100 1125 SER B CB  
17302 O OG  . SER B 1127 ? 0.3440 0.2729 0.3495 0.0073  -0.0173 -0.0100 1125 SER B OG  
17303 N N   . VAL B 1128 ? 0.2730 0.1928 0.2747 0.0046  -0.0168 -0.0036 1126 VAL B N   
17304 C CA  . VAL B 1128 ? 0.2638 0.1869 0.2689 0.0002  -0.0157 -0.0006 1126 VAL B CA  
17305 C C   . VAL B 1128 ? 0.2786 0.1978 0.2844 -0.0054 -0.0177 0.0001  1126 VAL B C   
17306 O O   . VAL B 1128 ? 0.3000 0.2104 0.3018 -0.0058 -0.0204 -0.0011 1126 VAL B O   
17307 C CB  . VAL B 1128 ? 0.2555 0.1744 0.2570 0.0014  -0.0152 0.0018  1126 VAL B CB  
17308 C CG1 . VAL B 1128 ? 0.2814 0.2052 0.2826 0.0066  -0.0133 0.0012  1126 VAL B CG1 
17309 C CG2 . VAL B 1128 ? 0.3104 0.2160 0.3051 0.0017  -0.0181 0.0018  1126 VAL B CG2 
17310 N N   . ALA B 1129 ? 0.2575 0.1834 0.2684 -0.0097 -0.0163 0.0022  1127 ALA B N   
17311 C CA  . ALA B 1129 ? 0.2479 0.1712 0.2601 -0.0156 -0.0178 0.0040  1127 ALA B CA  
17312 C C   . ALA B 1129 ? 0.2673 0.1913 0.2795 -0.0178 -0.0163 0.0075  1127 ALA B C   
17313 O O   . ALA B 1129 ? 0.2611 0.1942 0.2772 -0.0174 -0.0135 0.0085  1127 ALA B O   
17314 C CB  . ALA B 1129 ? 0.2697 0.2019 0.2884 -0.0188 -0.0174 0.0034  1127 ALA B CB  
17315 N N   . ILE B 1130 ? 0.2700 0.1838 0.2772 -0.0199 -0.0182 0.0093  1128 ILE B N   
17316 C CA  . ILE B 1130 ? 0.2839 0.1969 0.2899 -0.0219 -0.0170 0.0128  1128 ILE B CA  
17317 C C   . ILE B 1130 ? 0.2500 0.1658 0.2597 -0.0290 -0.0171 0.0153  1128 ILE B C   
17318 O O   . ILE B 1130 ? 0.2647 0.1752 0.2737 -0.0327 -0.0197 0.0150  1128 ILE B O   
17319 C CB  . ILE B 1130 ? 0.2993 0.1991 0.2972 -0.0200 -0.0190 0.0137  1128 ILE B CB  
17320 C CG1 . ILE B 1130 ? 0.3314 0.2283 0.3256 -0.0128 -0.0193 0.0109  1128 ILE B CG1 
17321 C CG2 . ILE B 1130 ? 0.3032 0.2029 0.2997 -0.0215 -0.0176 0.0174  1128 ILE B CG2 
17322 C CD1 . ILE B 1130 ? 0.3282 0.2114 0.3142 -0.0104 -0.0218 0.0111  1128 ILE B CD1 
17323 N N   . ASP B 1131 ? 0.2879 0.2123 0.3014 -0.0309 -0.0143 0.0177  1129 ASP B N   
17324 C CA  . ASP B 1131 ? 0.2714 0.2000 0.2888 -0.0375 -0.0139 0.0204  1129 ASP B CA  
17325 C C   . ASP B 1131 ? 0.3010 0.2178 0.3130 -0.0419 -0.0166 0.0228  1129 ASP B C   
17326 O O   . ASP B 1131 ? 0.2987 0.2088 0.3055 -0.0412 -0.0166 0.0250  1129 ASP B O   
17327 C CB  . ASP B 1131 ? 0.2725 0.2108 0.2931 -0.0379 -0.0103 0.0226  1129 ASP B CB  
17328 C CG  . ASP B 1131 ? 0.2778 0.2217 0.3024 -0.0445 -0.0095 0.0256  1129 ASP B CG  
17329 O OD1 . ASP B 1131 ? 0.2851 0.2304 0.3131 -0.0483 -0.0110 0.0251  1129 ASP B OD1 
17330 O OD2 . ASP B 1131 ? 0.3153 0.2623 0.3397 -0.0458 -0.0073 0.0285  1129 ASP B OD2 
17331 N N   . ALA B 1132 ? 0.2974 0.2115 0.3105 -0.0465 -0.0191 0.0225  1130 ALA B N   
17332 C CA  . ALA B 1132 ? 0.3034 0.2056 0.3113 -0.0512 -0.0220 0.0248  1130 ALA B CA  
17333 C C   . ALA B 1132 ? 0.3281 0.2329 0.3366 -0.0562 -0.0203 0.0294  1130 ALA B C   
17334 O O   . ALA B 1132 ? 0.3493 0.2432 0.3517 -0.0587 -0.0221 0.0319  1130 ALA B O   
17335 C CB  . ALA B 1132 ? 0.3254 0.2252 0.3348 -0.0556 -0.0250 0.0236  1130 ALA B CB  
17336 N N   . ALA B 1133 ? 0.3312 0.2501 0.3467 -0.0578 -0.0169 0.0305  1131 ALA B N   
17337 C CA  . ALA B 1133 ? 0.3752 0.2974 0.3914 -0.0626 -0.0151 0.0349  1131 ALA B CA  
17338 C C   . ALA B 1133 ? 0.3604 0.2770 0.3706 -0.0594 -0.0140 0.0368  1131 ALA B C   
17339 O O   . ALA B 1133 ? 0.3663 0.2825 0.3751 -0.0634 -0.0130 0.0407  1131 ALA B O   
17340 C CB  . ALA B 1133 ? 0.3484 0.2876 0.3734 -0.0641 -0.0115 0.0353  1131 ALA B CB  
17341 N N   . SER B 1134 ? 0.3261 0.2386 0.3328 -0.0523 -0.0141 0.0342  1132 SER B N   
17342 C CA  . SER B 1134 ? 0.3257 0.2322 0.3264 -0.0489 -0.0136 0.0359  1132 SER B CA  
17343 C C   . SER B 1134 ? 0.3156 0.2070 0.3085 -0.0517 -0.0167 0.0384  1132 SER B C   
17344 O O   . SER B 1134 ? 0.3683 0.2551 0.3564 -0.0510 -0.0162 0.0411  1132 SER B O   
17345 C CB  . SER B 1134 ? 0.3373 0.2428 0.3361 -0.0408 -0.0135 0.0324  1132 SER B CB  
17346 O OG  . SER B 1134 ? 0.3238 0.2190 0.3187 -0.0388 -0.0168 0.0298  1132 SER B OG  
17347 N N   . GLY B 1135 ? 0.3333 0.2163 0.3243 -0.0546 -0.0201 0.0374  1133 GLY B N   
17348 C CA  . GLY B 1135 ? 0.3821 0.2494 0.3651 -0.0572 -0.0235 0.0395  1133 GLY B CA  
17349 C C   . GLY B 1135 ? 0.4405 0.2957 0.4154 -0.0505 -0.0252 0.0382  1133 GLY B C   
17350 O O   . GLY B 1135 ? 0.4202 0.2625 0.3877 -0.0518 -0.0275 0.0406  1133 GLY B O   
17351 N N   . LEU B 1136 ? 0.3741 0.2332 0.3502 -0.0433 -0.0243 0.0345  1134 LEU B N   
17352 C CA  . LEU B 1136 ? 0.3789 0.2291 0.3482 -0.0362 -0.0254 0.0332  1134 LEU B CA  
17353 C C   . LEU B 1136 ? 0.4271 0.2668 0.3921 -0.0330 -0.0289 0.0296  1134 LEU B C   
17354 O O   . LEU B 1136 ? 0.4264 0.2612 0.3871 -0.0261 -0.0295 0.0275  1134 LEU B O   
17355 C CB  . LEU B 1136 ? 0.3659 0.2274 0.3389 -0.0301 -0.0221 0.0316  1134 LEU B CB  
17356 C CG  . LEU B 1136 ? 0.3772 0.2476 0.3529 -0.0320 -0.0189 0.0350  1134 LEU B CG  
17357 C CD1 . LEU B 1136 ? 0.4085 0.2911 0.3888 -0.0268 -0.0158 0.0330  1134 LEU B CD1 
17358 C CD2 . LEU B 1136 ? 0.4031 0.2629 0.3712 -0.0318 -0.0201 0.0384  1134 LEU B CD2 
17359 N N   . GLN B 1137 ? 0.4021 0.2381 0.3678 -0.0380 -0.0312 0.0290  1135 GLN B N   
17360 C CA  . GLN B 1137 ? 0.4112 0.2378 0.3728 -0.0352 -0.0344 0.0253  1135 GLN B CA  
17361 C C   . GLN B 1137 ? 0.5083 0.3189 0.4599 -0.0308 -0.0372 0.0251  1135 GLN B C   
17362 O O   . GLN B 1137 ? 0.4662 0.2721 0.4144 -0.0245 -0.0385 0.0215  1135 GLN B O   
17363 C CB  . GLN B 1137 ? 0.5057 0.3295 0.4688 -0.0423 -0.0369 0.0253  1135 GLN B CB  
17364 C CG  . GLN B 1137 ? 0.4444 0.2833 0.4172 -0.0451 -0.0348 0.0241  1135 GLN B CG  
17365 C CD  . GLN B 1137 ? 0.4109 0.2612 0.3901 -0.0509 -0.0319 0.0278  1135 GLN B CD  
17366 O OE1 . GLN B 1137 ? 0.3983 0.2466 0.3751 -0.0523 -0.0309 0.0313  1135 GLN B OE1 
17367 N NE2 . GLN B 1137 ? 0.4040 0.2662 0.3912 -0.0542 -0.0306 0.0271  1135 GLN B NE2 
17368 N N   . ALA B 1138 ? 0.4429 0.2452 0.3896 -0.0337 -0.0382 0.0290  1136 ALA B N   
17369 C CA  . ALA B 1138 ? 0.5007 0.2865 0.4372 -0.0297 -0.0412 0.0291  1136 ALA B CA  
17370 C C   . ALA B 1138 ? 0.5055 0.2938 0.4403 -0.0206 -0.0396 0.0276  1136 ALA B C   
17371 O O   . ALA B 1138 ? 0.5255 0.3014 0.4524 -0.0154 -0.0421 0.0265  1136 ALA B O   
17372 C CB  . ALA B 1138 ? 0.5013 0.2780 0.4330 -0.0353 -0.0426 0.0341  1136 ALA B CB  
17373 N N   . SER B 1139 ? 0.4565 0.2603 0.3985 -0.0187 -0.0357 0.0274  1137 SER B N   
17374 C CA  . SER B 1139 ? 0.5023 0.3100 0.4435 -0.0107 -0.0340 0.0262  1137 SER B CA  
17375 C C   . SER B 1139 ? 0.4958 0.3037 0.4365 -0.0039 -0.0346 0.0214  1137 SER B C   
17376 O O   . SER B 1139 ? 0.4800 0.2881 0.4183 0.0032  -0.0341 0.0202  1137 SER B O   
17377 C CB  . SER B 1139 ? 0.4535 0.2776 0.4023 -0.0114 -0.0297 0.0276  1137 SER B CB  
17378 O OG  . SER B 1139 ? 0.4837 0.3071 0.4314 -0.0160 -0.0290 0.0322  1137 SER B OG  
17379 N N   . LEU B 1140 ? 0.4590 0.2673 0.4019 -0.0060 -0.0356 0.0187  1138 LEU B N   
17380 C CA  . LEU B 1140 ? 0.4776 0.2862 0.4199 -0.0001 -0.0362 0.0141  1138 LEU B CA  
17381 C C   . LEU B 1140 ? 0.5452 0.3376 0.4795 0.0006  -0.0405 0.0123  1138 LEU B C   
17382 O O   . LEU B 1140 ? 0.5839 0.3757 0.5182 0.0024  -0.0415 0.0086  1138 LEU B O   
17383 C CB  . LEU B 1140 ? 0.4799 0.3019 0.4306 -0.0020 -0.0341 0.0121  1138 LEU B CB  
17384 C CG  . LEU B 1140 ? 0.4594 0.2973 0.4177 -0.0016 -0.0299 0.0131  1138 LEU B CG  
17385 C CD1 . LEU B 1140 ? 0.4409 0.2906 0.4065 -0.0026 -0.0282 0.0107  1138 LEU B CD1 
17386 C CD2 . LEU B 1140 ? 0.4965 0.3364 0.4527 0.0057  -0.0286 0.0127  1138 LEU B CD2 
17387 N N   . LYS B 1141 ? 0.5868 0.3655 0.5139 -0.0009 -0.0431 0.0148  1139 LYS B N   
17388 C CA  . LYS B 1141 ? 0.5714 0.3332 0.4898 0.0002  -0.0474 0.0130  1139 LYS B CA  
17389 C C   . LYS B 1141 ? 0.6426 0.4008 0.5563 0.0100  -0.0479 0.0093  1139 LYS B C   
17390 O O   . LYS B 1141 ? 0.6437 0.4058 0.5571 0.0157  -0.0462 0.0098  1139 LYS B O   
17391 C CB  . LYS B 1141 ? 0.5788 0.3264 0.4901 -0.0036 -0.0501 0.0168  1139 LYS B CB  
