data_9KK6
# 
_entry.id   9KK6 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9KK6         pdb_00009kk6 10.2210/pdb9kk6/pdb 
WWPDB D_1300053729 ?            ?                   
EMDB  EMD-62383    ?            ?                   
# 
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 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-05-21 ? 
2 'EM metadata'     1 0 2025-05-21 ? 
3 FSC               1 0 2025-05-21 ? 
4 'Half map'        1 0 2025-05-21 1 
5 'Half map'        1 0 2025-05-21 2 
6 Image             1 0 2025-05-21 ? 
7 Mask              1 0 2025-05-21 1 
8 'Primary map'     1 0 2025-05-21 ? 
# 
loop_
_pdbx_audit_revision_details.ordinal 
_pdbx_audit_revision_details.revision_ordinal 
_pdbx_audit_revision_details.data_content_type 
_pdbx_audit_revision_details.provider 
_pdbx_audit_revision_details.type 
_pdbx_audit_revision_details.description 
_pdbx_audit_revision_details.details 
1 1 'Structure model' repository 'Initial release' ? ? 
2 2 'EM metadata'     repository 'Initial release' ? ? 
3 3 FSC               repository 'Initial release' ? ? 
4 4 'Half map'        repository 'Initial release' ? ? 
5 5 'Half map'        repository 'Initial release' ? ? 
6 6 Image             repository 'Initial release' ? ? 
7 7 Mask              repository 'Initial release' ? ? 
8 8 'Primary map'     repository 'Initial release' ? ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9KK6 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-12 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_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_database_related.db_name        EMDB 
_pdbx_database_related.details        'Cryo-EM structure of vanadate-trapped atABCB19 in lipid nanodisc' 
_pdbx_database_related.db_id          EMD-62383 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              liaomf@sustech.edu.cn 
_pdbx_contact_author.name_first         Maofu 
_pdbx_contact_author.name_last          Liao 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-3481-450X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Liu, Y.'  1 0000-0002-8165-8845 
'Liao, M.' 2 0000-0002-3481-450X 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Cryo-EM structure of vanadate-trapped atABCB19 in lipid nanodisc' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
_citation_author.citation_id        primary 
_citation_author.name               'Liu, Y.' 
_citation_author.ordinal            1 
_citation_author.identifier_ORCID   0000-0002-8165-8845 
# 
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 'ABC transporter B family member 19' 136932.562 1 ? ? ? ? 
2 non-polymer syn 'VANADATE ION'                       114.939    2 ? ? ? ? 
3 non-polymer syn "ADENOSINE-5'-DIPHOSPHATE"           427.201    2 ? ? ? ? 
4 non-polymer syn 'MAGNESIUM ION'                      24.305     2 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'ABC transporter ABCB.19,AtABCB19,Multidrug resistance protein 11,P-glycoprotein 19' 
# 
_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       
;MSETNTTDAKTVPAEAEKKKEQSLPFFKLFSFADKFDYLLMFVGSLGAIVHGSSMPVFFLLFGQMVNGFGKNQMDLHQMV
HEVSRYSLYFVYLGLVVCFSSYAEIACWMYSGERQVAALRKKYLEAVLKQDVGFFDTDARTGDIVFSVSTDTLLVQDAIS
EKVGNFIHYLSTFLAGLVVGFVSAWKLALLSVAVIPGIAFAGGLYAYTLTGITSKSRESYANAGVIAEQAIAQVRTVYSY
VGESKALNAYSDAIQYTLKLGYKAGMAKGLGLGCTYGIACMSWALVFWYAGVFIRNGQTDGGKAFTAIFSAIVGGMSLGQ
SFSNLGAFSKGKAAGYKLMEIINQRPTIIQDPLDGKCLDQVHGNIEFKDVTFSYPSRPDVMIFRNFNIFFPSGKTVAVVG
GSGSGKSTVVSLIERFYDPNSGQILLDGVEIKTLQLKFLREQIGLVNQEPALFATTILENILYGKPDATMVEVEAAASAA
NAHSFITLLPKGYDTQVGERGVQLSGGQKQRIAIARAMLKDPKILLLDEATSALDASSESIVQEALDRVMVGRTTVVVAH
RLCTIRNVDSIAVIQQGQVVETGTHEELIAKSGAYASLIRFQEMVGTRDFSNPSTRRTRSTRLSHSLSTKSLSLRSGSLR
NLSYSYSTGADGRIEMISNAETDRKTRAPENYFYRLLKLNSPEWPYSIMGAVGSILSGFIGPTFAIVMSNMIEVFYYTDY
DSMERKTKEYVFIYIGAGLYAVGAYLIQHYFFSIMGENLTTRVRRMMLSAILRNEVGWFDEDEHNSSLIAARLATDAADV
KSAIAERISVILQNMTSLLTSFIVAFIVEWRVSLLILGTFPLLVLANFAQQLSLKGFAGDTAKAHAKTSMIAGEGVSNIR
TVAAFNAQSKILSLFCHELRVPQKRSLYRSQTSGFLFGLSQLALYGSEALILWYGAHLVSKGVSTFSKVIKVFVVLVITA
NSVAETVSLAPEIIRGGEAVGSVFSVLDRQTRIDPDDADADPVETIRGDIEFRHVDFAYPSRPDVMVFRDFNLRIRAGHS
QALVGASGSGKSSVIAMIERFYDPLAGKVMIDGKDIRRLNLKSLRLKIGLVQQEPALFAATIFDNIAYGKDGATESEVID
AARAANAHGFISGLPEGYKTPVGERGVQLSGGQKQRIAIARAVLKNPTVLLLDEATSALDAESECVLQEALERLMRGRTT
VVVAHRLSTIRGVDCIGVIQDGRIVEQGSHSELVSRPEGAYSRLLQLQTHRI
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSETNTTDAKTVPAEAEKKKEQSLPFFKLFSFADKFDYLLMFVGSLGAIVHGSSMPVFFLLFGQMVNGFGKNQMDLHQMV
HEVSRYSLYFVYLGLVVCFSSYAEIACWMYSGERQVAALRKKYLEAVLKQDVGFFDTDARTGDIVFSVSTDTLLVQDAIS
EKVGNFIHYLSTFLAGLVVGFVSAWKLALLSVAVIPGIAFAGGLYAYTLTGITSKSRESYANAGVIAEQAIAQVRTVYSY
VGESKALNAYSDAIQYTLKLGYKAGMAKGLGLGCTYGIACMSWALVFWYAGVFIRNGQTDGGKAFTAIFSAIVGGMSLGQ
SFSNLGAFSKGKAAGYKLMEIINQRPTIIQDPLDGKCLDQVHGNIEFKDVTFSYPSRPDVMIFRNFNIFFPSGKTVAVVG
GSGSGKSTVVSLIERFYDPNSGQILLDGVEIKTLQLKFLREQIGLVNQEPALFATTILENILYGKPDATMVEVEAAASAA
NAHSFITLLPKGYDTQVGERGVQLSGGQKQRIAIARAMLKDPKILLLDEATSALDASSESIVQEALDRVMVGRTTVVVAH
RLCTIRNVDSIAVIQQGQVVETGTHEELIAKSGAYASLIRFQEMVGTRDFSNPSTRRTRSTRLSHSLSTKSLSLRSGSLR
NLSYSYSTGADGRIEMISNAETDRKTRAPENYFYRLLKLNSPEWPYSIMGAVGSILSGFIGPTFAIVMSNMIEVFYYTDY
DSMERKTKEYVFIYIGAGLYAVGAYLIQHYFFSIMGENLTTRVRRMMLSAILRNEVGWFDEDEHNSSLIAARLATDAADV
KSAIAERISVILQNMTSLLTSFIVAFIVEWRVSLLILGTFPLLVLANFAQQLSLKGFAGDTAKAHAKTSMIAGEGVSNIR
TVAAFNAQSKILSLFCHELRVPQKRSLYRSQTSGFLFGLSQLALYGSEALILWYGAHLVSKGVSTFSKVIKVFVVLVITA
NSVAETVSLAPEIIRGGEAVGSVFSVLDRQTRIDPDDADADPVETIRGDIEFRHVDFAYPSRPDVMVFRDFNLRIRAGHS
QALVGASGSGKSSVIAMIERFYDPLAGKVMIDGKDIRRLNLKSLRLKIGLVQQEPALFAATIFDNIAYGKDGATESEVID
AARAANAHGFISGLPEGYKTPVGERGVQLSGGQKQRIAIARAVLKNPTVLLLDEATSALDAESECVLQEALERLMRGRTT
VVVAHRLSTIRGVDCIGVIQDGRIVEQGSHSELVSRPEGAYSRLLQLQTHRI
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'VANADATE ION'             VO4 
3 "ADENOSINE-5'-DIPHOSPHATE" ADP 
4 'MAGNESIUM ION'            MG  
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1    MET n 
1 2    SER n 
1 3    GLU n 
1 4    THR n 
1 5    ASN n 
1 6    THR n 
1 7    THR n 
1 8    ASP n 
1 9    ALA n 
1 10   LYS n 
1 11   THR n 
1 12   VAL n 
1 13   PRO n 
1 14   ALA n 
1 15   GLU n 
1 16   ALA n 
1 17   GLU n 
1 18   LYS n 
1 19   LYS n 
1 20   LYS n 
1 21   GLU n 
1 22   GLN n 
1 23   SER n 
1 24   LEU n 
1 25   PRO n 
1 26   PHE n 
1 27   PHE n 
1 28   LYS n 
1 29   LEU n 
1 30   PHE n 
1 31   SER n 
1 32   PHE n 
1 33   ALA n 
1 34   ASP n 
1 35   LYS n 
1 36   PHE n 
1 37   ASP n 
1 38   TYR n 
1 39   LEU n 
1 40   LEU n 
1 41   MET n 
1 42   PHE n 
1 43   VAL n 
1 44   GLY n 
1 45   SER n 
1 46   LEU n 
1 47   GLY n 
1 48   ALA n 
1 49   ILE n 
1 50   VAL n 
1 51   HIS n 
1 52   GLY n 
1 53   SER n 
1 54   SER n 
1 55   MET n 
1 56   PRO n 
1 57   VAL n 
1 58   PHE n 
1 59   PHE n 
1 60   LEU n 
1 61   LEU n 
1 62   PHE n 
1 63   GLY n 
1 64   GLN n 
1 65   MET n 
1 66   VAL n 
1 67   ASN n 
1 68   GLY n 
1 69   PHE n 
1 70   GLY n 
1 71   LYS n 
1 72   ASN n 
1 73   GLN n 
1 74   MET n 
1 75   ASP n 
1 76   LEU n 
1 77   HIS n 
1 78   GLN n 
1 79   MET n 
1 80   VAL n 
1 81   HIS n 
1 82   GLU n 
1 83   VAL n 
1 84   SER n 
1 85   ARG n 
1 86   TYR n 
1 87   SER n 
1 88   LEU n 
1 89   TYR n 
1 90   PHE n 
1 91   VAL n 
1 92   TYR n 
1 93   LEU n 
1 94   GLY n 
1 95   LEU n 
1 96   VAL n 
1 97   VAL n 
1 98   CYS n 
1 99   PHE n 
1 100  SER n 
1 101  SER n 
1 102  TYR n 
1 103  ALA n 
1 104  GLU n 
1 105  ILE n 
1 106  ALA n 
1 107  CYS n 
1 108  TRP n 
1 109  MET n 
1 110  TYR n 
1 111  SER n 
1 112  GLY n 
1 113  GLU n 
1 114  ARG n 
1 115  GLN n 
1 116  VAL n 
1 117  ALA n 
1 118  ALA n 
1 119  LEU n 
1 120  ARG n 
1 121  LYS n 
1 122  LYS n 
1 123  TYR n 
1 124  LEU n 
1 125  GLU n 
1 126  ALA n 
1 127  VAL n 
1 128  LEU n 
1 129  LYS n 
1 130  GLN n 
1 131  ASP n 
1 132  VAL n 
1 133  GLY n 
1 134  PHE n 
1 135  PHE n 
1 136  ASP n 
1 137  THR n 
1 138  ASP n 
1 139  ALA n 
1 140  ARG n 
1 141  THR n 
1 142  GLY n 
1 143  ASP n 
1 144  ILE n 
1 145  VAL n 
1 146  PHE n 
1 147  SER n 
1 148  VAL n 
1 149  SER n 
1 150  THR n 
1 151  ASP n 
1 152  THR n 
1 153  LEU n 
1 154  LEU n 
1 155  VAL n 
1 156  GLN n 
1 157  ASP n 
1 158  ALA n 
1 159  ILE n 
1 160  SER n 
1 161  GLU n 
1 162  LYS n 
1 163  VAL n 
1 164  GLY n 
1 165  ASN n 
1 166  PHE n 
1 167  ILE n 
1 168  HIS n 
1 169  TYR n 
1 170  LEU n 
1 171  SER n 
1 172  THR n 
1 173  PHE n 
1 174  LEU n 
1 175  ALA n 
1 176  GLY n 
1 177  LEU n 
1 178  VAL n 
1 179  VAL n 
1 180  GLY n 
1 181  PHE n 
1 182  VAL n 
1 183  SER n 
1 184  ALA n 
1 185  TRP n 
1 186  LYS n 
1 187  LEU n 
1 188  ALA n 
1 189  LEU n 
1 190  LEU n 
1 191  SER n 
1 192  VAL n 
1 193  ALA n 
1 194  VAL n 
1 195  ILE n 
1 196  PRO n 
1 197  GLY n 
1 198  ILE n 
1 199  ALA n 
1 200  PHE n 
1 201  ALA n 
1 202  GLY n 
1 203  GLY n 
1 204  LEU n 
1 205  TYR n 
1 206  ALA n 
1 207  TYR n 
1 208  THR n 
1 209  LEU n 
1 210  THR n 
1 211  GLY n 
1 212  ILE n 
1 213  THR n 
1 214  SER n 
1 215  LYS n 
1 216  SER n 
1 217  ARG n 
1 218  GLU n 
1 219  SER n 
1 220  TYR n 
1 221  ALA n 
1 222  ASN n 
1 223  ALA n 
1 224  GLY n 
1 225  VAL n 
1 226  ILE n 
1 227  ALA n 
1 228  GLU n 
1 229  GLN n 
1 230  ALA n 
1 231  ILE n 
1 232  ALA n 
1 233  GLN n 
1 234  VAL n 
1 235  ARG n 
1 236  THR n 
1 237  VAL n 
1 238  TYR n 
1 239  SER n 
1 240  TYR n 
1 241  VAL n 
1 242  GLY n 
1 243  GLU n 
1 244  SER n 
1 245  LYS n 
1 246  ALA n 
1 247  LEU n 
1 248  ASN n 
1 249  ALA n 
1 250  TYR n 
1 251  SER n 
1 252  ASP n 
1 253  ALA n 
1 254  ILE n 
1 255  GLN n 
1 256  TYR n 
1 257  THR n 
1 258  LEU n 
1 259  LYS n 
1 260  LEU n 
1 261  GLY n 
1 262  TYR n 
1 263  LYS n 
1 264  ALA n 
1 265  GLY n 
1 266  MET n 
1 267  ALA n 
1 268  LYS n 
1 269  GLY n 
1 270  LEU n 
1 271  GLY n 
1 272  LEU n 
1 273  GLY n 
1 274  CYS n 
1 275  THR n 
1 276  TYR n 
1 277  GLY n 
1 278  ILE n 
1 279  ALA n 
1 280  CYS n 
1 281  MET n 
1 282  SER n 
1 283  TRP n 
1 284  ALA n 
1 285  LEU n 
1 286  VAL n 
1 287  PHE n 
1 288  TRP n 
1 289  TYR n 
1 290  ALA n 
1 291  GLY n 
1 292  VAL n 
1 293  PHE n 
1 294  ILE n 
1 295  ARG n 
1 296  ASN n 
1 297  GLY n 
1 298  GLN n 
1 299  THR n 
1 300  ASP n 
1 301  GLY n 
1 302  GLY n 
1 303  LYS n 
1 304  ALA n 
1 305  PHE n 
1 306  THR n 
1 307  ALA n 
1 308  ILE n 
1 309  PHE n 
1 310  SER n 
1 311  ALA n 
1 312  ILE n 
1 313  VAL n 
1 314  GLY n 
1 315  GLY n 
1 316  MET n 
1 317  SER n 
1 318  LEU n 
1 319  GLY n 
1 320  GLN n 
1 321  SER n 
1 322  PHE n 
1 323  SER n 
1 324  ASN n 
1 325  LEU n 
1 326  GLY n 
1 327  ALA n 
1 328  PHE n 
1 329  SER n 
1 330  LYS n 
1 331  GLY n 
1 332  LYS n 
1 333  ALA n 
1 334  ALA n 
1 335  GLY n 
1 336  TYR n 
1 337  LYS n 
1 338  LEU n 
1 339  MET n 
1 340  GLU n 
1 341  ILE n 
1 342  ILE n 
1 343  ASN n 
1 344  GLN n 
1 345  ARG n 
1 346  PRO n 
1 347  THR n 
1 348  ILE n 
1 349  ILE n 
1 350  GLN n 
1 351  ASP n 
1 352  PRO n 
1 353  LEU n 
1 354  ASP n 
1 355  GLY n 
1 356  LYS n 
1 357  CYS n 
1 358  LEU n 
1 359  ASP n 
1 360  GLN n 
1 361  VAL n 
1 362  HIS n 
1 363  GLY n 
1 364  ASN n 
1 365  ILE n 
1 366  GLU n 
1 367  PHE n 
1 368  LYS n 
1 369  ASP n 
1 370  VAL n 
1 371  THR n 
1 372  PHE n 
1 373  SER n 
1 374  TYR n 
1 375  PRO n 
1 376  SER n 
1 377  ARG n 
1 378  PRO n 
1 379  ASP n 
1 380  VAL n 
1 381  MET n 
1 382  ILE n 
1 383  PHE n 
1 384  ARG n 
1 385  ASN n 
1 386  PHE n 
1 387  ASN n 
1 388  ILE n 
1 389  PHE n 
1 390  PHE n 
1 391  PRO n 
1 392  SER n 
1 393  GLY n 
1 394  LYS n 
1 395  THR n 
1 396  VAL n 
1 397  ALA n 
1 398  VAL n 
1 399  VAL n 
1 400  GLY n 
1 401  GLY n 
1 402  SER n 
1 403  GLY n 
1 404  SER n 
1 405  GLY n 
1 406  LYS n 
1 407  SER n 
1 408  THR n 
1 409  VAL n 
1 410  VAL n 
1 411  SER n 
1 412  LEU n 
1 413  ILE n 
1 414  GLU n 
1 415  ARG n 
1 416  PHE n 
1 417  TYR n 
1 418  ASP n 
1 419  PRO n 
1 420  ASN n 
1 421  SER n 
1 422  GLY n 
1 423  GLN n 
1 424  ILE n 
1 425  LEU n 
1 426  LEU n 
1 427  ASP n 
1 428  GLY n 
1 429  VAL n 
1 430  GLU n 
1 431  ILE n 
1 432  LYS n 
1 433  THR n 
1 434  LEU n 
1 435  GLN n 
1 436  LEU n 
1 437  LYS n 
1 438  PHE n 
1 439  LEU n 
1 440  ARG n 
1 441  GLU n 
1 442  GLN n 
1 443  ILE n 
1 444  GLY n 
1 445  LEU n 
1 446  VAL n 
1 447  ASN n 
1 448  GLN n 
1 449  GLU n 
1 450  PRO n 
1 451  ALA n 
1 452  LEU n 
1 453  PHE n 
1 454  ALA n 
1 455  THR n 
1 456  THR n 
1 457  ILE n 
1 458  LEU n 
1 459  GLU n 
1 460  ASN n 
1 461  ILE n 
1 462  LEU n 
1 463  TYR n 
1 464  GLY n 
1 465  LYS n 
1 466  PRO n 
1 467  ASP n 
1 468  ALA n 
1 469  THR n 
1 470  MET n 
1 471  VAL n 
1 472  GLU n 
1 473  VAL n 
1 474  GLU n 
1 475  ALA n 
1 476  ALA n 
1 477  ALA n 
1 478  SER n 
1 479  ALA n 
1 480  ALA n 
1 481  ASN n 
1 482  ALA n 
1 483  HIS n 
1 484  SER n 
1 485  PHE n 
1 486  ILE n 
1 487  THR n 
1 488  LEU n 
1 489  LEU n 
1 490  PRO n 
1 491  LYS n 
1 492  GLY n 
1 493  TYR n 
1 494  ASP n 
1 495  THR n 
1 496  GLN n 
1 497  VAL n 
1 498  GLY n 
1 499  GLU n 
1 500  ARG n 
1 501  GLY n 
1 502  VAL n 
1 503  GLN n 
1 504  LEU n 
1 505  SER n 
1 506  GLY n 
1 507  GLY n 
1 508  GLN n 
1 509  LYS n 
1 510  GLN n 
1 511  ARG n 
1 512  ILE n 
1 513  ALA n 
1 514  ILE n 
1 515  ALA n 
1 516  ARG n 
1 517  ALA n 
1 518  MET n 
1 519  LEU n 
1 520  LYS n 
1 521  ASP n 
1 522  PRO n 
1 523  LYS n 
1 524  ILE n 
1 525  LEU n 
1 526  LEU n 
1 527  LEU n 
1 528  ASP n 
1 529  GLU n 
1 530  ALA n 
1 531  THR n 
1 532  SER n 
1 533  ALA n 
1 534  LEU n 
1 535  ASP n 
1 536  ALA n 
1 537  SER n 
1 538  SER n 
1 539  GLU n 
1 540  SER n 
1 541  ILE n 
1 542  VAL n 
1 543  GLN n 
1 544  GLU n 
1 545  ALA n 
1 546  LEU n 
1 547  ASP n 
1 548  ARG n 
1 549  VAL n 
1 550  MET n 
1 551  VAL n 
1 552  GLY n 
1 553  ARG n 
1 554  THR n 
1 555  THR n 
1 556  VAL n 
1 557  VAL n 
1 558  VAL n 
1 559  ALA n 
1 560  HIS n 
1 561  ARG n 
1 562  LEU n 
1 563  CYS n 
1 564  THR n 
1 565  ILE n 
1 566  ARG n 
1 567  ASN n 
1 568  VAL n 
1 569  ASP n 
1 570  SER n 
1 571  ILE n 
1 572  ALA n 
1 573  VAL n 
1 574  ILE n 
1 575  GLN n 
1 576  GLN n 
1 577  GLY n 
1 578  GLN n 
1 579  VAL n 
1 580  VAL n 
1 581  GLU n 
1 582  THR n 
1 583  GLY n 
1 584  THR n 
1 585  HIS n 
1 586  GLU n 
1 587  GLU n 
1 588  LEU n 
1 589  ILE n 
1 590  ALA n 
1 591  LYS n 
1 592  SER n 
1 593  GLY n 
1 594  ALA n 
1 595  TYR n 
1 596  ALA n 
1 597  SER n 
1 598  LEU n 
1 599  ILE n 
1 600  ARG n 
1 601  PHE n 
1 602  GLN n 
1 603  GLU n 
1 604  MET n 
1 605  VAL n 
1 606  GLY n 
1 607  THR n 
1 608  ARG n 
1 609  ASP n 
1 610  PHE n 
1 611  SER n 
1 612  ASN n 
1 613  PRO n 
1 614  SER n 
1 615  THR n 
1 616  ARG n 
1 617  ARG n 
1 618  THR n 
1 619  ARG n 
1 620  SER n 
1 621  THR n 
1 622  ARG n 
1 623  LEU n 
1 624  SER n 
1 625  HIS n 
1 626  SER n 
1 627  LEU n 
1 628  SER n 
1 629  THR n 
1 630  LYS n 
1 631  SER n 
1 632  LEU n 
1 633  SER n 
1 634  LEU n 
1 635  ARG n 
1 636  SER n 
1 637  GLY n 
1 638  SER n 
1 639  LEU n 
1 640  ARG n 
1 641  ASN n 
1 642  LEU n 
1 643  SER n 
1 644  TYR n 
1 645  SER n 
1 646  TYR n 
1 647  SER n 
1 648  THR n 
1 649  GLY n 
1 650  ALA n 
1 651  ASP n 
1 652  GLY n 
1 653  ARG n 
1 654  ILE n 
1 655  GLU n 
1 656  MET n 
1 657  ILE n 
1 658  SER n 
1 659  ASN n 
1 660  ALA n 
1 661  GLU n 
1 662  THR n 
1 663  ASP n 
1 664  ARG n 
1 665  LYS n 
1 666  THR n 
1 667  ARG n 
1 668  ALA n 
1 669  PRO n 
1 670  GLU n 
1 671  ASN n 
1 672  TYR n 
1 673  PHE n 
1 674  TYR n 
1 675  ARG n 
1 676  LEU n 
1 677  LEU n 
1 678  LYS n 
1 679  LEU n 
1 680  ASN n 
1 681  SER n 
1 682  PRO n 
1 683  GLU n 
1 684  TRP n 
1 685  PRO n 
1 686  TYR n 
1 687  SER n 
1 688  ILE n 
1 689  MET n 
1 690  GLY n 
1 691  ALA n 
1 692  VAL n 
1 693  GLY n 
1 694  SER n 
1 695  ILE n 
1 696  LEU n 
1 697  SER n 
1 698  GLY n 
1 699  PHE n 
1 700  ILE n 
1 701  GLY n 
1 702  PRO n 
1 703  THR n 
1 704  PHE n 
1 705  ALA n 
1 706  ILE n 
1 707  VAL n 
1 708  MET n 
1 709  SER n 
1 710  ASN n 
1 711  MET n 
1 712  ILE n 
1 713  GLU n 
1 714  VAL n 
1 715  PHE n 
1 716  TYR n 
1 717  TYR n 
1 718  THR n 
1 719  ASP n 
1 720  TYR n 
1 721  ASP n 
1 722  SER n 
1 723  MET n 
1 724  GLU n 
1 725  ARG n 
1 726  LYS n 
1 727  THR n 
1 728  LYS n 
1 729  GLU n 
1 730  TYR n 
1 731  VAL n 
1 732  PHE n 
1 733  ILE n 
1 734  TYR n 
1 735  ILE n 
1 736  GLY n 
1 737  ALA n 
1 738  GLY n 
1 739  LEU n 
1 740  TYR n 
1 741  ALA n 
1 742  VAL n 
1 743  GLY n 
1 744  ALA n 
1 745  TYR n 
1 746  LEU n 
1 747  ILE n 
1 748  GLN n 
1 749  HIS n 
1 750  TYR n 
1 751  PHE n 
1 752  PHE n 
1 753  SER n 
1 754  ILE n 
1 755  MET n 
1 756  GLY n 
1 757  GLU n 
1 758  ASN n 
1 759  LEU n 
1 760  THR n 
1 761  THR n 
1 762  ARG n 
1 763  VAL n 
1 764  ARG n 
1 765  ARG n 
1 766  MET n 
1 767  MET n 
1 768  LEU n 
1 769  SER n 
1 770  ALA n 
1 771  ILE n 
1 772  LEU n 
1 773  ARG n 
1 774  ASN n 
1 775  GLU n 
1 776  VAL n 
1 777  GLY n 
1 778  TRP n 
1 779  PHE n 
1 780  ASP n 
1 781  GLU n 
1 782  ASP n 
1 783  GLU n 
1 784  HIS n 
1 785  ASN n 
1 786  SER n 
1 787  SER n 
1 788  LEU n 
1 789  ILE n 
1 790  ALA n 
1 791  ALA n 
1 792  ARG n 
1 793  LEU n 
1 794  ALA n 
1 795  THR n 
1 796  ASP n 
1 797  ALA n 
1 798  ALA n 
1 799  ASP n 
1 800  VAL n 
1 801  LYS n 
1 802  SER n 
1 803  ALA n 
1 804  ILE n 
1 805  ALA n 
1 806  GLU n 
1 807  ARG n 
1 808  ILE n 
1 809  SER n 
1 810  VAL n 
1 811  ILE n 
1 812  LEU n 
1 813  GLN n 
1 814  ASN n 
1 815  MET n 
1 816  THR n 
1 817  SER n 
1 818  LEU n 
1 819  LEU n 
1 820  THR n 
1 821  SER n 
1 822  PHE n 
1 823  ILE n 
1 824  VAL n 
1 825  ALA n 
1 826  PHE n 
1 827  ILE n 
1 828  VAL n 
1 829  GLU n 
1 830  TRP n 
1 831  ARG n 
1 832  VAL n 
1 833  SER n 
1 834  LEU n 
1 835  LEU n 
1 836  ILE n 
1 837  LEU n 
1 838  GLY n 
1 839  THR n 
1 840  PHE n 
1 841  PRO n 
1 842  LEU n 
1 843  LEU n 
1 844  VAL n 
1 845  LEU n 
1 846  ALA n 
1 847  ASN n 
1 848  PHE n 
1 849  ALA n 
1 850  GLN n 
1 851  GLN n 
1 852  LEU n 
1 853  SER n 
1 854  LEU n 
1 855  LYS n 
1 856  GLY n 
1 857  PHE n 
1 858  ALA n 
1 859  GLY n 
1 860  ASP n 
1 861  THR n 
1 862  ALA n 
1 863  LYS n 
1 864  ALA n 
1 865  HIS n 
1 866  ALA n 
1 867  LYS n 
1 868  THR n 
1 869  SER n 
1 870  MET n 
1 871  ILE n 
1 872  ALA n 
1 873  GLY n 
1 874  GLU n 
1 875  GLY n 
1 876  VAL n 
1 877  SER n 
1 878  ASN n 
1 879  ILE n 
1 880  ARG n 
1 881  THR n 
1 882  VAL n 
1 883  ALA n 
1 884  ALA n 
1 885  PHE n 
1 886  ASN n 
1 887  ALA n 
1 888  GLN n 
1 889  SER n 
1 890  LYS n 
1 891  ILE n 
1 892  LEU n 
1 893  SER n 
1 894  LEU n 
1 895  PHE n 
1 896  CYS n 
1 897  HIS n 
1 898  GLU n 
1 899  LEU n 
1 900  ARG n 
1 901  VAL n 
1 902  PRO n 
1 903  GLN n 
1 904  LYS n 
1 905  ARG n 
1 906  SER n 
1 907  LEU n 
1 908  TYR n 
1 909  ARG n 
1 910  SER n 
1 911  GLN n 
1 912  THR n 
1 913  SER n 
1 914  GLY n 
1 915  PHE n 
1 916  LEU n 
1 917  PHE n 
1 918  GLY n 
1 919  LEU n 
1 920  SER n 
1 921  GLN n 
1 922  LEU n 
1 923  ALA n 
1 924  LEU n 
1 925  TYR n 
1 926  GLY n 
1 927  SER n 
1 928  GLU n 
1 929  ALA n 
1 930  LEU n 
1 931  ILE n 
1 932  LEU n 
1 933  TRP n 
1 934  TYR n 
1 935  GLY n 
1 936  ALA n 
1 937  HIS n 
1 938  LEU n 
1 939  VAL n 
1 940  SER n 
1 941  LYS n 
1 942  GLY n 
1 943  VAL n 
1 944  SER n 
1 945  THR n 
1 946  PHE n 
1 947  SER n 
1 948  LYS n 
1 949  VAL n 
1 950  ILE n 
1 951  LYS n 
1 952  VAL n 
1 953  PHE n 
1 954  VAL n 
1 955  VAL n 
1 956  LEU n 
1 957  VAL n 
1 958  ILE n 
1 959  THR n 
1 960  ALA n 
1 961  ASN n 
1 962  SER n 
1 963  VAL n 
1 964  ALA n 
1 965  GLU n 
1 966  THR n 
1 967  VAL n 
1 968  SER n 
1 969  LEU n 
1 970  ALA n 
1 971  PRO n 
1 972  GLU n 
1 973  ILE n 
1 974  ILE n 
1 975  ARG n 
1 976  GLY n 
1 977  GLY n 
1 978  GLU n 
1 979  ALA n 
1 980  VAL n 
1 981  GLY n 
1 982  SER n 
1 983  VAL n 
1 984  PHE n 
1 985  SER n 
1 986  VAL n 
1 987  LEU n 
1 988  ASP n 
1 989  ARG n 
1 990  GLN n 
1 991  THR n 
1 992  ARG n 
1 993  ILE n 
1 994  ASP n 
1 995  PRO n 
1 996  ASP n 
1 997  ASP n 
1 998  ALA n 
1 999  ASP n 
1 1000 ALA n 
1 1001 ASP n 
1 1002 PRO n 
1 1003 VAL n 
1 1004 GLU n 
1 1005 THR n 
1 1006 ILE n 
1 1007 ARG n 
1 1008 GLY n 
1 1009 ASP n 
1 1010 ILE n 
1 1011 GLU n 
1 1012 PHE n 
1 1013 ARG n 
1 1014 HIS n 
1 1015 VAL n 
1 1016 ASP n 
1 1017 PHE n 
1 1018 ALA n 
1 1019 TYR n 
1 1020 PRO n 
1 1021 SER n 
1 1022 ARG n 
1 1023 PRO n 
1 1024 ASP n 
1 1025 VAL n 
1 1026 MET n 
1 1027 VAL n 
1 1028 PHE n 
1 1029 ARG n 
1 1030 ASP n 
1 1031 PHE n 
1 1032 ASN n 
1 1033 LEU n 
1 1034 ARG n 
1 1035 ILE n 
1 1036 ARG n 
1 1037 ALA n 
1 1038 GLY n 
1 1039 HIS n 
1 1040 SER n 
1 1041 GLN n 
1 1042 ALA n 
1 1043 LEU n 
1 1044 VAL n 
1 1045 GLY n 
1 1046 ALA n 
1 1047 SER n 
1 1048 GLY n 
1 1049 SER n 
1 1050 GLY n 
1 1051 LYS n 
1 1052 SER n 
1 1053 SER n 
1 1054 VAL n 
1 1055 ILE n 
1 1056 ALA n 
1 1057 MET n 
1 1058 ILE n 
1 1059 GLU n 
1 1060 ARG n 
1 1061 PHE n 
1 1062 TYR n 
1 1063 ASP n 
1 1064 PRO n 
1 1065 LEU n 
1 1066 ALA n 
1 1067 GLY n 
1 1068 LYS n 
1 1069 VAL n 
1 1070 MET n 
1 1071 ILE n 
1 1072 ASP n 
1 1073 GLY n 
1 1074 LYS n 
1 1075 ASP n 
1 1076 ILE n 
1 1077 ARG n 
1 1078 ARG n 
1 1079 LEU n 
1 1080 ASN n 
1 1081 LEU n 
1 1082 LYS n 
1 1083 SER n 
1 1084 LEU n 
1 1085 ARG n 
1 1086 LEU n 
1 1087 LYS n 
1 1088 ILE n 
1 1089 GLY n 
1 1090 LEU n 
1 1091 VAL n 
1 1092 GLN n 
1 1093 GLN n 
1 1094 GLU n 
1 1095 PRO n 
1 1096 ALA n 
1 1097 LEU n 
1 1098 PHE n 
1 1099 ALA n 
1 1100 ALA n 
1 1101 THR n 
1 1102 ILE n 
1 1103 PHE n 
1 1104 ASP n 
1 1105 ASN n 
1 1106 ILE n 
1 1107 ALA n 
1 1108 TYR n 
1 1109 GLY n 
1 1110 LYS n 
1 1111 ASP n 
1 1112 GLY n 
1 1113 ALA n 
1 1114 THR n 
1 1115 GLU n 
1 1116 SER n 
1 1117 GLU n 
1 1118 VAL n 
1 1119 ILE n 
1 1120 ASP n 
1 1121 ALA n 
1 1122 ALA n 
1 1123 ARG n 
1 1124 ALA n 
1 1125 ALA n 
1 1126 ASN n 
1 1127 ALA n 
1 1128 HIS n 
1 1129 GLY n 
1 1130 PHE n 
1 1131 ILE n 
1 1132 SER n 
1 1133 GLY n 
1 1134 LEU n 
1 1135 PRO n 
1 1136 GLU n 
1 1137 GLY n 
1 1138 TYR n 
1 1139 LYS n 
1 1140 THR n 
1 1141 PRO n 
1 1142 VAL n 
1 1143 GLY n 
1 1144 GLU n 
1 1145 ARG n 
1 1146 GLY n 
1 1147 VAL n 
1 1148 GLN n 
1 1149 LEU n 
1 1150 SER n 
1 1151 GLY n 
1 1152 GLY n 
1 1153 GLN n 
1 1154 LYS n 
1 1155 GLN n 
1 1156 ARG n 
1 1157 ILE n 
1 1158 ALA n 
1 1159 ILE n 
1 1160 ALA n 
1 1161 ARG n 
1 1162 ALA n 
1 1163 VAL n 
1 1164 LEU n 
1 1165 LYS n 
1 1166 ASN n 
1 1167 PRO n 
1 1168 THR n 
1 1169 VAL n 
1 1170 LEU n 
1 1171 LEU n 
1 1172 LEU n 
1 1173 ASP n 
1 1174 GLU n 
1 1175 ALA n 
1 1176 THR n 
1 1177 SER n 
1 1178 ALA n 
1 1179 LEU n 
1 1180 ASP n 
1 1181 ALA n 
1 1182 GLU n 
1 1183 SER n 
1 1184 GLU n 
1 1185 CYS n 
1 1186 VAL n 
1 1187 LEU n 
1 1188 GLN n 
1 1189 GLU n 
1 1190 ALA n 
1 1191 LEU n 
1 1192 GLU n 
1 1193 ARG n 
1 1194 LEU n 
1 1195 MET n 
1 1196 ARG n 
1 1197 GLY n 
1 1198 ARG n 
1 1199 THR n 
1 1200 THR n 
1 1201 VAL n 
1 1202 VAL n 
1 1203 VAL n 
1 1204 ALA n 
1 1205 HIS n 
1 1206 ARG n 
1 1207 LEU n 
1 1208 SER n 
1 1209 THR n 
1 1210 ILE n 
1 1211 ARG n 
1 1212 GLY n 
1 1213 VAL n 
1 1214 ASP n 
1 1215 CYS n 
1 1216 ILE n 
1 1217 GLY n 
1 1218 VAL n 
1 1219 ILE n 
1 1220 GLN n 
1 1221 ASP n 
1 1222 GLY n 
1 1223 ARG n 
1 1224 ILE n 
1 1225 VAL n 
1 1226 GLU n 
1 1227 GLN n 
1 1228 GLY n 
1 1229 SER n 
1 1230 HIS n 
1 1231 SER n 
1 1232 GLU n 
1 1233 LEU n 
1 1234 VAL n 
1 1235 SER n 
1 1236 ARG n 
1 1237 PRO n 
1 1238 GLU n 
1 1239 GLY n 
1 1240 ALA n 
1 1241 TYR n 
1 1242 SER n 
1 1243 ARG n 
1 1244 LEU n 
1 1245 LEU n 
1 1246 GLN n 
1 1247 LEU n 
1 1248 GLN n 
1 1249 THR n 
1 1250 HIS n 
1 1251 ARG n 
1 1252 ILE 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                   1252 
_entity_src_gen.gene_src_common_name               'thale cress' 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'ABCB19, MDR1, MDR11, PGP19, At3g28860, MLD15.2' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Arabidopsis thaliana' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     3702 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     9606 
_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 
ADP non-polymer         n "ADENOSINE-5'-DIPHOSPHATE" ? 'C10 H15 N5 O10 P2' 427.201 
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 
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 
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  
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 
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 
VO4 non-polymer         . 'VANADATE ION'             ? 'O4 V -3'           114.939 
# 
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    MET 1    1    ?    ?   ?   A . n 
A 1 2    SER 2    2    ?    ?   ?   A . n 
A 1 3    GLU 3    3    ?    ?   ?   A . n 
A 1 4    THR 4    4    ?    ?   ?   A . n 
A 1 5    ASN 5    5    ?    ?   ?   A . n 
A 1 6    THR 6    6    ?    ?   ?   A . n 
A 1 7    THR 7    7    ?    ?   ?   A . n 
A 1 8    ASP 8    8    ?    ?   ?   A . n 
A 1 9    ALA 9    9    ?    ?   ?   A . n 
A 1 10   LYS 10   10   ?    ?   ?   A . n 
A 1 11   THR 11   11   ?    ?   ?   A . n 
A 1 12   VAL 12   12   ?    ?   ?   A . n 
A 1 13   PRO 13   13   ?    ?   ?   A . n 
A 1 14   ALA 14   14   ?    ?   ?   A . n 
A 1 15   GLU 15   15   ?    ?   ?   A . n 
A 1 16   ALA 16   16   ?    ?   ?   A . n 
A 1 17   GLU 17   17   ?    ?   ?   A . n 
A 1 18   LYS 18   18   ?    ?   ?   A . n 
A 1 19   LYS 19   19   ?    ?   ?   A . n 
A 1 20   LYS 20   20   ?    ?   ?   A . n 
A 1 21   GLU 21   21   21   GLU GLU A . n 
A 1 22   GLN 22   22   22   GLN GLN A . n 
A 1 23   SER 23   23   23   SER SER A . n 
A 1 24   LEU 24   24   24   LEU LEU A . n 
A 1 25   PRO 25   25   25   PRO PRO A . n 
A 1 26   PHE 26   26   26   PHE PHE A . n 
A 1 27   PHE 27   27   27   PHE PHE A . n 
A 1 28   LYS 28   28   28   LYS LYS A . n 
A 1 29   LEU 29   29   29   LEU LEU A . n 
A 1 30   PHE 30   30   30   PHE PHE A . n 
A 1 31   SER 31   31   31   SER SER A . n 
A 1 32   PHE 32   32   32   PHE PHE A . n 
A 1 33   ALA 33   33   33   ALA ALA A . n 
A 1 34   ASP 34   34   34   ASP ASP A . n 
A 1 35   LYS 35   35   35   LYS LYS A . n 
A 1 36   PHE 36   36   36   PHE PHE A . n 
A 1 37   ASP 37   37   37   ASP ASP A . n 
A 1 38   TYR 38   38   38   TYR TYR A . n 
A 1 39   LEU 39   39   39   LEU LEU A . n 
A 1 40   LEU 40   40   40   LEU LEU A . n 
A 1 41   MET 41   41   41   MET MET A . n 
A 1 42   PHE 42   42   42   PHE PHE A . n 
A 1 43   VAL 43   43   43   VAL VAL A . n 
A 1 44   GLY 44   44   44   GLY GLY A . n 
A 1 45   SER 45   45   45   SER SER A . n 
A 1 46   LEU 46   46   46   LEU LEU A . n 
A 1 47   GLY 47   47   47   GLY GLY A . n 
A 1 48   ALA 48   48   48   ALA ALA A . n 
A 1 49   ILE 49   49   49   ILE ILE A . n 
A 1 50   VAL 50   50   50   VAL VAL A . n 
A 1 51   HIS 51   51   51   HIS HIS A . n 
A 1 52   GLY 52   52   52   GLY GLY A . n 
A 1 53   SER 53   53   53   SER SER A . n 
A 1 54   SER 54   54   54   SER SER A . n 
A 1 55   MET 55   55   55   MET MET A . n 
A 1 56   PRO 56   56   56   PRO PRO A . n 
A 1 57   VAL 57   57   57   VAL VAL A . n 
A 1 58   PHE 58   58   58   PHE PHE A . n 
A 1 59   PHE 59   59   59   PHE PHE A . n 
A 1 60   LEU 60   60   60   LEU LEU A . n 
A 1 61   LEU 61   61   61   LEU LEU A . n 
A 1 62   PHE 62   62   62   PHE PHE A . n 
A 1 63   GLY 63   63   63   GLY GLY A . n 
A 1 64   GLN 64   64   64   GLN GLN A . n 
A 1 65   MET 65   65   65   MET MET A . n 
A 1 66   VAL 66   66   66   VAL VAL A . n 
A 1 67   ASN 67   67   67   ASN ASN A . n 
A 1 68   GLY 68   68   68   GLY GLY A . n 
A 1 69   PHE 69   69   69   PHE PHE A . n 
A 1 70   GLY 70   70   70   GLY GLY A . n 
A 1 71   LYS 71   71   71   LYS LYS A . n 
A 1 72   ASN 72   72   72   ASN ASN A . n 
A 1 73   GLN 73   73   73   GLN GLN A . n 
A 1 74   MET 74   74   74   MET MET A . n 
A 1 75   ASP 75   75   75   ASP ASP A . n 
A 1 76   LEU 76   76   76   LEU LEU A . n 
A 1 77   HIS 77   77   77   HIS HIS A . n 
A 1 78   GLN 78   78   78   GLN GLN A . n 
A 1 79   MET 79   79   79   MET MET A . n 
A 1 80   VAL 80   80   80   VAL VAL A . n 
A 1 81   HIS 81   81   81   HIS HIS A . n 
A 1 82   GLU 82   82   82   GLU GLU A . n 
A 1 83   VAL 83   83   83   VAL VAL A . n 
A 1 84   SER 84   84   84   SER SER A . n 
A 1 85   ARG 85   85   85   ARG ARG A . n 
A 1 86   TYR 86   86   86   TYR TYR A . n 
A 1 87   SER 87   87   87   SER SER A . n 
A 1 88   LEU 88   88   88   LEU LEU A . n 
A 1 89   TYR 89   89   89   TYR TYR A . n 
A 1 90   PHE 90   90   90   PHE PHE A . n 
A 1 91   VAL 91   91   91   VAL VAL A . n 
A 1 92   TYR 92   92   92   TYR TYR A . n 
A 1 93   LEU 93   93   93   LEU LEU A . n 
A 1 94   GLY 94   94   94   GLY GLY A . n 
A 1 95   LEU 95   95   95   LEU LEU A . n 
A 1 96   VAL 96   96   96   VAL VAL A . n 
A 1 97   VAL 97   97   97   VAL VAL A . n 
A 1 98   CYS 98   98   98   CYS CYS A . n 
A 1 99   PHE 99   99   99   PHE PHE A . n 
A 1 100  SER 100  100  100  SER SER A . n 
A 1 101  SER 101  101  101  SER SER A . n 
A 1 102  TYR 102  102  102  TYR TYR A . n 
A 1 103  ALA 103  103  103  ALA ALA A . n 
A 1 104  GLU 104  104  104  GLU GLU A . n 
A 1 105  ILE 105  105  105  ILE ILE A . n 
A 1 106  ALA 106  106  106  ALA ALA A . n 
A 1 107  CYS 107  107  107  CYS CYS A . n 
A 1 108  TRP 108  108  108  TRP TRP A . n 
A 1 109  MET 109  109  109  MET MET A . n 
A 1 110  TYR 110  110  110  TYR TYR A . n 
A 1 111  SER 111  111  111  SER SER A . n 
A 1 112  GLY 112  112  112  GLY GLY A . n 
A 1 113  GLU 113  113  113  GLU GLU A . n 
A 1 114  ARG 114  114  114  ARG ARG A . n 
A 1 115  GLN 115  115  115  GLN GLN A . n 
A 1 116  VAL 116  116  116  VAL VAL A . n 
A 1 117  ALA 117  117  117  ALA ALA A . n 
A 1 118  ALA 118  118  118  ALA ALA A . n 
A 1 119  LEU 119  119  119  LEU LEU A . n 
A 1 120  ARG 120  120  120  ARG ARG A . n 
A 1 121  LYS 121  121  121  LYS LYS A . n 
A 1 122  LYS 122  122  122  LYS LYS A . n 
A 1 123  TYR 123  123  123  TYR TYR A . n 
A 1 124  LEU 124  124  124  LEU LEU A . n 
A 1 125  GLU 125  125  125  GLU GLU A . n 
A 1 126  ALA 126  126  126  ALA ALA A . n 
A 1 127  VAL 127  127  127  VAL VAL A . n 
A 1 128  LEU 128  128  128  LEU LEU A . n 
A 1 129  LYS 129  129  129  LYS LYS A . n 
A 1 130  GLN 130  130  130  GLN GLN A . n 
A 1 131  ASP 131  131  131  ASP ASP A . n 
A 1 132  VAL 132  132  132  VAL VAL A . n 
A 1 133  GLY 133  133  133  GLY GLY A . n 
A 1 134  PHE 134  134  134  PHE PHE A . n 
A 1 135  PHE 135  135  135  PHE PHE A . n 
A 1 136  ASP 136  136  136  ASP ASP A . n 
A 1 137  THR 137  137  137  THR THR A . n 
A 1 138  ASP 138  138  138  ASP ASP A . n 
A 1 139  ALA 139  139  139  ALA ALA A . n 
A 1 140  ARG 140  140  140  ARG ARG A . n 
A 1 141  THR 141  141  141  THR THR A . n 
A 1 142  GLY 142  142  142  GLY GLY A . n 
A 1 143  ASP 143  143  143  ASP ASP A . n 
A 1 144  ILE 144  144  144  ILE ILE A . n 
A 1 145  VAL 145  145  145  VAL VAL A . n 
A 1 146  PHE 146  146  146  PHE PHE A . n 
A 1 147  SER 147  147  147  SER SER A . n 
A 1 148  VAL 148  148  148  VAL VAL A . n 
A 1 149  SER 149  149  149  SER SER A . n 
A 1 150  THR 150  150  150  THR THR A . n 
A 1 151  ASP 151  151  151  ASP ASP A . n 
A 1 152  THR 152  152  152  THR THR A . n 
A 1 153  LEU 153  153  153  LEU LEU A . n 
A 1 154  LEU 154  154  154  LEU LEU A . n 
A 1 155  VAL 155  155  155  VAL VAL A . n 
A 1 156  GLN 156  156  156  GLN GLN A . n 
A 1 157  ASP 157  157  157  ASP ASP A . n 
A 1 158  ALA 158  158  158  ALA ALA A . n 
A 1 159  ILE 159  159  159  ILE ILE A . n 
A 1 160  SER 160  160  160  SER SER A . n 
A 1 161  GLU 161  161  161  GLU GLU A . n 
A 1 162  LYS 162  162  162  LYS LYS A . n 
A 1 163  VAL 163  163  163  VAL VAL A . n 
A 1 164  GLY 164  164  164  GLY GLY A . n 
A 1 165  ASN 165  165  165  ASN ASN A . n 
A 1 166  PHE 166  166  166  PHE PHE A . n 
A 1 167  ILE 167  167  167  ILE ILE A . n 
A 1 168  HIS 168  168  168  HIS HIS A . n 
A 1 169  TYR 169  169  169  TYR TYR A . n 
A 1 170  LEU 170  170  170  LEU LEU A . n 
A 1 171  SER 171  171  171  SER SER A . n 
A 1 172  THR 172  172  172  THR THR A . n 
A 1 173  PHE 173  173  173  PHE PHE A . n 
A 1 174  LEU 174  174  174  LEU LEU A . n 
A 1 175  ALA 175  175  175  ALA ALA A . n 
A 1 176  GLY 176  176  176  GLY GLY A . n 
A 1 177  LEU 177  177  177  LEU LEU A . n 
A 1 178  VAL 178  178  178  VAL VAL A . n 
A 1 179  VAL 179  179  179  VAL VAL A . n 
A 1 180  GLY 180  180  180  GLY GLY A . n 
A 1 181  PHE 181  181  181  PHE PHE A . n 
A 1 182  VAL 182  182  182  VAL VAL A . n 
A 1 183  SER 183  183  183  SER SER A . n 
A 1 184  ALA 184  184  184  ALA ALA A . n 
A 1 185  TRP 185  185  185  TRP TRP A . n 
A 1 186  LYS 186  186  186  LYS LYS A . n 
A 1 187  LEU 187  187  187  LEU LEU A . n 
A 1 188  ALA 188  188  188  ALA ALA A . n 
A 1 189  LEU 189  189  189  LEU LEU A . n 
A 1 190  LEU 190  190  190  LEU LEU A . n 
A 1 191  SER 191  191  191  SER SER A . n 
A 1 192  VAL 192  192  192  VAL VAL A . n 
A 1 193  ALA 193  193  193  ALA ALA A . n 
A 1 194  VAL 194  194  194  VAL VAL A . n 
A 1 195  ILE 195  195  195  ILE ILE A . n 
A 1 196  PRO 196  196  196  PRO PRO A . n 
A 1 197  GLY 197  197  197  GLY GLY A . n 
A 1 198  ILE 198  198  198  ILE ILE A . n 
A 1 199  ALA 199  199  199  ALA ALA A . n 
A 1 200  PHE 200  200  200  PHE PHE A . n 
A 1 201  ALA 201  201  201  ALA ALA A . n 
A 1 202  GLY 202  202  202  GLY GLY A . n 
A 1 203  GLY 203  203  203  GLY GLY A . n 
A 1 204  LEU 204  204  204  LEU LEU A . n 
A 1 205  TYR 205  205  205  TYR TYR A . n 
A 1 206  ALA 206  206  206  ALA ALA A . n 
A 1 207  TYR 207  207  207  TYR TYR A . n 
A 1 208  THR 208  208  208  THR THR A . n 
A 1 209  LEU 209  209  209  LEU LEU A . n 
A 1 210  THR 210  210  210  THR THR A . n 
A 1 211  GLY 211  211  211  GLY GLY A . n 
A 1 212  ILE 212  212  212  ILE ILE A . n 
A 1 213  THR 213  213  213  THR THR A . n 
A 1 214  SER 214  214  214  SER SER A . n 
A 1 215  LYS 215  215  215  LYS LYS A . n 
A 1 216  SER 216  216  216  SER SER A . n 
A 1 217  ARG 217  217  217  ARG ARG A . n 
A 1 218  GLU 218  218  218  GLU GLU A . n 
A 1 219  SER 219  219  219  SER SER A . n 
A 1 220  TYR 220  220  220  TYR TYR A . n 
A 1 221  ALA 221  221  221  ALA ALA A . n 
A 1 222  ASN 222  222  222  ASN ASN A . n 
A 1 223  ALA 223  223  223  ALA ALA A . n 
A 1 224  GLY 224  224  224  GLY GLY A . n 
A 1 225  VAL 225  225  225  VAL VAL A . n 
A 1 226  ILE 226  226  226  ILE ILE A . n 
A 1 227  ALA 227  227  227  ALA ALA A . n 
A 1 228  GLU 228  228  228  GLU GLU A . n 
A 1 229  GLN 229  229  229  GLN GLN A . n 
A 1 230  ALA 230  230  230  ALA ALA A . n 
A 1 231  ILE 231  231  231  ILE ILE A . n 
A 1 232  ALA 232  232  232  ALA ALA A . n 
A 1 233  GLN 233  233  233  GLN GLN A . n 
A 1 234  VAL 234  234  234  VAL VAL A . n 
A 1 235  ARG 235  235  235  ARG ARG A . n 
A 1 236  THR 236  236  236  THR THR A . n 
A 1 237  VAL 237  237  237  VAL VAL A . n 
A 1 238  TYR 238  238  238  TYR TYR A . n 
A 1 239  SER 239  239  239  SER SER A . n 
A 1 240  TYR 240  240  240  TYR TYR A . n 
A 1 241  VAL 241  241  241  VAL VAL A . n 
A 1 242  GLY 242  242  242  GLY GLY A . n 
A 1 243  GLU 243  243  243  GLU GLU A . n 
A 1 244  SER 244  244  244  SER SER A . n 
A 1 245  LYS 245  245  245  LYS LYS A . n 
A 1 246  ALA 246  246  246  ALA ALA A . n 
A 1 247  LEU 247  247  247  LEU LEU A . n 
A 1 248  ASN 248  248  248  ASN ASN A . n 
A 1 249  ALA 249  249  249  ALA ALA A . n 
A 1 250  TYR 250  250  250  TYR TYR A . n 
A 1 251  SER 251  251  251  SER SER A . n 
A 1 252  ASP 252  252  252  ASP ASP A . n 
A 1 253  ALA 253  253  253  ALA ALA A . n 
A 1 254  ILE 254  254  254  ILE ILE A . n 
A 1 255  GLN 255  255  255  GLN GLN A . n 
A 1 256  TYR 256  256  256  TYR TYR A . n 
A 1 257  THR 257  257  257  THR THR A . n 
A 1 258  LEU 258  258  258  LEU LEU A . n 
A 1 259  LYS 259  259  259  LYS LYS A . n 
A 1 260  LEU 260  260  260  LEU LEU A . n 
A 1 261  GLY 261  261  261  GLY GLY A . n 
A 1 262  TYR 262  262  262  TYR TYR A . n 
A 1 263  LYS 263  263  263  LYS LYS A . n 
A 1 264  ALA 264  264  264  ALA ALA A . n 
A 1 265  GLY 265  265  265  GLY GLY A . n 
A 1 266  MET 266  266  266  MET MET A . n 
A 1 267  ALA 267  267  267  ALA ALA A . n 
A 1 268  LYS 268  268  268  LYS LYS A . n 
A 1 269  GLY 269  269  269  GLY GLY A . n 
A 1 270  LEU 270  270  270  LEU LEU A . n 
A 1 271  GLY 271  271  271  GLY GLY A . n 
A 1 272  LEU 272  272  272  LEU LEU A . n 
A 1 273  GLY 273  273  273  GLY GLY A . n 
A 1 274  CYS 274  274  274  CYS CYS A . n 
A 1 275  THR 275  275  275  THR THR A . n 
A 1 276  TYR 276  276  276  TYR TYR A . n 
A 1 277  GLY 277  277  277  GLY GLY A . n 
A 1 278  ILE 278  278  278  ILE ILE A . n 
A 1 279  ALA 279  279  279  ALA ALA A . n 
A 1 280  CYS 280  280  280  CYS CYS A . n 
A 1 281  MET 281  281  281  MET MET A . n 
A 1 282  SER 282  282  282  SER SER A . n 
A 1 283  TRP 283  283  283  TRP TRP A . n 
A 1 284  ALA 284  284  284  ALA ALA A . n 
A 1 285  LEU 285  285  285  LEU LEU A . n 
A 1 286  VAL 286  286  286  VAL VAL A . n 
A 1 287  PHE 287  287  287  PHE PHE A . n 
A 1 288  TRP 288  288  288  TRP TRP A . n 
A 1 289  TYR 289  289  289  TYR TYR A . n 
A 1 290  ALA 290  290  290  ALA ALA A . n 
A 1 291  GLY 291  291  291  GLY GLY A . n 
A 1 292  VAL 292  292  292  VAL VAL A . n 
A 1 293  PHE 293  293  293  PHE PHE A . n 
A 1 294  ILE 294  294  294  ILE ILE A . n 
A 1 295  ARG 295  295  295  ARG ARG A . n 
A 1 296  ASN 296  296  296  ASN ASN A . n 
A 1 297  GLY 297  297  297  GLY GLY A . n 
A 1 298  GLN 298  298  298  GLN GLN A . n 
A 1 299  THR 299  299  299  THR THR A . n 
A 1 300  ASP 300  300  300  ASP ASP A . n 
A 1 301  GLY 301  301  301  GLY GLY A . n 
A 1 302  GLY 302  302  302  GLY GLY A . n 
A 1 303  LYS 303  303  303  LYS LYS A . n 
A 1 304  ALA 304  304  304  ALA ALA A . n 
A 1 305  PHE 305  305  305  PHE PHE A . n 
A 1 306  THR 306  306  306  THR THR A . n 
A 1 307  ALA 307  307  307  ALA ALA A . n 
A 1 308  ILE 308  308  308  ILE ILE A . n 
A 1 309  PHE 309  309  309  PHE PHE A . n 
A 1 310  SER 310  310  310  SER SER A . n 
A 1 311  ALA 311  311  311  ALA ALA A . n 
A 1 312  ILE 312  312  312  ILE ILE A . n 
A 1 313  VAL 313  313  313  VAL VAL A . n 
A 1 314  GLY 314  314  314  GLY GLY A . n 
A 1 315  GLY 315  315  315  GLY GLY A . n 
A 1 316  MET 316  316  316  MET MET A . n 
A 1 317  SER 317  317  317  SER SER A . n 
A 1 318  LEU 318  318  318  LEU LEU A . n 
A 1 319  GLY 319  319  319  GLY GLY A . n 
A 1 320  GLN 320  320  320  GLN GLN A . n 
A 1 321  SER 321  321  321  SER SER A . n 
A 1 322  PHE 322  322  322  PHE PHE A . n 
A 1 323  SER 323  323  323  SER SER A . n 
A 1 324  ASN 324  324  324  ASN ASN A . n 
A 1 325  LEU 325  325  325  LEU LEU A . n 
A 1 326  GLY 326  326  326  GLY GLY A . n 
A 1 327  ALA 327  327  327  ALA ALA A . n 
A 1 328  PHE 328  328  328  PHE PHE A . n 
A 1 329  SER 329  329  329  SER SER A . n 
A 1 330  LYS 330  330  330  LYS LYS A . n 
A 1 331  GLY 331  331  331  GLY GLY A . n 
A 1 332  LYS 332  332  332  LYS LYS A . n 
A 1 333  ALA 333  333  333  ALA ALA A . n 
A 1 334  ALA 334  334  334  ALA ALA A . n 
A 1 335  GLY 335  335  335  GLY GLY A . n 
A 1 336  TYR 336  336  336  TYR TYR A . n 
A 1 337  LYS 337  337  337  LYS LYS A . n 
A 1 338  LEU 338  338  338  LEU LEU A . n 
A 1 339  MET 339  339  339  MET MET A . n 
A 1 340  GLU 340  340  340  GLU GLU A . n 
A 1 341  ILE 341  341  341  ILE ILE A . n 
A 1 342  ILE 342  342  342  ILE ILE A . n 
A 1 343  ASN 343  343  343  ASN ASN A . n 
A 1 344  GLN 344  344  344  GLN GLN A . n 
A 1 345  ARG 345  345  345  ARG ARG A . n 
A 1 346  PRO 346  346  346  PRO PRO A . n 
A 1 347  THR 347  347  347  THR THR A . n 
A 1 348  ILE 348  348  348  ILE ILE A . n 
A 1 349  ILE 349  349  349  ILE ILE A . n 
A 1 350  GLN 350  350  350  GLN GLN A . n 
A 1 351  ASP 351  351  351  ASP ASP A . n 
A 1 352  PRO 352  352  352  PRO PRO A . n 
A 1 353  LEU 353  353  353  LEU LEU A . n 
A 1 354  ASP 354  354  354  ASP ASP A . n 
A 1 355  GLY 355  355  355  GLY GLY A . n 
A 1 356  LYS 356  356  356  LYS LYS A . n 
A 1 357  CYS 357  357  357  CYS CYS A . n 
A 1 358  LEU 358  358  358  LEU LEU A . n 
A 1 359  ASP 359  359  359  ASP ASP A . n 
A 1 360  GLN 360  360  360  GLN GLN A . n 
A 1 361  VAL 361  361  361  VAL VAL A . n 
A 1 362  HIS 362  362  362  HIS HIS A . n 
A 1 363  GLY 363  363  363  GLY GLY A . n 
A 1 364  ASN 364  364  364  ASN ASN A . n 
A 1 365  ILE 365  365  365  ILE ILE A . n 
A 1 366  GLU 366  366  366  GLU GLU A . n 
A 1 367  PHE 367  367  367  PHE PHE A . n 
A 1 368  LYS 368  368  368  LYS LYS A . n 
A 1 369  ASP 369  369  369  ASP ASP A . n 
A 1 370  VAL 370  370  370  VAL VAL A . n 
A 1 371  THR 371  371  371  THR THR A . n 
A 1 372  PHE 372  372  372  PHE PHE A . n 
A 1 373  SER 373  373  373  SER SER A . n 
A 1 374  TYR 374  374  374  TYR TYR A . n 
A 1 375  PRO 375  375  375  PRO PRO A . n 
A 1 376  SER 376  376  376  SER SER A . n 
A 1 377  ARG 377  377  377  ARG ARG A . n 
A 1 378  PRO 378  378  378  PRO PRO A . n 
A 1 379  ASP 379  379  379  ASP ASP A . n 
A 1 380  VAL 380  380  380  VAL VAL A . n 
A 1 381  MET 381  381  381  MET MET A . n 
A 1 382  ILE 382  382  382  ILE ILE A . n 
A 1 383  PHE 383  383  383  PHE PHE A . n 
A 1 384  ARG 384  384  384  ARG ARG A . n 
A 1 385  ASN 385  385  385  ASN ASN A . n 
A 1 386  PHE 386  386  386  PHE PHE A . n 
A 1 387  ASN 387  387  387  ASN ASN A . n 
A 1 388  ILE 388  388  388  ILE ILE A . n 
A 1 389  PHE 389  389  389  PHE PHE A . n 
A 1 390  PHE 390  390  390  PHE PHE A . n 
A 1 391  PRO 391  391  391  PRO PRO A . n 
A 1 392  SER 392  392  392  SER SER A . n 
A 1 393  GLY 393  393  393  GLY GLY A . n 
A 1 394  LYS 394  394  394  LYS LYS A . n 
A 1 395  THR 395  395  395  THR THR A . n 
A 1 396  VAL 396  396  396  VAL VAL A . n 
A 1 397  ALA 397  397  397  ALA ALA A . n 
A 1 398  VAL 398  398  398  VAL VAL A . n 
A 1 399  VAL 399  399  399  VAL VAL A . n 
A 1 400  GLY 400  400  400  GLY GLY A . n 
A 1 401  GLY 401  401  401  GLY GLY A . n 
A 1 402  SER 402  402  402  SER SER A . n 
A 1 403  GLY 403  403  403  GLY GLY A . n 
A 1 404  SER 404  404  404  SER SER A . n 
A 1 405  GLY 405  405  405  GLY GLY A . n 
A 1 406  LYS 406  406  406  LYS LYS A . n 
A 1 407  SER 407  407  407  SER SER A . n 
A 1 408  THR 408  408  408  THR THR A . n 
A 1 409  VAL 409  409  409  VAL VAL A . n 
A 1 410  VAL 410  410  410  VAL VAL A . n 
A 1 411  SER 411  411  411  SER SER A . n 
A 1 412  LEU 412  412  412  LEU LEU A . n 
A 1 413  ILE 413  413  413  ILE ILE A . n 
A 1 414  GLU 414  414  414  GLU GLU A . n 
A 1 415  ARG 415  415  415  ARG ARG A . n 
A 1 416  PHE 416  416  416  PHE PHE A . n 
A 1 417  TYR 417  417  417  TYR TYR A . n 
A 1 418  ASP 418  418  418  ASP ASP A . n 
A 1 419  PRO 419  419  419  PRO PRO A . n 
A 1 420  ASN 420  420  420  ASN ASN A . n 
A 1 421  SER 421  421  421  SER SER A . n 
A 1 422  GLY 422  422  422  GLY GLY A . n 
A 1 423  GLN 423  423  423  GLN GLN A . n 
A 1 424  ILE 424  424  424  ILE ILE A . n 
A 1 425  LEU 425  425  425  LEU LEU A . n 
A 1 426  LEU 426  426  426  LEU LEU A . n 
A 1 427  ASP 427  427  427  ASP ASP A . n 
A 1 428  GLY 428  428  428  GLY GLY A . n 
A 1 429  VAL 429  429  429  VAL VAL A . n 
A 1 430  GLU 430  430  430  GLU GLU A . n 
A 1 431  ILE 431  431  431  ILE ILE A . n 
A 1 432  LYS 432  432  432  LYS LYS A . n 
A 1 433  THR 433  433  433  THR THR A . n 
A 1 434  LEU 434  434  434  LEU LEU A . n 
A 1 435  GLN 435  435  435  GLN GLN A . n 
A 1 436  LEU 436  436  436  LEU LEU A . n 
A 1 437  LYS 437  437  437  LYS LYS A . n 
A 1 438  PHE 438  438  438  PHE PHE A . n 
A 1 439  LEU 439  439  439  LEU LEU A . n 
A 1 440  ARG 440  440  440  ARG ARG A . n 
A 1 441  GLU 441  441  441  GLU GLU A . n 
A 1 442  GLN 442  442  442  GLN GLN A . n 
A 1 443  ILE 443  443  443  ILE ILE A . n 
A 1 444  GLY 444  444  444  GLY GLY A . n 
A 1 445  LEU 445  445  445  LEU LEU A . n 
A 1 446  VAL 446  446  446  VAL VAL A . n 
A 1 447  ASN 447  447  447  ASN ASN A . n 
A 1 448  GLN 448  448  448  GLN GLN A . n 
A 1 449  GLU 449  449  449  GLU GLU A . n 
A 1 450  PRO 450  450  450  PRO PRO A . n 
A 1 451  ALA 451  451  451  ALA ALA A . n 
A 1 452  LEU 452  452  452  LEU LEU A . n 
A 1 453  PHE 453  453  453  PHE PHE A . n 
A 1 454  ALA 454  454  454  ALA ALA A . n 
A 1 455  THR 455  455  455  THR THR A . n 
A 1 456  THR 456  456  456  THR THR A . n 
A 1 457  ILE 457  457  457  ILE ILE A . n 
A 1 458  LEU 458  458  458  LEU LEU A . n 
A 1 459  GLU 459  459  459  GLU GLU A . n 
A 1 460  ASN 460  460  460  ASN ASN A . n 
A 1 461  ILE 461  461  461  ILE ILE A . n 
A 1 462  LEU 462  462  462  LEU LEU A . n 
A 1 463  TYR 463  463  463  TYR TYR A . n 
A 1 464  GLY 464  464  464  GLY GLY A . n 
A 1 465  LYS 465  465  465  LYS LYS A . n 
A 1 466  PRO 466  466  466  PRO PRO A . n 
A 1 467  ASP 467  467  467  ASP ASP A . n 
A 1 468  ALA 468  468  468  ALA ALA A . n 
A 1 469  THR 469  469  469  THR THR A . n 
A 1 470  MET 470  470  470  MET MET A . n 
A 1 471  VAL 471  471  471  VAL VAL A . n 
A 1 472  GLU 472  472  472  GLU GLU A . n 
A 1 473  VAL 473  473  473  VAL VAL A . n 
A 1 474  GLU 474  474  474  GLU GLU A . n 
A 1 475  ALA 475  475  475  ALA ALA A . n 
A 1 476  ALA 476  476  476  ALA ALA A . n 
A 1 477  ALA 477  477  477  ALA ALA A . n 
A 1 478  SER 478  478  478  SER SER A . n 
A 1 479  ALA 479  479  479  ALA ALA A . n 
A 1 480  ALA 480  480  480  ALA ALA A . n 
A 1 481  ASN 481  481  481  ASN ASN A . n 
A 1 482  ALA 482  482  482  ALA ALA A . n 
A 1 483  HIS 483  483  483  HIS HIS A . n 
A 1 484  SER 484  484  484  SER SER A . n 
A 1 485  PHE 485  485  485  PHE PHE A . n 
A 1 486  ILE 486  486  486  ILE ILE A . n 
A 1 487  THR 487  487  487  THR THR A . n 
A 1 488  LEU 488  488  488  LEU LEU A . n 
A 1 489  LEU 489  489  489  LEU LEU A . n 
A 1 490  PRO 490  490  490  PRO PRO A . n 
A 1 491  LYS 491  491  491  LYS LYS A . n 
A 1 492  GLY 492  492  492  GLY GLY A . n 
A 1 493  TYR 493  493  493  TYR TYR A . n 
A 1 494  ASP 494  494  494  ASP ASP A . n 
A 1 495  THR 495  495  495  THR THR A . n 
A 1 496  GLN 496  496  496  GLN GLN A . n 
A 1 497  VAL 497  497  497  VAL VAL A . n 
A 1 498  GLY 498  498  498  GLY GLY A . n 
A 1 499  GLU 499  499  499  GLU GLU A . n 
A 1 500  ARG 500  500  500  ARG ARG A . n 
A 1 501  GLY 501  501  501  GLY GLY A . n 
A 1 502  VAL 502  502  502  VAL VAL A . n 
A 1 503  GLN 503  503  503  GLN GLN A . n 
A 1 504  LEU 504  504  504  LEU LEU A . n 
A 1 505  SER 505  505  505  SER SER A . n 
A 1 506  GLY 506  506  506  GLY GLY A . n 
A 1 507  GLY 507  507  507  GLY GLY A . n 
A 1 508  GLN 508  508  508  GLN GLN A . n 
A 1 509  LYS 509  509  509  LYS LYS A . n 
A 1 510  GLN 510  510  510  GLN GLN A . n 
A 1 511  ARG 511  511  511  ARG ARG A . n 
A 1 512  ILE 512  512  512  ILE ILE A . n 
A 1 513  ALA 513  513  513  ALA ALA A . n 
A 1 514  ILE 514  514  514  ILE ILE A . n 
A 1 515  ALA 515  515  515  ALA ALA A . n 
A 1 516  ARG 516  516  516  ARG ARG A . n 
A 1 517  ALA 517  517  517  ALA ALA A . n 
A 1 518  MET 518  518  518  MET MET A . n 
A 1 519  LEU 519  519  519  LEU LEU A . n 
A 1 520  LYS 520  520  520  LYS LYS A . n 
A 1 521  ASP 521  521  521  ASP ASP A . n 
A 1 522  PRO 522  522  522  PRO PRO A . n 
A 1 523  LYS 523  523  523  LYS LYS A . n 
A 1 524  ILE 524  524  524  ILE ILE A . n 
A 1 525  LEU 525  525  525  LEU LEU A . n 
A 1 526  LEU 526  526  526  LEU LEU A . n 
A 1 527  LEU 527  527  527  LEU LEU A . n 
A 1 528  ASP 528  528  528  ASP ASP A . n 
A 1 529  GLU 529  529  529  GLU GLU A . n 
A 1 530  ALA 530  530  530  ALA ALA A . n 
A 1 531  THR 531  531  531  THR THR A . n 
A 1 532  SER 532  532  532  SER SER A . n 
A 1 533  ALA 533  533  533  ALA ALA A . n 
A 1 534  LEU 534  534  534  LEU LEU A . n 
A 1 535  ASP 535  535  535  ASP ASP A . n 
A 1 536  ALA 536  536  536  ALA ALA A . n 
A 1 537  SER 537  537  537  SER SER A . n 
A 1 538  SER 538  538  538  SER SER A . n 
A 1 539  GLU 539  539  539  GLU GLU A . n 
A 1 540  SER 540  540  540  SER SER A . n 
A 1 541  ILE 541  541  541  ILE ILE A . n 
A 1 542  VAL 542  542  542  VAL VAL A . n 
A 1 543  GLN 543  543  543  GLN GLN A . n 
A 1 544  GLU 544  544  544  GLU GLU A . n 
A 1 545  ALA 545  545  545  ALA ALA A . n 
A 1 546  LEU 546  546  546  LEU LEU A . n 
A 1 547  ASP 547  547  547  ASP ASP A . n 
A 1 548  ARG 548  548  548  ARG ARG A . n 
A 1 549  VAL 549  549  549  VAL VAL A . n 
A 1 550  MET 550  550  550  MET MET A . n 
A 1 551  VAL 551  551  551  VAL VAL A . n 
A 1 552  GLY 552  552  552  GLY GLY A . n 
A 1 553  ARG 553  553  553  ARG ARG A . n 
A 1 554  THR 554  554  554  THR THR A . n 
A 1 555  THR 555  555  555  THR THR A . n 
A 1 556  VAL 556  556  556  VAL VAL A . n 
A 1 557  VAL 557  557  557  VAL VAL A . n 