17392 N N   . ASN B 1142 ? 0.5936 0.3452 0.5038 0.0120  -0.0503 0.0054  1140 ASN B N   
17393 C CA  . ASN B 1142 ? 0.6022 0.3494 0.5072 0.0212  -0.0511 0.0015  1140 ASN B CA  
17394 C C   . ASN B 1142 ? 0.6160 0.3797 0.5278 0.0266  -0.0472 -0.0004 1140 ASN B C   
17395 O O   . ASN B 1142 ? 0.5899 0.3535 0.4987 0.0346  -0.0467 -0.0020 1140 ASN B O   
17396 C CB  . ASN B 1142 ? 0.6348 0.3684 0.5308 0.0261  -0.0533 0.0027  1140 ASN B CB  
17397 N N   . LEU B 1143 ? 0.5833 0.3612 0.5040 0.0223  -0.0444 -0.0001 1141 LEU B N   
17398 C CA  . LEU B 1143 ? 0.5514 0.3443 0.4783 0.0268  -0.0410 -0.0022 1141 LEU B CA  
17399 C C   . LEU B 1143 ? 0.4610 0.2509 0.3842 0.0328  -0.0421 -0.0068 1141 LEU B C   
17400 O O   . LEU B 1143 ? 0.5671 0.3478 0.4864 0.0309  -0.0449 -0.0087 1141 LEU B O   
17401 C CB  . LEU B 1143 ? 0.5167 0.3231 0.4529 0.0208  -0.0385 -0.0014 1141 LEU B CB  
17402 C CG  . LEU B 1143 ? 0.5881 0.4081 0.5318 0.0184  -0.0349 0.0014  1141 LEU B CG  
17403 C CD1 . LEU B 1143 ? 0.4547 0.2869 0.4064 0.0147  -0.0330 0.0004  1141 LEU B CD1 
17404 C CD2 . LEU B 1143 ? 0.5152 0.3415 0.4592 0.0252  -0.0327 0.0013  1141 LEU B CD2 
17405 N N   . PRO B 1144 ? 0.5217 0.3192 0.4459 0.0399  -0.0400 -0.0087 1142 PRO B N   
17406 C CA  . PRO B 1144 ? 0.5577 0.3556 0.4799 0.0450  -0.0403 -0.0131 1142 PRO B CA  
17407 C C   . PRO B 1144 ? 0.5394 0.3441 0.4669 0.0400  -0.0397 -0.0144 1142 PRO B C   
17408 O O   . PRO B 1144 ? 0.4696 0.2852 0.4047 0.0352  -0.0375 -0.0125 1142 PRO B O   
17409 C CB  . PRO B 1144 ? 0.5552 0.3647 0.4803 0.0519  -0.0373 -0.0138 1142 PRO B CB  
17410 C CG  . PRO B 1144 ? 0.5871 0.3968 0.5124 0.0520  -0.0366 -0.0102 1142 PRO B CG  
17411 C CD  . PRO B 1144 ? 0.5134 0.3206 0.4411 0.0433  -0.0372 -0.0069 1142 PRO B CD  
17412 N N   . GLN B 1145 ? 0.5684 0.3663 0.4914 0.0415  -0.0419 -0.0178 1143 GLN B N   
17413 C CA  . GLN B 1145 ? 0.4981 0.3016 0.4254 0.0372  -0.0417 -0.0193 1143 GLN B CA  
17414 C C   . GLN B 1145 ? 0.4986 0.3192 0.4339 0.0383  -0.0378 -0.0197 1143 GLN B C   
17415 O O   . GLN B 1145 ? 0.4358 0.2642 0.3773 0.0331  -0.0369 -0.0192 1143 GLN B O   
17416 C CB  . GLN B 1145 ? 0.5612 0.3549 0.4816 0.0399  -0.0446 -0.0233 1143 GLN B CB  
17417 N N   . THR B 1146 ? 0.4758 0.3024 0.4111 0.0450  -0.0357 -0.0205 1144 THR B N   
17418 C CA  . THR B 1146 ? 0.5030 0.3456 0.4457 0.0458  -0.0321 -0.0206 1144 THR B CA  
17419 C C   . THR B 1146 ? 0.4300 0.2811 0.3801 0.0400  -0.0302 -0.0172 1144 THR B C   
17420 O O   . THR B 1146 ? 0.4707 0.3322 0.4271 0.0371  -0.0283 -0.0172 1144 THR B O   
17421 C CB  . THR B 1146 ? 0.4960 0.3435 0.4374 0.0534  -0.0303 -0.0216 1144 THR B CB  
17422 O OG1 . THR B 1146 ? 0.5459 0.3877 0.4844 0.0553  -0.0309 -0.0194 1144 THR B OG1 
17423 C CG2 . THR B 1146 ? 0.5815 0.4242 0.5170 0.0595  -0.0314 -0.0255 1144 THR B CG2 
17424 N N   . VAL B 1147 ? 0.4139 0.2605 0.3628 0.0386  -0.0306 -0.0142 1145 VAL B N   
17425 C CA  . VAL B 1147 ? 0.3715 0.2258 0.3269 0.0332  -0.0287 -0.0109 1145 VAL B CA  
17426 C C   . VAL B 1147 ? 0.3841 0.2357 0.3416 0.0257  -0.0301 -0.0100 1145 VAL B C   
17427 O O   . VAL B 1147 ? 0.3878 0.2492 0.3521 0.0215  -0.0283 -0.0090 1145 VAL B O   
17428 C CB  . VAL B 1147 ? 0.3507 0.2016 0.3040 0.0342  -0.0286 -0.0079 1145 VAL B CB  
17429 C CG1 . VAL B 1147 ? 0.4017 0.2622 0.3617 0.0293  -0.0262 -0.0047 1145 VAL B CG1 
17430 C CG2 . VAL B 1147 ? 0.4016 0.2541 0.3522 0.0421  -0.0277 -0.0091 1145 VAL B CG2 
17431 N N   . GLY B 1148 ? 0.4285 0.2668 0.3800 0.0241  -0.0335 -0.0104 1146 GLY B N   
17432 C CA  . GLY B 1148 ? 0.4206 0.2562 0.3739 0.0166  -0.0352 -0.0094 1146 GLY B CA  
17433 C C   . GLY B 1148 ? 0.3944 0.2386 0.3530 0.0146  -0.0345 -0.0114 1146 GLY B C   
17434 O O   . GLY B 1148 ? 0.4281 0.2772 0.3920 0.0085  -0.0342 -0.0099 1146 GLY B O   
17435 N N   . LEU B 1149 ? 0.4119 0.2581 0.3689 0.0198  -0.0341 -0.0147 1147 LEU B N   
17436 C CA  . LEU B 1149 ? 0.4777 0.3319 0.4391 0.0183  -0.0335 -0.0166 1147 LEU B CA  
17437 C C   . LEU B 1149 ? 0.4137 0.2821 0.3838 0.0158  -0.0303 -0.0148 1147 LEU B C   
17438 O O   . LEU B 1149 ? 0.4317 0.3064 0.4064 0.0127  -0.0300 -0.0154 1147 LEU B O   
17439 C CB  . LEU B 1149 ? 0.5409 0.3957 0.4990 0.0247  -0.0332 -0.0202 1147 LEU B CB  
17440 C CG  . LEU B 1149 ? 0.6348 0.4764 0.5842 0.0277  -0.0365 -0.0229 1147 LEU B CG  
17441 C CD1 . LEU B 1149 ? 0.6195 0.4649 0.5672 0.0331  -0.0357 -0.0264 1147 LEU B CD1 
17442 C CD2 . LEU B 1149 ? 0.6841 0.5171 0.6318 0.0216  -0.0398 -0.0229 1147 LEU B CD2 
17443 N N   . ARG B 1150 ? 0.3570 0.2305 0.3291 0.0175  -0.0279 -0.0127 1148 ARG B N   
17444 C CA  . ARG B 1150 ? 0.3822 0.2685 0.3617 0.0157  -0.0248 -0.0111 1148 ARG B CA  
17445 C C   . ARG B 1150 ? 0.3255 0.2131 0.3086 0.0098  -0.0245 -0.0078 1148 ARG B C   
17446 O O   . ARG B 1150 ? 0.3044 0.2023 0.2935 0.0081  -0.0220 -0.0064 1148 ARG B O   
17447 C CB  . ARG B 1150 ? 0.3544 0.2465 0.3343 0.0209  -0.0224 -0.0109 1148 ARG B CB  
17448 C CG  . ARG B 1150 ? 0.3742 0.2703 0.3531 0.0260  -0.0216 -0.0138 1148 ARG B CG  
17449 C CD  . ARG B 1150 ? 0.3774 0.2858 0.3616 0.0273  -0.0184 -0.0131 1148 ARG B CD  
17450 N NE  . ARG B 1150 ? 0.3680 0.2800 0.3506 0.0328  -0.0175 -0.0153 1148 ARG B NE  
17451 C CZ  . ARG B 1150 ? 0.3744 0.2935 0.3586 0.0361  -0.0154 -0.0148 1148 ARG B CZ  
17452 N NH1 . ARG B 1150 ? 0.3286 0.2517 0.3157 0.0346  -0.0140 -0.0122 1148 ARG B NH1 
17453 N NH2 . ARG B 1150 ? 0.3210 0.2434 0.3036 0.0409  -0.0146 -0.0168 1148 ARG B NH2 
17454 N N   . VAL B 1151 ? 0.3841 0.2615 0.3634 0.0067  -0.0270 -0.0065 1149 VAL B N   
17455 C CA  . VAL B 1151 ? 0.3558 0.2334 0.3374 0.0014  -0.0267 -0.0030 1149 VAL B CA  
17456 C C   . VAL B 1151 ? 0.3630 0.2382 0.3463 -0.0050 -0.0288 -0.0027 1149 VAL B C   
17457 O O   . VAL B 1151 ? 0.3981 0.2633 0.3765 -0.0055 -0.0319 -0.0042 1149 VAL B O   
17458 C CB  . VAL B 1151 ? 0.3720 0.2395 0.3475 0.0026  -0.0278 -0.0011 1149 VAL B CB  
17459 C CG1 . VAL B 1151 ? 0.4205 0.2869 0.3977 -0.0040 -0.0279 0.0027  1149 VAL B CG1 
17460 C CG2 . VAL B 1151 ? 0.3735 0.2452 0.3484 0.0083  -0.0255 -0.0008 1149 VAL B CG2 
17461 N N   . SER B 1152 ? 0.3392 0.2237 0.3293 -0.0096 -0.0272 -0.0009 1150 SER B N   
17462 C CA  A SER B 1152 ? 0.3354 0.2185 0.3276 -0.0163 -0.0290 0.0002  1150 SER B CA  
17463 C CA  B SER B 1152 ? 0.3361 0.2197 0.3286 -0.0163 -0.0289 0.0002  1150 SER B CA  
17464 C C   . SER B 1152 ? 0.3123 0.1997 0.3080 -0.0209 -0.0274 0.0041  1150 SER B C   
17465 O O   . SER B 1152 ? 0.3402 0.2335 0.3376 -0.0188 -0.0246 0.0055  1150 SER B O   
17466 C CB  A SER B 1152 ? 0.3772 0.2686 0.3750 -0.0178 -0.0289 -0.0018 1150 SER B CB  
17467 C CB  B SER B 1152 ? 0.3742 0.2671 0.3727 -0.0177 -0.0285 -0.0017 1150 SER B CB  
17468 O OG  A SER B 1152 ? 0.3466 0.2508 0.3507 -0.0167 -0.0256 -0.0013 1150 SER B OG  
17469 O OG  B SER B 1152 ? 0.3532 0.2431 0.3486 -0.0134 -0.0298 -0.0052 1150 SER B OG  
17470 N N   . TRP B 1153 ? 0.3193 0.2030 0.3154 -0.0271 -0.0292 0.0058  1151 TRP B N   
17471 C CA  . TRP B 1153 ? 0.3106 0.1988 0.3101 -0.0322 -0.0278 0.0097  1151 TRP B CA  
17472 C C   . TRP B 1153 ? 0.3498 0.2485 0.3570 -0.0370 -0.0272 0.0098  1151 TRP B C   
17473 O O   . TRP B 1153 ? 0.3610 0.2575 0.3686 -0.0391 -0.0297 0.0080  1151 TRP B O   
17474 C CB  . TRP B 1153 ? 0.3567 0.2323 0.3502 -0.0361 -0.0304 0.0121  1151 TRP B CB  
17475 C CG  . TRP B 1153 ? 0.3596 0.2257 0.3458 -0.0312 -0.0307 0.0125  1151 TRP B CG  
17476 C CD1 . TRP B 1153 ? 0.3714 0.2265 0.3505 -0.0263 -0.0330 0.0099  1151 TRP B CD1 
17477 C CD2 . TRP B 1153 ? 0.3565 0.2233 0.3416 -0.0306 -0.0287 0.0155  1151 TRP B CD2 
17478 N NE1 . TRP B 1153 ? 0.3806 0.2299 0.3546 -0.0225 -0.0325 0.0112  1151 TRP B NE1 
17479 C CE2 . TRP B 1153 ? 0.3655 0.2216 0.3428 -0.0252 -0.0300 0.0147  1151 TRP B CE2 
17480 C CE3 . TRP B 1153 ? 0.3302 0.2058 0.3198 -0.0340 -0.0259 0.0188  1151 TRP B CE3 
17481 C CZ2 . TRP B 1153 ? 0.3787 0.2326 0.3529 -0.0231 -0.0288 0.0172  1151 TRP B CZ2 