A 1 558  VAL 558  558  558  VAL VAL A . n 
A 1 559  ALA 559  559  559  ALA ALA A . n 
A 1 560  HIS 560  560  560  HIS HIS A . n 
A 1 561  ARG 561  561  561  ARG ARG A . n 
A 1 562  LEU 562  562  562  LEU LEU A . n 
A 1 563  CYS 563  563  563  CYS CYS A . n 
A 1 564  THR 564  564  564  THR THR A . n 
A 1 565  ILE 565  565  565  ILE ILE A . n 
A 1 566  ARG 566  566  566  ARG ARG A . n 
A 1 567  ASN 567  567  567  ASN ASN A . n 
A 1 568  VAL 568  568  568  VAL VAL A . n 
A 1 569  ASP 569  569  569  ASP ASP A . n 
A 1 570  SER 570  570  570  SER SER A . n 
A 1 571  ILE 571  571  571  ILE ILE A . n 
A 1 572  ALA 572  572  572  ALA ALA A . n 
A 1 573  VAL 573  573  573  VAL VAL A . n 
A 1 574  ILE 574  574  574  ILE ILE A . n 
A 1 575  GLN 575  575  575  GLN GLN A . n 
A 1 576  GLN 576  576  576  GLN GLN A . n 
A 1 577  GLY 577  577  577  GLY GLY A . n 
A 1 578  GLN 578  578  578  GLN GLN A . n 
A 1 579  VAL 579  579  579  VAL VAL A . n 
A 1 580  VAL 580  580  580  VAL VAL A . n 
A 1 581  GLU 581  581  581  GLU GLU A . n 
A 1 582  THR 582  582  582  THR THR A . n 
A 1 583  GLY 583  583  583  GLY GLY A . n 
A 1 584  THR 584  584  584  THR THR A . n 
A 1 585  HIS 585  585  585  HIS HIS A . n 
A 1 586  GLU 586  586  586  GLU GLU A . n 
A 1 587  GLU 587  587  587  GLU GLU A . n 
A 1 588  LEU 588  588  588  LEU LEU A . n 
A 1 589  ILE 589  589  589  ILE ILE A . n 
A 1 590  ALA 590  590  590  ALA ALA A . n 
A 1 591  LYS 591  591  591  LYS LYS A . n 
A 1 592  SER 592  592  592  SER SER A . n 
A 1 593  GLY 593  593  593  GLY GLY A . n 
A 1 594  ALA 594  594  594  ALA ALA A . n 
A 1 595  TYR 595  595  595  TYR TYR A . n 
A 1 596  ALA 596  596  596  ALA ALA A . n 
A 1 597  SER 597  597  597  SER SER A . n 
A 1 598  LEU 598  598  598  LEU LEU A . n 
A 1 599  ILE 599  599  599  ILE ILE A . n 
A 1 600  ARG 600  600  600  ARG ARG A . n 
A 1 601  PHE 601  601  601  PHE PHE A . n 
A 1 602  GLN 602  602  602  GLN GLN A . n 
A 1 603  GLU 603  603  603  GLU GLU A . n 
A 1 604  MET 604  604  604  MET MET A . n 
A 1 605  VAL 605  605  605  VAL VAL A . n 
A 1 606  GLY 606  606  606  GLY GLY A . n 
A 1 607  THR 607  607  607  THR THR A . n 
A 1 608  ARG 608  608  ?    ?   ?   A . n 
A 1 609  ASP 609  609  ?    ?   ?   A . n 
A 1 610  PHE 610  610  ?    ?   ?   A . n 
A 1 611  SER 611  611  ?    ?   ?   A . n 
A 1 612  ASN 612  612  ?    ?   ?   A . n 
A 1 613  PRO 613  613  ?    ?   ?   A . n 
A 1 614  SER 614  614  ?    ?   ?   A . n 
A 1 615  THR 615  615  ?    ?   ?   A . n 
A 1 616  ARG 616  616  ?    ?   ?   A . n 
A 1 617  ARG 617  617  ?    ?   ?   A . n 
A 1 618  THR 618  618  ?    ?   ?   A . n 
A 1 619  ARG 619  619  ?    ?   ?   A . n 
A 1 620  SER 620  620  ?    ?   ?   A . n 
A 1 621  THR 621  621  ?    ?   ?   A . n 
A 1 622  ARG 622  622  ?    ?   ?   A . n 
A 1 623  LEU 623  623  ?    ?   ?   A . n 
A 1 624  SER 624  624  ?    ?   ?   A . n 
A 1 625  HIS 625  625  ?    ?   ?   A . n 
A 1 626  SER 626  626  ?    ?   ?   A . n 
A 1 627  LEU 627  627  ?    ?   ?   A . n 
A 1 628  SER 628  628  ?    ?   ?   A . n 
A 1 629  THR 629  629  ?    ?   ?   A . n 
A 1 630  LYS 630  630  ?    ?   ?   A . n 
A 1 631  SER 631  631  ?    ?   ?   A . n 
A 1 632  LEU 632  632  ?    ?   ?   A . n 
A 1 633  SER 633  633  ?    ?   ?   A . n 
A 1 634  LEU 634  634  ?    ?   ?   A . n 
A 1 635  ARG 635  635  ?    ?   ?   A . n 
A 1 636  SER 636  636  ?    ?   ?   A . n 
A 1 637  GLY 637  637  ?    ?   ?   A . n 
A 1 638  SER 638  638  ?    ?   ?   A . n 
A 1 639  LEU 639  639  ?    ?   ?   A . n 
A 1 640  ARG 640  640  ?    ?   ?   A . n 
A 1 641  ASN 641  641  ?    ?   ?   A . n 
A 1 642  LEU 642  642  ?    ?   ?   A . n 
A 1 643  SER 643  643  ?    ?   ?   A . n 
A 1 644  TYR 644  644  ?    ?   ?   A . n 
A 1 645  SER 645  645  ?    ?   ?   A . n 
A 1 646  TYR 646  646  ?    ?   ?   A . n 
A 1 647  SER 647  647  ?    ?   ?   A . n 
A 1 648  THR 648  648  ?    ?   ?   A . n 
A 1 649  GLY 649  649  ?    ?   ?   A . n 
A 1 650  ALA 650  650  ?    ?   ?   A . n 
A 1 651  ASP 651  651  ?    ?   ?   A . n 
A 1 652  GLY 652  652  ?    ?   ?   A . n 
A 1 653  ARG 653  653  ?    ?   ?   A . n 
A 1 654  ILE 654  654  ?    ?   ?   A . n 
A 1 655  GLU 655  655  ?    ?   ?   A . n 
A 1 656  MET 656  656  ?    ?   ?   A . n 
A 1 657  ILE 657  657  ?    ?   ?   A . n 
A 1 658  SER 658  658  ?    ?   ?   A . n 
A 1 659  ASN 659  659  ?    ?   ?   A . n 
A 1 660  ALA 660  660  ?    ?   ?   A . n 
A 1 661  GLU 661  661  ?    ?   ?   A . n 
A 1 662  THR 662  662  ?    ?   ?   A . n 
A 1 663  ASP 663  663  ?    ?   ?   A . n 
A 1 664  ARG 664  664  ?    ?   ?   A . n 
A 1 665  LYS 665  665  ?    ?   ?   A . n 
A 1 666  THR 666  666  ?    ?   ?   A . n 
A 1 667  ARG 667  667  ?    ?   ?   A . n 
A 1 668  ALA 668  668  ?    ?   ?   A . n 
A 1 669  PRO 669  669  ?    ?   ?   A . n 
A 1 670  GLU 670  670  670  GLU GLU A . n 
A 1 671  ASN 671  671  671  ASN ASN A . n 
A 1 672  TYR 672  672  672  TYR TYR A . n 
A 1 673  PHE 673  673  673  PHE PHE A . n 
A 1 674  TYR 674  674  674  TYR TYR A . n 
A 1 675  ARG 675  675  675  ARG ARG A . n 
A 1 676  LEU 676  676  676  LEU LEU A . n 
A 1 677  LEU 677  677  677  LEU LEU A . n 
A 1 678  LYS 678  678  678  LYS LYS A . n 
A 1 679  LEU 679  679  679  LEU LEU A . n 
A 1 680  ASN 680  680  680  ASN ASN A . n 
A 1 681  SER 681  681  681  SER SER A . n 
A 1 682  PRO 682  682  682  PRO PRO A . n 
A 1 683  GLU 683  683  683  GLU GLU A . n 
A 1 684  TRP 684  684  684  TRP TRP A . n 
A 1 685  PRO 685  685  685  PRO PRO A . n 
A 1 686  TYR 686  686  686  TYR TYR A . n 
A 1 687  SER 687  687  687  SER SER A . n 
A 1 688  ILE 688  688  688  ILE ILE A . n 
A 1 689  MET 689  689  689  MET MET A . n 
A 1 690  GLY 690  690  690  GLY GLY A . n 
A 1 691  ALA 691  691  691  ALA ALA A . n 
A 1 692  VAL 692  692  692  VAL VAL A . n 
A 1 693  GLY 693  693  693  GLY GLY A . n 
A 1 694  SER 694  694  694  SER SER A . n 
A 1 695  ILE 695  695  695  ILE ILE A . n 
A 1 696  LEU 696  696  696  LEU LEU A . n 
A 1 697  SER 697  697  697  SER SER A . n 
A 1 698  GLY 698  698  698  GLY GLY A . n 
A 1 699  PHE 699  699  699  PHE PHE A . n 
A 1 700  ILE 700  700  700  ILE ILE A . n 
A 1 701  GLY 701  701  701  GLY GLY A . n 
A 1 702  PRO 702  702  702  PRO PRO A . n 
A 1 703  THR 703  703  703  THR THR A . n 
A 1 704  PHE 704  704  704  PHE PHE A . n 
A 1 705  ALA 705  705  705  ALA ALA A . n 
A 1 706  ILE 706  706  706  ILE ILE A . n 
A 1 707  VAL 707  707  707  VAL VAL A . n 
A 1 708  MET 708  708  708  MET MET A . n 
A 1 709  SER 709  709  709  SER SER A . n 
A 1 710  ASN 710  710  710  ASN ASN A . n 
A 1 711  MET 711  711  711  MET MET A . n 
A 1 712  ILE 712  712  712  ILE ILE A . n 
A 1 713  GLU 713  713  713  GLU GLU A . n 
A 1 714  VAL 714  714  714  VAL VAL A . n 
A 1 715  PHE 715  715  715  PHE PHE A . n 
A 1 716  TYR 716  716  716  TYR TYR A . n 
A 1 717  TYR 717  717  717  TYR TYR A . n 
A 1 718  THR 718  718  718  THR THR A . n 
A 1 719  ASP 719  719  719  ASP ASP A . n 
A 1 720  TYR 720  720  720  TYR TYR A . n 
A 1 721  ASP 721  721  721  ASP ASP A . n 
A 1 722  SER 722  722  722  SER SER A . n 
A 1 723  MET 723  723  723  MET MET A . n 
A 1 724  GLU 724  724  724  GLU GLU A . n 
A 1 725  ARG 725  725  725  ARG ARG A . n 
A 1 726  LYS 726  726  726  LYS LYS A . n 
A 1 727  THR 727  727  727  THR THR A . n 
A 1 728  LYS 728  728  728  LYS LYS A . n 
A 1 729  GLU 729  729  729  GLU GLU A . n 
A 1 730  TYR 730  730  730  TYR TYR A . n 
A 1 731  VAL 731  731  731  VAL VAL A . n 
A 1 732  PHE 732  732  732  PHE PHE A . n 
A 1 733  ILE 733  733  733  ILE ILE A . n 
A 1 734  TYR 734  734  734  TYR TYR A . n 
A 1 735  ILE 735  735  735  ILE ILE A . n 
A 1 736  GLY 736  736  736  GLY GLY A . n 
A 1 737  ALA 737  737  737  ALA ALA A . n 
A 1 738  GLY 738  738  738  GLY GLY A . n 
A 1 739  LEU 739  739  739  LEU LEU A . n 
A 1 740  TYR 740  740  740  TYR TYR A . n 
A 1 741  ALA 741  741  741  ALA ALA A . n 
A 1 742  VAL 742  742  742  VAL VAL A . n 
A 1 743  GLY 743  743  743  GLY GLY A . n 
A 1 744  ALA 744  744  744  ALA ALA A . n 
A 1 745  TYR 745  745  745  TYR TYR A . n 
A 1 746  LEU 746  746  746  LEU LEU A . n 
A 1 747  ILE 747  747  747  ILE ILE A . n 
A 1 748  GLN 748  748  748  GLN GLN A . n 
A 1 749  HIS 749  749  749  HIS HIS A . n 
A 1 750  TYR 750  750  750  TYR TYR A . n 
A 1 751  PHE 751  751  751  PHE PHE A . n 
A 1 752  PHE 752  752  752  PHE PHE A . n 
A 1 753  SER 753  753  753  SER SER A . n 
A 1 754  ILE 754  754  754  ILE ILE A . n 
A 1 755  MET 755  755  755  MET MET A . n 
A 1 756  GLY 756  756  756  GLY GLY A . n 
A 1 757  GLU 757  757  757  GLU GLU A . n 
A 1 758  ASN 758  758  758  ASN ASN A . n 
A 1 759  LEU 759  759  759  LEU LEU A . n 
A 1 760  THR 760  760  760  THR THR A . n 
A 1 761  THR 761  761  761  THR THR A . n 
A 1 762  ARG 762  762  762  ARG ARG A . n 
A 1 763  VAL 763  763  763  VAL VAL A . n 
A 1 764  ARG 764  764  764  ARG ARG A . n 
A 1 765  ARG 765  765  765  ARG ARG A . n 
A 1 766  MET 766  766  766  MET MET A . n 
A 1 767  MET 767  767  767  MET MET A . n 
A 1 768  LEU 768  768  768  LEU LEU A . n 
A 1 769  SER 769  769  769  SER SER A . n 
A 1 770  ALA 770  770  770  ALA ALA A . n 
A 1 771  ILE 771  771  771  ILE ILE A . n 
A 1 772  LEU 772  772  772  LEU LEU A . n 
A 1 773  ARG 773  773  773  ARG ARG A . n 
A 1 774  ASN 774  774  774  ASN ASN A . n 
A 1 775  GLU 775  775  775  GLU GLU A . n 
A 1 776  VAL 776  776  776  VAL VAL A . n 
A 1 777  GLY 777  777  777  GLY GLY A . n 
A 1 778  TRP 778  778  778  TRP TRP A . n 
A 1 779  PHE 779  779  779  PHE PHE A . n 
A 1 780  ASP 780  780  780  ASP ASP A . n 
A 1 781  GLU 781  781  781  GLU GLU A . n 
A 1 782  ASP 782  782  782  ASP ASP A . n 
A 1 783  GLU 783  783  783  GLU GLU A . n 
A 1 784  HIS 784  784  784  HIS HIS A . n 
A 1 785  ASN 785  785  785  ASN ASN A . n 
A 1 786  SER 786  786  786  SER SER A . n 
A 1 787  SER 787  787  787  SER SER A . n 
A 1 788  LEU 788  788  788  LEU LEU A . n 
A 1 789  ILE 789  789  789  ILE ILE A . n 
A 1 790  ALA 790  790  790  ALA ALA A . n 
A 1 791  ALA 791  791  791  ALA ALA A . n 
A 1 792  ARG 792  792  792  ARG ARG A . n 
A 1 793  LEU 793  793  793  LEU LEU A . n 
A 1 794  ALA 794  794  794  ALA ALA A . n 
A 1 795  THR 795  795  795  THR THR A . n 
A 1 796  ASP 796  796  796  ASP ASP A . n 
A 1 797  ALA 797  797  797  ALA ALA A . n 
A 1 798  ALA 798  798  798  ALA ALA A . n 
A 1 799  ASP 799  799  799  ASP ASP A . n 
A 1 800  VAL 800  800  800  VAL VAL A . n 
A 1 801  LYS 801  801  801  LYS LYS A . n 
A 1 802  SER 802  802  802  SER SER A . n 
A 1 803  ALA 803  803  803  ALA ALA A . n 
A 1 804  ILE 804  804  804  ILE ILE A . n 
A 1 805  ALA 805  805  805  ALA ALA A . n 
A 1 806  GLU 806  806  806  GLU GLU A . n 
A 1 807  ARG 807  807  807  ARG ARG A . n 
A 1 808  ILE 808  808  808  ILE ILE A . n 
A 1 809  SER 809  809  809  SER SER A . n 
A 1 810  VAL 810  810  810  VAL VAL A . n 
A 1 811  ILE 811  811  811  ILE ILE A . n 
A 1 812  LEU 812  812  812  LEU LEU A . n 
A 1 813  GLN 813  813  813  GLN GLN A . n 
A 1 814  ASN 814  814  814  ASN ASN A . n 
A 1 815  MET 815  815  815  MET MET A . n 
A 1 816  THR 816  816  816  THR THR A . n 
A 1 817  SER 817  817  817  SER SER A . n 
A 1 818  LEU 818  818  818  LEU LEU A . n 
A 1 819  LEU 819  819  819  LEU LEU A . n 
A 1 820  THR 820  820  820  THR THR A . n 
A 1 821  SER 821  821  821  SER SER A . n 
A 1 822  PHE 822  822  822  PHE PHE A . n 
A 1 823  ILE 823  823  823  ILE ILE A . n 
A 1 824  VAL 824  824  824  VAL VAL A . n 
A 1 825  ALA 825  825  825  ALA ALA A . n 
A 1 826  PHE 826  826  826  PHE PHE A . n 
A 1 827  ILE 827  827  827  ILE ILE A . n 
A 1 828  VAL 828  828  828  VAL VAL A . n 
A 1 829  GLU 829  829  829  GLU GLU A . n 
A 1 830  TRP 830  830  830  TRP TRP A . n 
A 1 831  ARG 831  831  831  ARG ARG A . n 
A 1 832  VAL 832  832  832  VAL VAL A . n 
A 1 833  SER 833  833  833  SER SER A . n 
A 1 834  LEU 834  834  834  LEU LEU A . n 
A 1 835  LEU 835  835  835  LEU LEU A . n 
A 1 836  ILE 836  836  836  ILE ILE A . n 
A 1 837  LEU 837  837  837  LEU LEU A . n 
A 1 838  GLY 838  838  838  GLY GLY A . n 
A 1 839  THR 839  839  839  THR THR A . n 
A 1 840  PHE 840  840  840  PHE PHE A . n 
A 1 841  PRO 841  841  841  PRO PRO A . n 
A 1 842  LEU 842  842  842  LEU LEU A . n 
A 1 843  LEU 843  843  843  LEU LEU A . n 
A 1 844  VAL 844  844  844  VAL VAL A . n 
A 1 845  LEU 845  845  845  LEU LEU A . n 
A 1 846  ALA 846  846  846  ALA ALA A . n 
A 1 847  ASN 847  847  847  ASN ASN A . n 
A 1 848  PHE 848  848  848  PHE PHE A . n 
A 1 849  ALA 849  849  849  ALA ALA A . n 
A 1 850  GLN 850  850  850  GLN GLN A . n 
A 1 851  GLN 851  851  851  GLN GLN A . n 
A 1 852  LEU 852  852  852  LEU LEU A . n 
A 1 853  SER 853  853  853  SER SER A . n 
A 1 854  LEU 854  854  854  LEU LEU A . n 
A 1 855  LYS 855  855  855  LYS LYS A . n 
A 1 856  GLY 856  856  856  GLY GLY A . n 
A 1 857  PHE 857  857  857  PHE PHE A . n 
A 1 858  ALA 858  858  858  ALA ALA A . n 
A 1 859  GLY 859  859  859  GLY GLY A . n 
A 1 860  ASP 860  860  860  ASP ASP A . n 
A 1 861  THR 861  861  861  THR THR A . n 
A 1 862  ALA 862  862  862  ALA ALA A . n 
A 1 863  LYS 863  863  863  LYS LYS A . n 
A 1 864  ALA 864  864  864  ALA ALA A . n 
A 1 865  HIS 865  865  865  HIS HIS A . n 
A 1 866  ALA 866  866  866  ALA ALA A . n 
A 1 867  LYS 867  867  867  LYS LYS A . n 
A 1 868  THR 868  868  868  THR THR A . n 
A 1 869  SER 869  869  869  SER SER A . n 
A 1 870  MET 870  870  870  MET MET A . n 
A 1 871  ILE 871  871  871  ILE ILE A . n 
A 1 872  ALA 872  872  872  ALA ALA A . n 
A 1 873  GLY 873  873  873  GLY GLY A . n 
A 1 874  GLU 874  874  874  GLU GLU A . n 
A 1 875  GLY 875  875  875  GLY GLY A . n 
A 1 876  VAL 876  876  876  VAL VAL A . n 
A 1 877  SER 877  877  877  SER SER A . n 
A 1 878  ASN 878  878  878  ASN ASN A . n 
A 1 879  ILE 879  879  879  ILE ILE A . n 
A 1 880  ARG 880  880  880  ARG ARG A . n 
A 1 881  THR 881  881  881  THR THR A . n 
A 1 882  VAL 882  882  882  VAL VAL A . n 
A 1 883  ALA 883  883  883  ALA ALA A . n 
A 1 884  ALA 884  884  884  ALA ALA A . n 
A 1 885  PHE 885  885  885  PHE PHE A . n 
A 1 886  ASN 886  886  886  ASN ASN A . n 
A 1 887  ALA 887  887  887  ALA ALA A . n 
A 1 888  GLN 888  888  888  GLN GLN A . n 
A 1 889  SER 889  889  889  SER SER A . n 
A 1 890  LYS 890  890  890  LYS LYS A . n 
A 1 891  ILE 891  891  891  ILE ILE A . n 
A 1 892  LEU 892  892  892  LEU LEU A . n 
A 1 893  SER 893  893  893  SER SER A . n 
A 1 894  LEU 894  894  894  LEU LEU A . n 
A 1 895  PHE 895  895  895  PHE PHE A . n 
A 1 896  CYS 896  896  896  CYS CYS A . n 
A 1 897  HIS 897  897  897  HIS HIS A . n 
A 1 898  GLU 898  898  898  GLU GLU A . n 
A 1 899  LEU 899  899  899  LEU LEU A . n 
A 1 900  ARG 900  900  900  ARG ARG A . n 
A 1 901  VAL 901  901  901  VAL VAL A . n 
A 1 902  PRO 902  902  902  PRO PRO A . n 
A 1 903  GLN 903  903  903  GLN GLN A . n 
A 1 904  LYS 904  904  904  LYS LYS A . n 
A 1 905  ARG 905  905  905  ARG ARG A . n 
A 1 906  SER 906  906  906  SER SER A . n 
A 1 907  LEU 907  907  907  LEU LEU A . n 
A 1 908  TYR 908  908  908  TYR TYR A . n 
A 1 909  ARG 909  909  909  ARG ARG A . n 
A 1 910  SER 910  910  910  SER SER A . n 
A 1 911  GLN 911  911  911  GLN GLN A . n 
A 1 912  THR 912  912  912  THR THR A . n 
A 1 913  SER 913  913  913  SER SER A . n 
A 1 914  GLY 914  914  914  GLY GLY A . n 
A 1 915  PHE 915  915  915  PHE PHE A . n 
A 1 916  LEU 916  916  916  LEU LEU A . n 
A 1 917  PHE 917  917  917  PHE PHE A . n 
A 1 918  GLY 918  918  918  GLY GLY A . n 
A 1 919  LEU 919  919  919  LEU LEU A . n 
A 1 920  SER 920  920  920  SER SER A . n 
A 1 921  GLN 921  921  921  GLN GLN A . n 
A 1 922  LEU 922  922  922  LEU LEU A . n 
A 1 923  ALA 923  923  923  ALA ALA A . n 
A 1 924  LEU 924  924  924  LEU LEU A . n 
A 1 925  TYR 925  925  925  TYR TYR A . n 
A 1 926  GLY 926  926  926  GLY GLY A . n 
A 1 927  SER 927  927  927  SER SER A . n 
A 1 928  GLU 928  928  928  GLU GLU A . n 
A 1 929  ALA 929  929  929  ALA ALA A . n 
A 1 930  LEU 930  930  930  LEU LEU A . n 
A 1 931  ILE 931  931  931  ILE ILE A . n 
A 1 932  LEU 932  932  932  LEU LEU A . n 
A 1 933  TRP 933  933  933  TRP TRP A . n 
A 1 934  TYR 934  934  934  TYR TYR A . n 
A 1 935  GLY 935  935  935  GLY GLY A . n 
A 1 936  ALA 936  936  936  ALA ALA A . n 
A 1 937  HIS 937  937  937  HIS HIS A . n 
A 1 938  LEU 938  938  938  LEU LEU A . n 
A 1 939  VAL 939  939  939  VAL VAL A . n 
A 1 940  SER 940  940  940  SER SER A . n 
A 1 941  LYS 941  941  941  LYS LYS A . n 
A 1 942  GLY 942  942  942  GLY GLY A . n 
A 1 943  VAL 943  943  943  VAL VAL A . n 
A 1 944  SER 944  944  944  SER SER A . n 
A 1 945  THR 945  945  945  THR THR A . n 
A 1 946  PHE 946  946  946  PHE PHE A . n 
A 1 947  SER 947  947  947  SER SER A . n 
A 1 948  LYS 948  948  948  LYS LYS A . n 
A 1 949  VAL 949  949  949  VAL VAL A . n 
A 1 950  ILE 950  950  950  ILE ILE A . n 
A 1 951  LYS 951  951  951  LYS LYS A . n 
A 1 952  VAL 952  952  952  VAL VAL A . n 
A 1 953  PHE 953  953  953  PHE PHE A . n 
A 1 954  VAL 954  954  954  VAL VAL A . n 
A 1 955  VAL 955  955  955  VAL VAL A . n 
A 1 956  LEU 956  956  956  LEU LEU A . n 
A 1 957  VAL 957  957  957  VAL VAL A . n 
A 1 958  ILE 958  958  958  ILE ILE A . n 
A 1 959  THR 959  959  959  THR THR A . n 
A 1 960  ALA 960  960  960  ALA ALA A . n 
A 1 961  ASN 961  961  961  ASN ASN A . n 
A 1 962  SER 962  962  962  SER SER A . n 
A 1 963  VAL 963  963  963  VAL VAL A . n 
A 1 964  ALA 964  964  964  ALA ALA A . n 
A 1 965  GLU 965  965  965  GLU GLU A . n 
A 1 966  THR 966  966  966  THR THR A . n 
A 1 967  VAL 967  967  967  VAL VAL A . n 
A 1 968  SER 968  968  968  SER SER A . n 
A 1 969  LEU 969  969  969  LEU LEU A . n 
A 1 970  ALA 970  970  970  ALA ALA A . n 
A 1 971  PRO 971  971  971  PRO PRO A . n 
A 1 972  GLU 972  972  972  GLU GLU A . n 
A 1 973  ILE 973  973  973  ILE ILE A . n 
A 1 974  ILE 974  974  974  ILE ILE A . n 
A 1 975  ARG 975  975  975  ARG ARG A . n 
A 1 976  GLY 976  976  976  GLY GLY A . n 
A 1 977  GLY 977  977  977  GLY GLY A . n 
A 1 978  GLU 978  978  978  GLU GLU A . n 
A 1 979  ALA 979  979  979  ALA ALA A . n 
A 1 980  VAL 980  980  980  VAL VAL A . n 
A 1 981  GLY 981  981  981  GLY GLY A . n 
A 1 982  SER 982  982  982  SER SER A . n 
A 1 983  VAL 983  983  983  VAL VAL A . n 
A 1 984  PHE 984  984  984  PHE PHE A . n 
A 1 985  SER 985  985  985  SER SER A . n 
A 1 986  VAL 986  986  986  VAL VAL A . n 
A 1 987  LEU 987  987  987  LEU LEU A . n 
A 1 988  ASP 988  988  988  ASP ASP A . n 
A 1 989  ARG 989  989  989  ARG ARG A . n 
A 1 990  GLN 990  990  990  GLN GLN A . n 
A 1 991  THR 991  991  991  THR THR A . n 
A 1 992  ARG 992  992  992  ARG ARG A . n 
A 1 993  ILE 993  993  993  ILE ILE A . n 
A 1 994  ASP 994  994  994  ASP ASP A . n 
A 1 995  PRO 995  995  995  PRO PRO A . n 
A 1 996  ASP 996  996  996  ASP ASP A . n 
A 1 997  ASP 997  997  997  ASP ASP A . n 
A 1 998  ALA 998  998  998  ALA ALA A . n 
A 1 999  ASP 999  999  999  ASP ASP A . n 
A 1 1000 ALA 1000 1000 1000 ALA ALA A . n 
A 1 1001 ASP 1001 1001 1001 ASP ASP A . n 
A 1 1002 PRO 1002 1002 1002 PRO PRO A . n 
A 1 1003 VAL 1003 1003 1003 VAL VAL A . n 
A 1 1004 GLU 1004 1004 1004 GLU GLU A . n 
A 1 1005 THR 1005 1005 1005 THR THR A . n 
A 1 1006 ILE 1006 1006 1006 ILE ILE A . n 
A 1 1007 ARG 1007 1007 1007 ARG ARG A . n 
A 1 1008 GLY 1008 1008 1008 GLY GLY A . n 
A 1 1009 ASP 1009 1009 1009 ASP ASP A . n 
A 1 1010 ILE 1010 1010 1010 ILE ILE A . n 
A 1 1011 GLU 1011 1011 1011 GLU GLU A . n 
A 1 1012 PHE 1012 1012 1012 PHE PHE A . n 
A 1 1013 ARG 1013 1013 1013 ARG ARG A . n 
A 1 1014 HIS 1014 1014 1014 HIS HIS A . n 
A 1 1015 VAL 1015 1015 1015 VAL VAL A . n 
A 1 1016 ASP 1016 1016 1016 ASP ASP A . n 
A 1 1017 PHE 1017 1017 1017 PHE PHE A . n 
A 1 1018 ALA 1018 1018 1018 ALA ALA A . n 
A 1 1019 TYR 1019 1019 1019 TYR TYR A . n 
A 1 1020 PRO 1020 1020 1020 PRO PRO A . n 
A 1 1021 SER 1021 1021 1021 SER SER A . n 
A 1 1022 ARG 1022 1022 1022 ARG ARG A . n 
A 1 1023 PRO 1023 1023 1023 PRO PRO A . n 
A 1 1024 ASP 1024 1024 1024 ASP ASP A . n 
A 1 1025 VAL 1025 1025 1025 VAL VAL A . n 
A 1 1026 MET 1026 1026 1026 MET MET A . n 
A 1 1027 VAL 1027 1027 1027 VAL VAL A . n 
A 1 1028 PHE 1028 1028 1028 PHE PHE A . n 
A 1 1029 ARG 1029 1029 1029 ARG ARG A . n 
A 1 1030 ASP 1030 1030 1030 ASP ASP A . n 
A 1 1031 PHE 1031 1031 1031 PHE PHE A . n 
A 1 1032 ASN 1032 1032 1032 ASN ASN A . n 
A 1 1033 LEU 1033 1033 1033 LEU LEU A . n 
A 1 1034 ARG 1034 1034 1034 ARG ARG A . n 
A 1 1035 ILE 1035 1035 1035 ILE ILE A . n 
A 1 1036 ARG 1036 1036 1036 ARG ARG A . n 
A 1 1037 ALA 1037 1037 1037 ALA ALA A . n 
A 1 1038 GLY 1038 1038 1038 GLY GLY A . n 
A 1 1039 HIS 1039 1039 1039 HIS HIS A . n 
A 1 1040 SER 1040 1040 1040 SER SER A . n 
A 1 1041 GLN 1041 1041 1041 GLN GLN A . n 
A 1 1042 ALA 1042 1042 1042 ALA ALA A . n 
A 1 1043 LEU 1043 1043 1043 LEU LEU A . n 
A 1 1044 VAL 1044 1044 1044 VAL VAL A . n 
A 1 1045 GLY 1045 1045 1045 GLY GLY A . n 
A 1 1046 ALA 1046 1046 1046 ALA ALA A . n 
A 1 1047 SER 1047 1047 1047 SER SER A . n 
A 1 1048 GLY 1048 1048 1048 GLY GLY A . n 
A 1 1049 SER 1049 1049 1049 SER SER A . n 
A 1 1050 GLY 1050 1050 1050 GLY GLY A . n 
A 1 1051 LYS 1051 1051 1051 LYS LYS A . n 
A 1 1052 SER 1052 1052 1052 SER SER A . n 
A 1 1053 SER 1053 1053 1053 SER SER A . n 
A 1 1054 VAL 1054 1054 1054 VAL VAL A . n 
A 1 1055 ILE 1055 1055 1055 ILE ILE A . n 
A 1 1056 ALA 1056 1056 1056 ALA ALA A . n 
A 1 1057 MET 1057 1057 1057 MET MET A . n 
A 1 1058 ILE 1058 1058 1058 ILE ILE A . n 
A 1 1059 GLU 1059 1059 1059 GLU GLU A . n 
A 1 1060 ARG 1060 1060 1060 ARG ARG A . n 
A 1 1061 PHE 1061 1061 1061 PHE PHE A . n 
A 1 1062 TYR 1062 1062 1062 TYR TYR A . n 
A 1 1063 ASP 1063 1063 1063 ASP ASP A . n 
A 1 1064 PRO 1064 1064 1064 PRO PRO A . n 
A 1 1065 LEU 1065 1065 1065 LEU LEU A . n 
A 1 1066 ALA 1066 1066 1066 ALA ALA A . n 
A 1 1067 GLY 1067 1067 1067 GLY GLY A . n 
A 1 1068 LYS 1068 1068 1068 LYS LYS A . n 
A 1 1069 VAL 1069 1069 1069 VAL VAL A . n 
A 1 1070 MET 1070 1070 1070 MET MET A . n 
A 1 1071 ILE 1071 1071 1071 ILE ILE A . n 
A 1 1072 ASP 1072 1072 1072 ASP ASP A . n 
A 1 1073 GLY 1073 1073 1073 GLY GLY A . n 
A 1 1074 LYS 1074 1074 1074 LYS LYS A . n 
A 1 1075 ASP 1075 1075 1075 ASP ASP A . n 
A 1 1076 ILE 1076 1076 1076 ILE ILE A . n 
A 1 1077 ARG 1077 1077 1077 ARG ARG A . n 
A 1 1078 ARG 1078 1078 1078 ARG ARG A . n 
A 1 1079 LEU 1079 1079 1079 LEU LEU A . n 
A 1 1080 ASN 1080 1080 1080 ASN ASN A . n 
A 1 1081 LEU 1081 1081 1081 LEU LEU A . n 
A 1 1082 LYS 1082 1082 1082 LYS LYS A . n 
A 1 1083 SER 1083 1083 1083 SER SER A . n 
A 1 1084 LEU 1084 1084 1084 LEU LEU A . n 
A 1 1085 ARG 1085 1085 1085 ARG ARG A . n 
A 1 1086 LEU 1086 1086 1086 LEU LEU A . n 
A 1 1087 LYS 1087 1087 1087 LYS LYS A . n 
A 1 1088 ILE 1088 1088 1088 ILE ILE A . n 
A 1 1089 GLY 1089 1089 1089 GLY GLY A . n 
A 1 1090 LEU 1090 1090 1090 LEU LEU A . n 
A 1 1091 VAL 1091 1091 1091 VAL VAL A . n 
A 1 1092 GLN 1092 1092 1092 GLN GLN A . n 
A 1 1093 GLN 1093 1093 1093 GLN GLN A . n 
A 1 1094 GLU 1094 1094 1094 GLU GLU A . n 
A 1 1095 PRO 1095 1095 1095 PRO PRO A . n 
A 1 1096 ALA 1096 1096 1096 ALA ALA A . n 
A 1 1097 LEU 1097 1097 1097 LEU LEU A . n 
A 1 1098 PHE 1098 1098 1098 PHE PHE A . n 
A 1 1099 ALA 1099 1099 1099 ALA ALA A . n 
A 1 1100 ALA 1100 1100 1100 ALA ALA A . n 
A 1 1101 THR 1101 1101 1101 THR THR A . n 
A 1 1102 ILE 1102 1102 1102 ILE ILE A . n 
A 1 1103 PHE 1103 1103 1103 PHE PHE A . n 
A 1 1104 ASP 1104 1104 1104 ASP ASP A . n 
A 1 1105 ASN 1105 1105 1105 ASN ASN A . n 
A 1 1106 ILE 1106 1106 1106 ILE ILE A . n 
A 1 1107 ALA 1107 1107 1107 ALA ALA A . n 
A 1 1108 TYR 1108 1108 1108 TYR TYR A . n 
A 1 1109 GLY 1109 1109 1109 GLY GLY A . n 
A 1 1110 LYS 1110 1110 1110 LYS LYS A . n 
A 1 1111 ASP 1111 1111 1111 ASP ASP A . n 
A 1 1112 GLY 1112 1112 1112 GLY GLY A . n 
A 1 1113 ALA 1113 1113 1113 ALA ALA A . n 
A 1 1114 THR 1114 1114 1114 THR THR A . n 
A 1 1115 GLU 1115 1115 1115 GLU GLU A . n 
A 1 1116 SER 1116 1116 1116 SER SER A . n 
A 1 1117 GLU 1117 1117 1117 GLU GLU A . n 
A 1 1118 VAL 1118 1118 1118 VAL VAL A . n 
A 1 1119 ILE 1119 1119 1119 ILE ILE A . n 
A 1 1120 ASP 1120 1120 1120 ASP ASP A . n 
A 1 1121 ALA 1121 1121 1121 ALA ALA A . n 
A 1 1122 ALA 1122 1122 1122 ALA ALA A . n 
A 1 1123 ARG 1123 1123 1123 ARG ARG A . n 
A 1 1124 ALA 1124 1124 1124 ALA ALA A . n 
A 1 1125 ALA 1125 1125 1125 ALA ALA A . n 
A 1 1126 ASN 1126 1126 1126 ASN ASN A . n 
A 1 1127 ALA 1127 1127 1127 ALA ALA A . n 
A 1 1128 HIS 1128 1128 1128 HIS HIS A . n 
A 1 1129 GLY 1129 1129 1129 GLY GLY A . n 
A 1 1130 PHE 1130 1130 1130 PHE PHE A . n 
A 1 1131 ILE 1131 1131 1131 ILE ILE A . n 
A 1 1132 SER 1132 1132 1132 SER SER A . n 
A 1 1133 GLY 1133 1133 1133 GLY GLY A . n 
A 1 1134 LEU 1134 1134 1134 LEU LEU A . n 
A 1 1135 PRO 1135 1135 1135 PRO PRO A . n 
A 1 1136 GLU 1136 1136 1136 GLU GLU A . n 
A 1 1137 GLY 1137 1137 1137 GLY GLY A . n 
A 1 1138 TYR 1138 1138 1138 TYR TYR A . n 
A 1 1139 LYS 1139 1139 1139 LYS LYS A . n 
A 1 1140 THR 1140 1140 1140 THR THR A . n 
A 1 1141 PRO 1141 1141 1141 PRO PRO A . n 
A 1 1142 VAL 1142 1142 1142 VAL VAL A . n 
A 1 1143 GLY 1143 1143 1143 GLY GLY A . n 
A 1 1144 GLU 1144 1144 1144 GLU GLU A . n 
A 1 1145 ARG 1145 1145 1145 ARG ARG A . n 
A 1 1146 GLY 1146 1146 1146 GLY GLY A . n 
A 1 1147 VAL 1147 1147 1147 VAL VAL A . n 
A 1 1148 GLN 1148 1148 1148 GLN GLN A . n 
A 1 1149 LEU 1149 1149 1149 LEU LEU A . n 
A 1 1150 SER 1150 1150 1150 SER SER A . n 
A 1 1151 GLY 1151 1151 1151 GLY GLY A . n 
A 1 1152 GLY 1152 1152 1152 GLY GLY A . n 
A 1 1153 GLN 1153 1153 1153 GLN GLN A . n 
A 1 1154 LYS 1154 1154 1154 LYS LYS A . n 
A 1 1155 GLN 1155 1155 1155 GLN GLN A . n 
A 1 1156 ARG 1156 1156 1156 ARG ARG A . n 
A 1 1157 ILE 1157 1157 1157 ILE ILE A . n 
A 1 1158 ALA 1158 1158 1158 ALA ALA A . n 
A 1 1159 ILE 1159 1159 1159 ILE ILE A . n 
A 1 1160 ALA 1160 1160 1160 ALA ALA A . n 
A 1 1161 ARG 1161 1161 1161 ARG ARG A . n 
A 1 1162 ALA 1162 1162 1162 ALA ALA A . n 
A 1 1163 VAL 1163 1163 1163 VAL VAL A . n 
A 1 1164 LEU 1164 1164 1164 LEU LEU A . n 
A 1 1165 LYS 1165 1165 1165 LYS LYS A . n 
A 1 1166 ASN 1166 1166 1166 ASN ASN A . n 
A 1 1167 PRO 1167 1167 1167 PRO PRO A . n 
A 1 1168 THR 1168 1168 1168 THR THR A . n 
A 1 1169 VAL 1169 1169 1169 VAL VAL A . n 
A 1 1170 LEU 1170 1170 1170 LEU LEU A . n 
A 1 1171 LEU 1171 1171 1171 LEU LEU A . n 
A 1 1172 LEU 1172 1172 1172 LEU LEU A . n 
A 1 1173 ASP 1173 1173 1173 ASP ASP A . n 
A 1 1174 GLU 1174 1174 1174 GLU GLU A . n 
A 1 1175 ALA 1175 1175 1175 ALA ALA A . n 
A 1 1176 THR 1176 1176 1176 THR THR A . n 
A 1 1177 SER 1177 1177 1177 SER SER A . n 
A 1 1178 ALA 1178 1178 1178 ALA ALA A . n 
A 1 1179 LEU 1179 1179 1179 LEU LEU A . n 
A 1 1180 ASP 1180 1180 1180 ASP ASP A . n 
A 1 1181 ALA 1181 1181 1181 ALA ALA A . n 
A 1 1182 GLU 1182 1182 1182 GLU GLU A . n 
A 1 1183 SER 1183 1183 1183 SER SER A . n 
A 1 1184 GLU 1184 1184 1184 GLU GLU A . n 
A 1 1185 CYS 1185 1185 1185 CYS CYS A . n 
A 1 1186 VAL 1186 1186 1186 VAL VAL A . n 
A 1 1187 LEU 1187 1187 1187 LEU LEU A . n 
A 1 1188 GLN 1188 1188 1188 GLN GLN A . n 
A 1 1189 GLU 1189 1189 1189 GLU GLU A . n 
A 1 1190 ALA 1190 1190 1190 ALA ALA A . n 
A 1 1191 LEU 1191 1191 1191 LEU LEU A . n 
A 1 1192 GLU 1192 1192 1192 GLU GLU A . n 
A 1 1193 ARG 1193 1193 1193 ARG ARG A . n 
A 1 1194 LEU 1194 1194 1194 LEU LEU A . n 
A 1 1195 MET 1195 1195 1195 MET MET A . n 
A 1 1196 ARG 1196 1196 1196 ARG ARG A . n 
A 1 1197 GLY 1197 1197 1197 GLY GLY A . n 
A 1 1198 ARG 1198 1198 1198 ARG ARG A . n 
A 1 1199 THR 1199 1199 1199 THR THR A . n 
A 1 1200 THR 1200 1200 1200 THR THR A . n 
A 1 1201 VAL 1201 1201 1201 VAL VAL A . n 
A 1 1202 VAL 1202 1202 1202 VAL VAL A . n 
A 1 1203 VAL 1203 1203 1203 VAL VAL A . n 
A 1 1204 ALA 1204 1204 1204 ALA ALA A . n 
A 1 1205 HIS 1205 1205 1205 HIS HIS A . n 
A 1 1206 ARG 1206 1206 1206 ARG ARG A . n 
A 1 1207 LEU 1207 1207 1207 LEU LEU A . n 
A 1 1208 SER 1208 1208 1208 SER SER A . n 
A 1 1209 THR 1209 1209 1209 THR THR A . n 
A 1 1210 ILE 1210 1210 1210 ILE ILE A . n 
A 1 1211 ARG 1211 1211 1211 ARG ARG A . n 
A 1 1212 GLY 1212 1212 1212 GLY GLY A . n 
A 1 1213 VAL 1213 1213 1213 VAL VAL A . n 
A 1 1214 ASP 1214 1214 1214 ASP ASP A . n 
A 1 1215 CYS 1215 1215 1215 CYS CYS A . n 
A 1 1216 ILE 1216 1216 1216 ILE ILE A . n 
A 1 1217 GLY 1217 1217 1217 GLY GLY A . n 
A 1 1218 VAL 1218 1218 1218 VAL VAL A . n 
A 1 1219 ILE 1219 1219 1219 ILE ILE A . n 
A 1 1220 GLN 1220 1220 1220 GLN GLN A . n 
A 1 1221 ASP 1221 1221 1221 ASP ASP A . n 
A 1 1222 GLY 1222 1222 1222 GLY GLY A . n 
A 1 1223 ARG 1223 1223 1223 ARG ARG A . n 
A 1 1224 ILE 1224 1224 1224 ILE ILE A . n 
A 1 1225 VAL 1225 1225 1225 VAL VAL A . n 
A 1 1226 GLU 1226 1226 1226 GLU GLU A . n 
A 1 1227 GLN 1227 1227 1227 GLN GLN A . n 
A 1 1228 GLY 1228 1228 1228 GLY GLY A . n 
A 1 1229 SER 1229 1229 1229 SER SER A . n 
A 1 1230 HIS 1230 1230 1230 HIS HIS A . n 
A 1 1231 SER 1231 1231 1231 SER SER A . n 
A 1 1232 GLU 1232 1232 1232 GLU GLU A . n 
A 1 1233 LEU 1233 1233 1233 LEU LEU A . n 
A 1 1234 VAL 1234 1234 1234 VAL VAL A . n 
A 1 1235 SER 1235 1235 1235 SER SER A . n 
A 1 1236 ARG 1236 1236 1236 ARG ARG A . n 
A 1 1237 PRO 1237 1237 1237 PRO PRO A . n 
A 1 1238 GLU 1238 1238 1238 GLU GLU A . n 
A 1 1239 GLY 1239 1239 1239 GLY GLY A . n 
A 1 1240 ALA 1240 1240 1240 ALA ALA A . n 
A 1 1241 TYR 1241 1241 1241 TYR TYR A . n 
A 1 1242 SER 1242 1242 1242 SER SER A . n 
A 1 1243 ARG 1243 1243 1243 ARG ARG A . n 
A 1 1244 LEU 1244 1244 1244 LEU LEU A . n 
A 1 1245 LEU 1245 1245 1245 LEU LEU A . n 
A 1 1246 GLN 1246 1246 1246 GLN GLN A . n 
A 1 1247 LEU 1247 1247 1247 LEU LEU A . n 
A 1 1248 GLN 1248 1248 1248 GLN GLN A . n 
A 1 1249 THR 1249 1249 1249 THR THR A . n 
A 1 1250 HIS 1250 1250 1250 HIS HIS A . n 
A 1 1251 ARG 1251 1251 1251 ARG ARG A . n 
A 1 1252 ILE 1252 1252 1252 ILE ILE A . 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 ADP ? ? ADP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 MG  ? ? MG  ? ? 'SUBJECT OF INVESTIGATION' ? 
3 VO4 ? ? VO4 ? ? '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 
B 2 VO4 1 1301 601 VO4 VO4 A . 
C 3 ADP 1 1302 602 ADP ADP A . 
D 2 VO4 1 1303 601 VO4 VO4 A . 
E 3 ADP 1 1304 602 ADP ADP A . 
F 4 MG  1 1305 1   MG  MG  A . 
G 4 MG  1 1306 1   MG  MG  A . 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9KK6 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     1.00 
_cell.length_a_esd                 ? 
_cell.length_b                     1.00 
_cell.length_b_esd                 ? 
_cell.length_c                     1.00 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        ? 
_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                         9KK6 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 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                   9KK6 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 9KK6 
_refine.pdbx_diffrn_id                           ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             ? 
_refine.ls_d_res_high                            . 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
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 
'ELECTRON MICROSCOPY' ? 0.003  ? 9235  ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.598  ? 12509 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 27.439 ? 1293  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.041  ? 1438  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.003  ? 1584  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     9KK6 
_struct.title                        'Cryo-EM structure of vanadate-trapped atABCB19 in lipid nanodisc' 
_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        9KK6 
_struct_keywords.text            'ABCB19, Plant hormone transport, vandate-trapped, MEMBRANE PROTEIN' 
_struct_keywords.pdbx_keywords   'MEMBRANE PROTEIN' 
# 
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 2 ? 
C N N 3 ? 
D N N 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    AB19B_ARATH 
_struct_ref.pdbx_db_accession          Q9LJX0 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSETNTTDAKTVPAEAEKKKEQSLPFFKLFSFADKFDYLLMFVGSLGAIVHGSSMPVFFLLFGQMVNGFGKNQMDLHQMV
HEVSRYSLYFVYLGLVVCFSSYAEIACWMYSGERQVAALRKKYLEAVLKQDVGFFDTDARTGDIVFSVSTDTLLVQDAIS
EKVGNFIHYLSTFLAGLVVGFVSAWKLALLSVAVIPGIAFAGGLYAYTLTGITSKSRESYANAGVIAEQAIAQVRTVYSY
VGESKALNAYSDAIQYTLKLGYKAGMAKGLGLGCTYGIACMSWALVFWYAGVFIRNGQTDGGKAFTAIFSAIVGGMSLGQ
SFSNLGAFSKGKAAGYKLMEIINQRPTIIQDPLDGKCLDQVHGNIEFKDVTFSYPSRPDVMIFRNFNIFFPSGKTVAVVG
GSGSGKSTVVSLIERFYDPNSGQILLDGVEIKTLQLKFLREQIGLVNQEPALFATTILENILYGKPDATMVEVEAAASAA
NAHSFITLLPKGYDTQVGERGVQLSGGQKQRIAIARAMLKDPKILLLDEATSALDASSESIVQEALDRVMVGRTTVVVAH
RLCTIRNVDSIAVIQQGQVVETGTHEELIAKSGAYASLIRFQEMVGTRDFSNPSTRRTRSTRLSHSLSTKSLSLRSGSLR
NLSYSYSTGADGRIEMISNAETDRKTRAPENYFYRLLKLNSPEWPYSIMGAVGSILSGFIGPTFAIVMSNMIEVFYYTDY
DSMERKTKEYVFIYIGAGLYAVGAYLIQHYFFSIMGENLTTRVRRMMLSAILRNEVGWFDEDEHNSSLIAARLATDAADV
KSAIAERISVILQNMTSLLTSFIVAFIVEWRVSLLILGTFPLLVLANFAQQLSLKGFAGDTAKAHAKTSMIAGEGVSNIR
TVAAFNAQSKILSLFCHELRVPQKRSLYRSQTSGFLFGLSQLALYGSEALILWYGAHLVSKGVSTFSKVIKVFVVLVITA
NSVAETVSLAPEIIRGGEAVGSVFSVLDRQTRIDPDDADADPVETIRGDIEFRHVDFAYPSRPDVMVFRDFNLRIRAGHS
QALVGASGSGKSSVIAMIERFYDPLAGKVMIDGKDIRRLNLKSLRLKIGLVQQEPALFAATIFDNIAYGKDGATESEVID
AARAANAHGFISGLPEGYKTPVGERGVQLSGGQKQRIAIARAVLKNPTVLLLDEATSALDAESECVLQEALERLMRGRTT
VVVAHRLSTIRGVDCIGVIQDGRIVEQGSHSELVSRPEGAYSRLLQLQTHRI
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9KK6 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 1252 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q9LJX0 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1252 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       1252 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_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   ? 
_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 PRO A 25   ? PHE A 30   ? PRO A 25   PHE A 30   5 ? 6  
HELX_P HELX_P2  AA2 ASP A 34   ? ASN A 67   ? ASP A 34   ASN A 67   1 ? 34 
HELX_P HELX_P3  AA3 ASN A 67   ? ASN A 72   ? ASN A 67   ASN A 72   1 ? 6  
HELX_P HELX_P4  AA4 ASP A 75   ? LEU A 128  ? ASP A 75   LEU A 128  1 ? 54 
HELX_P HELX_P5  AA5 ASP A 131  ? ASP A 138  ? ASP A 131  ASP A 138  1 ? 8  
HELX_P HELX_P6  AA6 ARG A 140  ? ILE A 159  ? ARG A 140  ILE A 159  1 ? 20 
HELX_P HELX_P7  AA7 SER A 160  ? ALA A 184  ? SER A 160  ALA A 184  1 ? 25 
HELX_P HELX_P8  AA8 ALA A 184  ? VAL A 194  ? ALA A 184  VAL A 194  1 ? 11 
HELX_P HELX_P9  AA9 VAL A 194  ? GLN A 233  ? VAL A 194  GLN A 233  1 ? 40 
HELX_P HELX_P10 AB1 GLN A 233  ? TYR A 240  ? GLN A 233  TYR A 240  1 ? 8  
HELX_P HELX_P11 AB2 GLY A 242  ? ILE A 254  ? GLY A 242  ILE A 254  1 ? 13 
HELX_P HELX_P12 AB3 GLN A 255  ? GLY A 297  ? GLN A 255  GLY A 297  1 ? 43 
HELX_P HELX_P13 AB4 GLY A 301  ? GLN A 344  ? GLY A 301  GLN A 344  1 ? 44 
HELX_P HELX_P14 AB5 GLY A 405  ? GLU A 414  ? GLY A 405  GLU A 414  1 ? 10 
HELX_P HELX_P15 AB6 GLN A 435  ? GLN A 442  ? GLN A 435  GLN A 442  1 ? 8  
HELX_P HELX_P16 AB7 THR A 456  ? TYR A 463  ? THR A 456  TYR A 463  1 ? 8  
HELX_P HELX_P17 AB8 THR A 469  ? ALA A 480  ? THR A 469  ALA A 480  1 ? 12 
HELX_P HELX_P18 AB9 ALA A 482  ? LEU A 488  ? ALA A 482  LEU A 488  1 ? 7  
HELX_P HELX_P19 AC1 GLY A 498  ? VAL A 502  ? GLY A 498  VAL A 502  5 ? 5  
HELX_P HELX_P20 AC2 SER A 505  ? ASP A 521  ? SER A 505  ASP A 521  1 ? 17 
HELX_P HELX_P21 AC3 ALA A 536  ? MET A 550  ? ALA A 536  MET A 550  1 ? 15 
HELX_P HELX_P22 AC4 THR A 584  ? SER A 592  ? THR A 584  SER A 592  1 ? 9  
HELX_P HELX_P23 AC5 ALA A 594  ? THR A 607  ? ALA A 594  THR A 607  1 ? 14 
HELX_P HELX_P24 AC6 TYR A 672  ? LEU A 679  ? TYR A 672  LEU A 679  1 ? 8  
HELX_P HELX_P25 AC7 GLU A 683  ? THR A 718  ? GLU A 683  THR A 718  1 ? 36 
HELX_P HELX_P26 AC8 SER A 722  ? ASN A 774  ? SER A 722  ASN A 774  1 ? 53 
HELX_P HELX_P27 AC9 GLU A 775  ? ASP A 780  ? GLU A 775  ASP A 780  1 ? 6  
HELX_P HELX_P28 AD1 ASN A 785  ? GLU A 829  ? ASN A 785  GLU A 829  1 ? 45 
HELX_P HELX_P29 AD2 TRP A 830  ? GLY A 838  ? TRP A 830  GLY A 838  1 ? 9  
HELX_P HELX_P30 AD3 THR A 839  ? ASN A 878  ? THR A 839  ASN A 878  1 ? 40 
HELX_P HELX_P31 AD4 ASN A 878  ? PHE A 885  ? ASN A 878  PHE A 885  1 ? 8  
HELX_P HELX_P32 AD5 ALA A 887  ? GLY A 942  ? ALA A 887  GLY A 942  1 ? 56 
HELX_P HELX_P33 AD6 THR A 945  ? ALA A 964  ? THR A 945  ALA A 964  1 ? 20 
HELX_P HELX_P34 AD7 GLU A 965  ? ARG A 975  ? GLU A 965  ARG A 975  1 ? 11 
HELX_P HELX_P35 AD8 GLY A 976  ? ARG A 989  ? GLY A 976  ARG A 989  1 ? 14 
HELX_P HELX_P36 AD9 SER A 1052 ? GLU A 1059 ? SER A 1052 GLU A 1059 1 ? 8  
HELX_P HELX_P37 AE1 ASN A 1080 ? LYS A 1087 ? ASN A 1080 LYS A 1087 1 ? 8  
HELX_P HELX_P38 AE2 THR A 1101 ? ALA A 1107 ? THR A 1101 ALA A 1107 1 ? 7  
HELX_P HELX_P39 AE3 THR A 1114 ? ALA A 1125 ? THR A 1114 ALA A 1125 1 ? 12 
HELX_P HELX_P40 AE4 ALA A 1127 ? LEU A 1134 ? ALA A 1127 LEU A 1134 1 ? 8  
HELX_P HELX_P41 AE5 GLU A 1136 ? THR A 1140 ? GLU A 1136 THR A 1140 5 ? 5  
HELX_P HELX_P42 AE6 SER A 1150 ? ASN A 1166 ? SER A 1150 ASN A 1166 1 ? 17 
HELX_P HELX_P43 AE7 SER A 1183 ? MET A 1195 ? SER A 1183 MET A 1195 1 ? 13 
HELX_P HELX_P44 AE8 ARG A 1196 ? ARG A 1198 ? ARG A 1196 ARG A 1198 5 ? 3  
HELX_P HELX_P45 AE9 SER A 1229 ? ARG A 1236 ? SER A 1229 ARG A 1236 1 ? 8  
HELX_P HELX_P46 AF1 GLY A 1239 ? ILE A 1252 ? GLY A 1239 ILE A 1252 1 ? 14 
# 
_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 ? ? A SER 407  OG  ? ? ? 1_555 F MG  . MG  ? ? A SER 407  A MG  1305 1_555 ? ? ? ? ? ? ? 2.031 ? ? 
metalc2  metalc ? ? A GLN 448  OE1 ? ? ? 1_555 F MG  . MG  ? ? A GLN 448  A MG  1305 1_555 ? ? ? ? ? ? ? 2.169 ? ? 
metalc3  metalc ? ? A GLU 529  OE1 ? ? ? 1_555 F MG  . MG  ? ? A GLU 529  A MG  1305 1_555 ? ? ? ? ? ? ? 2.816 ? ? 
metalc4  metalc ? ? A SER 1052 OG  ? ? ? 1_555 G MG  . MG  ? ? A SER 1052 A MG  1306 1_555 ? ? ? ? ? ? ? 2.218 ? ? 
metalc5  metalc ? ? A GLN 1093 OE1 ? ? ? 1_555 G MG  . MG  ? ? A GLN 1093 A MG  1306 1_555 ? ? ? ? ? ? ? 2.367 ? ? 
metalc6  metalc ? ? A GLN 1093 NE2 ? ? ? 1_555 G MG  . MG  ? ? A GLN 1093 A MG  1306 1_555 ? ? ? ? ? ? ? 2.898 ? ? 
metalc7  metalc ? ? B VO4 .    V   ? ? ? 1_555 C ADP . O3B ? ? A VO4 1301 A ADP 1302 1_555 ? ? ? ? ? ? ? 2.782 ? ? 
metalc8  metalc ? ? B VO4 .    O3  ? ? ? 1_555 F MG  . MG  ? ? A VO4 1301 A MG  1305 1_555 ? ? ? ? ? ? ? 2.098 ? ? 
metalc9  metalc ? ? C ADP .    O1B ? ? ? 1_555 F MG  . MG  ? ? A ADP 1302 A MG  1305 1_555 ? ? ? ? ? ? ? 2.726 ? ? 
metalc10 metalc ? ? D VO4 .    V   ? ? ? 1_555 E ADP . O3B ? ? A VO4 1303 A ADP 1304 1_555 ? ? ? ? ? ? ? 2.781 ? ? 
metalc11 metalc ? ? D VO4 .    O3  ? ? ? 1_555 G MG  . MG  ? ? A VO4 1303 A MG  1306 1_555 ? ? ? ? ? ? ? 2.111 ? ? 
# 
_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  OG  ? A SER 407  ? A SER 407  ? 1_555 MG ? F MG  . ? A MG  1305 ? 1_555 OE1 ? A GLN 448  ? A GLN 448  ? 1_555 133.0 ? 
2  OG  ? A SER 407  ? A SER 407  ? 1_555 MG ? F MG  . ? A MG  1305 ? 1_555 OE1 ? A GLU 529  ? A GLU 529  ? 1_555 79.4  ? 
3  OE1 ? A GLN 448  ? A GLN 448  ? 1_555 MG ? F MG  . ? A MG  1305 ? 1_555 OE1 ? A GLU 529  ? A GLU 529  ? 1_555 70.5  ? 
4  OG  ? A SER 407  ? A SER 407  ? 1_555 MG ? F MG  . ? A MG  1305 ? 1_555 O3  ? B VO4 .    ? A VO4 1301 ? 1_555 120.3 ? 
5  OE1 ? A GLN 448  ? A GLN 448  ? 1_555 MG ? F MG  . ? A MG  1305 ? 1_555 O3  ? B VO4 .    ? A VO4 1301 ? 1_555 87.4  ? 
6  OE1 ? A GLU 529  ? A GLU 529  ? 1_555 MG ? F MG  . ? A MG  1305 ? 1_555 O3  ? B VO4 .    ? A VO4 1301 ? 1_555 76.8  ? 
7  OG  ? A SER 407  ? A SER 407  ? 1_555 MG ? F MG  . ? A MG  1305 ? 1_555 O1B ? C ADP .    ? A ADP 1302 ? 1_555 70.3  ? 
8  OE1 ? A GLN 448  ? A GLN 448  ? 1_555 MG ? F MG  . ? A MG  1305 ? 1_555 O1B ? C ADP .    ? A ADP 1302 ? 1_555 156.0 ? 
9  OE1 ? A GLU 529  ? A GLU 529  ? 1_555 MG ? F MG  . ? A MG  1305 ? 1_555 O1B ? C ADP .    ? A ADP 1302 ? 1_555 116.1 ? 
10 O3  ? B VO4 .    ? A VO4 1301 ? 1_555 MG ? F MG  . ? A MG  1305 ? 1_555 O1B ? C ADP .    ? A ADP 1302 ? 1_555 72.8  ? 
11 OG  ? A SER 1052 ? A SER 1052 ? 1_555 MG ? G MG  . ? A MG  1306 ? 1_555 OE1 ? A GLN 1093 ? A GLN 1093 ? 1_555 121.1 ? 
12 OG  ? A SER 1052 ? A SER 1052 ? 1_555 MG ? G MG  . ? A MG  1306 ? 1_555 NE2 ? A GLN 1093 ? A GLN 1093 ? 1_555 123.3 ? 
13 OE1 ? A GLN 1093 ? A GLN 1093 ? 1_555 MG ? G MG  . ? A MG  1306 ? 1_555 NE2 ? A GLN 1093 ? A GLN 1093 ? 1_555 49.2  ? 
14 OG  ? A SER 1052 ? A SER 1052 ? 1_555 MG ? G MG  . ? A MG  1306 ? 1_555 O3  ? D VO4 .    ? A VO4 1303 ? 1_555 92.7  ? 
15 OE1 ? A GLN 1093 ? A GLN 1093 ? 1_555 MG ? G MG  . ? A MG  1306 ? 1_555 O3  ? D VO4 .    ? A VO4 1303 ? 1_555 99.0  ? 
16 NE2 ? A GLN 1093 ? A GLN 1093 ? 1_555 MG ? G MG  . ? A MG  1306 ? 1_555 O3  ? D VO4 .    ? A VO4 1303 ? 1_555 139.8 ? 
17 O3B ? C ADP .    ? A ADP 1302 ? 1_555 V  ? B VO4 . ? A VO4 1301 ? 1_555 O1  ? B VO4 .    ? A VO4 1301 ? 1_555 70.8  ? 
18 O3B ? C ADP .    ? A ADP 1302 ? 1_555 V  ? B VO4 . ? A VO4 1301 ? 1_555 O2  ? B VO4 .    ? A VO4 1301 ? 1_555 179.4 ? 
19 O1  ? B VO4 .    ? A VO4 1301 ? 1_555 V  ? B VO4 . ? A VO4 1301 ? 1_555 O2  ? B VO4 .    ? A VO4 1301 ? 1_555 109.1 ? 
20 O3B ? C ADP .    ? A ADP 1302 ? 1_555 V  ? B VO4 . ? A VO4 1301 ? 1_555 O3  ? B VO4 .    ? A VO4 1301 ? 1_555 71.3  ? 
21 O1  ? B VO4 .    ? A VO4 1301 ? 1_555 V  ? B VO4 . ? A VO4 1301 ? 1_555 O3  ? B VO4 .    ? A VO4 1301 ? 1_555 109.7 ? 
22 O2  ? B VO4 .    ? A VO4 1301 ? 1_555 V  ? B VO4 . ? A VO4 1301 ? 1_555 O3  ? B VO4 .    ? A VO4 1301 ? 1_555 109.2 ? 
23 O3B ? C ADP .    ? A ADP 1302 ? 1_555 V  ? B VO4 . ? A VO4 1301 ? 1_555 O4  ? B VO4 .    ? A VO4 1301 ? 1_555 69.8  ? 
24 O1  ? B VO4 .    ? A VO4 1301 ? 1_555 V  ? B VO4 . ? A VO4 1301 ? 1_555 O4  ? B VO4 .    ? A VO4 1301 ? 1_555 109.5 ? 
25 O2  ? B VO4 .    ? A VO4 1301 ? 1_555 V  ? B VO4 . ? A VO4 1301 ? 1_555 O4  ? B VO4 .    ? A VO4 1301 ? 1_555 109.7 ? 
26 O3  ? B VO4 .    ? A VO4 1301 ? 1_555 V  ? B VO4 . ? A VO4 1301 ? 1_555 O4  ? B VO4 .    ? A VO4 1301 ? 1_555 109.6 ? 
27 O3B ? E ADP .    ? A ADP 1304 ? 1_555 V  ? D VO4 . ? A VO4 1303 ? 1_555 O1  ? D VO4 .    ? A VO4 1303 ? 1_555 70.8  ? 
28 O3B ? E ADP .    ? A ADP 1304 ? 1_555 V  ? D VO4 . ? A VO4 1303 ? 1_555 O2  ? D VO4 .    ? A VO4 1303 ? 1_555 179.4 ? 
29 O1  ? D VO4 .    ? A VO4 1303 ? 1_555 V  ? D VO4 . ? A VO4 1303 ? 1_555 O2  ? D VO4 .    ? A VO4 1303 ? 1_555 109.2 ? 
30 O3B ? E ADP .    ? A ADP 1304 ? 1_555 V  ? D VO4 . ? A VO4 1303 ? 1_555 O3  ? D VO4 .    ? A VO4 1303 ? 1_555 71.3  ? 
31 O1  ? D VO4 .    ? A VO4 1303 ? 1_555 V  ? D VO4 . ? A VO4 1303 ? 1_555 O3  ? D VO4 .    ? A VO4 1303 ? 1_555 109.7 ? 
32 O2  ? D VO4 .    ? A VO4 1303 ? 1_555 V  ? D VO4 . ? A VO4 1303 ? 1_555 O3  ? D VO4 .    ? A VO4 1303 ? 1_555 109.2 ? 
33 O3B ? E ADP .    ? A ADP 1304 ? 1_555 V  ? D VO4 . ? A VO4 1303 ? 1_555 O4  ? D VO4 .    ? A VO4 1303 ? 1_555 69.8  ? 
34 O1  ? D VO4 .    ? A VO4 1303 ? 1_555 V  ? D VO4 . ? A VO4 1303 ? 1_555 O4  ? D VO4 .    ? A VO4 1303 ? 1_555 109.5 ? 
35 O2  ? D VO4 .    ? A VO4 1303 ? 1_555 V  ? D VO4 . ? A VO4 1303 ? 1_555 O4  ? D VO4 .    ? A VO4 1303 ? 1_555 109.6 ? 
36 O3  ? D VO4 .    ? A VO4 1303 ? 1_555 V  ? D VO4 . ? A VO4 1303 ? 1_555 O4  ? D VO4 .    ? A VO4 1303 ? 1_555 109.6 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 6 ? 
AA3 ? 3 ? 
AA4 ? 3 ? 
AA5 ? 3 ? 
# 
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 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? 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 383  ? PHE A 390  ? PHE A 383  PHE A 390  
AA1 2 ILE A 365  ? PHE A 372  ? ILE A 365  PHE A 372  
AA1 3 SER A 421  ? LEU A 426  ? SER A 421  LEU A 426  
AA2 1 ILE A 443  ? VAL A 446  ? ILE A 443  VAL A 446  
AA2 2 ILE A 524  ? LEU A 527  ? ILE A 524  LEU A 527  
AA2 3 THR A 554  ? VAL A 558  ? THR A 554  VAL A 558  
AA2 4 THR A 395  ? VAL A 399  ? THR A 395  VAL A 399  
AA2 5 SER A 570  ? ILE A 574  ? SER A 570  ILE A 574  
AA2 6 VAL A 579  ? GLY A 583  ? VAL A 579  GLY A 583  
AA3 1 PHE A 1028 ? PHE A 1031 ? PHE A 1028 PHE A 1031 
AA3 2 ILE A 1010 ? PHE A 1017 ? ILE A 1010 PHE A 1017 
AA3 3 ARG A 1034 ? ILE A 1035 ? ARG A 1034 ILE A 1035 
AA4 1 PHE A 1028 ? PHE A 1031 ? PHE A 1028 PHE A 1031 
AA4 2 ILE A 1010 ? PHE A 1017 ? ILE A 1010 PHE A 1017 
AA4 3 ALA A 1066 ? MET A 1070 ? ALA A 1066 MET A 1070 
AA5 1 ILE A 1088 ? LEU A 1090 ? ILE A 1088 LEU A 1090 
AA5 2 VAL A 1169 ? LEU A 1171 ? VAL A 1169 LEU A 1171 
AA5 3 THR A 1199 ? THR A 1200 ? THR A 1199 THR A 1200 
# 
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 O ILE A 388  ? O ILE A 388  N PHE A 367  ? N PHE A 367  
AA1 2 3 N GLU A 366  ? N GLU A 366  O LEU A 425  ? O LEU A 425  
AA2 1 2 N GLY A 444  ? N GLY A 444  O ILE A 524  ? O ILE A 524  
AA2 2 3 N LEU A 527  ? N LEU A 527  O VAL A 558  ? O VAL A 558  
AA2 3 4 O VAL A 557  ? O VAL A 557  N VAL A 398  ? N VAL A 398  
AA2 4 5 N VAL A 399  ? N VAL A 399  O ILE A 574  ? O ILE A 574  
AA2 5 6 N ILE A 571  ? N ILE A 571  O GLY A 583  ? O GLY A 583  
AA3 1 2 O PHE A 1028 ? O PHE A 1028 N PHE A 1017 ? N PHE A 1017 
AA3 2 3 N ILE A 1010 ? N ILE A 1010 O ILE A 1035 ? O ILE A 1035 
AA4 1 2 O PHE A 1028 ? O PHE A 1028 N PHE A 1017 ? N PHE A 1017 
AA4 2 3 N GLU A 1011 ? N GLU A 1011 O MET A 1070 ? O MET A 1070 
AA5 1 2 N GLY A 1089 ? N GLY A 1089 O LEU A 1171 ? O LEU A 1171 
AA5 2 3 N LEU A 1170 ? N LEU A 1170 O THR A 1199 ? O THR A 1199 
# 
_pdbx_entry_details.entry_id                   9KK6 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_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 ASN A 72   ? ? -142.74 18.02   
2  1 ALA A 139  ? ? -171.24 136.80  
3  1 PRO A 346  ? ? -68.20  -179.25 
4  1 ILE A 349  ? ? -123.04 -62.40  
5  1 GLN A 350  ? ? 48.96   20.96   
6  1 LEU A 353  ? ? -120.03 -61.18  
7  1 GLN A 360  ? ? -97.00  33.17   
8  1 ASP A 369  ? ? 38.58   48.54   
9  1 GLU A 414  ? ? -85.04  46.01   
10 1 ARG A 415  ? ? 35.34   46.50   
11 1 LEU A 426  ? ? -94.54  48.90   
12 1 ASP A 427  ? ? 70.57   -12.58  
13 1 ASP A 521  ? ? 53.08   70.73   
14 1 ASP A 528  ? ? -79.37  -164.61 
15 1 ASP A 535  ? ? -66.61  -72.52  
16 1 ALA A 536  ? ? -136.03 -39.78  
17 1 ASP A 547  ? ? -85.19  42.12   
18 1 GLN A 575  ? ? -125.62 -169.80 
19 1 SER A 592  ? ? 71.76   -13.08  
20 1 ASN A 680  ? ? -99.23  35.19   
21 1 GLU A 683  ? ? -96.25  58.40   
22 1 THR A 718  ? ? 73.38   -13.71  
23 1 ASP A 719  ? ? 32.89   57.98   
24 1 TYR A 720  ? ? -81.77  46.93   
25 1 ASP A 721  ? ? -125.60 -50.95  
26 1 SER A 722  ? ? -140.39 23.81   
27 1 ALA A 887  ? ? -140.93 21.15   
28 1 SER A 944  ? ? 62.87   64.14   
29 1 THR A 945  ? ? -78.67  -165.04 
30 1 ASP A 997  ? ? 68.00   -6.64   
31 1 ALA A 998  ? ? 66.22   -7.06   
32 1 ASP A 1001 ? ? 47.78   74.32   
33 1 PRO A 1023 ? ? -77.60  44.02   
34 1 GLU A 1136 ? ? -92.78  49.47   
35 1 TYR A 1138 ? ? -91.95  49.69   
36 1 VAL A 1142 ? ? -97.20  -62.25  
37 1 ARG A 1145 ? ? 68.51   -3.37   
38 1 THR A 1176 ? ? -90.12  59.91   
39 1 ASP A 1214 ? ? -120.98 -68.55  
40 1 CYS A 1215 ? ? -149.07 49.08   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9KK6 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         ? 
_em_3d_fitting.ref_protocol      ? 
# 
_em_3d_reconstruction.entry_id                    9KK6 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  3.7 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               58202 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       '20mM Tris-HCl,pH 7.8, 150mM NaCl' 
_em_buffer.pH            7.8 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'vanadate-trapped atABCB19 in lipid nanodisc' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        9KK6 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'TFS KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           ? 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             1000 
_em_imaging.nominal_defocus_max             2000 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           ? 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         ? 
# 
_em_sample_support.id               1 
_em_sample_support.film_material    ? 
_em_sample_support.method           ? 
_em_sample_support.grid_material    ? 
_em_sample_support.grid_mesh_size   ? 
_em_sample_support.grid_type        Quantifoil 
_em_sample_support.details          ? 
_em_sample_support.specimen_id      1 
_em_sample_support.citation_id      ? 
# 
_em_vitrification.entry_id              9KK6 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              100 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   277 
_em_vitrification.instrument            'FEI VITROBOT MARK IV' 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9KK6 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
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 MET 1   ? A MET 1   
2  1 Y 1 A SER 2   ? A SER 2   
3  1 Y 1 A GLU 3   ? A GLU 3   
4  1 Y 1 A THR 4   ? A THR 4   
5  1 Y 1 A ASN 5   ? A ASN 5   
6  1 Y 1 A THR 6   ? A THR 6   
7  1 Y 1 A THR 7   ? A THR 7   
8  1 Y 1 A ASP 8   ? A ASP 8   
9  1 Y 1 A ALA 9   ? A ALA 9   
10 1 Y 1 A LYS 10  ? A LYS 10  
11 1 Y 1 A THR 11  ? A THR 11  
12 1 Y 1 A VAL 12  ? A VAL 12  
13 1 Y 1 A PRO 13  ? A PRO 13  
14 1 Y 1 A ALA 14  ? A ALA 14  
15 1 Y 1 A GLU 15  ? A GLU 15  
16 1 Y 1 A ALA 16  ? A ALA 16  
17 1 Y 1 A GLU 17  ? A GLU 17  
18 1 Y 1 A LYS 18  ? A LYS 18  
19 1 Y 1 A LYS 19  ? A LYS 19  
20 1 Y 1 A LYS 20  ? A LYS 20  
21 1 Y 1 A ARG 608 ? A ARG 608 
22 1 Y 1 A ASP 609 ? A ASP 609 
23 1 Y 1 A PHE 610 ? A PHE 610 
24 1 Y 1 A SER 611 ? A SER 611 
25 1 Y 1 A ASN 612 ? A ASN 612 
26 1 Y 1 A PRO 613 ? A PRO 613 
27 1 Y 1 A SER 614 ? A SER 614 
28 1 Y 1 A THR 615 ? A THR 615 
29 1 Y 1 A ARG 616 ? A ARG 616 
30 1 Y 1 A ARG 617 ? A ARG 617 
31 1 Y 1 A THR 618 ? A THR 618 
32 1 Y 1 A ARG 619 ? A ARG 619 
33 1 Y 1 A SER 620 ? A SER 620 
34 1 Y 1 A THR 621 ? A THR 621 
35 1 Y 1 A ARG 622 ? A ARG 622 
36 1 Y 1 A LEU 623 ? A LEU 623 
37 1 Y 1 A SER 624 ? A SER 624 
38 1 Y 1 A HIS 625 ? A HIS 625 
39 1 Y 1 A SER 626 ? A SER 626 
40 1 Y 1 A LEU 627 ? A LEU 627 
41 1 Y 1 A SER 628 ? A SER 628 
42 1 Y 1 A THR 629 ? A THR 629 
43 1 Y 1 A LYS 630 ? A LYS 630 
44 1 Y 1 A SER 631 ? A SER 631 
45 1 Y 1 A LEU 632 ? A LEU 632 
46 1 Y 1 A SER 633 ? A SER 633 
47 1 Y 1 A LEU 634 ? A LEU 634 
48 1 Y 1 A ARG 635 ? A ARG 635 
49 1 Y 1 A SER 636 ? A SER 636 
50 1 Y 1 A GLY 637 ? A GLY 637 
51 1 Y 1 A SER 638 ? A SER 638 
52 1 Y 1 A LEU 639 ? A LEU 639 
53 1 Y 1 A ARG 640 ? A ARG 640 
54 1 Y 1 A ASN 641 ? A ASN 641 
55 1 Y 1 A LEU 642 ? A LEU 642 
56 1 Y 1 A SER 643 ? A SER 643 
57 1 Y 1 A TYR 644 ? A TYR 644 
58 1 Y 1 A SER 645 ? A SER 645 
59 1 Y 1 A TYR 646 ? A TYR 646 
60 1 Y 1 A SER 647 ? A SER 647 
61 1 Y 1 A THR 648 ? A THR 648 
62 1 Y 1 A GLY 649 ? A GLY 649 
63 1 Y 1 A ALA 650 ? A ALA 650 
64 1 Y 1 A ASP 651 ? A ASP 651 
65 1 Y 1 A GLY 652 ? A GLY 652 
66 1 Y 1 A ARG 653 ? A ARG 653 
67 1 Y 1 A ILE 654 ? A ILE 654 
68 1 Y 1 A GLU 655 ? A GLU 655 
69 1 Y 1 A MET 656 ? A MET 656 
70 1 Y 1 A ILE 657 ? A ILE 657 
71 1 Y 1 A SER 658 ? A SER 658 
72 1 Y 1 A ASN 659 ? A ASN 659 
73 1 Y 1 A ALA 660 ? A ALA 660 
74 1 Y 1 A GLU 661 ? A GLU 661 
75 1 Y 1 A THR 662 ? A THR 662 
76 1 Y 1 A ASP 663 ? A ASP 663 
77 1 Y 1 A ARG 664 ? A ARG 664 
78 1 Y 1 A LYS 665 ? A LYS 665 
79 1 Y 1 A THR 666 ? A THR 666 
80 1 Y 1 A ARG 667 ? A ARG 667 
81 1 Y 1 A ALA 668 ? A ALA 668 
82 1 Y 1 A PRO 669 ? A PRO 669 
# 
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 
ADP PB     P  N N 1   
ADP O1B    O  N N 2   
ADP O2B    O  N N 3   
ADP O3B    O  N N 4   
ADP PA     P  N S 5   
ADP O1A    O  N N 6   
ADP O2A    O  N N 7   
ADP O3A    O  N N 8   
ADP "O5'"  O  N N 9   
ADP "C5'"  C  N N 10  
ADP "C4'"  C  N R 11  
ADP "O4'"  O  N N 12  
ADP "C3'"  C  N S 13  
ADP "O3'"  O  N N 14  
ADP "C2'"  C  N R 15  
ADP "O2'"  O  N N 16  
ADP "C1'"  C  N R 17  
ADP N9     N  Y N 18  
ADP C8     C  Y N 19  
ADP N7     N  Y N 20  
ADP C5     C  Y N 21  
ADP C6     C  Y N 22  
ADP N6     N  N N 23  
ADP N1     N  Y N 24  
ADP C2     C  Y N 25  
ADP N3     N  Y N 26  
ADP C4     C  Y N 27  
ADP HOB2   H  N N 28  
ADP HOB3   H  N N 29  
ADP HOA2   H  N N 30  
ADP "H5'1" H  N N 31  
ADP "H5'2" H  N N 32  
ADP "H4'"  H  N N 33  
ADP "H3'"  H  N N 34  
ADP "HO3'" H  N N 35  
ADP "H2'"  H  N N 36  
ADP "HO2'" H  N N 37  
ADP "H1'"  H  N N 38  
ADP H8     H  N N 39  
ADP HN61   H  N N 40  
ADP HN62   H  N N 41  
ADP H2     H  N N 42  
ALA N      N  N N 43  
ALA CA     C  N S 44  
ALA C      C  N N 45  
ALA O      O  N N 46  
ALA CB     C  N N 47  
ALA OXT    O  N N 48  
ALA H      H  N N 49  
ALA H2     H  N N 50  
ALA HA     H  N N 51  
ALA HB1    H  N N 52  
ALA HB2    H  N N 53  
ALA HB3    H  N N 54  
ALA HXT    H  N N 55  
ARG N      N  N N 56  
ARG CA     C  N S 57  
ARG C      C  N N 58  
ARG O      O  N N 59  
ARG CB     C  N N 60  
ARG CG     C  N N 61  
ARG CD     C  N N 62  
ARG NE     N  N N 63  
ARG CZ     C  N N 64  
ARG NH1    N  N N 65  
ARG NH2    N  N N 66  
ARG OXT    O  N N 67  
ARG H      H  N N 68  
ARG H2     H  N N 69  
ARG HA     H  N N 70  
ARG HB2    H  N N 71  
ARG HB3    H  N N 72  
ARG HG2    H  N N 73  
ARG HG3    H  N N 74  
ARG HD2    H  N N 75  
ARG HD3    H  N N 76  
ARG HE     H  N N 77  
ARG HH11   H  N N 78  
ARG HH12   H  N N 79  
ARG HH21   H  N N 80  
ARG HH22   H  N N 81  
ARG HXT    H  N N 82  
ASN N      N  N N 83  
ASN CA     C  N S 84  
ASN C      C  N N 85  
ASN O      O  N N 86  
ASN CB     C  N N 87  
ASN CG     C  N N 88  
ASN OD1    O  N N 89  
ASN ND2    N  N N 90  
ASN OXT    O  N N 91  
ASN H      H  N N 92  
ASN H2     H  N N 93  
ASN HA     H  N N 94  
ASN HB2    H  N N 95  
ASN HB3    H  N N 96  
ASN HD21   H  N N 97  
ASN HD22   H  N N 98  
ASN HXT    H  N N 99  
ASP N      N  N N 100 
ASP CA     C  N S 101 
ASP C      C  N N 102 
ASP O      O  N N 103 
ASP CB     C  N N 104 
ASP CG     C  N N 105 
ASP OD1    O  N N 106 
ASP OD2    O  N N 107 
ASP OXT    O  N N 108 
ASP H      H  N N 109 
ASP H2     H  N N 110 
ASP HA     H  N N 111 
ASP HB2    H  N N 112 
ASP HB3    H  N N 113 
ASP HD2    H  N N 114 
ASP HXT    H  N N 115 
CYS N      N  N N 116 
CYS CA     C  N R 117 
CYS C      C  N N 118 
CYS O      O  N N 119 
CYS CB     C  N N 120 
CYS SG     S  N N 121 
CYS OXT    O  N N 122 
CYS H      H  N N 123 
CYS H2     H  N N 124 
CYS HA     H  N N 125 
CYS HB2    H  N N 126 
CYS HB3    H  N N 127 
CYS HG     H  N N 128 
CYS HXT    H  N N 129 
GLN N      N  N N 130 
GLN CA     C  N S 131 
GLN C      C  N N 132 
GLN O      O  N N 133 
GLN CB     C  N N 134 
GLN CG     C  N N 135 
GLN CD     C  N N 136 
GLN OE1    O  N N 137 
GLN NE2    N  N N 138 
GLN OXT    O  N N 139 
GLN H      H  N N 140 
GLN H2     H  N N 141 
GLN HA     H  N N 142 
GLN HB2    H  N N 143 
GLN HB3    H  N N 144 
GLN HG2    H  N N 145 
GLN HG3    H  N N 146 
GLN HE21   H  N N 147 
GLN HE22   H  N N 148 
GLN HXT    H  N N 149 
GLU N      N  N N 150 
GLU CA     C  N S 151 
GLU C      C  N N 152 
GLU O      O  N N 153 
GLU CB     C  N N 154 
GLU CG     C  N N 155 
GLU CD     C  N N 156 
GLU OE1    O  N N 157 
GLU OE2    O  N N 158 
GLU OXT    O  N N 159 
GLU H      H  N N 160 
GLU H2     H  N N 161 
GLU HA     H  N N 162 
GLU HB2    H  N N 163 
GLU HB3    H  N N 164 
GLU HG2    H  N N 165 
GLU HG3    H  N N 166 
GLU HE2    H  N N 167 
GLU HXT    H  N N 168 
GLY N      N  N N 169 
GLY CA     C  N N 170 
GLY C      C  N N 171 
GLY O      O  N N 172 
GLY OXT    O  N N 173 
GLY H      H  N N 174 
GLY H2     H  N N 175 
GLY HA2    H  N N 176 
GLY HA3    H  N N 177 
GLY HXT    H  N N 178 
HIS N      N  N N 179 
HIS CA     C  N S 180 
HIS C      C  N N 181 
HIS O      O  N N 182 
HIS CB     C  N N 183 
HIS CG     C  Y N 184 
HIS ND1    N  Y N 185 
HIS CD2    C  Y N 186 
HIS CE1    C  Y N 187 
HIS NE2    N  Y N 188 
HIS OXT    O  N N 189 
HIS H      H  N N 190 
HIS H2     H  N N 191 
HIS HA     H  N N 192 
HIS HB2    H  N N 193 
HIS HB3    H  N N 194 
HIS HD1    H  N N 195 
HIS HD2    H  N N 196 
HIS HE1    H  N N 197 
HIS HE2    H  N N 198 
HIS HXT    H  N N 199 
ILE N      N  N N 200 
ILE CA     C  N S 201 
ILE C      C  N N 202 
ILE O      O  N N 203 
ILE CB     C  N S 204 
ILE CG1    C  N N 205 
ILE CG2    C  N N 206 
ILE CD1    C  N N 207 
ILE OXT    O  N N 208 
ILE H      H  N N 209 
ILE H2     H  N N 210 
ILE HA     H  N N 211 
ILE HB     H  N N 212 
ILE HG12   H  N N 213 
ILE HG13   H  N N 214 
ILE HG21   H  N N 215 
ILE HG22   H  N N 216 
ILE HG23   H  N N 217 
ILE HD11   H  N N 218 
ILE HD12   H  N N 219 
ILE HD13   H  N N 220 
ILE HXT    H  N N 221 
LEU N      N  N N 222 
LEU CA     C  N S 223 
LEU C      C  N N 224 
LEU O      O  N N 225 
LEU CB     C  N N 226 
LEU CG     C  N N 227 
LEU CD1    C  N N 228 
LEU CD2    C  N N 229 
LEU OXT    O  N N 230 
LEU H      H  N N 231 
LEU H2     H  N N 232 
LEU HA     H  N N 233 
LEU HB2    H  N N 234 
LEU HB3    H  N N 235 
LEU HG     H  N N 236 
LEU HD11   H  N N 237 
LEU HD12   H  N N 238 
LEU HD13   H  N N 239 
LEU HD21   H  N N 240 
LEU HD22   H  N N 241 
LEU HD23   H  N N 242 
LEU HXT    H  N N 243 
LYS N      N  N N 244 
LYS CA     C  N S 245 
LYS C      C  N N 246 
LYS O      O  N N 247 
LYS CB     C  N N 248 
LYS CG     C  N N 249 
LYS CD     C  N N 250 
LYS CE     C  N N 251 
LYS NZ     N  N N 252 
LYS OXT    O  N N 253 
LYS H      H  N N 254 
LYS H2     H  N N 255 
LYS HA     H  N N 256 
LYS HB2    H  N N 257 
LYS HB3    H  N N 258 
LYS HG2    H  N N 259 
LYS HG3    H  N N 260 
LYS HD2    H  N N 261 
LYS HD3    H  N N 262 
LYS HE2    H  N N 263 
LYS HE3    H  N N 264 
LYS HZ1    H  N N 265 
LYS HZ2    H  N N 266 
LYS HZ3    H  N N 267 
LYS HXT    H  N N 268 
MET N      N  N N 269 
MET CA     C  N S 270 
MET C      C  N N 271 
MET O      O  N N 272 
MET CB     C  N N 273 
MET CG     C  N N 274 
MET SD     S  N N 275 
MET CE     C  N N 276 
MET OXT    O  N N 277 
MET H      H  N N 278 
MET H2     H  N N 279 
MET HA     H  N N 280 
MET HB2    H  N N 281 
MET HB3    H  N N 282 
MET HG2    H  N N 283 
MET HG3    H  N N 284 
MET HE1    H  N N 285 
MET HE2    H  N N 286 
MET HE3    H  N N 287 
MET HXT    H  N N 288 
MG  MG     MG N N 289 
PHE N      N  N N 290 
PHE CA     C  N S 291 
PHE C      C  N N 292 
PHE O      O  N N 293 
PHE CB     C  N N 294 
PHE CG     C  Y N 295 
PHE CD1    C  Y N 296 
PHE CD2    C  Y N 297 
PHE CE1    C  Y N 298 
PHE CE2    C  Y N 299 
PHE CZ     C  Y N 300 
PHE OXT    O  N N 301 
PHE H      H  N N 302 
PHE H2     H  N N 303 
PHE HA     H  N N 304 
PHE HB2    H  N N 305 
PHE HB3    H  N N 306 
PHE HD1    H  N N 307 
PHE HD2    H  N N 308 
PHE HE1    H  N N 309 
PHE HE2    H  N N 310 
PHE HZ     H  N N 311 
PHE HXT    H  N N 312 
PRO N      N  N N 313 
PRO CA     C  N S 314 
PRO C      C  N N 315 
PRO O      O  N N 316 
PRO CB     C  N N 317 
PRO CG     C  N N 318 
PRO CD     C  N N 319 
PRO OXT    O  N N 320 
PRO H      H  N N 321 
PRO HA     H  N N 322 
PRO HB2    H  N N 323 
PRO HB3    H  N N 324 
PRO HG2    H  N N 325 
PRO HG3    H  N N 326 
PRO HD2    H  N N 327 
PRO HD3    H  N N 328 
PRO HXT    H  N N 329 
SER N      N  N N 330 
SER CA     C  N S 331 
SER C      C  N N 332 
SER O      O  N N 333 
SER CB     C  N N 334 
SER OG     O  N N 335 
SER OXT    O  N N 336 
SER H      H  N N 337 
SER H2     H  N N 338 
SER HA     H  N N 339 
SER HB2    H  N N 340 
SER HB3    H  N N 341 
SER HG     H  N N 342 
SER HXT    H  N N 343 
THR N      N  N N 344 
THR CA     C  N S 345 
THR C      C  N N 346 
THR O      O  N N 347 
THR CB     C  N R 348 
THR OG1    O  N N 349 
THR CG2    C  N N 350 
THR OXT    O  N N 351 
THR H      H  N N 352 
THR H2     H  N N 353 
THR HA     H  N N 354 
THR HB     H  N N 355 
THR HG1    H  N N 356 
THR HG21   H  N N 357 
THR HG22   H  N N 358 
THR HG23   H  N N 359 
THR HXT    H  N N 360 
TRP N      N  N N 361 
TRP CA     C  N S 362 
TRP C      C  N N 363 
TRP O      O  N N 364 
TRP CB     C  N N 365 
TRP CG     C  Y N 366 
TRP CD1    C  Y N 367 
TRP CD2    C  Y N 368 
TRP NE1    N  Y N 369 
TRP CE2    C  Y N 370 
TRP CE3    C  Y N 371 
TRP CZ2    C  Y N 372 
TRP CZ3    C  Y N 373 
TRP CH2    C  Y N 374 
TRP OXT    O  N N 375 
TRP H      H  N N 376 
TRP H2     H  N N 377 
TRP HA     H  N N 378 
TRP HB2    H  N N 379 
TRP HB3    H  N N 380 
TRP HD1    H  N N 381 
TRP HE1    H  N N 382 
TRP HE3    H  N N 383 
TRP HZ2    H  N N 384 
TRP HZ3    H  N N 385 
TRP HH2    H  N N 386 
TRP HXT    H  N N 387 
TYR N      N  N N 388 
TYR CA     C  N S 389 
TYR C      C  N N 390 
TYR O      O  N N 391 
TYR CB     C  N N 392 
TYR CG     C  Y N 393 
TYR CD1    C  Y N 394 
TYR CD2    C  Y N 395 
TYR CE1    C  Y N 396 
TYR CE2    C  Y N 397 
TYR CZ     C  Y N 398 
TYR OH     O  N N 399 
TYR OXT    O  N N 400 
TYR H      H  N N 401 
TYR H2     H  N N 402 
TYR HA     H  N N 403 
TYR HB2    H  N N 404 
TYR HB3    H  N N 405 
TYR HD1    H  N N 406 
TYR HD2    H  N N 407 
TYR HE1    H  N N 408 
TYR HE2    H  N N 409 
TYR HH     H  N N 410 
TYR HXT    H  N N 411 
VAL N      N  N N 412 
VAL CA     C  N S 413 
VAL C      C  N N 414 
VAL O      O  N N 415 
VAL CB     C  N N 416 
VAL CG1    C  N N 417 
VAL CG2    C  N N 418 
VAL OXT    O  N N 419 
VAL H      H  N N 420 
VAL H2     H  N N 421 
VAL HA     H  N N 422 
VAL HB     H  N N 423 
VAL HG11   H  N N 424 
VAL HG12   H  N N 425 
VAL HG13   H  N N 426 
VAL HG21   H  N N 427 
VAL HG22   H  N N 428 
VAL HG23   H  N N 429 
VAL HXT    H  N N 430 
VO4 V      V  N N 431 
VO4 O1     O  N N 432 
VO4 O2     O  N N 433 
VO4 O3     O  N N 434 
VO4 O4     O  N N 435 
# 
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 
ADP PB    O1B    doub N N 1   
ADP PB    O2B    sing N N 2   
ADP PB    O3B    sing N N 3   
ADP PB    O3A    sing N N 4   
ADP O2B   HOB2   sing N N 5   
ADP O3B   HOB3   sing N N 6   
ADP PA    O1A    doub N N 7   
ADP PA    O2A    sing N N 8   
ADP PA    O3A    sing N N 9   
ADP PA    "O5'"  sing N N 10  
ADP O2A   HOA2   sing N N 11  
ADP "O5'" "C5'"  sing N N 12  
ADP "C5'" "C4'"  sing N N 13  
ADP "C5'" "H5'1" sing N N 14  
ADP "C5'" "H5'2" sing N N 15  
ADP "C4'" "O4'"  sing N N 16  
ADP "C4'" "C3'"  sing N N 17  
ADP "C4'" "H4'"  sing N N 18  
ADP "O4'" "C1'"  sing N N 19  
ADP "C3'" "O3'"  sing N N 20  
ADP "C3'" "C2'"  sing N N 21  
ADP "C3'" "H3'"  sing N N 22  
ADP "O3'" "HO3'" sing N N 23  
ADP "C2'" "O2'"  sing N N 24  
ADP "C2'" "C1'"  sing N N 25  
ADP "C2'" "H2'"  sing N N 26  
ADP "O2'" "HO2'" sing N N 27  
ADP "C1'" N9     sing N N 28  
ADP "C1'" "H1'"  sing N N 29  
ADP N9    C8     sing Y N 30  
ADP N9    C4     sing Y N 31  
ADP C8    N7     doub Y N 32  
ADP C8    H8     sing N N 33  
ADP N7    C5     sing Y N 34  
ADP C5    C6     sing Y N 35  
ADP C5    C4     doub Y N 36  
ADP C6    N6     sing N N 37  
ADP C6    N1     doub Y N 38  
ADP N6    HN61   sing N N 39  
ADP N6    HN62   sing N N 40  
ADP N1    C2     sing Y N 41  
ADP C2    N3     doub Y N 42  
ADP C2    H2     sing N N 43  
ADP N3    C4     sing Y N 44  
ALA N     CA     sing N N 45  
ALA N     H      sing N N 46  
ALA N     H2     sing N N 47  
ALA CA    C      sing N N 48  
ALA CA    CB     sing N N 49  
ALA CA    HA     sing N N 50  
ALA C     O      doub N N 51  
ALA C     OXT    sing N N 52  
ALA CB    HB1    sing N N 53  
ALA CB    HB2    sing N N 54  
ALA CB    HB3    sing N N 55  
ALA OXT   HXT    sing N N 56  
ARG N     CA     sing N N 57  
ARG N     H      sing N N 58  
ARG N     H2     sing N N 59  
ARG CA    C      sing N N 60  
ARG CA    CB     sing N N 61  
ARG CA    HA     sing N N 62  
ARG C     O      doub N N 63  
ARG C     OXT    sing N N 64  
ARG CB    CG     sing N N 65  
ARG CB    HB2    sing N N 66  
ARG CB    HB3    sing N N 67  
ARG CG    CD     sing N N 68  
ARG CG    HG2    sing N N 69  
ARG CG    HG3    sing N N 70  
ARG CD    NE     sing N N 71  
ARG CD    HD2    sing N N 72  
ARG CD    HD3    sing N N 73  
ARG NE    CZ     sing N N 74  
ARG NE    HE     sing N N 75  
ARG CZ    NH1    sing N N 76  
ARG CZ    NH2    doub N N 77  
ARG NH1   HH11   sing N N 78  
ARG NH1   HH12   sing N N 79  
ARG NH2   HH21   sing N N 80  
ARG NH2   HH22   sing N N 81  
ARG OXT   HXT    sing N N 82  
ASN N     CA     sing N N 83  
ASN N     H      sing N N 84  
ASN N     H2     sing N N 85  
ASN CA    C      sing N N 86  
ASN CA    CB     sing N N 87  
ASN CA    HA     sing N N 88  
ASN C     O      doub N N 89  
ASN C     OXT    sing N N 90  
ASN CB    CG     sing N N 91  
ASN CB    HB2    sing N N 92  
ASN CB    HB3    sing N N 93  
ASN CG    OD1    doub N N 94  
ASN CG    ND2    sing N N 95  
ASN ND2   HD21   sing N N 96  
ASN ND2   HD22   sing N N 97  
ASN OXT   HXT    sing N N 98  
ASP N     CA     sing N N 99  
ASP N     H      sing N N 100 
ASP N     H2     sing N N 101 
ASP CA    C      sing N N 102 
ASP CA    CB     sing N N 103 
ASP CA    HA     sing N N 104 
ASP C     O      doub N N 105 
ASP C     OXT    sing N N 106 
ASP CB    CG     sing N N 107 
ASP CB    HB2    sing N N 108 
ASP CB    HB3    sing N N 109 
ASP CG    OD1    doub N N 110 
ASP CG    OD2    sing N N 111 
ASP OD2   HD2    sing N N 112 
ASP OXT   HXT    sing N N 113 
CYS N     CA     sing N N 114 
CYS N     H      sing N N 115 
CYS N     H2     sing N N 116 
CYS CA    C      sing N N 117 
CYS CA    CB     sing N N 118 
CYS CA    HA     sing N N 119 
CYS C     O      doub N N 120 
CYS C     OXT    sing N N 121 
CYS CB    SG     sing N N 122 
CYS CB    HB2    sing N N 123 
CYS CB    HB3    sing N N 124 
CYS SG    HG     sing N N 125 
CYS OXT   HXT    sing N N 126 
GLN N     CA     sing N N 127 
GLN N     H      sing N N 128 
GLN N     H2     sing N N 129 
GLN CA    C      sing N N 130 
GLN CA    CB     sing N N 131 
GLN CA    HA     sing N N 132 
GLN C     O      doub N N 133 
GLN C     OXT    sing N N 134 
GLN CB    CG     sing N N 135 
GLN CB    HB2    sing N N 136 
GLN CB    HB3    sing N N 137 
GLN CG    CD     sing N N 138 
GLN CG    HG2    sing N N 139 
GLN CG    HG3    sing N N 140 
GLN CD    OE1    doub N N 141 
GLN CD    NE2    sing N N 142 
GLN NE2   HE21   sing N N 143 
GLN NE2   HE22   sing N N 144 
GLN OXT   HXT    sing N N 145 
GLU N     CA     sing N N 146 
GLU N     H      sing N N 147 
GLU N     H2     sing N N 148 
GLU CA    C      sing N N 149 
GLU CA    CB     sing N N 150 
GLU CA    HA     sing N N 151 
GLU C     O      doub N N 152 
GLU C     OXT    sing N N 153 
GLU CB    CG     sing N N 154 
GLU CB    HB2    sing N N 155 
GLU CB    HB3    sing N N 156 
GLU CG    CD     sing N N 157 
GLU CG    HG2    sing N N 158 
GLU CG    HG3    sing N N 159 
GLU CD    OE1    doub N N 160 
GLU CD    OE2    sing N N 161 
GLU OE2   HE2    sing N N 162 
GLU OXT   HXT    sing N N 163 
GLY N     CA     sing N N 164 
GLY N     H      sing N N 165 
GLY N     H2     sing N N 166 
GLY CA    C      sing N N 167 
GLY CA    HA2    sing N N 168 
GLY CA    HA3    sing N N 169 
GLY C     O      doub N N 170 
GLY C     OXT    sing N N 171 
GLY OXT   HXT    sing N N 172 
HIS N     CA     sing N N 173 
HIS N     H      sing N N 174 
HIS N     H2     sing N N 175 
HIS CA    C      sing N N 176 
HIS CA    CB     sing N N 177 
HIS CA    HA     sing N N 178 
HIS C     O      doub N N 179 
HIS C     OXT    sing N N 180 
HIS CB    CG     sing N N 181 
HIS CB    HB2    sing N N 182 
HIS CB    HB3    sing N N 183 
HIS CG    ND1    sing Y N 184 
HIS CG    CD2    doub Y N 185 
HIS ND1   CE1    doub Y N 186 
HIS ND1   HD1    sing N N 187 
HIS CD2   NE2    sing Y N 188 
HIS CD2   HD2    sing N N 189 
HIS CE1   NE2    sing Y N 190 
HIS CE1   HE1    sing N N 191 
HIS NE2   HE2    sing N N 192 
HIS OXT   HXT    sing N N 193 
ILE N     CA     sing N N 194 
ILE N     H      sing N N 195 
ILE N     H2     sing N N 196 
ILE CA    C      sing N N 197 
ILE CA    CB     sing N N 198 
ILE CA    HA     sing N N 199 
ILE C     O      doub N N 200 
ILE C     OXT    sing N N 201 
ILE CB    CG1    sing N N 202 
ILE CB    CG2    sing N N 203 
ILE CB    HB     sing N N 204 
ILE CG1   CD1    sing N N 205 
ILE CG1   HG12   sing N N 206 
ILE CG1   HG13   sing N N 207 
ILE CG2   HG21   sing N N 208 
ILE CG2   HG22   sing N N 209 
ILE CG2   HG23   sing N N 210 
ILE CD1   HD11   sing N N 211 
ILE CD1   HD12   sing N N 212 
ILE CD1   HD13   sing N N 213 
ILE OXT   HXT    sing N N 214 
LEU N     CA     sing N N 215 
LEU N     H      sing N N 216 
LEU N     H2     sing N N 217 
LEU CA    C      sing N N 218 
LEU CA    CB     sing N N 219 
LEU CA    HA     sing N N 220 
LEU C     O      doub N N 221 
LEU C     OXT    sing N N 222 
LEU CB    CG     sing N N 223 
LEU CB    HB2    sing N N 224 
LEU CB    HB3    sing N N 225 
LEU CG    CD1    sing N N 226 
LEU CG    CD2    sing N N 227 
LEU CG    HG     sing N N 228 
LEU CD1   HD11   sing N N 229 
LEU CD1   HD12   sing N N 230 
LEU CD1   HD13   sing N N 231 
LEU CD2   HD21   sing N N 232 
LEU CD2   HD22   sing N N 233 
LEU CD2   HD23   sing N N 234 
LEU OXT   HXT    sing N N 235 
LYS N     CA     sing N N 236 
LYS N     H      sing N N 237 
LYS N     H2     sing N N 238 
LYS CA    C      sing N N 239 
LYS CA    CB     sing N N 240 
LYS CA    HA     sing N N 241 
LYS C     O      doub N N 242 
LYS C     OXT    sing N N 243 
LYS CB    CG     sing N N 244 
LYS CB    HB2    sing N N 245 
LYS CB    HB3    sing N N 246 
LYS CG    CD     sing N N 247 
LYS CG    HG2    sing N N 248 
LYS CG    HG3    sing N N 249 
LYS CD    CE     sing N N 250 
LYS CD    HD2    sing N N 251 
LYS CD    HD3    sing N N 252 
LYS CE    NZ     sing N N 253 
LYS CE    HE2    sing N N 254 
LYS CE    HE3    sing N N 255 
LYS NZ    HZ1    sing N N 256 
LYS NZ    HZ2    sing N N 257 
LYS NZ    HZ3    sing N N 258 
LYS OXT   HXT    sing N N 259 
MET N     CA     sing N N 260 
MET N     H      sing N N 261 
MET N     H2     sing N N 262 
MET CA    C      sing N N 263 
MET CA    CB     sing N N 264 
MET CA    HA     sing N N 265 
MET C     O      doub N N 266 
MET C     OXT    sing N N 267 
MET CB    CG     sing N N 268 
MET CB    HB2    sing N N 269 
MET CB    HB3    sing N N 270 
MET CG    SD     sing N N 271 
MET CG    HG2    sing N N 272 
MET CG    HG3    sing N N 273 
MET SD    CE     sing N N 274 
MET CE    HE1    sing N N 275 
MET CE    HE2    sing N N 276 
MET CE    HE3    sing N N 277 
MET OXT   HXT    sing N N 278 
PHE N     CA     sing N N 279 
PHE N     H      sing N N 280 
PHE N     H2     sing N N 281 
PHE CA    C      sing N N 282 
PHE CA    CB     sing N N 283 
PHE CA    HA     sing N N 284 
PHE C     O      doub N N 285 
PHE C     OXT    sing N N 286 
PHE CB    CG     sing N N 287 
PHE CB    HB2    sing N N 288 
PHE CB    HB3    sing N N 289 
PHE CG    CD1    doub Y N 290 
PHE CG    CD2    sing Y N 291 
PHE CD1   CE1    sing Y N 292 
PHE CD1   HD1    sing N N 293 
PHE CD2   CE2    doub Y N 294 
PHE CD2   HD2    sing N N 295 
PHE CE1   CZ     doub Y N 296 
PHE CE1   HE1    sing N N 297 
PHE CE2   CZ     sing Y N 298 
PHE CE2   HE2    sing N N 299 
PHE CZ    HZ     sing N N 300 
PHE OXT   HXT    sing N N 301 
PRO N     CA     sing N N 302 
PRO N     CD     sing N N 303 
PRO N     H      sing N N 304 
PRO CA    C      sing N N 305 
PRO CA    CB     sing N N 306 
PRO CA    HA     sing N N 307 
PRO C     O      doub N N 308 
PRO C     OXT    sing N N 309 
PRO CB    CG     sing N N 310 
PRO CB    HB2    sing N N 311 
PRO CB    HB3    sing N N 312 
PRO CG    CD     sing N N 313 
PRO CG    HG2    sing N N 314 
PRO CG    HG3    sing N N 315 
PRO CD    HD2    sing N N 316 
PRO CD    HD3    sing N N 317 
PRO OXT   HXT    sing N N 318 
SER N     CA     sing N N 319 
SER N     H      sing N N 320 
SER N     H2     sing N N 321 
SER CA    C      sing N N 322 
SER CA    CB     sing N N 323 
SER CA    HA     sing N N 324 
SER C     O      doub N N 325 
SER C     OXT    sing N N 326 
SER CB    OG     sing N N 327 
SER CB    HB2    sing N N 328 
SER CB    HB3    sing N N 329 
SER OG    HG     sing N N 330 
SER OXT   HXT    sing N N 331 
THR N     CA     sing N N 332 
THR N     H      sing N N 333 
THR N     H2     sing N N 334 
THR CA    C      sing N N 335 
THR CA    CB     sing N N 336 
THR CA    HA     sing N N 337 
THR C     O      doub N N 338 
THR C     OXT    sing N N 339 
THR CB    OG1    sing N N 340 
THR CB    CG2    sing N N 341 
THR CB    HB     sing N N 342 
THR OG1   HG1    sing N N 343 
THR CG2   HG21   sing N N 344 
THR CG2   HG22   sing N N 345 
THR CG2   HG23   sing N N 346 
THR OXT   HXT    sing N N 347 
TRP N     CA     sing N N 348 
TRP N     H      sing N N 349 
TRP N     H2     sing N N 350 
TRP CA    C      sing N N 351 
TRP CA    CB     sing N N 352 
TRP CA    HA     sing N N 353 
TRP C     O      doub N N 354 
TRP C     OXT    sing N N 355 
TRP CB    CG     sing N N 356 
TRP CB    HB2    sing N N 357 
TRP CB    HB3    sing N N 358 
TRP CG    CD1    doub Y N 359 
TRP CG    CD2    sing Y N 360 
TRP CD1   NE1    sing Y N 361 
TRP CD1   HD1    sing N N 362 
TRP CD2   CE2    doub Y N 363 
TRP CD2   CE3    sing Y N 364 
TRP NE1   CE2    sing Y N 365 
TRP NE1   HE1    sing N N 366 
TRP CE2   CZ2    sing Y N 367 
TRP CE3   CZ3    doub Y N 368 
TRP CE3   HE3    sing N N 369 
TRP CZ2   CH2    doub Y N 370 
TRP CZ2   HZ2    sing N N 371 
TRP CZ3   CH2    sing Y N 372 
TRP CZ3   HZ3    sing N N 373 
TRP CH2   HH2    sing N N 374 
TRP OXT   HXT    sing N N 375 
TYR N     CA     sing N N 376 
TYR N     H      sing N N 377 
TYR N     H2     sing N N 378 
TYR CA    C      sing N N 379 
TYR CA    CB     sing N N 380 
TYR CA    HA     sing N N 381 
TYR C     O      doub N N 382 
TYR C     OXT    sing N N 383 
TYR CB    CG     sing N N 384 
TYR CB    HB2    sing N N 385 
TYR CB    HB3    sing N N 386 
TYR CG    CD1    doub Y N 387 
TYR CG    CD2    sing Y N 388 
TYR CD1   CE1    sing Y N 389 
TYR CD1   HD1    sing N N 390 
TYR CD2   CE2    doub Y N 391 
TYR CD2   HD2    sing N N 392 
TYR CE1   CZ     doub Y N 393 
TYR CE1   HE1    sing N N 394 
TYR CE2   CZ     sing Y N 395 
TYR CE2   HE2    sing N N 396 
TYR CZ    OH     sing N N 397 
TYR OH    HH     sing N N 398 
TYR OXT   HXT    sing N N 399 
VAL N     CA     sing N N 400 
VAL N     H      sing N N 401 
VAL N     H2     sing N N 402 
VAL CA    C      sing N N 403 
VAL CA    CB     sing N N 404 
VAL CA    HA     sing N N 405 
VAL C     O      doub N N 406 
VAL C     OXT    sing N N 407 
VAL CB    CG1    sing N N 408 
VAL CB    CG2    sing N N 409 
VAL CB    HB     sing N N 410 
VAL CG1   HG11   sing N N 411 
VAL CG1   HG12   sing N N 412 
VAL CG1   HG13   sing N N 413 
VAL CG2   HG21   sing N N 414 
VAL CG2   HG22   sing N N 415 
VAL CG2   HG23   sing N N 416 
VAL OXT   HXT    sing N N 417 
VO4 V     O1     doub N N 418 
VO4 V     O2     sing N N 419 
VO4 V     O3     sing N N 420 
VO4 V     O4     sing N N 421 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-11-12 
_em_admin.deposition_site    PDBJ 
_em_admin.entry_id           9KK6 
_em_admin.last_update        2025-05-21 
_em_admin.map_release_date   2025-05-21 
_em_admin.title              'Cryo-EM structure of vanadate-trapped atABCB19 in lipid nanodisc' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_molwt.entity_assembly_id   1 
_em_entity_assembly_molwt.experimental_flag    NO 
_em_entity_assembly_molwt.id                   1 
_em_entity_assembly_molwt.units                MEGADALTONS 
_em_entity_assembly_molwt.value                0.13679 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          3702 
_em_entity_assembly_naturalsource.organism             'Arabidopsis thaliana' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          9606 
_em_entity_assembly_recombinant.organism             'Homo sapiens' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         50 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'FEI FALCON IV (4k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'MODEL REFINEMENT'              ? 1  ? ? ? PHENIX 1.18.2_3874: 
'IMAGE ACQUISITION'             ? 2  1 1 1 ?      ?            
'PARTICLE SELECTION'            ? 3  1 1 1 ?      ?            
'VOLUME SELECTION'              ? 4  1 1 1 ?      ?            
CLASSIFICATION                  ? 5  1 1 1 ?      ?            
MASKING                         ? 6  1 1 1 ?      ?            
RECONSTRUCTION                  ? 7  1 1 1 ?      ?            
'INITIAL EULER ASSIGNMENT'      ? 8  1 1 1 ?      ?            
'FINAL EULER ASSIGNMENT'        ? 9  1 1 1 ?      ?            
'CTF CORRECTION'                ? 10 1 1 1 ?      ?            
'LAYERLINE INDEXING'            ? 11 1 1 1 ?      ?            
'DIFFRACTION INDEXING'          ? 12 1 1 1 ?      ?            
'MODEL FITTING'                 ? 13 1 1 1 ?      ?            
'SERIES ALIGNMENT'              ? 14 1 1 1 ?      ?            
'MOLECULAR REPLACEMENT'         ? 15 1 1 1 ?      ?            
'LATTICE DISTORTION CORRECTION' ? 16 1 1 1 ?      ?            
'SYMMETRY DETERMINATION'        ? 17 1 1 1 ?      ?            
'CRYSTALLOGRAPHY MERGING'       ? 18 1 1 1 ?      ?            
OTHER                           ? 19 1 1 1 ?      ?            
# 
_em_specimen.concentration           2.0 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    9KK6 
_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]   1.000000 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   1.000000 
_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]   1.000000 
_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  
V  
# 
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     . GLU A 1 21   ? 119.066 87.505  119.155 1.00 35.64  ? 21   GLU A N     1 
ATOM   2    C  CA    . GLU A 1 21   ? 118.039 87.589  120.187 1.00 35.64  ? 21   GLU A CA    1 
ATOM   3    C  C     . GLU A 1 21   ? 116.659 87.270  119.622 1.00 35.64  ? 21   GLU A C     1 
ATOM   4    O  O     . GLU A 1 21   ? 116.449 87.310  118.410 1.00 35.64  ? 21   GLU A O     1 
ATOM   5    C  CB    . GLU A 1 21   ? 118.038 88.979  120.829 1.00 35.64  ? 21   GLU A CB    1 
ATOM   6    C  CG    . GLU A 1 21   ? 119.167 89.212  121.821 1.00 35.64  ? 21   GLU A CG    1 
ATOM   7    C  CD    . GLU A 1 21   ? 120.470 89.595  121.146 1.00 35.64  ? 21   GLU A CD    1 
ATOM   8    O  OE1   . GLU A 1 21   ? 120.479 89.739  119.905 1.00 35.64  ? 21   GLU A OE1   1 
ATOM   9    O  OE2   . GLU A 1 21   ? 121.484 89.757  121.856 1.00 35.64  ? 21   GLU A OE2   1 
ATOM   10   N  N     . GLN A 1 22   ? 115.723 86.956  120.512 1.00 31.72  ? 22   GLN A N     1 
ATOM   11   C  CA    . GLN A 1 22   ? 114.375 86.602  120.094 1.00 31.72  ? 22   GLN A CA    1 
ATOM   12   C  C     . GLN A 1 22   ? 113.652 87.811  119.512 1.00 31.72  ? 22   GLN A C     1 
ATOM   13   O  O     . GLN A 1 22   ? 113.877 88.954  119.916 1.00 31.72  ? 22   GLN A O     1 
ATOM   14   C  CB    . GLN A 1 22   ? 113.582 86.039  121.274 1.00 31.72  ? 22   GLN A CB    1 
ATOM   15   C  CG    . GLN A 1 22   ? 114.058 84.685  121.828 1.00 31.72  ? 22   GLN A CG    1 
ATOM   16   C  CD    . GLN A 1 22   ? 114.116 83.544  120.809 1.00 31.72  ? 22   GLN A CD    1 
ATOM   17   O  OE1   . GLN A 1 22   ? 114.513 83.715  119.657 1.00 31.72  ? 22   GLN A OE1   1 
ATOM   18   N  NE2   . GLN A 1 22   ? 113.715 82.358  121.252 1.00 31.72  ? 22   GLN A NE2   1 
ATOM   19   N  N     . SER A 1 23   ? 112.778 87.545  118.543 1.00 30.63  ? 23   SER A N     1 
ATOM   20   C  CA    . SER A 1 23   ? 111.978 88.584  117.914 1.00 30.63  ? 23   SER A CA    1 
ATOM   21   C  C     . SER A 1 23   ? 110.576 88.056  117.649 1.00 30.63  ? 23   SER A C     1 
ATOM   22   O  O     . SER A 1 23   ? 110.404 86.907  117.233 1.00 30.63  ? 23   SER A O     1 
ATOM   23   C  CB    . SER A 1 23   ? 112.617 89.066  116.607 1.00 30.63  ? 23   SER A CB    1 
ATOM   24   O  OG    . SER A 1 23   ? 113.102 87.975  115.844 1.00 30.63  ? 23   SER A OG    1 
ATOM   25   N  N     . LEU A 1 24   ? 109.583 88.902  117.896 1.00 27.94  ? 24   LEU A N     1 
ATOM   26   C  CA    . LEU A 1 24   ? 108.197 88.523  117.670 1.00 27.94  ? 24   LEU A CA    1 
ATOM   27   C  C     . LEU A 1 24   ? 107.895 88.484  116.174 1.00 27.94  ? 24   LEU A C     1 
ATOM   28   O  O     . LEU A 1 24   ? 108.382 89.331  115.422 1.00 27.94  ? 24   LEU A O     1 
ATOM   29   C  CB    . LEU A 1 24   ? 107.263 89.515  118.358 1.00 27.94  ? 24   LEU A CB    1 
ATOM   30   C  CG    . LEU A 1 24   ? 105.818 89.090  118.600 1.00 27.94  ? 24   LEU A CG    1 
ATOM   31   C  CD1   . LEU A 1 24   ? 105.726 88.198  119.823 1.00 27.94  ? 24   LEU A CD1   1 
ATOM   32   C  CD2   . LEU A 1 24   ? 104.938 90.315  118.757 1.00 27.94  ? 24   LEU A CD2   1 
ATOM   33   N  N     . PRO A 1 25   ? 107.095 87.522  115.715 1.00 27.34  ? 25   PRO A N     1 
ATOM   34   C  CA    . PRO A 1 25   ? 106.682 87.525  114.307 1.00 27.34  ? 25   PRO A CA    1 
ATOM   35   C  C     . PRO A 1 25   ? 105.891 88.780  113.970 1.00 27.34  ? 25   PRO A C     1 
ATOM   36   O  O     . PRO A 1 25   ? 105.175 89.333  114.807 1.00 27.34  ? 25   PRO A O     1 
ATOM   37   C  CB    . PRO A 1 25   ? 105.818 86.263  114.181 1.00 27.34  ? 25   PRO A CB    1 
ATOM   38   C  CG    . PRO A 1 25   ? 105.454 85.892  115.583 1.00 27.34  ? 25   PRO A CG    1 
ATOM   39   C  CD    . PRO A 1 25   ? 106.597 86.338  116.434 1.00 27.34  ? 25   PRO A CD    1 
ATOM   40   N  N     . PHE A 1 26   ? 106.038 89.232  112.722 1.00 26.01  ? 26   PHE A N     1 
ATOM   41   C  CA    . PHE A 1 26   ? 105.447 90.506  112.322 1.00 26.01  ? 26   PHE A CA    1 
ATOM   42   C  C     . PHE A 1 26   ? 103.927 90.475  112.417 1.00 26.01  ? 26   PHE A C     1 
ATOM   43   O  O     . PHE A 1 26   ? 103.309 91.449  112.860 1.00 26.01  ? 26   PHE A O     1 
ATOM   44   C  CB    . PHE A 1 26   ? 105.883 90.870  110.904 1.00 26.01  ? 26   PHE A CB    1 
ATOM   45   C  CG    . PHE A 1 26   ? 105.363 92.199  110.439 1.00 26.01  ? 26   PHE A CG    1 
ATOM   46   C  CD1   . PHE A 1 26   ? 105.483 93.319  111.241 1.00 26.01  ? 26   PHE A CD1   1 
ATOM   47   C  CD2   . PHE A 1 26   ? 104.750 92.327  109.204 1.00 26.01  ? 26   PHE A CD2   1 
ATOM   48   C  CE1   . PHE A 1 26   ? 105.005 94.543  110.821 1.00 26.01  ? 26   PHE A CE1   1 
ATOM   49   C  CE2   . PHE A 1 26   ? 104.269 93.549  108.779 1.00 26.01  ? 26   PHE A CE2   1 
ATOM   50   C  CZ    . PHE A 1 26   ? 104.397 94.658  109.589 1.00 26.01  ? 26   PHE A CZ    1 
ATOM   51   N  N     . PHE A 1 27   ? 103.306 89.369  112.003 1.00 30.06  ? 27   PHE A N     1 
ATOM   52   C  CA    . PHE A 1 27   ? 101.851 89.283  112.034 1.00 30.06  ? 27   PHE A CA    1 
ATOM   53   C  C     . PHE A 1 27   ? 101.291 89.376  113.447 1.00 30.06  ? 27   PHE A C     1 
ATOM   54   O  O     . PHE A 1 27   ? 100.137 89.780  113.617 1.00 30.06  ? 27   PHE A O     1 
ATOM   55   C  CB    . PHE A 1 27   ? 101.382 87.986  111.376 1.00 30.06  ? 27   PHE A CB    1 
ATOM   56   C  CG    . PHE A 1 27   ? 99.888  87.837  111.332 1.00 30.06  ? 27   PHE A CG    1 
ATOM   57   C  CD1   . PHE A 1 27   ? 99.133  88.554  110.420 1.00 30.06  ? 27   PHE A CD1   1 
ATOM   58   C  CD2   . PHE A 1 27   ? 99.239  86.980  112.206 1.00 30.06  ? 27   PHE A CD2   1 
ATOM   59   C  CE1   . PHE A 1 27   ? 97.757  88.419  110.380 1.00 30.06  ? 27   PHE A CE1   1 
ATOM   60   C  CE2   . PHE A 1 27   ? 97.864  86.840  112.170 1.00 30.06  ? 27   PHE A CE2   1 
ATOM   61   C  CZ    . PHE A 1 27   ? 97.122  87.561  111.256 1.00 30.06  ? 27   PHE A CZ    1 
ATOM   62   N  N     . LYS A 1 28   ? 102.079 89.019  114.462 1.00 27.89  ? 28   LYS A N     1 
ATOM   63   C  CA    . LYS A 1 28   ? 101.596 89.066  115.836 1.00 27.89  ? 28   LYS A CA    1 
ATOM   64   C  C     . LYS A 1 28   ? 101.389 90.485  116.345 1.00 27.89  ? 28   LYS A C     1 
ATOM   65   O  O     . LYS A 1 28   ? 100.785 90.658  117.408 1.00 27.89  ? 28   LYS A O     1 
ATOM   66   C  CB    . LYS A 1 28   ? 102.567 88.326  116.757 1.00 27.89  ? 28   LYS A CB    1 
ATOM   67   C  CG    . LYS A 1 28   ? 101.900 87.641  117.937 1.00 27.89  ? 28   LYS A CG    1 
ATOM   68   C  CD    . LYS A 1 28   ? 101.121 86.416  117.492 1.00 27.89  ? 28   LYS A CD    1 
ATOM   69   C  CE    . LYS A 1 28   ? 102.054 85.293  117.071 1.00 27.89  ? 28   LYS A CE    1 
ATOM   70   N  NZ    . LYS A 1 28   ? 101.329 84.208  116.354 1.00 27.89  ? 28   LYS A NZ    1 
ATOM   71   N  N     . LEU A 1 29   ? 101.874 91.499  115.624 1.00 24.77  ? 29   LEU A N     1 
ATOM   72   C  CA    . LEU A 1 29   ? 101.683 92.875  116.067 1.00 24.77  ? 29   LEU A CA    1 
ATOM   73   C  C     . LEU A 1 29   ? 100.218 93.290  116.006 1.00 24.77  ? 29   LEU A C     1 
ATOM   74   O  O     . LEU A 1 29   ? 99.777  94.121  116.808 1.00 24.77  ? 29   LEU A O     1 
ATOM   75   C  CB    . LEU A 1 29   ? 102.541 93.822  115.229 1.00 24.77  ? 29   LEU A CB    1 
ATOM   76   C  CG    . LEU A 1 29   ? 104.001 93.970  115.663 1.00 24.77  ? 29   LEU A CG    1 
ATOM   77   C  CD1   . LEU A 1 29   ? 104.663 95.129  114.940 1.00 24.77  ? 29   LEU A CD1   1 
ATOM   78   C  CD2   . LEU A 1 29   ? 104.096 94.154  117.167 1.00 24.77  ? 29   LEU A CD2   1 
ATOM   79   N  N     . PHE A 1 30   ? 99.453  92.730  115.070 1.00 25.79  ? 30   PHE A N     1 
ATOM   80   C  CA    . PHE A 1 30   ? 98.025  93.029  114.955 1.00 25.79  ? 30   PHE A CA    1 
ATOM   81   C  C     . PHE A 1 30   ? 97.238  92.123  115.903 1.00 25.79  ? 30   PHE A C     1 
ATOM   82   O  O     . PHE A 1 30   ? 96.498  91.223  115.501 1.00 25.79  ? 30   PHE A O     1 
ATOM   83   C  CB    . PHE A 1 30   ? 97.561  92.872  113.512 1.00 25.79  ? 30   PHE A CB    1 
ATOM   84   C  CG    . PHE A 1 30   ? 98.404  93.618  112.518 1.00 25.79  ? 30   PHE A CG    1 
ATOM   85   C  CD1   . PHE A 1 30   ? 98.122  94.934  112.202 1.00 25.79  ? 30   PHE A CD1   1 
ATOM   86   C  CD2   . PHE A 1 30   ? 99.472  93.000  111.892 1.00 25.79  ? 30   PHE A CD2   1 
ATOM   87   C  CE1   . PHE A 1 30   ? 98.893  95.621  111.287 1.00 25.79  ? 30   PHE A CE1   1 
ATOM   88   C  CE2   . PHE A 1 30   ? 100.245 93.684  110.976 1.00 25.79  ? 30   PHE A CE2   1 
ATOM   89   C  CZ    . PHE A 1 30   ? 99.956  94.995  110.674 1.00 25.79  ? 30   PHE A CZ    1 
ATOM   90   N  N     . SER A 1 31   ? 97.418  92.382  117.200 1.00 28.89  ? 31   SER A N     1 
ATOM   91   C  CA    . SER A 1 31   ? 96.754  91.616  118.248 1.00 28.89  ? 31   SER A CA    1 
ATOM   92   C  C     . SER A 1 31   ? 95.870  92.492  119.127 1.00 28.89  ? 31   SER A C     1 
ATOM   93   O  O     . SER A 1 31   ? 95.498  92.083  120.231 1.00 28.89  ? 31   SER A O     1 
ATOM   94   C  CB    . SER A 1 31   ? 97.783  90.876  119.105 1.00 28.89  ? 31   SER A CB    1 
ATOM   95   O  OG    . SER A 1 31   ? 98.656  91.785  119.751 1.00 28.89  ? 31   SER A OG    1 
ATOM   96   N  N     . PHE A 1 32   ? 95.530  93.696  118.665 1.00 29.47  ? 32   PHE A N     1 
ATOM   97   C  CA    . PHE A 1 32   ? 94.667  94.591  119.425 1.00 29.47  ? 32   PHE A CA    1 
ATOM   98   C  C     . PHE A 1 32   ? 93.660  95.290  118.521 1.00 29.47  ? 32   PHE A C     1 
ATOM   99   O  O     . PHE A 1 32   ? 93.257  96.425  118.797 1.00 29.47  ? 32   PHE A O     1 
ATOM   100  C  CB    . PHE A 1 32   ? 95.489  95.628  120.191 1.00 29.47  ? 32   PHE A CB    1 
ATOM   101  C  CG    . PHE A 1 32   ? 96.378  95.036  121.246 1.00 29.47  ? 32   PHE A CG    1 
ATOM   102  C  CD1   . PHE A 1 32   ? 95.895  94.796  122.520 1.00 29.47  ? 32   PHE A CD1   1 
ATOM   103  C  CD2   . PHE A 1 32   ? 97.695  94.720  120.963 1.00 29.47  ? 32   PHE A CD2   1 
ATOM   104  C  CE1   . PHE A 1 32   ? 96.710  94.252  123.493 1.00 29.47  ? 32   PHE A CE1   1 
ATOM   105  C  CE2   . PHE A 1 32   ? 98.513  94.176  121.932 1.00 29.47  ? 32   PHE A CE2   1 
ATOM   106  C  CZ    . PHE A 1 32   ? 98.020  93.942  123.198 1.00 29.47  ? 32   PHE A CZ    1 
ATOM   107  N  N     . ALA A 1 33   ? 93.240  94.631  117.446 1.00 31.29  ? 33   ALA A N     1 
ATOM   108  C  CA    . ALA A 1 33   ? 92.334  95.210  116.465 1.00 31.29  ? 33   ALA A CA    1 
ATOM   109  C  C     . ALA A 1 33   ? 90.953  94.585  116.604 1.00 31.29  ? 33   ALA A C     1 
ATOM   110  O  O     . ALA A 1 33   ? 90.820  93.357  116.605 1.00 31.29  ? 33   ALA A O     1 
ATOM   111  C  CB    . ALA A 1 33   ? 92.866  95.006  115.046 1.00 31.29  ? 33   ALA A CB    1 
ATOM   112  N  N     . ASP A 1 34   ? 89.934  95.431  116.715 1.00 33.34  ? 34   ASP A N     1 
ATOM   113  C  CA    . ASP A 1 34   ? 88.555  94.977  116.792 1.00 33.34  ? 34   ASP A CA    1 
ATOM   114  C  C     . ASP A 1 34   ? 87.965  94.909  115.385 1.00 33.34  ? 34   ASP A C     1 
ATOM   115  O  O     . ASP A 1 34   ? 88.681  94.983  114.383 1.00 33.34  ? 34   ASP A O     1 
ATOM   116  C  CB    . ASP A 1 34   ? 87.744  95.893  117.707 1.00 33.34  ? 34   ASP A CB    1 
ATOM   117  C  CG    . ASP A 1 34   ? 87.716  97.328  117.220 1.00 33.34  ? 34   ASP A CG    1 
ATOM   118  O  OD1   . ASP A 1 34   ? 88.503  97.670  116.313 1.00 33.34  ? 34   ASP A OD1   1 
ATOM   119  O  OD2   . ASP A 1 34   ? 86.903  98.117  117.746 1.00 33.34  ? 34   ASP A OD2   1 
ATOM   120  N  N     . LYS A 1 35   ? 86.641  94.760  115.296 1.00 34.61  ? 35   LYS A N     1 
ATOM   121  C  CA    . LYS A 1 35   ? 85.989  94.721  113.991 1.00 34.61  ? 35   LYS A CA    1 
ATOM   122  C  C     . LYS A 1 35   ? 86.170  96.035  113.242 1.00 34.61  ? 35   LYS A C     1 
ATOM   123  O  O     . LYS A 1 35   ? 86.398  96.038  112.027 1.00 34.61  ? 35   LYS A O     1 
ATOM   124  C  CB    . LYS A 1 35   ? 84.504  94.397  114.156 1.00 34.61  ? 35   LYS A CB    1 
ATOM   125  C  CG    . LYS A 1 35   ? 83.731  94.323  112.847 1.00 34.61  ? 35   LYS A CG    1 
ATOM   126  C  CD    . LYS A 1 35   ? 82.840  95.543  112.663 1.00 34.61  ? 35   LYS A CD    1 
ATOM   127  C  CE    . LYS A 1 35   ? 82.006  95.438  111.399 1.00 34.61  ? 35   LYS A CE    1 
ATOM   128  N  NZ    . LYS A 1 35   ? 81.151  96.641  111.203 1.00 34.61  ? 35   LYS A NZ    1 
ATOM   129  N  N     . PHE A 1 36   ? 86.066  97.164  113.949 1.00 32.70  ? 36   PHE A N     1 
ATOM   130  C  CA    . PHE A 1 36   ? 86.210  98.461  113.294 1.00 32.70  ? 36   PHE A CA    1 
ATOM   131  C  C     . PHE A 1 36   ? 87.607  98.636  112.713 1.00 32.70  ? 36   PHE A C     1 
ATOM   132  O  O     . PHE A 1 36   ? 87.764  99.154  111.601 1.00 32.70  ? 36   PHE A O     1 
ATOM   133  C  CB    . PHE A 1 36   ? 85.895  99.585  114.280 1.00 32.70  ? 36   PHE A CB    1 
ATOM   134  C  CG    . PHE A 1 36   ? 85.596  100.902 113.621 1.00 32.70  ? 36   PHE A CG    1 
ATOM   135  C  CD1   . PHE A 1 36   ? 84.429  101.081 112.899 1.00 32.70  ? 36   PHE A CD1   1 
ATOM   136  C  CD2   . PHE A 1 36   ? 86.484  101.959 113.721 1.00 32.70  ? 36   PHE A CD2   1 
ATOM   137  C  CE1   . PHE A 1 36   ? 84.152  102.292 112.291 1.00 32.70  ? 36   PHE A CE1   1 
ATOM   138  C  CE2   . PHE A 1 36   ? 86.212  103.172 113.116 1.00 32.70  ? 36   PHE A CE2   1 
ATOM   139  C  CZ    . PHE A 1 36   ? 85.046  103.338 112.401 1.00 32.70  ? 36   PHE A CZ    1 
ATOM   140  N  N     . ASP A 1 37   ? 88.635  98.213  113.451 1.00 30.35  ? 37   ASP A N     1 
ATOM   141  C  CA    . ASP A 1 37   ? 90.000  98.333  112.950 1.00 30.35  ? 37   ASP A CA    1 
ATOM   142  C  C     . ASP A 1 37   ? 90.224  97.443  111.734 1.00 30.35  ? 37   ASP A C     1 
ATOM   143  O  O     . ASP A 1 37   ? 90.946  97.825  110.804 1.00 30.35  ? 37   ASP A O     1 
ATOM   144  C  CB    . ASP A 1 37   ? 90.996  97.996  114.057 1.00 30.35  ? 37   ASP A CB    1 
ATOM   145  C  CG    . ASP A 1 37   ? 91.154  99.122  115.055 1.00 30.35  ? 37   ASP A CG    1 
ATOM   146  O  OD1   . ASP A 1 37   ? 91.138  100.297 114.634 1.00 30.35  ? 37   ASP A OD1   1 
ATOM   147  O  OD2   . ASP A 1 37   ? 91.293  98.833  116.262 1.00 30.35  ? 37   ASP A OD2   1 
ATOM   148  N  N     . TYR A 1 38   ? 89.622  96.251  111.725 1.00 30.89  ? 38   TYR A N     1 
ATOM   149  C  CA    . TYR A 1 38   ? 89.744  95.371  110.567 1.00 30.89  ? 38   TYR A CA    1 
ATOM   150  C  C     . TYR A 1 38   ? 89.156  96.020  109.322 1.00 30.89  ? 38   TYR A C     1 
ATOM   151  O  O     . TYR A 1 38   ? 89.745  95.949  108.238 1.00 30.89  ? 38   TYR A O     1 
ATOM   152  C  CB    . TYR A 1 38   ? 89.061  94.032  110.847 1.00 30.89  ? 38   TYR A CB    1 
ATOM   153  C  CG    . TYR A 1 38   ? 89.800  93.157  111.834 1.00 30.89  ? 38   TYR A CG    1 
ATOM   154  C  CD1   . TYR A 1 38   ? 91.186  93.169  111.899 1.00 30.89  ? 38   TYR A CD1   1 
ATOM   155  C  CD2   . TYR A 1 38   ? 89.111  92.317  112.698 1.00 30.89  ? 38   TYR A CD2   1 
ATOM   156  C  CE1   . TYR A 1 38   ? 91.866  92.373  112.799 1.00 30.89  ? 38   TYR A CE1   1 
ATOM   157  C  CE2   . TYR A 1 38   ? 89.783  91.516  113.602 1.00 30.89  ? 38   TYR A CE2   1 
ATOM   158  C  CZ    . TYR A 1 38   ? 91.161  91.549  113.648 1.00 30.89  ? 38   TYR A CZ    1 
ATOM   159  O  OH    . TYR A 1 38   ? 91.835  90.754  114.545 1.00 30.89  ? 38   TYR A OH    1 
ATOM   160  N  N     . LEU A 1 39   ? 87.996  96.665  109.461 1.00 30.89  ? 39   LEU A N     1 
ATOM   161  C  CA    . LEU A 1 39   ? 87.387  97.352  108.327 1.00 30.89  ? 39   LEU A CA    1 
ATOM   162  C  C     . LEU A 1 39   ? 88.274  98.485  107.825 1.00 30.89  ? 39   LEU A C     1 
ATOM   163  O  O     . LEU A 1 39   ? 88.445  98.660  106.612 1.00 30.89  ? 39   LEU A O     1 
ATOM   164  C  CB    . LEU A 1 39   ? 86.011  97.887  108.721 1.00 30.89  ? 39   LEU A CB    1 
ATOM   165  C  CG    . LEU A 1 39   ? 85.247  98.660  107.647 1.00 30.89  ? 39   LEU A CG    1 
ATOM   166  C  CD1   . LEU A 1 39   ? 84.785  97.725  106.542 1.00 30.89  ? 39   LEU A CD1   1 
ATOM   167  C  CD2   . LEU A 1 39   ? 84.070  99.401  108.259 1.00 30.89  ? 39   LEU A CD2   1 
ATOM   168  N  N     . LEU A 1 40   ? 88.844  99.267  108.744 1.00 27.81  ? 40   LEU A N     1 
ATOM   169  C  CA    . LEU A 1 40   ? 89.709  100.370 108.340 1.00 27.81  ? 40   LEU A CA    1 
ATOM   170  C  C     . LEU A 1 40   ? 90.947  99.863  107.614 1.00 27.81  ? 40   LEU A C     1 
ATOM   171  O  O     . LEU A 1 40   ? 91.350  100.428 106.590 1.00 27.81  ? 40   LEU A O     1 
ATOM   172  C  CB    . LEU A 1 40   ? 90.103  101.203 109.557 1.00 27.81  ? 40   LEU A CB    1 
ATOM   173  C  CG    . LEU A 1 40   ? 89.015  102.124 110.106 1.00 27.81  ? 40   LEU A CG    1 
ATOM   174  C  CD1   . LEU A 1 40   ? 89.403  102.655 111.473 1.00 27.81  ? 40   LEU A CD1   1 
ATOM   175  C  CD2   . LEU A 1 40   ? 88.749  103.264 109.141 1.00 27.81  ? 40   LEU A CD2   1 
ATOM   176  N  N     . MET A 1 41   ? 91.564  98.795  108.124 1.00 28.76  ? 41   MET A N     1 
ATOM   177  C  CA    . MET A 1 41   ? 92.742  98.250  107.457 1.00 28.76  ? 41   MET A CA    1 
ATOM   178  C  C     . MET A 1 41   ? 92.386  97.661  106.098 1.00 28.76  ? 41   MET A C     1 
ATOM   179  O  O     . MET A 1 41   ? 93.165  97.779  105.147 1.00 28.76  ? 41   MET A O     1 
ATOM   180  C  CB    . MET A 1 41   ? 93.425  97.210  108.343 1.00 28.76  ? 41   MET A CB    1 
ATOM   181  C  CG    . MET A 1 41   ? 94.032  97.796  109.608 1.00 28.76  ? 41   MET A CG    1 
ATOM   182  S  SD    . MET A 1 41   ? 94.895  96.581  110.620 1.00 28.76  ? 41   MET A SD    1 
ATOM   183  C  CE    . MET A 1 41   ? 93.514  95.691  111.324 1.00 28.76  ? 41   MET A CE    1 
ATOM   184  N  N     . PHE A 1 42   ? 91.214  97.033  105.981 1.00 31.36  ? 42   PHE A N     1 
ATOM   185  C  CA    . PHE A 1 42   ? 90.783  96.521  104.684 1.00 31.36  ? 42   PHE A CA    1 
ATOM   186  C  C     . PHE A 1 42   ? 90.592  97.650  103.677 1.00 31.36  ? 42   PHE A C     1 
ATOM   187  O  O     . PHE A 1 42   ? 91.030  97.547  102.523 1.00 31.36  ? 42   PHE A O     1 
ATOM   188  C  CB    . PHE A 1 42   ? 89.492  95.721  104.844 1.00 31.36  ? 42   PHE A CB    1 
ATOM   189  C  CG    . PHE A 1 42   ? 88.873  95.305  103.545 1.00 31.36  ? 42   PHE A CG    1 
ATOM   190  C  CD1   . PHE A 1 42   ? 89.464  94.330  102.763 1.00 31.36  ? 42   PHE A CD1   1 
ATOM   191  C  CD2   . PHE A 1 42   ? 87.697  95.888  103.106 1.00 31.36  ? 42   PHE A CD2   1 
ATOM   192  C  CE1   . PHE A 1 42   ? 88.896  93.944  101.566 1.00 31.36  ? 42   PHE A CE1   1 
ATOM   193  C  CE2   . PHE A 1 42   ? 87.123  95.506  101.911 1.00 31.36  ? 42   PHE A CE2   1 
ATOM   194  C  CZ    . PHE A 1 42   ? 87.723  94.533  101.139 1.00 31.36  ? 42   PHE A CZ    1 
ATOM   195  N  N     . VAL A 1 43   ? 89.944  98.739  104.099 1.00 28.86  ? 43   VAL A N     1 
ATOM   196  C  CA    . VAL A 1 43   ? 89.737  99.875  103.203 1.00 28.86  ? 43   VAL A CA    1 
ATOM   197  C  C     . VAL A 1 43   ? 91.073  100.487 102.801 1.00 28.86  ? 43   VAL A C     1 
ATOM   198  O  O     . VAL A 1 43   ? 91.290  100.833 101.632 1.00 28.86  ? 43   VAL A O     1 
ATOM   199  C  CB    . VAL A 1 43   ? 88.809  100.913 103.858 1.00 28.86  ? 43   VAL A CB    1 
ATOM   200  C  CG1   . VAL A 1 43   ? 88.753  102.177 103.021 1.00 28.86  ? 43   VAL A CG1   1 
ATOM   201  C  CG2   . VAL A 1 43   ? 87.417  100.336 104.035 1.00 28.86  ? 43   VAL A CG2   1 
ATOM   202  N  N     . GLY A 1 44   ? 91.988  100.633 103.761 1.00 29.93  ? 44   GLY A N     1 
ATOM   203  C  CA    . GLY A 1 44   ? 93.299  101.173 103.441 1.00 29.93  ? 44   GLY A CA    1 
ATOM   204  C  C     . GLY A 1 44   ? 94.070  100.299 102.471 1.00 29.93  ? 44   GLY A C     1 
ATOM   205  O  O     . GLY A 1 44   ? 94.712  100.801 101.545 1.00 29.93  ? 44   GLY A O     1 
ATOM   206  N  N     . SER A 1 45   ? 94.019  98.980  102.669 1.00 30.35  ? 45   SER A N     1 
ATOM   207  C  CA    . SER A 1 45   ? 94.695  98.071  101.752 1.00 30.35  ? 45   SER A CA    1 
ATOM   208  C  C     . SER A 1 45   ? 94.104  98.164  100.353 1.00 30.35  ? 45   SER A C     1 
ATOM   209  O  O     . SER A 1 45   ? 94.842  98.177  99.361  1.00 30.35  ? 45   SER A O     1 
ATOM   210  C  CB    . SER A 1 45   ? 94.613  96.638  102.275 1.00 30.35  ? 45   SER A CB    1 
ATOM   211  O  OG    . SER A 1 45   ? 93.325  96.092  102.059 1.00 30.35  ? 45   SER A OG    1 
ATOM   212  N  N     . LEU A 1 46   ? 92.774  98.234  100.251 1.00 31.11  ? 46   LEU A N     1 
ATOM   213  C  CA    . LEU A 1 46   ? 92.147  98.359  98.938  1.00 31.11  ? 46   LEU A CA    1 
ATOM   214  C  C     . LEU A 1 46   ? 92.555  99.657  98.252  1.00 31.11  ? 46   LEU A C     1 
ATOM   215  O  O     . LEU A 1 46   ? 92.875  99.666  97.054  1.00 31.11  ? 46   LEU A O     1 
ATOM   216  C  CB    . LEU A 1 46   ? 90.627  98.279  99.071  1.00 31.11  ? 46   LEU A CB    1 
ATOM   217  C  CG    . LEU A 1 46   ? 89.861  98.009  97.776  1.00 31.11  ? 46   LEU A CG    1 
ATOM   218  C  CD1   . LEU A 1 46   ? 90.503  96.870  97.000  1.00 31.11  ? 46   LEU A CD1   1 
ATOM   219  C  CD2   . LEU A 1 46   ? 88.403  97.704  98.073  1.00 31.11  ? 46   LEU A CD2   1 
ATOM   220  N  N     . GLY A 1 47   ? 92.559  100.764 98.997  1.00 31.02  ? 47   GLY A N     1 
ATOM   221  C  CA    . GLY A 1 47   ? 92.964  102.032 98.414  1.00 31.02  ? 47   GLY A CA    1 
ATOM   222  C  C     . GLY A 1 47   ? 94.409  102.025 97.954  1.00 31.02  ? 47   GLY A C     1 
ATOM   223  O  O     . GLY A 1 47   ? 94.727  102.513 96.865  1.00 31.02  ? 47   GLY A O     1 
ATOM   224  N  N     . ALA A 1 48   ? 95.303  101.466 98.774  1.00 29.44  ? 48   ALA A N     1 
ATOM   225  C  CA    . ALA A 1 48   ? 96.707  101.387 98.391  1.00 29.44  ? 48   ALA A CA    1 
ATOM   226  C  C     . ALA A 1 48   ? 96.894  100.511 97.160  1.00 29.44  ? 48   ALA A C     1 
ATOM   227  O  O     . ALA A 1 48   ? 97.697  100.833 96.277  1.00 29.44  ? 48   ALA A O     1 
ATOM   228  C  CB    . ALA A 1 48   ? 97.541  100.861 99.558  1.00 29.44  ? 48   ALA A CB    1 