17482 C CZ3 . TRP B 1153 ? 0.3512 0.2244 0.3374 -0.0321 -0.0246 0.0213  1151 TRP B CZ3 
17483 C CH2 . TRP B 1153 ? 0.4013 0.2637 0.3800 -0.0267 -0.0261 0.0205  1151 TRP B CH2 
17484 N N   . SER B 1154 ? 0.2910 0.2012 0.3043 -0.0384 -0.0240 0.0117  1152 SER B N   
17485 C CA  . SER B 1154 ? 0.2989 0.2205 0.3200 -0.0419 -0.0232 0.0117  1152 SER B CA  
17486 C C   . SER B 1154 ? 0.2982 0.2239 0.3226 -0.0483 -0.0223 0.0154  1152 SER B C   
17487 O O   . SER B 1154 ? 0.2935 0.2221 0.3180 -0.0482 -0.0198 0.0179  1152 SER B O   
17488 C CB  . SER B 1154 ? 0.3222 0.2555 0.3482 -0.0377 -0.0201 0.0102  1152 SER B CB  
17489 O OG  . SER B 1154 ? 0.3010 0.2447 0.3343 -0.0410 -0.0195 0.0102  1152 SER B OG  
17490 N N   . LYS B 1155 ? 0.3010 0.2272 0.3280 -0.0540 -0.0244 0.0159  1153 LYS B N   
17491 C CA  . LYS B 1155 ? 0.3309 0.2642 0.3629 -0.0604 -0.0234 0.0193  1153 LYS B CA  
17492 C C   . LYS B 1155 ? 0.3413 0.2898 0.3822 -0.0610 -0.0214 0.0185  1153 LYS B C   
17493 O O   . LYS B 1155 ? 0.3432 0.2994 0.3893 -0.0664 -0.0207 0.0208  1153 LYS B O   
17494 C CB  . LYS B 1155 ? 0.3720 0.2966 0.4014 -0.0669 -0.0271 0.0207  1153 LYS B CB  
17495 N N   . ASP B 1156 ? 0.2583 0.2113 0.3010 -0.0556 -0.0206 0.0153  1154 ASP B N   
17496 C CA  . ASP B 1156 ? 0.2641 0.2302 0.3146 -0.0556 -0.0193 0.0141  1154 ASP B CA  
17497 C C   . ASP B 1156 ? 0.2531 0.2223 0.3034 -0.0486 -0.0175 0.0114  1154 ASP B C   
17498 O O   . ASP B 1156 ? 0.2612 0.2272 0.3100 -0.0457 -0.0193 0.0085  1154 ASP B O   
17499 C CB  . ASP B 1156 ? 0.2696 0.2352 0.3222 -0.0589 -0.0226 0.0127  1154 ASP B CB  
17500 C CG  . ASP B 1156 ? 0.2285 0.2081 0.2896 -0.0598 -0.0215 0.0121  1154 ASP B CG  
17501 O OD1 . ASP B 1156 ? 0.2491 0.2371 0.3134 -0.0557 -0.0186 0.0114  1154 ASP B OD1 
17502 O OD2 . ASP B 1156 ? 0.2742 0.2560 0.3386 -0.0644 -0.0238 0.0123  1154 ASP B OD2 
17503 N N   . TRP B 1157 ? 0.2129 0.1883 0.2647 -0.0462 -0.0141 0.0125  1155 TRP B N   
17504 C CA  . TRP B 1157 ? 0.2503 0.2276 0.3011 -0.0399 -0.0125 0.0102  1155 TRP B CA  
17505 C C   . TRP B 1157 ? 0.2791 0.2637 0.3346 -0.0381 -0.0127 0.0076  1155 TRP B C   
17506 O O   . TRP B 1157 ? 0.2602 0.2423 0.3135 -0.0338 -0.0132 0.0050  1155 TRP B O   
17507 C CB  . TRP B 1157 ? 0.2429 0.2261 0.2946 -0.0382 -0.0089 0.0118  1155 TRP B CB  
17508 C CG  . TRP B 1157 ? 0.2451 0.2221 0.2923 -0.0395 -0.0084 0.0146  1155 TRP B CG  
17509 C CD1 . TRP B 1157 ? 0.2370 0.2024 0.2785 -0.0413 -0.0108 0.0156  1155 TRP B CD1 
17510 C CD2 . TRP B 1157 ? 0.2386 0.2201 0.2859 -0.0388 -0.0053 0.0167  1155 TRP B CD2 
17511 N NE1 . TRP B 1157 ? 0.2670 0.2296 0.3053 -0.0420 -0.0094 0.0184  1155 TRP B NE1 
17512 C CE2 . TRP B 1157 ? 0.2485 0.2211 0.2904 -0.0405 -0.0061 0.0191  1155 TRP B CE2 
17513 C CE3 . TRP B 1157 ? 0.2191 0.2111 0.2704 -0.0370 -0.0022 0.0167  1155 TRP B CE3 
17514 C CZ2 . TRP B 1157 ? 0.2850 0.2591 0.3252 -0.0405 -0.0037 0.0217  1155 TRP B CZ2 
17515 C CZ3 . TRP B 1157 ? 0.2622 0.2557 0.3118 -0.0369 0.0002  0.0190  1155 TRP B CZ3 
17516 C CH2 . TRP B 1157 ? 0.2930 0.2778 0.3372 -0.0386 -0.0006 0.0215  1155 TRP B CH2 
17517 N N   . ALA B 1158 ? 0.2398 0.2337 0.3017 -0.0413 -0.0123 0.0083  1156 ALA B N   
17518 C CA  . ALA B 1158 ? 0.2421 0.2431 0.3084 -0.0392 -0.0124 0.0059  1156 ALA B CA  
17519 C C   . ALA B 1158 ? 0.2603 0.2553 0.3248 -0.0394 -0.0160 0.0037  1156 ALA B C   
17520 O O   . ALA B 1158 ? 0.2928 0.2893 0.3575 -0.0358 -0.0164 0.0012  1156 ALA B O   
17521 C CB  . ALA B 1158 ? 0.2054 0.2184 0.2792 -0.0421 -0.0112 0.0071  1156 ALA B CB  
17522 N N   . ALA B 1159 ? 0.2372 0.2251 0.2993 -0.0435 -0.0186 0.0046  1157 ALA B N   
17523 C CA  . ALA B 1159 ? 0.2824 0.2640 0.3421 -0.0438 -0.0222 0.0023  1157 ALA B CA  
17524 C C   . ALA B 1159 ? 0.3030 0.2743 0.3554 -0.0392 -0.0230 0.0003  1157 ALA B C   
17525 O O   . ALA B 1159 ? 0.2892 0.2573 0.3397 -0.0374 -0.0251 -0.0022 1157 ALA B O   
17526 C CB  . ALA B 1159 ? 0.2678 0.2449 0.3273 -0.0500 -0.0250 0.0038  1157 ALA B CB  
17527 N N   . ASP B 1160 ? 0.2766 0.2430 0.3247 -0.0373 -0.0214 0.0014  1158 ASP B N   
17528 C CA  . ASP B 1160 ? 0.2921 0.2485 0.3331 -0.0333 -0.0223 -0.0002 1158 ASP B CA  
17529 C C   . ASP B 1160 ? 0.2979 0.2580 0.3385 -0.0274 -0.0201 -0.0018 1158 ASP B C   
17530 O O   . ASP B 1160 ? 0.3504 0.3037 0.3856 -0.0236 -0.0206 -0.0033 1158 ASP B O   
17531 C CB  . ASP B 1160 ? 0.2628 0.2109 0.2989 -0.0344 -0.0223 0.0020  1158 ASP B CB  
17532 C CG  . ASP B 1160 ? 0.3178 0.2591 0.3524 -0.0401 -0.0253 0.0033  1158 ASP B CG  
17533 O OD1 . ASP B 1160 ? 0.3849 0.3267 0.4214 -0.0426 -0.0277 0.0021  1158 ASP B OD1 
17534 O OD2 . ASP B 1160 ? 0.3489 0.2842 0.3802 -0.0423 -0.0254 0.0057  1158 ASP B OD2 
17535 N N   . GLY B 1161 ? 0.2451 0.2157 0.2912 -0.0267 -0.0177 -0.0016 1159 GLY B N   
17536 C CA  . GLY B 1161 ? 0.2607 0.2351 0.3068 -0.0217 -0.0158 -0.0031 1159 GLY B CA  
17537 C C   . GLY B 1161 ? 0.3387 0.3134 0.3847 -0.0198 -0.0175 -0.0058 1159 GLY B C   
17538 O O   . GLY B 1161 ? 0.3576 0.3281 0.4026 -0.0218 -0.0202 -0.0068 1159 GLY B O   
17539 N N   . PRO B 1162 ? 0.3720 0.3514 0.4189 -0.0161 -0.0159 -0.0071 1160 PRO B N   
17540 C CA  . PRO B 1162 ? 0.2906 0.2754 0.3389 -0.0139 -0.0128 -0.0062 1160 PRO B CA  
17541 C C   . PRO B 1162 ? 0.3103 0.2894 0.3535 -0.0112 -0.0119 -0.0059 1160 PRO B C   
17542 O O   . PRO B 1162 ? 0.3212 0.2936 0.3596 -0.0091 -0.0132 -0.0072 1160 PRO B O   
17543 C CB  . PRO B 1162 ? 0.3863 0.3761 0.4363 -0.0111 -0.0124 -0.0081 1160 PRO B CB  
17544 C CG  . PRO B 1162 ? 0.3561 0.3399 0.4024 -0.0100 -0.0149 -0.0102 1160 PRO B CG  
17545 C CD  . PRO B 1162 ? 0.4120 0.3910 0.4579 -0.0139 -0.0173 -0.0096 1160 PRO B CD  
17546 N N   . PHE B 1163 ? 0.2524 0.2344 0.2964 -0.0112 -0.0097 -0.0041 1161 PHE B N   
17547 C CA  . PHE B 1163 ? 0.2314 0.2098 0.2712 -0.0082 -0.0086 -0.0036 1161 PHE B CA  
17548 C C   . PHE B 1163 ? 0.2329 0.2169 0.2736 -0.0048 -0.0067 -0.0046 1161 PHE B C   
17549 O O   . PHE B 1163 ? 0.2472 0.2373 0.2915 -0.0048 -0.0062 -0.0055 1161 PHE B O   
17550 C CB  . PHE B 1163 ? 0.2483 0.2257 0.2878 -0.0104 -0.0075 -0.0009 1161 PHE B CB  
17551 C CG  . PHE B 1163 ? 0.2668 0.2389 0.3056 -0.0146 -0.0095 0.0003  1161 PHE B CG  
17552 C CD1 . PHE B 1163 ? 0.3052 0.2677 0.3391 -0.0142 -0.0120 -0.0006 1161 PHE B CD1 
17553 C CD2 . PHE B 1163 ? 0.2644 0.2410 0.3073 -0.0189 -0.0090 0.0022  1161 PHE B CD2 
17554 C CE1 . PHE B 1163 ? 0.3000 0.2568 0.3328 -0.0182 -0.0142 0.0004  1161 PHE B CE1 
17555 C CE2 . PHE B 1163 ? 0.2667 0.2384 0.3089 -0.0232 -0.0110 0.0035  1161 PHE B CE2 
17556 C CZ  . PHE B 1163 ? 0.2820 0.2432 0.3190 -0.0230 -0.0137 0.0026  1161 PHE B CZ  
17557 N N   . ALA B 1164 ? 0.2618 0.2434 0.2990 -0.0018 -0.0058 -0.0045 1162 ALA B N   
17558 C CA  . ALA B 1164 ? 0.2623 0.2488 0.2999 0.0012  -0.0041 -0.0053 1162 ALA B CA  
17559 C C   . ALA B 1164 ? 0.2698 0.2583 0.3069 0.0020  -0.0022 -0.0036 1162 ALA B C   
17560 O O   . ALA B 1164 ? 0.3153 0.3067 0.3518 0.0046  -0.0010 -0.0040 1162 ALA B O   
17561 C CB  . ALA B 1164 ? 0.3039 0.2871 0.3378 0.0045  -0.0050 -0.0071 1162 ALA B CB  
17562 N N   . GLY B 1165 ? 0.2277 0.2149 0.2650 -0.0005 -0.0019 -0.0015 1163 GLY B N   
17563 C CA  . GLY B 1165 ? 0.2549 0.2437 0.2914 0.0000  -0.0002 0.0003  1163 GLY B CA  
17564 C C   . GLY B 1165 ? 0.2288 0.2133 0.2640 -0.0028 -0.0006 0.0026  1163 GLY B C   
17565 O O   . GLY B 1165 ? 0.2298 0.2093 0.2643 -0.0050 -0.0024 0.0026  1163 GLY B O   
17566 N N   . ALA B 1166 ? 0.2151 0.2014 0.2498 -0.0030 0.0010  0.0046  1164 ALA B N   
17567 C CA  . ALA B 1166 ? 0.2396 0.2217 0.2727 -0.0060 0.0007  0.0071  1164 ALA B CA  
17568 C C   . ALA B 1166 ? 0.2468 0.2277 0.2767 -0.0043 0.0018  0.0088  1164 ALA B C   
17569 O O   . ALA B 1166 ? 0.2484 0.2349 0.2792 -0.0024 0.0035  0.0086  1164 ALA B O   
17570 C CB  . ALA B 1166 ? 0.2269 0.2148 0.2646 -0.0101 0.0017  0.0084  1164 ALA B CB  
17571 N N   . LEU B 1167 ? 0.2216 0.1947 0.2473 -0.0050 0.0005  0.0105  1165 LEU B N   