ATOM   229  N  N     . ILE A 1 49   ? 96.163  99.397  97.085  1.00 29.60  ? 49   ILE A N     1 
ATOM   230  C  CA    . ILE A 1 49   ? 96.271  98.512  95.929  1.00 29.60  ? 49   ILE A CA    1 
ATOM   231  C  C     . ILE A 1 49   ? 95.822  99.230  94.663  1.00 29.60  ? 49   ILE A C     1 
ATOM   232  O  O     . ILE A 1 49   ? 96.481  99.144  93.618  1.00 29.60  ? 49   ILE A O     1 
ATOM   233  C  CB    . ILE A 1 49   ? 95.465  97.223  96.170  1.00 29.60  ? 49   ILE A CB    1 
ATOM   234  C  CG1   . ILE A 1 49   ? 96.258  96.261  97.054  1.00 29.60  ? 49   ILE A CG1   1 
ATOM   235  C  CG2   . ILE A 1 49   ? 95.102  96.559  94.853  1.00 29.60  ? 49   ILE A CG2   1 
ATOM   236  C  CD1   . ILE A 1 49   ? 95.399  95.258  97.790  1.00 29.60  ? 49   ILE A CD1   1 
ATOM   237  N  N     . VAL A 1 50   ? 94.699  99.951  94.733  1.00 30.31  ? 50   VAL A N     1 
ATOM   238  C  CA    . VAL A 1 50   ? 94.220  100.681 93.559  1.00 30.31  ? 50   VAL A CA    1 
ATOM   239  C  C     . VAL A 1 50   ? 95.224  101.751 93.146  1.00 30.31  ? 50   VAL A C     1 
ATOM   240  O  O     . VAL A 1 50   ? 95.543  101.904 91.957  1.00 30.31  ? 50   VAL A O     1 
ATOM   241  C  CB    . VAL A 1 50   ? 92.831  101.286 93.834  1.00 30.31  ? 50   VAL A CB    1 
ATOM   242  C  CG1   . VAL A 1 50   ? 92.439  102.236 92.717  1.00 30.31  ? 50   VAL A CG1   1 
ATOM   243  C  CG2   . VAL A 1 50   ? 91.797  100.184 93.983  1.00 30.31  ? 50   VAL A CG2   1 
ATOM   244  N  N     . HIS A 1 51   ? 95.743  102.503 94.122  1.00 29.97  ? 51   HIS A N     1 
ATOM   245  C  CA    . HIS A 1 51   ? 96.718  103.545 93.823  1.00 29.97  ? 51   HIS A CA    1 
ATOM   246  C  C     . HIS A 1 51   ? 97.955  102.964 93.153  1.00 29.97  ? 51   HIS A C     1 
ATOM   247  O  O     . HIS A 1 51   ? 98.466  103.526 92.177  1.00 29.97  ? 51   HIS A O     1 
ATOM   248  C  CB    . HIS A 1 51   ? 97.098  104.279 95.109  1.00 29.97  ? 51   HIS A CB    1 
ATOM   249  C  CG    . HIS A 1 51   ? 98.124  105.353 94.921  1.00 29.97  ? 51   HIS A CG    1 
ATOM   250  N  ND1   . HIS A 1 51   ? 98.898  105.827 95.957  1.00 29.97  ? 51   HIS A ND1   1 
ATOM   251  C  CD2   . HIS A 1 51   ? 98.495  106.052 93.823  1.00 29.97  ? 51   HIS A CD2   1 
ATOM   252  C  CE1   . HIS A 1 51   ? 99.708  106.767 95.504  1.00 29.97  ? 51   HIS A CE1   1 
ATOM   253  N  NE2   . HIS A 1 51   ? 99.484  106.923 94.212  1.00 29.97  ? 51   HIS A NE2   1 
ATOM   254  N  N     . GLY A 1 52   ? 98.449  101.835 93.659  1.00 30.96  ? 52   GLY A N     1 
ATOM   255  C  CA    . GLY A 1 52   ? 99.620  101.222 93.060  1.00 30.96  ? 52   GLY A CA    1 
ATOM   256  C  C     . GLY A 1 52   ? 99.363  100.692 91.664  1.00 30.96  ? 52   GLY A C     1 
ATOM   257  O  O     . GLY A 1 52   ? 100.192 100.860 90.766  1.00 30.96  ? 52   GLY A O     1 
ATOM   258  N  N     . SER A 1 53   ? 98.214  100.049 91.457  1.00 34.05  ? 53   SER A N     1 
ATOM   259  C  CA    . SER A 1 53   ? 97.948  99.371  90.195  1.00 34.05  ? 53   SER A CA    1 
ATOM   260  C  C     . SER A 1 53   ? 97.418  100.293 89.105  1.00 34.05  ? 53   SER A C     1 
ATOM   261  O  O     . SER A 1 53   ? 97.312  99.855  87.955  1.00 34.05  ? 53   SER A O     1 
ATOM   262  C  CB    . SER A 1 53   ? 96.954  98.229  90.417  1.00 34.05  ? 53   SER A CB    1 
ATOM   263  O  OG    . SER A 1 53   ? 96.620  97.603  89.191  1.00 34.05  ? 53   SER A OG    1 
ATOM   264  N  N     . SER A 1 54   ? 97.073  101.542 89.428  1.00 37.75  ? 54   SER A N     1 
ATOM   265  C  CA    . SER A 1 54   ? 96.550  102.443 88.402  1.00 37.75  ? 54   SER A CA    1 
ATOM   266  C  C     . SER A 1 54   ? 97.569  102.692 87.291  1.00 37.75  ? 54   SER A C     1 
ATOM   267  O  O     . SER A 1 54   ? 97.229  102.654 86.103  1.00 37.75  ? 54   SER A O     1 
ATOM   268  C  CB    . SER A 1 54   ? 96.123  103.765 89.038  1.00 37.75  ? 54   SER A CB    1 
ATOM   269  O  OG    . SER A 1 54   ? 97.250  104.511 89.461  1.00 37.75  ? 54   SER A OG    1 
ATOM   270  N  N     . MET A 1 55   ? 98.824  102.950 87.660  1.00 44.43  ? 55   MET A N     1 
ATOM   271  C  CA    . MET A 1 55   ? 99.813  103.416 86.686  1.00 44.43  ? 55   MET A CA    1 
ATOM   272  C  C     . MET A 1 55   ? 100.131 102.414 85.579  1.00 44.43  ? 55   MET A C     1 
ATOM   273  O  O     . MET A 1 55   ? 100.159 102.821 84.403  1.00 44.43  ? 55   MET A O     1 
ATOM   274  C  CB    . MET A 1 55   ? 101.089 103.840 87.422  1.00 44.43  ? 55   MET A CB    1 
ATOM   275  C  CG    . MET A 1 55   ? 102.186 104.365 86.513  1.00 44.43  ? 55   MET A CG    1 
ATOM   276  S  SD    . MET A 1 55   ? 103.151 105.681 87.275  1.00 44.43  ? 55   MET A SD    1 
ATOM   277  C  CE    . MET A 1 55   ? 101.970 107.025 87.234  1.00 44.43  ? 55   MET A CE    1 
ATOM   278  N  N     . PRO A 1 56   ? 100.413 101.133 85.858  1.00 46.28  ? 56   PRO A N     1 
ATOM   279  C  CA    . PRO A 1 56   ? 100.855 100.244 84.764  1.00 46.28  ? 56   PRO A CA    1 
ATOM   280  C  C     . PRO A 1 56   ? 99.834  100.072 83.651  1.00 46.28  ? 56   PRO A C     1 
ATOM   281  O  O     . PRO A 1 56   ? 100.195 100.159 82.471  1.00 46.28  ? 56   PRO A O     1 
ATOM   282  C  CB    . PRO A 1 56   ? 101.143 98.926  85.494  1.00 46.28  ? 56   PRO A CB    1 
ATOM   283  C  CG    . PRO A 1 56   ? 101.489 99.345  86.873  1.00 46.28  ? 56   PRO A CG    1 
ATOM   284  C  CD    . PRO A 1 56   ? 100.535 100.462 87.164  1.00 46.28  ? 56   PRO A CD    1 
ATOM   285  N  N     . VAL A 1 57   ? 98.566  99.824  83.984  1.00 49.71  ? 57   VAL A N     1 
ATOM   286  C  CA    . VAL A 1 57   ? 97.555  99.695  82.938  1.00 49.71  ? 57   VAL A CA    1 
ATOM   287  C  C     . VAL A 1 57   ? 97.341  101.027 82.230  1.00 49.71  ? 57   VAL A C     1 
ATOM   288  O  O     . VAL A 1 57   ? 97.056  101.064 81.023  1.00 49.71  ? 57   VAL A O     1 
ATOM   289  C  CB    . VAL A 1 57   ? 96.242  99.141  83.522  1.00 49.71  ? 57   VAL A CB    1 
ATOM   290  C  CG1   . VAL A 1 57   ? 96.442  97.714  84.001  1.00 49.71  ? 57   VAL A CG1   1 
ATOM   291  C  CG2   . VAL A 1 57   ? 95.751  100.017 84.660  1.00 49.71  ? 57   VAL A CG2   1 
ATOM   292  N  N     . PHE A 1 58   ? 97.481  102.139 82.954  1.00 52.33  ? 58   PHE A N     1 
ATOM   293  C  CA    . PHE A 1 58   ? 97.345  103.445 82.321  1.00 52.33  ? 58   PHE A CA    1 
ATOM   294  C  C     . PHE A 1 58   ? 98.412  103.648 81.254  1.00 52.33  ? 58   PHE A C     1 
ATOM   295  O  O     . PHE A 1 58   ? 98.121  104.124 80.154  1.00 52.33  ? 58   PHE A O     1 
ATOM   296  C  CB    . PHE A 1 58   ? 97.417  104.556 83.364  1.00 52.33  ? 58   PHE A CB    1 
ATOM   297  C  CG    . PHE A 1 58   ? 97.361  105.930 82.771  1.00 52.33  ? 58   PHE A CG    1 
ATOM   298  C  CD1   . PHE A 1 58   ? 96.176  106.428 82.261  1.00 52.33  ? 58   PHE A CD1   1 
ATOM   299  C  CD2   . PHE A 1 58   ? 98.498  106.713 82.699  1.00 52.33  ? 58   PHE A CD2   1 
ATOM   300  C  CE1   . PHE A 1 58   ? 96.123  107.690 81.705  1.00 52.33  ? 58   PHE A CE1   1 
ATOM   301  C  CE2   . PHE A 1 58   ? 98.453  107.974 82.144  1.00 52.33  ? 58   PHE A CE2   1 
ATOM   302  C  CZ    . PHE A 1 58   ? 97.263  108.464 81.647  1.00 52.33  ? 58   PHE A CZ    1 
ATOM   303  N  N     . PHE A 1 59   ? 99.660  103.284 81.551  1.00 57.13  ? 59   PHE A N     1 
ATOM   304  C  CA    . PHE A 1 59   ? 100.683 103.412 80.520  1.00 57.13  ? 59   PHE A CA    1 
ATOM   305  C  C     . PHE A 1 59   ? 100.597 102.312 79.472  1.00 57.13  ? 59   PHE A C     1 
ATOM   306  O  O     . PHE A 1 59   ? 101.085 102.503 78.354  1.00 57.13  ? 59   PHE A O     1 
ATOM   307  C  CB    . PHE A 1 59   ? 102.079 103.459 81.141  1.00 57.13  ? 59   PHE A CB    1 
ATOM   308  C  CG    . PHE A 1 59   ? 102.506 104.843 81.544  1.00 57.13  ? 59   PHE A CG    1 
ATOM   309  C  CD1   . PHE A 1 59   ? 101.565 105.837 81.744  1.00 57.13  ? 59   PHE A CD1   1 
ATOM   310  C  CD2   . PHE A 1 59   ? 103.842 105.159 81.694  1.00 57.13  ? 59   PHE A CD2   1 
ATOM   311  C  CE1   . PHE A 1 59   ? 101.945 107.115 82.108  1.00 57.13  ? 59   PHE A CE1   1 
ATOM   312  C  CE2   . PHE A 1 59   ? 104.227 106.439 82.056  1.00 57.13  ? 59   PHE A CE2   1 
ATOM   313  C  CZ    . PHE A 1 59   ? 103.279 107.414 82.263  1.00 57.13  ? 59   PHE A CZ    1 
ATOM   314  N  N     . LEU A 1 60   ? 99.953  101.188 79.790  1.00 56.95  ? 60   LEU A N     1 
ATOM   315  C  CA    . LEU A 1 60   ? 99.591  100.236 78.746  1.00 56.95  ? 60   LEU A CA    1 
ATOM   316  C  C     . LEU A 1 60   ? 98.671  100.890 77.724  1.00 56.95  ? 60   LEU A C     1 
ATOM   317  O  O     . LEU A 1 60   ? 98.835  100.701 76.513  1.00 56.95  ? 60   LEU A O     1 
ATOM   318  C  CB    . LEU A 1 60   ? 98.924  99.007  79.364  1.00 56.95  ? 60   LEU A CB    1 
ATOM   319  C  CG    . LEU A 1 60   ? 98.178  98.061  78.419  1.00 56.95  ? 60   LEU A CG    1 
ATOM   320  C  CD1   . LEU A 1 60   ? 99.121  97.449  77.394  1.00 56.95  ? 60   LEU A CD1   1 
ATOM   321  C  CD2   . LEU A 1 60   ? 97.458  96.977  79.204  1.00 56.95  ? 60   LEU A CD2   1 
ATOM   322  N  N     . LEU A 1 61   ? 97.693  101.663 78.200  1.00 62.42  ? 61   LEU A N     1 
ATOM   323  C  CA    . LEU A 1 61   ? 96.870  102.464 77.295  1.00 62.42  ? 61   LEU A CA    1 
ATOM   324  C  C     . LEU A 1 61   ? 97.696  103.543 76.599  1.00 62.42  ? 61   LEU A C     1 
ATOM   325  O  O     . LEU A 1 61   ? 97.497  103.822 75.411  1.00 62.42  ? 61   LEU A O     1 
ATOM   326  C  CB    . LEU A 1 61   ? 95.708  103.090 78.067  1.00 62.42  ? 61   LEU A CB    1 
ATOM   327  C  CG    . LEU A 1 61   ? 94.623  103.802 77.257  1.00 62.42  ? 61   LEU A CG    1 
ATOM   328  C  CD1   . LEU A 1 61   ? 93.247  103.449 77.792  1.00 62.42  ? 61   LEU A CD1   1 
ATOM   329  C  CD2   . LEU A 1 61   ? 94.834  105.307 77.285  1.00 62.42  ? 61   LEU A CD2   1 
ATOM   330  N  N     . PHE A 1 62   ? 98.621  104.163 77.335  1.00 76.01  ? 62   PHE A N     1 
ATOM   331  C  CA    . PHE A 1 62   ? 99.436  105.258 76.810  1.00 76.01  ? 62   PHE A CA    1 
ATOM   332  C  C     . PHE A 1 62   ? 100.336 104.797 75.667  1.00 76.01  ? 62   PHE A C     1 
ATOM   333  O  O     . PHE A 1 62   ? 100.708 105.599 74.799  1.00 76.01  ? 62   PHE A O     1 
ATOM   334  C  CB    . PHE A 1 62   ? 100.272 105.839 77.953  1.00 76.01  ? 62   PHE A CB    1 
ATOM   335  C  CG    . PHE A 1 62   ? 100.989 107.111 77.616  1.00 76.01  ? 62   PHE A CG    1 
ATOM   336  C  CD1   . PHE A 1 62   ? 100.291 108.224 77.183  1.00 76.01  ? 62   PHE A CD1   1 
ATOM   337  C  CD2   . PHE A 1 62   ? 102.364 107.201 77.756  1.00 76.01  ? 62   PHE A CD2   1 
ATOM   338  C  CE1   . PHE A 1 62   ? 100.950 109.400 76.891  1.00 76.01  ? 62   PHE A CE1   1 
ATOM   339  C  CE2   . PHE A 1 62   ? 103.031 108.372 77.457  1.00 76.01  ? 62   PHE A CE2   1 
ATOM   340  C  CZ    . PHE A 1 62   ? 102.324 109.473 77.022  1.00 76.01  ? 62   PHE A CZ    1 
ATOM   341  N  N     . GLY A 1 63   ? 100.712 103.518 75.661  1.00 81.28  ? 63   GLY A N     1 
ATOM   342  C  CA    . GLY A 1 63   ? 101.548 102.988 74.596  1.00 81.28  ? 63   GLY A CA    1 
ATOM   343  C  C     . GLY A 1 63   ? 100.950 103.141 73.212  1.00 81.28  ? 63   GLY A C     1 
ATOM   344  O  O     . GLY A 1 63   ? 101.695 103.208 72.227  1.00 81.28  ? 63   GLY A O     1 
ATOM   345  N  N     . GLN A 1 64   ? 99.621  103.226 73.116  1.00 82.38  ? 64   GLN A N     1 
ATOM   346  C  CA    . GLN A 1 64   ? 98.983  103.391 71.815  1.00 82.38  ? 64   GLN A CA    1 
ATOM   347  C  C     . GLN A 1 64   ? 99.424  104.688 71.147  1.00 82.38  ? 64   GLN A C     1 
ATOM   348  O  O     . GLN A 1 64   ? 99.650  104.721 69.932  1.00 82.38  ? 64   GLN A O     1 
ATOM   349  C  CB    . GLN A 1 64   ? 97.462  103.341 71.969  1.00 82.38  ? 64   GLN A CB    1 
ATOM   350  C  CG    . GLN A 1 64   ? 96.691  103.306 70.656  1.00 82.38  ? 64   GLN A CG    1 
ATOM   351  C  CD    . GLN A 1 64   ? 96.437  104.686 70.085  1.00 82.38  ? 64   GLN A CD    1 
ATOM   352  O  OE1   . GLN A 1 64   ? 96.325  105.664 70.823  1.00 82.38  ? 64   GLN A OE1   1 
ATOM   353  N  NE2   . GLN A 1 64   ? 96.345  104.772 68.763  1.00 82.38  ? 64   GLN A NE2   1 
ATOM   354  N  N     . MET A 1 65   ? 99.552  105.769 71.920  1.00 83.84  ? 65   MET A N     1 
ATOM   355  C  CA    . MET A 1 65   ? 100.098 107.006 71.378  1.00 83.84  ? 65   MET A CA    1 
ATOM   356  C  C     . MET A 1 65   ? 101.616 107.053 71.442  1.00 83.84  ? 65   MET A C     1 
ATOM   357  O  O     . MET A 1 65   ? 102.230 107.786 70.658  1.00 83.84  ? 65   MET A O     1 
ATOM   358  C  CB    . MET A 1 65   ? 99.522  108.225 72.108  1.00 83.84  ? 65   MET A CB    1 
ATOM   359  C  CG    . MET A 1 65   ? 100.006 108.419 73.536  1.00 83.84  ? 65   MET A CG    1 
ATOM   360  S  SD    . MET A 1 65   ? 101.541 109.366 73.629  1.00 83.84  ? 65   MET A SD    1 
ATOM   361  C  CE    . MET A 1 65   ? 100.957 110.997 73.189  1.00 83.84  ? 65   MET A CE    1 
ATOM   362  N  N     . VAL A 1 66   ? 102.234 106.309 72.365  1.00 88.16  ? 66   VAL A N     1 
ATOM   363  C  CA    . VAL A 1 66   ? 103.689 106.179 72.351  1.00 88.16  ? 66   VAL A CA    1 
ATOM   364  C  C     . VAL A 1 66   ? 104.156 105.597 71.024  1.00 88.16  ? 66   VAL A C     1 
ATOM   365  O  O     . VAL A 1 66   ? 105.256 105.910 70.555  1.00 88.16  ? 66   VAL A O     1 
ATOM   366  C  CB    . VAL A 1 66   ? 104.174 105.325 73.545  1.00 88.16  ? 66   VAL A CB    1 
ATOM   367  C  CG1   . VAL A 1 66   ? 105.669 105.054 73.452  1.00 88.16  ? 66   VAL A CG1   1 
ATOM   368  C  CG2   . VAL A 1 66   ? 103.859 106.023 74.852  1.00 88.16  ? 66   VAL A CG2   1 
ATOM   369  N  N     . ASN A 1 67   ? 103.314 104.789 70.379  1.00 93.40  ? 67   ASN A N     1 
ATOM   370  C  CA    . ASN A 1 67   ? 103.581 104.276 69.041  1.00 93.40  ? 67   ASN A CA    1 
ATOM   371  C  C     . ASN A 1 67   ? 103.237 105.291 67.955  1.00 93.40  ? 67   ASN A C     1 
ATOM   372  O  O     . ASN A 1 67   ? 102.979 104.908 66.805  1.00 93.40  ? 67   ASN A O     1 
ATOM   373  C  CB    . ASN A 1 67   ? 102.809 102.976 68.815  1.00 93.40  ? 67   ASN A CB    1 
ATOM   374  C  CG    . ASN A 1 67   ? 103.348 101.828 69.641  1.00 93.40  ? 67   ASN A CG    1 
ATOM   375  O  OD1   . ASN A 1 67   ? 104.560 101.655 69.770  1.00 93.40  ? 67   ASN A OD1   1 
ATOM   376  N  ND2   . ASN A 1 67   ? 102.447 101.031 70.204  1.00 93.40  ? 67   ASN A ND2   1 
ATOM   377  N  N     . GLY A 1 68   ? 103.212 106.581 68.296  1.00 99.10  ? 68   GLY A N     1 
ATOM   378  C  CA    . GLY A 1 68   ? 102.798 107.613 67.360  1.00 99.10  ? 68   GLY A CA    1 
ATOM   379  C  C     . GLY A 1 68   ? 103.652 107.711 66.113  1.00 99.10  ? 68   GLY A C     1 
ATOM   380  O  O     . GLY A 1 68   ? 103.185 108.238 65.098  1.00 99.10  ? 68   GLY A O     1 
ATOM   381  N  N     . PHE A 1 69   ? 104.890 107.216 66.160  1.00 104.28 ? 69   PHE A N     1 
ATOM   382  C  CA    . PHE A 1 69   ? 105.738 107.225 64.974  1.00 104.28 ? 69   PHE A CA    1 
ATOM   383  C  C     . PHE A 1 69   ? 105.187 106.351 63.854  1.00 104.28 ? 69   PHE A C     1 
ATOM   384  O  O     . PHE A 1 69   ? 105.619 106.498 62.706  1.00 104.28 ? 69   PHE A O     1 
ATOM   385  C  CB    . PHE A 1 69   ? 107.156 106.775 65.337  1.00 104.28 ? 69   PHE A CB    1 
ATOM   386  C  CG    . PHE A 1 69   ? 108.113 106.793 64.179  1.00 104.28 ? 69   PHE A CG    1 
ATOM   387  C  CD1   . PHE A 1 69   ? 108.630 107.988 63.709  1.00 104.28 ? 69   PHE A CD1   1 
ATOM   388  C  CD2   . PHE A 1 69   ? 108.491 105.614 63.557  1.00 104.28 ? 69   PHE A CD2   1 
ATOM   389  C  CE1   . PHE A 1 69   ? 109.507 108.008 62.641  1.00 104.28 ? 69   PHE A CE1   1 
ATOM   390  C  CE2   . PHE A 1 69   ? 109.368 105.627 62.489  1.00 104.28 ? 69   PHE A CE2   1 
ATOM   391  C  CZ    . PHE A 1 69   ? 109.877 106.826 62.030  1.00 104.28 ? 69   PHE A CZ    1 
ATOM   392  N  N     . GLY A 1 70   ? 104.246 105.459 64.151  1.00 105.46 ? 70   GLY A N     1 
ATOM   393  C  CA    . GLY A 1 70   ? 103.637 104.638 63.125  1.00 105.46 ? 70   GLY A CA    1 
ATOM   394  C  C     . GLY A 1 70   ? 102.135 104.511 63.264  1.00 105.46 ? 70   GLY A C     1 
ATOM   395  O  O     . GLY A 1 70   ? 101.491 103.828 62.460  1.00 105.46 ? 70   GLY A O     1 
ATOM   396  N  N     . LYS A 1 71   ? 101.558 105.157 64.277  1.00 103.72 ? 71   LYS A N     1 
ATOM   397  C  CA    . LYS A 1 71   ? 100.117 105.057 64.492  1.00 103.72 ? 71   LYS A CA    1 
ATOM   398  C  C     . LYS A 1 71   ? 99.332  106.075 63.666  1.00 103.72 ? 71   LYS A C     1 
ATOM   399  O  O     . LYS A 1 71   ? 98.508  105.696 62.827  1.00 103.72 ? 71   LYS A O     1 
ATOM   400  C  CB    . LYS A 1 71   ? 99.796  105.221 65.982  1.00 103.72 ? 71   LYS A CB    1 
ATOM   401  C  CG    . LYS A 1 71   ? 99.966  103.951 66.798  1.00 103.72 ? 71   LYS A CG    1 
ATOM   402  C  CD    . LYS A 1 71   ? 99.260  102.773 66.148  1.00 103.72 ? 71   LYS A CD    1 
ATOM   403  C  CE    . LYS A 1 71   ? 99.881  101.452 66.576  1.00 103.72 ? 71   LYS A CE    1 
ATOM   404  N  NZ    . LYS A 1 71   ? 101.198 101.210 65.924  1.00 103.72 ? 71   LYS A NZ    1 
ATOM   405  N  N     . ASN A 1 72   ? 99.574  107.372 63.890  1.00 103.60 ? 72   ASN A N     1 
ATOM   406  C  CA    . ASN A 1 72   ? 98.787  108.390 63.202  1.00 103.60 ? 72   ASN A CA    1 
ATOM   407  C  C     . ASN A 1 72   ? 99.604  109.615 62.801  1.00 103.60 ? 72   ASN A C     1 
ATOM   408  O  O     . ASN A 1 72   ? 99.020  110.674 62.541  1.00 103.60 ? 72   ASN A O     1 
ATOM   409  C  CB    . ASN A 1 72   ? 97.604  108.834 64.069  1.00 103.60 ? 72   ASN A CB    1 
ATOM   410  C  CG    . ASN A 1 72   ? 96.572  107.742 64.248  1.00 103.60 ? 72   ASN A CG    1 
ATOM   411  O  OD1   . ASN A 1 72   ? 96.367  107.239 65.353  1.00 103.60 ? 72   ASN A OD1   1 
ATOM   412  N  ND2   . ASN A 1 72   ? 95.921  107.361 63.156  1.00 103.60 ? 72   ASN A ND2   1 
ATOM   413  N  N     . GLN A 1 73   ? 100.935 109.514 62.760  1.00 106.01 ? 73   GLN A N     1 
ATOM   414  C  CA    . GLN A 1 73   ? 101.752 110.680 62.443  1.00 106.01 ? 73   GLN A CA    1 
ATOM   415  C  C     . GLN A 1 73   ? 101.581 111.136 61.001  1.00 106.01 ? 73   GLN A C     1 
ATOM   416  O  O     . GLN A 1 73   ? 101.974 112.260 60.669  1.00 106.01 ? 73   GLN A O     1 
ATOM   417  C  CB    . GLN A 1 73   ? 103.227 110.385 62.730  1.00 106.01 ? 73   GLN A CB    1 
ATOM   418  C  CG    . GLN A 1 73   ? 104.040 109.997 61.506  1.00 106.01 ? 73   GLN A CG    1 
ATOM   419  C  CD    . GLN A 1 73   ? 103.956 108.516 61.201  1.00 106.01 ? 73   GLN A CD    1 
ATOM   420  O  OE1   . GLN A 1 73   ? 103.204 107.781 61.840  1.00 106.01 ? 73   GLN A OE1   1 
ATOM   421  N  NE2   . GLN A 1 73   ? 104.730 108.069 60.219  1.00 106.01 ? 73   GLN A NE2   1 
ATOM   422  N  N     . MET A 1 74   ? 101.001 110.295 60.142  1.00 108.52 ? 74   MET A N     1 
ATOM   423  C  CA    . MET A 1 74   ? 100.796 110.680 58.750  1.00 108.52 ? 74   MET A CA    1 
ATOM   424  C  C     . MET A 1 74   ? 99.860  111.877 58.639  1.00 108.52 ? 74   MET A C     1 
ATOM   425  O  O     . MET A 1 74   ? 100.098 112.788 57.838  1.00 108.52 ? 74   MET A O     1 
ATOM   426  C  CB    . MET A 1 74   ? 100.251 109.494 57.955  1.00 108.52 ? 74   MET A CB    1 
ATOM   427  C  CG    . MET A 1 74   ? 101.162 108.279 57.953  1.00 108.52 ? 74   MET A CG    1 
ATOM   428  S  SD    . MET A 1 74   ? 100.733 107.087 59.234  1.00 108.52 ? 74   MET A SD    1 
ATOM   429  C  CE    . MET A 1 74   ? 99.147  106.508 58.639  1.00 108.52 ? 74   MET A CE    1 
ATOM   430  N  N     . ASP A 1 75   ? 98.792  111.894 59.433  1.00 104.31 ? 75   ASP A N     1 
ATOM   431  C  CA    . ASP A 1 75   ? 97.845  113.003 59.456  1.00 104.31 ? 75   ASP A CA    1 
ATOM   432  C  C     . ASP A 1 75   ? 98.115  113.836 60.704  1.00 104.31 ? 75   ASP A C     1 
ATOM   433  O  O     . ASP A 1 75   ? 97.876  113.380 61.827  1.00 104.31 ? 75   ASP A O     1 
ATOM   434  C  CB    . ASP A 1 75   ? 96.406  112.493 59.432  1.00 104.31 ? 75   ASP A CB    1 
ATOM   435  C  CG    . ASP A 1 75   ? 95.461  113.450 58.734  1.00 104.31 ? 75   ASP A CG    1 
ATOM   436  O  OD1   . ASP A 1 75   ? 95.944  114.314 57.972  1.00 104.31 ? 75   ASP A OD1   1 
ATOM   437  O  OD2   . ASP A 1 75   ? 94.235  113.338 58.945  1.00 104.31 ? 75   ASP A OD2   1 
ATOM   438  N  N     . LEU A 1 76   ? 98.617  115.056 60.505  1.00 97.99  ? 76   LEU A N     1 
ATOM   439  C  CA    . LEU A 1 76   ? 98.934  115.921 61.636  1.00 97.99  ? 76   LEU A CA    1 
ATOM   440  C  C     . LEU A 1 76   ? 97.678  116.384 62.364  1.00 97.99  ? 76   LEU A C     1 
ATOM   441  O  O     . LEU A 1 76   ? 97.736  116.698 63.558  1.00 97.99  ? 76   LEU A O     1 
ATOM   442  C  CB    . LEU A 1 76   ? 99.743  117.127 61.159  1.00 97.99  ? 76   LEU A CB    1 
ATOM   443  C  CG    . LEU A 1 76   ? 100.347 118.023 62.242  1.00 97.99  ? 76   LEU A CG    1 
ATOM   444  C  CD1   . LEU A 1 76   ? 101.460 117.297 62.980  1.00 97.99  ? 76   LEU A CD1   1 
ATOM   445  C  CD2   . LEU A 1 76   ? 100.852 119.327 61.647  1.00 97.99  ? 76   LEU A CD2   1 
ATOM   446  N  N     . HIS A 1 77   ? 96.540  116.428 61.667  1.00 97.71  ? 77   HIS A N     1 
ATOM   447  C  CA    . HIS A 1 77   ? 95.317  116.942 62.274  1.00 97.71  ? 77   HIS A CA    1 
ATOM   448  C  C     . HIS A 1 77   ? 94.848  116.053 63.421  1.00 97.71  ? 77   HIS A C     1 
ATOM   449  O  O     . HIS A 1 77   ? 94.366  116.551 64.445  1.00 97.71  ? 77   HIS A O     1 
ATOM   450  C  CB    . HIS A 1 77   ? 94.225  117.075 61.212  1.00 97.71  ? 77   HIS A CB    1 
ATOM   451  C  CG    . HIS A 1 77   ? 92.979  117.745 61.702  1.00 97.71  ? 77   HIS A CG    1 
ATOM   452  N  ND1   . HIS A 1 77   ? 91.799  117.730 60.990  1.00 97.71  ? 77   HIS A ND1   1 
ATOM   453  C  CD2   . HIS A 1 77   ? 92.732  118.460 62.825  1.00 97.71  ? 77   HIS A CD2   1 
ATOM   454  C  CE1   . HIS A 1 77   ? 90.876  118.400 61.657  1.00 97.71  ? 77   HIS A CE1   1 
ATOM   455  N  NE2   . HIS A 1 77   ? 91.416  118.853 62.774  1.00 97.71  ? 77   HIS A NE2   1 
ATOM   456  N  N     . GLN A 1 78   ? 94.969  114.735 63.268  1.00 96.57  ? 78   GLN A N     1 
ATOM   457  C  CA    . GLN A 1 78   ? 94.481  113.817 64.289  1.00 96.57  ? 78   GLN A CA    1 
ATOM   458  C  C     . GLN A 1 78   ? 95.404  113.718 65.498  1.00 96.57  ? 78   GLN A C     1 
ATOM   459  O  O     . GLN A 1 78   ? 94.937  113.363 66.587  1.00 96.57  ? 78   GLN A O     1 
ATOM   460  C  CB    . GLN A 1 78   ? 94.265  112.432 63.678  1.00 96.57  ? 78   GLN A CB    1 
ATOM   461  C  CG    . GLN A 1 78   ? 93.142  112.398 62.653  1.00 96.57  ? 78   GLN A CG    1 
ATOM   462  C  CD    . GLN A 1 78   ? 92.950  111.028 62.040  1.00 96.57  ? 78   GLN A CD    1 
ATOM   463  O  OE1   . GLN A 1 78   ? 93.701  110.097 62.328  1.00 96.57  ? 78   GLN A OE1   1 
ATOM   464  N  NE2   . GLN A 1 78   ? 91.942  110.898 61.185  1.00 96.57  ? 78   GLN A NE2   1 
ATOM   465  N  N     . MET A 1 79   ? 96.693  114.026 65.335  1.00 89.89  ? 79   MET A N     1 
ATOM   466  C  CA    . MET A 1 79   ? 97.621  113.959 66.461  1.00 89.89  ? 79   MET A CA    1 
ATOM   467  C  C     . MET A 1 79   ? 97.207  114.888 67.594  1.00 89.89  ? 79   MET A C     1 
ATOM   468  O  O     . MET A 1 79   ? 97.194  114.482 68.761  1.00 89.89  ? 79   MET A O     1 
ATOM   469  C  CB    . MET A 1 79   ? 99.040  114.281 65.994  1.00 89.89  ? 79   MET A CB    1 
ATOM   470  C  CG    . MET A 1 79   ? 99.843  113.080 65.532  1.00 89.89  ? 79   MET A CG    1 
ATOM   471  S  SD    . MET A 1 79   ? 99.876  111.831 66.837  1.00 89.89  ? 79   MET A SD    1 
ATOM   472  C  CE    . MET A 1 79   ? 100.236 110.336 65.931  1.00 89.89  ? 79   MET A CE    1 
ATOM   473  N  N     . VAL A 1 80   ? 96.873  116.140 67.273  1.00 87.30  ? 80   VAL A N     1 
ATOM   474  C  CA    . VAL A 1 80   ? 96.571  117.107 68.325  1.00 87.30  ? 80   VAL A CA    1 
ATOM   475  C  C     . VAL A 1 80   ? 95.307  116.711 69.080  1.00 87.30  ? 80   VAL A C     1 
ATOM   476  O  O     . VAL A 1 80   ? 95.268  116.758 70.315  1.00 87.30  ? 80   VAL A O     1 
ATOM   477  C  CB    . VAL A 1 80   ? 96.475  118.529 67.740  1.00 87.30  ? 80   VAL A CB    1 
ATOM   478  C  CG1   . VAL A 1 80   ? 97.854  119.027 67.358  1.00 87.30  ? 80   VAL A CG1   1 
ATOM   479  C  CG2   . VAL A 1 80   ? 95.560  118.555 66.530  1.00 87.30  ? 80   VAL A CG2   1 
ATOM   480  N  N     . HIS A 1 81   ? 94.261  116.297 68.358  1.00 86.36  ? 81   HIS A N     1 
ATOM   481  C  CA    . HIS A 1 81   ? 93.036  115.860 69.021  1.00 86.36  ? 81   HIS A CA    1 
ATOM   482  C  C     . HIS A 1 81   ? 93.286  114.629 69.883  1.00 86.36  ? 81   HIS A C     1 
ATOM   483  O  O     . HIS A 1 81   ? 92.809  114.551 71.024  1.00 86.36  ? 81   HIS A O     1 
ATOM   484  C  CB    . HIS A 1 81   ? 91.951  115.573 67.984  1.00 86.36  ? 81   HIS A CB    1 
ATOM   485  C  CG    . HIS A 1 81   ? 91.521  116.777 67.207  1.00 86.36  ? 81   HIS A CG    1 
ATOM   486  N  ND1   . HIS A 1 81   ? 90.872  117.845 67.788  1.00 86.36  ? 81   HIS A ND1   1 
ATOM   487  C  CD2   . HIS A 1 81   ? 91.648  117.084 65.894  1.00 86.36  ? 81   HIS A CD2   1 
ATOM   488  C  CE1   . HIS A 1 81   ? 90.616  118.756 66.866  1.00 86.36  ? 81   HIS A CE1   1 
ATOM   489  N  NE2   . HIS A 1 81   ? 91.077  118.319 65.708  1.00 86.36  ? 81   HIS A NE2   1 
ATOM   490  N  N     . GLU A 1 82   ? 94.041  113.660 69.357  1.00 82.19  ? 82   GLU A N     1 
ATOM   491  C  CA    . GLU A 1 82   ? 94.302  112.438 70.109  1.00 82.19  ? 82   GLU A CA    1 
ATOM   492  C  C     . GLU A 1 82   ? 95.077  112.729 71.388  1.00 82.19  ? 82   GLU A C     1 
ATOM   493  O  O     . GLU A 1 82   ? 94.745  112.205 72.458  1.00 82.19  ? 82   GLU A O     1 
ATOM   494  C  CB    . GLU A 1 82   ? 95.060  111.442 69.234  1.00 82.19  ? 82   GLU A CB    1 
ATOM   495  C  CG    . GLU A 1 82   ? 95.070  110.025 69.773  1.00 82.19  ? 82   GLU A CG    1 
ATOM   496  C  CD    . GLU A 1 82   ? 95.691  109.042 68.802  1.00 82.19  ? 82   GLU A CD    1 
ATOM   497  O  OE1   . GLU A 1 82   ? 96.177  109.483 67.740  1.00 82.19  ? 82   GLU A OE1   1 
ATOM   498  O  OE2   . GLU A 1 82   ? 95.689  107.829 69.097  1.00 82.19  ? 82   GLU A OE2   1 
ATOM   499  N  N     . VAL A 1 83   ? 96.103  113.578 71.306  1.00 76.22  ? 83   VAL A N     1 
ATOM   500  C  CA    . VAL A 1 83   ? 96.922  113.829 72.486  1.00 76.22  ? 83   VAL A CA    1 
ATOM   501  C  C     . VAL A 1 83   ? 96.187  114.730 73.471  1.00 76.22  ? 83   VAL A C     1 
ATOM   502  O  O     . VAL A 1 83   ? 96.408  114.647 74.683  1.00 76.22  ? 83   VAL A O     1 
ATOM   503  C  CB    . VAL A 1 83   ? 98.288  114.411 72.087  1.00 76.22  ? 83   VAL A CB    1 
ATOM   504  C  CG1   . VAL A 1 83   ? 99.057  113.413 71.237  1.00 76.22  ? 83   VAL A CG1   1 
ATOM   505  C  CG2   . VAL A 1 83   ? 98.111  115.707 71.360  1.00 76.22  ? 83   VAL A CG2   1 
ATOM   506  N  N     . SER A 1 84   ? 95.294  115.597 72.984  1.00 72.84  ? 84   SER A N     1 
ATOM   507  C  CA    . SER A 1 84   ? 94.448  116.354 73.901  1.00 72.84  ? 84   SER A CA    1 
ATOM   508  C  C     . SER A 1 84   ? 93.505  115.428 74.661  1.00 72.84  ? 84   SER A C     1 
ATOM   509  O  O     . SER A 1 84   ? 93.318  115.573 75.879  1.00 72.84  ? 84   SER A O     1 
ATOM   510  C  CB    . SER A 1 84   ? 93.661  117.415 73.133  1.00 72.84  ? 84   SER A CB    1 
ATOM   511  O  OG    . SER A 1 84   ? 92.687  116.817 72.297  1.00 72.84  ? 84   SER A OG    1 
ATOM   512  N  N     . ARG A 1 85   ? 92.912  114.459 73.960  1.00 69.82  ? 85   ARG A N     1 
ATOM   513  C  CA    . ARG A 1 85   ? 92.074  113.478 74.639  1.00 69.82  ? 85   ARG A CA    1 
ATOM   514  C  C     . ARG A 1 85   ? 92.883  112.686 75.657  1.00 69.82  ? 85   ARG A C     1 
ATOM   515  O  O     . ARG A 1 85   ? 92.400  112.389 76.755  1.00 69.82  ? 85   ARG A O     1 
ATOM   516  C  CB    . ARG A 1 85   ? 91.426  112.539 73.623  1.00 69.82  ? 85   ARG A CB    1 
ATOM   517  C  CG    . ARG A 1 85   ? 90.261  113.149 72.857  1.00 69.82  ? 85   ARG A CG    1 
ATOM   518  C  CD    . ARG A 1 85   ? 89.418  112.156 72.023  1.00 69.82  ? 85   ARG A CD    1 
ATOM   519  N  NE    . ARG A 1 85   ? 90.161  111.102 71.326  1.00 69.82  ? 85   ARG A NE    1 
ATOM   520  C  CZ    . ARG A 1 85   ? 90.593  109.970 71.879  1.00 69.82  ? 85   ARG A CZ    1 
ATOM   521  N  NH1   . ARG A 1 85   ? 91.263  109.091 71.148  1.00 69.82  ? 85   ARG A NH1   1 
ATOM   522  N  NH2   . ARG A 1 85   ? 90.320  109.693 73.148  1.00 69.82  ? 85   ARG A NH2   1 
ATOM   523  N  N     . TYR A 1 86   ? 94.123  112.336 75.311  1.00 67.58  ? 86   TYR A N     1 
ATOM   524  C  CA    . TYR A 1 86   ? 94.954  111.594 76.253  1.00 67.58  ? 86   TYR A CA    1 
ATOM   525  C  C     . TYR A 1 86   ? 95.364  112.451 77.445  1.00 67.58  ? 86   TYR A C     1 
ATOM   526  O  O     . TYR A 1 86   ? 95.516  111.930 78.553  1.00 67.58  ? 86   TYR A O     1 
ATOM   527  C  CB    . TYR A 1 86   ? 96.174  111.023 75.536  1.00 67.58  ? 86   TYR A CB    1 
ATOM   528  C  CG    . TYR A 1 86   ? 95.839  109.770 74.764  1.00 67.58  ? 86   TYR A CG    1 
ATOM   529  C  CD1   . TYR A 1 86   ? 94.799  108.946 75.170  1.00 67.58  ? 86   TYR A CD1   1 
ATOM   530  C  CD2   . TYR A 1 86   ? 96.544  109.418 73.625  1.00 67.58  ? 86   TYR A CD2   1 
ATOM   531  C  CE1   . TYR A 1 86   ? 94.478  107.803 74.472  1.00 67.58  ? 86   TYR A CE1   1 
ATOM   532  C  CE2   . TYR A 1 86   ? 96.228  108.276 72.918  1.00 67.58  ? 86   TYR A CE2   1 
ATOM   533  C  CZ    . TYR A 1 86   ? 95.196  107.472 73.347  1.00 67.58  ? 86   TYR A CZ    1 
ATOM   534  O  OH    . TYR A 1 86   ? 94.880  106.333 72.645  1.00 67.58  ? 86   TYR A OH    1 
ATOM   535  N  N     . SER A 1 87   ? 95.539  113.758 77.247  1.00 56.63  ? 87   SER A N     1 
ATOM   536  C  CA    . SER A 1 87   ? 95.758  114.651 78.380  1.00 56.63  ? 87   SER A CA    1 
ATOM   537  C  C     . SER A 1 87   ? 94.542  114.674 79.298  1.00 56.63  ? 87   SER A C     1 
ATOM   538  O  O     . SER A 1 87   ? 94.677  114.673 80.529  1.00 56.63  ? 87   SER A O     1 
ATOM   539  C  CB    . SER A 1 87   ? 96.086  116.057 77.882  1.00 56.63  ? 87   SER A CB    1 
ATOM   540  O  OG    . SER A 1 87   ? 96.257  116.955 78.963  1.00 56.63  ? 87   SER A OG    1 
ATOM   541  N  N     . LEU A 1 88   ? 93.342  114.691 78.715  1.00 53.45  ? 88   LEU A N     1 
ATOM   542  C  CA    . LEU A 1 88   ? 92.131  114.612 79.530  1.00 53.45  ? 88   LEU A CA    1 
ATOM   543  C  C     . LEU A 1 88   ? 92.068  113.294 80.298  1.00 53.45  ? 88   LEU A C     1 
ATOM   544  O  O     . LEU A 1 88   ? 91.671  113.262 81.471  1.00 53.45  ? 88   LEU A O     1 
ATOM   545  C  CB    . LEU A 1 88   ? 90.893  114.785 78.652  1.00 53.45  ? 88   LEU A CB    1 
ATOM   546  C  CG    . LEU A 1 88   ? 89.570  114.946 79.401  1.00 53.45  ? 88   LEU A CG    1 
ATOM   547  C  CD1   . LEU A 1 88   ? 89.539  116.264 80.155  1.00 53.45  ? 88   LEU A CD1   1 
ATOM   548  C  CD2   . LEU A 1 88   ? 88.398  114.847 78.440  1.00 53.45  ? 88   LEU A CD2   1 
ATOM   549  N  N     . TYR A 1 89   ? 92.452  112.194 79.648  1.00 54.60  ? 89   TYR A N     1 
ATOM   550  C  CA    . TYR A 1 89   ? 92.502  110.904 80.333  1.00 54.60  ? 89   TYR A CA    1 
ATOM   551  C  C     . TYR A 1 89   ? 93.521  110.918 81.467  1.00 54.60  ? 89   TYR A C     1 
ATOM   552  O  O     . TYR A 1 89   ? 93.300  110.311 82.522  1.00 54.60  ? 89   TYR A O     1 
ATOM   553  C  CB    . TYR A 1 89   ? 92.821  109.784 79.342  1.00 54.60  ? 89   TYR A CB    1 
ATOM   554  C  CG    . TYR A 1 89   ? 91.691  109.413 78.401  1.00 54.60  ? 89   TYR A CG    1 
ATOM   555  C  CD1   . TYR A 1 89   ? 91.605  108.134 77.869  1.00 54.60  ? 89   TYR A CD1   1 
ATOM   556  C  CD2   . TYR A 1 89   ? 90.700  110.326 78.067  1.00 54.60  ? 89   TYR A CD2   1 
ATOM   557  C  CE1   . TYR A 1 89   ? 90.579  107.782 77.015  1.00 54.60  ? 89   TYR A CE1   1 
ATOM   558  C  CE2   . TYR A 1 89   ? 89.671  109.984 77.213  1.00 54.60  ? 89   TYR A CE2   1 
ATOM   559  C  CZ    . TYR A 1 89   ? 89.614  108.710 76.691  1.00 54.60  ? 89   TYR A CZ    1 
ATOM   560  O  OH    . TYR A 1 89   ? 88.588  108.363 75.843  1.00 54.60  ? 89   TYR A OH    1 
ATOM   561  N  N     . PHE A 1 90   ? 94.652  111.593 81.262  1.00 50.23  ? 90   PHE A N     1 
ATOM   562  C  CA    . PHE A 1 90   ? 95.650  111.694 82.320  1.00 50.23  ? 90   PHE A CA    1 
ATOM   563  C  C     . PHE A 1 90   ? 95.109  112.501 83.495  1.00 50.23  ? 90   PHE A C     1 
ATOM   564  O  O     . PHE A 1 90   ? 95.397  112.195 84.657  1.00 50.23  ? 90   PHE A O     1 
ATOM   565  C  CB    . PHE A 1 90   ? 96.933  112.318 81.771  1.00 50.23  ? 90   PHE A CB    1 
ATOM   566  C  CG    . PHE A 1 90   ? 98.061  112.357 82.758  1.00 50.23  ? 90   PHE A CG    1 
ATOM   567  C  CD1   . PHE A 1 90   ? 98.778  111.210 83.048  1.00 50.23  ? 90   PHE A CD1   1 
ATOM   568  C  CD2   . PHE A 1 90   ? 98.409  113.533 83.396  1.00 50.23  ? 90   PHE A CD2   1 
ATOM   569  C  CE1   . PHE A 1 90   ? 99.819  111.233 83.952  1.00 50.23  ? 90   PHE A CE1   1 
ATOM   570  C  CE2   . PHE A 1 90   ? 99.451  113.560 84.303  1.00 50.23  ? 90   PHE A CE2   1 
ATOM   571  C  CZ    . PHE A 1 90   ? 100.155 112.409 84.581  1.00 50.23  ? 90   PHE A CZ    1 
ATOM   572  N  N     . VAL A 1 91   ? 94.306  113.528 83.209  1.00 47.37  ? 91   VAL A N     1 
ATOM   573  C  CA    . VAL A 1 91   ? 93.634  114.265 84.279  1.00 47.37  ? 91   VAL A CA    1 
ATOM   574  C  C     . VAL A 1 91   ? 92.663  113.358 85.030  1.00 47.37  ? 91   VAL A C     1 
ATOM   575  O  O     . VAL A 1 91   ? 92.558  113.415 86.263  1.00 47.37  ? 91   VAL A O     1 
ATOM   576  C  CB    . VAL A 1 91   ? 92.921  115.507 83.712  1.00 47.37  ? 91   VAL A CB    1 
ATOM   577  C  CG1   . VAL A 1 91   ? 92.119  116.201 84.801  1.00 47.37  ? 91   VAL A CG1   1 
ATOM   578  C  CG2   . VAL A 1 91   ? 93.929  116.464 83.112  1.00 47.37  ? 91   VAL A CG2   1 
ATOM   579  N  N     . TYR A 1 92   ? 91.920  112.525 84.297  1.00 47.75  ? 92   TYR A N     1 
ATOM   580  C  CA    . TYR A 1 92   ? 91.027  111.570 84.952  1.00 47.75  ? 92   TYR A CA    1 
ATOM   581  C  C     . TYR A 1 92   ? 91.804  110.640 85.874  1.00 47.75  ? 92   TYR A C     1 
ATOM   582  O  O     . TYR A 1 92   ? 91.376  110.361 87.002  1.00 47.75  ? 92   TYR A O     1 
ATOM   583  C  CB    . TYR A 1 92   ? 90.259  110.756 83.911  1.00 47.75  ? 92   TYR A CB    1 
ATOM   584  C  CG    . TYR A 1 92   ? 89.180  111.518 83.179  1.00 47.75  ? 92   TYR A CG    1 
ATOM   585  C  CD1   . TYR A 1 92   ? 88.921  112.851 83.466  1.00 47.75  ? 92   TYR A CD1   1 
ATOM   586  C  CD2   . TYR A 1 92   ? 88.415  110.898 82.201  1.00 47.75  ? 92   TYR A CD2   1 
ATOM   587  C  CE1   . TYR A 1 92   ? 87.934  113.545 82.796  1.00 47.75  ? 92   TYR A CE1   1 
ATOM   588  C  CE2   . TYR A 1 92   ? 87.427  111.583 81.526  1.00 47.75  ? 92   TYR A CE2   1 
ATOM   589  C  CZ    . TYR A 1 92   ? 87.190  112.906 81.827  1.00 47.75  ? 92   TYR A CZ    1 
ATOM   590  O  OH    . TYR A 1 92   ? 86.205  113.591 81.156  1.00 47.75  ? 92   TYR A OH    1 
ATOM   591  N  N     . LEU A 1 93   ? 92.953  110.151 85.406  1.00 43.83  ? 93   LEU A N     1 
ATOM   592  C  CA    . LEU A 1 93   ? 93.807  109.328 86.254  1.00 43.83  ? 93   LEU A CA    1 
ATOM   593  C  C     . LEU A 1 93   ? 94.282  110.108 87.471  1.00 43.83  ? 93   LEU A C     1 
ATOM   594  O  O     . LEU A 1 93   ? 94.433  109.544 88.560  1.00 43.83  ? 93   LEU A O     1 
ATOM   595  C  CB    . LEU A 1 93   ? 95.005  108.811 85.462  1.00 43.83  ? 93   LEU A CB    1 
ATOM   596  C  CG    . LEU A 1 93   ? 95.858  107.798 86.224  1.00 43.83  ? 93   LEU A CG    1 
ATOM   597  C  CD1   . LEU A 1 93   ? 95.245  106.408 86.149  1.00 43.83  ? 93   LEU A CD1   1 
ATOM   598  C  CD2   . LEU A 1 93   ? 97.292  107.801 85.732  1.00 43.83  ? 93   LEU A CD2   1 
ATOM   599  N  N     . GLY A 1 94   ? 94.545  111.403 87.299  1.00 42.74  ? 94   GLY A N     1 
ATOM   600  C  CA    . GLY A 1 94   ? 94.919  112.226 88.436  1.00 42.74  ? 94   GLY A CA    1 
ATOM   601  C  C     . GLY A 1 94   ? 93.833  112.282 89.492  1.00 42.74  ? 94   GLY A C     1 
ATOM   602  O  O     . GLY A 1 94   ? 94.108  112.149 90.687  1.00 42.74  ? 94   GLY A O     1 
ATOM   603  N  N     . LEU A 1 95   ? 92.583  112.467 89.065  1.00 41.55  ? 95   LEU A N     1 
ATOM   604  C  CA    . LEU A 1 95   ? 91.467  112.428 90.012  1.00 41.55  ? 95   LEU A CA    1 
ATOM   605  C  C     . LEU A 1 95   ? 91.363  111.065 90.689  1.00 41.55  ? 95   LEU A C     1 
ATOM   606  O  O     . LEU A 1 95   ? 91.118  110.976 91.900  1.00 41.55  ? 95   LEU A O     1 
ATOM   607  C  CB    . LEU A 1 95   ? 90.144  112.785 89.327  1.00 41.55  ? 95   LEU A CB    1 
ATOM   608  C  CG    . LEU A 1 95   ? 89.759  114.226 88.961  1.00 41.55  ? 95   LEU A CG    1 
ATOM   609  C  CD1   . LEU A 1 95   ? 90.827  114.989 88.202  1.00 41.55  ? 95   LEU A CD1   1 
ATOM   610  C  CD2   . LEU A 1 95   ? 88.448  114.228 88.184  1.00 41.55  ? 95   LEU A CD2   1 
ATOM   611  N  N     . VAL A 1 96   ? 91.536  109.988 89.919  1.00 36.71  ? 96   VAL A N     1 
ATOM   612  C  CA    . VAL A 1 96   ? 91.428  108.647 90.493  1.00 36.71  ? 96   VAL A CA    1 
ATOM   613  C  C     . VAL A 1 96   ? 92.500  108.429 91.556  1.00 36.71  ? 96   VAL A C     1 
ATOM   614  O  O     . VAL A 1 96   ? 92.224  107.900 92.640  1.00 36.71  ? 96   VAL A O     1 
ATOM   615  C  CB    . VAL A 1 96   ? 91.503  107.579 89.386  1.00 36.71  ? 96   VAL A CB    1 
ATOM   616  C  CG1   . VAL A 1 96   ? 91.636  106.194 89.994  1.00 36.71  ? 96   VAL A CG1   1 
ATOM   617  C  CG2   . VAL A 1 96   ? 90.273  107.653 88.496  1.00 36.71  ? 96   VAL A CG2   1 
ATOM   618  N  N     . VAL A 1 97   ? 93.735  108.841 91.266  1.00 35.70  ? 97   VAL A N     1 
ATOM   619  C  CA    . VAL A 1 97   ? 94.826  108.676 92.223  1.00 35.70  ? 97   VAL A CA    1 
ATOM   620  C  C     . VAL A 1 97   ? 94.602  109.554 93.448  1.00 35.70  ? 97   VAL A C     1 
ATOM   621  O  O     . VAL A 1 97   ? 94.875  109.142 94.583  1.00 35.70  ? 97   VAL A O     1 
ATOM   622  C  CB    . VAL A 1 97   ? 96.178  108.972 91.547  1.00 35.70  ? 97   VAL A CB    1 
ATOM   623  C  CG1   . VAL A 1 97   ? 97.248  109.263 92.587  1.00 35.70  ? 97   VAL A CG1   1 
ATOM   624  C  CG2   . VAL A 1 97   ? 96.595  107.804 90.669  1.00 35.70  ? 97   VAL A CG2   1 
ATOM   625  N  N     . CYS A 1 98   ? 94.098  110.774 93.244  1.00 39.03  ? 98   CYS A N     1 
ATOM   626  C  CA    . CYS A 1 98   ? 93.819  111.660 94.369  1.00 39.03  ? 98   CYS A CA    1 
ATOM   627  C  C     . CYS A 1 98   ? 92.779  111.054 95.301  1.00 39.03  ? 98   CYS A C     1 
ATOM   628  O  O     . CYS A 1 98   ? 92.915  111.117 96.528  1.00 39.03  ? 98   CYS A O     1 
ATOM   629  C  CB    . CYS A 1 98   ? 93.349  113.022 93.858  1.00 39.03  ? 98   CYS A CB    1 
ATOM   630  S  SG    . CYS A 1 98   ? 92.728  114.122 95.150  1.00 39.03  ? 98   CYS A SG    1 
ATOM   631  N  N     . PHE A 1 99   ? 91.723  110.470 94.733  1.00 39.40  ? 99   PHE A N     1 
ATOM   632  C  CA    . PHE A 1 99   ? 90.709  109.826 95.563  1.00 39.40  ? 99   PHE A CA    1 
ATOM   633  C  C     . PHE A 1 99   ? 91.268  108.592 96.264  1.00 39.40  ? 99   PHE A C     1 
ATOM   634  O  O     . PHE A 1 99   ? 90.976  108.347 97.440  1.00 39.40  ? 99   PHE A O     1 
ATOM   635  C  CB    . PHE A 1 99   ? 89.488  109.462 94.719  1.00 39.40  ? 99   PHE A CB    1 
ATOM   636  C  CG    . PHE A 1 99   ? 88.662  110.646 94.308  1.00 39.40  ? 99   PHE A CG    1 
ATOM   637  C  CD1   . PHE A 1 99   ? 88.822  111.872 94.935  1.00 39.40  ? 99   PHE A CD1   1 
ATOM   638  C  CD2   . PHE A 1 99   ? 87.719  110.532 93.301  1.00 39.40  ? 99   PHE A CD2   1 
ATOM   639  C  CE1   . PHE A 1 99   ? 88.062  112.962 94.560  1.00 39.40  ? 99   PHE A CE1   1 
ATOM   640  C  CE2   . PHE A 1 99   ? 86.955  111.619 92.921  1.00 39.40  ? 99   PHE A CE2   1 
ATOM   641  C  CZ    . PHE A 1 99   ? 87.127  112.835 93.552  1.00 39.40  ? 99   PHE A CZ    1 
ATOM   642  N  N     . SER A 1 100  ? 92.075  107.799 95.554  1.00 33.66  ? 100  SER A N     1 
ATOM   643  C  CA    . SER A 1 100  ? 92.601  106.570 96.143  1.00 33.66  ? 100  SER A CA    1 
ATOM   644  C  C     . SER A 1 100  ? 93.616  106.863 97.241  1.00 33.66  ? 100  SER A C     1 
ATOM   645  O  O     . SER A 1 100  ? 93.621  106.198 98.283  1.00 33.66  ? 100  SER A O     1 
ATOM   646  C  CB    . SER A 1 100  ? 93.225  105.694 95.059  1.00 33.66  ? 100  SER A CB    1 
ATOM   647  O  OG    . SER A 1 100  ? 92.248  105.268 94.127  1.00 33.66  ? 100  SER A OG    1 
ATOM   648  N  N     . SER A 1 101  ? 94.489  107.850 97.025  1.00 33.42  ? 101  SER A N     1 
ATOM   649  C  CA    . SER A 1 101  ? 95.526  108.145 98.010  1.00 33.42  ? 101  SER A CA    1 
ATOM   650  C  C     . SER A 1 101  ? 94.924  108.663 99.309  1.00 33.42  ? 101  SER A C     1 
ATOM   651  O  O     . SER A 1 101  ? 95.494  108.465 100.388 1.00 33.42  ? 101  SER A O     1 
ATOM   652  C  CB    . SER A 1 101  ? 96.522  109.153 97.441  1.00 33.42  ? 101  SER A CB    1 
ATOM   653  O  OG    . SER A 1 101  ? 95.937  110.438 97.329  1.00 33.42  ? 101  SER A OG    1 
ATOM   654  N  N     . TYR A 1 102  ? 93.779  109.342 99.227  1.00 35.23  ? 102  TYR A N     1 
ATOM   655  C  CA    . TYR A 1 102  ? 93.106  109.813 100.433 1.00 35.23  ? 102  TYR A CA    1 
ATOM   656  C  C     . TYR A 1 102  ? 92.661  108.652 101.312 1.00 35.23  ? 102  TYR A C     1 
ATOM   657  O  O     . TYR A 1 102  ? 92.800  108.697 102.539 1.00 35.23  ? 102  TYR A O     1 
ATOM   658  C  CB    . TYR A 1 102  ? 91.906  110.682 100.061 1.00 35.23  ? 102  TYR A CB    1 
ATOM   659  C  CG    . TYR A 1 102  ? 91.177  111.236 101.261 1.00 35.23  ? 102  TYR A CG    1 
ATOM   660  C  CD1   . TYR A 1 102  ? 91.700  112.293 101.989 1.00 35.23  ? 102  TYR A CD1   1 
ATOM   661  C  CD2   . TYR A 1 102  ? 89.966  110.695 101.672 1.00 35.23  ? 102  TYR A CD2   1 
ATOM   662  C  CE1   . TYR A 1 102  ? 91.039  112.800 103.088 1.00 35.23  ? 102  TYR A CE1   1 
ATOM   663  C  CE2   . TYR A 1 102  ? 89.297  111.194 102.770 1.00 35.23  ? 102  TYR A CE2   1 
ATOM   664  C  CZ    . TYR A 1 102  ? 89.838  112.247 103.474 1.00 35.23  ? 102  TYR A CZ    1 
ATOM   665  O  OH    . TYR A 1 102  ? 89.175  112.750 104.569 1.00 35.23  ? 102  TYR A OH    1 
ATOM   666  N  N     . ALA A 1 103  ? 92.112  107.604 100.697 1.00 31.52  ? 103  ALA A N     1 
ATOM   667  C  CA    . ALA A 1 103  ? 91.540  106.508 101.471 1.00 31.52  ? 103  ALA A CA    1 
ATOM   668  C  C     . ALA A 1 103  ? 92.616  105.740 102.228 1.00 31.52  ? 103  ALA A C     1 
ATOM   669  O  O     . ALA A 1 103  ? 92.473  105.466 103.424 1.00 31.52  ? 103  ALA A O     1 
ATOM   670  C  CB    . ALA A 1 103  ? 90.756  105.573 100.551 1.00 31.52  ? 103  ALA A CB    1 
ATOM   671  N  N     . GLU A 1 104  ? 93.708  105.388 101.548 1.00 29.50  ? 104  GLU A N     1 
ATOM   672  C  CA    . GLU A 1 104  ? 94.689  104.496 102.157 1.00 29.50  ? 104  GLU A CA    1 
ATOM   673  C  C     . GLU A 1 104  ? 95.545  105.218 103.192 1.00 29.50  ? 104  GLU A C     1 
ATOM   674  O  O     . GLU A 1 104  ? 96.027  104.596 104.144 1.00 29.50  ? 104  GLU A O     1 
ATOM   675  C  CB    . GLU A 1 104  ? 95.558  103.851 101.076 1.00 29.50  ? 104  GLU A CB    1 
ATOM   676  C  CG    . GLU A 1 104  ? 96.355  104.813 100.216 1.00 29.50  ? 104  GLU A CG    1 
ATOM   677  C  CD    . GLU A 1 104  ? 97.785  104.966 100.691 1.00 29.50  ? 104  GLU A CD    1 
ATOM   678  O  OE1   . GLU A 1 104  ? 98.228  104.138 101.513 1.00 29.50  ? 104  GLU A OE1   1 
ATOM   679  O  OE2   . GLU A 1 104  ? 98.471  105.900 100.228 1.00 29.50  ? 104  GLU A OE2   1 
ATOM   680  N  N     . ILE A 1 105  ? 95.755  106.524 103.023 1.00 28.61  ? 105  ILE A N     1 
ATOM   681  C  CA    . ILE A 1 105  ? 96.540  107.275 104.001 1.00 28.61  ? 105  ILE A CA    1 
ATOM   682  C  C     . ILE A 1 105  ? 95.727  107.519 105.267 1.00 28.61  ? 105  ILE A C     1 
ATOM   683  O  O     . ILE A 1 105  ? 96.210  107.314 106.387 1.00 28.61  ? 105  ILE A O     1 
ATOM   684  C  CB    . ILE A 1 105  ? 97.043  108.595 103.392 1.00 28.61  ? 105  ILE A CB    1 
ATOM   685  C  CG1   . ILE A 1 105  ? 98.130  108.320 102.354 1.00 28.61  ? 105  ILE A CG1   1 
ATOM   686  C  CG2   . ILE A 1 105  ? 97.574  109.513 104.478 1.00 28.61  ? 105  ILE A CG2   1 
ATOM   687  C  CD1   . ILE A 1 105  ? 99.318  107.570 102.905 1.00 28.61  ? 105  ILE A CD1   1 
ATOM   688  N  N     . ALA A 1 106  ? 94.479  107.964 105.108 1.00 29.45  ? 106  ALA A N     1 
ATOM   689  C  CA    . ALA A 1 106  ? 93.670  108.329 106.267 1.00 29.45  ? 106  ALA A CA    1 
ATOM   690  C  C     . ALA A 1 106  ? 93.271  107.102 107.077 1.00 29.45  ? 106  ALA A C     1 
ATOM   691  O  O     . ALA A 1 106  ? 93.350  107.106 108.311 1.00 29.45  ? 106  ALA A O     1 
ATOM   692  C  CB    . ALA A 1 106  ? 92.432  109.103 105.819 1.00 29.45  ? 106  ALA A CB    1 
ATOM   693  N  N     . CYS A 1 107  ? 92.828  106.041 106.399 1.00 28.22  ? 107  CYS A N     1 
ATOM   694  C  CA    . CYS A 1 107  ? 92.363  104.853 107.109 1.00 28.22  ? 107  CYS A CA    1 
ATOM   695  C  C     . CYS A 1 107  ? 93.497  104.174 107.867 1.00 28.22  ? 107  CYS A C     1 
ATOM   696  O  O     . CYS A 1 107  ? 93.305  103.710 108.996 1.00 28.22  ? 107  CYS A O     1 
ATOM   697  C  CB    . CYS A 1 107  ? 91.710  103.879 106.131 1.00 28.22  ? 107  CYS A CB    1 
ATOM   698  S  SG    . CYS A 1 107  ? 90.145  104.466 105.447 1.00 28.22  ? 107  CYS A SG    1 
ATOM   699  N  N     . TRP A 1 108  ? 94.683  104.097 107.261 1.00 25.83  ? 108  TRP A N     1 
ATOM   700  C  CA    . TRP A 1 108  ? 95.804  103.440 107.926 1.00 25.83  ? 108  TRP A CA    1 
ATOM   701  C  C     . TRP A 1 108  ? 96.279  104.232 109.137 1.00 25.83  ? 108  TRP A C     1 
ATOM   702  O  O     . TRP A 1 108  ? 96.587  103.649 110.182 1.00 25.83  ? 108  TRP A O     1 
ATOM   703  C  CB    . TRP A 1 108  ? 96.951  103.227 106.940 1.00 25.83  ? 108  TRP A CB    1 
ATOM   704  C  CG    . TRP A 1 108  ? 96.924  101.890 106.275 1.00 25.83  ? 108  TRP A CG    1 
ATOM   705  C  CD1   . TRP A 1 108  ? 96.769  101.642 104.944 1.00 25.83  ? 108  TRP A CD1   1 
ATOM   706  C  CD2   . TRP A 1 108  ? 97.060  100.613 106.908 1.00 25.83  ? 108  TRP A CD2   1 
ATOM   707  N  NE1   . TRP A 1 108  ? 96.798  100.290 104.708 1.00 25.83  ? 108  TRP A NE1   1 
ATOM   708  C  CE2   . TRP A 1 108  ? 96.977  99.636  105.898 1.00 25.83  ? 108  TRP A CE2   1 
ATOM   709  C  CE3   . TRP A 1 108  ? 97.245  100.201 108.230 1.00 25.83  ? 108  TRP A CE3   1 
ATOM   710  C  CZ2   . TRP A 1 108  ? 97.071  98.274  106.168 1.00 25.83  ? 108  TRP A CZ2   1 
ATOM   711  C  CZ3   . TRP A 1 108  ? 97.337  98.848  108.496 1.00 25.83  ? 108  TRP A CZ3   1 
ATOM   712  C  CH2   . TRP A 1 108  ? 97.251  97.901  107.471 1.00 25.83  ? 108  TRP A CH2   1 
ATOM   713  N  N     . MET A 1 109  ? 96.357  105.559 109.017 1.00 27.58  ? 109  MET A N     1 
ATOM   714  C  CA    . MET A 1 109  ? 96.811  106.368 110.144 1.00 27.58  ? 109  MET A CA    1 
ATOM   715  C  C     . MET A 1 109  ? 95.842  106.281 111.316 1.00 27.58  ? 109  MET A C     1 
ATOM   716  O  O     . MET A 1 109  ? 96.265  106.203 112.475 1.00 27.58  ? 109  MET A O     1 
ATOM   717  C  CB    . MET A 1 109  ? 97.002  107.820 109.713 1.00 27.58  ? 109  MET A CB    1 
ATOM   718  C  CG    . MET A 1 109  ? 98.249  108.471 110.289 1.00 27.58  ? 109  MET A CG    1 
ATOM   719  S  SD    . MET A 1 109  ? 98.687  110.008 109.459 1.00 27.58  ? 109  MET A SD    1 
ATOM   720  C  CE    . MET A 1 109  ? 99.295  109.386 107.896 1.00 27.58  ? 109  MET A CE    1 
ATOM   721  N  N     . TYR A 1 110  ? 94.537  106.306 111.037 1.00 28.35  ? 110  TYR A N     1 
ATOM   722  C  CA    . TYR A 1 110  ? 93.554  106.189 112.109 1.00 28.35  ? 110  TYR A CA    1 
ATOM   723  C  C     . TYR A 1 110  ? 93.620  104.821 112.775 1.00 28.35  ? 110  TYR A C     1 
ATOM   724  O  O     . TYR A 1 110  ? 93.519  104.716 114.003 1.00 28.35  ? 110  TYR A O     1 
ATOM   725  C  CB    . TYR A 1 110  ? 92.151  106.453 111.570 1.00 28.35  ? 110  TYR A CB    1 
ATOM   726  C  CG    . TYR A 1 110  ? 91.126  106.693 112.652 1.00 28.35  ? 110  TYR A CG    1 
ATOM   727  C  CD1   . TYR A 1 110  ? 91.454  107.400 113.800 1.00 28.35  ? 110  TYR A CD1   1 
ATOM   728  C  CD2   . TYR A 1 110  ? 89.833  106.208 112.529 1.00 28.35  ? 110  TYR A CD2   1 
ATOM   729  C  CE1   . TYR A 1 110  ? 90.522  107.619 114.794 1.00 28.35  ? 110  TYR A CE1   1 
ATOM   730  C  CE2   . TYR A 1 110  ? 88.894  106.422 113.518 1.00 28.35  ? 110  TYR A CE2   1 
ATOM   731  C  CZ    . TYR A 1 110  ? 89.243  107.129 114.648 1.00 28.35  ? 110  TYR A CZ    1 
ATOM   732  O  OH    . TYR A 1 110  ? 88.310  107.344 115.634 1.00 28.35  ? 110  TYR A OH    1 
ATOM   733  N  N     . SER A 1 111  ? 93.783  103.761 111.983 1.00 26.89  ? 111  SER A N     1 
ATOM   734  C  CA    . SER A 1 111  ? 93.857  102.420 112.552 1.00 26.89  ? 111  SER A CA    1 
ATOM   735  C  C     . SER A 1 111  ? 95.096  102.256 113.422 1.00 26.89  ? 111  SER A C     1 
ATOM   736  O  O     . SER A 1 111  ? 95.044  101.608 114.473 1.00 26.89  ? 111  SER A O     1 
ATOM   737  C  CB    . SER A 1 111  ? 93.844  101.375 111.438 1.00 26.89  ? 111  SER A CB    1 
ATOM   738  O  OG    . SER A 1 111  ? 93.949  100.067 111.971 1.00 26.89  ? 111  SER A OG    1 
ATOM   739  N  N     . GLY A 1 112  ? 96.222  102.827 112.995 1.00 25.75  ? 112  GLY A N     1 
ATOM   740  C  CA    . GLY A 1 112  ? 97.438  102.716 113.783 1.00 25.75  ? 112  GLY A CA    1 
ATOM   741  C  C     . GLY A 1 112  ? 97.341  103.424 115.120 1.00 25.75  ? 112  GLY A C     1 
ATOM   742  O  O     . GLY A 1 112  ? 97.823  102.920 116.136 1.00 25.75  ? 112  GLY A O     1 
ATOM   743  N  N     . GLU A 1 113  ? 96.723  104.607 115.137 1.00 29.63  ? 113  GLU A N     1 
ATOM   744  C  CA    . GLU A 1 113  ? 96.602  105.363 116.380 1.00 29.63  ? 113  GLU A CA    1 
ATOM   745  C  C     . GLU A 1 113  ? 95.706  104.642 117.381 1.00 29.63  ? 113  GLU A C     1 
ATOM   746  O  O     . GLU A 1 113  ? 95.976  104.644 118.587 1.00 29.63  ? 113  GLU A O     1 
ATOM   747  C  CB    . GLU A 1 113  ? 96.069  106.765 116.090 1.00 29.63  ? 113  GLU A CB    1 
ATOM   748  C  CG    . GLU A 1 113  ? 95.940  107.654 117.320 1.00 29.63  ? 113  GLU A CG    1 
ATOM   749  C  CD    . GLU A 1 113  ? 97.261  107.869 118.040 1.00 29.63  ? 113  GLU A CD    1 
ATOM   750  O  OE1   . GLU A 1 113  ? 97.944  108.871 117.742 1.00 29.63  ? 113  GLU A OE1   1 
ATOM   751  O  OE2   . GLU A 1 113  ? 97.609  107.048 118.914 1.00 29.63  ? 113  GLU A OE2   1 
ATOM   752  N  N     . ARG A 1 114  ? 94.621  104.033 116.899 1.00 28.77  ? 114  ARG A N     1 
ATOM   753  C  CA    . ARG A 1 114  ? 93.723  103.312 117.797 1.00 28.77  ? 114  ARG A CA    1 
ATOM   754  C  C     . ARG A 1 114  ? 94.409  102.104 118.422 1.00 28.77  ? 114  ARG A C     1 
ATOM   755  O  O     . ARG A 1 114  ? 94.249  101.841 119.619 1.00 28.77  ? 114  ARG A O     1 
ATOM   756  C  CB    . ARG A 1 114  ? 92.465  102.879 117.046 1.00 28.77  ? 114  ARG A CB    1 
ATOM   757  C  CG    . ARG A 1 114  ? 91.411  103.961 116.918 1.00 28.77  ? 114  ARG A CG    1 
ATOM   758  C  CD    . ARG A 1 114  ? 90.048  103.357 116.636 1.00 28.77  ? 114  ARG A CD    1 
ATOM   759  N  NE    . ARG A 1 114  ? 89.594  102.511 117.735 1.00 28.77  ? 114  ARG A NE    1 
ATOM   760  C  CZ    . ARG A 1 114  ? 88.525  101.723 117.679 1.00 28.77  ? 114  ARG A CZ    1 
ATOM   761  N  NH1   . ARG A 1 114  ? 87.796  101.671 116.575 1.00 28.77  ? 114  ARG A NH1   1 
ATOM   762  N  NH2   . ARG A 1 114  ? 88.185  100.986 118.727 1.00 28.77  ? 114  ARG A NH2   1 
ATOM   763  N  N     . GLN A 1 115  ? 95.175  101.355 117.626 1.00 24.80  ? 115  GLN A N     1 
ATOM   764  C  CA    . GLN A 1 115  ? 95.781  100.124 118.123 1.00 24.80  ? 115  GLN A CA    1 
ATOM   765  C  C     . GLN A 1 115  ? 96.838  100.406 119.184 1.00 24.80  ? 115  GLN A C     1 
ATOM   766  O  O     . GLN A 1 115  ? 96.931  99.682  120.182 1.00 24.80  ? 115  GLN A O     1 
ATOM   767  C  CB    . GLN A 1 115  ? 96.384  99.333  116.964 1.00 24.80  ? 115  GLN A CB    1 
ATOM   768  C  CG    . GLN A 1 115  ? 95.354  98.628  116.101 1.00 24.80  ? 115  GLN A CG    1 
ATOM   769  C  CD    . GLN A 1 115  ? 95.977  97.617  115.164 1.00 24.80  ? 115  GLN A CD    1 
ATOM   770  O  OE1   . GLN A 1 115  ? 97.104  97.172  115.375 1.00 24.80  ? 115  GLN A OE1   1 
ATOM   771  N  NE2   . GLN A 1 115  ? 95.247  97.251  114.119 1.00 24.80  ? 115  GLN A NE2   1 
ATOM   772  N  N     . VAL A 1 116  ? 97.649  101.447 118.986 1.00 23.98  ? 116  VAL A N     1 
ATOM   773  C  CA    . VAL A 1 116  ? 98.741  101.715 119.918 1.00 23.98  ? 116  VAL A CA    1 
ATOM   774  C  C     . VAL A 1 116  ? 98.201  102.184 121.266 1.00 23.98  ? 116  VAL A C     1 
ATOM   775  O  O     . VAL A 1 116  ? 98.800  101.912 122.313 1.00 23.98  ? 116  VAL A O     1 
ATOM   776  C  CB    . VAL A 1 116  ? 99.736  102.723 119.312 1.00 23.98  ? 116  VAL A CB    1 
ATOM   777  C  CG1   . VAL A 1 116  ? 99.101  104.093 119.157 1.00 23.98  ? 116  VAL A CG1   1 
ATOM   778  C  CG2   . VAL A 1 116  ? 100.993 102.806 120.163 1.00 23.98  ? 116  VAL A CG2   1 
ATOM   779  N  N     . ALA A 1 117  ? 97.071  102.895 121.269 1.00 24.32  ? 117  ALA A N     1 
ATOM   780  C  CA    . ALA A 1 117  ? 96.487  103.343 122.530 1.00 24.32  ? 117  ALA A CA    1 
ATOM   781  C  C     . ALA A 1 117  ? 96.021  102.160 123.370 1.00 24.32  ? 117  ALA A C     1 
ATOM   782  O  O     . ALA A 1 117  ? 96.283  102.093 124.579 1.00 24.32  ? 117  ALA A O     1 
ATOM   783  C  CB    . ALA A 1 117  ? 95.329  104.302 122.258 1.00 24.32  ? 117  ALA A CB    1 
ATOM   784  N  N     . ALA A 1 118  ? 95.326  101.211 122.739 1.00 21.92  ? 118  ALA A N     1 
ATOM   785  C  CA    . ALA A 1 118  ? 94.895  100.015 123.453 1.00 21.92  ? 118  ALA A CA    1 
ATOM   786  C  C     . ALA A 1 118  ? 96.091  99.204  123.929 1.00 21.92  ? 118  ALA A C     1 
ATOM   787  O  O     . ALA A 1 118  ? 96.072  98.648  125.032 1.00 21.92  ? 118  ALA A O     1 
ATOM   788  C  CB    . ALA A 1 118  ? 93.989  99.167  122.562 1.00 21.92  ? 118  ALA A CB    1 
ATOM   789  N  N     . LEU A 1 119  ? 97.140  99.122  123.107 1.00 21.35  ? 119  LEU A N     1 
ATOM   790  C  CA    . LEU A 1 119  ? 98.345  98.411  123.517 1.00 21.35  ? 119  LEU A CA    1 
ATOM   791  C  C     . LEU A 1 119  ? 98.976  99.062  124.739 1.00 21.35  ? 119  LEU A C     1 
ATOM   792  O  O     . LEU A 1 119  ? 99.399  98.369  125.669 1.00 21.35  ? 119  LEU A O     1 
ATOM   793  C  CB    . LEU A 1 119  ? 99.344  98.359  122.361 1.00 21.35  ? 119  LEU A CB    1 
ATOM   794  C  CG    . LEU A 1 119  ? 100.519 97.387  122.484 1.00 21.35  ? 119  LEU A CG    1 
ATOM   795  C  CD1   . LEU A 1 119  ? 100.839 96.778  121.131 1.00 21.35  ? 119  LEU A CD1   1 
ATOM   796  C  CD2   . LEU A 1 119  ? 101.743 98.083  123.054 1.00 21.35  ? 119  LEU A CD2   1 
ATOM   797  N  N     . ARG A 1 120  ? 99.046  100.394 124.757 1.00 21.45  ? 120  ARG A N     1 
ATOM   798  C  CA    . ARG A 1 120  ? 99.616  101.092 125.904 1.00 21.45  ? 120  ARG A CA    1 
ATOM   799  C  C     . ARG A 1 120  ? 98.785  100.860 127.160 1.00 21.45  ? 120  ARG A C     1 
ATOM   800  O  O     . ARG A 1 120  ? 99.334  100.600 128.240 1.00 21.45  ? 120  ARG A O     1 
ATOM   801  C  CB    . ARG A 1 120  ? 99.728  102.585 125.599 1.00 21.45  ? 120  ARG A CB    1 
ATOM   802  C  CG    . ARG A 1 120  ? 101.002 103.233 126.102 1.00 21.45  ? 120  ARG A CG    1 
ATOM   803  C  CD    . ARG A 1 120  ? 100.915 104.747 126.012 1.00 21.45  ? 120  ARG A CD    1 
ATOM   804  N  NE    . ARG A 1 120  ? 100.652 105.203 124.649 1.00 21.45  ? 120  ARG A NE    1 
ATOM   805  C  CZ    . ARG A 1 120  ? 101.563 105.761 123.859 1.00 21.45  ? 120  ARG A CZ    1 
ATOM   806  N  NH1   . ARG A 1 120  ? 101.234 106.146 122.634 1.00 21.45  ? 120  ARG A NH1   1 
ATOM   807  N  NH2   . ARG A 1 120  ? 102.802 105.936 124.293 1.00 21.45  ? 120  ARG A NH2   1 
ATOM   808  N  N     . LYS A 1 121  ? 97.457  100.945 127.039 1.00 20.18  ? 121  LYS A N     1 
ATOM   809  C  CA    . LYS A 1 121  ? 96.598  100.725 128.200 1.00 20.18  ? 121  LYS A CA    1 
ATOM   810  C  C     . LYS A 1 121  ? 96.737  99.302  128.728 1.00 20.18  ? 121  LYS A C     1 
ATOM   811  O  O     . LYS A 1 121  ? 96.858  99.088  129.943 1.00 20.18  ? 121  LYS A O     1 
ATOM   812  C  CB    . LYS A 1 121  ? 95.145  101.024 127.837 1.00 20.18  ? 121  LYS A CB    1 
ATOM   813  C  CG    . LYS A 1 121  ? 94.699  102.435 128.178 1.00 20.18  ? 121  LYS A CG    1 
ATOM   814  C  CD    . LYS A 1 121  ? 93.672  102.945 127.178 1.00 20.18  ? 121  LYS A CD    1 
ATOM   815  C  CE    . LYS A 1 121  ? 92.404  102.108 127.211 1.00 20.18  ? 121  LYS A CE    1 
ATOM   816  N  NZ    . LYS A 1 121  ? 91.253  102.818 126.589 1.00 20.18  ? 121  LYS A NZ    1 
ATOM   817  N  N     . LYS A 1 122  ? 96.735  98.316  127.828 1.00 18.61  ? 122  LYS A N     1 
ATOM   818  C  CA    . LYS A 1 122  ? 96.885  96.927  128.243 1.00 18.61  ? 122  LYS A CA    1 
ATOM   819  C  C     . LYS A 1 122  ? 98.243  96.689  128.888 1.00 18.61  ? 122  LYS A C     1 
ATOM   820  O  O     . LYS A 1 122  ? 98.345  95.963  129.883 1.00 18.61  ? 122  LYS A O     1 
ATOM   821  C  CB    . LYS A 1 122  ? 96.689  96.000  127.044 1.00 18.61  ? 122  LYS A CB    1 
ATOM   822  C  CG    . LYS A 1 122  ? 96.660  94.523  127.395 1.00 18.61  ? 122  LYS A CG    1 
ATOM   823  C  CD    . LYS A 1 122  ? 95.584  94.221  128.423 1.00 18.61  ? 122  LYS A CD    1 
ATOM   824  C  CE    . LYS A 1 122  ? 95.218  92.746  128.421 1.00 18.61  ? 122  LYS A CE    1 
ATOM   825  N  NZ    . LYS A 1 122  ? 96.172  91.933  129.224 1.00 18.61  ? 122  LYS A NZ    1 
ATOM   826  N  N     . TYR A 1 123  ? 99.299  97.287  128.333 1.00 18.64  ? 123  TYR A N     1 
ATOM   827  C  CA    . TYR A 1 123  ? 100.626 97.114  128.910 1.00 18.64  ? 123  TYR A CA    1 
ATOM   828  C  C     . TYR A 1 123  ? 100.697 97.702  130.309 1.00 18.64  ? 123  TYR A C     1 
ATOM   829  O  O     . TYR A 1 123  ? 101.274 97.090  131.215 1.00 18.64  ? 123  TYR A O     1 
ATOM   830  C  CB    . TYR A 1 123  ? 101.685 97.751  128.012 1.00 18.64  ? 123  TYR A CB    1 
ATOM   831  C  CG    . TYR A 1 123  ? 103.029 97.907  128.684 1.00 18.64  ? 123  TYR A CG    1 
ATOM   832  C  CD1   . TYR A 1 123  ? 103.924 96.849  128.739 1.00 18.64  ? 123  TYR A CD1   1 
ATOM   833  C  CD2   . TYR A 1 123  ? 103.402 99.109  129.267 1.00 18.64  ? 123  TYR A CD2   1 
ATOM   834  C  CE1   . TYR A 1 123  ? 105.152 96.984  129.353 1.00 18.64  ? 123  TYR A CE1   1 
ATOM   835  C  CE2   . TYR A 1 123  ? 104.625 99.251  129.885 1.00 18.64  ? 123  TYR A CE2   1 
ATOM   836  C  CZ    . TYR A 1 123  ? 105.497 98.188  129.924 1.00 18.64  ? 123  TYR A CZ    1 
ATOM   837  O  OH    . TYR A 1 123  ? 106.718 98.331  130.539 1.00 18.64  ? 123  TYR A OH    1 
ATOM   838  N  N     . LEU A 1 124  ? 100.128 98.893  130.506 1.00 20.05  ? 124  LEU A N     1 
ATOM   839  C  CA    . LEU A 1 124  ? 100.135 99.481  131.841 1.00 20.05  ? 124  LEU A CA    1 
ATOM   840  C  C     . LEU A 1 124  ? 99.354  98.618  132.823 1.00 20.05  ? 124  LEU A C     1 
ATOM   841  O  O     . LEU A 1 124  ? 99.804  98.387  133.953 1.00 20.05  ? 124  LEU A O     1 
ATOM   842  C  CB    . LEU A 1 124  ? 99.565  100.895 131.810 1.00 20.05  ? 124  LEU A CB    1 
ATOM   843  C  CG    . LEU A 1 124  ? 99.669  101.608 133.158 1.00 20.05  ? 124  LEU A CG    1 
ATOM   844  C  CD1   . LEU A 1 124  ? 101.070 101.473 133.734 1.00 20.05  ? 124  LEU A CD1   1 
ATOM   845  C  CD2   . LEU A 1 124  ? 99.282  103.062 133.026 1.00 20.05  ? 124  LEU A CD2   1 
ATOM   846  N  N     . GLU A 1 125  ? 98.186  98.120  132.405 1.00 21.59  ? 125  GLU A N     1 
ATOM   847  C  CA    . GLU A 1 125  ? 97.393  97.276  133.293 1.00 21.59  ? 125  GLU A CA    1 
ATOM   848  C  C     . GLU A 1 125  ? 98.136  95.995  133.647 1.00 21.59  ? 125  GLU A C     1 
ATOM   849  O  O     . GLU A 1 125  ? 98.061  95.519  134.786 1.00 21.59  ? 125  GLU A O     1 
ATOM   850  C  CB    . GLU A 1 125  ? 96.044  96.947  132.651 1.00 21.59  ? 125  GLU A CB    1 
ATOM   851  C  CG    . GLU A 1 125  ? 95.069  96.081  133.482 1.00 21.59  ? 125  GLU A CG    1 
ATOM   852  C  CD    . GLU A 1 125  ? 94.894  96.488  134.953 1.00 21.59  ? 125  GLU A CD    1 
ATOM   853  O  OE1   . GLU A 1 125  ? 94.111  95.808  135.649 1.00 21.59  ? 125  GLU A OE1   1 
ATOM   854  O  OE2   . GLU A 1 125  ? 95.476  97.490  135.420 1.00 21.59  ? 125  GLU A OE2   1 
ATOM   855  N  N     . ALA A 1 126  ? 98.849  95.416  132.681 1.00 19.42  ? 126  ALA A N     1 
ATOM   856  C  CA    . ALA A 1 126  ? 99.571  94.177  132.943 1.00 19.42  ? 126  ALA A CA    1 
ATOM   857  C  C     . ALA A 1 126  ? 100.778 94.412  133.843 1.00 19.42  ? 126  ALA A C     1 
ATOM   858  O  O     . ALA A 1 126  ? 101.065 93.596  134.724 1.00 19.42  ? 126  ALA A O     1 
ATOM   859  C  CB    . ALA A 1 126  ? 99.999  93.532  131.627 1.00 19.42  ? 126  ALA A CB    1 
ATOM   860  N  N     . VAL A 1 127  ? 101.498 95.516  133.639 1.00 18.68  ? 127  VAL A N     1 
ATOM   861  C  CA    . VAL A 1 127  ? 102.695 95.748  134.439 1.00 18.68  ? 127  VAL A CA    1 
ATOM   862  C  C     . VAL A 1 127  ? 102.326 96.188  135.850 1.00 18.68  ? 127  VAL A C     1 
ATOM   863  O  O     . VAL A 1 127  ? 103.093 95.966  136.793 1.00 18.68  ? 127  VAL A O     1 
ATOM   864  C  CB    . VAL A 1 127  ? 103.624 96.770  133.758 1.00 18.68  ? 127  VAL A CB    1 
ATOM   865  C  CG1   . VAL A 1 127  ? 102.969 98.136  133.686 1.00 18.68  ? 127  VAL A CG1   1 
ATOM   866  C  CG2   . VAL A 1 127  ? 104.959 96.849  134.479 1.00 18.68  ? 127  VAL A CG2   1 
ATOM   867  N  N     . LEU A 1 128  ? 101.156 96.798  136.032 1.00 21.38  ? 128  LEU A N     1 
ATOM   868  C  CA    . LEU A 1 128  ? 100.741 97.219  137.363 1.00 21.38  ? 128  LEU A CA    1 
ATOM   869  C  C     . LEU A 1 128  ? 100.125 96.080  138.169 1.00 21.38  ? 128  LEU A C     1 
ATOM   870  O  O     . LEU A 1 128  ? 99.877  96.249  139.368 1.00 21.38  ? 128  LEU A O     1 
ATOM   871  C  CB    . LEU A 1 128  ? 99.762  98.392  137.239 1.00 21.38  ? 128  LEU A CB    1 
ATOM   872  C  CG    . LEU A 1 128  ? 99.242  99.102  138.487 1.00 21.38  ? 128  LEU A CG    1 
ATOM   873  C  CD1   . LEU A 1 128  ? 100.392 99.749  139.234 1.00 21.38  ? 128  LEU A CD1   1 
ATOM   874  C  CD2   . LEU A 1 128  ? 98.203  100.138 138.104 1.00 21.38  ? 128  LEU A CD2   1 
ATOM   875  N  N     . LYS A 1 129  ? 99.904  94.918  137.554 1.00 23.39  ? 129  LYS A N     1 
ATOM   876  C  CA    . LYS A 1 129  ? 99.321  93.773  138.240 1.00 23.39  ? 129  LYS A CA    1 
ATOM   877  C  C     . LYS A 1 129  ? 100.360 92.831  138.835 1.00 23.39  ? 129  LYS A C     1 
ATOM   878  O  O     . LYS A 1 129  ? 100.010 92.007  139.686 1.00 23.39  ? 129  LYS A O     1 
ATOM   879  C  CB    . LYS A 1 129  ? 98.426  92.981  137.278 1.00 23.39  ? 129  LYS A CB    1 
ATOM   880  C  CG    . LYS A 1 129  ? 97.402  92.091  137.960 1.00 23.39  ? 129  LYS A CG    1 
ATOM   881  C  CD    . LYS A 1 129  ? 96.631  91.256  136.950 1.00 23.39  ? 129  LYS A CD    1 
ATOM   882  C  CE    . LYS A 1 129  ? 96.075  92.110  135.824 1.00 23.39  ? 129  LYS A CE    1 
ATOM   883  N  NZ    . LYS A 1 129  ? 95.670  91.284  134.653 1.00 23.39  ? 129  LYS A NZ    1 
ATOM   884  N  N     . GLN A 1 130  ? 101.618 92.932  138.414 1.00 25.77  ? 130  GLN A N     1 
ATOM   885  C  CA    . GLN A 1 130  ? 102.660 92.063  138.942 1.00 25.77  ? 130  GLN A CA    1 
ATOM   886  C  C     . GLN A 1 130  ? 102.912 92.358  140.417 1.00 25.77  ? 130  GLN A C     1 
ATOM   887  O  O     . GLN A 1 130  ? 102.765 93.490  140.883 1.00 25.77  ? 130  GLN A O     1 
ATOM   888  C  CB    . GLN A 1 130  ? 103.953 92.238  138.150 1.00 25.77  ? 130  GLN A CB    1 
ATOM   889  C  CG    . GLN A 1 130  ? 103.789 92.087  136.650 1.00 25.77  ? 130  GLN A CG    1 
ATOM   890  C  CD    . GLN A 1 130  ? 103.462 90.669  136.242 1.00 25.77  ? 130  GLN A CD    1 
ATOM   891  O  OE1   . GLN A 1 130  ? 103.986 89.712  136.809 1.00 25.77  ? 130  GLN A OE1   1 
ATOM   892  N  NE2   . GLN A 1 130  ? 102.592 90.526  135.251 1.00 25.77  ? 130  GLN A NE2   1 
ATOM   893  N  N     . ASP A 1 131  ? 103.300 91.320  141.152 1.00 30.32  ? 131  ASP A N     1 
ATOM   894  C  CA    . ASP A 1 131  ? 103.551 91.449  142.578 1.00 30.32  ? 131  ASP A CA    1 
ATOM   895  C  C     . ASP A 1 131  ? 104.880 92.160  142.822 1.00 30.32  ? 131  ASP A C     1 
ATOM   896  O  O     . ASP A 1 131  ? 105.615 92.506  141.893 1.00 30.32  ? 131  ASP A O     1 
ATOM   897  C  CB    . ASP A 1 131  ? 103.539 90.078  143.246 1.00 30.32  ? 131  ASP A CB    1 
ATOM   898  C  CG    . ASP A 1 131  ? 104.619 89.163  142.710 1.00 30.32  ? 131  ASP A CG    1 
ATOM   899  O  OD1   . ASP A 1 131  ? 105.096 89.403  141.581 1.00 30.32  ? 131  ASP A OD1   1 
ATOM   900  O  OD2   . ASP A 1 131  ? 104.994 88.204  143.416 1.00 30.32  ? 131  ASP A OD2   1 
ATOM   901  N  N     . VAL A 1 132  ? 105.194 92.381  144.101 1.00 28.61  ? 132  VAL A N     1 
ATOM   902  C  CA    . VAL A 1 132  ? 106.454 93.027  144.453 1.00 28.61  ? 132  VAL A CA    1 
ATOM   903  C  C     . VAL A 1 132  ? 107.635 92.113  144.160 1.00 28.61  ? 132  VAL A C     1 
ATOM   904  O  O     . VAL A 1 132  ? 108.766 92.585  143.993 1.00 28.61  ? 132  VAL A O     1 
ATOM   905  C  CB    . VAL A 1 132  ? 106.437 93.465  145.927 1.00 28.61  ? 132  VAL A CB    1 
ATOM   906  C  CG1   . VAL A 1 132  ? 105.461 94.610  146.127 1.00 28.61  ? 132  VAL A CG1   1 
ATOM   907  C  CG2   . VAL A 1 132  ? 106.073 92.295  146.817 1.00 28.61  ? 132  VAL A CG2   1 
ATOM   908  N  N     . GLY A 1 133  ? 107.404 90.800  144.099 1.00 29.81  ? 133  GLY A N     1 
ATOM   909  C  CA    . GLY A 1 133  ? 108.494 89.878  143.823 1.00 29.81  ? 133  GLY A CA    1 
ATOM   910  C  C     . GLY A 1 133  ? 109.094 90.067  142.443 1.00 29.81  ? 133  GLY A C     1 
ATOM   911  O  O     . GLY A 1 133  ? 110.310 89.967  142.266 1.00 29.81  ? 133  GLY A O     1 
ATOM   912  N  N     . PHE A 1 134  ? 108.250 90.337  141.446 1.00 25.11  ? 134  PHE A N     1 
ATOM   913  C  CA    . PHE A 1 134  ? 108.747 90.529  140.088 1.00 25.11  ? 134  PHE A CA    1 
ATOM   914  C  C     . PHE A 1 134  ? 109.574 91.802  139.974 1.00 25.11  ? 134  PHE A C     1 
ATOM   915  O  O     . PHE A 1 134  ? 110.521 91.868  139.183 1.00 25.11  ? 134  PHE A O     1 
ATOM   916  C  CB    . PHE A 1 134  ? 107.577 90.557  139.105 1.00 25.11  ? 134  PHE A CB    1 
ATOM   917  C  CG    . PHE A 1 134  ? 107.945 91.043  137.733 1.00 25.11  ? 134  PHE A CG    1 
ATOM   918  C  CD1   . PHE A 1 134  ? 108.727 90.268  136.896 1.00 25.11  ? 134  PHE A CD1   1 
ATOM   919  C  CD2   . PHE A 1 134  ? 107.500 92.272  137.277 1.00 25.11  ? 134  PHE A CD2   1 
ATOM   920  C  CE1   . PHE A 1 134  ? 109.063 90.712  135.633 1.00 25.11  ? 134  PHE A CE1   1 
ATOM   921  C  CE2   . PHE A 1 134  ? 107.833 92.720  136.016 1.00 25.11  ? 134  PHE A CE2   1 
ATOM   922  C  CZ    . PHE A 1 134  ? 108.615 91.939  135.193 1.00 25.11  ? 134  PHE A CZ    1 
ATOM   923  N  N     . PHE A 1 135  ? 109.232 92.827  140.758 1.00 25.43  ? 135  PHE A N     1 
ATOM   924  C  CA    . PHE A 1 135  ? 109.895 94.118  140.612 1.00 25.43  ? 135  PHE A CA    1 
ATOM   925  C  C     . PHE A 1 135  ? 111.296 94.104  141.211 1.00 25.43  ? 135  PHE A C     1 
ATOM   926  O  O     . PHE A 1 135  ? 112.183 94.826  140.743 1.00 25.43  ? 135  PHE A O     1 
ATOM   927  C  CB    . PHE A 1 135  ? 109.046 95.217  141.247 1.00 25.43  ? 135  PHE A CB    1 
ATOM   928  C  CG    . PHE A 1 135  ? 107.889 95.648  140.397 1.00 25.43  ? 135  PHE A CG    1 
ATOM   929  C  CD1   . PHE A 1 135  ? 108.101 96.338  139.217 1.00 25.43  ? 135  PHE A CD1   1 
ATOM   930  C  CD2   . PHE A 1 135  ? 106.591 95.355  140.772 1.00 25.43  ? 135  PHE A CD2   1 
ATOM   931  C  CE1   . PHE A 1 135  ? 107.040 96.731  138.430 1.00 25.43  ? 135  PHE A CE1   1 
ATOM   932  C  CE2   . PHE A 1 135  ? 105.526 95.746  139.988 1.00 25.43  ? 135  PHE A CE2   1 
ATOM   933  C  CZ    . PHE A 1 135  ? 105.751 96.435  138.816 1.00 25.43  ? 135  PHE A CZ    1 
ATOM   934  N  N     . ASP A 1 136  ? 111.517 93.298  142.248 1.00 27.62  ? 136  ASP A N     1 
ATOM   935  C  CA    . ASP A 1 136  ? 112.819 93.285  142.903 1.00 27.62  ? 136  ASP A CA    1 
ATOM   936  C  C     . ASP A 1 136  ? 113.836 92.396  142.198 1.00 27.62  ? 136  ASP A C     1 
ATOM   937  O  O     . ASP A 1 136  ? 115.032 92.503  142.489 1.00 27.62  ? 136  ASP A O     1 
ATOM   938  C  CB    . ASP A 1 136  ? 112.675 92.844  144.362 1.00 27.62  ? 136  ASP A CB    1 
ATOM   939  C  CG    . ASP A 1 136  ? 112.024 91.480  144.505 1.00 27.62  ? 136  ASP A CG    1 
ATOM   940  O  OD1   . ASP A 1 136  ? 112.560 90.491  143.963 1.00 27.62  ? 136  ASP A OD1   1 
ATOM   941  O  OD2   . ASP A 1 136  ? 110.974 91.396  145.172 1.00 27.62  ? 136  ASP A OD2   1 
ATOM   942  N  N     . THR A 1 137  ? 113.399 91.528  141.286 1.00 29.14  ? 137  THR A N     1 
ATOM   943  C  CA    . THR A 1 137  ? 114.324 90.596  140.650 1.00 29.14  ? 137  THR A CA    1 
ATOM   944  C  C     . THR A 1 137  ? 114.814 91.090  139.288 1.00 29.14  ? 137  THR A C     1 
ATOM   945  O  O     . THR A 1 137  ? 116.019 91.061  139.021 1.00 29.14  ? 137  THR A O     1 
ATOM   946  C  CB    . THR A 1 137  ? 113.679 89.203  140.552 1.00 29.14  ? 137  THR A CB    1 
ATOM   947  O  OG1   . THR A 1 137  ? 114.631 88.259  140.042 1.00 29.14  ? 137  THR A OG1   1 
ATOM   948  C  CG2   . THR A 1 137  ? 112.411 89.204  139.703 1.00 29.14  ? 137  THR A CG2   1 
ATOM   949  N  N     . ASP A 1 138  ? 113.912 91.548  138.417 1.00 29.61  ? 138  ASP A N     1 
ATOM   950  C  CA    . ASP A 1 138  ? 114.334 92.203  137.175 1.00 29.61  ? 138  ASP A CA    1 
ATOM   951  C  C     . ASP A 1 138  ? 113.257 93.220  136.791 1.00 29.61  ? 138  ASP A C     1 
ATOM   952  O  O     . ASP A 1 138  ? 112.300 92.894  136.086 1.00 29.61  ? 138  ASP A O     1 
ATOM   953  C  CB    . ASP A 1 138  ? 114.587 91.198  136.060 1.00 29.61  ? 138  ASP A CB    1 
ATOM   954  C  CG    . ASP A 1 138  ? 113.461 90.195  135.905 1.00 29.61  ? 138  ASP A CG    1 
ATOM   955  O  OD1   . ASP A 1 138  ? 112.679 90.320  134.939 1.00 29.61  ? 138  ASP A OD1   1 
ATOM   956  O  OD2   . ASP A 1 138  ? 113.368 89.272  136.738 1.00 29.61  ? 138  ASP A OD2   1 
ATOM   957  N  N     . ALA A 1 139  ? 113.440 94.454  137.253 1.00 27.80  ? 139  ALA A N     1 
ATOM   958  C  CA    . ALA A 1 139  ? 112.566 95.565  136.906 1.00 27.80  ? 139  ALA A CA    1 
ATOM   959  C  C     . ALA A 1 139  ? 113.189 96.848  137.426 1.00 27.80  ? 139  ALA A C     1 
ATOM   960  O  O     . ALA A 1 139  ? 113.689 96.885  138.553 1.00 27.80  ? 139  ALA A O     1 
ATOM   961  C  CB    . ALA A 1 139  ? 111.159 95.389  137.491 1.00 27.80  ? 139  ALA A CB    1 
ATOM   962  N  N     . ARG A 1 140  ? 113.159 97.891  136.603 1.00 26.08  ? 140  ARG A N     1 
ATOM   963  C  CA    . ARG A 1 140  ? 113.664 99.195  136.998 1.00 26.08  ? 140  ARG A CA    1 
ATOM   964  C  C     . ARG A 1 140  ? 112.699 100.267 136.521 1.00 26.08  ? 140  ARG A C     1 
ATOM   965  O  O     . ARG A 1 140  ? 112.036 100.115 135.491 1.00 26.08  ? 140  ARG A O     1 
ATOM   966  C  CB    . ARG A 1 140  ? 115.066 99.456  136.431 1.00 26.08  ? 140  ARG A CB    1 
ATOM   967  C  CG    . ARG A 1 140  ? 116.187 98.762  137.186 1.00 26.08  ? 140  ARG A CG    1 
ATOM   968  C  CD    . ARG A 1 140  ? 116.472 97.384  136.613 1.00 26.08  ? 140  ARG A CD    1 
ATOM   969  N  NE    . ARG A 1 140  ? 116.574 97.405  135.157 1.00 26.08  ? 140  ARG A NE    1 
ATOM   970  C  CZ    . ARG A 1 140  ? 117.670 97.745  134.488 1.00 26.08  ? 140  ARG A CZ    1 
ATOM   971  N  NH1   . ARG A 1 140  ? 117.669 97.734  133.162 1.00 26.08  ? 140  ARG A NH1   1 
ATOM   972  N  NH2   . ARG A 1 140  ? 118.768 98.095  135.143 1.00 26.08  ? 140  ARG A NH2   1 
ATOM   973  N  N     . THR A 1 141  ? 112.622 101.356 137.287 1.00 25.39  ? 141  THR A N     1 
ATOM   974  C  CA    . THR A 1 141  ? 111.767 102.469 136.891 1.00 25.39  ? 141  THR A CA    1 
ATOM   975  C  C     . THR A 1 141  ? 112.228 103.066 135.569 1.00 25.39  ? 141  THR A C     1 
ATOM   976  O  O     . THR A 1 141  ? 111.407 103.375 134.697 1.00 25.39  ? 141  THR A O     1 
ATOM   977  C  CB    . THR A 1 141  ? 111.748 103.535 137.985 1.00 25.39  ? 141  THR A CB    1 
ATOM   978  O  OG1   . THR A 1 141  ? 111.647 102.903 139.266 1.00 25.39  ? 141  THR A OG1   1 
ATOM   979  C  CG2   . THR A 1 141  ? 110.564 104.468 137.793 1.00 25.39  ? 141  THR A CG2   1 
ATOM   980  N  N     . GLY A 1 142  ? 113.541 103.231 135.399 1.00 25.78  ? 142  GLY A N     1 
ATOM   981  C  CA    . GLY A 1 142  ? 114.056 103.727 134.134 1.00 25.78  ? 142  GLY A CA    1 
ATOM   982  C  C     . GLY A 1 142  ? 113.769 102.788 132.980 1.00 25.78  ? 142  GLY A C     1 
ATOM   983  O  O     . GLY A 1 142  ? 113.426 103.228 131.880 1.00 25.78  ? 142  GLY A O     1 
ATOM   984  N  N     . ASP A 1 143  ? 113.908 101.483 133.214 1.00 25.38  ? 143  ASP A N     1 
ATOM   985  C  CA    . ASP A 1 143  ? 113.612 100.505 132.174 1.00 25.38  ? 143  ASP A CA    1 
ATOM   986  C  C     . ASP A 1 143  ? 112.147 100.595 131.761 1.00 25.38  ? 143  ASP A C     1 
ATOM   987  O  O     . ASP A 1 143  ? 111.825 100.603 130.568 1.00 25.38  ? 143  ASP A O     1 
ATOM   988  C  CB    . ASP A 1 143  ? 113.968 99.102  132.681 1.00 25.38  ? 143  ASP A CB    1 
ATOM   989  C  CG    . ASP A 1 143  ? 113.748 98.002  131.643 1.00 25.38  ? 143  ASP A CG    1 
ATOM   990  O  OD1   . ASP A 1 143  ? 112.897 98.135  130.741 1.00 25.38  ? 143  ASP A OD1   1 
ATOM   991  O  OD2   . ASP A 1 143  ? 114.450 96.974  131.740 1.00 25.38  ? 143  ASP A OD2   1 
ATOM   992  N  N     . ILE A 1 144  ? 111.246 100.689 132.742 1.00 22.60  ? 144  ILE A N     1 
ATOM   993  C  CA    . ILE A 1 144  ? 109.819 100.773 132.439 1.00 22.60  ? 144  ILE A CA    1 
ATOM   994  C  C     . ILE A 1 144  ? 109.504 102.059 131.683 1.00 22.60  ? 144  ILE A C     1 
ATOM   995  O  O     . ILE A 1 144  ? 108.734 102.053 130.714 1.00 22.60  ? 144  ILE A O     1 
ATOM   996  C  CB    . ILE A 1 144  ? 108.990 100.657 133.731 1.00 22.60  ? 144  ILE A CB    1 
ATOM   997  C  CG1   . ILE A 1 144  ? 109.168 99.273  134.355 1.00 22.60  ? 144  ILE A CG1   1 
ATOM   998  C  CG2   . ILE A 1 144  ? 107.523 100.927 133.448 1.00 22.60  ? 144  ILE A CG2   1 
ATOM   999  C  CD1   . ILE A 1 144  ? 108.482 98.167  133.589 1.00 22.60  ? 144  ILE A CD1   1 
ATOM   1000 N  N     . VAL A 1 145  ? 110.090 103.179 132.111 1.00 22.07  ? 145  VAL A N     1 
ATOM   1001 C  CA    . VAL A 1 145  ? 109.833 104.456 131.449 1.00 22.07  ? 145  VAL A CA    1 
ATOM   1002 C  C     . VAL A 1 145  ? 110.318 104.414 130.005 1.00 22.07  ? 145  VAL A C     1 
ATOM   1003 O  O     . VAL A 1 145  ? 109.620 104.853 129.082 1.00 22.07  ? 145  VAL A O     1 
ATOM   1004 C  CB    . VAL A 1 145  ? 110.487 105.607 132.231 1.00 22.07  ? 145  VAL A CB    1 
ATOM   1005 C  CG1   . VAL A 1 145  ? 110.545 106.861 131.379 1.00 22.07  ? 145  VAL A CG1   1 
ATOM   1006 C  CG2   . VAL A 1 145  ? 109.723 105.871 133.515 1.00 22.07  ? 145  VAL A CG2   1 
ATOM   1007 N  N     . PHE A 1 146  ? 111.523 103.880 129.785 1.00 23.02  ? 146  PHE A N     1 
ATOM   1008 C  CA    . PHE A 1 146  ? 112.049 103.791 128.427 1.00 23.02  ? 146  PHE A CA    1 
ATOM   1009 C  C     . PHE A 1 146  ? 111.202 102.864 127.567 1.00 23.02  ? 146  PHE A C     1 
ATOM   1010 O  O     . PHE A 1 146  ? 110.978 103.139 126.383 1.00 23.02  ? 146  PHE A O     1 
ATOM   1011 C  CB    . PHE A 1 146  ? 113.502 103.319 128.450 1.00 23.02  ? 146  PHE A CB    1 
ATOM   1012 C  CG    . PHE A 1 146  ? 114.075 103.071 127.084 1.00 23.02  ? 146  PHE A CG    1 
ATOM   1013 C  CD1   . PHE A 1 146  ? 114.538 104.122 126.312 1.00 23.02  ? 146  PHE A CD1   1 
ATOM   1014 C  CD2   . PHE A 1 146  ? 114.149 101.787 126.570 1.00 23.02  ? 146  PHE A CD2   1 
ATOM   1015 C  CE1   . PHE A 1 146  ? 115.063 103.898 125.055 1.00 23.02  ? 146  PHE A CE1   1 
ATOM   1016 C  CE2   . PHE A 1 146  ? 114.672 101.558 125.314 1.00 23.02  ? 146  PHE A CE2   1 
ATOM   1017 C  CZ    . PHE A 1 146  ? 115.130 102.615 124.556 1.00 23.02  ? 146  PHE A CZ    1 
ATOM   1018 N  N     . SER A 1 147  ? 110.730 101.755 128.139 1.00 22.42  ? 147  SER A N     1 
ATOM   1019 C  CA    . SER A 1 147  ? 109.889 100.836 127.381 1.00 22.42  ? 147  SER A CA    1 
ATOM   1020 C  C     . SER A 1 147  ? 108.571 101.495 126.994 1.00 22.42  ? 147  SER A C     1 
ATOM   1021 O  O     . SER A 1 147  ? 108.062 101.288 125.886 1.00 22.42  ? 147  SER A O     1 
ATOM   1022 C  CB    . SER A 1 147  ? 109.643 99.564  128.190 1.00 22.42  ? 147  SER A CB    1 
ATOM   1023 O  OG    . SER A 1 147  ? 109.122 98.535  127.370 1.00 22.42  ? 147  SER A OG    1 
ATOM   1024 N  N     . VAL A 1 148  ? 107.998 102.288 127.902 1.00 21.46  ? 148  VAL A N     1 
ATOM   1025 C  CA    . VAL A 1 148  ? 106.742 102.979 127.608 1.00 21.46  ? 148  VAL A CA    1 
ATOM   1026 C  C     . VAL A 1 148  ? 106.954 104.025 126.520 1.00 21.46  ? 148  VAL A C     1 
ATOM   1027 O  O     . VAL A 1 148  ? 106.162 104.143 125.577 1.00 21.46  ? 148  VAL A O     1 
ATOM   1028 C  CB    . VAL A 1 148  ? 106.162 103.614 128.883 1.00 21.46  ? 148  VAL A CB    1 
ATOM   1029 C  CG1   . VAL A 1 148  ? 105.040 104.574 128.532 1.00 21.46  ? 148  VAL A CG1   1 
ATOM   1030 C  CG2   . VAL A 1 148  ? 105.662 102.543 129.827 1.00 21.46  ? 148  VAL A CG2   1 
ATOM   1031 N  N     . SER A 1 149  ? 108.033 104.800 126.635 1.00 23.26  ? 149  SER A N     1 
ATOM   1032 C  CA    . SER A 1 149  ? 108.222 105.944 125.749 1.00 23.26  ? 149  SER A CA    1 
ATOM   1033 C  C     . SER A 1 149  ? 108.628 105.505 124.346 1.00 23.26  ? 149  SER A C     1 
ATOM   1034 O  O     . SER A 1 149  ? 107.937 105.797 123.364 1.00 23.26  ? 149  SER A O     1 
ATOM   1035 C  CB    . SER A 1 149  ? 109.266 106.891 126.339 1.00 23.26  ? 149  SER A CB    1 
ATOM   1036 O  OG    . SER A 1 149  ? 110.572 106.516 125.937 1.00 23.26  ? 149  SER A OG    1 
ATOM   1037 N  N     . THR A 1 150  ? 109.753 104.797 124.232 1.00 24.98  ? 150  THR A N     1 
ATOM   1038 C  CA    . THR A 1 150  ? 110.359 104.582 122.921 1.00 24.98  ? 150  THR A CA    1 
ATOM   1039 C  C     . THR A 1 150  ? 109.698 103.432 122.170 1.00 24.98  ? 150  THR A C     1 
ATOM   1040 O  O     . THR A 1 150  ? 109.371 103.562 120.984 1.00 24.98  ? 150  THR A O     1 
ATOM   1041 C  CB    . THR A 1 150  ? 111.856 104.326 123.075 1.00 24.98  ? 150  THR A CB    1 
ATOM   1042 O  OG1   . THR A 1 150  ? 112.439 105.365 123.871 1.00 24.98  ? 150  THR A OG1   1 
ATOM   1043 C  CG2   . THR A 1 150  ? 112.532 104.296 121.712 1.00 24.98  ? 150  THR A CG2   1 
ATOM   1044 N  N     . ASP A 1 151  ? 109.502 102.294 122.838 1.00 26.99  ? 151  ASP A N     1 
ATOM   1045 C  CA    . ASP A 1 151  ? 109.057 101.092 122.135 1.00 26.99  ? 151  ASP A CA    1 
ATOM   1046 C  C     . ASP A 1 151  ? 107.661 101.264 121.548 1.00 26.99  ? 151  ASP A C     1 
ATOM   1047 O  O     . ASP A 1 151  ? 107.388 100.804 120.431 1.00 26.99  ? 151  ASP A O     1 
ATOM   1048 C  CB    . ASP A 1 151  ? 109.103 99.893  123.078 1.00 26.99  ? 151  ASP A CB    1 
ATOM   1049 C  CG    . ASP A 1 151  ? 110.517 99.513  123.467 1.00 26.99  ? 151  ASP A CG    1 
ATOM   1050 O  OD1   . ASP A 1 151  ? 111.440 99.749  122.661 1.00 26.99  ? 151  ASP A OD1   1 
ATOM   1051 O  OD2   . ASP A 1 151  ? 110.706 98.977  124.580 1.00 26.99  ? 151  ASP A OD2   1 
ATOM   1052 N  N     . THR A 1 152  ? 106.760 101.916 122.286 1.00 23.46  ? 152  THR A N     1 
ATOM   1053 C  CA    . THR A 1 152  ? 105.419 102.153 121.762 1.00 23.46  ? 152  THR A CA    1 
ATOM   1054 C  C     . THR A 1 152  ? 105.460 103.038 120.523 1.00 23.46  ? 152  THR A C     1 
ATOM   1055 O  O     . THR A 1 152  ? 104.678 102.839 119.587 1.00 23.46  ? 152  THR A O     1 
ATOM   1056 C  CB    . THR A 1 152  ? 104.532 102.774 122.840 1.00 23.46  ? 152  THR A CB    1 
ATOM   1057 O  OG1   . THR A 1 152  ? 105.050 104.058 123.208 1.00 23.46  ? 152  THR A OG1   1 
ATOM   1058 C  CG2   . THR A 1 152  ? 104.478 101.876 124.066 1.00 23.46  ? 152  THR A CG2   1 
ATOM   1059 N  N     . LEU A 1 153  ? 106.368 104.017 120.495 1.00 23.78  ? 153  LEU A N     1 
ATOM   1060 C  CA    . LEU A 1 153  ? 106.528 104.843 119.302 1.00 23.78  ? 153  LEU A CA    1 
ATOM   1061 C  C     . LEU A 1 153  ? 106.976 104.006 118.111 1.00 23.78  ? 153  LEU A C     1 
ATOM   1062 O  O     . LEU A 1 153  ? 106.481 104.186 116.992 1.00 23.78  ? 153  LEU A O     1 
ATOM   1063 C  CB    . LEU A 1 153  ? 107.528 105.966 119.574 1.00 23.78  ? 153  LEU A CB    1 
ATOM   1064 C  CG    . LEU A 1 153  ? 107.037 107.125 120.443 1.00 23.78  ? 153  LEU A CG    1 
ATOM   1065 C  CD1   . LEU A 1 153  ? 107.948 108.331 120.289 1.00 23.78  ? 153  LEU A CD1   1 
ATOM   1066 C  CD2   . LEU A 1 153  ? 105.602 107.489 120.103 1.00 23.78  ? 153  LEU A CD2   1 
ATOM   1067 N  N     . LEU A 1 154  ? 107.916 103.085 118.332 1.00 23.86  ? 154  LEU A N     1 
ATOM   1068 C  CA    . LEU A 1 154  ? 108.368 102.215 117.252 1.00 23.86  ? 154  LEU A CA    1 
ATOM   1069 C  C     . LEU A 1 154  ? 107.236 101.331 116.746 1.00 23.86  ? 154  LEU A C     1 
ATOM   1070 O  O     . LEU A 1 154  ? 107.088 101.136 115.534 1.00 23.86  ? 154  LEU A O     1 
ATOM   1071 C  CB    . LEU A 1 154  ? 109.545 101.362 117.721 1.00 23.86  ? 154  LEU A CB    1 
ATOM   1072 C  CG    . LEU A 1 154  ? 110.872 102.095 117.915 1.00 23.86  ? 154  LEU A CG    1 
ATOM   1073 C  CD1   . LEU A 1 154  ? 111.950 101.139 118.393 1.00 23.86  ? 154  LEU A CD1   1 
ATOM   1074 C  CD2   . LEU A 1 154  ? 111.292 102.781 116.628 1.00 23.86  ? 154  LEU A CD2   1 
ATOM   1075 N  N     . VAL A 1 155  ? 106.428 100.788 117.657 1.00 24.54  ? 155  VAL A N     1 
ATOM   1076 C  CA    . VAL A 1 155  ? 105.306 99.952  117.238 1.00 24.54  ? 155  VAL A CA    1 
ATOM   1077 C  C     . VAL A 1 155  ? 104.283 100.777 116.464 1.00 24.54  ? 155  VAL A C     1 
ATOM   1078 O  O     . VAL A 1 155  ? 103.706 100.308 115.475 1.00 24.54  ? 155  VAL A O     1 
ATOM   1079 C  CB    . VAL A 1 155  ? 104.680 99.250  118.455 1.00 24.54  ? 155  VAL A CB    1 
ATOM   1080 C  CG1   . VAL A 1 155  ? 103.350 98.619  118.084 1.00 24.54  ? 155  VAL A CG1   1 
ATOM   1081 C  CG2   . VAL A 1 155  ? 105.628 98.197  118.982 1.00 24.54  ? 155  VAL A CG2   1 
ATOM   1082 N  N     . GLN A 1 156  ? 104.047 102.020 116.894 1.00 24.64  ? 156  GLN A N     1 
ATOM   1083 C  CA    . GLN A 1 156  ? 103.143 102.898 116.159 1.00 24.64  ? 156  GLN A CA    1 
ATOM   1084 C  C     . GLN A 1 156  ? 103.665 103.172 114.756 1.00 24.64  ? 156  GLN A C     1 
ATOM   1085 O  O     . GLN A 1 156  ? 102.895 103.187 113.789 1.00 24.64  ? 156  GLN A O     1 
ATOM   1086 C  CB    . GLN A 1 156  ? 102.949 104.207 116.925 1.00 24.64  ? 156  GLN A CB    1 
ATOM   1087 C  CG    . GLN A 1 156  ? 101.952 105.158 116.291 1.00 24.64  ? 156  GLN A CG    1 
ATOM   1088 C  CD    . GLN A 1 156  ? 102.073 106.568 116.832 1.00 24.64  ? 156  GLN A CD    1 
ATOM   1089 O  OE1   . GLN A 1 156  ? 103.166 107.130 116.888 1.00 24.64  ? 156  GLN A OE1   1 
ATOM   1090 N  NE2   . GLN A 1 156  ? 100.949 107.145 117.237 1.00 24.64  ? 156  GLN A NE2   1 
ATOM   1091 N  N     . ASP A 1 157  ? 104.974 103.394 114.626 1.00 25.62  ? 157  ASP A N     1 
ATOM   1092 C  CA    . ASP A 1 157  ? 105.564 103.601 113.307 1.00 25.62  ? 157  ASP A CA    1 
ATOM   1093 C  C     . ASP A 1 157  ? 105.515 102.335 112.461 1.00 25.62  ? 157  ASP A C     1 
ATOM   1094 O  O     . ASP A 1 157  ? 105.495 102.417 111.228 1.00 25.62  ? 157  ASP A O     1 
ATOM   1095 C  CB    . ASP A 1 157  ? 107.008 104.083 113.444 1.00 25.62  ? 157  ASP A CB    1 
ATOM   1096 C  CG    . ASP A 1 157  ? 107.101 105.547 113.818 1.00 25.62  ? 157  ASP A CG    1 
ATOM   1097 O  OD1   . ASP A 1 157  ? 106.092 106.104 114.298 1.00 25.62  ? 157  ASP A OD1   1 
ATOM   1098 O  OD2   . ASP A 1 157  ? 108.184 106.140 113.635 1.00 25.62  ? 157  ASP A OD2   1 
ATOM   1099 N  N     . ALA A 1 158  ? 105.503 101.163 113.097 1.00 22.10  ? 158  ALA A N     1 
ATOM   1100 C  CA    . ALA A 1 158  ? 105.537 99.913  112.345 1.00 22.10  ? 158  ALA A CA    1 
ATOM   1101 C  C     . ALA A 1 158  ? 104.214 99.643  111.636 1.00 22.10  ? 158  ALA A C     1 
ATOM   1102 O  O     . ALA A 1 158  ? 104.203 99.178  110.491 1.00 22.10  ? 158  ALA A O     1 
ATOM   1103 C  CB    . ALA A 1 158  ? 105.891 98.753  113.274 1.00 22.10  ? 158  ALA A CB    1 
ATOM   1104 N  N     . ILE A 1 159  ? 103.091 99.921  112.298 1.00 22.60  ? 159  ILE A N     1 
ATOM   1105 C  CA    . ILE A 1 159  ? 101.772 99.607  111.757 1.00 22.60  ? 159  ILE A CA    1 
ATOM   1106 C  C     . ILE A 1 159  ? 101.062 100.845 111.216 1.00 22.60  ? 159  ILE A C     1 
ATOM   1107 O  O     . ILE A 1 159  ? 99.861  100.793 110.936 1.00 22.60  ? 159  ILE A O     1 
ATOM   1108 C  CB    . ILE A 1 159  ? 100.908 98.892  112.805 1.00 22.60  ? 159  ILE A CB    1 
ATOM   1109 C  CG1   . ILE A 1 159  ? 100.682 99.797  114.016 1.00 22.60  ? 159  ILE A CG1   1 
ATOM   1110 C  CG2   . ILE A 1 159  ? 101.561 97.591  113.231 1.00 22.60  ? 159  ILE A CG2   1 
ATOM   1111 C  CD1   . ILE A 1 159  ? 99.659  99.266  114.989 1.00 22.60  ? 159  ILE A CD1   1 
ATOM   1112 N  N     . SER A 1 160  ? 101.778 101.956 111.060 1.00 24.12  ? 160  SER A N     1 
ATOM   1113 C  CA    . SER A 1 160  ? 101.217 103.172 110.483 1.00 24.12  ? 160  SER A CA    1 
ATOM   1114 C  C     . SER A 1 160  ? 101.195 103.079 108.964 1.00 24.12  ? 160  SER A C     1 
ATOM   1115 O  O     . SER A 1 160  ? 101.327 101.988 108.402 1.00 24.12  ? 160  SER A O     1 
ATOM   1116 C  CB    . SER A 1 160  ? 102.008 104.401 110.932 1.00 24.12  ? 160  SER A CB    1 
ATOM   1117 O  OG    . SER A 1 160  ? 101.716 104.729 112.279 1.00 24.12  ? 160  SER A OG    1 
ATOM   1118 N  N     . GLU A 1 161  ? 101.025 104.219 108.293 1.00 27.19  ? 161  GLU A N     1 
ATOM   1119 C  CA    . GLU A 1 161  ? 100.908 104.272 106.839 1.00 27.19  ? 161  GLU A CA    1 
ATOM   1120 C  C     . GLU A 1 161  ? 102.140 103.726 106.121 1.00 27.19  ? 161  GLU A C     1 
ATOM   1121 O  O     . GLU A 1 161  ? 102.156 103.652 104.887 1.00 27.19  ? 161  GLU A O     1 
ATOM   1122 C  CB    . GLU A 1 161  ? 100.637 105.709 106.387 1.00 27.19  ? 161  GLU A CB    1 
ATOM   1123 C  CG    . GLU A 1 161  ? 101.879 106.576 106.290 1.00 27.19  ? 161  GLU A CG    1 
ATOM   1124 C  CD    . GLU A 1 161  ? 102.427 106.963 107.647 1.00 27.19  ? 161  GLU A CD    1 
ATOM   1125 O  OE1   . GLU A 1 161  ? 101.633 107.054 108.606 1.00 27.19  ? 161  GLU A OE1   1 
ATOM   1126 O  OE2   . GLU A 1 161  ? 103.652 107.177 107.757 1.00 27.19  ? 161  GLU A OE2   1 
ATOM   1127 N  N     . LYS A 1 162  ? 103.179 103.354 106.874 1.00 27.08  ? 162  LYS A N     1 
ATOM   1128 C  CA    . LYS A 1 162  ? 104.314 102.662 106.273 1.00 27.08  ? 162  LYS A CA    1 
ATOM   1129 C  C     . LYS A 1 162  ? 103.868 101.370 105.601 1.00 27.08  ? 162  LYS A C     1 
ATOM   1130 O  O     . LYS A 1 162  ? 104.330 101.037 104.502 1.00 27.08  ? 162  LYS A O     1 
ATOM   1131 C  CB    . LYS A 1 162  ? 105.374 102.370 107.334 1.00 27.08  ? 162  LYS A CB    1 
ATOM   1132 C  CG    . LYS A 1 162  ? 105.989 103.605 107.962 1.00 27.08  ? 162  LYS A CG    1 
ATOM   1133 C  CD    . LYS A 1 162  ? 106.706 104.451 106.929 1.00 27.08  ? 162  LYS A CD    1 
ATOM   1134 C  CE    . LYS A 1 162  ? 107.645 105.446 107.592 1.00 27.08  ? 162  LYS A CE    1 
ATOM   1135 N  NZ    . LYS A 1 162  ? 108.671 104.766 108.430 1.00 27.08  ? 162  LYS A NZ    1 
ATOM   1136 N  N     . VAL A 1 163  ? 102.966 100.630 106.249 1.00 25.49  ? 163  VAL A N     1 
ATOM   1137 C  CA    . VAL A 1 163  ? 102.406 99.432  105.635 1.00 25.49  ? 163  VAL A CA    1 
ATOM   1138 C  C     . VAL A 1 163  ? 101.648 99.796  104.367 1.00 25.49  ? 163  VAL A C     1 
ATOM   1139 O  O     . VAL A 1 163  ? 101.686 99.065  103.371 1.00 25.49  ? 163  VAL A O     1 
ATOM   1140 C  CB    . VAL A 1 163  ? 101.508 98.685  106.637 1.00 25.49  ? 163  VAL A CB    1 
ATOM   1141 C  CG1   . VAL A 1 163  ? 101.087 97.341  106.071 1.00 25.49  ? 163  VAL A CG1   1 
ATOM   1142 C  CG2   . VAL A 1 163  ? 102.230 98.506  107.960 1.00 25.49  ? 163  VAL A CG2   1 
ATOM   1143 N  N     . GLY A 1 164  ? 100.949 100.932 104.382 1.00 28.10  ? 164  GLY A N     1 
ATOM   1144 C  CA    . GLY A 1 164  ? 100.260 101.378 103.183 1.00 28.10  ? 164  GLY A CA    1 
ATOM   1145 C  C     . GLY A 1 164  ? 101.209 101.643 102.030 1.00 28.10  ? 164  GLY A C     1 
ATOM   1146 O  O     . GLY A 1 164  ? 100.954 101.231 100.897 1.00 28.10  ? 164  GLY A O     1 
ATOM   1147 N  N     . ASN A 1 165  ? 102.323 102.325 102.306 1.00 29.17  ? 165  ASN A N     1 
ATOM   1148 C  CA    . ASN A 1 165  ? 103.306 102.589 101.259 1.00 29.17  ? 165  ASN A CA    1 
ATOM   1149 C  C     . ASN A 1 165  ? 103.925 101.296 100.743 1.00 29.17  ? 165  ASN A C     1 
ATOM   1150 O  O     . ASN A 1 165  ? 104.137 101.137 99.533  1.00 29.17  ? 165  ASN A O     1 
ATOM   1151 C  CB    . ASN A 1 165  ? 104.391 103.529 101.781 1.00 29.17  ? 165  ASN A CB    1 
ATOM   1152 C  CG    . ASN A 1 165  ? 103.896 104.949 101.960 1.00 29.17  ? 165  ASN A CG    1 
ATOM   1153 O  OD1   . ASN A 1 165  ? 103.082 105.437 101.177 1.00 29.17  ? 165  ASN A OD1   1 
ATOM   1154 N  ND2   . ASN A 1 165  ? 104.387 105.622 102.992 1.00 29.17  ? 165  ASN A ND2   1 
ATOM   1155 N  N     . PHE A 1 166  ? 104.232 100.365 101.648 1.00 26.38  ? 166  PHE A N     1 
ATOM   1156 C  CA    . PHE A 1 166  ? 104.811 99.094  101.226 1.00 26.38  ? 166  PHE A CA    1 
ATOM   1157 C  C     . PHE A 1 166  ? 103.843 98.316  100.342 1.00 26.38  ? 166  PHE A C     1 
ATOM   1158 O  O     . PHE A 1 166  ? 104.241 97.754  99.312  1.00 26.38  ? 166  PHE A O     1 
ATOM   1159 C  CB    . PHE A 1 166  ? 105.208 98.272  102.451 1.00 26.38  ? 166  PHE A CB    1 
ATOM   1160 C  CG    . PHE A 1 166  ? 105.853 96.961  102.120 1.00 26.38  ? 166  PHE A CG    1 
ATOM   1161 C  CD1   . PHE A 1 166  ? 107.165 96.912  101.684 1.00 26.38  ? 166  PHE A CD1   1 
ATOM   1162 C  CD2   . PHE A 1 166  ? 105.152 95.777  102.251 1.00 26.38  ? 166  PHE A CD2   1 
ATOM   1163 C  CE1   . PHE A 1 166  ? 107.764 95.706  101.380 1.00 26.38  ? 166  PHE A CE1   1 
ATOM   1164 C  CE2   . PHE A 1 166  ? 105.746 94.568  101.950 1.00 26.38  ? 166  PHE A CE2   1 
ATOM   1165 C  CZ    . PHE A 1 166  ? 107.053 94.534  101.513 1.00 26.38  ? 166  PHE A CZ    1 
ATOM   1166 N  N     . ILE A 1 167  ? 102.564 98.284  100.721 1.00 28.08  ? 167  ILE A N     1 
ATOM   1167 C  CA    . ILE A 1 167  ? 101.564 97.599  99.910  1.00 28.08  ? 167  ILE A CA    1 
ATOM   1168 C  C     . ILE A 1 167  ? 101.403 98.294  98.566  1.00 28.08  ? 167  ILE A C     1 
ATOM   1169 O  O     . ILE A 1 167  ? 101.219 97.640  97.535  1.00 28.08  ? 167  ILE A O     1 
ATOM   1170 C  CB    . ILE A 1 167  ? 100.229 97.508  100.670 1.00 28.08  ? 167  ILE A CB    1 
ATOM   1171 C  CG1   . ILE A 1 167  ? 100.372 96.606  101.894 1.00 28.08  ? 167  ILE A CG1   1 
ATOM   1172 C  CG2   . ILE A 1 167  ? 99.131  96.976  99.766  1.00 28.08  ? 167  ILE A CG2   1 
ATOM   1173 C  CD1   . ILE A 1 167  ? 99.272  96.787  102.911 1.00 28.08  ? 167  ILE A CD1   1 
ATOM   1174 N  N     . HIS A 1 168  ? 101.474 99.627  98.551  1.00 29.47  ? 168  HIS A N     1 
ATOM   1175 C  CA    . HIS A 1 168  ? 101.385 100.366 97.296  1.00 29.47  ? 168  HIS A CA    1 
ATOM   1176 C  C     . HIS A 1 168  ? 102.519 99.986  96.351  1.00 29.47  ? 168  HIS A C     1 
ATOM   1177 O  O     . HIS A 1 168  ? 102.294 99.719  95.165  1.00 29.47  ? 168  HIS A O     1 
ATOM   1178 C  CB    . HIS A 1 168  ? 101.393 101.867 97.585  1.00 29.47  ? 168  HIS A CB    1 
ATOM   1179 C  CG    . HIS A 1 168  ? 101.798 102.711 96.418  1.00 29.47  ? 168  HIS A CG    1 
ATOM   1180 N  ND1   . HIS A 1 168  ? 103.112 103.025 96.148  1.00 29.47  ? 168  HIS A ND1   1 
ATOM   1181 C  CD2   . HIS A 1 168  ? 101.062 103.319 95.459  1.00 29.47  ? 168  HIS A CD2   1 
ATOM   1182 C  CE1   . HIS A 1 168  ? 103.169 103.784 95.069  1.00 29.47  ? 168  HIS A CE1   1 
ATOM   1183 N  NE2   . HIS A 1 168  ? 101.939 103.977 94.631  1.00 29.47  ? 168  HIS A NE2   1 
ATOM   1184 N  N     . TYR A 1 169  ? 103.750 99.947  96.867  1.00 30.21  ? 169  TYR A N     1 
ATOM   1185 C  CA    . TYR A 1 169  ? 104.889 99.594  96.023  1.00 30.21  ? 169  TYR A CA    1 
ATOM   1186 C  C     . TYR A 1 169  ? 104.790 98.156  95.526  1.00 30.21  ? 169  TYR A C     1 
ATOM   1187 O  O     . TYR A 1 169  ? 105.052 97.877  94.347  1.00 30.21  ? 169  TYR A O     1 
ATOM   1188 C  CB    . TYR A 1 169  ? 106.194 99.811  96.784  1.00 30.21  ? 169  TYR A CB    1 
ATOM   1189 C  CG    . TYR A 1 169  ? 106.539 101.267 96.987  1.00 30.21  ? 169  TYR A CG    1 
ATOM   1190 C  CD1   . TYR A 1 169  ? 106.281 102.203 95.997  1.00 30.21  ? 169  TYR A CD1   1 
ATOM   1191 C  CD2   . TYR A 1 169  ? 107.118 101.706 98.168  1.00 30.21  ? 169  TYR A CD2   1 
ATOM   1192 C  CE1   . TYR A 1 169  ? 106.592 103.535 96.177  1.00 30.21  ? 169  TYR A CE1   1 
ATOM   1193 C  CE2   . TYR A 1 169  ? 107.431 103.036 98.358  1.00 30.21  ? 169  TYR A CE2   1 
ATOM   1194 C  CZ    . TYR A 1 169  ? 107.166 103.946 97.359  1.00 30.21  ? 169  TYR A CZ    1 
ATOM   1195 O  OH    . TYR A 1 169  ? 107.478 105.273 97.543  1.00 30.21  ? 169  TYR A OH    1 
ATOM   1196 N  N     . LEU A 1 170  ? 104.411 97.228  96.409  1.00 31.52  ? 170  LEU A N     1 
ATOM   1197 C  CA    . LEU A 1 170  ? 104.274 95.837  95.991  1.00 31.52  ? 170  LEU A CA    1 
ATOM   1198 C  C     . LEU A 1 170  ? 103.184 95.682  94.939  1.00 31.52  ? 170  LEU A C     1 
ATOM   1199 O  O     . LEU A 1 170  ? 103.349 94.935  93.966  1.00 31.52  ? 170  LEU A O     1 
ATOM   1200 C  CB    . LEU A 1 170  ? 103.984 94.949  97.200  1.00 31.52  ? 170  LEU A CB    1 
ATOM   1201 C  CG    . LEU A 1 170  ? 105.198 94.285  97.849  1.00 31.52  ? 170  LEU A CG    1 
ATOM   1202 C  CD1   . LEU A 1 170  ? 104.756 93.230  98.848  1.00 31.52  ? 170  LEU A CD1   1 
ATOM   1203 C  CD2   . LEU A 1 170  ? 106.106 93.682  96.792  1.00 31.52  ? 170  LEU A CD2   1 
ATOM   1204 N  N     . SER A 1 171  ? 102.061 96.381  95.115  1.00 33.14  ? 171  SER A N     1 
ATOM   1205 C  CA    . SER A 1 171  ? 100.986 96.318  94.135  1.00 33.14  ? 171  SER A CA    1 
ATOM   1206 C  C     . SER A 1 171  ? 101.430 96.891  92.799  1.00 33.14  ? 171  SER A C     1 
ATOM   1207 O  O     . SER A 1 171  ? 101.073 96.362  91.743  1.00 33.14  ? 171  SER A O     1 
ATOM   1208 C  CB    . SER A 1 171  ? 99.758  97.062  94.658  1.00 33.14  ? 171  SER A CB    1 
ATOM   1209 O  OG    . SER A 1 171  ? 100.023 98.447  94.779  1.00 33.14  ? 171  SER A OG    1 
ATOM   1210 N  N     . THR A 1 172  ? 102.210 97.976  92.824  1.00 35.56  ? 172  THR A N     1 
ATOM   1211 C  CA    . THR A 1 172  ? 102.739 98.523  91.578  1.00 35.56  ? 172  THR A CA    1 
ATOM   1212 C  C     . THR A 1 172  ? 103.628 97.511  90.868  1.00 35.56  ? 172  THR A C     1 
ATOM   1213 O  O     . THR A 1 172  ? 103.517 97.320  89.650  1.00 35.56  ? 172  THR A O     1 
ATOM   1214 C  CB    . THR A 1 172  ? 103.519 99.809  91.852  1.00 35.56  ? 172  THR A CB    1 
ATOM   1215 O  OG1   . THR A 1 172  ? 102.653 100.778 92.453  1.00 35.56  ? 172  THR A OG1   1 
ATOM   1216 C  CG2   . THR A 1 172  ? 104.072 100.376 90.561  1.00 35.56  ? 172  THR A CG2   1 
ATOM   1217 N  N     . PHE A 1 173  ? 104.512 96.846  91.616  1.00 40.83  ? 173  PHE A N     1 
ATOM   1218 C  CA    . PHE A 1 173  ? 105.401 95.863  91.002  1.00 40.83  ? 173  PHE A CA    1 
ATOM   1219 C  C     . PHE A 1 173  ? 104.613 94.702  90.403  1.00 40.83  ? 173  PHE A C     1 
ATOM   1220 O  O     . PHE A 1 173  ? 104.879 94.270  89.274  1.00 40.83  ? 173  PHE A O     1 
ATOM   1221 C  CB    . PHE A 1 173  ? 106.414 95.357  92.029  1.00 40.83  ? 173  PHE A CB    1 
ATOM   1222 C  CG    . PHE A 1 173  ? 107.221 94.183  91.556  1.00 40.83  ? 173  PHE A CG    1 
ATOM   1223 C  CD1   . PHE A 1 173  ? 108.182 94.336  90.573  1.00 40.83  ? 173  PHE A CD1   1 
ATOM   1224 C  CD2   . PHE A 1 173  ? 107.023 92.925  92.100  1.00 40.83  ? 173  PHE A CD2   1 
ATOM   1225 C  CE1   . PHE A 1 173  ? 108.926 93.257  90.136  1.00 40.83  ? 173  PHE A CE1   1 
ATOM   1226 C  CE2   . PHE A 1 173  ? 107.766 91.843  91.667  1.00 40.83  ? 173  PHE A CE2   1 
ATOM   1227 C  CZ    . PHE A 1 173  ? 108.718 92.010  90.684  1.00 40.83  ? 173  PHE A CZ    1 
ATOM   1228 N  N     . LEU A 1 174  ? 103.630 94.186  91.146  1.00 43.51  ? 174  LEU A N     1 
ATOM   1229 C  CA    . LEU A 1 174  ? 102.831 93.076  90.633  1.00 43.51  ? 174  LEU A CA    1 
ATOM   1230 C  C     . LEU A 1 174  ? 101.996 93.492  89.427  1.00 43.51  ? 174  LEU A C     1 
ATOM   1231 O  O     . LEU A 1 174  ? 101.831 92.710  88.484  1.00 43.51  ? 174  LEU A O     1 
ATOM   1232 C  CB    . LEU A 1 174  ? 101.940 92.499  91.735  1.00 43.51  ? 174  LEU A CB    1 
ATOM   1233 C  CG    . LEU A 1 174  ? 102.535 91.434  92.667  1.00 43.51  ? 174  LEU A CG    1 
ATOM   1234 C  CD1   . LEU A 1 174  ? 102.886 90.187  91.870  1.00 43.51  ? 174  LEU A CD1   1 
ATOM   1235 C  CD2   . LEU A 1 174  ? 103.749 91.922  93.441  1.00 43.51  ? 174  LEU A CD2   1 
ATOM   1236 N  N     . ALA A 1 175  ? 101.454 94.711  89.438  1.00 44.94  ? 175  ALA A N     1 
ATOM   1237 C  CA    . ALA A 1 175  ? 100.691 95.188  88.290  1.00 44.94  ? 175  ALA A CA    1 
ATOM   1238 C  C     . ALA A 1 175  ? 101.578 95.319  87.060  1.00 44.94  ? 175  ALA A C     1 
ATOM   1239 O  O     . ALA A 1 175  ? 101.165 94.972  85.947  1.00 44.94  ? 175  ALA A O     1 
ATOM   1240 C  CB    . ALA A 1 175  ? 100.023 96.521  88.619  1.00 44.94  ? 175  ALA A CB    1 
ATOM   1241 N  N     . GLY A 1 176  ? 102.802 95.819  87.240  1.00 48.65  ? 176  GLY A N     1 
ATOM   1242 C  CA    . GLY A 1 176  ? 103.736 95.867  86.127  1.00 48.65  ? 176  GLY A CA    1 
ATOM   1243 C  C     . GLY A 1 176  ? 104.073 94.486  85.598  1.00 48.65  ? 176  GLY A C     1 
ATOM   1244 O  O     . GLY A 1 176  ? 104.170 94.280  84.386  1.00 48.65  ? 176  GLY A O     1 
ATOM   1245 N  N     . LEU A 1 177  ? 104.250 93.520  86.501  1.00 53.08  ? 177  LEU A N     1 
ATOM   1246 C  CA    . LEU A 1 177  ? 104.519 92.150  86.074  1.00 53.08  ? 177  LEU A CA    1 
ATOM   1247 C  C     . LEU A 1 177  ? 103.350 91.583  85.276  1.00 53.08  ? 177  LEU A C     1 
ATOM   1248 O  O     . LEU A 1 177  ? 103.549 90.926  84.245  1.00 53.08  ? 177  LEU A O     1 
ATOM   1249 C  CB    . LEU A 1 177  ? 104.819 91.283  87.298  1.00 53.08  ? 177  LEU A CB    1 
ATOM   1250 C  CG    . LEU A 1 177  ? 105.306 89.841  87.141  1.00 53.08  ? 177  LEU A CG    1 
ATOM   1251 C  CD1   . LEU A 1 177  ? 106.121 89.467  88.363  1.00 53.08  ? 177  LEU A CD1   1 
ATOM   1252 C  CD2   . LEU A 1 177  ? 104.152 88.865  86.967  1.00 53.08  ? 177  LEU A CD2   1 
ATOM   1253 N  N     . VAL A 1 178  ? 102.122 91.828  85.737  1.00 50.98  ? 178  VAL A N     1 
ATOM   1254 C  CA    . VAL A 1 178  ? 100.943 91.335  85.028  1.00 50.98  ? 178  VAL A CA    1 
ATOM   1255 C  C     . VAL A 1 178  ? 100.833 91.990  83.657  1.00 50.98  ? 178  VAL A C     1 
ATOM   1256 O  O     . VAL A 1 178  ? 100.491 91.335  82.665  1.00 50.98  ? 178  VAL A O     1 
ATOM   1257 C  CB    . VAL A 1 178  ? 99.675  91.564  85.872  1.00 50.98  ? 178  VAL A CB    1 
ATOM   1258 C  CG1   . VAL A 1 178  ? 98.429  91.269  85.054  1.00 50.98  ? 178  VAL A CG1   1 
ATOM   1259 C  CG2   . VAL A 1 178  ? 99.708  90.699  87.120  1.00 50.98  ? 178  VAL A CG2   1 
ATOM   1260 N  N     . VAL A 1 179  ? 101.119 93.292  83.580  1.00 54.10  ? 179  VAL A N     1 
ATOM   1261 C  CA    . VAL A 1 179  ? 101.112 93.984  82.294  1.00 54.10  ? 179  VAL A CA    1 
ATOM   1262 C  C     . VAL A 1 179  ? 102.143 93.368  81.357  1.00 54.10  ? 179  VAL A C     1 
ATOM   1263 O  O     . VAL A 1 179  ? 101.876 93.153  80.168  1.00 54.10  ? 179  VAL A O     1 
ATOM   1264 C  CB    . VAL A 1 179  ? 101.355 95.491  82.500  1.00 54.10  ? 179  VAL A CB    1 
ATOM   1265 C  CG1   . VAL A 1 179  ? 101.831 96.140  81.212  1.00 54.10  ? 179  VAL A CG1   1 
ATOM   1266 C  CG2   . VAL A 1 179  ? 100.092 96.165  83.005  1.00 54.10  ? 179  VAL A CG2   1 
ATOM   1267 N  N     . GLY A 1 180  ? 103.333 93.069  81.879  1.00 58.44  ? 180  GLY A N     1 
ATOM   1268 C  CA    . GLY A 1 180  ? 104.342 92.408  81.067  1.00 58.44  ? 180  GLY A CA    1 
ATOM   1269 C  C     . GLY A 1 180  ? 103.897 91.043  80.576  1.00 58.44  ? 180  GLY A C     1 
ATOM   1270 O  O     . GLY A 1 180  ? 104.225 90.639  79.459  1.00 58.44  ? 180  GLY A O     1 
ATOM   1271 N  N     . PHE A 1 181  ? 103.148 90.312  81.408  1.00 63.09  ? 181  PHE A N     1 
ATOM   1272 C  CA    . PHE A 1 181  ? 102.608 89.023  80.981  1.00 63.09  ? 181  PHE A CA    1 
ATOM   1273 C  C     . PHE A 1 181  ? 101.714 89.171  79.756  1.00 63.09  ? 181  PHE A C     1 
ATOM   1274 O  O     . PHE A 1 181  ? 101.706 88.302  78.877  1.00 63.09  ? 181  PHE A O     1 
ATOM   1275 C  CB    . PHE A 1 181  ? 101.829 88.367  82.124  1.00 63.09  ? 181  PHE A CB    1 
ATOM   1276 C  CG    . PHE A 1 181  ? 102.673 87.524  83.037  1.00 63.09  ? 181  PHE A CG    1 
ATOM   1277 C  CD1   . PHE A 1 181  ? 102.084 86.708  83.989  1.00 63.09  ? 181  PHE A CD1   1 
ATOM   1278 C  CD2   . PHE A 1 181  ? 104.048 87.524  82.927  1.00 63.09  ? 181  PHE A CD2   1 
ATOM   1279 C  CE1   . PHE A 1 181  ? 102.859 85.925  84.827  1.00 63.09  ? 181  PHE A CE1   1 
ATOM   1280 C  CE2   . PHE A 1 181  ? 104.829 86.746  83.759  1.00 63.09  ? 181  PHE A CE2   1 
ATOM   1281 C  CZ    . PHE A 1 181  ? 104.234 85.944  84.710  1.00 63.09  ? 181  PHE A CZ    1 
ATOM   1282 N  N     . VAL A 1 182  ? 100.948 90.261  79.684  1.00 63.27  ? 182  VAL A N     1 
ATOM   1283 C  CA    . VAL A 1 182  ? 99.965  90.410  78.614  1.00 63.27  ? 182  VAL A CA    1 
ATOM   1284 C  C     . VAL A 1 182  ? 100.645 90.649  77.271  1.00 63.27  ? 182  VAL A C     1 
ATOM   1285 O  O     . VAL A 1 182  ? 100.273 90.046  76.257  1.00 63.27  ? 182  VAL A O     1 