17572 C CA  . LEU B 1167 ? 0.2265 0.1975 0.2487 -0.0038 0.0013  0.0126  1165 LEU B CA  
17573 C C   . LEU B 1167 ? 0.2614 0.2304 0.2832 -0.0083 0.0014  0.0156  1165 LEU B C   
17574 O O   . LEU B 1167 ? 0.2571 0.2204 0.2781 -0.0111 -0.0003 0.0161  1165 LEU B O   
17575 C CB  . LEU B 1167 ? 0.2423 0.2054 0.2592 -0.0002 -0.0004 0.0121  1165 LEU B CB  
17576 C CG  . LEU B 1167 ? 0.2199 0.1849 0.2370 0.0041  -0.0007 0.0092  1165 LEU B CG  
17577 C CD1 . LEU B 1167 ? 0.2618 0.2188 0.2735 0.0077  -0.0024 0.0088  1165 LEU B CD1 
17578 C CD2 . LEU B 1167 ? 0.2698 0.2432 0.2890 0.0061  0.0014  0.0089  1165 LEU B CD2 
17579 N N   . VAL B 1168 ? 0.2242 0.1977 0.2463 -0.0091 0.0035  0.0177  1166 VAL B N   
17580 C CA  . VAL B 1168 ? 0.2731 0.2466 0.2954 -0.0137 0.0041  0.0207  1166 VAL B CA  
17581 C C   . VAL B 1168 ? 0.2603 0.2306 0.2780 -0.0128 0.0046  0.0233  1166 VAL B C   
17582 O O   . VAL B 1168 ? 0.2692 0.2429 0.2860 -0.0094 0.0058  0.0228  1166 VAL B O   
17583 C CB  . VAL B 1168 ? 0.2594 0.2435 0.2874 -0.0160 0.0065  0.0208  1166 VAL B CB  
17584 C CG1 . VAL B 1168 ? 0.2647 0.2497 0.2931 -0.0210 0.0074  0.0241  1166 VAL B CG1 
17585 C CG2 . VAL B 1168 ? 0.2633 0.2509 0.2959 -0.0164 0.0058  0.0181  1166 VAL B CG2 
17586 N N   . GLU B 1169 ? 0.2751 0.2383 0.2894 -0.0159 0.0036  0.0261  1167 GLU B N   
17587 C CA  . GLU B 1169 ? 0.2706 0.2301 0.2801 -0.0157 0.0039  0.0291  1167 GLU B CA  
17588 C C   . GLU B 1169 ? 0.2868 0.2492 0.2974 -0.0212 0.0054  0.0323  1167 GLU B C   
17589 O O   . GLU B 1169 ? 0.3186 0.2792 0.3308 -0.0256 0.0045  0.0331  1167 GLU B O   
17590 C CB  . GLU B 1169 ? 0.2897 0.2368 0.2929 -0.0143 0.0011  0.0298  1167 GLU B CB  
17591 C CG  . GLU B 1169 ? 0.3129 0.2551 0.3107 -0.0143 0.0011  0.0331  1167 GLU B CG  
17592 C CD  . GLU B 1169 ? 0.3571 0.2859 0.3485 -0.0138 -0.0020 0.0342  1167 GLU B CD  
17593 O OE1 . GLU B 1169 ? 0.3176 0.2407 0.3088 -0.0141 -0.0041 0.0325  1167 GLU B OE1 
17594 O OE2 . GLU B 1169 ? 0.3676 0.2912 0.3539 -0.0129 -0.0024 0.0367  1167 GLU B OE2 
17595 N N   . GLY B 1170 ? 0.3137 0.2809 0.3235 -0.0211 0.0076  0.0342  1168 GLY B N   
17596 C CA  . GLY B 1170 ? 0.2943 0.2644 0.3046 -0.0262 0.0091  0.0376  1168 GLY B CA  
17597 C C   . GLY B 1170 ? 0.3168 0.2951 0.3274 -0.0252 0.0120  0.0385  1168 GLY B C   
17598 O O   . GLY B 1170 ? 0.3090 0.2906 0.3195 -0.0207 0.0127  0.0365  1168 GLY B O   
17599 N N   . ASP B 1171 ? 0.3405 0.3220 0.3512 -0.0296 0.0138  0.0418  1169 ASP B N   
17600 C CA  . ASP B 1171 ? 0.3354 0.3254 0.3465 -0.0289 0.0167  0.0426  1169 ASP B CA  
17601 C C   . ASP B 1171 ? 0.3713 0.3726 0.3892 -0.0287 0.0189  0.0399  1169 ASP B C   
17602 O O   . ASP B 1171 ? 0.3181 0.3206 0.3403 -0.0291 0.0179  0.0377  1169 ASP B O   
17603 C CB  . ASP B 1171 ? 0.3548 0.3442 0.3629 -0.0335 0.0180  0.0471  1169 ASP B CB  
17604 C CG  . ASP B 1171 ? 0.4309 0.4240 0.4430 -0.0395 0.0187  0.0488  1169 ASP B CG  
17605 O OD1 . ASP B 1171 ? 0.3692 0.3659 0.3868 -0.0403 0.0183  0.0465  1169 ASP B OD1 
17606 O OD2 . ASP B 1171 ? 0.5097 0.5022 0.5194 -0.0438 0.0197  0.0528  1169 ASP B OD2 
17607 N N   . ALA B 1172 ? 0.3442 0.3537 0.3627 -0.0277 0.0216  0.0401  1170 ALA B N   
17608 C CA  . ALA B 1172 ? 0.3110 0.3307 0.3351 -0.0264 0.0235  0.0372  1170 ALA B CA  
17609 C C   . ALA B 1172 ? 0.3403 0.3649 0.3701 -0.0305 0.0240  0.0374  1170 ALA B C   
17610 O O   . ALA B 1172 ? 0.3153 0.3438 0.3499 -0.0292 0.0236  0.0344  1170 ALA B O   
17611 C CB  . ALA B 1172 ? 0.3417 0.3688 0.3647 -0.0252 0.0264  0.0378  1170 ALA B CB  
17612 N N   . GLU B 1173 ? 0.3366 0.3614 0.3660 -0.0355 0.0247  0.0409  1171 GLU B N   
17613 C CA  . GLU B 1173 ? 0.3340 0.3643 0.3691 -0.0397 0.0251  0.0413  1171 GLU B CA  
17614 C C   . GLU B 1173 ? 0.2905 0.3143 0.3272 -0.0403 0.0219  0.0396  1171 GLU B C   
17615 O O   . GLU B 1173 ? 0.2999 0.3293 0.3424 -0.0409 0.0218  0.0376  1171 GLU B O   
17616 C CB  . GLU B 1173 ? 0.4260 0.4573 0.4599 -0.0454 0.0263  0.0458  1171 GLU B CB  
17617 N N   . ARG B 1174 ? 0.3135 0.3257 0.3451 -0.0401 0.0192  0.0404  1172 ARG B N   
17618 C CA  . ARG B 1174 ? 0.2913 0.2965 0.3235 -0.0402 0.0161  0.0386  1172 ARG B CA  
17619 C C   . ARG B 1174 ? 0.2602 0.2683 0.2954 -0.0353 0.0157  0.0343  1172 ARG B C   
17620 O O   . ARG B 1174 ? 0.3064 0.3160 0.3457 -0.0360 0.0145  0.0323  1172 ARG B O   
17621 C CB  . ARG B 1174 ? 0.3336 0.3255 0.3588 -0.0398 0.0135  0.0401  1172 ARG B CB  
17622 C CG  . ARG B 1174 ? 0.3062 0.2896 0.3308 -0.0393 0.0101  0.0381  1172 ARG B CG  
17623 C CD  . ARG B 1174 ? 0.3385 0.3229 0.3670 -0.0448 0.0091  0.0388  1172 ARG B CD  
17624 N NE  . ARG B 1174 ? 0.3700 0.3459 0.3973 -0.0441 0.0057  0.0367  1172 ARG B NE  
17625 C CZ  . ARG B 1174 ? 0.3973 0.3741 0.4284 -0.0474 0.0043  0.0358  1172 ARG B CZ  
17626 N NH1 . ARG B 1174 ? 0.3360 0.3225 0.3730 -0.0516 0.0058  0.0369  1172 ARG B NH1 
17627 N NH2 . ARG B 1174 ? 0.3367 0.3052 0.3659 -0.0461 0.0012  0.0337  1172 ARG B NH2 
17628 N N   . ILE B 1175 ? 0.2592 0.2682 0.2922 -0.0305 0.0166  0.0329  1173 ILE B N   
17629 C CA  . ILE B 1175 ? 0.2618 0.2734 0.2972 -0.0261 0.0162  0.0289  1173 ILE B CA  
17630 C C   . ILE B 1175 ? 0.2645 0.2863 0.3063 -0.0268 0.0178  0.0273  1173 ILE B C   
17631 O O   . ILE B 1175 ? 0.2479 0.2706 0.2929 -0.0257 0.0166  0.0246  1173 ILE B O   
17632 C CB  . ILE B 1175 ? 0.2979 0.3095 0.3298 -0.0216 0.0170  0.0281  1173 ILE B CB  
17633 C CG1 . ILE B 1175 ? 0.3204 0.3216 0.3464 -0.0199 0.0149  0.0291  1173 ILE B CG1 
17634 C CG2 . ILE B 1175 ? 0.2789 0.2950 0.3137 -0.0177 0.0172  0.0244  1173 ILE B CG2 
17635 C CD1 . ILE B 1175 ? 0.3218 0.3233 0.3442 -0.0161 0.0156  0.0290  1173 ILE B CD1 
17636 N N   . ARG B 1176 ? 0.2956 0.3255 0.3392 -0.0284 0.0206  0.0288  1174 ARG B N   
17637 C CA  . ARG B 1176 ? 0.2638 0.3040 0.3136 -0.0286 0.0221  0.0272  1174 ARG B CA  
17638 C C   . ARG B 1176 ? 0.2664 0.3072 0.3205 -0.0323 0.0206  0.0272  1174 ARG B C   
17639 O O   . ARG B 1176 ? 0.2622 0.3070 0.3207 -0.0310 0.0201  0.0246  1174 ARG B O   
17640 C CB  . ARG B 1176 ? 0.2791 0.3279 0.3297 -0.0298 0.0254  0.0290  1174 ARG B CB  
17641 C CG  . ARG B 1176 ? 0.3533 0.4131 0.4099 -0.0289 0.0272  0.0270  1174 ARG B CG  
17642 C CD  . ARG B 1176 ? 0.4071 0.4761 0.4652 -0.0311 0.0305  0.0292  1174 ARG B CD  
17643 N NE  . ARG B 1176 ? 0.4621 0.5296 0.5148 -0.0302 0.0321  0.0309  1174 ARG B NE  
17644 C CZ  . ARG B 1176 ? 0.5568 0.6276 0.6077 -0.0262 0.0337  0.0293  1174 ARG B CZ  
17645 N NH1 . ARG B 1176 ? 0.4876 0.5630 0.5415 -0.0226 0.0339  0.0258  1174 ARG B NH1 
17646 N NH2 . ARG B 1176 ? 0.5290 0.5980 0.5746 -0.0258 0.0349  0.0312  1174 ARG B NH2 
17647 N N   . ALA B 1177 ? 0.2620 0.2985 0.3148 -0.0370 0.0198  0.0303  1175 ALA B N   
17648 C CA  . ALA B 1177 ? 0.2607 0.2977 0.3175 -0.0410 0.0181  0.0305  1175 ALA B CA  
17649 C C   . ALA B 1177 ? 0.2330 0.2631 0.2895 -0.0390 0.0150  0.0277  1175 ALA B C   
17650 O O   . ALA B 1177 ? 0.2559 0.2896 0.3170 -0.0397 0.0140  0.0259  1175 ALA B O   
17651 C CB  . ALA B 1177 ? 0.2731 0.3052 0.3274 -0.0467 0.0175  0.0345  1175 ALA B CB  
17652 N N   . VAL B 1178 ? 0.2838 0.3040 0.3346 -0.0363 0.0134  0.0272  1176 VAL B N   
17653 C CA  . VAL B 1178 ? 0.2327 0.2464 0.2826 -0.0341 0.0106  0.0245  1176 VAL B CA  
17654 C C   . VAL B 1178 ? 0.2434 0.2632 0.2967 -0.0299 0.0113  0.0210  1176 VAL B C   
17655 O O   . VAL B 1178 ? 0.2770 0.2971 0.3330 -0.0297 0.0097  0.0189  1176 VAL B O   
17656 C CB  . VAL B 1178 ? 0.2786 0.2812 0.3216 -0.0318 0.0091  0.0249  1176 VAL B CB  
17657 C CG1 . VAL B 1178 ? 0.2651 0.2619 0.3071 -0.0287 0.0066  0.0218  1176 VAL B CG1 
17658 C CG2 . VAL B 1178 ? 0.2906 0.2857 0.3301 -0.0362 0.0078  0.0282  1176 VAL B CG2 
17659 N N   . ASN B 1179 ? 0.2537 0.2782 0.3065 -0.0268 0.0135  0.0205  1177 ASN B N   
17660 C CA  . ASN B 1179 ? 0.2673 0.2970 0.3227 -0.0229 0.0141  0.0174  1177 ASN B CA  
17661 C C   . ASN B 1179 ? 0.2714 0.3094 0.3331 -0.0244 0.0145  0.0165  1177 ASN B C   