ATOM   1286 C  CB    . VAL A 1 182  ? 98.977  91.539  78.956  1.00 63.27  ? 182  VAL A CB    1 
ATOM   1287 C  CG1   . VAL A 1 182  ? 98.017  91.771  77.801  1.00 63.27  ? 182  VAL A CG1   1 
ATOM   1288 C  CG2   . VAL A 1 182  ? 98.214  91.210  80.229  1.00 63.27  ? 182  VAL A CG2   1 
ATOM   1289 N  N     . SER A 1 183  ? 101.652 91.524  77.234  1.00 68.50  ? 183  SER A N     1 
ATOM   1290 C  CA    . SER A 1 183  ? 102.205 91.958  75.953  1.00 68.50  ? 183  SER A CA    1 
ATOM   1291 C  C     . SER A 1 183  ? 103.152 90.917  75.362  1.00 68.50  ? 183  SER A C     1 
ATOM   1292 O  O     . SER A 1 183  ? 102.896 90.370  74.284  1.00 68.50  ? 183  SER A O     1 
ATOM   1293 C  CB    . SER A 1 183  ? 102.917 93.303  76.121  1.00 68.50  ? 183  SER A CB    1 
ATOM   1294 O  OG    . SER A 1 183  ? 104.037 93.183  76.980  1.00 68.50  ? 183  SER A OG    1 
ATOM   1295 N  N     . ALA A 1 184  ? 104.255 90.635  76.053  1.00 73.04  ? 184  ALA A N     1 
ATOM   1296 C  CA    . ALA A 1 184  ? 105.229 89.642  75.604  1.00 73.04  ? 184  ALA A CA    1 
ATOM   1297 C  C     . ALA A 1 184  ? 105.774 88.939  76.836  1.00 73.04  ? 184  ALA A C     1 
ATOM   1298 O  O     . ALA A 1 184  ? 106.285 89.599  77.745  1.00 73.04  ? 184  ALA A O     1 
ATOM   1299 C  CB    . ALA A 1 184  ? 106.358 90.291  74.801  1.00 73.04  ? 184  ALA A CB    1 
ATOM   1300 N  N     . TRP A 1 185  ? 105.675 87.607  76.864  1.00 75.82  ? 185  TRP A N     1 
ATOM   1301 C  CA    . TRP A 1 185  ? 105.851 86.902  78.130  1.00 75.82  ? 185  TRP A CA    1 
ATOM   1302 C  C     . TRP A 1 185  ? 107.315 86.843  78.558  1.00 75.82  ? 185  TRP A C     1 
ATOM   1303 O  O     . TRP A 1 185  ? 107.618 87.086  79.728  1.00 75.82  ? 185  TRP A O     1 
ATOM   1304 C  CB    . TRP A 1 185  ? 105.231 85.500  78.054  1.00 75.82  ? 185  TRP A CB    1 
ATOM   1305 C  CG    . TRP A 1 185  ? 105.786 84.570  77.011  1.00 75.82  ? 185  TRP A CG    1 
ATOM   1306 C  CD1   . TRP A 1 185  ? 107.027 84.004  76.986  1.00 75.82  ? 185  TRP A CD1   1 
ATOM   1307 C  CD2   . TRP A 1 185  ? 105.107 84.094  75.845  1.00 75.82  ? 185  TRP A CD2   1 
ATOM   1308 N  NE1   . TRP A 1 185  ? 107.163 83.208  75.876  1.00 75.82  ? 185  TRP A NE1   1 
ATOM   1309 C  CE2   . TRP A 1 185  ? 105.997 83.247  75.158  1.00 75.82  ? 185  TRP A CE2   1 
ATOM   1310 C  CE3   . TRP A 1 185  ? 103.832 84.305  75.314  1.00 75.82  ? 185  TRP A CE3   1 
ATOM   1311 C  CZ2   . TRP A 1 185  ? 105.654 82.611  73.967  1.00 75.82  ? 185  TRP A CZ2   1 
ATOM   1312 C  CZ3   . TRP A 1 185  ? 103.493 83.673  74.132  1.00 75.82  ? 185  TRP A CZ3   1 
ATOM   1313 C  CH2   . TRP A 1 185  ? 104.400 82.837  73.472  1.00 75.82  ? 185  TRP A CH2   1 
ATOM   1314 N  N     . LYS A 1 186  ? 108.238 86.588  77.624  1.00 73.91  ? 186  LYS A N     1 
ATOM   1315 C  CA    . LYS A 1 186  ? 109.624 86.294  77.999  1.00 73.91  ? 186  LYS A CA    1 
ATOM   1316 C  C     . LYS A 1 186  ? 110.222 87.415  78.837  1.00 73.91  ? 186  LYS A C     1 
ATOM   1317 O  O     . LYS A 1 186  ? 110.958 87.170  79.806  1.00 73.91  ? 186  LYS A O     1 
ATOM   1318 C  CB    . LYS A 1 186  ? 110.474 86.065  76.747  1.00 73.91  ? 186  LYS A CB    1 
ATOM   1319 C  CG    . LYS A 1 186  ? 110.171 84.785  75.992  1.00 73.91  ? 186  LYS A CG    1 
ATOM   1320 C  CD    . LYS A 1 186  ? 110.979 83.614  76.533  1.00 73.91  ? 186  LYS A CD    1 
ATOM   1321 C  CE    . LYS A 1 186  ? 112.423 84.003  76.799  1.00 73.91  ? 186  LYS A CE    1 
ATOM   1322 N  NZ    . LYS A 1 186  ? 113.275 82.807  77.031  1.00 73.91  ? 186  LYS A NZ    1 
ATOM   1323 N  N     . LEU A 1 187  ? 109.907 88.655  78.478  1.00 71.88  ? 187  LEU A N     1 
ATOM   1324 C  CA    . LEU A 1 187  ? 110.455 89.798  79.191  1.00 71.88  ? 187  LEU A CA    1 
ATOM   1325 C  C     . LEU A 1 187  ? 110.004 89.762  80.648  1.00 71.88  ? 187  LEU A C     1 
ATOM   1326 O  O     . LEU A 1 187  ? 110.796 89.986  81.576  1.00 71.88  ? 187  LEU A O     1 
ATOM   1327 C  CB    . LEU A 1 187  ? 109.983 91.074  78.492  1.00 71.88  ? 187  LEU A CB    1 
ATOM   1328 C  CG    . LEU A 1 187  ? 110.488 91.282  77.049  1.00 71.88  ? 187  LEU A CG    1 
ATOM   1329 C  CD1   . LEU A 1 187  ? 109.854 92.514  76.394  1.00 71.88  ? 187  LEU A CD1   1 
ATOM   1330 C  CD2   . LEU A 1 187  ? 112.000 91.270  76.875  1.00 71.88  ? 187  LEU A CD2   1 
ATOM   1331 N  N     . ALA A 1 188  ? 108.732 89.424  80.863  1.00 72.52  ? 188  ALA A N     1 
ATOM   1332 C  CA    . ALA A 1 188  ? 108.184 89.347  82.208  1.00 72.52  ? 188  ALA A CA    1 
ATOM   1333 C  C     . ALA A 1 188  ? 108.658 88.103  82.952  1.00 72.52  ? 188  ALA A C     1 
ATOM   1334 O  O     . ALA A 1 188  ? 108.756 88.129  84.182  1.00 72.52  ? 188  ALA A O     1 
ATOM   1335 C  CB    . ALA A 1 188  ? 106.661 89.396  82.138  1.00 72.52  ? 188  ALA A CB    1 
ATOM   1336 N  N     . LEU A 1 189  ? 108.966 87.011  82.242  1.00 72.07  ? 189  LEU A N     1 
ATOM   1337 C  CA    . LEU A 1 189  ? 109.635 85.891  82.905  1.00 72.07  ? 189  LEU A CA    1 
ATOM   1338 C  C     . LEU A 1 189  ? 110.996 86.302  83.447  1.00 72.07  ? 189  LEU A C     1 
ATOM   1339 O  O     . LEU A 1 189  ? 111.371 85.896  84.551  1.00 72.07  ? 189  LEU A O     1 
ATOM   1340 C  CB    . LEU A 1 189  ? 109.770 84.671  81.987  1.00 72.07  ? 189  LEU A CB    1 
ATOM   1341 C  CG    . LEU A 1 189  ? 108.583 83.730  81.729  1.00 72.07  ? 189  LEU A CG    1 
ATOM   1342 C  CD1   . LEU A 1 189  ? 107.487 84.307  80.866  1.00 72.07  ? 189  LEU A CD1   1 
ATOM   1343 C  CD2   . LEU A 1 189  ? 109.088 82.437  81.120  1.00 72.07  ? 189  LEU A CD2   1 
ATOM   1344 N  N     . LEU A 1 190  ? 111.753 87.104  82.696  1.00 68.86  ? 190  LEU A N     1 
ATOM   1345 C  CA    . LEU A 1 190  ? 112.984 87.655  83.266  1.00 68.86  ? 190  LEU A CA    1 
ATOM   1346 C  C     . LEU A 1 190  ? 112.683 88.529  84.484  1.00 68.86  ? 190  LEU A C     1 
ATOM   1347 O  O     . LEU A 1 190  ? 113.338 88.411  85.536  1.00 68.86  ? 190  LEU A O     1 
ATOM   1348 C  CB    . LEU A 1 190  ? 113.746 88.462  82.215  1.00 68.86  ? 190  LEU A CB    1 
ATOM   1349 C  CG    . LEU A 1 190  ? 113.900 87.813  80.837  1.00 68.86  ? 190  LEU A CG    1 
ATOM   1350 C  CD1   . LEU A 1 190  ? 114.645 88.727  79.875  1.00 68.86  ? 190  LEU A CD1   1 
ATOM   1351 C  CD2   . LEU A 1 190  ? 114.586 86.455  80.932  1.00 68.86  ? 190  LEU A CD2   1 
ATOM   1352 N  N     . SER A 1 191  ? 111.685 89.410  84.357  1.00 68.51  ? 191  SER A N     1 
ATOM   1353 C  CA    . SER A 1 191  ? 111.352 90.339  85.433  1.00 68.51  ? 191  SER A CA    1 
ATOM   1354 C  C     . SER A 1 191  ? 110.827 89.641  86.685  1.00 68.51  ? 191  SER A C     1 
ATOM   1355 O  O     . SER A 1 191  ? 110.875 90.227  87.771  1.00 68.51  ? 191  SER A O     1 
ATOM   1356 C  CB    . SER A 1 191  ? 110.328 91.362  84.940  1.00 68.51  ? 191  SER A CB    1 
ATOM   1357 O  OG    . SER A 1 191  ? 110.886 92.196  83.940  1.00 68.51  ? 191  SER A OG    1 
ATOM   1358 N  N     . VAL A 1 192  ? 110.308 88.421  86.558  1.00 65.56  ? 192  VAL A N     1 
ATOM   1359 C  CA    . VAL A 1 192  ? 109.855 87.664  87.720  1.00 65.56  ? 192  VAL A CA    1 
ATOM   1360 C  C     . VAL A 1 192  ? 110.930 86.710  88.232  1.00 65.56  ? 192  VAL A C     1 
ATOM   1361 O  O     . VAL A 1 192  ? 110.941 86.394  89.431  1.00 65.56  ? 192  VAL A O     1 
ATOM   1362 C  CB    . VAL A 1 192  ? 108.553 86.889  87.412  1.00 65.56  ? 192  VAL A CB    1 
ATOM   1363 C  CG1   . VAL A 1 192  ? 108.807 85.773  86.419  1.00 65.56  ? 192  VAL A CG1   1 
ATOM   1364 C  CG2   . VAL A 1 192  ? 107.927 86.339  88.685  1.00 65.56  ? 192  VAL A CG2   1 
ATOM   1365 N  N     . ALA A 1 193  ? 111.838 86.253  87.370  1.00 68.33  ? 193  ALA A N     1 
ATOM   1366 C  CA    . ALA A 1 193  ? 112.936 85.415  87.822  1.00 68.33  ? 193  ALA A CA    1 
ATOM   1367 C  C     . ALA A 1 193  ? 114.019 86.212  88.530  1.00 68.33  ? 193  ALA A C     1 
ATOM   1368 O  O     . ALA A 1 193  ? 114.866 85.614  89.203  1.00 68.33  ? 193  ALA A O     1 
ATOM   1369 C  CB    . ALA A 1 193  ? 113.543 84.655  86.642  1.00 68.33  ? 193  ALA A CB    1 
ATOM   1370 N  N     . VAL A 1 194  ? 114.029 87.541  88.383  1.00 64.42  ? 194  VAL A N     1 
ATOM   1371 C  CA    . VAL A 1 194  ? 115.002 88.336  89.136  1.00 64.42  ? 194  VAL A CA    1 
ATOM   1372 C  C     . VAL A 1 194  ? 114.591 88.597  90.578  1.00 64.42  ? 194  VAL A C     1 
ATOM   1373 O  O     . VAL A 1 194  ? 115.324 89.287  91.298  1.00 64.42  ? 194  VAL A O     1 
ATOM   1374 C  CB    . VAL A 1 194  ? 115.279 89.686  88.447  1.00 64.42  ? 194  VAL A CB    1 
ATOM   1375 C  CG1   . VAL A 1 194  ? 116.121 89.470  87.204  1.00 64.42  ? 194  VAL A CG1   1 
ATOM   1376 C  CG2   . VAL A 1 194  ? 113.981 90.388  88.109  1.00 64.42  ? 194  VAL A CG2   1 
ATOM   1377 N  N     . ILE A 1 195  ? 113.448 88.069  91.028  1.00 61.58  ? 195  ILE A N     1 
ATOM   1378 C  CA    . ILE A 1 195  ? 112.992 88.324  92.402  1.00 61.58  ? 195  ILE A CA    1 
ATOM   1379 C  C     . ILE A 1 195  ? 113.925 87.762  93.475  1.00 61.58  ? 195  ILE A C     1 
ATOM   1380 O  O     . ILE A 1 195  ? 114.185 88.468  94.465  1.00 61.58  ? 195  ILE A O     1 
ATOM   1381 C  CB    . ILE A 1 195  ? 111.546 87.827  92.578  1.00 61.58  ? 195  ILE A CB    1 
ATOM   1382 C  CG1   . ILE A 1 195  ? 110.594 88.611  91.678  1.00 61.58  ? 195  ILE A CG1   1 
ATOM   1383 C  CG2   . ILE A 1 195  ? 111.109 87.935  94.030  1.00 61.58  ? 195  ILE A CG2   1 
ATOM   1384 C  CD1   . ILE A 1 195  ? 109.208 88.020  91.614  1.00 61.58  ? 195  ILE A CD1   1 
ATOM   1385 N  N     . PRO A 1 196  ? 114.429 86.521  93.374  1.00 59.35  ? 196  PRO A N     1 
ATOM   1386 C  CA    . PRO A 1 196  ? 115.124 85.927  94.532  1.00 59.35  ? 196  PRO A CA    1 
ATOM   1387 C  C     . PRO A 1 196  ? 116.287 86.743  95.066  1.00 59.35  ? 196  PRO A C     1 
ATOM   1388 O  O     . PRO A 1 196  ? 116.539 86.704  96.275  1.00 59.35  ? 196  PRO A O     1 
ATOM   1389 C  CB    . PRO A 1 196  ? 115.594 84.570  93.992  1.00 59.35  ? 196  PRO A CB    1 
ATOM   1390 C  CG    . PRO A 1 196  ? 114.595 84.226  92.969  1.00 59.35  ? 196  PRO A CG    1 
ATOM   1391 C  CD    . PRO A 1 196  ? 114.245 85.523  92.303  1.00 59.35  ? 196  PRO A CD    1 
ATOM   1392 N  N     . GLY A 1 197  ? 117.009 87.476  94.218  1.00 57.45  ? 197  GLY A N     1 
ATOM   1393 C  CA    . GLY A 1 197  ? 118.081 88.317  94.729  1.00 57.45  ? 197  GLY A CA    1 
ATOM   1394 C  C     . GLY A 1 197  ? 117.571 89.393  95.670  1.00 57.45  ? 197  GLY A C     1 
ATOM   1395 O  O     . GLY A 1 197  ? 118.110 89.591  96.765  1.00 57.45  ? 197  GLY A O     1 
ATOM   1396 N  N     . ILE A 1 198  ? 116.507 90.090  95.261  1.00 54.04  ? 198  ILE A N     1 
ATOM   1397 C  CA    . ILE A 1 198  ? 115.904 91.106  96.119  1.00 54.04  ? 198  ILE A CA    1 
ATOM   1398 C  C     . ILE A 1 198  ? 115.361 90.471  97.391  1.00 54.04  ? 198  ILE A C     1 
ATOM   1399 O  O     . ILE A 1 198  ? 115.511 91.021  98.490  1.00 54.04  ? 198  ILE A O     1 
ATOM   1400 C  CB    . ILE A 1 198  ? 114.808 91.880  95.361  1.00 54.04  ? 198  ILE A CB    1 
ATOM   1401 C  CG1   . ILE A 1 198  ? 115.407 92.705  94.218  1.00 54.04  ? 198  ILE A CG1   1 
ATOM   1402 C  CG2   . ILE A 1 198  ? 114.026 92.777  96.309  1.00 54.04  ? 198  ILE A CG2   1 
ATOM   1403 C  CD1   . ILE A 1 198  ? 115.470 91.987  92.894  1.00 54.04  ? 198  ILE A CD1   1 
ATOM   1404 N  N     . ALA A 1 199  ? 114.722 89.304  97.267  1.00 53.58  ? 199  ALA A N     1 
ATOM   1405 C  CA    . ALA A 1 199  ? 114.174 88.640  98.447  1.00 53.58  ? 199  ALA A CA    1 
ATOM   1406 C  C     . ALA A 1 199  ? 115.273 88.291  99.446  1.00 53.58  ? 199  ALA A C     1 
ATOM   1407 O  O     . ALA A 1 199  ? 115.132 88.524  100.653 1.00 53.58  ? 199  ALA A O     1 
ATOM   1408 C  CB    . ALA A 1 199  ? 113.404 87.387  98.030  1.00 53.58  ? 199  ALA A CB    1 
ATOM   1409 N  N     . PHE A 1 200  ? 116.384 87.738  98.955  1.00 51.44  ? 200  PHE A N     1 
ATOM   1410 C  CA    . PHE A 1 200  ? 117.473 87.329  99.835  1.00 51.44  ? 200  PHE A CA    1 
ATOM   1411 C  C     . PHE A 1 200  ? 118.126 88.543  100.489 1.00 51.44  ? 200  PHE A C     1 
ATOM   1412 O  O     . PHE A 1 200  ? 118.443 88.524  101.689 1.00 51.44  ? 200  PHE A O     1 
ATOM   1413 C  CB    . PHE A 1 200  ? 118.486 86.511  99.027  1.00 51.44  ? 200  PHE A CB    1 
ATOM   1414 C  CG    . PHE A 1 200  ? 119.479 85.747  99.861  1.00 51.44  ? 200  PHE A CG    1 
ATOM   1415 C  CD1   . PHE A 1 200  ? 120.471 86.391  100.579 1.00 51.44  ? 200  PHE A CD1   1 
ATOM   1416 C  CD2   . PHE A 1 200  ? 119.416 84.365  99.915  1.00 51.44  ? 200  PHE A CD2   1 
ATOM   1417 C  CE1   . PHE A 1 200  ? 121.375 85.667  101.334 1.00 51.44  ? 200  PHE A CE1   1 
ATOM   1418 C  CE2   . PHE A 1 200  ? 120.316 83.641  100.670 1.00 51.44  ? 200  PHE A CE2   1 
ATOM   1419 C  CZ    . PHE A 1 200  ? 121.296 84.293  101.380 1.00 51.44  ? 200  PHE A CZ    1 
ATOM   1420 N  N     . ALA A 1 201  ? 118.326 89.615  99.714  1.00 47.13  ? 201  ALA A N     1 
ATOM   1421 C  CA    . ALA A 1 201  ? 118.886 90.839  100.278 1.00 47.13  ? 201  ALA A CA    1 
ATOM   1422 C  C     . ALA A 1 201  ? 117.981 91.409  101.361 1.00 47.13  ? 201  ALA A C     1 
ATOM   1423 O  O     . ALA A 1 201  ? 118.458 91.833  102.421 1.00 47.13  ? 201  ALA A O     1 
ATOM   1424 C  CB    . ALA A 1 201  ? 119.116 91.869  99.174  1.00 47.13  ? 201  ALA A CB    1 
ATOM   1425 N  N     . GLY A 1 202  ? 116.669 91.420  101.117 1.00 41.27  ? 202  GLY A N     1 
ATOM   1426 C  CA    . GLY A 1 202  ? 115.744 91.908  102.126 1.00 41.27  ? 202  GLY A CA    1 
ATOM   1427 C  C     . GLY A 1 202  ? 115.748 91.056  103.379 1.00 41.27  ? 202  GLY A C     1 
ATOM   1428 O  O     . GLY A 1 202  ? 115.652 91.575  104.493 1.00 41.27  ? 202  GLY A O     1 
ATOM   1429 N  N     . GLY A 1 203  ? 115.859 89.736  103.215 1.00 40.36  ? 203  GLY A N     1 
ATOM   1430 C  CA    . GLY A 1 203  ? 115.929 88.866  104.379 1.00 40.36  ? 203  GLY A CA    1 
ATOM   1431 C  C     . GLY A 1 203  ? 117.155 89.136  105.231 1.00 40.36  ? 203  GLY A C     1 
ATOM   1432 O  O     . GLY A 1 203  ? 117.063 89.258  106.459 1.00 40.36  ? 203  GLY A O     1 
ATOM   1433 N  N     . LEU A 1 204  ? 118.323 89.246  104.588 1.00 39.85  ? 204  LEU A N     1 
ATOM   1434 C  CA    . LEU A 1 204  ? 119.537 89.569  105.336 1.00 39.85  ? 204  LEU A CA    1 
ATOM   1435 C  C     . LEU A 1 204  ? 119.418 90.923  106.018 1.00 39.85  ? 204  LEU A C     1 
ATOM   1436 O  O     . LEU A 1 204  ? 119.814 91.081  107.181 1.00 39.85  ? 204  LEU A O     1 
ATOM   1437 C  CB    . LEU A 1 204  ? 120.758 89.558  104.419 1.00 39.85  ? 204  LEU A CB    1 
ATOM   1438 C  CG    . LEU A 1 204  ? 121.216 88.239  103.809 1.00 39.85  ? 204  LEU A CG    1 
ATOM   1439 C  CD1   . LEU A 1 204  ? 122.360 88.502  102.844 1.00 39.85  ? 204  LEU A CD1   1 
ATOM   1440 C  CD2   . LEU A 1 204  ? 121.638 87.274  104.899 1.00 39.85  ? 204  LEU A CD2   1 
ATOM   1441 N  N     . TYR A 1 205  ? 118.881 91.914  105.304 1.00 34.57  ? 205  TYR A N     1 
ATOM   1442 C  CA    . TYR A 1 205  ? 118.745 93.253  105.862 1.00 34.57  ? 205  TYR A CA    1 
ATOM   1443 C  C     . TYR A 1 205  ? 117.845 93.240  107.091 1.00 34.57  ? 205  TYR A C     1 
ATOM   1444 O  O     . TYR A 1 205  ? 118.181 93.825  108.128 1.00 34.57  ? 205  TYR A O     1 
ATOM   1445 C  CB    . TYR A 1 205  ? 118.198 94.187  104.782 1.00 34.57  ? 205  TYR A CB    1 
ATOM   1446 C  CG    . TYR A 1 205  ? 117.970 95.613  105.210 1.00 34.57  ? 205  TYR A CG    1 
ATOM   1447 C  CD1   . TYR A 1 205  ? 119.032 96.430  105.562 1.00 34.57  ? 205  TYR A CD1   1 
ATOM   1448 C  CD2   . TYR A 1 205  ? 116.695 96.154  105.228 1.00 34.57  ? 205  TYR A CD2   1 
ATOM   1449 C  CE1   . TYR A 1 205  ? 118.826 97.739  105.937 1.00 34.57  ? 205  TYR A CE1   1 
ATOM   1450 C  CE2   . TYR A 1 205  ? 116.482 97.460  105.602 1.00 34.57  ? 205  TYR A CE2   1 
ATOM   1451 C  CZ    . TYR A 1 205  ? 117.549 98.248  105.959 1.00 34.57  ? 205  TYR A CZ    1 
ATOM   1452 O  OH    . TYR A 1 205  ? 117.338 99.553  106.335 1.00 34.57  ? 205  TYR A OH    1 
ATOM   1453 N  N     . ALA A 1 206  ? 116.707 92.547  107.002 1.00 31.66  ? 206  ALA A N     1 
ATOM   1454 C  CA    . ALA A 1 206  ? 115.786 92.478  108.130 1.00 31.66  ? 206  ALA A CA    1 
ATOM   1455 C  C     . ALA A 1 206  ? 116.418 91.774  109.323 1.00 31.66  ? 206  ALA A C     1 
ATOM   1456 O  O     . ALA A 1 206  ? 116.302 92.245  110.461 1.00 31.66  ? 206  ALA A O     1 
ATOM   1457 C  CB    . ALA A 1 206  ? 114.498 91.770  107.712 1.00 31.66  ? 206  ALA A CB    1 
ATOM   1458 N  N     . TYR A 1 207  ? 117.093 90.646  109.085 1.00 32.76  ? 207  TYR A N     1 
ATOM   1459 C  CA    . TYR A 1 207  ? 117.712 89.912  110.186 1.00 32.76  ? 207  TYR A CA    1 
ATOM   1460 C  C     . TYR A 1 207  ? 118.771 90.760  110.886 1.00 32.76  ? 207  TYR A C     1 
ATOM   1461 O  O     . TYR A 1 207  ? 118.782 90.879  112.124 1.00 32.76  ? 207  TYR A O     1 
ATOM   1462 C  CB    . TYR A 1 207  ? 118.313 88.609  109.656 1.00 32.76  ? 207  TYR A CB    1 
ATOM   1463 C  CG    . TYR A 1 207  ? 118.927 87.721  110.712 1.00 32.76  ? 207  TYR A CG    1 
ATOM   1464 C  CD1   . TYR A 1 207  ? 118.337 87.579  111.959 1.00 32.76  ? 207  TYR A CD1   1 
ATOM   1465 C  CD2   . TYR A 1 207  ? 120.094 87.015  110.456 1.00 32.76  ? 207  TYR A CD2   1 
ATOM   1466 C  CE1   . TYR A 1 207  ? 118.896 86.765  112.925 1.00 32.76  ? 207  TYR A CE1   1 
ATOM   1467 C  CE2   . TYR A 1 207  ? 120.661 86.199  111.414 1.00 32.76  ? 207  TYR A CE2   1 
ATOM   1468 C  CZ    . TYR A 1 207  ? 120.058 86.077  112.647 1.00 32.76  ? 207  TYR A CZ    1 
ATOM   1469 O  OH    . TYR A 1 207  ? 120.618 85.265  113.606 1.00 32.76  ? 207  TYR A OH    1 
ATOM   1470 N  N     . THR A 1 208  ? 119.661 91.376  110.103 1.00 31.89  ? 208  THR A N     1 
ATOM   1471 C  CA    . THR A 1 208  ? 120.729 92.177  110.686 1.00 31.89  ? 208  THR A CA    1 
ATOM   1472 C  C     . THR A 1 208  ? 120.172 93.381  111.436 1.00 31.89  ? 208  THR A C     1 
ATOM   1473 O  O     . THR A 1 208  ? 120.648 93.714  112.528 1.00 31.89  ? 208  THR A O     1 
ATOM   1474 C  CB    . THR A 1 208  ? 121.701 92.622  109.595 1.00 31.89  ? 208  THR A CB    1 
ATOM   1475 O  OG1   . THR A 1 208  ? 122.131 91.479  108.847 1.00 31.89  ? 208  THR A OG1   1 
ATOM   1476 C  CG2   . THR A 1 208  ? 122.914 93.290  110.205 1.00 31.89  ? 208  THR A CG2   1 
ATOM   1477 N  N     . LEU A 1 209  ? 119.157 94.044  110.872 1.00 32.52  ? 209  LEU A N     1 
ATOM   1478 C  CA    . LEU A 1 209  ? 118.577 95.199  111.547 1.00 32.52  ? 209  LEU A CA    1 
ATOM   1479 C  C     . LEU A 1 209  ? 117.869 94.803  112.833 1.00 32.52  ? 209  LEU A C     1 
ATOM   1480 O  O     . LEU A 1 209  ? 117.933 95.537  113.822 1.00 32.52  ? 209  LEU A O     1 
ATOM   1481 C  CB    . LEU A 1 209  ? 117.629 95.947  110.611 1.00 32.52  ? 209  LEU A CB    1 
ATOM   1482 C  CG    . LEU A 1 209  ? 118.267 97.084  109.813 1.00 32.52  ? 209  LEU A CG    1 
ATOM   1483 C  CD1   . LEU A 1 209  ? 118.673 98.201  110.758 1.00 32.52  ? 209  LEU A CD1   1 
ATOM   1484 C  CD2   . LEU A 1 209  ? 119.478 96.599  109.045 1.00 32.52  ? 209  LEU A CD2   1 
ATOM   1485 N  N     . THR A 1 210  ? 117.191 93.653  112.850 1.00 30.61  ? 210  THR A N     1 
ATOM   1486 C  CA    . THR A 1 210  ? 116.561 93.204  114.088 1.00 30.61  ? 210  THR A CA    1 
ATOM   1487 C  C     . THR A 1 210  ? 117.606 92.959  115.169 1.00 30.61  ? 210  THR A C     1 
ATOM   1488 O  O     . THR A 1 210  ? 117.443 93.389  116.319 1.00 30.61  ? 210  THR A O     1 
ATOM   1489 C  CB    . THR A 1 210  ? 115.739 91.939  113.839 1.00 30.61  ? 210  THR A CB    1 
ATOM   1490 O  OG1   . THR A 1 210  ? 116.488 91.034  113.021 1.00 30.61  ? 210  THR A OG1   1 
ATOM   1491 C  CG2   . THR A 1 210  ? 114.432 92.281  113.146 1.00 30.61  ? 210  THR A CG2   1 
ATOM   1492 N  N     . GLY A 1 211  ? 118.700 92.283  114.810 1.00 30.65  ? 211  GLY A N     1 
ATOM   1493 C  CA    . GLY A 1 211  ? 119.751 92.048  115.791 1.00 30.65  ? 211  GLY A CA    1 
ATOM   1494 C  C     . GLY A 1 211  ? 120.356 93.338  116.316 1.00 30.65  ? 211  GLY A C     1 
ATOM   1495 O  O     . GLY A 1 211  ? 120.517 93.524  117.530 1.00 30.65  ? 211  GLY A O     1 
ATOM   1496 N  N     . ILE A 1 212  ? 120.683 94.258  115.405 1.00 31.22  ? 212  ILE A N     1 
ATOM   1497 C  CA    . ILE A 1 212  ? 121.304 95.516  115.806 1.00 31.22  ? 212  ILE A CA    1 
ATOM   1498 C  C     . ILE A 1 212  ? 120.345 96.346  116.649 1.00 31.22  ? 212  ILE A C     1 
ATOM   1499 O  O     . ILE A 1 212  ? 120.755 97.006  117.610 1.00 31.22  ? 212  ILE A O     1 
ATOM   1500 C  CB    . ILE A 1 212  ? 121.794 96.288  114.568 1.00 31.22  ? 212  ILE A CB    1 
ATOM   1501 C  CG1   . ILE A 1 212  ? 122.877 95.488  113.846 1.00 31.22  ? 212  ILE A CG1   1 
ATOM   1502 C  CG2   . ILE A 1 212  ? 122.317 97.657  114.956 1.00 31.22  ? 212  ILE A CG2   1 
ATOM   1503 C  CD1   . ILE A 1 212  ? 123.231 96.036  112.494 1.00 31.22  ? 212  ILE A CD1   1 
ATOM   1504 N  N     . THR A 1 213  ? 119.055 96.330  116.304 1.00 28.49  ? 213  THR A N     1 
ATOM   1505 C  CA    . THR A 1 213  ? 118.069 97.066  117.085 1.00 28.49  ? 213  THR A CA    1 
ATOM   1506 C  C     . THR A 1 213  ? 117.950 96.499  118.491 1.00 28.49  ? 213  THR A C     1 
ATOM   1507 O  O     . THR A 1 213  ? 117.839 97.255  119.461 1.00 28.49  ? 213  THR A O     1 
ATOM   1508 C  CB    . THR A 1 213  ? 116.715 97.041  116.380 1.00 28.49  ? 213  THR A CB    1 
ATOM   1509 O  OG1   . THR A 1 213  ? 116.839 97.649  115.088 1.00 28.49  ? 213  THR A OG1   1 
ATOM   1510 C  CG2   . THR A 1 213  ? 115.678 97.801  117.190 1.00 28.49  ? 213  THR A CG2   1 
ATOM   1511 N  N     . SER A 1 214  ? 117.971 95.170  118.625 1.00 27.18  ? 214  SER A N     1 
ATOM   1512 C  CA    . SER A 1 214  ? 117.936 94.574  119.958 1.00 27.18  ? 214  SER A CA    1 
ATOM   1513 C  C     . SER A 1 214  ? 119.143 95.008  120.782 1.00 27.18  ? 214  SER A C     1 
ATOM   1514 O  O     . SER A 1 214  ? 119.007 95.421  121.943 1.00 27.18  ? 214  SER A O     1 
ATOM   1515 C  CB    . SER A 1 214  ? 117.875 93.051  119.851 1.00 27.18  ? 214  SER A CB    1 
ATOM   1516 O  OG    . SER A 1 214  ? 116.622 92.625  119.350 1.00 27.18  ? 214  SER A OG    1 
ATOM   1517 N  N     . LYS A 1 215  ? 120.338 94.939  120.187 1.00 28.56  ? 215  LYS A N     1 
ATOM   1518 C  CA    . LYS A 1 215  ? 121.538 95.331  120.923 1.00 28.56  ? 215  LYS A CA    1 
ATOM   1519 C  C     . LYS A 1 215  ? 121.500 96.807  121.309 1.00 28.56  ? 215  LYS A C     1 
ATOM   1520 O  O     . LYS A 1 215  ? 121.850 97.173  122.439 1.00 28.56  ? 215  LYS A O     1 
ATOM   1521 C  CB    . LYS A 1 215  ? 122.789 95.024  120.101 1.00 28.56  ? 215  LYS A CB    1 
ATOM   1522 C  CG    . LYS A 1 215  ? 122.857 93.601  119.580 1.00 28.56  ? 215  LYS A CG    1 
ATOM   1523 C  CD    . LYS A 1 215  ? 123.579 92.686  120.550 1.00 28.56  ? 215  LYS A CD    1 
ATOM   1524 C  CE    . LYS A 1 215  ? 123.964 91.378  119.882 1.00 28.56  ? 215  LYS A CE    1 
ATOM   1525 N  NZ    . LYS A 1 215  ? 124.706 91.609  118.612 1.00 28.56  ? 215  LYS A NZ    1 
ATOM   1526 N  N     . SER A 1 216  ? 121.072 97.670  120.385 1.00 29.21  ? 216  SER A N     1 
ATOM   1527 C  CA    . SER A 1 216  ? 121.032 99.101  120.666 1.00 29.21  ? 216  SER A CA    1 
ATOM   1528 C  C     . SER A 1 216  ? 119.981 99.435  121.717 1.00 29.21  ? 216  SER A C     1 
ATOM   1529 O  O     . SER A 1 216  ? 120.191 100.326 122.545 1.00 29.21  ? 216  SER A O     1 
ATOM   1530 C  CB    . SER A 1 216  ? 120.772 99.880  119.377 1.00 29.21  ? 216  SER A CB    1 
ATOM   1531 O  OG    . SER A 1 216  ? 119.510 99.548  118.827 1.00 29.21  ? 216  SER A OG    1 
ATOM   1532 N  N     . ARG A 1 217  ? 118.840 98.742  121.694 1.00 27.50  ? 217  ARG A N     1 
ATOM   1533 C  CA    . ARG A 1 217  ? 117.830 98.950  122.725 1.00 27.50  ? 217  ARG A CA    1 
ATOM   1534 C  C     . ARG A 1 217  ? 118.358 98.545  124.093 1.00 27.50  ? 217  ARG A C     1 
ATOM   1535 O  O     . ARG A 1 217  ? 118.138 99.250  125.086 1.00 27.50  ? 217  ARG A O     1 
ATOM   1536 C  CB    . ARG A 1 217  ? 116.562 98.168  122.381 1.00 27.50  ? 217  ARG A CB    1 
ATOM   1537 C  CG    . ARG A 1 217  ? 115.341 98.559  123.196 1.00 27.50  ? 217  ARG A CG    1 
ATOM   1538 C  CD    . ARG A 1 217  ? 115.036 97.533  124.274 1.00 27.50  ? 217  ARG A CD    1 
ATOM   1539 N  NE    . ARG A 1 217  ? 113.821 97.864  125.014 1.00 27.50  ? 217  ARG A NE    1 
ATOM   1540 C  CZ    . ARG A 1 217  ? 113.679 97.710  126.326 1.00 27.50  ? 217  ARG A CZ    1 
ATOM   1541 N  NH1   . ARG A 1 217  ? 112.537 98.039  126.914 1.00 27.50  ? 217  ARG A NH1   1 
ATOM   1542 N  NH2   . ARG A 1 217  ? 114.678 97.228  127.053 1.00 27.50  ? 217  ARG A NH2   1 
ATOM   1543 N  N     . GLU A 1 218  ? 119.066 97.415  124.163 1.00 26.29  ? 218  GLU A N     1 
ATOM   1544 C  CA    . GLU A 1 218  ? 119.672 97.012  125.429 1.00 26.29  ? 218  GLU A CA    1 
ATOM   1545 C  C     . GLU A 1 218  ? 120.677 98.052  125.907 1.00 26.29  ? 218  GLU A C     1 
ATOM   1546 O  O     . GLU A 1 218  ? 120.725 98.387  127.096 1.00 26.29  ? 218  GLU A O     1 
ATOM   1547 C  CB    . GLU A 1 218  ? 120.338 95.644  125.284 1.00 26.29  ? 218  GLU A CB    1 
ATOM   1548 C  CG    . GLU A 1 218  ? 120.986 95.129  126.561 1.00 26.29  ? 218  GLU A CG    1 
ATOM   1549 C  CD    . GLU A 1 218  ? 120.130 95.364  127.791 1.00 26.29  ? 218  GLU A CD    1 
ATOM   1550 O  OE1   . GLU A 1 218  ? 120.550 96.144  128.671 1.00 26.29  ? 218  GLU A OE1   1 
ATOM   1551 O  OE2   . GLU A 1 218  ? 119.035 94.770  127.878 1.00 26.29  ? 218  GLU A OE2   1 
ATOM   1552 N  N     . SER A 1 219  ? 121.492 98.577  124.989 1.00 25.59  ? 219  SER A N     1 
ATOM   1553 C  CA    . SER A 1 219  ? 122.470 99.593  125.367 1.00 25.59  ? 219  SER A CA    1 
ATOM   1554 C  C     . SER A 1 219  ? 121.791 100.864 125.867 1.00 25.59  ? 219  SER A C     1 
ATOM   1555 O  O     . SER A 1 219  ? 122.227 101.461 126.857 1.00 25.59  ? 219  SER A O     1 
ATOM   1556 C  CB    . SER A 1 219  ? 123.385 99.906  124.184 1.00 25.59  ? 219  SER A CB    1 
ATOM   1557 O  OG    . SER A 1 219  ? 124.186 98.786  123.851 1.00 25.59  ? 219  SER A OG    1 
ATOM   1558 N  N     . TYR A 1 220  ? 120.723 101.293 125.191 1.00 26.21  ? 220  TYR A N     1 
ATOM   1559 C  CA    . TYR A 1 220  ? 120.049 102.532 125.567 1.00 26.21  ? 220  TYR A CA    1 
ATOM   1560 C  C     . TYR A 1 220  ? 119.320 102.392 126.897 1.00 26.21  ? 220  TYR A C     1 
ATOM   1561 O  O     . TYR A 1 220  ? 119.246 103.353 127.671 1.00 26.21  ? 220  TYR A O     1 
ATOM   1562 C  CB    . TYR A 1 220  ? 119.072 102.953 124.470 1.00 26.21  ? 220  TYR A CB    1 
ATOM   1563 C  CG    . TYR A 1 220  ? 119.729 103.572 123.259 1.00 26.21  ? 220  TYR A CG    1 
ATOM   1564 C  CD1   . TYR A 1 220  ? 119.159 103.451 121.999 1.00 26.21  ? 220  TYR A CD1   1 
ATOM   1565 C  CD2   . TYR A 1 220  ? 120.915 104.283 123.375 1.00 26.21  ? 220  TYR A CD2   1 
ATOM   1566 C  CE1   . TYR A 1 220  ? 119.752 104.017 120.889 1.00 26.21  ? 220  TYR A CE1   1 
ATOM   1567 C  CE2   . TYR A 1 220  ? 121.516 104.853 122.271 1.00 26.21  ? 220  TYR A CE2   1 
ATOM   1568 C  CZ    . TYR A 1 220  ? 120.931 104.716 121.031 1.00 26.21  ? 220  TYR A CZ    1 
ATOM   1569 O  OH    . TYR A 1 220  ? 121.527 105.282 119.927 1.00 26.21  ? 220  TYR A OH    1 
ATOM   1570 N  N     . ALA A 1 221  ? 118.764 101.209 127.174 1.00 24.56  ? 221  ALA A N     1 
ATOM   1571 C  CA    . ALA A 1 221  ? 118.012 101.022 128.412 1.00 24.56  ? 221  ALA A CA    1 
ATOM   1572 C  C     . ALA A 1 221  ? 118.894 101.241 129.635 1.00 24.56  ? 221  ALA A C     1 
ATOM   1573 O  O     . ALA A 1 221  ? 118.469 101.869 130.611 1.00 24.56  ? 221  ALA A O     1 
ATOM   1574 C  CB    . ALA A 1 221  ? 117.388 99.628  128.443 1.00 24.56  ? 221  ALA A CB    1 
ATOM   1575 N  N     . ASN A 1 222  ? 120.125 100.726 129.603 1.00 24.67  ? 222  ASN A N     1 
ATOM   1576 C  CA    . ASN A 1 222  ? 121.045 100.938 130.715 1.00 24.67  ? 222  ASN A CA    1 
ATOM   1577 C  C     . ASN A 1 222  ? 121.384 102.413 130.879 1.00 24.67  ? 222  ASN A C     1 
ATOM   1578 O  O     . ASN A 1 222  ? 121.489 102.911 132.005 1.00 24.67  ? 222  ASN A O     1 
ATOM   1579 C  CB    . ASN A 1 222  ? 122.318 100.119 130.509 1.00 24.67  ? 222  ASN A CB    1 
ATOM   1580 C  CG    . ASN A 1 222  ? 122.291 98.806  131.258 1.00 24.67  ? 222  ASN A CG    1 
ATOM   1581 O  OD1   . ASN A 1 222  ? 121.827 98.737  132.395 1.00 24.67  ? 222  ASN A OD1   1 
ATOM   1582 N  ND2   . ASN A 1 222  ? 122.793 97.754  130.624 1.00 24.67  ? 222  ASN A ND2   1 
ATOM   1583 N  N     . ALA A 1 223  ? 121.574 103.124 129.766 1.00 23.31  ? 223  ALA A N     1 
ATOM   1584 C  CA    . ALA A 1 223  ? 121.915 104.540 129.842 1.00 23.31  ? 223  ALA A CA    1 
ATOM   1585 C  C     . ALA A 1 223  ? 120.790 105.351 130.472 1.00 23.31  ? 223  ALA A C     1 
ATOM   1586 O  O     . ALA A 1 223  ? 121.043 106.255 131.277 1.00 23.31  ? 223  ALA A O     1 
ATOM   1587 C  CB    . ALA A 1 223  ? 122.247 105.074 128.449 1.00 23.31  ? 223  ALA A CB    1 
ATOM   1588 N  N     . GLY A 1 224  ? 119.541 105.045 130.118 1.00 23.63  ? 224  GLY A N     1 
ATOM   1589 C  CA    . GLY A 1 224  ? 118.423 105.796 130.666 1.00 23.63  ? 224  GLY A CA    1 
ATOM   1590 C  C     . GLY A 1 224  ? 118.271 105.620 132.164 1.00 23.63  ? 224  GLY A C     1 
ATOM   1591 O  O     . GLY A 1 224  ? 117.943 106.572 132.879 1.00 23.63  ? 224  GLY A O     1 
ATOM   1592 N  N     . VAL A 1 225  ? 118.499 104.403 132.660 1.00 22.13  ? 225  VAL A N     1 
ATOM   1593 C  CA    . VAL A 1 225  ? 118.392 104.145 134.093 1.00 22.13  ? 225  VAL A CA    1 
ATOM   1594 C  C     . VAL A 1 225  ? 119.436 104.946 134.860 1.00 22.13  ? 225  VAL A C     1 
ATOM   1595 O  O     . VAL A 1 225  ? 119.149 105.515 135.920 1.00 22.13  ? 225  VAL A O     1 
ATOM   1596 C  CB    . VAL A 1 225  ? 118.517 102.636 134.373 1.00 22.13  ? 225  VAL A CB    1 
ATOM   1597 C  CG1   . VAL A 1 225  ? 118.766 102.382 135.850 1.00 22.13  ? 225  VAL A CG1   1 
ATOM   1598 C  CG2   . VAL A 1 225  ? 117.270 101.907 133.903 1.00 22.13  ? 225  VAL A CG2   1 
ATOM   1599 N  N     . ILE A 1 226  ? 120.661 105.004 134.336 1.00 20.66  ? 226  ILE A N     1 
ATOM   1600 C  CA    . ILE A 1 226  ? 121.740 105.701 135.030 1.00 20.66  ? 226  ILE A CA    1 
ATOM   1601 C  C     . ILE A 1 226  ? 121.431 107.187 135.156 1.00 20.66  ? 226  ILE A C     1 
ATOM   1602 O  O     . ILE A 1 226  ? 121.638 107.792 136.215 1.00 20.66  ? 226  ILE A O     1 
ATOM   1603 C  CB    . ILE A 1 226  ? 123.078 105.459 134.309 1.00 20.66  ? 226  ILE A CB    1 
ATOM   1604 C  CG1   . ILE A 1 226  ? 123.509 104.001 134.471 1.00 20.66  ? 226  ILE A CG1   1 
ATOM   1605 C  CG2   . ILE A 1 226  ? 124.148 106.390 134.844 1.00 20.66  ? 226  ILE A CG2   1 
ATOM   1606 C  CD1   . ILE A 1 226  ? 124.669 103.607 133.589 1.00 20.66  ? 226  ILE A CD1   1 
ATOM   1607 N  N     . ALA A 1 227  ? 120.932 107.801 134.081 1.00 21.42  ? 227  ALA A N     1 
ATOM   1608 C  CA    . ALA A 1 227  ? 120.636 109.230 134.115 1.00 21.42  ? 227  ALA A CA    1 
ATOM   1609 C  C     . ALA A 1 227  ? 119.514 109.540 135.099 1.00 21.42  ? 227  ALA A C     1 
ATOM   1610 O  O     . ALA A 1 227  ? 119.613 110.480 135.897 1.00 21.42  ? 227  ALA A O     1 
ATOM   1611 C  CB    . ALA A 1 227  ? 120.276 109.723 132.714 1.00 21.42  ? 227  ALA A CB    1 
ATOM   1612 N  N     . GLU A 1 228  ? 118.433 108.759 135.054 1.00 23.40  ? 228  GLU A N     1 
ATOM   1613 C  CA    . GLU A 1 228  ? 117.300 109.012 135.939 1.00 23.40  ? 228  GLU A CA    1 
ATOM   1614 C  C     . GLU A 1 228  ? 117.674 108.790 137.398 1.00 23.40  ? 228  GLU A C     1 
ATOM   1615 O  O     . GLU A 1 228  ? 117.214 109.523 138.281 1.00 23.40  ? 228  GLU A O     1 
ATOM   1616 C  CB    . GLU A 1 228  ? 116.118 108.128 135.546 1.00 23.40  ? 228  GLU A CB    1 
ATOM   1617 C  CG    . GLU A 1 228  ? 115.025 108.059 136.594 1.00 23.40  ? 228  GLU A CG    1 
ATOM   1618 C  CD    . GLU A 1 228  ? 113.967 107.034 136.261 1.00 23.40  ? 228  GLU A CD    1 
ATOM   1619 O  OE1   . GLU A 1 228  ? 113.816 106.708 135.066 1.00 23.40  ? 228  GLU A OE1   1 
ATOM   1620 O  OE2   . GLU A 1 228  ? 113.288 106.552 137.192 1.00 23.40  ? 228  GLU A OE2   1 
ATOM   1621 N  N     . GLN A 1 229  ? 118.503 107.783 137.673 1.00 19.54  ? 229  GLN A N     1 
ATOM   1622 C  CA    . GLN A 1 229  ? 118.948 107.547 139.042 1.00 19.54  ? 229  GLN A CA    1 
ATOM   1623 C  C     . GLN A 1 229  ? 119.724 108.741 139.582 1.00 19.54  ? 229  GLN A C     1 
ATOM   1624 O  O     . GLN A 1 229  ? 119.552 109.128 140.743 1.00 19.54  ? 229  GLN A O     1 
ATOM   1625 C  CB    . GLN A 1 229  ? 119.798 106.279 139.102 1.00 19.54  ? 229  GLN A CB    1 
ATOM   1626 C  CG    . GLN A 1 229  ? 120.057 105.768 140.504 1.00 19.54  ? 229  GLN A CG    1 
ATOM   1627 C  CD    . GLN A 1 229  ? 121.420 105.126 140.638 1.00 19.54  ? 229  GLN A CD    1 
ATOM   1628 O  OE1   . GLN A 1 229  ? 121.548 104.014 141.149 1.00 19.54  ? 229  GLN A OE1   1 
ATOM   1629 N  NE2   . GLN A 1 229  ? 122.450 105.825 140.178 1.00 19.54  ? 229  GLN A NE2   1 
ATOM   1630 N  N     . ALA A 1 230  ? 120.586 109.334 138.756 1.00 20.50  ? 230  ALA A N     1 
ATOM   1631 C  CA    . ALA A 1 230  ? 121.327 110.514 139.188 1.00 20.50  ? 230  ALA A CA    1 
ATOM   1632 C  C     . ALA A 1 230  ? 120.409 111.719 139.343 1.00 20.50  ? 230  ALA A C     1 
ATOM   1633 O  O     . ALA A 1 230  ? 120.599 112.541 140.245 1.00 20.50  ? 230  ALA A O     1 
ATOM   1634 C  CB    . ALA A 1 230  ? 122.451 110.819 138.200 1.00 20.50  ? 230  ALA A CB    1 
ATOM   1635 N  N     . ILE A 1 231  ? 119.410 111.845 138.467 1.00 20.40  ? 231  ILE A N     1 
ATOM   1636 C  CA    . ILE A 1 231  ? 118.530 113.010 138.508 1.00 20.40  ? 231  ILE A CA    1 
ATOM   1637 C  C     . ILE A 1 231  ? 117.634 112.973 139.741 1.00 20.40  ? 231  ILE A C     1 
ATOM   1638 O  O     . ILE A 1 231  ? 117.438 113.993 140.411 1.00 20.40  ? 231  ILE A O     1 
ATOM   1639 C  CB    . ILE A 1 231  ? 117.707 113.101 137.210 1.00 20.40  ? 231  ILE A CB    1 
ATOM   1640 C  CG1   . ILE A 1 231  ? 118.588 113.577 136.055 1.00 20.40  ? 231  ILE A CG1   1 
ATOM   1641 C  CG2   . ILE A 1 231  ? 116.523 114.035 137.387 1.00 20.40  ? 231  ILE A CG2   1 
ATOM   1642 C  CD1   . ILE A 1 231  ? 118.075 113.174 134.695 1.00 20.40  ? 231  ILE A CD1   1 
ATOM   1643 N  N     . ALA A 1 232  ? 117.079 111.801 140.062 1.00 19.46  ? 232  ALA A N     1 
ATOM   1644 C  CA    . ALA A 1 232  ? 116.112 111.708 141.152 1.00 19.46  ? 232  ALA A CA    1 
ATOM   1645 C  C     . ALA A 1 232  ? 116.741 112.084 142.488 1.00 19.46  ? 232  ALA A C     1 
ATOM   1646 O  O     . ALA A 1 232  ? 116.155 112.838 143.273 1.00 19.46  ? 232  ALA A O     1 
ATOM   1647 C  CB    . ALA A 1 232  ? 115.523 110.300 141.211 1.00 19.46  ? 232  ALA A CB    1 
ATOM   1648 N  N     . GLN A 1 233  ? 117.932 111.567 142.765 1.00 21.29  ? 233  GLN A N     1 
ATOM   1649 C  CA    . GLN A 1 233  ? 118.646 111.887 144.001 1.00 21.29  ? 233  GLN A CA    1 
ATOM   1650 C  C     . GLN A 1 233  ? 119.646 113.015 143.758 1.00 21.29  ? 233  GLN A C     1 
ATOM   1651 O  O     . GLN A 1 233  ? 120.854 112.870 143.943 1.00 21.29  ? 233  GLN A O     1 
ATOM   1652 C  CB    . GLN A 1 233  ? 119.335 110.642 144.548 1.00 21.29  ? 233  GLN A CB    1 
ATOM   1653 C  CG    . GLN A 1 233  ? 118.393 109.483 144.801 1.00 21.29  ? 233  GLN A CG    1 
ATOM   1654 C  CD    . GLN A 1 233  ? 119.114 108.250 145.294 1.00 21.29  ? 233  GLN A CD    1 
ATOM   1655 O  OE1   . GLN A 1 233  ? 120.320 108.279 145.536 1.00 21.29  ? 233  GLN A OE1   1 
ATOM   1656 N  NE2   . GLN A 1 233  ? 118.381 107.154 145.440 1.00 21.29  ? 233  GLN A NE2   1 
ATOM   1657 N  N     . VAL A 1 234  ? 119.113 114.161 143.334 1.00 20.37  ? 234  VAL A N     1 
ATOM   1658 C  CA    . VAL A 1 234  ? 119.969 115.285 142.972 1.00 20.37  ? 234  VAL A CA    1 
ATOM   1659 C  C     . VAL A 1 234  ? 120.692 115.829 144.198 1.00 20.37  ? 234  VAL A C     1 
ATOM   1660 O  O     . VAL A 1 234  ? 121.844 116.268 144.108 1.00 20.37  ? 234  VAL A O     1 
ATOM   1661 C  CB    . VAL A 1 234  ? 119.151 116.374 142.255 1.00 20.37  ? 234  VAL A CB    1 
ATOM   1662 C  CG1   . VAL A 1 234  ? 118.066 116.927 143.164 1.00 20.37  ? 234  VAL A CG1   1 
ATOM   1663 C  CG2   . VAL A 1 234  ? 120.062 117.484 141.760 1.00 20.37  ? 234  VAL A CG2   1 
ATOM   1664 N  N     . ARG A 1 235  ? 120.037 115.809 145.362 1.00 22.51  ? 235  ARG A N     1 
ATOM   1665 C  CA    . ARG A 1 235  ? 120.673 116.329 146.568 1.00 22.51  ? 235  ARG A CA    1 
ATOM   1666 C  C     . ARG A 1 235  ? 121.891 115.499 146.955 1.00 22.51  ? 235  ARG A C     1 
ATOM   1667 O  O     . ARG A 1 235  ? 122.940 116.051 147.307 1.00 22.51  ? 235  ARG A O     1 
ATOM   1668 C  CB    . ARG A 1 235  ? 119.664 116.373 147.715 1.00 22.51  ? 235  ARG A CB    1 
ATOM   1669 C  CG    . ARG A 1 235  ? 118.781 117.609 147.714 1.00 22.51  ? 235  ARG A CG    1 
ATOM   1670 C  CD    . ARG A 1 235  ? 117.370 117.278 148.166 1.00 22.51  ? 235  ARG A CD    1 
ATOM   1671 N  NE    . ARG A 1 235  ? 116.442 118.376 147.917 1.00 22.51  ? 235  ARG A NE    1 
ATOM   1672 C  CZ    . ARG A 1 235  ? 115.611 118.431 146.881 1.00 22.51  ? 235  ARG A CZ    1 
ATOM   1673 N  NH1   . ARG A 1 235  ? 115.589 117.446 145.993 1.00 22.51  ? 235  ARG A NH1   1 
ATOM   1674 N  NH2   . ARG A 1 235  ? 114.801 119.469 146.733 1.00 22.51  ? 235  ARG A NH2   1 
ATOM   1675 N  N     . THR A 1 236  ? 121.775 114.172 146.888 1.00 23.42  ? 236  THR A N     1 
ATOM   1676 C  CA    . THR A 1 236  ? 122.910 113.314 147.213 1.00 23.42  ? 236  THR A CA    1 
ATOM   1677 C  C     . THR A 1 236  ? 124.014 113.439 146.169 1.00 23.42  ? 236  THR A C     1 
ATOM   1678 O  O     . THR A 1 236  ? 125.202 113.417 146.509 1.00 23.42  ? 236  THR A O     1 
ATOM   1679 C  CB    . THR A 1 236  ? 122.452 111.862 147.340 1.00 23.42  ? 236  THR A CB    1 
ATOM   1680 O  OG1   . THR A 1 236  ? 121.435 111.767 148.344 1.00 23.42  ? 236  THR A OG1   1 
ATOM   1681 C  CG2   . THR A 1 236  ? 123.616 110.965 147.726 1.00 23.42  ? 236  THR A CG2   1 
ATOM   1682 N  N     . VAL A 1 237  ? 123.640 113.573 144.895 1.00 20.71  ? 237  VAL A N     1 
ATOM   1683 C  CA    . VAL A 1 237  ? 124.636 113.732 143.838 1.00 20.71  ? 237  VAL A CA    1 
ATOM   1684 C  C     . VAL A 1 237  ? 125.415 115.027 144.029 1.00 20.71  ? 237  VAL A C     1 
ATOM   1685 O  O     . VAL A 1 237  ? 126.639 115.064 143.860 1.00 20.71  ? 237  VAL A O     1 
ATOM   1686 C  CB    . VAL A 1 237  ? 123.960 113.671 142.457 1.00 20.71  ? 237  VAL A CB    1 
ATOM   1687 C  CG1   . VAL A 1 237  ? 124.857 114.279 141.396 1.00 20.71  ? 237  VAL A CG1   1 
ATOM   1688 C  CG2   . VAL A 1 237  ? 123.615 112.237 142.103 1.00 20.71  ? 237  VAL A CG2   1 
ATOM   1689 N  N     . TYR A 1 238  ? 124.721 116.110 144.381 1.00 21.04  ? 238  TYR A N     1 
ATOM   1690 C  CA    . TYR A 1 238  ? 125.405 117.383 144.587 1.00 21.04  ? 238  TYR A CA    1 
ATOM   1691 C  C     . TYR A 1 238  ? 126.254 117.360 145.852 1.00 21.04  ? 238  TYR A C     1 
ATOM   1692 O  O     . TYR A 1 238  ? 127.388 117.851 145.850 1.00 21.04  ? 238  TYR A O     1 
ATOM   1693 C  CB    . TYR A 1 238  ? 124.392 118.525 144.645 1.00 21.04  ? 238  TYR A CB    1 
ATOM   1694 C  CG    . TYR A 1 238  ? 123.821 118.921 143.301 1.00 21.04  ? 238  TYR A CG    1 
ATOM   1695 C  CD1   . TYR A 1 238  ? 124.099 118.184 142.160 1.00 21.04  ? 238  TYR A CD1   1 
ATOM   1696 C  CD2   . TYR A 1 238  ? 123.003 120.035 143.177 1.00 21.04  ? 238  TYR A CD2   1 
ATOM   1697 C  CE1   . TYR A 1 238  ? 123.577 118.542 140.935 1.00 21.04  ? 238  TYR A CE1   1 
ATOM   1698 C  CE2   . TYR A 1 238  ? 122.479 120.400 141.956 1.00 21.04  ? 238  TYR A CE2   1 
ATOM   1699 C  CZ    . TYR A 1 238  ? 122.769 119.650 140.839 1.00 21.04  ? 238  TYR A CZ    1 
ATOM   1700 O  OH    . TYR A 1 238  ? 122.250 120.008 139.618 1.00 21.04  ? 238  TYR A OH    1 
ATOM   1701 N  N     . SER A 1 239  ? 125.725 116.798 146.942 1.00 24.67  ? 239  SER A N     1 
ATOM   1702 C  CA    . SER A 1 239  ? 126.454 116.795 148.207 1.00 24.67  ? 239  SER A CA    1 
ATOM   1703 C  C     . SER A 1 239  ? 127.760 116.021 148.090 1.00 24.67  ? 239  SER A C     1 
ATOM   1704 O  O     . SER A 1 239  ? 128.826 116.516 148.471 1.00 24.67  ? 239  SER A O     1 
ATOM   1705 C  CB    . SER A 1 239  ? 125.575 116.211 149.312 1.00 24.67  ? 239  SER A CB    1 
ATOM   1706 O  OG    . SER A 1 239  ? 125.309 114.840 149.075 1.00 24.67  ? 239  SER A OG    1 
ATOM   1707 N  N     . TYR A 1 240  ? 127.694 114.799 147.570 1.00 25.76  ? 240  TYR A N     1 
ATOM   1708 C  CA    . TYR A 1 240  ? 128.880 114.005 147.253 1.00 25.76  ? 240  TYR A CA    1 
ATOM   1709 C  C     . TYR A 1 240  ? 129.154 114.224 145.770 1.00 25.76  ? 240  TYR A C     1 
ATOM   1710 O  O     . TYR A 1 240  ? 128.615 113.520 144.915 1.00 25.76  ? 240  TYR A O     1 
ATOM   1711 C  CB    . TYR A 1 240  ? 128.660 112.532 147.576 1.00 25.76  ? 240  TYR A CB    1 
ATOM   1712 C  CG    . TYR A 1 240  ? 128.382 112.257 149.033 1.00 25.76  ? 240  TYR A CG    1 
ATOM   1713 C  CD1   . TYR A 1 240  ? 129.413 112.203 149.957 1.00 25.76  ? 240  TYR A CD1   1 
ATOM   1714 C  CD2   . TYR A 1 240  ? 127.087 112.057 149.485 1.00 25.76  ? 240  TYR A CD2   1 
ATOM   1715 C  CE1   . TYR A 1 240  ? 129.164 111.952 151.289 1.00 25.76  ? 240  TYR A CE1   1 
ATOM   1716 C  CE2   . TYR A 1 240  ? 126.828 111.807 150.816 1.00 25.76  ? 240  TYR A CE2   1 
ATOM   1717 C  CZ    . TYR A 1 240  ? 127.870 111.756 151.713 1.00 25.76  ? 240  TYR A CZ    1 
ATOM   1718 O  OH    . TYR A 1 240  ? 127.620 111.508 153.042 1.00 25.76  ? 240  TYR A OH    1 
ATOM   1719 N  N     . VAL A 1 241  ? 130.007 115.206 145.472 1.00 25.16  ? 241  VAL A N     1 
ATOM   1720 C  CA    . VAL A 1 241  ? 130.191 115.703 144.112 1.00 25.16  ? 241  VAL A CA    1 
ATOM   1721 C  C     . VAL A 1 241  ? 130.491 114.547 143.162 1.00 25.16  ? 241  VAL A C     1 
ATOM   1722 O  O     . VAL A 1 241  ? 131.500 113.845 143.295 1.00 25.16  ? 241  VAL A O     1 
ATOM   1723 C  CB    . VAL A 1 241  ? 131.277 116.801 144.082 1.00 25.16  ? 241  VAL A CB    1 
ATOM   1724 C  CG1   . VAL A 1 241  ? 132.650 116.261 144.466 1.00 25.16  ? 241  VAL A CG1   1 
ATOM   1725 C  CG2   . VAL A 1 241  ? 131.332 117.463 142.724 1.00 25.16  ? 241  VAL A CG2   1 
ATOM   1726 N  N     . GLY A 1 242  ? 129.576 114.308 142.227 1.00 24.21  ? 242  GLY A N     1 
ATOM   1727 C  CA    . GLY A 1 242  ? 129.667 113.142 141.376 1.00 24.21  ? 242  GLY A CA    1 
ATOM   1728 C  C     . GLY A 1 242  ? 129.106 113.311 139.981 1.00 24.21  ? 242  GLY A C     1 
ATOM   1729 O  O     . GLY A 1 242  ? 128.795 112.315 139.322 1.00 24.21  ? 242  GLY A O     1 
ATOM   1730 N  N     . GLU A 1 243  ? 128.950 114.554 139.518 1.00 26.67  ? 243  GLU A N     1 
ATOM   1731 C  CA    . GLU A 1 243  ? 128.443 114.770 138.166 1.00 26.67  ? 243  GLU A CA    1 
ATOM   1732 C  C     . GLU A 1 243  ? 129.386 114.192 137.118 1.00 26.67  ? 243  GLU A C     1 
ATOM   1733 O  O     . GLU A 1 243  ? 128.936 113.673 136.090 1.00 26.67  ? 243  GLU A O     1 
ATOM   1734 C  CB    . GLU A 1 243  ? 128.204 116.258 137.913 1.00 26.67  ? 243  GLU A CB    1 
ATOM   1735 C  CG    . GLU A 1 243  ? 127.412 116.957 139.002 1.00 26.67  ? 243  GLU A CG    1 
ATOM   1736 C  CD    . GLU A 1 243  ? 128.297 117.641 140.016 1.00 26.67  ? 243  GLU A CD    1 
ATOM   1737 O  OE1   . GLU A 1 243  ? 129.096 116.935 140.661 1.00 26.67  ? 243  GLU A OE1   1 
ATOM   1738 O  OE2   . GLU A 1 243  ? 128.197 118.877 140.168 1.00 26.67  ? 243  GLU A OE2   1 
ATOM   1739 N  N     . SER A 1 244  ? 130.697 114.286 137.349 1.00 26.32  ? 244  SER A N     1 
ATOM   1740 C  CA    . SER A 1 244  ? 131.645 113.712 136.400 1.00 26.32  ? 244  SER A CA    1 
ATOM   1741 C  C     . SER A 1 244  ? 131.483 112.201 136.311 1.00 26.32  ? 244  SER A C     1 
ATOM   1742 O  O     . SER A 1 244  ? 131.530 111.627 135.216 1.00 26.32  ? 244  SER A O     1 
ATOM   1743 C  CB    . SER A 1 244  ? 133.076 114.074 136.792 1.00 26.32  ? 244  SER A CB    1 
ATOM   1744 O  OG    . SER A 1 244  ? 133.579 113.176 137.766 1.00 26.32  ? 244  SER A OG    1 
ATOM   1745 N  N     . LYS A 1 245  ? 131.290 111.538 137.454 1.00 27.00  ? 245  LYS A N     1 
ATOM   1746 C  CA    . LYS A 1 245  ? 131.120 110.088 137.450 1.00 27.00  ? 245  LYS A CA    1 
ATOM   1747 C  C     . LYS A 1 245  ? 129.863 109.679 136.693 1.00 27.00  ? 245  LYS A C     1 
ATOM   1748 O  O     . LYS A 1 245  ? 129.890 108.735 135.895 1.00 27.00  ? 245  LYS A O     1 
ATOM   1749 C  CB    . LYS A 1 245  ? 131.078 109.563 138.884 1.00 27.00  ? 245  LYS A CB    1 
ATOM   1750 C  CG    . LYS A 1 245  ? 132.421 109.585 139.589 1.00 27.00  ? 245  LYS A CG    1 
ATOM   1751 C  CD    . LYS A 1 245  ? 132.314 109.009 140.988 1.00 27.00  ? 245  LYS A CD    1 
ATOM   1752 C  CE    . LYS A 1 245  ? 132.576 110.074 142.038 1.00 27.00  ? 245  LYS A CE    1 
ATOM   1753 N  NZ    . LYS A 1 245  ? 132.917 109.484 143.360 1.00 27.00  ? 245  LYS A NZ    1 
ATOM   1754 N  N     . ALA A 1 246  ? 128.751 110.378 136.932 1.00 26.83  ? 246  ALA A N     1 
ATOM   1755 C  CA    . ALA A 1 246  ? 127.512 110.055 136.233 1.00 26.83  ? 246  ALA A CA    1 
ATOM   1756 C  C     . ALA A 1 246  ? 127.649 110.283 134.734 1.00 26.83  ? 246  ALA A C     1 
ATOM   1757 O  O     . ALA A 1 246  ? 127.184 109.467 133.929 1.00 26.83  ? 246  ALA A O     1 
ATOM   1758 C  CB    . ALA A 1 246  ? 126.357 110.879 136.799 1.00 26.83  ? 246  ALA A CB    1 
ATOM   1759 N  N     . LEU A 1 247  ? 128.286 111.388 134.339 1.00 27.21  ? 247  LEU A N     1 
ATOM   1760 C  CA    . LEU A 1 247  ? 128.480 111.662 132.919 1.00 27.21  ? 247  LEU A CA    1 
ATOM   1761 C  C     . LEU A 1 247  ? 129.360 110.604 132.266 1.00 27.21  ? 247  LEU A C     1 
ATOM   1762 O  O     . LEU A 1 247  ? 129.074 110.152 131.151 1.00 27.21  ? 247  LEU A O     1 
ATOM   1763 C  CB    . LEU A 1 247  ? 129.087 113.051 132.731 1.00 27.21  ? 247  LEU A CB    1 
ATOM   1764 C  CG    . LEU A 1 247  ? 128.142 114.231 132.953 1.00 27.21  ? 247  LEU A CG    1 
ATOM   1765 C  CD1   . LEU A 1 247  ? 128.904 115.541 132.881 1.00 27.21  ? 247  LEU A CD1   1 
ATOM   1766 C  CD2   . LEU A 1 247  ? 127.018 114.207 131.935 1.00 27.21  ? 247  LEU A CD2   1 
ATOM   1767 N  N     . ASN A 1 248  ? 130.438 110.201 132.941 1.00 26.81  ? 248  ASN A N     1 
ATOM   1768 C  CA    . ASN A 1 248  ? 131.310 109.172 132.384 1.00 26.81  ? 248  ASN A CA    1 
ATOM   1769 C  C     . ASN A 1 248  ? 130.582 107.841 132.257 1.00 26.81  ? 248  ASN A C     1 
ATOM   1770 O  O     . ASN A 1 248  ? 130.732 107.138 131.252 1.00 26.81  ? 248  ASN A O     1 
ATOM   1771 C  CB    . ASN A 1 248  ? 132.564 109.022 133.244 1.00 26.81  ? 248  ASN A CB    1 
ATOM   1772 C  CG    . ASN A 1 248  ? 133.447 110.250 133.201 1.00 26.81  ? 248  ASN A CG    1 
ATOM   1773 O  OD1   . ASN A 1 248  ? 133.423 111.011 132.234 1.00 26.81  ? 248  ASN A OD1   1 
ATOM   1774 N  ND2   . ASN A 1 248  ? 134.238 110.448 134.248 1.00 26.81  ? 248  ASN A ND2   1 
ATOM   1775 N  N     . ALA A 1 249  ? 129.785 107.479 133.266 1.00 26.07  ? 249  ALA A N     1 
ATOM   1776 C  CA    . ALA A 1 249  ? 129.019 106.240 133.186 1.00 26.07  ? 249  ALA A CA    1 
ATOM   1777 C  C     . ALA A 1 249  ? 128.014 106.289 132.043 1.00 26.07  ? 249  ALA A C     1 
ATOM   1778 O  O     . ALA A 1 249  ? 127.852 105.308 131.307 1.00 26.07  ? 249  ALA A O     1 
ATOM   1779 C  CB    . ALA A 1 249  ? 128.311 105.972 134.513 1.00 26.07  ? 249  ALA A CB    1 
ATOM   1780 N  N     . TYR A 1 250  ? 127.334 107.425 131.874 1.00 26.92  ? 250  TYR A N     1 
ATOM   1781 C  CA    . TYR A 1 250  ? 126.376 107.561 130.782 1.00 26.92  ? 250  TYR A CA    1 
ATOM   1782 C  C     . TYR A 1 250  ? 127.063 107.460 129.426 1.00 26.92  ? 250  TYR A C     1 
ATOM   1783 O  O     . TYR A 1 250  ? 126.551 106.801 128.513 1.00 26.92  ? 250  TYR A O     1 
ATOM   1784 C  CB    . TYR A 1 250  ? 125.627 108.885 130.905 1.00 26.92  ? 250  TYR A CB    1 
ATOM   1785 C  CG    . TYR A 1 250  ? 124.465 109.023 129.951 1.00 26.92  ? 250  TYR A CG    1 
ATOM   1786 C  CD1   . TYR A 1 250  ? 123.258 108.389 130.203 1.00 26.92  ? 250  TYR A CD1   1 
ATOM   1787 C  CD2   . TYR A 1 250  ? 124.572 109.793 128.803 1.00 26.92  ? 250  TYR A CD2   1 
ATOM   1788 C  CE1   . TYR A 1 250  ? 122.192 108.514 129.336 1.00 26.92  ? 250  TYR A CE1   1 
ATOM   1789 C  CE2   . TYR A 1 250  ? 123.511 109.924 127.931 1.00 26.92  ? 250  TYR A CE2   1 
ATOM   1790 C  CZ    . TYR A 1 250  ? 122.323 109.282 128.202 1.00 26.92  ? 250  TYR A CZ    1 
ATOM   1791 O  OH    . TYR A 1 250  ? 121.262 109.408 127.336 1.00 26.92  ? 250  TYR A OH    1 
ATOM   1792 N  N     . SER A 1 251  ? 128.220 108.107 129.272 1.00 29.39  ? 251  SER A N     1 
ATOM   1793 C  CA    . SER A 1 251  ? 128.941 108.037 128.005 1.00 29.39  ? 251  SER A CA    1 
ATOM   1794 C  C     . SER A 1 251  ? 129.425 106.622 127.723 1.00 29.39  ? 251  SER A C     1 
ATOM   1795 O  O     . SER A 1 251  ? 129.382 106.164 126.576 1.00 29.39  ? 251  SER A O     1 
ATOM   1796 C  CB    . SER A 1 251  ? 130.115 109.013 128.010 1.00 29.39  ? 251  SER A CB    1 
ATOM   1797 O  OG    . SER A 1 251  ? 131.199 108.497 128.760 1.00 29.39  ? 251  SER A OG    1 
ATOM   1798 N  N     . ASP A 1 252  ? 129.896 105.915 128.752 1.00 32.04  ? 252  ASP A N     1 
ATOM   1799 C  CA    . ASP A 1 252  ? 130.356 104.546 128.552 1.00 32.04  ? 252  ASP A CA    1 
ATOM   1800 C  C     . ASP A 1 252  ? 129.204 103.599 128.246 1.00 32.04  ? 252  ASP A C     1 
ATOM   1801 O  O     . ASP A 1 252  ? 129.391 102.613 127.525 1.00 32.04  ? 252  ASP A O     1 
ATOM   1802 C  CB    . ASP A 1 252  ? 131.122 104.061 129.780 1.00 32.04  ? 252  ASP A CB    1 
ATOM   1803 C  CG    . ASP A 1 252  ? 131.757 102.704 129.566 1.00 32.04  ? 252  ASP A CG    1 
ATOM   1804 O  OD1   . ASP A 1 252  ? 132.704 102.612 128.757 1.00 32.04  ? 252  ASP A OD1   1 
ATOM   1805 O  OD2   . ASP A 1 252  ? 131.306 101.728 130.202 1.00 32.04  ? 252  ASP A OD2   1 
ATOM   1806 N  N     . ALA A 1 253  ? 128.013 103.872 128.783 1.00 26.93  ? 253  ALA A N     1 
ATOM   1807 C  CA    . ALA A 1 253  ? 126.877 102.990 128.548 1.00 26.93  ? 253  ALA A CA    1 
ATOM   1808 C  C     . ALA A 1 253  ? 126.411 103.003 127.098 1.00 26.93  ? 253  ALA A C     1 
ATOM   1809 O  O     . ALA A 1 253  ? 125.679 102.095 126.691 1.00 26.93  ? 253  ALA A O     1 
ATOM   1810 C  CB    . ALA A 1 253  ? 125.718 103.371 129.468 1.00 26.93  ? 253  ALA A CB    1 
ATOM   1811 N  N     . ILE A 1 254  ? 126.812 104.001 126.314 1.00 28.27  ? 254  ILE A N     1 
ATOM   1812 C  CA    . ILE A 1 254  ? 126.391 104.102 124.921 1.00 28.27  ? 254  ILE A CA    1 
ATOM   1813 C  C     . ILE A 1 254  ? 127.603 103.985 124.007 1.00 28.27  ? 254  ILE A C     1 
ATOM   1814 O  O     . ILE A 1 254  ? 127.655 104.611 122.943 1.00 28.27  ? 254  ILE A O     1 
ATOM   1815 C  CB    . ILE A 1 254  ? 125.629 105.414 124.658 1.00 28.27  ? 254  ILE A CB    1 
ATOM   1816 C  CG1   . ILE A 1 254  ? 126.403 106.605 125.222 1.00 28.27  ? 254  ILE A CG1   1 
ATOM   1817 C  CG2   . ILE A 1 254  ? 124.237 105.352 125.260 1.00 28.27  ? 254  ILE A CG2   1 
ATOM   1818 C  CD1   . ILE A 1 254  ? 125.664 107.918 125.108 1.00 28.27  ? 254  ILE A CD1   1 
ATOM   1819 N  N     . GLN A 1 255  ? 128.596 103.199 124.423 1.00 37.08  ? 255  GLN A N     1 
ATOM   1820 C  CA    . GLN A 1 255  ? 129.788 103.023 123.601 1.00 37.08  ? 255  GLN A CA    1 
ATOM   1821 C  C     . GLN A 1 255  ? 129.537 102.085 122.425 1.00 37.08  ? 255  GLN A C     1 
ATOM   1822 O  O     . GLN A 1 255  ? 130.024 102.335 121.317 1.00 37.08  ? 255  GLN A O     1 
ATOM   1823 C  CB    . GLN A 1 255  ? 130.940 102.502 124.459 1.00 37.08  ? 255  GLN A CB    1 
ATOM   1824 C  CG    . GLN A 1 255  ? 132.317 102.845 123.919 1.00 37.08  ? 255  GLN A CG    1 
ATOM   1825 C  CD    . GLN A 1 255  ? 132.907 101.732 123.077 1.00 37.08  ? 255  GLN A CD    1 
ATOM   1826 O  OE1   . GLN A 1 255  ? 132.339 100.645 122.977 1.00 37.08  ? 255  GLN A OE1   1 
ATOM   1827 N  NE2   . GLN A 1 255  ? 134.057 101.998 122.467 1.00 37.08  ? 255  GLN A NE2   1 
ATOM   1828 N  N     . TYR A 1 256  ? 128.783 101.005 122.641 1.00 39.26  ? 256  TYR A N     1 
ATOM   1829 C  CA    . TYR A 1 256  ? 128.615 99.987  121.608 1.00 39.26  ? 256  TYR A CA    1 
ATOM   1830 C  C     . TYR A 1 256  ? 127.635 100.414 120.523 1.00 39.26  ? 256  TYR A C     1 
ATOM   1831 O  O     . TYR A 1 256  ? 127.708 99.909  119.392 1.00 39.26  ? 256  TYR A O     1 
ATOM   1832 C  CB    . TYR A 1 256  ? 128.144 98.677  122.238 1.00 39.26  ? 256  TYR A CB    1 
ATOM   1833 C  CG    . TYR A 1 256  ? 128.802 98.364  123.562 1.00 39.26  ? 256  TYR A CG    1 
ATOM   1834 C  CD1   . TYR A 1 256  ? 130.185 98.346  123.689 1.00 39.26  ? 256  TYR A CD1   1 
ATOM   1835 C  CD2   . TYR A 1 256  ? 128.037 98.095  124.687 1.00 39.26  ? 256  TYR A CD2   1 
ATOM   1836 C  CE1   . TYR A 1 256  ? 130.785 98.064  124.901 1.00 39.26  ? 256  TYR A CE1   1 
ATOM   1837 C  CE2   . TYR A 1 256  ? 128.627 97.812  125.901 1.00 39.26  ? 256  TYR A CE2   1 
ATOM   1838 C  CZ    . TYR A 1 256  ? 130.000 97.798  126.003 1.00 39.26  ? 256  TYR A CZ    1 
ATOM   1839 O  OH    . TYR A 1 256  ? 130.588 97.516  127.214 1.00 39.26  ? 256  TYR A OH    1 
ATOM   1840 N  N     . THR A 1 257  ? 126.715 101.326 120.849 1.00 36.60  ? 257  THR A N     1 
ATOM   1841 C  CA    . THR A 1 257  ? 125.703 101.724 119.880 1.00 36.60  ? 257  THR A CA    1 
ATOM   1842 C  C     . THR A 1 257  ? 126.331 102.380 118.659 1.00 36.60  ? 257  THR A C     1 
ATOM   1843 O  O     . THR A 1 257  ? 125.770 102.303 117.564 1.00 36.60  ? 257  THR A O     1 
ATOM   1844 C  CB    . THR A 1 257  ? 124.675 102.654 120.529 1.00 36.60  ? 257  THR A CB    1 
ATOM   1845 O  OG1   . THR A 1 257  ? 123.602 102.895 119.610 1.00 36.60  ? 257  THR A OG1   1 
ATOM   1846 C  CG2   . THR A 1 257  ? 125.306 103.980 120.916 1.00 36.60  ? 257  THR A CG2   1 
ATOM   1847 N  N     . LEU A 1 258  ? 127.507 102.992 118.815 1.00 34.85  ? 258  LEU A N     1 
ATOM   1848 C  CA    . LEU A 1 258  ? 128.198 103.562 117.663 1.00 34.85  ? 258  LEU A CA    1 
ATOM   1849 C  C     . LEU A 1 258  ? 128.546 102.483 116.645 1.00 34.85  ? 258  LEU A C     1 
ATOM   1850 O  O     . LEU A 1 258  ? 128.223 102.605 115.458 1.00 34.85  ? 258  LEU A O     1 
ATOM   1851 C  CB    . LEU A 1 258  ? 129.458 104.298 118.119 1.00 34.85  ? 258  LEU A CB    1 
ATOM   1852 C  CG    . LEU A 1 258  ? 129.240 105.517 119.015 1.00 34.85  ? 258  LEU A CG    1 
ATOM   1853 C  CD1   . LEU A 1 258  ? 130.559 106.008 119.584 1.00 34.85  ? 258  LEU A CD1   1 
ATOM   1854 C  CD2   . LEU A 1 258  ? 128.543 106.619 118.241 1.00 34.85  ? 258  LEU A CD2   1 
ATOM   1855 N  N     . LYS A 1 259  ? 129.203 101.411 117.094 1.00 36.41  ? 259  LYS A N     1 
ATOM   1856 C  CA    . LYS A 1 259  ? 129.579 100.342 116.175 1.00 36.41  ? 259  LYS A CA    1 
ATOM   1857 C  C     . LYS A 1 259  ? 128.352 99.635  115.616 1.00 36.41  ? 259  LYS A C     1 
ATOM   1858 O  O     . LYS A 1 259  ? 128.309 99.298  114.425 1.00 36.41  ? 259  LYS A O     1 
ATOM   1859 C  CB    . LYS A 1 259  ? 130.504 99.347  116.874 1.00 36.41  ? 259  LYS A CB    1 
ATOM   1860 C  CG    . LYS A 1 259  ? 131.938 99.826  116.986 1.00 36.41  ? 259  LYS A CG    1 
ATOM   1861 C  CD    . LYS A 1 259  ? 132.647 99.755  115.643 1.00 36.41  ? 259  LYS A CD    1 
ATOM   1862 C  CE    . LYS A 1 259  ? 133.388 98.439  115.468 1.00 36.41  ? 259  LYS A CE    1 
ATOM   1863 N  NZ    . LYS A 1 259  ? 134.528 98.576  114.518 1.00 36.41  ? 259  LYS A NZ    1 
ATOM   1864 N  N     . LEU A 1 260  ? 127.342 99.399  116.460 1.00 35.28  ? 260  LEU A N     1 
ATOM   1865 C  CA    . LEU A 1 260  ? 126.123 98.762  115.963 1.00 35.28  ? 260  LEU A CA    1 
ATOM   1866 C  C     . LEU A 1 260  ? 125.451 99.609  114.887 1.00 35.28  ? 260  LEU A C     1 
ATOM   1867 O  O     . LEU A 1 260  ? 125.003 99.081  113.862 1.00 35.28  ? 260  LEU A O     1 
ATOM   1868 C  CB    . LEU A 1 260  ? 125.158 98.467  117.113 1.00 35.28  ? 260  LEU A CB    1 
ATOM   1869 C  CG    . LEU A 1 260  ? 125.367 97.178  117.921 1.00 35.28  ? 260  LEU A CG    1 
ATOM   1870 C  CD1   . LEU A 1 260  ? 125.158 95.977  117.013 1.00 35.28  ? 260  LEU A CD1   1 
ATOM   1871 C  CD2   . LEU A 1 260  ? 126.723 97.087  118.600 1.00 35.28  ? 260  LEU A CD2   1 
ATOM   1872 N  N     . GLY A 1 261  ? 125.384 100.925 115.090 1.00 36.10  ? 261  GLY A N     1 
ATOM   1873 C  CA    . GLY A 1 261  ? 124.807 101.791 114.077 1.00 36.10  ? 261  GLY A CA    1 
ATOM   1874 C  C     . GLY A 1 261  ? 125.643 101.868 112.814 1.00 36.10  ? 261  GLY A C     1 
ATOM   1875 O  O     . GLY A 1 261  ? 125.103 101.992 111.713 1.00 36.10  ? 261  GLY A O     1 
ATOM   1876 N  N     . TYR A 1 262  ? 126.970 101.817 112.953 1.00 35.05  ? 262  TYR A N     1 
ATOM   1877 C  CA    . TYR A 1 262  ? 127.826 101.776 111.772 1.00 35.05  ? 262  TYR A CA    1 
ATOM   1878 C  C     . TYR A 1 262  ? 127.535 100.532 110.945 1.00 35.05  ? 262  TYR A C     1 
ATOM   1879 O  O     . TYR A 1 262  ? 127.419 100.597 109.714 1.00 35.05  ? 262  TYR A O     1 
ATOM   1880 C  CB    . TYR A 1 262  ? 129.301 101.808 112.178 1.00 35.05  ? 262  TYR A CB    1 
ATOM   1881 C  CG    . TYR A 1 262  ? 129.743 103.079 112.863 1.00 35.05  ? 262  TYR A CG    1 
ATOM   1882 C  CD1   . TYR A 1 262  ? 128.993 104.240 112.772 1.00 35.05  ? 262  TYR A CD1   1 
ATOM   1883 C  CD2   . TYR A 1 262  ? 130.920 103.117 113.598 1.00 35.05  ? 262  TYR A CD2   1 
ATOM   1884 C  CE1   . TYR A 1 262  ? 129.397 105.400 113.400 1.00 35.05  ? 262  TYR A CE1   1 
ATOM   1885 C  CE2   . TYR A 1 262  ? 131.333 104.274 114.226 1.00 35.05  ? 262  TYR A CE2   1 
ATOM   1886 C  CZ    . TYR A 1 262  ? 130.568 105.412 114.124 1.00 35.05  ? 262  TYR A CZ    1 
ATOM   1887 O  OH    . TYR A 1 262  ? 130.975 106.567 114.748 1.00 35.05  ? 262  TYR A OH    1 
ATOM   1888 N  N     . LYS A 1 263  ? 127.408 99.385  111.615 1.00 35.58  ? 263  LYS A N     1 
ATOM   1889 C  CA    . LYS A 1 263  ? 127.082 98.149  110.910 1.00 35.58  ? 263  LYS A CA    1 
ATOM   1890 C  C     . LYS A 1 263  ? 125.704 98.230  110.265 1.00 35.58  ? 263  LYS A C     1 
ATOM   1891 O  O     . LYS A 1 263  ? 125.507 97.755  109.140 1.00 35.58  ? 263  LYS A O     1 
ATOM   1892 C  CB    . LYS A 1 263  ? 127.163 96.961  111.867 1.00 35.58  ? 263  LYS A CB    1 
ATOM   1893 C  CG    . LYS A 1 263  ? 128.529 96.779  112.503 1.00 35.58  ? 263  LYS A CG    1 
ATOM   1894 C  CD    . LYS A 1 263  ? 128.837 95.316  112.757 1.00 35.58  ? 263  LYS A CD    1 
ATOM   1895 C  CE    . LYS A 1 263  ? 130.306 95.122  113.090 1.00 35.58  ? 263  LYS A CE    1 
ATOM   1896 N  NZ    . LYS A 1 263  ? 131.180 95.983  112.245 1.00 35.58  ? 263  LYS A NZ    1 
ATOM   1897 N  N     . ALA A 1 264  ? 124.735 98.828  110.965 1.00 35.33  ? 264  ALA A N     1 
ATOM   1898 C  CA    . ALA A 1 264  ? 123.396 98.973  110.400 1.00 35.33  ? 264  ALA A CA    1 
ATOM   1899 C  C     . ALA A 1 264  ? 123.410 99.856  109.158 1.00 35.33  ? 264  ALA A C     1 
ATOM   1900 O  O     . ALA A 1 264  ? 122.747 99.548  108.160 1.00 35.33  ? 264  ALA A O     1 
ATOM   1901 C  CB    . ALA A 1 264  ? 122.442 99.538  111.450 1.00 35.33  ? 264  ALA A CB    1 
ATOM   1902 N  N     . GLY A 1 265  ? 124.154 100.962 109.204 1.00 36.78  ? 265  GLY A N     1 
ATOM   1903 C  CA    . GLY A 1 265  ? 124.253 101.827 108.040 1.00 36.78  ? 265  GLY A CA    1 
ATOM   1904 C  C     . GLY A 1 265  ? 124.944 101.154 106.871 1.00 36.78  ? 265  GLY A C     1 
ATOM   1905 O  O     . GLY A 1 265  ? 124.532 101.313 105.719 1.00 36.78  ? 265  GLY A O     1 
ATOM   1906 N  N     . MET A 1 266  ? 126.007 100.395 107.148 1.00 39.86  ? 266  MET A N     1 
ATOM   1907 C  CA    . MET A 1 266  ? 126.672 99.652  106.083 1.00 39.86  ? 266  MET A CA    1 
ATOM   1908 C  C     . MET A 1 266  ? 125.734 98.622  105.468 1.00 39.86  ? 266  MET A C     1 
ATOM   1909 O  O     . MET A 1 266  ? 125.740 98.415  104.249 1.00 39.86  ? 266  MET A O     1 
ATOM   1910 C  CB    . MET A 1 266  ? 127.934 98.977  106.616 1.00 39.86  ? 266  MET A CB    1 
ATOM   1911 C  CG    . MET A 1 266  ? 129.083 99.933  106.876 1.00 39.86  ? 266  MET A CG    1 
ATOM   1912 S  SD    . MET A 1 266  ? 130.689 99.115  106.876 1.00 39.86  ? 266  MET A SD    1 
ATOM   1913 C  CE    . MET A 1 266  ? 130.292 97.586  107.720 1.00 39.86  ? 266  MET A CE    1 
ATOM   1914 N  N     . ALA A 1 267  ? 124.923 97.962  106.298 1.00 39.71  ? 267  ALA A N     1 
ATOM   1915 C  CA    . ALA A 1 267  ? 123.960 96.996  105.780 1.00 39.71  ? 267  ALA A CA    1 
ATOM   1916 C  C     . ALA A 1 267  ? 122.924 97.668  104.889 1.00 39.71  ? 267  ALA A C     1 
ATOM   1917 O  O     . ALA A 1 267  ? 122.544 97.122  103.846 1.00 39.71  ? 267  ALA A O     1 
ATOM   1918 C  CB    . ALA A 1 267  ? 123.280 96.263  106.935 1.00 39.71  ? 267  ALA A CB    1 
ATOM   1919 N  N     . LYS A 1 268  ? 122.449 98.851  105.286 1.00 39.77  ? 268  LYS A N     1 
ATOM   1920 C  CA    . LYS A 1 268  ? 121.438 99.548  104.496 1.00 39.77  ? 268  LYS A CA    1 
ATOM   1921 C  C     . LYS A 1 268  ? 121.984 99.944  103.131 1.00 39.77  ? 268  LYS A C     1 
ATOM   1922 O  O     . LYS A 1 268  ? 121.305 99.792  102.109 1.00 39.77  ? 268  LYS A O     1 
ATOM   1923 C  CB    . LYS A 1 268  ? 120.935 100.776 105.255 1.00 39.77  ? 268  LYS A CB    1 
ATOM   1924 C  CG    . LYS A 1 268  ? 120.221 101.793 104.381 1.00 39.77  ? 268  LYS A CG    1 
ATOM   1925 C  CD    . LYS A 1 268  ? 118.787 101.375 104.109 1.00 39.77  ? 268  LYS A CD    1 
ATOM   1926 C  CE    . LYS A 1 268  ? 117.861 102.579 104.047 1.00 39.77  ? 268  LYS A CE    1 
ATOM   1927 N  NZ    . LYS A 1 268  ? 116.640 102.303 103.241 1.00 39.77  ? 268  LYS A NZ    1 
ATOM   1928 N  N     . GLY A 1 269  ? 123.214 100.457 103.095 1.00 41.02  ? 269  GLY A N     1 
ATOM   1929 C  CA    . GLY A 1 269  ? 123.811 100.823 101.822 1.00 41.02  ? 269  GLY A CA    1 
ATOM   1930 C  C     . GLY A 1 269  ? 124.022 99.629  100.912 1.00 41.02  ? 269  GLY A C     1 
ATOM   1931 O  O     . GLY A 1 269  ? 123.796 99.710  99.702  1.00 41.02  ? 269  GLY A O     1 
ATOM   1932 N  N     . LEU A 1 270  ? 124.462 98.504  101.480 1.00 42.37  ? 270  LEU A N     1 
ATOM   1933 C  CA    . LEU A 1 270  ? 124.717 97.318  100.671 1.00 42.37  ? 270  LEU A CA    1 
ATOM   1934 C  C     . LEU A 1 270  ? 123.432 96.767  100.064 1.00 42.37  ? 270  LEU A C     1 
ATOM   1935 O  O     . LEU A 1 270  ? 123.418 96.354  98.899  1.00 42.37  ? 270  LEU A O     1 
ATOM   1936 C  CB    . LEU A 1 270  ? 125.415 96.251  101.513 1.00 42.37  ? 270  LEU A CB    1 
ATOM   1937 C  CG    . LEU A 1 270  ? 126.928 96.413  101.664 1.00 42.37  ? 270  LEU A CG    1 
ATOM   1938 C  CD1   . LEU A 1 270  ? 127.402 95.857  102.997 1.00 42.37  ? 270  LEU A CD1   1 
ATOM   1939 C  CD2   . LEU A 1 270  ? 127.647 95.735  100.511 1.00 42.37  ? 270  LEU A CD2   1 
ATOM   1940 N  N     . GLY A 1 271  ? 122.346 96.740  100.839 1.00 41.99  ? 271  GLY A N     1 
ATOM   1941 C  CA    . GLY A 1 271  ? 121.105 96.174  100.330 1.00 41.99  ? 271  GLY A CA    1 
ATOM   1942 C  C     . GLY A 1 271  ? 120.529 96.965  99.171  1.00 41.99  ? 271  GLY A C     1 
ATOM   1943 O  O     . GLY A 1 271  ? 120.146 96.399  98.143  1.00 41.99  ? 271  GLY A O     1 
ATOM   1944 N  N     . LEU A 1 272  ? 120.466 98.291  99.321  1.00 39.88  ? 272  LEU A N     1 
ATOM   1945 C  CA    . LEU A 1 272  ? 119.941 99.135  98.252  1.00 39.88  ? 272  LEU A CA    1 
ATOM   1946 C  C     . LEU A 1 272  ? 120.812 99.048  97.007  1.00 39.88  ? 272  LEU A C     1 
ATOM   1947 O  O     . LEU A 1 272  ? 120.301 98.967  95.882  1.00 39.88  ? 272  LEU A O     1 
ATOM   1948 C  CB    . LEU A 1 272  ? 119.836 100.581 98.731  1.00 39.88  ? 272  LEU A CB    1 
ATOM   1949 C  CG    . LEU A 1 272  ? 118.478 101.009 99.283  1.00 39.88  ? 272  LEU A CG    1 
ATOM   1950 C  CD1   . LEU A 1 272  ? 118.563 102.393 99.895  1.00 39.88  ? 272  LEU A CD1   1 
ATOM   1951 C  CD2   . LEU A 1 272  ? 117.434 100.974 98.186  1.00 39.88  ? 272  LEU A CD2   1 
ATOM   1952 N  N     . GLY A 1 273  ? 122.133 99.064  97.192  1.00 46.63  ? 273  GLY A N     1 
ATOM   1953 C  CA    . GLY A 1 273  ? 123.027 98.935  96.056  1.00 46.63  ? 273  GLY A CA    1 
ATOM   1954 C  C     . GLY A 1 273  ? 122.863 97.612  95.337  1.00 46.63  ? 273  GLY A C     1 
ATOM   1955 O  O     . GLY A 1 273  ? 122.819 97.568  94.108  1.00 46.63  ? 273  GLY A O     1 
ATOM   1956 N  N     . CYS A 1 274  ? 122.761 96.517  96.092  1.00 49.78  ? 274  CYS A N     1 
ATOM   1957 C  CA    . CYS A 1 274  ? 122.570 95.211  95.471  1.00 49.78  ? 274  CYS A CA    1 
ATOM   1958 C  C     . CYS A 1 274  ? 121.251 95.151  94.714  1.00 49.78  ? 274  CYS A C     1 
ATOM   1959 O  O     . CYS A 1 274  ? 121.188 94.608  93.604  1.00 49.78  ? 274  CYS A O     1 
ATOM   1960 C  CB    . CYS A 1 274  ? 122.633 94.111  96.530  1.00 49.78  ? 274  CYS A CB    1 
ATOM   1961 S  SG    . CYS A 1 274  ? 122.477 92.436  95.870  1.00 49.78  ? 274  CYS A SG    1 
ATOM   1962 N  N     . THR A 1 275  ? 120.186 95.708  95.296  1.00 48.63  ? 275  THR A N     1 
ATOM   1963 C  CA    . THR A 1 275  ? 118.893 95.720  94.619  1.00 48.63  ? 275  THR A CA    1 
ATOM   1964 C  C     . THR A 1 275  ? 118.972 96.491  93.306  1.00 48.63  ? 275  THR A C     1 
ATOM   1965 O  O     . THR A 1 275  ? 118.523 96.007  92.258  1.00 48.63  ? 275  THR A O     1 
ATOM   1966 C  CB    . THR A 1 275  ? 117.828 96.324  95.536  1.00 48.63  ? 275  THR A CB    1 
ATOM   1967 O  OG1   . THR A 1 275  ? 117.468 95.373  96.544  1.00 48.63  ? 275  THR A OG1   1 
ATOM   1968 C  CG2   . THR A 1 275  ? 116.589 96.703  94.743  1.00 48.63  ? 275  THR A CG2   1 
ATOM   1969 N  N     . TYR A 1 276  ? 119.564 97.688  93.340  1.00 46.80  ? 276  TYR A N     1 
ATOM   1970 C  CA    . TYR A 1 276  ? 119.641 98.499  92.129  1.00 46.80  ? 276  TYR A CA    1 
ATOM   1971 C  C     . TYR A 1 276  ? 120.551 97.860  91.088  1.00 46.80  ? 276  TYR A C     1 
ATOM   1972 O  O     . TYR A 1 276  ? 120.274 97.934  89.887  1.00 46.80  ? 276  TYR A O     1 
ATOM   1973 C  CB    . TYR A 1 276  ? 120.109 99.912  92.470  1.00 46.80  ? 276  TYR A CB    1 
ATOM   1974 C  CG    . TYR A 1 276  ? 118.970 100.871 92.727  1.00 46.80  ? 276  TYR A CG    1 
ATOM   1975 C  CD1   . TYR A 1 276  ? 118.372 100.947 93.976  1.00 46.80  ? 276  TYR A CD1   1 
ATOM   1976 C  CD2   . TYR A 1 276  ? 118.489 101.695 91.720  1.00 46.80  ? 276  TYR A CD2   1 
ATOM   1977 C  CE1   . TYR A 1 276  ? 117.330 101.818 94.217  1.00 46.80  ? 276  TYR A CE1   1 
ATOM   1978 C  CE2   . TYR A 1 276  ? 117.447 102.570 91.952  1.00 46.80  ? 276  TYR A CE2   1 
ATOM   1979 C  CZ    . TYR A 1 276  ? 116.871 102.627 93.203  1.00 46.80  ? 276  TYR A CZ    1 
ATOM   1980 O  OH    . TYR A 1 276  ? 115.833 103.497 93.441  1.00 46.80  ? 276  TYR A OH    1 
ATOM   1981 N  N     . GLY A 1 277  ? 121.634 97.216  91.525  1.00 53.89  ? 277  GLY A N     1 
ATOM   1982 C  CA    . GLY A 1 277  ? 122.507 96.536  90.583  1.00 53.89  ? 277  GLY A CA    1 
ATOM   1983 C  C     . GLY A 1 277  ? 121.835 95.354  89.912  1.00 53.89  ? 277  GLY A C     1 
ATOM   1984 O  O     . GLY A 1 277  ? 121.964 95.164  88.698  1.00 53.89  ? 277  GLY A O     1 
ATOM   1985 N  N     . ILE A 1 278  ? 121.114 94.541  90.688  1.00 55.42  ? 278  ILE A N     1 
ATOM   1986 C  CA    . ILE A 1 278  ? 120.369 93.430  90.104  1.00 55.42  ? 278  ILE A CA    1 
ATOM   1987 C  C     . ILE A 1 278  ? 119.333 93.954  89.122  1.00 55.42  ? 278  ILE A C     1 
ATOM   1988 O  O     . ILE A 1 278  ? 119.149 93.398  88.030  1.00 55.42  ? 278  ILE A O     1 
ATOM   1989 C  CB    . ILE A 1 278  ? 119.724 92.576  91.211  1.00 55.42  ? 278  ILE A CB    1 
ATOM   1990 C  CG1   . ILE A 1 278  ? 120.798 91.805  91.977  1.00 55.42  ? 278  ILE A CG1   1 
ATOM   1991 C  CG2   . ILE A 1 278  ? 118.705 91.619  90.623  1.00 55.42  ? 278  ILE A CG2   1 
ATOM   1992 C  CD1   . ILE A 1 278  ? 121.565 90.825  91.120  1.00 55.42  ? 278  ILE A CD1   1 
ATOM   1993 N  N     . ALA A 1 279  ? 118.654 95.045  89.484  1.00 60.29  ? 279  ALA A N     1 
ATOM   1994 C  CA    . ALA A 1 279  ? 117.695 95.652  88.569  1.00 60.29  ? 279  ALA A CA    1 
ATOM   1995 C  C     . ALA A 1 279  ? 118.372 96.107  87.282  1.00 60.29  ? 279  ALA A C     1 
ATOM   1996 O  O     . ALA A 1 279  ? 117.822 95.932  86.191  1.00 60.29  ? 279  ALA A O     1 
ATOM   1997 C  CB    . ALA A 1 279  ? 116.989 96.824  89.251  1.00 60.29  ? 279  ALA A CB    1 
ATOM   1998 N  N     . CYS A 1 280  ? 119.566 96.694  87.388  1.00 61.46  ? 280  CYS A N     1 
ATOM   1999 C  CA    . CYS A 1 280  ? 120.258 97.186  86.199  1.00 61.46  ? 280  CYS A CA    1 
ATOM   2000 C  C     . CYS A 1 280  ? 120.688 96.045  85.283  1.00 61.46  ? 280  CYS A C     1 
ATOM   2001 O  O     . CYS A 1 280  ? 120.547 96.142  84.058  1.00 61.46  ? 280  CYS A O     1 
ATOM   2002 C  CB    . CYS A 1 280  ? 121.463 98.032  86.606  1.00 61.46  ? 280  CYS A CB    1 
ATOM   2003 S  SG    . CYS A 1 280  ? 121.034 99.667  87.240  1.00 61.46  ? 280  CYS A SG    1 
ATOM   2004 N  N     . MET A 1 281  ? 121.230 94.964  85.850  1.00 62.93  ? 281  MET A N     1 
ATOM   2005 C  CA    . MET A 1 281  ? 121.588 93.820  85.012  1.00 62.93  ? 281  MET A CA    1 
ATOM   2006 C  C     . MET A 1 281  ? 120.353 93.205  84.368  1.00 62.93  ? 281  MET A C     1 
ATOM   2007 O  O     . MET A 1 281  ? 120.387 92.806  83.195  1.00 62.93  ? 281  MET A O     1 
ATOM   2008 C  CB    . MET A 1 281  ? 122.359 92.768  85.811  1.00 62.93  ? 281  MET A CB    1 
ATOM   2009 C  CG    . MET A 1 281  ? 123.354 93.322  86.806  1.00 62.93  ? 281  MET A CG    1 
ATOM   2010 S  SD    . MET A 1 281  ? 124.690 92.168  87.166  1.00 62.93  ? 281  MET A SD    1 
ATOM   2011 C  CE    . MET A 1 281  ? 123.778 90.807  87.888  1.00 62.93  ? 281  MET A CE    1 
ATOM   2012 N  N     . SER A 1 282  ? 119.250 93.123  85.116  1.00 62.52  ? 282  SER A N     1 
ATOM   2013 C  CA    . SER A 1 282  ? 118.008 92.628  84.535  1.00 62.52  ? 282  SER A CA    1 
ATOM   2014 C  C     . SER A 1 282  ? 117.550 93.515  83.387  1.00 62.52  ? 282  SER A C     1 
ATOM   2015 O  O     . SER A 1 282  ? 117.090 93.017  82.355  1.00 62.52  ? 282  SER A O     1 
ATOM   2016 C  CB    . SER A 1 282  ? 116.924 92.540  85.606  1.00 62.52  ? 282  SER A CB    1 
ATOM   2017 O  OG    . SER A 1 282  ? 115.654 92.312  85.021  1.00 62.52  ? 282  SER A OG    1 
ATOM   2018 N  N     . TRP A 1 283  ? 117.669 94.835  83.549  1.00 62.21  ? 283  TRP A N     1 
ATOM   2019 C  CA    . TRP A 1 283  ? 117.271 95.757  82.491  1.00 62.21  ? 283  TRP A CA    1 
ATOM   2020 C  C     . TRP A 1 283  ? 118.149 95.597  81.256  1.00 62.21  ? 283  TRP A C     1 
ATOM   2021 O  O     . TRP A 1 283  ? 117.655 95.638  80.125  1.00 62.21  ? 283  TRP A O     1 
ATOM   2022 C  CB    . TRP A 1 283  ? 117.315 97.196  83.003  1.00 62.21  ? 283  TRP A CB    1 
ATOM   2023 C  CG    . TRP A 1 283  ? 116.370 97.450  84.133  1.00 62.21  ? 283  TRP A CG    1 
ATOM   2024 C  CD1   . TRP A 1 283  ? 115.280 96.705  84.472  1.00 62.21  ? 283  TRP A CD1   1 
ATOM   2025 C  CD2   . TRP A 1 283  ? 116.435 98.520  85.084  1.00 62.21  ? 283  TRP A CD2   1 
ATOM   2026 N  NE1   . TRP A 1 283  ? 114.660 97.245  85.571  1.00 62.21  ? 283  TRP A NE1   1 
ATOM   2027 C  CE2   . TRP A 1 283  ? 115.350 98.360  85.966  1.00 62.21  ? 283  TRP A CE2   1 
ATOM   2028 C  CE3   . TRP A 1 283  ? 117.304 99.597  85.273  1.00 62.21  ? 283  TRP A CE3   1 
ATOM   2029 C  CZ2   . TRP A 1 283  ? 115.110 99.237  87.019  1.00 62.21  ? 283  TRP A CZ2   1 
ATOM   2030 C  CZ3   . TRP A 1 283  ? 117.064 100.467 86.320  1.00 62.21  ? 283  TRP A CZ3   1 
ATOM   2031 C  CH2   . TRP A 1 283  ? 115.976 100.282 87.179  1.00 62.21  ? 283  TRP A CH2   1 
ATOM   2032 N  N     . ALA A 1 284  ? 119.456 95.415  81.448  1.00 67.98  ? 284  ALA A N     1 
ATOM   2033 C  CA    . ALA A 1 284  ? 120.341 95.216  80.304  1.00 67.98  ? 284  ALA A CA    1 
ATOM   2034 C  C     . ALA A 1 284  ? 119.989 93.935  79.556  1.00 67.98  ? 284  ALA A C     1 
ATOM   2035 O  O     . ALA A 1 284  ? 119.886 93.924  78.320  1.00 67.98  ? 284  ALA A O     1 
ATOM   2036 C  CB    . ALA A 1 284  ? 121.798 95.188  80.767  1.00 67.98  ? 284  ALA A CB    1 
ATOM   2037 N  N     . LEU A 1 285  ? 119.791 92.841  80.296  1.00 71.03  ? 285  LEU A N     1 
ATOM   2038 C  CA    . LEU A 1 285  ? 119.453 91.573  79.658  1.00 71.03  ? 285  LEU A CA    1 
ATOM   2039 C  C     . LEU A 1 285  ? 118.106 91.655  78.950  1.00 71.03  ? 285  LEU A C     1 
ATOM   2040 O  O     . LEU A 1 285  ? 117.944 91.135  77.837  1.00 71.03  ? 285  LEU A O     1 
ATOM   2041 C  CB    . LEU A 1 285  ? 119.449 90.453  80.697  1.00 71.03  ? 285  LEU A CB    1 
ATOM   2042 C  CG    . LEU A 1 285  ? 119.305 89.028  80.165  1.00 71.03  ? 285  LEU A CG    1 
ATOM   2043 C  CD1   . LEU A 1 285  ? 120.279 88.793  79.021  1.00 71.03  ? 285  LEU A CD1   1 
ATOM   2044 C  CD2   . LEU A 1 285  ? 119.525 88.019  81.279  1.00 71.03  ? 285  LEU A CD2   1 
ATOM   2045 N  N     . VAL A 1 286  ? 117.126 92.305  79.583  1.00 71.42  ? 286  VAL A N     1 
ATOM   2046 C  CA    . VAL A 1 286  ? 115.800 92.411  78.990  1.00 71.42  ? 286  VAL A CA    1 
ATOM   2047 C  C     . VAL A 1 286  ? 115.850 93.295  77.750  1.00 71.42  ? 286  VAL A C     1 
ATOM   2048 O  O     . VAL A 1 286  ? 115.148 93.031  76.770  1.00 71.42  ? 286  VAL A O     1 
ATOM   2049 C  CB    . VAL A 1 286  ? 114.782 92.910  80.042  1.00 71.42  ? 286  VAL A CB    1 
ATOM   2050 C  CG1   . VAL A 1 286  ? 114.899 94.395  80.298  1.00 71.42  ? 286  VAL A CG1   1 
ATOM   2051 C  CG2   . VAL A 1 286  ? 113.374 92.556  79.657  1.00 71.42  ? 286  VAL A CG2   1 
ATOM   2052 N  N     . PHE A 1 287  ? 116.709 94.322  77.745  1.00 74.54  ? 287  PHE A N     1 
ATOM   2053 C  CA    . PHE A 1 287  ? 116.872 95.144  76.549  1.00 74.54  ? 287  PHE A CA    1 
ATOM   2054 C  C     . PHE A 1 287  ? 117.478 94.343  75.407  1.00 74.54  ? 287  PHE A C     1 
ATOM   2055 O  O     . PHE A 1 287  ? 117.019 94.437  74.263  1.00 74.54  ? 287  PHE A O     1 
ATOM   2056 C  CB    . PHE A 1 287  ? 117.755 96.357  76.846  1.00 74.54  ? 287  PHE A CB    1 
ATOM   2057 C  CG    . PHE A 1 287  ? 117.017 97.521  77.426  1.00 74.54  ? 287  PHE A CG    1 
ATOM   2058 C  CD1   . PHE A 1 287  ? 117.607 98.770  77.478  1.00 74.54  ? 287  PHE A CD1   1 
ATOM   2059 C  CD2   . PHE A 1 287  ? 115.750 97.367  77.955  1.00 74.54  ? 287  PHE A CD2   1 
ATOM   2060 C  CE1   . PHE A 1 287  ? 116.932 99.848  78.010  1.00 74.54  ? 287  PHE A CE1   1 
ATOM   2061 C  CE2   . PHE A 1 287  ? 115.081 98.440  78.501  1.00 74.54  ? 287  PHE A CE2   1 
ATOM   2062 C  CZ    . PHE A 1 287  ? 115.672 99.681  78.529  1.00 74.54  ? 287  PHE A CZ    1 
ATOM   2063 N  N     . TRP A 1 288  ? 118.521 93.561  75.696  1.00 81.15  ? 288  TRP A N     1 
ATOM   2064 C  CA    . TRP A 1 288  ? 119.151 92.766  74.645  1.00 81.15  ? 288  TRP A CA    1 
ATOM   2065 C  C     . TRP A 1 288  ? 118.177 91.746  74.066  1.00 81.15  ? 288  TRP A C     1 
ATOM   2066 O  O     . TRP A 1 288  ? 118.085 91.581  72.839  1.00 81.15  ? 288  TRP A O     1 
ATOM   2067 C  CB    . TRP A 1 288  ? 120.396 92.072  75.193  1.00 81.15  ? 288  TRP A CB    1 
ATOM   2068 C  CG    . TRP A 1 288  ? 121.094 91.209  74.193  1.00 81.15  ? 288  TRP A CG    1 
ATOM   2069 C  CD1   . TRP A 1 288  ? 121.215 89.852  74.227  1.00 81.15  ? 288  TRP A CD1   1 
ATOM   2070 C  CD2   . TRP A 1 288  ? 121.774 91.643  73.011  1.00 81.15  ? 288  TRP A CD2   1 
ATOM   2071 N  NE1   . TRP A 1 288  ? 121.926 89.413  73.138  1.00 81.15  ? 288  TRP A NE1   1 
ATOM   2072 C  CE2   . TRP A 1 288  ? 122.281 90.494  72.375  1.00 81.15  ? 288  TRP A CE2   1 
ATOM   2073 C  CE3   . TRP A 1 288  ? 122.003 92.892  72.427  1.00 81.15  ? 288  TRP A CE3   1 
ATOM   2074 C  CZ2   . TRP A 1 288  ? 123.002 90.555  71.186  1.00 81.15  ? 288  TRP A CZ2   1 
ATOM   2075 C  CZ3   . TRP A 1 288  ? 122.719 92.951  71.246  1.00 81.15  ? 288  TRP A CZ3   1 
ATOM   2076 C  CH2   . TRP A 1 288  ? 123.210 91.791  70.639  1.00 81.15  ? 288  TRP A CH2   1 
ATOM   2077 N  N     . TYR A 1 289  ? 117.436 91.054  74.935  1.00 84.04  ? 289  TYR A N     1 
ATOM   2078 C  CA    . TYR A 1 289  ? 116.470 90.076  74.446  1.00 84.04  ? 289  TYR A CA    1 
ATOM   2079 C  C     . TYR A 1 289  ? 115.327 90.747  73.694  1.00 84.04  ? 289  TYR A C     1 
ATOM   2080 O  O     . TYR A 1 289  ? 114.842 90.208  72.695  1.00 84.04  ? 289  TYR A O     1 
ATOM   2081 C  CB    . TYR A 1 289  ? 115.947 89.219  75.597  1.00 84.04  ? 289  TYR A CB    1 
ATOM   2082 C  CG    . TYR A 1 289  ? 116.935 88.171  76.056  1.00 84.04  ? 289  TYR A CG    1 
ATOM   2083 C  CD1   . TYR A 1 289  ? 118.003 87.797  75.249  1.00 84.04  ? 289  TYR A CD1   1 
ATOM   2084 C  CD2   . TYR A 1 289  ? 116.797 87.549  77.288  1.00 84.04  ? 289  TYR A CD2   1 
ATOM   2085 C  CE1   . TYR A 1 289  ? 118.908 86.837  75.660  1.00 84.04  ? 289  TYR A CE1   1 
ATOM   2086 C  CE2   . TYR A 1 289  ? 117.697 86.587  77.709  1.00 84.04  ? 289  TYR A CE2   1 
ATOM   2087 C  CZ    . TYR A 1 289  ? 118.750 86.236  76.891  1.00 84.04  ? 289  TYR A CZ    1 
ATOM   2088 O  OH    . TYR A 1 289  ? 119.648 85.280  77.307  1.00 84.04  ? 289  TYR A OH    1 
ATOM   2089 N  N     . ALA A 1 290  ? 114.892 91.928  74.138  1.00 83.96  ? 290  ALA A N     1 
ATOM   2090 C  CA    . ALA A 1 290  ? 113.873 92.653  73.390  1.00 83.96  ? 290  ALA A CA    1 
ATOM   2091 C  C     . ALA A 1 290  ? 114.378 93.024  72.004  1.00 83.96  ? 290  ALA A C     1 
ATOM   2092 O  O     . ALA A 1 290  ? 113.639 92.924  71.019  1.00 83.96  ? 290  ALA A O     1 
ATOM   2093 C  CB    . ALA A 1 290  ? 113.442 93.900  74.160  1.00 83.96  ? 290  ALA A CB    1 
ATOM   2094 N  N     . GLY A 1 291  ? 115.637 93.452  71.909  1.00 88.55  ? 291  GLY A N     1 
ATOM   2095 C  CA    . GLY A 1 291  ? 116.194 93.784  70.607  1.00 88.55  ? 291  GLY A CA    1 
ATOM   2096 C  C     . GLY A 1 291  ? 116.237 92.589  69.676  1.00 88.55  ? 291  GLY A C     1 
ATOM   2097 O  O     . GLY A 1 291  ? 115.833 92.675  68.511  1.00 88.55  ? 291  GLY A O     1 
ATOM   2098 N  N     . VAL A 1 292  ? 116.714 91.448  70.180  1.00 88.53  ? 292  VAL A N     1 
ATOM   2099 C  CA    . VAL A 1 292  ? 116.767 90.274  69.311  1.00 88.53  ? 292  VAL A CA    1 
ATOM   2100 C  C     . VAL A 1 292  ? 115.358 89.794  68.971  1.00 88.53  ? 292  VAL A C     1 
ATOM   2101 O  O     . VAL A 1 292  ? 115.136 89.220  67.897  1.00 88.53  ? 292  VAL A O     1 
ATOM   2102 C  CB    . VAL A 1 292  ? 117.622 89.150  69.929  1.00 88.53  ? 292  VAL A CB    1 
ATOM   2103 C  CG1   . VAL A 1 292  ? 119.058 89.621  70.128  1.00 88.53  ? 292  VAL A CG1   1 
ATOM   2104 C  CG2   . VAL A 1 292  ? 117.025 88.643  71.223  1.00 88.53  ? 292  VAL A CG2   1 
ATOM   2105 N  N     . PHE A 1 293  ? 114.384 90.028  69.856  1.00 92.03  ? 293  PHE A N     1 
ATOM   2106 C  CA    . PHE A 1 293  ? 113.006 89.653  69.551  1.00 92.03  ? 293  PHE A CA    1 
ATOM   2107 C  C     . PHE A 1 293  ? 112.426 90.523  68.442  1.00 92.03  ? 293  PHE A C     1 
ATOM   2108 O  O     . PHE A 1 293  ? 111.753 90.014  67.538  1.00 92.03  ? 293  PHE A O     1 
ATOM   2109 C  CB    . PHE A 1 293  ? 112.140 89.745  70.809  1.00 92.03  ? 293  PHE A CB    1 
ATOM   2110 C  CG    . PHE A 1 293  ? 112.484 88.731  71.864  1.00 92.03  ? 293  PHE A CG    1 
ATOM   2111 C  CD1   . PHE A 1 293  ? 113.265 87.627  71.562  1.00 92.03  ? 293  PHE A CD1   1 
ATOM   2112 C  CD2   . PHE A 1 293  ? 112.032 88.888  73.164  1.00 92.03  ? 293  PHE A CD2   1 
ATOM   2113 C  CE1   . PHE A 1 293  ? 113.582 86.698  72.534  1.00 92.03  ? 293  PHE A CE1   1 
ATOM   2114 C  CE2   . PHE A 1 293  ? 112.348 87.963  74.140  1.00 92.03  ? 293  PHE A CE2   1 
ATOM   2115 C  CZ    . PHE A 1 293  ? 113.123 86.867  73.824  1.00 92.03  ? 293  PHE A CZ    1 
ATOM   2116 N  N     . ILE A 1 294  ? 112.665 91.837  68.496  1.00 90.93  ? 294  ILE A N     1 
ATOM   2117 C  CA    . ILE A 1 294  ? 112.229 92.707  67.405  1.00 90.93  ? 294  ILE A CA    1 
ATOM   2118 C  C     . ILE A 1 294  ? 112.923 92.316  66.109  1.00 90.93  ? 294  ILE A C     1 
ATOM   2119 O  O     . ILE A 1 294  ? 112.340 92.410  65.022  1.00 90.93  ? 294  ILE A O     1 
ATOM   2120 C  CB    . ILE A 1 294  ? 112.461 94.192  67.744  1.00 90.93  ? 294  ILE A CB    1 
ATOM   2121 C  CG1   . ILE A 1 294  ? 111.950 94.521  69.145  1.00 90.93  ? 294  ILE A CG1   1 
ATOM   2122 C  CG2   . ILE A 1 294  ? 111.789 95.083  66.711  1.00 90.93  ? 294  ILE A CG2   1 
ATOM   2123 C  CD1   . ILE A 1 294  ? 111.942 96.002  69.464  1.00 90.93  ? 294  ILE A CD1   1 
ATOM   2124 N  N     . ARG A 1 295  ? 114.180 91.875  66.200  1.00 96.18  ? 295  ARG A N     1 
ATOM   2125 C  CA    . ARG A 1 295  ? 114.847 91.348  65.013  1.00 96.18  ? 295  ARG A CA    1 
ATOM   2126 C  C     . ARG A 1 295  ? 114.127 90.116  64.482  1.00 96.18  ? 295  ARG A C     1 
ATOM   2127 O  O     . ARG A 1 295  ? 113.974 89.952  63.266  1.00 96.18  ? 295  ARG A O     1 
ATOM   2128 C  CB    . ARG A 1 295  ? 116.305 91.023  65.324  1.00 96.18  ? 295  ARG A CB    1 
ATOM   2129 C  CG    . ARG A 1 295  ? 117.205 91.043  64.102  1.00 96.18  ? 295  ARG A CG    1 
ATOM   2130 C  CD    . ARG A 1 295  ? 118.661 91.151  64.510  1.00 96.18  ? 295  ARG A CD    1 
ATOM   2131 N  NE    . ARG A 1 295  ? 118.818 92.015  65.676  1.00 96.18  ? 295  ARG A NE    1 
ATOM   2132 C  CZ    . ARG A 1 295  ? 118.654 93.334  65.668  1.00 96.18  ? 295  ARG A CZ    1 
ATOM   2133 N  NH1   . ARG A 1 295  ? 118.332 93.966  64.546  1.00 96.18  ? 295  ARG A NH1   1 
ATOM   2134 N  NH2   . ARG A 1 295  ? 118.818 94.022  66.788  1.00 96.18  ? 295  ARG A NH2   1 
ATOM   2135 N  N     . ASN A 1 296  ? 113.682 89.235  65.380  1.00 96.84  ? 296  ASN A N     1 
ATOM   2136 C  CA    . ASN A 1 296  ? 112.881 88.091  64.957  1.00 96.84  ? 296  ASN A CA    1 
ATOM   2137 C  C     . ASN A 1 296  ? 111.559 88.542  64.349  1.00 96.84  ? 296  ASN A C     1 
ATOM   2138 O  O     . ASN A 1 296  ? 111.088 87.960  63.365  1.00 96.84  ? 296  ASN A O     1 
ATOM   2139 C  CB    . ASN A 1 296  ? 112.636 87.153  66.138  1.00 96.84  ? 296  ASN A CB    1 
ATOM   2140 C  CG    . ASN A 1 296  ? 113.922 86.627  66.741  1.00 96.84  ? 296  ASN A CG    1 
ATOM   2141 O  OD1   . ASN A 1 296  ? 114.051 86.520  67.960  1.00 96.84  ? 296  ASN A OD1   1 
ATOM   2142 N  ND2   . ASN A 1 296  ? 114.883 86.295  65.887  1.00 96.84  ? 296  ASN A ND2   1 
ATOM   2143 N  N     . GLY A 1 297  ? 110.946 89.576  64.922  1.00 102.22 ? 297  GLY A N     1 
ATOM   2144 C  CA    . GLY A 1 297  ? 109.686 90.096  64.435  1.00 102.22 ? 297  GLY A CA    1 
ATOM   2145 C  C     . GLY A 1 297  ? 108.465 89.664  65.215  1.00 102.22 ? 297  GLY A C     1 
ATOM   2146 O  O     . GLY A 1 297  ? 107.352 90.072  64.862  1.00 102.22 ? 297  GLY A O     1 
ATOM   2147 N  N     . GLN A 1 298  ? 108.633 88.852  66.261  1.00 100.29 ? 298  GLN A N     1 
ATOM   2148 C  CA    . GLN A 1 298  ? 107.484 88.399  67.037  1.00 100.29 ? 298  GLN A CA    1 
ATOM   2149 C  C     . GLN A 1 298  ? 106.863 89.531  67.846  1.00 100.29 ? 298  GLN A C     1 
ATOM   2150 O  O     . GLN A 1 298  ? 105.656 89.507  68.113  1.00 100.29 ? 298  GLN A O     1 
ATOM   2151 C  CB    . GLN A 1 298  ? 107.892 87.245  67.951  1.00 100.29 ? 298  GLN A CB    1 
ATOM   2152 C  CG    . GLN A 1 298  ? 109.059 87.558  68.869  1.00 100.29 ? 298  GLN A CG    1 
ATOM   2153 C  CD    . GLN A 1 298  ? 109.488 86.357  69.688  1.00 100.29 ? 298  GLN A CD    1 
ATOM   2154 O  OE1   . GLN A 1 298  ? 108.888 85.286  69.601  1.00 100.29 ? 298  GLN A OE1   1 
ATOM   2155 N  NE2   . GLN A 1 298  ? 110.530 86.530  70.489  1.00 100.29 ? 298  GLN A NE2   1 
ATOM   2156 N  N     . THR A 1 299  ? 107.656 90.519  68.245  1.00 97.34  ? 299  THR A N     1 
ATOM   2157 C  CA    . THR A 1 299  ? 107.165 91.671  68.984  1.00 97.34  ? 299  THR A CA    1 
ATOM   2158 C  C     . THR A 1 299  ? 107.254 92.920  68.118  1.00 97.34  ? 299  THR A C     1 
ATOM   2159 O  O     . THR A 1 299  ? 108.057 92.991  67.182  1.00 97.34  ? 299  THR A O     1 
ATOM   2160 C  CB    . THR A 1 299  ? 107.953 91.878  70.282  1.00 97.34  ? 299  THR A CB    1 
ATOM   2161 O  OG1   . THR A 1 299  ? 107.487 93.060  70.944  1.00 97.34  ? 299  THR A OG1   1 
ATOM   2162 C  CG2   . THR A 1 299  ? 109.436 92.017  69.988  1.00 97.34  ? 299  THR A CG2   1 
ATOM   2163 N  N     . ASP A 1 300  ? 106.414 93.906  68.430  1.00 97.87  ? 300  ASP A N     1 
ATOM   2164 C  CA    . ASP A 1 300  ? 106.308 95.134  67.639  1.00 97.87  ? 300  ASP A CA    1 
ATOM   2165 C  C     . ASP A 1 300  ? 106.159 96.382  68.516  1.00 97.87  ? 300  ASP A C     1 
ATOM   2166 O  O     . ASP A 1 300  ? 105.053 96.824  68.838  1.00 97.87  ? 300  ASP A O     1 
ATOM   2167 C  CB    . ASP A 1 300  ? 105.169 94.985  66.612  1.00 97.87  ? 300  ASP A CB    1 
ATOM   2168 C  CG    . ASP A 1 300  ? 103.798 94.779  67.253  1.00 97.87  ? 300  ASP A CG    1 
ATOM   2169 O  OD1   . ASP A 1 300  ? 103.700 94.700  68.495  1.00 97.87  ? 300  ASP A OD1   1 
ATOM   2170 O  OD2   . ASP A 1 300  ? 102.807 94.693  66.497  1.00 97.87  ? 300  ASP A OD2   1 
ATOM   2171 N  N     . GLY A 1 301  ? 107.292 96.980  68.879  1.00 93.67  ? 301  GLY A N     1 
ATOM   2172 C  CA    . GLY A 1 301  ? 107.277 98.297  69.486  1.00 93.67  ? 301  GLY A CA    1 
ATOM   2173 C  C     . GLY A 1 301  ? 106.581 98.407  70.828  1.00 93.67  ? 301  GLY A C     1 
ATOM   2174 O  O     . GLY A 1 301  ? 107.139 98.037  71.868  1.00 93.67  ? 301  GLY A O     1 
ATOM   2175 N  N     . GLY A 1 302  ? 105.372 98.970  70.809  1.00 92.64  ? 302  GLY A N     1 
ATOM   2176 C  CA    . GLY A 1 302  ? 104.592 99.248  72.000  1.00 92.64  ? 302  GLY A CA    1 
ATOM   2177 C  C     . GLY A 1 302  ? 104.583 98.165  73.059  1.00 92.64  ? 302  GLY A C     1 
ATOM   2178 O  O     . GLY A 1 302  ? 104.593 98.473  74.252  1.00 92.64  ? 302  GLY A O     1 
ATOM   2179 N  N     . LYS A 1 303  ? 104.566 96.896  72.647  1.00 87.95  ? 303  LYS A N     1 
ATOM   2180 C  CA    . LYS A 1 303  ? 104.636 95.812  73.622  1.00 87.95  ? 303  LYS A CA    1 
ATOM   2181 C  C     . LYS A 1 303  ? 105.959 95.843  74.379  1.00 87.95  ? 303  LYS A C     1 
ATOM   2182 O  O     . LYS A 1 303  ? 105.985 95.753  75.616  1.00 87.95  ? 303  LYS A O     1 
ATOM   2183 C  CB    . LYS A 1 303  ? 104.448 94.467  72.921  1.00 87.95  ? 303  LYS A CB    1 
ATOM   2184 C  CG    . LYS A 1 303  ? 103.305 94.452  71.921  1.00 87.95  ? 303  LYS A CG    1 
ATOM   2185 C  CD    . LYS A 1 303  ? 101.974 94.713  72.602  1.00 87.95  ? 303  LYS A CD    1 
ATOM   2186 C  CE    . LYS A 1 303  ? 100.832 94.702  71.599  1.00 87.95  ? 303  LYS A CE    1 
ATOM   2187 N  NZ    . LYS A 1 303  ? 99.524  94.997  72.246  1.00 87.95  ? 303  LYS A NZ    1 
ATOM   2188 N  N     . ALA A 1 304  ? 107.068 95.979  73.648  1.00 84.91  ? 304  ALA A N     1 
ATOM   2189 C  CA    . ALA A 1 304  ? 108.372 96.091  74.289  1.00 84.91  ? 304  ALA A CA    1 
ATOM   2190 C  C     . ALA A 1 304  ? 108.447 97.338  75.157  1.00 84.91  ? 304  ALA A C     1 
ATOM   2191 O  O     . ALA A 1 304  ? 109.011 97.304  76.256  1.00 84.91  ? 304  ALA A O     1 
ATOM   2192 C  CB    . ALA A 1 304  ? 109.477 96.100  73.234  1.00 84.91  ? 304  ALA A CB    1 
ATOM   2193 N  N     . PHE A 1 305  ? 107.886 98.449  74.676  1.00 84.81  ? 305  PHE A N     1 
ATOM   2194 C  CA    . PHE A 1 305  ? 107.853 99.672  75.475  1.00 84.81  ? 305  PHE A CA    1 
ATOM   2195 C  C     . PHE A 1 305  ? 107.129 99.455  76.800  1.00 84.81  ? 305  PHE A C     1 
ATOM   2196 O  O     . PHE A 1 305  ? 107.630 99.845  77.864  1.00 84.81  ? 305  PHE A O     1 
ATOM   2197 C  CB    . PHE A 1 305  ? 107.184 100.793 74.681  1.00 84.81  ? 305  PHE A CB    1 
ATOM   2198 C  CG    . PHE A 1 305  ? 107.151 102.112 75.399  1.00 84.81  ? 305  PHE A CG    1 
ATOM   2199 C  CD1   . PHE A 1 305  ? 108.250 102.951 75.383  1.00 84.81  ? 305  PHE A CD1   1 
ATOM   2200 C  CD2   . PHE A 1 305  ? 106.017 102.513 76.085  1.00 84.81  ? 305  PHE A CD2   1 
ATOM   2201 C  CE1   . PHE A 1 305  ? 108.219 104.165 76.038  1.00 84.81  ? 305  PHE A CE1   1 
ATOM   2202 C  CE2   . PHE A 1 305  ? 105.981 103.725 76.745  1.00 84.81  ? 305  PHE A CE2   1 
ATOM   2203 C  CZ    . PHE A 1 305  ? 107.084 104.552 76.722  1.00 84.81  ? 305  PHE A CZ    1 
ATOM   2204 N  N     . THR A 1 306  ? 105.947 98.838  76.752  1.00 77.56  ? 306  THR A N     1 
ATOM   2205 C  CA    . THR A 1 306  ? 105.167 98.616  77.964  1.00 77.56  ? 306  THR A CA    1 
ATOM   2206 C  C     . THR A 1 306  ? 105.908 97.701  78.929  1.00 77.56  ? 306  THR A C     1 
ATOM   2207 O  O     . THR A 1 306  ? 105.972 97.971  80.135  1.00 77.56  ? 306  THR A O     1 
ATOM   2208 C  CB    . THR A 1 306  ? 103.801 98.026  77.609  1.00 77.56  ? 306  THR A CB    1 
ATOM   2209 O  OG1   . THR A 1 306  ? 103.975 96.916  76.720  1.00 77.56  ? 306  THR A OG1   1 
ATOM   2210 C  CG2   . THR A 1 306  ? 102.927 99.072  76.938  1.00 77.56  ? 306  THR A CG2   1 
ATOM   2211 N  N     . ALA A 1 307  ? 106.484 96.612  78.411  1.00 74.13  ? 307  ALA A N     1 
ATOM   2212 C  CA    . ALA A 1 307  ? 107.213 95.691  79.277  1.00 74.13  ? 307  ALA A CA    1 
ATOM   2213 C  C     . ALA A 1 307  ? 108.421 96.368  79.913  1.00 74.13  ? 307  ALA A C     1 
ATOM   2214 O  O     . ALA A 1 307  ? 108.693 96.181  81.107  1.00 74.13  ? 307  ALA A O     1 
ATOM   2215 C  CB    . ALA A 1 307  ? 107.642 94.457  78.485  1.00 74.13  ? 307  ALA A CB    1 
ATOM   2216 N  N     . ILE A 1 308  ? 109.150 97.168  79.133  1.00 72.53  ? 308  ILE A N     1 
ATOM   2217 C  CA    . ILE A 1 308  ? 110.335 97.850  79.645  1.00 72.53  ? 308  ILE A CA    1 
ATOM   2218 C  C     . ILE A 1 308  ? 109.949 98.826  80.748  1.00 72.53  ? 308  ILE A C     1 
ATOM   2219 O  O     . ILE A 1 308  ? 110.583 98.876  81.812  1.00 72.53  ? 308  ILE A O     1 
ATOM   2220 C  CB    . ILE A 1 308  ? 111.070 98.561  78.496  1.00 72.53  ? 308  ILE A CB    1 
ATOM   2221 C  CG1   . ILE A 1 308  ? 111.901 97.559  77.695  1.00 72.53  ? 308  ILE A CG1   1 
ATOM   2222 C  CG2   . ILE A 1 308  ? 111.930 99.694  79.030  1.00 72.53  ? 308  ILE A CG2   1 
ATOM   2223 C  CD1   . ILE A 1 308  ? 112.242 98.030  76.298  1.00 72.53  ? 308  ILE A CD1   1 
ATOM   2224 N  N     . PHE A 1 309  ? 108.905 99.622  80.506  1.00 67.29  ? 309  PHE A N     1 
ATOM   2225 C  CA    . PHE A 1 309  ? 108.481 100.589 81.512  1.00 67.29  ? 309  PHE A CA    1 
ATOM   2226 C  C     . PHE A 1 309  ? 108.005 99.887  82.776  1.00 67.29  ? 309  PHE A C     1 
ATOM   2227 O  O     . PHE A 1 309  ? 108.303 100.331 83.894  1.00 67.29  ? 309  PHE A O     1 
ATOM   2228 C  CB    . PHE A 1 309  ? 107.385 101.492 80.949  1.00 67.29  ? 309  PHE A CB    1 
ATOM   2229 C  CG    . PHE A 1 309  ? 107.289 102.815 81.644  1.00 67.29  ? 309  PHE A CG    1 
ATOM   2230 C  CD1   . PHE A 1 309  ? 106.546 102.954 82.802  1.00 67.29  ? 309  PHE A CD1   1 
ATOM   2231 C  CD2   . PHE A 1 309  ? 107.960 103.919 81.147  1.00 67.29  ? 309  PHE A CD2   1 
ATOM   2232 C  CE1   . PHE A 1 309  ? 106.468 104.171 83.446  1.00 67.29  ? 309  PHE A CE1   1 
ATOM   2233 C  CE2   . PHE A 1 309  ? 107.884 105.137 81.786  1.00 67.29  ? 309  PHE A CE2   1 
ATOM   2234 C  CZ    . PHE A 1 309  ? 107.139 105.263 82.938  1.00 67.29  ? 309  PHE A CZ    1 
ATOM   2235 N  N     . SER A 1 310  ? 107.272 98.781  82.619  1.00 63.46  ? 310  SER A N     1 
ATOM   2236 C  CA    . SER A 1 310  ? 106.818 98.025  83.780  1.00 63.46  ? 310  SER A CA    1 
ATOM   2237 C  C     . SER A 1 310  ? 107.995 97.506  84.595  1.00 63.46  ? 310  SER A C     1 
ATOM   2238 O  O     . SER A 1 310  ? 107.996 97.605  85.827  1.00 63.46  ? 310  SER A O     1 
ATOM   2239 C  CB    . SER A 1 310  ? 105.925 96.871  83.328  1.00 63.46  ? 310  SER A CB    1 
ATOM   2240 O  OG    . SER A 1 310  ? 104.875 97.335  82.497  1.00 63.46  ? 310  SER A OG    1 
ATOM   2241 N  N     . ALA A 1 311  ? 109.011 96.957  83.923  1.00 61.10  ? 311  ALA A N     1 
ATOM   2242 C  CA    . ALA A 1 311  ? 110.174 96.443  84.641  1.00 61.10  ? 311  ALA A CA    1 
ATOM   2243 C  C     . ALA A 1 311  ? 110.909 97.557  85.377  1.00 61.10  ? 311  ALA A C     1 
ATOM   2244 O  O     . ALA A 1 311  ? 111.314 97.388  86.539  1.00 61.10  ? 311  ALA A O     1 
ATOM   2245 C  CB    . ALA A 1 311  ? 111.116 95.730  83.672  1.00 61.10  ? 311  ALA A CB    1 
ATOM   2246 N  N     . ILE A 1 312  ? 111.087 98.706  84.719  1.00 57.83  ? 312  ILE A N     1 
ATOM   2247 C  CA    . ILE A 1 312  ? 111.798 99.818  85.346  1.00 57.83  ? 312  ILE A CA    1 
ATOM   2248 C  C     . ILE A 1 312  ? 111.050 100.292 86.586  1.00 57.83  ? 312  ILE A C     1 
ATOM   2249 O  O     . ILE A 1 312  ? 111.641 100.495 87.657  1.00 57.83  ? 312  ILE A O     1 
ATOM   2250 C  CB    . ILE A 1 312  ? 112.000 100.963 84.338  1.00 57.83  ? 312  ILE A CB    1 
ATOM   2251 C  CG1   . ILE A 1 312  ? 113.045 100.573 83.292  1.00 57.83  ? 312  ILE A CG1   1 
ATOM   2252 C  CG2   . ILE A 1 312  ? 112.411 102.239 85.054  1.00 57.83  ? 312  ILE A CG2   1 
ATOM   2253 C  CD1   . ILE A 1 312  ? 113.335 101.664 82.288  1.00 57.83  ? 312  ILE A CD1   1 
ATOM   2254 N  N     . VAL A 1 313  ? 109.731 100.454 86.464  1.00 53.23  ? 313  VAL A N     1 
ATOM   2255 C  CA    . VAL A 1 313  ? 108.941 100.933 87.592  1.00 53.23  ? 313  VAL A CA    1 
ATOM   2256 C  C     . VAL A 1 313  ? 108.937 99.906  88.719  1.00 53.23  ? 313  VAL A C     1 
ATOM   2257 O  O     . VAL A 1 313  ? 108.960 100.268 89.900  1.00 53.23  ? 313  VAL A O     1 
ATOM   2258 C  CB    . VAL A 1 313  ? 107.518 101.290 87.130  1.00 53.23  ? 313  VAL A CB    1 
ATOM   2259 C  CG1   . VAL A 1 313  ? 106.617 101.546 88.320  1.00 53.23  ? 313  VAL A CG1   1 
ATOM   2260 C  CG2   . VAL A 1 313  ? 107.560 102.512 86.240  1.00 53.23  ? 313  VAL A CG2   1 
ATOM   2261 N  N     . GLY A 1 314  ? 108.921 98.615  88.381  1.00 49.69  ? 314  GLY A N     1 
ATOM   2262 C  CA    . GLY A 1 314  ? 108.967 97.597  89.419  1.00 49.69  ? 314  GLY A CA    1 
ATOM   2263 C  C     . GLY A 1 314  ? 110.260 97.633  90.212  1.00 49.69  ? 314  GLY A C     1 
ATOM   2264 O  O     . GLY A 1 314  ? 110.251 97.583  91.448  1.00 49.69  ? 314  GLY A O     1 
ATOM   2265 N  N     . GLY A 1 315  ? 111.393 97.722  89.510  1.00 45.85  ? 315  GLY A N     1 
ATOM   2266 C  CA    . GLY A 1 315  ? 112.665 97.828  90.210  1.00 45.85  ? 315  GLY A CA    1 
ATOM   2267 C  C     . GLY A 1 315  ? 112.742 99.070  91.078  1.00 45.85  ? 315  GLY A C     1 
ATOM   2268 O  O     . GLY A 1 315  ? 113.205 99.019  92.225  1.00 45.85  ? 315  GLY A O     1 
ATOM   2269 N  N     . MET A 1 316  ? 112.265 100.198 90.548  1.00 46.27  ? 316  MET A N     1 
ATOM   2270 C  CA    . MET A 1 316  ? 112.239 101.439 91.313  1.00 46.27  ? 316  MET A CA    1 
ATOM   2271 C  C     . MET A 1 316  ? 111.377 101.311 92.567  1.00 46.27  ? 316  MET A C     1 
ATOM   2272 O  O     . MET A 1 316  ? 111.766 101.768 93.650  1.00 46.27  ? 316  MET A O     1 
ATOM   2273 C  CB    . MET A 1 316  ? 111.731 102.556 90.408  1.00 46.27  ? 316  MET A CB    1 
ATOM   2274 C  CG    . MET A 1 316  ? 111.639 103.919 91.027  1.00 46.27  ? 316  MET A CG    1 
ATOM   2275 S  SD    . MET A 1 316  ? 111.437 105.118 89.703  1.00 46.27  ? 316  MET A SD    1 
ATOM   2276 C  CE    . MET A 1 316  ? 110.149 106.130 90.401  1.00 46.27  ? 316  MET A CE    1 
ATOM   2277 N  N     . SER A 1 317  ? 110.205 100.686 92.440  1.00 40.88  ? 317  SER A N     1 
ATOM   2278 C  CA    . SER A 1 317  ? 109.317 100.524 93.585  1.00 40.88  ? 317  SER A CA    1 
ATOM   2279 C  C     . SER A 1 317  ? 109.939 99.628  94.647  1.00 40.88  ? 317  SER A C     1 
ATOM   2280 O  O     . SER A 1 317  ? 109.793 99.889  95.847  1.00 40.88  ? 317  SER A O     1 
ATOM   2281 C  CB    . SER A 1 317  ? 107.974 99.960  93.126  1.00 40.88  ? 317  SER A CB    1 
ATOM   2282 O  OG    . SER A 1 317  ? 107.499 100.650 91.984  1.00 40.88  ? 317  SER A OG    1 
ATOM   2283 N  N     . LEU A 1 318  ? 110.621 98.560  94.230  1.00 38.69  ? 318  LEU A N     1 
ATOM   2284 C  CA    . LEU A 1 318  ? 111.302 97.710  95.204  1.00 38.69  ? 318  LEU A CA    1 
ATOM   2285 C  C     . LEU A 1 318  ? 112.384 98.489  95.945  1.00 38.69  ? 318  LEU A C     1 
ATOM   2286 O  O     . LEU A 1 318  ? 112.502 98.402  97.182  1.00 38.69  ? 318  LEU A O     1 
ATOM   2287 C  CB    . LEU A 1 318  ? 111.901 96.492  94.502  1.00 38.69  ? 318  LEU A CB    1 
ATOM   2288 C  CG    . LEU A 1 318  ? 111.059 95.215  94.475  1.00 38.69  ? 318  LEU A CG    1 
ATOM   2289 C  CD1   . LEU A 1 318  ? 109.662 95.481  93.935  1.00 38.69  ? 318  LEU A CD1   1 
ATOM   2290 C  CD2   . LEU A 1 318  ? 111.754 94.146  93.649  1.00 38.69  ? 318  LEU A CD2   1 
ATOM   2291 N  N     . GLY A 1 319  ? 113.176 99.267  95.203  1.00 36.84  ? 319  GLY A N     1 
ATOM   2292 C  CA    . GLY A 1 319  ? 114.190 100.090 95.840  1.00 36.84  ? 319  GLY A CA    1 
ATOM   2293 C  C     . GLY A 1 319  ? 113.596 101.072 96.831  1.00 36.84  ? 319  GLY A C     1 
ATOM   2294 O  O     . GLY A 1 319  ? 114.190 101.355 97.873  1.00 36.84  ? 319  GLY A O     1 
ATOM   2295 N  N     . GLN A 1 320  ? 112.415 101.606 96.518  1.00 36.88  ? 320  GLN A N     1 
ATOM   2296 C  CA    . GLN A 1 320  ? 111.750 102.509 97.454  1.00 36.88  ? 320  GLN A CA    1 
ATOM   2297 C  C     . GLN A 1 320  ? 111.260 101.771 98.698  1.00 36.88  ? 320  GLN A C     1 
ATOM   2298 O  O     . GLN A 1 320  ? 111.414 102.267 99.820  1.00 36.88  ? 320  GLN A O     1 
ATOM   2299 C  CB    . GLN A 1 320  ? 110.589 103.221 96.760  1.00 36.88  ? 320  GLN A CB    1 
ATOM   2300 C  CG    . GLN A 1 320  ? 111.011 104.182 95.661  1.00 36.88  ? 320  GLN A CG    1 
ATOM   2301 C  CD    . GLN A 1 320  ? 111.806 105.359 96.188  1.00 36.88  ? 320  GLN A CD    1 
ATOM   2302 O  OE1   . GLN A 1 320  ? 111.279 106.206 96.909  1.00 36.88  ? 320  GLN A OE1   1 
ATOM   2303 N  NE2   . GLN A 1 320  ? 113.081 105.420 95.826  1.00 36.88  ? 320  GLN A NE2   1 
ATOM   2304 N  N     . SER A 1 321  ? 110.669 100.585 98.523  1.00 33.09  ? 321  SER A N     1 
ATOM   2305 C  CA    . SER A 1 321  ? 110.066 99.851  99.634  1.00 33.09  ? 321  SER A CA    1 
ATOM   2306 C  C     . SER A 1 321  ? 111.093 99.219  100.568 1.00 33.09  ? 321  SER A C     1 
ATOM   2307 O  O     . SER A 1 321  ? 110.717 98.749  101.655 1.00 33.09  ? 321  SER A O     1 
ATOM   2308 C  CB    . SER A 1 321  ? 109.130 98.769  99.094  1.00 33.09  ? 321  SER A CB    1 
ATOM   2309 O  OG    . SER A 1 321  ? 109.861 97.651  98.625  1.00 33.09  ? 321  SER A OG    1 
ATOM   2310 N  N     . PHE A 1 322  ? 112.361 99.164  100.156 1.00 35.31  ? 322  PHE A N     1 
ATOM   2311 C  CA    . PHE A 1 322  ? 113.410 98.664  101.046 1.00 35.31  ? 322  PHE A CA    1 
ATOM   2312 C  C     . PHE A 1 322  ? 113.390 99.361  102.413 1.00 35.31  ? 322  PHE A C     1 
ATOM   2313 O  O     . PHE A 1 322  ? 113.534 98.711  103.463 1.00 35.31  ? 322  PHE A O     1 
ATOM   2314 C  CB    . PHE A 1 322  ? 114.768 98.848  100.370 1.00 35.31  ? 322  PHE A CB    1 
ATOM   2315 C  CG    . PHE A 1 322  ? 115.863 98.017  100.961 1.00 35.31  ? 322  PHE A CG    1 
ATOM   2316 C  CD1   . PHE A 1 322  ? 115.967 96.672  100.655 1.00 35.31  ? 322  PHE A CD1   1 
ATOM   2317 C  CD2   . PHE A 1 322  ? 116.797 98.581  101.812 1.00 35.31  ? 322  PHE A CD2   1 
ATOM   2318 C  CE1   . PHE A 1 322  ? 116.979 95.904  101.192 1.00 35.31  ? 322  PHE A CE1   1 
ATOM   2319 C  CE2   . PHE A 1 322  ? 117.811 97.817  102.352 1.00 35.31  ? 322  PHE A CE2   1 
ATOM   2320 C  CZ    . PHE A 1 322  ? 117.902 96.477  102.040 1.00 35.31  ? 322  PHE A CZ    1 
ATOM   2321 N  N     . SER A 1 323  ? 113.216 100.686 102.422 1.00 32.34  ? 323  SER A N     1 
ATOM   2322 C  CA    . SER A 1 323  ? 113.231 101.432 103.679 1.00 32.34  ? 323  SER A CA    1 
ATOM   2323 C  C     . SER A 1 323  ? 112.057 101.050 104.576 1.00 32.34  ? 323  SER A C     1 
ATOM   2324 O  O     . SER A 1 323  ? 112.212 100.933 105.800 1.00 32.34  ? 323  SER A O     1 
ATOM   2325 C  CB    . SER A 1 323  ? 113.225 102.933 103.395 1.00 32.34  ? 323  SER A CB    1 
ATOM   2326 O  OG    . SER A 1 323  ? 114.375 103.315 102.662 1.00 32.34  ? 323  SER A OG    1 
ATOM   2327 N  N     . ASN A 1 324  ? 110.872 100.868 103.990 1.00 30.16  ? 324  ASN A N     1 
ATOM   2328 C  CA    . ASN A 1 324  ? 109.730 100.410 104.774 1.00 30.16  ? 324  ASN A CA    1 
ATOM   2329 C  C     . ASN A 1 324  ? 109.989 99.026  105.350 1.00 30.16  ? 324  ASN A C     1 
ATOM   2330 O  O     . ASN A 1 324  ? 109.561 98.720  106.471 1.00 30.16  ? 324  ASN A O     1 
ATOM   2331 C  CB    . ASN A 1 324  ? 108.467 100.410 103.915 1.00 30.16  ? 324  ASN A CB    1 
ATOM   2332 C  CG    . ASN A 1 324  ? 108.178 101.764 103.306 1.00 30.16  ? 324  ASN A CG    1 
ATOM   2333 O  OD1   . ASN A 1 324  ? 108.702 102.783 103.755 1.00 30.16  ? 324  ASN A OD1   1 
ATOM   2334 N  ND2   . ASN A 1 324  ? 107.338 101.784 102.279 1.00 30.16  ? 324  ASN A ND2   1 
ATOM   2335 N  N     . LEU A 1 325  ? 110.691 98.175  104.597 1.00 26.75  ? 325  LEU A N     1 
ATOM   2336 C  CA    . LEU A 1 325  ? 111.067 96.869  105.136 1.00 26.75  ? 325  LEU A CA    1 
ATOM   2337 C  C     . LEU A 1 325  ? 111.939 97.020  106.379 1.00 26.75  ? 325  LEU A C     1 
ATOM   2338 O  O     . LEU A 1 325  ? 111.725 96.339  107.394 1.00 26.75  ? 325  LEU A O     1 
ATOM   2339 C  CB    . LEU A 1 325  ? 111.785 96.049  104.064 1.00 26.75  ? 325  LEU A CB    1 
ATOM   2340 C  CG    . LEU A 1 325  ? 112.062 94.575  104.360 1.00 26.75  ? 325  LEU A CG    1 
ATOM   2341 C  CD1   . LEU A 1 325  ? 111.918 93.755  103.091 1.00 26.75  ? 325  LEU A CD1   1 
ATOM   2342 C  CD2   . LEU A 1 325  ? 113.449 94.391  104.947 1.00 26.75  ? 325  LEU A CD2   1 