17662 O O   . ASN B 1179 ? 0.2744 0.3135 0.3385 -0.0225 0.0134  0.0138  1177 ASN B O   
17663 C CB  . ASN B 1179 ? 0.2404 0.2736 0.2939 -0.0199 0.0164  0.0174  1177 ASN B CB  
17664 C CG  . ASN B 1179 ? 0.3505 0.3851 0.4043 -0.0155 0.0162  0.0142  1177 ASN B CG  
17665 O OD1 . ASN B 1179 ? 0.3237 0.3539 0.3770 -0.0140 0.0142  0.0124  1177 ASN B OD1 
17666 N ND2 . ASN B 1179 ? 0.2916 0.3321 0.3457 -0.0135 0.0183  0.0136  1177 ASN B ND2 
17667 N N   . LYS B 1180 ? 0.2618 0.3061 0.3263 -0.0279 0.0162  0.0187  1178 LYS B N   
17668 C CA  . LYS B 1180 ? 0.2325 0.2854 0.3033 -0.0296 0.0166  0.0180  1178 LYS B CA  
17669 C C   . LYS B 1180 ? 0.2572 0.3063 0.3300 -0.0318 0.0136  0.0173  1178 LYS B C   
17670 O O   . LYS B 1180 ? 0.2548 0.3081 0.3316 -0.0307 0.0128  0.0151  1178 LYS B O   
17671 C CB  . LYS B 1180 ? 0.2840 0.3443 0.3573 -0.0332 0.0190  0.0209  1178 LYS B CB  
17672 N N   . ALA B 1181 ? 0.2405 0.2811 0.3099 -0.0349 0.0117  0.0191  1179 ALA B N   
17673 C CA  . ALA B 1181 ? 0.2289 0.2650 0.2994 -0.0371 0.0086  0.0183  1179 ALA B CA  
17674 C C   . ALA B 1181 ? 0.2307 0.2623 0.2997 -0.0328 0.0068  0.0150  1179 ALA B C   
17675 O O   . ALA B 1181 ? 0.2401 0.2729 0.3121 -0.0331 0.0050  0.0132  1179 ALA B O   
17676 C CB  . ALA B 1181 ? 0.2463 0.2729 0.3125 -0.0410 0.0069  0.0208  1179 ALA B CB  
17677 N N   . ILE B 1182 ? 0.2394 0.2662 0.3038 -0.0289 0.0072  0.0141  1180 ILE B N   
17678 C CA  . ILE B 1182 ? 0.2418 0.2648 0.3046 -0.0250 0.0058  0.0112  1180 ILE B CA  
17679 C C   . ILE B 1182 ? 0.2258 0.2569 0.2930 -0.0225 0.0066  0.0089  1180 ILE B C   
17680 O O   . ILE B 1182 ? 0.2249 0.2551 0.2932 -0.0213 0.0048  0.0067  1180 ILE B O   
17681 C CB  . ILE B 1182 ? 0.2578 0.2749 0.3151 -0.0215 0.0062  0.0111  1180 ILE B CB  
17682 C CG1 . ILE B 1182 ? 0.2469 0.2540 0.2993 -0.0232 0.0043  0.0126  1180 ILE B CG1 
17683 C CG2 . ILE B 1182 ? 0.2680 0.2843 0.3245 -0.0172 0.0055  0.0081  1180 ILE B CG2 
17684 C CD1 . ILE B 1182 ? 0.2770 0.2788 0.3240 -0.0201 0.0048  0.0131  1180 ILE B CD1 
17685 N N   . ALA B 1183 ? 0.2612 0.3001 0.3307 -0.0217 0.0092  0.0094  1181 ALA B N   
17686 C CA  . ALA B 1183 ? 0.2636 0.3097 0.3369 -0.0192 0.0099  0.0072  1181 ALA B CA  
17687 C C   . ALA B 1183 ? 0.2700 0.3207 0.3486 -0.0214 0.0086  0.0067  1181 ALA B C   
17688 O O   . ALA B 1183 ? 0.3029 0.3568 0.3838 -0.0191 0.0080  0.0045  1181 ALA B O   
17689 C CB  . ALA B 1183 ? 0.2683 0.3217 0.3427 -0.0180 0.0130  0.0078  1181 ALA B CB  
17690 N N   . ALA B 1184 ? 0.2354 0.2862 0.3156 -0.0260 0.0079  0.0088  1182 ALA B N   
17691 C CA  . ALA B 1184 ? 0.2855 0.3409 0.3708 -0.0286 0.0065  0.0085  1182 ALA B CA  
17692 C C   . ALA B 1184 ? 0.2519 0.2998 0.3356 -0.0292 0.0030  0.0072  1182 ALA B C   
17693 O O   . ALA B 1184 ? 0.2638 0.3148 0.3514 -0.0313 0.0013  0.0067  1182 ALA B O   
17694 C CB  . ALA B 1184 ? 0.2816 0.3416 0.3698 -0.0338 0.0073  0.0115  1182 ALA B CB  
17695 N N   . LEU B 1185 ? 0.2255 0.2639 0.3035 -0.0273 0.0019  0.0064  1183 LEU B N   
17696 C CA  . LEU B 1185 ? 0.2238 0.2551 0.2999 -0.0276 -0.0012 0.0050  1183 LEU B CA  
17697 C C   . LEU B 1185 ? 0.2538 0.2884 0.3321 -0.0246 -0.0021 0.0023  1183 LEU B C   
17698 O O   . LEU B 1185 ? 0.2890 0.3268 0.3673 -0.0209 -0.0005 0.0011  1183 LEU B O   
17699 C CB  . LEU B 1185 ? 0.2423 0.2632 0.3117 -0.0258 -0.0020 0.0048  1183 LEU B CB  
17700 C CG  . LEU B 1185 ? 0.2082 0.2238 0.2742 -0.0285 -0.0016 0.0075  1183 LEU B CG  
17701 C CD1 . LEU B 1185 ? 0.2322 0.2386 0.2917 -0.0254 -0.0021 0.0069  1183 LEU B CD1 
17702 C CD2 . LEU B 1185 ? 0.2338 0.2466 0.3007 -0.0337 -0.0038 0.0088  1183 LEU B CD2 
17703 N N   . PRO B 1186 ? 0.2638 0.2971 0.3435 -0.0260 -0.0048 0.0012  1184 PRO B N   
17704 C CA  . PRO B 1186 ? 0.2743 0.3096 0.3554 -0.0231 -0.0060 -0.0013 1184 PRO B CA  
17705 C C   . PRO B 1186 ? 0.2544 0.2824 0.3299 -0.0194 -0.0065 -0.0030 1184 PRO B C   
17706 O O   . PRO B 1186 ? 0.2818 0.3025 0.3525 -0.0193 -0.0065 -0.0024 1184 PRO B O   
17707 C CB  . PRO B 1186 ? 0.3392 0.3740 0.4224 -0.0262 -0.0090 -0.0017 1184 PRO B CB  
17708 C CG  . PRO B 1186 ? 0.3269 0.3538 0.4065 -0.0297 -0.0101 -0.0001 1184 PRO B CG  
17709 C CD  . PRO B 1186 ? 0.2823 0.3108 0.3615 -0.0305 -0.0073 0.0022  1184 PRO B CD  
17710 N N   . GLY B 1187 ? 0.2606 0.2908 0.3368 -0.0163 -0.0068 -0.0050 1185 GLY B N   
17711 C CA  . GLY B 1187 ? 0.2753 0.2995 0.3466 -0.0131 -0.0074 -0.0066 1185 GLY B CA  
17712 C C   . GLY B 1187 ? 0.2677 0.2924 0.3369 -0.0101 -0.0049 -0.0064 1185 GLY B C   
17713 O O   . GLY B 1187 ? 0.3003 0.3312 0.3722 -0.0093 -0.0030 -0.0061 1185 GLY B O   
17714 N N   . PRO B 1188 ? 0.2094 0.2277 0.2736 -0.0084 -0.0050 -0.0068 1186 PRO B N   
17715 C CA  . PRO B 1188 ? 0.2352 0.2542 0.2973 -0.0056 -0.0030 -0.0069 1186 PRO B CA  
17716 C C   . PRO B 1188 ? 0.2490 0.2706 0.3117 -0.0064 -0.0008 -0.0050 1186 PRO B C   
17717 O O   . PRO B 1188 ? 0.2546 0.2751 0.3177 -0.0091 -0.0007 -0.0033 1186 PRO B O   
17718 C CB  . PRO B 1188 ? 0.2955 0.3072 0.3523 -0.0040 -0.0039 -0.0075 1186 PRO B CB  
17719 C CG  . PRO B 1188 ? 0.3794 0.3860 0.4351 -0.0064 -0.0058 -0.0071 1186 PRO B CG  
17720 C CD  . PRO B 1188 ? 0.2823 0.2928 0.3425 -0.0089 -0.0070 -0.0072 1186 PRO B CD  
17721 N N   . LEU B 1189 ? 0.2296 0.2546 0.2922 -0.0042 0.0010  -0.0052 1187 LEU B N   
17722 C CA  . LEU B 1189 ? 0.2329 0.2602 0.2953 -0.0044 0.0033  -0.0036 1187 LEU B CA  
17723 C C   . LEU B 1189 ? 0.2694 0.2907 0.3271 -0.0037 0.0034  -0.0029 1187 LEU B C   
17724 O O   . LEU B 1189 ? 0.2920 0.3109 0.3469 -0.0012 0.0031  -0.0040 1187 LEU B O   
17725 C CB  . LEU B 1189 ? 0.2263 0.2587 0.2896 -0.0021 0.0049  -0.0044 1187 LEU B CB  
17726 C CG  . LEU B 1189 ? 0.2777 0.3171 0.3457 -0.0025 0.0056  -0.0047 1187 LEU B CG  
17727 C CD1 . LEU B 1189 ? 0.3652 0.4051 0.4353 -0.0021 0.0035  -0.0064 1187 LEU B CD1 
17728 C CD2 . LEU B 1189 ? 0.2638 0.3071 0.3315 -0.0003 0.0075  -0.0052 1187 LEU B CD2 
17729 N N   . LEU B 1190 ? 0.2225 0.2417 0.2793 -0.0058 0.0037  -0.0009 1188 LEU B N   
17730 C CA  . LEU B 1190 ? 0.2305 0.2433 0.2826 -0.0049 0.0034  -0.0002 1188 LEU B CA  
17731 C C   . LEU B 1190 ? 0.2328 0.2475 0.2832 -0.0031 0.0053  0.0006  1188 LEU B C   
17732 O O   . LEU B 1190 ? 0.2271 0.2466 0.2793 -0.0040 0.0071  0.0018  1188 LEU B O   
17733 C CB  . LEU B 1190 ? 0.2370 0.2453 0.2881 -0.0080 0.0025  0.0017  1188 LEU B CB  
17734 C CG  . LEU B 1190 ? 0.2284 0.2336 0.2806 -0.0102 0.0002  0.0011  1188 LEU B CG  
17735 C CD1 . LEU B 1190 ? 0.2473 0.2459 0.2967 -0.0128 -0.0009 0.0029  1188 LEU B CD1 
17736 C CD2 . LEU B 1190 ? 0.2661 0.2679 0.3164 -0.0077 -0.0015 -0.0014 1188 LEU B CD2 
17737 N N   . LEU B 1191 ? 0.2490 0.2602 0.2959 -0.0005 0.0050  0.0000  1189 LEU B N   
17738 C CA  . LEU B 1191 ? 0.2294 0.2414 0.2739 0.0011  0.0064  0.0009  1189 LEU B CA  
17739 C C   . LEU B 1191 ? 0.2545 0.2622 0.2965 -0.0002 0.0064  0.0032  1189 LEU B C   
17740 O O   . LEU B 1191 ? 0.2845 0.2860 0.3237 0.0003  0.0050  0.0033  1189 LEU B O   
17741 C CB  . LEU B 1191 ? 0.2611 0.2715 0.3031 0.0042  0.0059  -0.0005 1189 LEU B CB  
17742 C CG  . LEU B 1191 ? 0.2544 0.2679 0.2951 0.0061  0.0073  -0.0003 1189 LEU B CG  
17743 C CD1 . LEU B 1191 ? 0.2579 0.2714 0.2973 0.0086  0.0067  -0.0019 1189 LEU B CD1 
17744 C CD2 . LEU B 1191 ? 0.2453 0.2563 0.2832 0.0063  0.0078  0.0017  1189 LEU B CD2 
17745 N N   . VAL B 1192 ? 0.2299 0.2409 0.2729 -0.0019 0.0080  0.0050  1190 VAL B N   
17746 C CA  . VAL B 1192 ? 0.2277 0.2351 0.2685 -0.0038 0.0081  0.0075  1190 VAL B CA  
17747 C C   . VAL B 1192 ? 0.2493 0.2559 0.2865 -0.0016 0.0090  0.0085  1190 VAL B C   
17748 O O   . VAL B 1192 ? 0.2777 0.2894 0.3155 -0.0002 0.0105  0.0081  1190 VAL B O   
17749 C CB  . VAL B 1192 ? 0.2822 0.2941 0.3261 -0.0073 0.0094  0.0091  1190 VAL B CB  
17750 C CG1 . VAL B 1192 ? 0.2515 0.2595 0.2928 -0.0096 0.0095  0.0121  1190 VAL B CG1 
17751 C CG2 . VAL B 1192 ? 0.2550 0.2684 0.3029 -0.0094 0.0083  0.0081  1190 VAL B CG2 
17752 N N   . GLN B 1193 ? 0.2310 0.2309 0.2643 -0.0012 0.0079  0.0098  1191 GLN B N   
17753 C CA  . GLN B 1193 ? 0.2252 0.2239 0.2549 0.0006  0.0085  0.0113  1191 GLN B CA  
17754 C C   . GLN B 1193 ? 0.2729 0.2673 0.3003 -0.0021 0.0084  0.0142  1191 GLN B C   
17755 O O   . GLN B 1193 ? 0.2520 0.2402 0.2782 -0.0037 0.0068  0.0148  1191 GLN B O   
17756 C CB  . GLN B 1193 ? 0.2407 0.2350 0.2672 0.0041  0.0071  0.0102  1191 GLN B CB  
17757 C CG  . GLN B 1193 ? 0.2275 0.2256 0.2558 0.0065  0.0070  0.0075  1191 GLN B CG  
17758 C CD  . GLN B 1193 ? 0.2655 0.2611 0.2907 0.0101  0.0062  0.0069  1191 GLN B CD  
17759 O OE1 . GLN B 1193 ? 0.2769 0.2739 0.3003 0.0117  0.0068  0.0078  1191 GLN B OE1 
17760 N NE2 . GLN B 1193 ? 0.2521 0.2443 0.2766 0.0116  0.0048  0.0053  1191 GLN B NE2 
17761 N N   . ALA B 1194 ? 0.2779 0.2753 0.3044 -0.0026 0.0101  0.0161  1192 ALA B N   
17762 C CA  . ALA B 1194 ? 0.2737 0.2675 0.2977 -0.0054 0.0102  0.0192  1192 ALA B CA  
17763 C C   . ALA B 1194 ? 0.2874 0.2788 0.3068 -0.0033 0.0104  0.0209  1192 ALA B C   
17764 O O   . ALA B 1194 ? 0.3339 0.3294 0.3531 -0.0005 0.0112  0.0199  1192 ALA B O   
17765 C CB  . ALA B 1194 ? 0.3049 0.3052 0.3323 -0.0090 0.0122  0.0205  1192 ALA B CB  
17766 N N   . ALA B 1195 ? 0.2876 0.2722 0.3032 -0.0048 0.0094  0.0235  1193 ALA B N   
17767 C CA  . ALA B 1195 ? 0.2914 0.2731 0.3022 -0.0030 0.0094  0.0255  1193 ALA B CA  
17768 C C   . ALA B 1195 ? 0.3474 0.3238 0.3552 -0.0067 0.0092  0.0290  1193 ALA B C   
17769 O O   . ALA B 1195 ? 0.3016 0.2740 0.3101 -0.0099 0.0082  0.0296  1193 ALA B O   
17770 C CB  . ALA B 1195 ? 0.3031 0.2792 0.3107 0.0014  0.0074  0.0243  1193 ALA B CB  
17771 N N   . SER B 1196 ? 0.3434 0.3199 0.3477 -0.0064 0.0100  0.0315  1194 SER B N   
17772 C CA  . SER B 1196 ? 0.3400 0.3102 0.3403 -0.0095 0.0095  0.0352  1194 SER B CA  
17773 C C   . SER B 1196 ? 0.3523 0.3114 0.3472 -0.0071 0.0066  0.0357  1194 SER B C   
17774 O O   . SER B 1196 ? 0.3416 0.2995 0.3356 -0.0024 0.0055  0.0335  1194 SER B O   
17775 C CB  . SER B 1196 ? 0.3222 0.2964 0.3203 -0.0100 0.0114  0.0377  1194 SER B CB  
17776 O OG  . SER B 1196 ? 0.3977 0.3711 0.3925 -0.0054 0.0108  0.0372  1194 SER B OG  
17777 N N   . SER B 1197 ? 0.3289 0.2800 0.3202 -0.0103 0.0054  0.0386  1195 SER B N   
17778 C CA  . SER B 1197 ? 0.3501 0.2897 0.3353 -0.0079 0.0026  0.0395  1195 SER B CA  
17779 C C   . SER B 1197 ? 0.3368 0.2765 0.3183 -0.0032 0.0025  0.0400  1195 SER B C   
17780 O O   . SER B 1197 ? 0.3754 0.3101 0.3542 0.0015  0.0005  0.0386  1195 SER B O   
17781 C CB  . SER B 1197 ? 0.3917 0.3227 0.3728 -0.0127 0.0015  0.0432  1195 SER B CB  
17782 O OG  . SER B 1197 ? 0.3953 0.3256 0.3797 -0.0171 0.0011  0.0428  1195 SER B OG  
17783 N N   . GLY B 1198 ? 0.3830 0.3288 0.3643 -0.0042 0.0046  0.0419  1196 GLY B N   
17784 C CA  . GLY B 1198 ? 0.4264 0.3730 0.4043 0.0001  0.0045  0.0424  1196 GLY B CA  
17785 C C   . GLY B 1198 ? 0.4414 0.3944 0.4226 0.0048  0.0046  0.0387  1196 GLY B C   
17786 O O   . GLY B 1198 ? 0.4102 0.3611 0.3887 0.0094  0.0032  0.0381  1196 GLY B O   
17787 N N   . GLU B 1199 ? 0.3622 0.3234 0.3493 0.0036  0.0063  0.0361  1197 GLU B N   
17788 C CA  . GLU B 1199 ? 0.3880 0.3551 0.3782 0.0075  0.0064  0.0327  1197 GLU B CA  
17789 C C   . GLU B 1199 ? 0.4027 0.3639 0.3921 0.0108  0.0041  0.0308  1197 GLU B C   
17790 O O   . GLU B 1199 ? 0.4181 0.3809 0.4070 0.0152  0.0033  0.0292  1197 GLU B O   
17791 C CB  . GLU B 1199 ? 0.4284 0.4041 0.4246 0.0054  0.0084  0.0306  1197 GLU B CB  
17792 N N   . ILE B 1200 ? 0.3333 0.2879 0.3224 0.0087  0.0029  0.0308  1198 ILE B N   
17793 C CA  . ILE B 1200 ? 0.3461 0.2944 0.3338 0.0119  0.0006  0.0289  1198 ILE B CA  
17794 C C   . ILE B 1200 ? 0.4261 0.3679 0.4080 0.0161  -0.0012 0.0301  1198 ILE B C   
17795 O O   . ILE B 1200 ? 0.3778 0.3192 0.3592 0.0209  -0.0024 0.0280  1198 ILE B O   
17796 C CB  . ILE B 1200 ? 0.3272 0.2685 0.3147 0.0084  -0.0005 0.0290  1198 ILE B CB  
17797 C CG1 . ILE B 1200 ? 0.3222 0.2708 0.3160 0.0053  0.0010  0.0271  1198 ILE B CG1 
17798 C CG2 . ILE B 1200 ? 0.3490 0.2816 0.3333 0.0119  -0.0032 0.0274  1198 ILE B CG2 
17799 C CD1 . ILE B 1200 ? 0.3474 0.2902 0.3416 0.0014  -0.0002 0.0272  1198 ILE B CD1 
17800 N N   . ALA B 1201 ? 0.4085 0.3455 0.3860 0.0146  -0.0015 0.0336  1199 ALA B N   
17801 C CA  . ALA B 1201 ? 0.4432 0.3733 0.4148 0.0187  -0.0035 0.0350  1199 ALA B CA  
17802 C C   . ALA B 1201 ? 0.4233 0.3609 0.3954 0.0229  -0.0029 0.0344  1199 ALA B C   
17803 O O   . ALA B 1201 ? 0.4968 0.4320 0.4664 0.0280  -0.0046 0.0337  1199 ALA B O   
17804 C CB  . ALA B 1201 ? 0.4460 0.3683 0.4124 0.0155  -0.0042 0.0391  1199 ALA B CB  
17805 N N   . ARG B 1202 ? 0.4440 0.3910 0.4194 0.0208  -0.0005 0.0345  1200 ARG B N   
17806 C CA  . ARG B 1202 ? 0.4739 0.4283 0.4497 0.0239  0.0001  0.0341  1200 ARG B CA  
17807 C C   . ARG B 1202 ? 0.5137 0.4755 0.4941 0.0267  0.0004  0.0305  1200 ARG B C   
17808 O O   . ARG B 1202 ? 0.4834 0.4481 0.4632 0.0310  -0.0004 0.0297  1200 ARG B O   
17809 C CB  . ARG B 1202 ? 0.5462 0.5070 0.5230 0.0204  0.0023  0.0358  1200 ARG B CB  
17810 C CG  . ARG B 1202 ? 0.6320 0.5868 0.6040 0.0173  0.0024  0.0398  1200 ARG B CG  
17811 C CD  . ARG B 1202 ? 0.6947 0.6569 0.6675 0.0145  0.0048  0.0411  1200 ARG B CD  
17812 N NE  . ARG B 1202 ? 0.6453 0.6160 0.6241 0.0123  0.0070  0.0387  1200 ARG B NE  
17813 C CZ  . ARG B 1202 ? 0.6291 0.6014 0.6103 0.0078  0.0087  0.0393  1200 ARG B CZ  
17814 N NH1 . ARG B 1202 ? 0.6468 0.6133 0.6252 0.0042  0.0087  0.0424  1200 ARG B NH1 
17815 N NH2 . ARG B 1202 ? 0.6080 0.5881 0.5946 0.0067  0.0105  0.0367  1200 ARG B NH2 
17816 N N   . ASN B 1203 ? 0.4238 0.3891 0.4089 0.0243  0.0016  0.0283  1201 ASN B N   
17817 C CA  . ASN B 1203 ? 0.4458 0.4192 0.4355 0.0260  0.0023  0.0252  1201 ASN B CA  
17818 C C   . ASN B 1203 ? 0.4290 0.3994 0.4200 0.0278  0.0011  0.0228  1201 ASN B C   
17819 O O   . ASN B 1203 ? 0.3741 0.3420 0.3668 0.0250  0.0014  0.0221  1201 ASN B O   
17820 C CB  . ASN B 1203 ? 0.4318 0.4123 0.4258 0.0221  0.0046  0.0245  1201 ASN B CB  
17821 C CG  . ASN B 1203 ? 0.4133 0.4014 0.4117 0.0234  0.0052  0.0214  1201 ASN B CG  
17822 O OD1 . ASN B 1203 ? 0.4824 0.4719 0.4809 0.0270  0.0042  0.0200  1201 ASN B OD1 
17823 N ND2 . ASN B 1203 ? 0.4536 0.4469 0.4556 0.0204  0.0069  0.0204  1201 ASN B ND2 
17824 N N   . PRO B 1204 ? 0.4655 0.4365 0.4558 0.0325  -0.0001 0.0214  1202 PRO B N   
17825 C CA  . PRO B 1204 ? 0.4258 0.3943 0.4170 0.0345  -0.0010 0.0190  1202 PRO B CA  
17826 C C   . PRO B 1204 ? 0.4060 0.3805 0.4023 0.0323  0.0003  0.0165  1202 PRO B C   
17827 O O   . PRO B 1204 ? 0.4452 0.4168 0.4421 0.0327  -0.0003 0.0147  1202 PRO B O   
17828 C CB  . PRO B 1204 ? 0.5572 0.5278 0.5470 0.0401  -0.0021 0.0181  1202 PRO B CB  
17829 C CG  . PRO B 1204 ? 0.5038 0.4815 0.4942 0.0403  -0.0013 0.0193  1202 PRO B CG  
17830 C CD  . PRO B 1204 ? 0.5297 0.5043 0.5183 0.0363  -0.0006 0.0220  1202 PRO B CD  
17831 N N   . ASP B 1205 ? 0.3622 0.3444 0.3617 0.0301  0.0020  0.0164  1203 ASP B N   
17832 C CA  . ASP B 1205 ? 0.4402 0.4276 0.4442 0.0280  0.0032  0.0143  1203 ASP B CA  
17833 C C   . ASP B 1205 ? 0.4237 0.4109 0.4294 0.0233  0.0044  0.0152  1203 ASP B C   
17834 O O   . ASP B 1205 ? 0.3841 0.3771 0.3934 0.0214  0.0057  0.0139  1203 ASP B O   
17835 C CB  . ASP B 1205 ? 0.4093 0.4056 0.4158 0.0291  0.0041  0.0131  1203 ASP B CB  
17836 C CG  . ASP B 1205 ? 0.5171 0.5155 0.5233 0.0333  0.0031  0.0117  1203 ASP B CG  
17837 O OD1 . ASP B 1205 ? 0.4482 0.4420 0.4533 0.0353  0.0020  0.0108  1203 ASP B OD1 
17838 O OD2 . ASP B 1205 ? 0.5532 0.5579 0.5602 0.0346  0.0033  0.0115  1203 ASP B OD2 
17839 N N   . ALA B 1206 ? 0.3807 0.3613 0.3837 0.0214  0.0040  0.0174  1204 ALA B N   
17840 C CA  . ALA B 1206 ? 0.3741 0.3551 0.3789 0.0168  0.0051  0.0184  1204 ALA B CA  
17841 C C   . ALA B 1206 ? 0.3673 0.3502 0.3762 0.0151  0.0054  0.0162  1204 ALA B C   
17842 O O   . ALA B 1206 ? 0.3439 0.3320 0.3561 0.0124  0.0069  0.0159  1204 ALA B O   
17843 C CB  . ALA B 1206 ? 0.3804 0.3530 0.3814 0.0149  0.0042  0.0211  1204 ALA B CB  
17844 N N   . TYR B 1207 ? 0.2981 0.2770 0.3066 0.0168  0.0039  0.0145  1205 TYR B N   
17845 C CA  . TYR B 1207 ? 0.3009 0.2819 0.3129 0.0159  0.0040  0.0121  1205 TYR B CA  
17846 C C   . TYR B 1207 ? 0.2997 0.2848 0.3126 0.0193  0.0039  0.0098  1205 TYR B C   
17847 O O   . TYR B 1207 ? 0.3925 0.3753 0.4028 0.0229  0.0029  0.0096  1205 TYR B O   
17848 C CB  . TYR B 1207 ? 0.2873 0.2605 0.2979 0.0148  0.0023  0.0119  1205 TYR B CB  
17849 C CG  . TYR B 1207 ? 0.2687 0.2378 0.2785 0.0108  0.0022  0.0143  1205 TYR B CG  
17850 C CD1 . TYR B 1207 ? 0.2606 0.2349 0.2742 0.0069  0.0038  0.0148  1205 TYR B CD1 
17851 C CD2 . TYR B 1207 ? 0.2762 0.2362 0.2814 0.0108  0.0006  0.0160  1205 TYR B CD2 
17852 C CE1 . TYR B 1207 ? 0.2463 0.2178 0.2595 0.0029  0.0038  0.0172  1205 TYR B CE1 
17853 C CE2 . TYR B 1207 ? 0.3043 0.2605 0.3086 0.0065  0.0005  0.0184  1205 TYR B CE2 
17854 C CZ  . TYR B 1207 ? 0.2774 0.2399 0.2860 0.0025  0.0022  0.0191  1205 TYR B CZ  
17855 O OH  . TYR B 1207 ? 0.2828 0.2425 0.2909 -0.0021 0.0023  0.0216  1205 TYR B OH  
17856 N N   . CYS B 1208 ? 0.2368 0.2283 0.2535 0.0183  0.0050  0.0083  1206 CYS B N   
17857 C CA  . CYS B 1208 ? 0.2315 0.2279 0.2494 0.0208  0.0051  0.0063  1206 CYS B CA  
17858 C C   . CYS B 1208 ? 0.2238 0.2182 0.2424 0.0216  0.0041  0.0043  1206 CYS B C   
17859 O O   . CYS B 1208 ? 0.2262 0.2201 0.2469 0.0191  0.0041  0.0035  1206 CYS B O   
17860 C CB  . CYS B 1208 ? 0.2913 0.2948 0.3122 0.0193  0.0065  0.0058  1206 CYS B CB  
17861 S SG  . CYS B 1208 ? 0.2878 0.2973 0.3100 0.0215  0.0066  0.0038  1206 CYS B SG  
17862 N N   . LEU B 1209 ? 0.2258 0.2195 0.2427 0.0251  0.0033  0.0033  1207 LEU B N   
17863 C CA  . LEU B 1209 ? 0.2143 0.2060 0.2311 0.0261  0.0025  0.0013  1207 LEU B CA  
17864 C C   . LEU B 1209 ? 0.2223 0.2200 0.2424 0.0252  0.0032  -0.0004 1207 LEU B C   
17865 O O   . LEU B 1209 ? 0.2244 0.2208 0.2449 0.0252  0.0027  -0.0020 1207 LEU B O   
17866 C CB  . LEU B 1209 ? 0.1928 0.1823 0.2066 0.0304  0.0015  0.0007  1207 LEU B CB  
17867 C CG  . LEU B 1209 ? 0.2522 0.2347 0.2620 0.0320  0.0005  0.0023  1207 LEU B CG  
17868 C CD1 . LEU B 1209 ? 0.3105 0.2908 0.3174 0.0368  -0.0006 0.0011  1207 LEU B CD1 
17869 C CD2 . LEU B 1209 ? 0.2846 0.2597 0.2933 0.0290  -0.0004 0.0031  1207 LEU B CD2 
17870 N N   . ASN B 1210 ? 0.2243 0.2283 0.2464 0.0244  0.0044  -0.0001 1208 ASN B N   
17871 C CA  . ASN B 1210 ? 0.2491 0.2580 0.2738 0.0234  0.0049  -0.0015 1208 ASN B CA  
17872 C C   . ASN B 1210 ? 0.2519 0.2589 0.2784 0.0207  0.0048  -0.0022 1208 ASN B C   
17873 O O   . ASN B 1210 ? 0.2484 0.2569 0.2762 0.0205  0.0046  -0.0038 1208 ASN B O   
17874 C CB  . ASN B 1210 ? 0.2829 0.2975 0.3090 0.0224  0.0060  -0.0010 1208 ASN B CB  
17875 C CG  . ASN B 1210 ? 0.2783 0.2958 0.3028 0.0248  0.0060  -0.0004 1208 ASN B CG  
17876 O OD1 . ASN B 1210 ? 0.3431 0.3583 0.3655 0.0274  0.0054  0.0000  1208 ASN B OD1 
17877 N ND2 . ASN B 1210 ? 0.3464 0.3690 0.3719 0.0241  0.0067  -0.0002 1208 ASN B ND2 
17878 N N   . TRP B 1211 ? 0.2064 0.2105 0.2332 0.0187  0.0048  -0.0010 1209 TRP B N   
17879 C CA  . TRP B 1211 ? 0.2153 0.2189 0.2446 0.0159  0.0047  -0.0015 1209 TRP B CA  
17880 C C   . TRP B 1211 ? 0.2308 0.2286 0.2590 0.0156  0.0033  -0.0021 1209 TRP B C   
17881 O O   . TRP B 1211 ? 0.2566 0.2539 0.2868 0.0133  0.0029  -0.0025 1209 TRP B O   
17882 C CB  . TRP B 1211 ? 0.2900 0.2947 0.3205 0.0135  0.0057  0.0002  1209 TRP B CB  
17883 C CG  . TRP B 1211 ? 0.2468 0.2560 0.2772 0.0141  0.0070  0.0009  1209 TRP B CG  
17884 C CD1 . TRP B 1211 ? 0.2664 0.2754 0.2954 0.0138  0.0076  0.0028  1209 TRP B CD1 
17885 C CD2 . TRP B 1211 ? 0.2216 0.2357 0.2530 0.0149  0.0075  -0.0003 1209 TRP B CD2 
17886 N NE1 . TRP B 1211 ? 0.2549 0.2686 0.2838 0.0146  0.0085  0.0027  1209 TRP B NE1 
17887 C CE2 . TRP B 1211 ? 0.2484 0.2652 0.2789 0.0152  0.0084  0.0009  1209 TRP B CE2 
17888 C CE3 . TRP B 1211 ? 0.2444 0.2608 0.2770 0.0153  0.0072  -0.0021 1209 TRP B CE3 
17889 C CZ2 . TRP B 1211 ? 0.2391 0.2604 0.2699 0.0157  0.0089  0.0001  1209 TRP B CZ2 
17890 C CZ3 . TRP B 1211 ? 0.2449 0.2656 0.2778 0.0158  0.0077  -0.0026 1209 TRP B CZ3 
17891 C CH2 . TRP B 1211 ? 0.2535 0.2766 0.2855 0.0159  0.0085  -0.0016 1209 TRP B CH2 
17892 N N   . LEU B 1212 ? 0.2153 0.2086 0.2402 0.0180  0.0023  -0.0022 1210 LEU B N   
17893 C CA  . LEU B 1212 ? 0.2038 0.1905 0.2267 0.0180  0.0007  -0.0028 1210 LEU B CA  
17894 C C   . LEU B 1212 ? 0.2095 0.1961 0.2315 0.0202  0.0000  -0.0050 1210 LEU B C   
17895 O O   . LEU B 1212 ? 0.2095 0.1904 0.2291 0.0209  -0.0014 -0.0059 1210 LEU B O   
17896 C CB  . LEU B 1212 ? 0.2026 0.1830 0.2217 0.0192  -0.0001 -0.0014 1210 LEU B CB  
17897 C CG  . LEU B 1212 ? 0.2000 0.1791 0.2198 0.0161  0.0003  0.0009  1210 LEU B CG  
17898 C CD1 . LEU B 1212 ? 0.2476 0.2216 0.2634 0.0177  -0.0002 0.0026  1210 LEU B CD1 
17899 C CD2 . LEU B 1212 ? 0.2244 0.2002 0.2454 0.0125  -0.0006 0.0009  1210 LEU B CD2 
17900 N N   . VAL B 1213 ? 0.2278 0.2205 0.2513 0.0213  0.0010  -0.0058 1211 VAL B N   
17901 C CA  . VAL B 1213 ? 0.2198 0.2135 0.2427 0.0229  0.0006  -0.0077 1211 VAL B CA  
17902 C C   . VAL B 1213 ? 0.2198 0.2176 0.2459 0.0205  0.0009  -0.0084 1211 VAL B C   
17903 O O   . VAL B 1213 ? 0.2309 0.2319 0.2595 0.0186  0.0018  -0.0075 1211 VAL B O   
17904 C CB  . VAL B 1213 ? 0.2153 0.2128 0.2369 0.0261  0.0012  -0.0080 1211 VAL B CB  
17905 C CG1 . VAL B 1213 ? 0.2360 0.2290 0.2541 0.0292  0.0006  -0.0078 1211 VAL B CG1 
17906 C CG2 . VAL B 1213 ? 0.2368 0.2403 0.2605 0.0254  0.0026  -0.0069 1211 VAL B CG2 
17907 N N   . GLU B 1214 ? 0.2370 0.2343 0.2626 0.0209  0.0002  -0.0100 1212 GLU B N   
17908 C CA  . GLU B 1214 ? 0.2579 0.2586 0.2859 0.0192  0.0003  -0.0107 1212 GLU B CA  
17909 C C   . GLU B 1214 ? 0.1861 0.1912 0.2136 0.0207  0.0010  -0.0114 1212 GLU B C   
17910 O O   . GLU B 1214 ? 0.2052 0.2095 0.2301 0.0230  0.0007  -0.0122 1212 GLU B O   
17911 C CB  . GLU B 1214 ? 0.2635 0.2606 0.2914 0.0180  -0.0012 -0.0118 1212 GLU B CB  
17912 C CG  . GLU B 1214 ? 0.3027 0.3033 0.3330 0.0164  -0.0012 -0.0124 1212 GLU B CG  
17913 C CD  . GLU B 1214 ? 0.4426 0.4402 0.4726 0.0155  -0.0029 -0.0137 1212 GLU B CD  
17914 O OE1 . GLU B 1214 ? 0.4168 0.4097 0.4458 0.0150  -0.0041 -0.0138 1212 GLU B OE1 
17915 O OE2 . GLU B 1214 ? 0.4957 0.4955 0.5263 0.0153  -0.0031 -0.0145 1212 GLU B OE2 
17916 N N   . GLU B 1215 ? 0.2024 0.2119 0.2319 0.0194  0.0017  -0.0110 1213 GLU B N   
17917 C CA  . GLU B 1215 ? 0.1766 0.1903 0.2057 0.0201  0.0022  -0.0115 1213 GLU B CA  
17918 C C   . GLU B 1215 ? 0.1865 0.1994 0.2153 0.0194  0.0014  -0.0127 1213 GLU B C   
17919 O O   . GLU B 1215 ? 0.1929 0.2045 0.2233 0.0176  0.0007  -0.0129 1213 GLU B O   
17920 C CB  . GLU B 1215 ? 0.1875 0.2052 0.2184 0.0188  0.0031  -0.0107 1213 GLU B CB  
17921 C CG  . GLU B 1215 ? 0.2396 0.2587 0.2706 0.0194  0.0039  -0.0095 1213 GLU B CG  
17922 C CD  . GLU B 1215 ? 0.2028 0.2250 0.2354 0.0178  0.0045  -0.0090 1213 GLU B CD  
17923 O OE1 . GLU B 1215 ? 0.1946 0.2157 0.2287 0.0164  0.0046  -0.0088 1213 GLU B OE1 
17924 O OE2 . GLU B 1215 ? 0.2256 0.2514 0.2578 0.0179  0.0049  -0.0089 1213 GLU B OE2 
17925 N N   . VAL B 1216 ? 0.1854 0.1997 0.2122 0.0207  0.0014  -0.0133 1214 VAL B N   
17926 C CA  . VAL B 1216 ? 0.1801 0.1942 0.2063 0.0200  0.0007  -0.0142 1214 VAL B CA  
17927 C C   . VAL B 1216 ? 0.1846 0.2035 0.2102 0.0200  0.0015  -0.0140 1214 VAL B C   
17928 O O   . VAL B 1216 ? 0.1948 0.2165 0.2193 0.0216  0.0023  -0.0137 1214 VAL B O   
17929 C CB  . VAL B 1216 ? 0.1982 0.2085 0.2219 0.0214  -0.0002 -0.0154 1214 VAL B CB  
17930 C CG1 . VAL B 1216 ? 0.2270 0.2375 0.2496 0.0207  -0.0009 -0.0163 1214 VAL B CG1 
17931 C CG2 . VAL B 1216 ? 0.2249 0.2303 0.2492 0.0208  -0.0013 -0.0156 1214 VAL B CG2 
17932 N N   . SER B 1217 ? 0.1691 0.1889 0.1954 0.0181  0.0011  -0.0139 1215 SER B N   
17933 C CA  . SER B 1217 ? 0.1645 0.1879 0.1899 0.0173  0.0016  -0.0136 1215 SER B CA  
17934 C C   . SER B 1217 ? 0.1584 0.1805 0.1817 0.0172  0.0008  -0.0143 1215 SER B C   
17935 O O   . SER B 1217 ? 0.1932 0.2118 0.2166 0.0166  -0.0004 -0.0150 1215 SER B O   
17936 C CB  . SER B 1217 ? 0.2049 0.2294 0.2319 0.0153  0.0015  -0.0130 1215 SER B CB  
17937 O OG  . SER B 1217 ? 0.2303 0.2565 0.2559 0.0139  0.0013  -0.0127 1215 SER B OG  
17938 N N   . ALA B 1218 ? 0.1720 0.1973 0.1934 0.0177  0.0014  -0.0142 1216 ALA B N   
17939 C CA  . ALA B 1218 ? 0.1801 0.2046 0.1990 0.0174  0.0008  -0.0147 1216 ALA B CA  
17940 C C   . ALA B 1218 ? 0.1997 0.2284 0.2177 0.0158  0.0014  -0.0137 1216 ALA B C   
17941 O O   . ALA B 1218 ? 0.2278 0.2612 0.2459 0.0161  0.0026  -0.0130 1216 ALA B O   
17942 C CB  . ALA B 1218 ? 0.1947 0.2186 0.2112 0.0199  0.0011  -0.0157 1216 ALA B CB  
17943 N N   . SER B 1219 ? 0.1787 0.2056 0.1956 0.0138  0.0004  -0.0135 1217 SER B N   
17944 C CA  . SER B 1219 ? 0.1852 0.2151 0.2007 0.0117  0.0007  -0.0124 1217 SER B CA  
17945 C C   . SER B 1219 ? 0.1866 0.2159 0.1989 0.0116  0.0003  -0.0126 1217 SER B C   
17946 O O   . SER B 1219 ? 0.1943 0.2193 0.2056 0.0114  -0.0011 -0.0131 1217 SER B O   
17947 C CB  . SER B 1219 ? 0.1883 0.2159 0.2047 0.0095  -0.0004 -0.0118 1217 SER B CB  
17948 O OG  . SER B 1219 ? 0.2040 0.2337 0.2186 0.0071  -0.0004 -0.0106 1217 SER B OG  
17949 N N   . ILE B 1220 ? 0.2129 0.2469 0.2235 0.0119  0.0016  -0.0121 1218 ILE B N   
17950 C CA  . ILE B 1220 ? 0.1986 0.2330 0.2058 0.0121  0.0016  -0.0122 1218 ILE B CA  
17951 C C   . ILE B 1220 ? 0.2174 0.2548 0.2229 0.0090  0.0018  -0.0105 1218 ILE B C   
17952 O O   . ILE B 1220 ? 0.2148 0.2577 0.2213 0.0081  0.0030  -0.0094 1218 ILE B O   
17953 C CB  . ILE B 1220 ? 0.2324 0.2701 0.2384 0.0151  0.0030  -0.0130 1218 ILE B CB  
17954 C CG1 . ILE B 1220 ? 0.2980 0.3318 0.3052 0.0179  0.0025  -0.0146 1218 ILE B CG1 
17955 C CG2 . ILE B 1220 ? 0.2636 0.3019 0.2657 0.0152  0.0031  -0.0132 1218 ILE B CG2 
17956 C CD1 . ILE B 1220 ? 0.3984 0.4354 0.4077 0.0199  0.0037  -0.0147 1218 ILE B CD1 
17957 N N   . ASN B 1221 ? 0.1924 0.2262 0.1954 0.0073  0.0005  -0.0101 1219 ASN B N   
17958 C CA  . ASN B 1221 ? 0.2001 0.2358 0.2006 0.0042  0.0005  -0.0084 1219 ASN B CA  
17959 C C   . ASN B 1221 ? 0.2227 0.2637 0.2206 0.0048  0.0021  -0.0080 1219 ASN B C   
17960 O O   . ASN B 1221 ? 0.2600 0.2989 0.2550 0.0060  0.0018  -0.0088 1219 ASN B O   
17961 C CB  . ASN B 1221 ? 0.1831 0.2124 0.1814 0.0026  -0.0016 -0.0081 1219 ASN B CB  
17962 C CG  . ASN B 1221 ? 0.2138 0.2438 0.2087 -0.0008 -0.0019 -0.0062 1219 ASN B CG  
17963 O OD1 . ASN B 1221 ? 0.2330 0.2686 0.2276 -0.0025 -0.0005 -0.0048 1219 ASN B OD1 
17964 N ND2 . ASN B 1221 ? 0.2491 0.2734 0.2412 -0.0018 -0.0038 -0.0059 1219 ASN B ND2 
17965 N N   . THR B 1222 ? 0.1990 0.2471 0.1979 0.0040  0.0038  -0.0069 1220 THR B N   
17966 C CA  . THR B 1222 ? 0.1973 0.2518 0.1941 0.0048  0.0056  -0.0066 1220 THR B CA  
17967 C C   . THR B 1222 ? 0.2703 0.3269 0.2639 0.0011  0.0057  -0.0045 1220 THR B C   
17968 O O   . THR B 1222 ? 0.3401 0.4031 0.3320 0.0012  0.0074  -0.0039 1220 THR B O   
17969 C CB  . THR B 1222 ? 0.2504 0.3126 0.2502 0.0065  0.0075  -0.0066 1220 THR B CB  
17970 O OG1 . THR B 1222 ? 0.2705 0.3355 0.2726 0.0033  0.0074  -0.0050 1220 THR B OG1 
17971 C CG2 . THR B 1222 ? 0.2558 0.3155 0.2580 0.0105  0.0075  -0.0086 1220 THR B CG2 
17972 N N   . ALA B 1223 ? 0.2480 0.2993 0.2406 -0.0022 0.0039  -0.0034 1221 ALA B N   
17973 C CA  . ALA B 1223 ? 0.3047 0.3558 0.2934 -0.0059 0.0034  -0.0014 1221 ALA B CA  
17974 C C   . ALA B 1223 ? 0.3951 0.4394 0.3800 -0.0054 0.0019  -0.0019 1221 ALA B C   
17975 O O   . ALA B 1223 ? 0.4436 0.4861 0.4246 -0.0084 0.0011  -0.0002 1221 ALA B O   
17976 C CB  . ALA B 1223 ? 0.3408 0.3898 0.3300 -0.0100 0.0022  0.0003  1221 ALA B CB  
17977 N N   . ALA B 1224 ? 0.3968 0.4371 0.3824 -0.0017 0.0012  -0.0042 1222 ALA B N   
17978 C CA  . ALA B 1224 ? 0.4499 0.4831 0.4325 -0.0014 -0.0008 -0.0048 1222 ALA B CA  
17979 C C   . ALA B 1224 ? 0.5666 0.6012 0.5441 -0.0018 -0.0004 -0.0041 1222 ALA B C   
17980 O O   . ALA B 1224 ? 0.4850 0.5140 0.4590 -0.0028 -0.0022 -0.0037 1222 ALA B O   
17981 C CB  . ALA B 1224 ? 0.3877 0.4172 0.3725 0.0023  -0.0016 -0.0073 1222 ALA B CB  
17982 N N   . ALA B 1225 ? 0.4513 0.4933 0.4280 -0.0009 0.0021  -0.0040 1223 ALA B N   
17983 C CA  . ALA B 1225 ? 0.5015 0.5457 0.4731 -0.0014 0.0029  -0.0032 1223 ALA B CA  
17984 C C   . ALA B 1225 ? 0.5939 0.6397 0.5627 -0.0062 0.0029  -0.0001 1223 ALA B C   
17985 O O   . ALA B 1225 ? 0.5164 0.5639 0.4806 -0.0072 0.0035  0.0009  1223 ALA B O   
17986 C CB  . ALA B 1225 ? 0.5150 0.5671 0.4866 0.0016  0.0056  -0.0042 1223 ALA B CB  
17987 N N   . GLY B 1226 ? 0.5143 0.5593 0.4855 -0.0093 0.0021  0.0013  1224 GLY B N   
17988 C CA  . GLY B 1226 ? 0.4883 0.5336 0.4566 -0.0143 0.0017  0.0043  1224 GLY B CA  
17989 C C   . GLY B 1226 ? 0.5729 0.6266 0.5434 -0.0171 0.0037  0.0061  1224 GLY B C   
17990 O O   . GLY B 1226 ? 0.4699 0.5247 0.4377 -0.0217 0.0035  0.0088  1224 GLY B O   
17991 N N   . GLY B 1227 ? 0.4254 0.4851 0.4006 -0.0146 0.0054  0.0048  1225 GLY B N   
17992 C CA  . GLY B 1227 ? 0.4502 0.5188 0.4280 -0.0170 0.0071  0.0064  1225 GLY B CA  
17993 C C   . GLY B 1227 ? 0.5334 0.6064 0.5165 -0.0133 0.0083  0.0044  1225 GLY B C   
17994 O O   . GLY B 1227 ? 0.4783 0.5481 0.4626 -0.0089 0.0081  0.0020  1225 GLY B O   
17995 N N   . ASN B 1228 ? 0.4125 0.4931 0.3986 -0.0154 0.0094  0.0057  1226 ASN B N   
17996 C CA  . ASN B 1228 ? 0.4631 0.5482 0.4543 -0.0124 0.0104  0.0043  1226 ASN B CA  
17997 C C   . ASN B 1228 ? 0.5502 0.6473 0.5427 -0.0107 0.0132  0.0046  1226 ASN B C   
17998 O O   . ASN B 1228 ? 0.5527 0.6576 0.5454 -0.0143 0.0143  0.0068  1226 ASN B O   
17999 C CB  . ASN B 1228 ? 0.4423 0.5265 0.4362 -0.0157 0.0091  0.0054  1226 ASN B CB  
18000 C CG  . ASN B 1228 ? 0.5235 0.6112 0.5223 -0.0126 0.0097  0.0040  1226 ASN B CG  
18001 O OD1 . ASN B 1228 ? 0.5424 0.6371 0.5431 -0.0091 0.0116  0.0031  1226 ASN B OD1 
18002 N ND2 . ASN B 1228 ? 0.4777 0.5603 0.4783 -0.0138 0.0081  0.0038  1226 ASN B ND2 
18003 N N   . ALA B 1229 ? 0.5227 0.6211 0.5159 -0.0051 0.0143  0.0022  1227 ALA B N   
18004 C CA  . ALA B 1229 ? 0.6151 0.7245 0.6093 -0.0024 0.0170  0.0020  1227 ALA B CA  
18005 C C   . ALA B 1229 ? 0.6051 0.7233 0.6041 -0.0036 0.0179  0.0031  1227 ALA B C   
18006 O O   . ALA B 1229 ? 0.6072 0.7359 0.6068 -0.0055 0.0196  0.0049  1227 ALA B O   
18007 C CB  . ALA B 1229 ? 0.4914 0.5988 0.4855 0.0041  0.0176  -0.0010 1227 ALA B CB  
18008 N N   . SER B 1230 ? 0.5806 0.6950 0.5829 -0.0025 0.0166  0.0022  1228 SER B N   
18009 C CA  . SER B 1230 ? 0.5572 0.6797 0.5640 -0.0031 0.0172  0.0030  1228 SER B CA  
18010 C C   . SER B 1230 ? 0.6165 0.7434 0.6234 -0.0097 0.0169  0.0059  1228 SER B C   
18011 O O   . SER B 1230 ? 0.5970 0.7346 0.6068 -0.0109 0.0181  0.0072  1228 SER B O   
18012 C CB  . SER B 1230 ? 0.5421 0.6582 0.5517 -0.0013 0.0157  0.0016  1228 SER B CB  
18013 N N   . LEU B 1231 ? 0.5833 0.7022 0.5871 -0.0140 0.0151  0.0071  1229 LEU B N   
18014 C CA  . LEU B 1231 ? 0.5861 0.7075 0.5892 -0.0206 0.0144  0.0099  1229 LEU B CA  
18015 C C   . LEU B 1231 ? 0.6320 0.7584 0.6316 -0.0233 0.0158  0.0118  1229 LEU B C   
18016 O O   . LEU B 1231 ? 0.7250 0.8601 0.7252 -0.0275 0.0167  0.0142  1229 LEU B O   
18017 C CB  . LEU B 1231 ? 0.5928 0.7021 0.5939 -0.0238 0.0115  0.0102  1229 LEU B CB  
18018 C CG  . LEU B 1231 ? 0.4540 0.5609 0.4581 -0.0252 0.0099  0.0100  1229 LEU B CG  
18019 C CD1 . LEU B 1231 ? 0.5728 0.6794 0.5805 -0.0196 0.0103  0.0075  1229 LEU B CD1 
18020 C CD2 . LEU B 1231 ? 0.3484 0.4434 0.3494 -0.0285 0.0072  0.0104  1229 LEU B CD2 
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