ATOM   2343 N  N     . GLY A 1 326  ? 112.923 97.917  106.320 1.00 24.13  ? 326  GLY A N     1 
ATOM   2344 C  CA    . GLY A 1 326  ? 113.751 98.159  107.497 1.00 24.13  ? 326  GLY A CA    1 
ATOM   2345 C  C     . GLY A 1 326  ? 112.955 98.679  108.682 1.00 24.13  ? 326  GLY A C     1 
ATOM   2346 O  O     . GLY A 1 326  ? 113.181 98.275  109.833 1.00 24.13  ? 326  GLY A O     1 
ATOM   2347 N  N     . ALA A 1 327  ? 112.015 99.589  108.417 1.00 23.33  ? 327  ALA A N     1 
ATOM   2348 C  CA    . ALA A 1 327  ? 111.171 100.115 109.486 1.00 23.33  ? 327  ALA A CA    1 
ATOM   2349 C  C     . ALA A 1 327  ? 110.347 99.008  110.132 1.00 23.33  ? 327  ALA A C     1 
ATOM   2350 O  O     . ALA A 1 327  ? 110.200 98.968  111.360 1.00 23.33  ? 327  ALA A O     1 
ATOM   2351 C  CB    . ALA A 1 327  ? 110.262 101.218 108.947 1.00 23.33  ? 327  ALA A CB    1 
ATOM   2352 N  N     . PHE A 1 328  ? 109.807 98.097  109.319 1.00 23.57  ? 328  PHE A N     1 
ATOM   2353 C  CA    . PHE A 1 328  ? 109.062 96.966  109.866 1.00 23.57  ? 328  PHE A CA    1 
ATOM   2354 C  C     . PHE A 1 328  ? 109.954 96.088  110.733 1.00 23.57  ? 328  PHE A C     1 
ATOM   2355 O  O     . PHE A 1 328  ? 109.517 95.577  111.774 1.00 23.57  ? 328  PHE A O     1 
ATOM   2356 C  CB    . PHE A 1 328  ? 108.448 96.136  108.739 1.00 23.57  ? 328  PHE A CB    1 
ATOM   2357 C  CG    . PHE A 1 328  ? 107.487 96.896  107.877 1.00 23.57  ? 328  PHE A CG    1 
ATOM   2358 C  CD1   . PHE A 1 328  ? 106.806 97.992  108.371 1.00 23.57  ? 328  PHE A CD1   1 
ATOM   2359 C  CD2   . PHE A 1 328  ? 107.261 96.506  106.569 1.00 23.57  ? 328  PHE A CD2   1 
ATOM   2360 C  CE1   . PHE A 1 328  ? 105.922 98.689  107.576 1.00 23.57  ? 328  PHE A CE1   1 
ATOM   2361 C  CE2   . PHE A 1 328  ? 106.378 97.198  105.770 1.00 23.57  ? 328  PHE A CE2   1 
ATOM   2362 C  CZ    . PHE A 1 328  ? 105.708 98.291  106.274 1.00 23.57  ? 328  PHE A CZ    1 
ATOM   2363 N  N     . SER A 1 329  ? 111.202 95.881  110.306 1.00 23.97  ? 329  SER A N     1 
ATOM   2364 C  CA    . SER A 1 329  ? 112.131 95.084  111.106 1.00 23.97  ? 329  SER A CA    1 
ATOM   2365 C  C     . SER A 1 329  ? 112.335 95.699  112.488 1.00 23.97  ? 329  SER A C     1 
ATOM   2366 O  O     . SER A 1 329  ? 112.243 95.008  113.514 1.00 23.97  ? 329  SER A O     1 
ATOM   2367 C  CB    . SER A 1 329  ? 113.466 94.948  110.375 1.00 23.97  ? 329  SER A CB    1 
ATOM   2368 O  OG    . SER A 1 329  ? 113.279 94.464  109.058 1.00 23.97  ? 329  SER A OG    1 
ATOM   2369 N  N     . LYS A 1 330  ? 112.604 97.005  112.536 1.00 23.62  ? 330  LYS A N     1 
ATOM   2370 C  CA    . LYS A 1 330  ? 112.781 97.655  113.835 1.00 23.62  ? 330  LYS A CA    1 
ATOM   2371 C  C     . LYS A 1 330  ? 111.505 97.579  114.669 1.00 23.62  ? 330  LYS A C     1 
ATOM   2372 O  O     . LYS A 1 330  ? 111.554 97.354  115.891 1.00 23.62  ? 330  LYS A O     1 
ATOM   2373 C  CB    . LYS A 1 330  ? 113.213 99.108  113.647 1.00 23.62  ? 330  LYS A CB    1 
ATOM   2374 C  CG    . LYS A 1 330  ? 114.464 99.280  112.807 1.00 23.62  ? 330  LYS A CG    1 
ATOM   2375 C  CD    . LYS A 1 330  ? 114.518 100.659 112.172 1.00 23.62  ? 330  LYS A CD    1 
ATOM   2376 C  CE    . LYS A 1 330  ? 114.395 101.752 113.220 1.00 23.62  ? 330  LYS A CE    1 
ATOM   2377 N  NZ    . LYS A 1 330  ? 115.408 101.599 114.300 1.00 23.62  ? 330  LYS A NZ    1 
ATOM   2378 N  N     . GLY A 1 331  ? 110.351 97.761  114.023 1.00 25.08  ? 331  GLY A N     1 
ATOM   2379 C  CA    . GLY A 1 331  ? 109.093 97.714  114.748 1.00 25.08  ? 331  GLY A CA    1 
ATOM   2380 C  C     . GLY A 1 331  ? 108.848 96.372  115.408 1.00 25.08  ? 331  GLY A C     1 
ATOM   2381 O  O     . GLY A 1 331  ? 108.453 96.304  116.572 1.00 25.08  ? 331  GLY A O     1 
ATOM   2382 N  N     . LYS A 1 332  ? 109.085 95.282  114.673 1.00 25.73  ? 332  LYS A N     1 
ATOM   2383 C  CA    . LYS A 1 332  ? 108.895 93.959  115.264 1.00 25.73  ? 332  LYS A CA    1 
ATOM   2384 C  C     . LYS A 1 332  ? 109.930 93.678  116.348 1.00 25.73  ? 332  LYS A C     1 
ATOM   2385 O  O     . LYS A 1 332  ? 109.615 93.019  117.354 1.00 25.73  ? 332  LYS A O     1 
ATOM   2386 C  CB    . LYS A 1 332  ? 108.921 92.882  114.173 1.00 25.73  ? 332  LYS A CB    1 
ATOM   2387 C  CG    . LYS A 1 332  ? 110.251 92.708  113.467 1.00 25.73  ? 332  LYS A CG    1 
ATOM   2388 C  CD    . LYS A 1 332  ? 110.172 91.677  112.352 1.00 25.73  ? 332  LYS A CD    1 
ATOM   2389 C  CE    . LYS A 1 332  ? 110.015 90.272  112.890 1.00 25.73  ? 332  LYS A CE    1 
ATOM   2390 N  NZ    . LYS A 1 332  ? 111.227 89.838  113.630 1.00 25.73  ? 332  LYS A NZ    1 
ATOM   2391 N  N     . ALA A 1 333  ? 111.152 94.199  116.186 1.00 26.87  ? 333  ALA A N     1 
ATOM   2392 C  CA    . ALA A 1 333  ? 112.159 94.032  117.230 1.00 26.87  ? 333  ALA A CA    1 
ATOM   2393 C  C     . ALA A 1 333  ? 111.707 94.660  118.543 1.00 26.87  ? 333  ALA A C     1 
ATOM   2394 O  O     . ALA A 1 333  ? 111.919 94.087  119.617 1.00 26.87  ? 333  ALA A O     1 
ATOM   2395 C  CB    . ALA A 1 333  ? 113.490 94.632  116.778 1.00 26.87  ? 333  ALA A CB    1 
ATOM   2396 N  N     . ALA A 1 334  ? 111.088 95.843  118.481 1.00 27.03  ? 334  ALA A N     1 
ATOM   2397 C  CA    . ALA A 1 334  ? 110.583 96.460  119.711 1.00 27.03  ? 334  ALA A CA    1 
ATOM   2398 C  C     . ALA A 1 334  ? 109.303 95.779  120.201 1.00 27.03  ? 334  ALA A C     1 
ATOM   2399 O  O     . ALA A 1 334  ? 109.058 95.681  121.417 1.00 27.03  ? 334  ALA A O     1 
ATOM   2400 C  CB    . ALA A 1 334  ? 110.346 97.952  119.492 1.00 27.03  ? 334  ALA A CB    1 
ATOM   2401 N  N     . GLY A 1 335  ? 108.471 95.317  119.266 1.00 26.84  ? 335  GLY A N     1 
ATOM   2402 C  CA    . GLY A 1 335  ? 107.223 94.680  119.637 1.00 26.84  ? 335  GLY A CA    1 
ATOM   2403 C  C     . GLY A 1 335  ? 107.420 93.403  120.421 1.00 26.84  ? 335  GLY A C     1 
ATOM   2404 O  O     . GLY A 1 335  ? 106.603 93.072  121.283 1.00 26.84  ? 335  GLY A O     1 
ATOM   2405 N  N     . TYR A 1 336  ? 108.492 92.662  120.132 1.00 29.61  ? 336  TYR A N     1 
ATOM   2406 C  CA    . TYR A 1 336  ? 108.783 91.478  120.939 1.00 29.61  ? 336  TYR A CA    1 
ATOM   2407 C  C     . TYR A 1 336  ? 108.950 91.845  122.408 1.00 29.61  ? 336  TYR A C     1 
ATOM   2408 O  O     . TYR A 1 336  ? 108.356 91.216  123.294 1.00 29.61  ? 336  TYR A O     1 
ATOM   2409 C  CB    . TYR A 1 336  ? 110.040 90.773  120.436 1.00 29.61  ? 336  TYR A CB    1 
ATOM   2410 C  CG    . TYR A 1 336  ? 110.640 89.847  121.473 1.00 29.61  ? 336  TYR A CG    1 
ATOM   2411 C  CD1   . TYR A 1 336  ? 109.998 88.670  121.834 1.00 29.61  ? 336  TYR A CD1   1 
ATOM   2412 C  CD2   . TYR A 1 336  ? 111.837 90.159  122.104 1.00 29.61  ? 336  TYR A CD2   1 
ATOM   2413 C  CE1   . TYR A 1 336  ? 110.535 87.824  122.785 1.00 29.61  ? 336  TYR A CE1   1 
ATOM   2414 C  CE2   . TYR A 1 336  ? 112.382 89.318  123.057 1.00 29.61  ? 336  TYR A CE2   1 
ATOM   2415 C  CZ    . TYR A 1 336  ? 111.727 88.153  123.393 1.00 29.61  ? 336  TYR A CZ    1 
ATOM   2416 O  OH    . TYR A 1 336  ? 112.265 87.313  124.339 1.00 29.61  ? 336  TYR A OH    1 
ATOM   2417 N  N     . LYS A 1 337  ? 109.760 92.870  122.683 1.00 28.82  ? 337  LYS A N     1 
ATOM   2418 C  CA    . LYS A 1 337  ? 110.008 93.269  124.063 1.00 28.82  ? 337  LYS A CA    1 
ATOM   2419 C  C     . LYS A 1 337  ? 108.736 93.767  124.732 1.00 28.82  ? 337  LYS A C     1 
ATOM   2420 O  O     . LYS A 1 337  ? 108.501 93.489  125.913 1.00 28.82  ? 337  LYS A O     1 
ATOM   2421 C  CB    . LYS A 1 337  ? 111.095 94.340  124.118 1.00 28.82  ? 337  LYS A CB    1 
ATOM   2422 C  CG    . LYS A 1 337  ? 111.698 94.529  125.498 1.00 28.82  ? 337  LYS A CG    1 
ATOM   2423 C  CD    . LYS A 1 337  ? 112.327 93.241  126.000 1.00 28.82  ? 337  LYS A CD    1 
ATOM   2424 C  CE    . LYS A 1 337  ? 112.690 93.341  127.472 1.00 28.82  ? 337  LYS A CE    1 
ATOM   2425 N  NZ    . LYS A 1 337  ? 113.914 94.162  127.687 1.00 28.82  ? 337  LYS A NZ    1 
ATOM   2426 N  N     . LEU A 1 338  ? 107.905 94.518  124.003 1.00 27.00  ? 338  LEU A N     1 
ATOM   2427 C  CA    . LEU A 1 338  ? 106.643 94.955  124.601 1.00 27.00  ? 338  LEU A CA    1 
ATOM   2428 C  C     . LEU A 1 338  ? 105.726 93.775  124.913 1.00 27.00  ? 338  LEU A C     1 
ATOM   2429 O  O     . LEU A 1 338  ? 105.119 93.717  125.988 1.00 27.00  ? 338  LEU A O     1 
ATOM   2430 C  CB    . LEU A 1 338  ? 105.928 95.965  123.705 1.00 27.00  ? 338  LEU A CB    1 
ATOM   2431 C  CG    . LEU A 1 338  ? 106.643 97.299  123.542 1.00 27.00  ? 338  LEU A CG    1 
ATOM   2432 C  CD1   . LEU A 1 338  ? 105.922 98.165  122.534 1.00 27.00  ? 338  LEU A CD1   1 
ATOM   2433 C  CD2   . LEU A 1 338  ? 106.708 97.990  124.893 1.00 27.00  ? 338  LEU A CD2   1 
ATOM   2434 N  N     . MET A 1 339  ? 105.614 92.821  123.987 1.00 27.65  ? 339  MET A N     1 
ATOM   2435 C  CA    . MET A 1 339  ? 104.659 91.732  124.168 1.00 27.65  ? 339  MET A CA    1 
ATOM   2436 C  C     . MET A 1 339  ? 105.121 90.752  125.237 1.00 27.65  ? 339  MET A C     1 
ATOM   2437 O  O     . MET A 1 339  ? 104.298 90.066  125.855 1.00 27.65  ? 339  MET A O     1 
ATOM   2438 C  CB    . MET A 1 339  ? 104.434 91.003  122.844 1.00 27.65  ? 339  MET A CB    1 
ATOM   2439 C  CG    . MET A 1 339  ? 103.040 90.418  122.679 1.00 27.65  ? 339  MET A CG    1 
ATOM   2440 S  SD    . MET A 1 339  ? 101.787 91.660  122.309 1.00 27.65  ? 339  MET A SD    1 
ATOM   2441 C  CE    . MET A 1 339  ? 102.454 92.383  120.814 1.00 27.65  ? 339  MET A CE    1 
ATOM   2442 N  N     . GLU A 1 340  ? 106.433 90.658  125.463 1.00 31.73  ? 340  GLU A N     1 
ATOM   2443 C  CA    . GLU A 1 340  ? 106.935 89.672  126.416 1.00 31.73  ? 340  GLU A CA    1 
ATOM   2444 C  C     . GLU A 1 340  ? 106.498 90.002  127.840 1.00 31.73  ? 340  GLU A C     1 
ATOM   2445 O  O     . GLU A 1 340  ? 106.210 89.097  128.632 1.00 31.73  ? 340  GLU A O     1 
ATOM   2446 C  CB    . GLU A 1 340  ? 108.458 89.577  126.319 1.00 31.73  ? 340  GLU A CB    1 
ATOM   2447 C  CG    . GLU A 1 340  ? 109.068 88.414  127.093 1.00 31.73  ? 340  GLU A CG    1 
ATOM   2448 C  CD    . GLU A 1 340  ? 109.285 88.721  128.559 1.00 31.73  ? 340  GLU A CD    1 
ATOM   2449 O  OE1   . GLU A 1 340  ? 109.493 89.905  128.894 1.00 31.73  ? 340  GLU A OE1   1 
ATOM   2450 O  OE2   . GLU A 1 340  ? 109.240 87.778  129.376 1.00 31.73  ? 340  GLU A OE2   1 
ATOM   2451 N  N     . ILE A 1 341  ? 106.452 91.290  128.189 1.00 29.66  ? 341  ILE A N     1 
ATOM   2452 C  CA    . ILE A 1 341  ? 106.109 91.681  129.554 1.00 29.66  ? 341  ILE A CA    1 
ATOM   2453 C  C     . ILE A 1 341  ? 104.634 91.426  129.845 1.00 29.66  ? 341  ILE A C     1 
ATOM   2454 O  O     . ILE A 1 341  ? 104.281 90.901  130.908 1.00 29.66  ? 341  ILE A O     1 
ATOM   2455 C  CB    . ILE A 1 341  ? 106.477 93.155  129.798 1.00 29.66  ? 341  ILE A CB    1 
ATOM   2456 C  CG1   . ILE A 1 341  ? 107.972 93.382  129.570 1.00 29.66  ? 341  ILE A CG1   1 
ATOM   2457 C  CG2   . ILE A 1 341  ? 106.079 93.576  131.203 1.00 29.66  ? 341  ILE A CG2   1 
ATOM   2458 C  CD1   . ILE A 1 341  ? 108.855 92.582  130.495 1.00 29.66  ? 341  ILE A CD1   1 
ATOM   2459 N  N     . ILE A 1 342  ? 103.751 91.798  128.917 1.00 27.10  ? 342  ILE A N     1 
ATOM   2460 C  CA    . ILE A 1 342  ? 102.318 91.718  129.188 1.00 27.10  ? 342  ILE A CA    1 
ATOM   2461 C  C     . ILE A 1 342  ? 101.861 90.267  129.263 1.00 27.10  ? 342  ILE A C     1 
ATOM   2462 O  O     . ILE A 1 342  ? 100.995 89.918  130.074 1.00 27.10  ? 342  ILE A O     1 
ATOM   2463 C  CB    . ILE A 1 342  ? 101.524 92.514  128.136 1.00 27.10  ? 342  ILE A CB    1 
ATOM   2464 C  CG1   . ILE A 1 342  ? 101.726 91.939  126.735 1.00 27.10  ? 342  ILE A CG1   1 
ATOM   2465 C  CG2   . ILE A 1 342  ? 101.957 93.959  128.144 1.00 27.10  ? 342  ILE A CG2   1 
ATOM   2466 C  CD1   . ILE A 1 342  ? 100.796 92.529  125.700 1.00 27.10  ? 342  ILE A CD1   1 
ATOM   2467 N  N     . ASN A 1 343  ? 102.425 89.400  128.421 1.00 29.63  ? 343  ASN A N     1 
ATOM   2468 C  CA    . ASN A 1 343  ? 102.026 87.999  128.407 1.00 29.63  ? 343  ASN A CA    1 
ATOM   2469 C  C     . ASN A 1 343  ? 102.499 87.238  129.636 1.00 29.63  ? 343  ASN A C     1 
ATOM   2470 O  O     . ASN A 1 343  ? 102.005 86.133  129.882 1.00 29.63  ? 343  ASN A O     1 
ATOM   2471 C  CB    . ASN A 1 343  ? 102.551 87.316  127.145 1.00 29.63  ? 343  ASN A CB    1 
ATOM   2472 C  CG    . ASN A 1 343  ? 101.503 87.223  126.059 1.00 29.63  ? 343  ASN A CG    1 
ATOM   2473 O  OD1   . ASN A 1 343  ? 100.462 87.876  126.128 1.00 29.63  ? 343  ASN A OD1   1 
ATOM   2474 N  ND2   . ASN A 1 343  ? 101.770 86.408  125.046 1.00 29.63  ? 343  ASN A ND2   1 
ATOM   2475 N  N     . GLN A 1 344  ? 103.439 87.790  130.402 1.00 31.44  ? 344  GLN A N     1 
ATOM   2476 C  CA    . GLN A 1 344  ? 103.896 87.140  131.623 1.00 31.44  ? 344  GLN A CA    1 
ATOM   2477 C  C     . GLN A 1 344  ? 102.756 87.046  132.626 1.00 31.44  ? 344  GLN A C     1 
ATOM   2478 O  O     . GLN A 1 344  ? 102.300 88.066  133.153 1.00 31.44  ? 344  GLN A O     1 
ATOM   2479 C  CB    . GLN A 1 344  ? 105.077 87.897  132.230 1.00 31.44  ? 344  GLN A CB    1 
ATOM   2480 C  CG    . GLN A 1 344  ? 105.582 87.299  133.531 1.00 31.44  ? 344  GLN A CG    1 
ATOM   2481 C  CD    . GLN A 1 344  ? 107.010 87.699  133.841 1.00 31.44  ? 344  GLN A CD    1 
ATOM   2482 O  OE1   . GLN A 1 344  ? 107.310 88.172  134.937 1.00 31.44  ? 344  GLN A OE1   1 
ATOM   2483 N  NE2   . GLN A 1 344  ? 107.900 87.512  132.874 1.00 31.44  ? 344  GLN A NE2   1 
ATOM   2484 N  N     . ARG A 1 345  ? 102.288 85.830  132.889 1.00 37.04  ? 345  ARG A N     1 
ATOM   2485 C  CA    . ARG A 1 345  ? 101.215 85.638  133.847 1.00 37.04  ? 345  ARG A CA    1 
ATOM   2486 C  C     . ARG A 1 345  ? 101.686 86.026  135.248 1.00 37.04  ? 345  ARG A C     1 
ATOM   2487 O  O     . ARG A 1 345  ? 102.857 85.846  135.590 1.00 37.04  ? 345  ARG A O     1 
ATOM   2488 C  CB    . ARG A 1 345  ? 100.741 84.188  133.831 1.00 37.04  ? 345  ARG A CB    1 
ATOM   2489 C  CG    . ARG A 1 345  ? 101.849 83.176  134.052 1.00 37.04  ? 345  ARG A CG    1 
ATOM   2490 C  CD    . ARG A 1 345  ? 101.339 81.752  133.895 1.00 37.04  ? 345  ARG A CD    1 
ATOM   2491 N  NE    . ARG A 1 345  ? 102.286 80.766  134.409 1.00 37.04  ? 345  ARG A NE    1 
ATOM   2492 C  CZ    . ARG A 1 345  ? 103.432 80.443  133.816 1.00 37.04  ? 345  ARG A CZ    1 
ATOM   2493 N  NH1   . ARG A 1 345  ? 103.785 81.024  132.678 1.00 37.04  ? 345  ARG A NH1   1 
ATOM   2494 N  NH2   . ARG A 1 345  ? 104.226 79.532  134.362 1.00 37.04  ? 345  ARG A NH2   1 
ATOM   2495 N  N     . PRO A 1 346  ? 100.791 86.566  136.077 1.00 37.66  ? 346  PRO A N     1 
ATOM   2496 C  CA    . PRO A 1 346  ? 101.208 87.029  137.407 1.00 37.66  ? 346  PRO A CA    1 
ATOM   2497 C  C     . PRO A 1 346  ? 101.606 85.887  138.325 1.00 37.66  ? 346  PRO A C     1 
ATOM   2498 O  O     . PRO A 1 346  ? 101.567 84.717  137.935 1.00 37.66  ? 346  PRO A O     1 
ATOM   2499 C  CB    . PRO A 1 346  ? 99.965  87.759  137.928 1.00 37.66  ? 346  PRO A CB    1 
ATOM   2500 C  CG    . PRO A 1 346  ? 98.831  87.126  137.203 1.00 37.66  ? 346  PRO A CG    1 
ATOM   2501 C  CD    . PRO A 1 346  ? 99.354  86.783  135.839 1.00 37.66  ? 346  PRO A CD    1 
ATOM   2502 N  N     . THR A 1 347  ? 101.982 86.221  139.554 1.00 45.59  ? 347  THR A N     1 
ATOM   2503 C  CA    . THR A 1 347  ? 102.384 85.220  140.531 1.00 45.59  ? 347  THR A CA    1 
ATOM   2504 C  C     . THR A 1 347  ? 101.113 84.562  141.077 1.00 45.59  ? 347  THR A C     1 
ATOM   2505 O  O     . THR A 1 347  ? 100.014 84.761  140.552 1.00 45.59  ? 347  THR A O     1 
ATOM   2506 C  CB    . THR A 1 347  ? 103.256 85.872  141.605 1.00 45.59  ? 347  THR A CB    1 
ATOM   2507 O  OG1   . THR A 1 347  ? 104.203 86.739  140.971 1.00 45.59  ? 347  THR A OG1   1 
ATOM   2508 C  CG2   . THR A 1 347  ? 104.051 84.826  142.383 1.00 45.59  ? 347  THR A CG2   1 
ATOM   2509 N  N     . ILE A 1 348  ? 101.244 83.757  142.133 1.00 55.59  ? 348  ILE A N     1 
ATOM   2510 C  CA    . ILE A 1 348  ? 100.095 83.037  142.664 1.00 55.59  ? 348  ILE A CA    1 
ATOM   2511 C  C     . ILE A 1 348  ? 99.052  84.012  143.193 1.00 55.59  ? 348  ILE A C     1 
ATOM   2512 O  O     . ILE A 1 348  ? 99.375  85.019  143.838 1.00 55.59  ? 348  ILE A O     1 
ATOM   2513 C  CB    . ILE A 1 348  ? 100.539 82.057  143.762 1.00 55.59  ? 348  ILE A CB    1 
ATOM   2514 C  CG1   . ILE A 1 348  ? 101.255 82.807  144.889 1.00 55.59  ? 348  ILE A CG1   1 
ATOM   2515 C  CG2   . ILE A 1 348  ? 101.438 80.977  143.180 1.00 55.59  ? 348  ILE A CG2   1 
ATOM   2516 C  CD1   . ILE A 1 348  ? 101.314 82.047  146.189 1.00 55.59  ? 348  ILE A CD1   1 
ATOM   2517 N  N     . ILE A 1 349  ? 97.788  83.726  142.892 1.00 63.48  ? 349  ILE A N     1 
ATOM   2518 C  CA    . ILE A 1 349  ? 96.668  84.408  143.527 1.00 63.48  ? 349  ILE A CA    1 
ATOM   2519 C  C     . ILE A 1 349  ? 95.774  83.360  144.185 1.00 63.48  ? 349  ILE A C     1 
ATOM   2520 O  O     . ILE A 1 349  ? 95.609  83.359  145.410 1.00 63.48  ? 349  ILE A O     1 
ATOM   2521 C  CB    . ILE A 1 349  ? 95.911  85.296  142.518 1.00 63.48  ? 349  ILE A CB    1 
ATOM   2522 C  CG1   . ILE A 1 349  ? 95.603  84.538  141.221 1.00 63.48  ? 349  ILE A CG1   1 
ATOM   2523 C  CG2   . ILE A 1 349  ? 96.723  86.541  142.202 1.00 63.48  ? 349  ILE A CG2   1 
ATOM   2524 C  CD1   . ILE A 1 349  ? 94.680  85.280  140.279 1.00 63.48  ? 349  ILE A CD1   1 
ATOM   2525 N  N     . GLN A 1 350  ? 95.201  82.460  143.376 1.00 72.26  ? 350  GLN A N     1 
ATOM   2526 C  CA    . GLN A 1 350  ? 94.575  81.211  143.833 1.00 72.26  ? 350  GLN A CA    1 
ATOM   2527 C  C     . GLN A 1 350  ? 93.603  81.447  144.995 1.00 72.26  ? 350  GLN A C     1 
ATOM   2528 O  O     . GLN A 1 350  ? 93.238  80.529  145.729 1.00 72.26  ? 350  GLN A O     1 
ATOM   2529 C  CB    . GLN A 1 350  ? 95.673  80.189  144.184 1.00 72.26  ? 350  GLN A CB    1 
ATOM   2530 C  CG    . GLN A 1 350  ? 95.274  78.718  144.429 1.00 72.26  ? 350  GLN A CG    1 
ATOM   2531 C  CD    . GLN A 1 350  ? 94.905  78.410  145.869 1.00 72.26  ? 350  GLN A CD    1 
ATOM   2532 O  OE1   . GLN A 1 350  ? 95.416  79.031  146.800 1.00 72.26  ? 350  GLN A OE1   1 
ATOM   2533 N  NE2   . GLN A 1 350  ? 94.010  77.446  146.057 1.00 72.26  ? 350  GLN A NE2   1 
ATOM   2534 N  N     . ASP A 1 351  ? 93.123  82.674  145.154 1.00 74.81  ? 351  ASP A N     1 
ATOM   2535 C  CA    . ASP A 1 351  ? 92.421  82.940  146.403 1.00 74.81  ? 351  ASP A CA    1 
ATOM   2536 C  C     . ASP A 1 351  ? 90.984  82.408  146.506 1.00 74.81  ? 351  ASP A C     1 
ATOM   2537 O  O     . ASP A 1 351  ? 90.591  82.019  147.612 1.00 74.81  ? 351  ASP A O     1 
ATOM   2538 C  CB    . ASP A 1 351  ? 92.505  84.441  146.750 1.00 74.81  ? 351  ASP A CB    1 
ATOM   2539 C  CG    . ASP A 1 351  ? 91.885  85.363  145.709 1.00 74.81  ? 351  ASP A CG    1 
ATOM   2540 O  OD1   . ASP A 1 351  ? 91.426  84.910  144.652 1.00 74.81  ? 351  ASP A OD1   1 
ATOM   2541 O  OD2   . ASP A 1 351  ? 91.859  86.586  145.965 1.00 74.81  ? 351  ASP A OD2   1 
ATOM   2542 N  N     . PRO A 1 352  ? 90.144  82.346  145.435 1.00 87.28  ? 352  PRO A N     1 
ATOM   2543 C  CA    . PRO A 1 352  ? 88.760  81.918  145.681 1.00 87.28  ? 352  PRO A CA    1 
ATOM   2544 C  C     . PRO A 1 352  ? 88.600  80.402  145.716 1.00 87.28  ? 352  PRO A C     1 
ATOM   2545 O  O     . PRO A 1 352  ? 88.573  79.762  144.659 1.00 87.28  ? 352  PRO A O     1 
ATOM   2546 C  CB    . PRO A 1 352  ? 88.006  82.535  144.499 1.00 87.28  ? 352  PRO A CB    1 
ATOM   2547 C  CG    . PRO A 1 352  ? 89.008  82.469  143.368 1.00 87.28  ? 352  PRO A CG    1 
ATOM   2548 C  CD    . PRO A 1 352  ? 90.402  82.376  143.981 1.00 87.28  ? 352  PRO A CD    1 
ATOM   2549 N  N     . LEU A 1 353  ? 88.488  79.800  146.901 1.00 93.34  ? 353  LEU A N     1 
ATOM   2550 C  CA    . LEU A 1 353  ? 88.120  78.389  146.979 1.00 93.34  ? 353  LEU A CA    1 
ATOM   2551 C  C     . LEU A 1 353  ? 86.831  78.166  147.759 1.00 93.34  ? 353  LEU A C     1 
ATOM   2552 O  O     . LEU A 1 353  ? 85.859  77.653  147.194 1.00 93.34  ? 353  LEU A O     1 
ATOM   2553 C  CB    . LEU A 1 353  ? 89.270  77.577  147.591 1.00 93.34  ? 353  LEU A CB    1 
ATOM   2554 C  CG    . LEU A 1 353  ? 89.094  76.058  147.616 1.00 93.34  ? 353  LEU A CG    1 
ATOM   2555 C  CD1   . LEU A 1 353  ? 89.387  75.461  146.249 1.00 93.34  ? 353  LEU A CD1   1 
ATOM   2556 C  CD2   . LEU A 1 353  ? 89.988  75.436  148.677 1.00 93.34  ? 353  LEU A CD2   1 
ATOM   2557 N  N     . ASP A 1 354  ? 86.786  78.535  149.040 1.00 96.28  ? 354  ASP A N     1 
ATOM   2558 C  CA    . ASP A 1 354  ? 85.562  78.413  149.823 1.00 96.28  ? 354  ASP A CA    1 
ATOM   2559 C  C     . ASP A 1 354  ? 85.162  79.746  150.445 1.00 96.28  ? 354  ASP A C     1 
ATOM   2560 O  O     . ASP A 1 354  ? 84.003  80.163  150.353 1.00 96.28  ? 354  ASP A O     1 
ATOM   2561 C  CB    . ASP A 1 354  ? 85.717  77.335  150.903 1.00 96.28  ? 354  ASP A CB    1 
ATOM   2562 C  CG    . ASP A 1 354  ? 86.977  77.504  151.735 1.00 96.28  ? 354  ASP A CG    1 
ATOM   2563 O  OD1   . ASP A 1 354  ? 87.471  78.642  151.864 1.00 96.28  ? 354  ASP A OD1   1 
ATOM   2564 O  OD2   . ASP A 1 354  ? 87.476  76.488  152.263 1.00 96.28  ? 354  ASP A OD2   1 
ATOM   2565 N  N     . GLY A 1 355  ? 86.120  80.416  151.081 1.00 90.01  ? 355  GLY A N     1 
ATOM   2566 C  CA    . GLY A 1 355  ? 85.853  81.654  151.785 1.00 90.01  ? 355  GLY A CA    1 
ATOM   2567 C  C     . GLY A 1 355  ? 85.893  82.871  150.887 1.00 90.01  ? 355  GLY A C     1 
ATOM   2568 O  O     . GLY A 1 355  ? 86.771  83.727  151.028 1.00 90.01  ? 355  GLY A O     1 
ATOM   2569 N  N     . LYS A 1 356  ? 84.945  82.950  149.951 1.00 81.83  ? 356  LYS A N     1 
ATOM   2570 C  CA    . LYS A 1 356  ? 84.890  84.095  149.049 1.00 81.83  ? 356  LYS A CA    1 
ATOM   2571 C  C     . LYS A 1 356  ? 84.649  85.389  149.815 1.00 81.83  ? 356  LYS A C     1 
ATOM   2572 O  O     . LYS A 1 356  ? 85.300  86.407  149.552 1.00 81.83  ? 356  LYS A O     1 
ATOM   2573 C  CB    . LYS A 1 356  ? 83.800  83.878  147.998 1.00 81.83  ? 356  LYS A CB    1 
ATOM   2574 C  CG    . LYS A 1 356  ? 83.676  84.995  146.974 1.00 81.83  ? 356  LYS A CG    1 
ATOM   2575 C  CD    . LYS A 1 356  ? 82.511  85.920  147.296 1.00 81.83  ? 356  LYS A CD    1 
ATOM   2576 C  CE    . LYS A 1 356  ? 81.182  85.193  147.186 1.00 81.83  ? 356  LYS A CE    1 
ATOM   2577 N  NZ    . LYS A 1 356  ? 80.040  86.079  147.543 1.00 81.83  ? 356  LYS A NZ    1 
ATOM   2578 N  N     . CYS A 1 357  ? 83.721  85.369  150.771 1.00 79.77  ? 357  CYS A N     1 
ATOM   2579 C  CA    . CYS A 1 357  ? 83.403  86.559  151.557 1.00 79.77  ? 357  CYS A CA    1 
ATOM   2580 C  C     . CYS A 1 357  ? 82.842  86.090  152.895 1.00 79.77  ? 357  CYS A C     1 
ATOM   2581 O  O     . CYS A 1 357  ? 81.678  85.686  152.975 1.00 79.77  ? 357  CYS A O     1 
ATOM   2582 C  CB    . CYS A 1 357  ? 82.418  87.458  150.820 1.00 79.77  ? 357  CYS A CB    1 
ATOM   2583 S  SG    . CYS A 1 357  ? 81.982  88.973  151.703 1.00 79.77  ? 357  CYS A SG    1 
ATOM   2584 N  N     . LEU A 1 358  ? 83.669  86.146  153.933 1.00 79.42  ? 358  LEU A N     1 
ATOM   2585 C  CA    . LEU A 1 358  ? 83.262  85.765  155.278 1.00 79.42  ? 358  LEU A CA    1 
ATOM   2586 C  C     . LEU A 1 358  ? 82.858  87.012  156.054 1.00 79.42  ? 358  LEU A C     1 
ATOM   2587 O  O     . LEU A 1 358  ? 83.588  88.009  156.066 1.00 79.42  ? 358  LEU A O     1 
ATOM   2588 C  CB    . LEU A 1 358  ? 84.381  85.009  156.002 1.00 79.42  ? 358  LEU A CB    1 
ATOM   2589 C  CG    . LEU A 1 358  ? 85.637  85.727  156.508 1.00 79.42  ? 358  LEU A CG    1 
ATOM   2590 C  CD1   . LEU A 1 358  ? 86.380  84.850  157.501 1.00 79.42  ? 358  LEU A CD1   1 
ATOM   2591 C  CD2   . LEU A 1 358  ? 86.555  86.120  155.364 1.00 79.42  ? 358  LEU A CD2   1 
ATOM   2592 N  N     . ASP A 1 359  ? 81.684  86.962  156.676 1.00 80.51  ? 359  ASP A N     1 
ATOM   2593 C  CA    . ASP A 1 359  ? 81.168  88.077  157.456 1.00 80.51  ? 359  ASP A CA    1 
ATOM   2594 C  C     . ASP A 1 359  ? 81.573  88.008  158.921 1.00 80.51  ? 359  ASP A C     1 
ATOM   2595 O  O     . ASP A 1 359  ? 81.236  88.917  159.686 1.00 80.51  ? 359  ASP A O     1 
ATOM   2596 C  CB    . ASP A 1 359  ? 79.641  88.135  157.348 1.00 80.51  ? 359  ASP A CB    1 
ATOM   2597 C  CG    . ASP A 1 359  ? 79.095  89.530  157.568 1.00 80.51  ? 359  ASP A CG    1 
ATOM   2598 O  OD1   . ASP A 1 359  ? 79.872  90.499  157.439 1.00 80.51  ? 359  ASP A OD1   1 
ATOM   2599 O  OD2   . ASP A 1 359  ? 77.891  89.659  157.871 1.00 80.51  ? 359  ASP A OD2   1 
ATOM   2600 N  N     . GLN A 1 360  ? 82.288  86.959  159.327 1.00 80.67  ? 360  GLN A N     1 
ATOM   2601 C  CA    . GLN A 1 360  ? 82.722  86.783  160.706 1.00 80.67  ? 360  GLN A CA    1 
ATOM   2602 C  C     . GLN A 1 360  ? 84.153  87.262  160.925 1.00 80.67  ? 360  GLN A C     1 
ATOM   2603 O  O     . GLN A 1 360  ? 84.881  86.688  161.742 1.00 80.67  ? 360  GLN A O     1 
ATOM   2604 C  CB    . GLN A 1 360  ? 82.582  85.319  161.121 1.00 80.67  ? 360  GLN A CB    1 
ATOM   2605 C  CG    . GLN A 1 360  ? 81.148  84.826  161.175 1.00 80.67  ? 360  GLN A CG    1 
ATOM   2606 C  CD    . GLN A 1 360  ? 80.311  85.584  162.185 1.00 80.67  ? 360  GLN A CD    1 
ATOM   2607 O  OE1   . GLN A 1 360  ? 79.456  86.391  161.821 1.00 80.67  ? 360  GLN A OE1   1 
ATOM   2608 N  NE2   . GLN A 1 360  ? 80.555  85.329  163.465 1.00 80.67  ? 360  GLN A NE2   1 
ATOM   2609 N  N     . VAL A 1 361  ? 84.573  88.302  160.205 1.00 71.59  ? 361  VAL A N     1 
ATOM   2610 C  CA    . VAL A 1 361  ? 85.938  88.793  160.331 1.00 71.59  ? 361  VAL A CA    1 
ATOM   2611 C  C     . VAL A 1 361  ? 86.123  89.447  161.695 1.00 71.59  ? 361  VAL A C     1 
ATOM   2612 O  O     . VAL A 1 361  ? 85.315  90.283  162.123 1.00 71.59  ? 361  VAL A O     1 
ATOM   2613 C  CB    . VAL A 1 361  ? 86.277  89.753  159.179 1.00 71.59  ? 361  VAL A CB    1 
ATOM   2614 C  CG1   . VAL A 1 361  ? 85.376  90.981  159.196 1.00 71.59  ? 361  VAL A CG1   1 
ATOM   2615 C  CG2   . VAL A 1 361  ? 87.739  90.162  159.244 1.00 71.59  ? 361  VAL A CG2   1 
ATOM   2616 N  N     . HIS A 1 362  ? 87.171  89.032  162.405 1.00 70.44  ? 362  HIS A N     1 
ATOM   2617 C  CA    . HIS A 1 362  ? 87.510  89.625  163.690 1.00 70.44  ? 362  HIS A CA    1 
ATOM   2618 C  C     . HIS A 1 362  ? 89.008  89.797  163.893 1.00 70.44  ? 362  HIS A C     1 
ATOM   2619 O  O     . HIS A 1 362  ? 89.415  90.259  164.963 1.00 70.44  ? 362  HIS A O     1 
ATOM   2620 C  CB    . HIS A 1 362  ? 86.943  88.778  164.841 1.00 70.44  ? 362  HIS A CB    1 
ATOM   2621 C  CG    . HIS A 1 362  ? 85.448  88.712  164.866 1.00 70.44  ? 362  HIS A CG    1 
ATOM   2622 N  ND1   . HIS A 1 362  ? 84.738  87.710  164.241 1.00 70.44  ? 362  HIS A ND1   1 
ATOM   2623 C  CD2   . HIS A 1 362  ? 84.529  89.522  165.443 1.00 70.44  ? 362  HIS A CD2   1 
ATOM   2624 C  CE1   . HIS A 1 362  ? 83.445  87.906  164.431 1.00 70.44  ? 362  HIS A CE1   1 
ATOM   2625 N  NE2   . HIS A 1 362  ? 83.292  88.998  165.157 1.00 70.44  ? 362  HIS A NE2   1 
ATOM   2626 N  N     . GLY A 1 363  ? 89.829  89.459  162.918 1.00 64.24  ? 363  GLY A N     1 
ATOM   2627 C  CA    . GLY A 1 363  ? 91.281  89.460  163.101 1.00 64.24  ? 363  GLY A CA    1 
ATOM   2628 C  C     . GLY A 1 363  ? 91.802  88.066  163.459 1.00 64.24  ? 363  GLY A C     1 
ATOM   2629 O  O     . GLY A 1 363  ? 91.659  87.135  162.672 1.00 64.24  ? 363  GLY A O     1 
ATOM   2630 N  N     . ASN A 1 364  ? 92.391  87.945  164.647 1.00 63.17  ? 364  ASN A N     1 
ATOM   2631 C  CA    . ASN A 1 364  ? 92.912  86.678  165.158 1.00 63.17  ? 364  ASN A CA    1 
ATOM   2632 C  C     . ASN A 1 364  ? 93.866  86.031  164.153 1.00 63.17  ? 364  ASN A C     1 
ATOM   2633 O  O     . ASN A 1 364  ? 93.619  84.950  163.616 1.00 63.17  ? 364  ASN A O     1 
ATOM   2634 C  CB    . ASN A 1 364  ? 91.772  85.729  165.534 1.00 63.17  ? 364  ASN A CB    1 
ATOM   2635 C  CG    . ASN A 1 364  ? 91.231  85.991  166.925 1.00 63.17  ? 364  ASN A CG    1 
ATOM   2636 O  OD1   . ASN A 1 364  ? 91.428  87.067  167.487 1.00 63.17  ? 364  ASN A OD1   1 
ATOM   2637 N  ND2   . ASN A 1 364  ? 90.543  85.005  167.488 1.00 63.17  ? 364  ASN A ND2   1 
ATOM   2638 N  N     . ILE A 1 365  ? 94.972  86.728  163.901 1.00 58.47  ? 365  ILE A N     1 
ATOM   2639 C  CA    . ILE A 1 365  ? 95.985  86.230  162.978 1.00 58.47  ? 365  ILE A CA    1 
ATOM   2640 C  C     . ILE A 1 365  ? 96.726  85.074  163.636 1.00 58.47  ? 365  ILE A C     1 
ATOM   2641 O  O     . ILE A 1 365  ? 97.315  85.226  164.712 1.00 58.47  ? 365  ILE A O     1 
ATOM   2642 C  CB    . ILE A 1 365  ? 96.951  87.350  162.572 1.00 58.47  ? 365  ILE A CB    1 
ATOM   2643 C  CG1   . ILE A 1 365  ? 96.265  88.334  161.625 1.00 58.47  ? 365  ILE A CG1   1 
ATOM   2644 C  CG2   . ILE A 1 365  ? 98.188  86.770  161.914 1.00 58.47  ? 365  ILE A CG2   1 
ATOM   2645 C  CD1   . ILE A 1 365  ? 95.799  87.703  160.339 1.00 58.47  ? 365  ILE A CD1   1 
ATOM   2646 N  N     . GLU A 1 366  ? 96.700  83.911  162.991 1.00 59.15  ? 366  GLU A N     1 
ATOM   2647 C  CA    . GLU A 1 366  ? 97.383  82.723  163.481 1.00 59.15  ? 366  GLU A CA    1 
ATOM   2648 C  C     . GLU A 1 366  ? 98.600  82.432  162.614 1.00 59.15  ? 366  GLU A C     1 
ATOM   2649 O  O     . GLU A 1 366  ? 98.485  82.326  161.390 1.00 59.15  ? 366  GLU A O     1 
ATOM   2650 C  CB    . GLU A 1 366  ? 96.450  81.505  163.473 1.00 59.15  ? 366  GLU A CB    1 
ATOM   2651 C  CG    . GLU A 1 366  ? 95.282  81.499  164.476 1.00 59.15  ? 366  GLU A CG    1 
ATOM   2652 C  CD    . GLU A 1 366  ? 95.628  81.929  165.901 1.00 59.15  ? 366  GLU A CD    1 
ATOM   2653 O  OE1   . GLU A 1 366  ? 94.677  82.129  166.684 1.00 59.15  ? 366  GLU A OE1   1 
ATOM   2654 O  OE2   . GLU A 1 366  ? 96.819  82.014  166.269 1.00 59.15  ? 366  GLU A OE2   1 
ATOM   2655 N  N     . PHE A 1 367  ? 99.759  82.295  163.255 1.00 51.29  ? 367  PHE A N     1 
ATOM   2656 C  CA    . PHE A 1 367  ? 100.999 81.914  162.589 1.00 51.29  ? 367  PHE A CA    1 
ATOM   2657 C  C     . PHE A 1 367  ? 101.448 80.572  163.149 1.00 51.29  ? 367  PHE A C     1 
ATOM   2658 O  O     . PHE A 1 367  ? 101.595 80.425  164.367 1.00 51.29  ? 367  PHE A O     1 
ATOM   2659 C  CB    . PHE A 1 367  ? 102.083 82.973  162.794 1.00 51.29  ? 367  PHE A CB    1 
ATOM   2660 C  CG    . PHE A 1 367  ? 102.190 83.961  161.668 1.00 51.29  ? 367  PHE A CG    1 
ATOM   2661 C  CD1   . PHE A 1 367  ? 101.197 84.901  161.456 1.00 51.29  ? 367  PHE A CD1   1 
ATOM   2662 C  CD2   . PHE A 1 367  ? 103.289 83.957  160.827 1.00 51.29  ? 367  PHE A CD2   1 
ATOM   2663 C  CE1   . PHE A 1 367  ? 101.295 85.813  160.421 1.00 51.29  ? 367  PHE A CE1   1 
ATOM   2664 C  CE2   . PHE A 1 367  ? 103.392 84.868  159.793 1.00 51.29  ? 367  PHE A CE2   1 
ATOM   2665 C  CZ    . PHE A 1 367  ? 102.394 85.796  159.590 1.00 51.29  ? 367  PHE A CZ    1 
ATOM   2666 N  N     . LYS A 1 368  ? 101.665 79.599  162.267 1.00 53.33  ? 368  LYS A N     1 
ATOM   2667 C  CA    . LYS A 1 368  ? 102.018 78.243  162.672 1.00 53.33  ? 368  LYS A CA    1 
ATOM   2668 C  C     . LYS A 1 368  ? 103.158 77.734  161.805 1.00 53.33  ? 368  LYS A C     1 
ATOM   2669 O  O     . LYS A 1 368  ? 103.004 77.626  160.584 1.00 53.33  ? 368  LYS A O     1 
ATOM   2670 C  CB    . LYS A 1 368  ? 100.811 77.306  162.566 1.00 53.33  ? 368  LYS A CB    1 
ATOM   2671 C  CG    . LYS A 1 368  ? 99.718  77.577  163.583 1.00 53.33  ? 368  LYS A CG    1 
ATOM   2672 C  CD    . LYS A 1 368  ? 98.505  76.703  163.319 1.00 53.33  ? 368  LYS A CD    1 
ATOM   2673 C  CE    . LYS A 1 368  ? 98.795  75.249  163.650 1.00 53.33  ? 368  LYS A CE    1 
ATOM   2674 N  NZ    . LYS A 1 368  ? 97.584  74.396  163.506 1.00 53.33  ? 368  LYS A NZ    1 
ATOM   2675 N  N     . ASP A 1 369  ? 104.286 77.415  162.444 1.00 54.80  ? 369  ASP A N     1 
ATOM   2676 C  CA    . ASP A 1 369  ? 105.472 76.818  161.813 1.00 54.80  ? 369  ASP A CA    1 
ATOM   2677 C  C     . ASP A 1 369  ? 105.744 77.396  160.425 1.00 54.80  ? 369  ASP A C     1 
ATOM   2678 O  O     . ASP A 1 369  ? 105.985 76.679  159.452 1.00 54.80  ? 369  ASP A O     1 
ATOM   2679 C  CB    . ASP A 1 369  ? 105.365 75.288  161.771 1.00 54.80  ? 369  ASP A CB    1 
ATOM   2680 C  CG    . ASP A 1 369  ? 104.089 74.790  161.107 1.00 54.80  ? 369  ASP A CG    1 
ATOM   2681 O  OD1   . ASP A 1 369  ? 103.826 75.145  159.940 1.00 54.80  ? 369  ASP A OD1   1 
ATOM   2682 O  OD2   . ASP A 1 369  ? 103.344 74.032  161.762 1.00 54.80  ? 369  ASP A OD2   1 
ATOM   2683 N  N     . VAL A 1 370  ? 105.727 78.722  160.347 1.00 50.10  ? 370  VAL A N     1 
ATOM   2684 C  CA    . VAL A 1 370  ? 105.899 79.428  159.084 1.00 50.10  ? 370  VAL A CA    1 
ATOM   2685 C  C     . VAL A 1 370  ? 107.372 79.771  158.907 1.00 50.10  ? 370  VAL A C     1 
ATOM   2686 O  O     . VAL A 1 370  ? 107.962 80.463  159.743 1.00 50.10  ? 370  VAL A O     1 
ATOM   2687 C  CB    . VAL A 1 370  ? 105.030 80.692  159.033 1.00 50.10  ? 370  VAL A CB    1 
ATOM   2688 C  CG1   . VAL A 1 370  ? 105.486 81.603  157.908 1.00 50.10  ? 370  VAL A CG1   1 
ATOM   2689 C  CG2   . VAL A 1 370  ? 103.573 80.317  158.858 1.00 50.10  ? 370  VAL A CG2   1 
ATOM   2690 N  N     . THR A 1 371  ? 107.964 79.284  157.823 1.00 47.28  ? 371  THR A N     1 
ATOM   2691 C  CA    . THR A 1 371  ? 109.314 79.643  157.423 1.00 47.28  ? 371  THR A CA    1 
ATOM   2692 C  C     . THR A 1 371  ? 109.250 80.565  156.214 1.00 47.28  ? 371  THR A C     1 
ATOM   2693 O  O     . THR A 1 371  ? 108.245 80.615  155.500 1.00 47.28  ? 371  THR A O     1 
ATOM   2694 C  CB    . THR A 1 371  ? 110.145 78.399  157.093 1.00 47.28  ? 371  THR A CB    1 
ATOM   2695 O  OG1   . THR A 1 371  ? 109.610 77.760  155.928 1.00 47.28  ? 371  THR A OG1   1 
ATOM   2696 C  CG2   . THR A 1 371  ? 110.118 77.420  158.255 1.00 47.28  ? 371  THR A CG2   1 
ATOM   2697 N  N     . PHE A 1 372  ? 110.332 81.307  155.988 1.00 40.92  ? 372  PHE A N     1 
ATOM   2698 C  CA    . PHE A 1 372  ? 110.339 82.270  154.895 1.00 40.92  ? 372  PHE A CA    1 
ATOM   2699 C  C     . PHE A 1 372  ? 111.769 82.588  154.490 1.00 40.92  ? 372  PHE A C     1 
ATOM   2700 O  O     . PHE A 1 372  ? 112.622 82.830  155.349 1.00 40.92  ? 372  PHE A O     1 
ATOM   2701 C  CB    . PHE A 1 372  ? 109.605 83.552  155.296 1.00 40.92  ? 372  PHE A CB    1 
ATOM   2702 C  CG    . PHE A 1 372  ? 109.515 84.563  154.196 1.00 40.92  ? 372  PHE A CG    1 
ATOM   2703 C  CD1   . PHE A 1 372  ? 109.107 84.189  152.928 1.00 40.92  ? 372  PHE A CD1   1 
ATOM   2704 C  CD2   . PHE A 1 372  ? 109.838 85.887  154.428 1.00 40.92  ? 372  PHE A CD2   1 
ATOM   2705 C  CE1   . PHE A 1 372  ? 109.024 85.115  151.914 1.00 40.92  ? 372  PHE A CE1   1 
ATOM   2706 C  CE2   . PHE A 1 372  ? 109.757 86.819  153.418 1.00 40.92  ? 372  PHE A CE2   1 
ATOM   2707 C  CZ    . PHE A 1 372  ? 109.350 86.432  152.159 1.00 40.92  ? 372  PHE A CZ    1 
ATOM   2708 N  N     . SER A 1 373  ? 112.020 82.592  153.182 1.00 41.87  ? 373  SER A N     1 
ATOM   2709 C  CA    . SER A 1 373  ? 113.296 83.011  152.620 1.00 41.87  ? 373  SER A CA    1 
ATOM   2710 C  C     . SER A 1 373  ? 113.022 83.923  151.436 1.00 41.87  ? 373  SER A C     1 
ATOM   2711 O  O     . SER A 1 373  ? 112.226 83.578  150.558 1.00 41.87  ? 373  SER A O     1 
ATOM   2712 C  CB    . SER A 1 373  ? 114.137 81.808  152.181 1.00 41.87  ? 373  SER A CB    1 
ATOM   2713 O  OG    . SER A 1 373  ? 113.445 81.030  151.222 1.00 41.87  ? 373  SER A OG    1 
ATOM   2714 N  N     . TYR A 1 374  ? 113.678 85.079  151.415 1.00 42.32  ? 374  TYR A N     1 
ATOM   2715 C  CA    . TYR A 1 374  ? 113.429 86.054  150.367 1.00 42.32  ? 374  TYR A CA    1 
ATOM   2716 C  C     . TYR A 1 374  ? 113.960 85.552  149.025 1.00 42.32  ? 374  TYR A C     1 
ATOM   2717 O  O     . TYR A 1 374  ? 114.959 84.831  148.973 1.00 42.32  ? 374  TYR A O     1 
ATOM   2718 C  CB    . TYR A 1 374  ? 114.076 87.388  150.719 1.00 42.32  ? 374  TYR A CB    1 
ATOM   2719 C  CG    . TYR A 1 374  ? 113.204 88.272  151.577 1.00 42.32  ? 374  TYR A CG    1 
ATOM   2720 C  CD1   . TYR A 1 374  ? 112.071 88.876  151.055 1.00 42.32  ? 374  TYR A CD1   1 
ATOM   2721 C  CD2   . TYR A 1 374  ? 113.508 88.496  152.910 1.00 42.32  ? 374  TYR A CD2   1 
ATOM   2722 C  CE1   . TYR A 1 374  ? 111.269 89.683  151.835 1.00 42.32  ? 374  TYR A CE1   1 
ATOM   2723 C  CE2   . TYR A 1 374  ? 112.712 89.301  153.698 1.00 42.32  ? 374  TYR A CE2   1 
ATOM   2724 C  CZ    . TYR A 1 374  ? 111.594 89.891  153.155 1.00 42.32  ? 374  TYR A CZ    1 
ATOM   2725 O  OH    . TYR A 1 374  ? 110.798 90.694  153.935 1.00 42.32  ? 374  TYR A OH    1 
ATOM   2726 N  N     . PRO A 1 375  ? 113.297 85.911  147.923 1.00 37.99  ? 375  PRO A N     1 
ATOM   2727 C  CA    . PRO A 1 375  ? 113.784 85.478  146.603 1.00 37.99  ? 375  PRO A CA    1 
ATOM   2728 C  C     . PRO A 1 375  ? 115.182 85.971  146.277 1.00 37.99  ? 375  PRO A C     1 
ATOM   2729 O  O     . PRO A 1 375  ? 115.932 85.265  145.591 1.00 37.99  ? 375  PRO A O     1 
ATOM   2730 C  CB    . PRO A 1 375  ? 112.743 86.061  145.638 1.00 37.99  ? 375  PRO A CB    1 
ATOM   2731 C  CG    . PRO A 1 375  ? 111.529 86.287  146.472 1.00 37.99  ? 375  PRO A CG    1 
ATOM   2732 C  CD    . PRO A 1 375  ? 112.030 86.654  147.830 1.00 37.99  ? 375  PRO A CD    1 
ATOM   2733 N  N     . SER A 1 376  ? 115.554 87.167  146.739 1.00 42.46  ? 376  SER A N     1 
ATOM   2734 C  CA    . SER A 1 376  ? 116.880 87.696  146.436 1.00 42.46  ? 376  SER A CA    1 
ATOM   2735 C  C     . SER A 1 376  ? 117.978 86.856  147.078 1.00 42.46  ? 376  SER A C     1 
ATOM   2736 O  O     . SER A 1 376  ? 119.011 86.594  146.452 1.00 42.46  ? 376  SER A O     1 
ATOM   2737 C  CB    . SER A 1 376  ? 116.982 89.150  146.891 1.00 42.46  ? 376  SER A CB    1 
ATOM   2738 O  OG    . SER A 1 376  ? 118.288 89.656  146.681 1.00 42.46  ? 376  SER A OG    1 
ATOM   2739 N  N     . ARG A 1 377  ? 117.776 86.426  148.321 1.00 39.92  ? 377  ARG A N     1 
ATOM   2740 C  CA    . ARG A 1 377  ? 118.749 85.617  149.056 1.00 39.92  ? 377  ARG A CA    1 
ATOM   2741 C  C     . ARG A 1 377  ? 118.050 84.376  149.594 1.00 39.92  ? 377  ARG A C     1 
ATOM   2742 O  O     . ARG A 1 377  ? 117.775 84.270  150.795 1.00 39.92  ? 377  ARG A O     1 
ATOM   2743 C  CB    . ARG A 1 377  ? 119.391 86.420  150.187 1.00 39.92  ? 377  ARG A CB    1 
ATOM   2744 C  CG    . ARG A 1 377  ? 120.530 87.322  149.745 1.00 39.92  ? 377  ARG A CG    1 
ATOM   2745 C  CD    . ARG A 1 377  ? 120.021 88.690  149.322 1.00 39.92  ? 377  ARG A CD    1 
ATOM   2746 N  NE    . ARG A 1 377  ? 119.277 89.353  150.388 1.00 39.92  ? 377  ARG A NE    1 
ATOM   2747 C  CZ    . ARG A 1 377  ? 119.834 90.093  151.340 1.00 39.92  ? 377  ARG A CZ    1 
ATOM   2748 N  NH1   . ARG A 1 377  ? 119.078 90.658  152.270 1.00 39.92  ? 377  ARG A NH1   1 
ATOM   2749 N  NH2   . ARG A 1 377  ? 121.147 90.270  151.363 1.00 39.92  ? 377  ARG A NH2   1 
ATOM   2750 N  N     . PRO A 1 378  ? 117.749 83.409  148.724 1.00 42.63  ? 378  PRO A N     1 
ATOM   2751 C  CA    . PRO A 1 378  ? 117.001 82.223  149.172 1.00 42.63  ? 378  PRO A CA    1 
ATOM   2752 C  C     . PRO A 1 378  ? 117.750 81.363  150.175 1.00 42.63  ? 378  PRO A C     1 
ATOM   2753 O  O     . PRO A 1 378  ? 117.112 80.580  150.889 1.00 42.63  ? 378  PRO A O     1 
ATOM   2754 C  CB    . PRO A 1 378  ? 116.739 81.461  147.867 1.00 42.63  ? 378  PRO A CB    1 
ATOM   2755 C  CG    . PRO A 1 378  ? 117.835 81.896  146.956 1.00 42.63  ? 378  PRO A CG    1 
ATOM   2756 C  CD    . PRO A 1 378  ? 118.117 83.329  147.300 1.00 42.63  ? 378  PRO A CD    1 
ATOM   2757 N  N     . ASP A 1 379  ? 119.078 81.472  150.250 1.00 44.16  ? 379  ASP A N     1 
ATOM   2758 C  CA    . ASP A 1 379  ? 119.827 80.638  151.184 1.00 44.16  ? 379  ASP A CA    1 
ATOM   2759 C  C     . ASP A 1 379  ? 119.617 81.068  152.631 1.00 44.16  ? 379  ASP A C     1 
ATOM   2760 O  O     . ASP A 1 379  ? 119.568 80.218  153.526 1.00 44.16  ? 379  ASP A O     1 
ATOM   2761 C  CB    . ASP A 1 379  ? 121.314 80.651  150.825 1.00 44.16  ? 379  ASP A CB    1 
ATOM   2762 C  CG    . ASP A 1 379  ? 121.934 82.033  150.927 1.00 44.16  ? 379  ASP A CG    1 
ATOM   2763 O  OD1   . ASP A 1 379  ? 123.163 82.146  150.737 1.00 44.16  ? 379  ASP A OD1   1 
ATOM   2764 O  OD2   . ASP A 1 379  ? 121.196 83.011  151.172 1.00 44.16  ? 379  ASP A OD2   1 
ATOM   2765 N  N     . VAL A 1 380  ? 119.492 82.368  152.882 1.00 43.30  ? 380  VAL A N     1 
ATOM   2766 C  CA    . VAL A 1 380  ? 119.305 82.868  154.239 1.00 43.30  ? 380  VAL A CA    1 
ATOM   2767 C  C     . VAL A 1 380  ? 117.872 82.601  154.677 1.00 43.30  ? 380  VAL A C     1 
ATOM   2768 O  O     . VAL A 1 380  ? 116.919 82.935  153.964 1.00 43.30  ? 380  VAL A O     1 
ATOM   2769 C  CB    . VAL A 1 380  ? 119.641 84.365  154.319 1.00 43.30  ? 380  VAL A CB    1 
ATOM   2770 C  CG1   . VAL A 1 380  ? 119.301 84.912  155.695 1.00 43.30  ? 380  VAL A CG1   1 
ATOM   2771 C  CG2   . VAL A 1 380  ? 121.110 84.594  154.006 1.00 43.30  ? 380  VAL A CG2   1 
ATOM   2772 N  N     . MET A 1 381  ? 117.717 81.994  155.851 1.00 45.18  ? 381  MET A N     1 
ATOM   2773 C  CA    . MET A 1 381  ? 116.407 81.680  156.412 1.00 45.18  ? 381  MET A CA    1 
ATOM   2774 C  C     . MET A 1 381  ? 116.048 82.748  157.438 1.00 45.18  ? 381  MET A C     1 
ATOM   2775 O  O     . MET A 1 381  ? 116.618 82.783  158.533 1.00 45.18  ? 381  MET A O     1 
ATOM   2776 C  CB    . MET A 1 381  ? 116.405 80.289  157.042 1.00 45.18  ? 381  MET A CB    1 
ATOM   2777 C  CG    . MET A 1 381  ? 116.269 79.156  156.040 1.00 45.18  ? 381  MET A CG    1 
ATOM   2778 S  SD    . MET A 1 381  ? 114.999 79.477  154.803 1.00 45.18  ? 381  MET A SD    1 
ATOM   2779 C  CE    . MET A 1 381  ? 114.545 77.809  154.342 1.00 45.18  ? 381  MET A CE    1 
ATOM   2780 N  N     . ILE A 1 382  ? 115.105 83.620  157.079 1.00 47.42  ? 382  ILE A N     1 
ATOM   2781 C  CA    . ILE A 1 382  ? 114.685 84.676  157.995 1.00 47.42  ? 382  ILE A CA    1 
ATOM   2782 C  C     . ILE A 1 382  ? 113.896 84.093  159.161 1.00 47.42  ? 382  ILE A C     1 
ATOM   2783 O  O     . ILE A 1 382  ? 114.105 84.470  160.320 1.00 47.42  ? 382  ILE A O     1 
ATOM   2784 C  CB    . ILE A 1 382  ? 113.873 85.743  157.240 1.00 47.42  ? 382  ILE A CB    1 
ATOM   2785 C  CG1   . ILE A 1 382  ? 114.705 86.351  156.112 1.00 47.42  ? 382  ILE A CG1   1 
ATOM   2786 C  CG2   . ILE A 1 382  ? 113.414 86.832  158.191 1.00 47.42  ? 382  ILE A CG2   1 
ATOM   2787 C  CD1   . ILE A 1 382  ? 115.957 87.047  156.587 1.00 47.42  ? 382  ILE A CD1   1 
ATOM   2788 N  N     . PHE A 1 383  ? 112.985 83.165  158.879 1.00 51.43  ? 383  PHE A N     1 
ATOM   2789 C  CA    . PHE A 1 383  ? 112.112 82.580  159.886 1.00 51.43  ? 383  PHE A CA    1 
ATOM   2790 C  C     . PHE A 1 383  ? 112.305 81.071  159.930 1.00 51.43  ? 383  PHE A C     1 
ATOM   2791 O  O     . PHE A 1 383  ? 112.531 80.433  158.898 1.00 51.43  ? 383  PHE A O     1 
ATOM   2792 C  CB    . PHE A 1 383  ? 110.643 82.904  159.600 1.00 51.43  ? 383  PHE A CB    1 
ATOM   2793 C  CG    . PHE A 1 383  ? 110.234 84.287  160.015 1.00 51.43  ? 383  PHE A CG    1 
ATOM   2794 C  CD1   . PHE A 1 383  ? 111.026 85.030  160.872 1.00 51.43  ? 383  PHE A CD1   1 
ATOM   2795 C  CD2   . PHE A 1 383  ? 109.055 84.842  159.549 1.00 51.43  ? 383  PHE A CD2   1 
ATOM   2796 C  CE1   . PHE A 1 383  ? 110.650 86.302  161.255 1.00 51.43  ? 383  PHE A CE1   1 
ATOM   2797 C  CE2   . PHE A 1 383  ? 108.675 86.112  159.928 1.00 51.43  ? 383  PHE A CE2   1 
ATOM   2798 C  CZ    . PHE A 1 383  ? 109.473 86.842  160.782 1.00 51.43  ? 383  PHE A CZ    1 
ATOM   2799 N  N     . ARG A 1 384  ? 112.207 80.505  161.133 1.00 59.50  ? 384  ARG A N     1 
ATOM   2800 C  CA    . ARG A 1 384  ? 112.346 79.064  161.342 1.00 59.50  ? 384  ARG A CA    1 
ATOM   2801 C  C     . ARG A 1 384  ? 111.359 78.661  162.433 1.00 59.50  ? 384  ARG A C     1 
ATOM   2802 O  O     . ARG A 1 384  ? 111.594 78.931  163.615 1.00 59.50  ? 384  ARG A O     1 
ATOM   2803 C  CB    . ARG A 1 384  ? 113.775 78.695  161.722 1.00 59.50  ? 384  ARG A CB    1 
ATOM   2804 C  CG    . ARG A 1 384  ? 114.693 78.443  160.539 1.00 59.50  ? 384  ARG A CG    1 
ATOM   2805 C  CD    . ARG A 1 384  ? 114.382 77.118  159.866 1.00 59.50  ? 384  ARG A CD    1 
ATOM   2806 N  NE    . ARG A 1 384  ? 115.453 76.703  158.964 1.00 59.50  ? 384  ARG A NE    1 
ATOM   2807 C  CZ    . ARG A 1 384  ? 115.350 75.710  158.087 1.00 59.50  ? 384  ARG A CZ    1 
ATOM   2808 N  NH1   . ARG A 1 384  ? 114.220 75.024  157.989 1.00 59.50  ? 384  ARG A NH1   1 
ATOM   2809 N  NH2   . ARG A 1 384  ? 116.377 75.402  157.307 1.00 59.50  ? 384  ARG A NH2   1 
ATOM   2810 N  N     . ASN A 1 385  ? 110.261 78.018  162.032 1.00 57.70  ? 385  ASN A N     1 
ATOM   2811 C  CA    . ASN A 1 385  ? 109.209 77.583  162.951 1.00 57.70  ? 385  ASN A CA    1 
ATOM   2812 C  C     . ASN A 1 385  ? 108.660 78.768  163.748 1.00 57.70  ? 385  ASN A C     1 
ATOM   2813 O  O     . ASN A 1 385  ? 108.775 78.841  164.973 1.00 57.70  ? 385  ASN A O     1 
ATOM   2814 C  CB    . ASN A 1 385  ? 109.716 76.476  163.881 1.00 57.70  ? 385  ASN A CB    1 
ATOM   2815 C  CG    . ASN A 1 385  ? 109.628 75.103  163.252 1.00 57.70  ? 385  ASN A CG    1 
ATOM   2816 O  OD1   . ASN A 1 385  ? 109.401 74.971  162.050 1.00 57.70  ? 385  ASN A OD1   1 
ATOM   2817 N  ND2   . ASN A 1 385  ? 109.806 74.068  164.064 1.00 57.70  ? 385  ASN A ND2   1 
ATOM   2818 N  N     . PHE A 1 386  ? 108.055 79.704  163.023 1.00 54.61  ? 386  PHE A N     1 
ATOM   2819 C  CA    . PHE A 1 386  ? 107.563 80.944  163.607 1.00 54.61  ? 386  PHE A CA    1 
ATOM   2820 C  C     . PHE A 1 386  ? 106.110 80.772  164.037 1.00 54.61  ? 386  PHE A C     1 
ATOM   2821 O  O     . PHE A 1 386  ? 105.257 80.401  163.224 1.00 54.61  ? 386  PHE A O     1 
ATOM   2822 C  CB    . PHE A 1 386  ? 107.695 82.092  162.610 1.00 54.61  ? 386  PHE A CB    1 
ATOM   2823 C  CG    . PHE A 1 386  ? 107.282 83.421  163.162 1.00 54.61  ? 386  PHE A CG    1 
ATOM   2824 C  CD1   . PHE A 1 386  ? 107.962 83.983  164.228 1.00 54.61  ? 386  PHE A CD1   1 
ATOM   2825 C  CD2   . PHE A 1 386  ? 106.211 84.107  162.620 1.00 54.61  ? 386  PHE A CD2   1 
ATOM   2826 C  CE1   . PHE A 1 386  ? 107.583 85.206  164.738 1.00 54.61  ? 386  PHE A CE1   1 
ATOM   2827 C  CE2   . PHE A 1 386  ? 105.826 85.329  163.128 1.00 54.61  ? 386  PHE A CE2   1 
ATOM   2828 C  CZ    . PHE A 1 386  ? 106.513 85.879  164.189 1.00 54.61  ? 386  PHE A CZ    1 
ATOM   2829 N  N     . ASN A 1 387  ? 105.833 81.047  165.312 1.00 56.11  ? 387  ASN A N     1 
ATOM   2830 C  CA    . ASN A 1 387  ? 104.490 80.969  165.871 1.00 56.11  ? 387  ASN A CA    1 
ATOM   2831 C  C     . ASN A 1 387  ? 104.213 82.232  166.673 1.00 56.11  ? 387  ASN A C     1 
ATOM   2832 O  O     . ASN A 1 387  ? 105.065 82.671  167.451 1.00 56.11  ? 387  ASN A O     1 
ATOM   2833 C  CB    . ASN A 1 387  ? 104.329 79.733  166.765 1.00 56.11  ? 387  ASN A CB    1 
ATOM   2834 C  CG    . ASN A 1 387  ? 104.029 78.472  165.975 1.00 56.11  ? 387  ASN A CG    1 
ATOM   2835 O  OD1   . ASN A 1 387  ? 104.490 78.304  164.848 1.00 56.11  ? 387  ASN A OD1   1 
ATOM   2836 N  ND2   . ASN A 1 387  ? 103.252 77.575  166.571 1.00 56.11  ? 387  ASN A ND2   1 
ATOM   2837 N  N     . ILE A 1 388  ? 103.025 82.809  166.488 1.00 58.43  ? 388  ILE A N     1 
ATOM   2838 C  CA    . ILE A 1 388  ? 102.636 84.023  167.200 1.00 58.43  ? 388  ILE A CA    1 
ATOM   2839 C  C     . ILE A 1 388  ? 101.120 84.138  167.137 1.00 58.43  ? 388  ILE A C     1 
ATOM   2840 O  O     . ILE A 1 388  ? 100.478 83.604  166.231 1.00 58.43  ? 388  ILE A O     1 
ATOM   2841 C  CB    . ILE A 1 388  ? 103.335 85.274  166.603 1.00 58.43  ? 388  ILE A CB    1 
ATOM   2842 C  CG1   . ILE A 1 388  ? 103.133 86.496  167.503 1.00 58.43  ? 388  ILE A CG1   1 
ATOM   2843 C  CG2   . ILE A 1 388  ? 102.825 85.557  165.200 1.00 58.43  ? 388  ILE A CG2   1 
ATOM   2844 C  CD1   . ILE A 1 388  ? 104.036 87.659  167.164 1.00 58.43  ? 388  ILE A CD1   1 
ATOM   2845 N  N     . PHE A 1 389  ? 100.541 84.837  168.114 1.00 59.72  ? 389  PHE A N     1 
ATOM   2846 C  CA    . PHE A 1 389  ? 99.098  84.998  168.230 1.00 59.72  ? 389  PHE A CA    1 
ATOM   2847 C  C     . PHE A 1 389  ? 98.749  86.479  168.276 1.00 59.72  ? 389  PHE A C     1 
ATOM   2848 O  O     . PHE A 1 389  ? 99.405  87.258  168.974 1.00 59.72  ? 389  PHE A O     1 
ATOM   2849 C  CB    . PHE A 1 389  ? 98.572  84.287  169.486 1.00 59.72  ? 389  PHE A CB    1 
ATOM   2850 C  CG    . PHE A 1 389  ? 97.078  84.345  169.644 1.00 59.72  ? 389  PHE A CG    1 
ATOM   2851 C  CD1   . PHE A 1 389  ? 96.242  84.301  168.542 1.00 59.72  ? 389  PHE A CD1   1 
ATOM   2852 C  CD2   . PHE A 1 389  ? 96.510  84.433  170.904 1.00 59.72  ? 389  PHE A CD2   1 
ATOM   2853 C  CE1   . PHE A 1 389  ? 94.870  84.354  168.693 1.00 59.72  ? 389  PHE A CE1   1 
ATOM   2854 C  CE2   . PHE A 1 389  ? 95.139  84.482  171.060 1.00 59.72  ? 389  PHE A CE2   1 
ATOM   2855 C  CZ    . PHE A 1 389  ? 94.318  84.442  169.953 1.00 59.72  ? 389  PHE A CZ    1 
ATOM   2856 N  N     . PHE A 1 390  ? 97.710  86.860  167.532 1.00 60.71  ? 390  PHE A N     1 
ATOM   2857 C  CA    . PHE A 1 390  ? 97.221  88.238  167.475 1.00 60.71  ? 390  PHE A CA    1 
ATOM   2858 C  C     . PHE A 1 390  ? 95.734  88.235  167.803 1.00 60.71  ? 390  PHE A C     1 
ATOM   2859 O  O     . PHE A 1 390  ? 94.889  88.333  166.905 1.00 60.71  ? 390  PHE A O     1 
ATOM   2860 C  CB    . PHE A 1 390  ? 97.471  88.867  166.102 1.00 60.71  ? 390  PHE A CB    1 
ATOM   2861 C  CG    . PHE A 1 390  ? 98.920  89.131  165.806 1.00 60.71  ? 390  PHE A CG    1 
ATOM   2862 C  CD1   . PHE A 1 390  ? 99.661  89.980  166.609 1.00 60.71  ? 390  PHE A CD1   1 
ATOM   2863 C  CD2   . PHE A 1 390  ? 99.535  88.543  164.715 1.00 60.71  ? 390  PHE A CD2   1 
ATOM   2864 C  CE1   . PHE A 1 390  ? 100.993 90.229  166.335 1.00 60.71  ? 390  PHE A CE1   1 
ATOM   2865 C  CE2   . PHE A 1 390  ? 100.866 88.788  164.435 1.00 60.71  ? 390  PHE A CE2   1 
ATOM   2866 C  CZ    . PHE A 1 390  ? 101.595 89.632  165.247 1.00 60.71  ? 390  PHE A CZ    1 
ATOM   2867 N  N     . PRO A 1 391  ? 95.379  88.139  169.082 1.00 62.50  ? 391  PRO A N     1 
ATOM   2868 C  CA    . PRO A 1 391  ? 93.962  88.054  169.451 1.00 62.50  ? 391  PRO A CA    1 
ATOM   2869 C  C     . PRO A 1 391  ? 93.197  89.324  169.110 1.00 62.50  ? 391  PRO A C     1 
ATOM   2870 O  O     . PRO A 1 391  ? 93.753  90.423  169.062 1.00 62.50  ? 391  PRO A O     1 
ATOM   2871 C  CB    . PRO A 1 391  ? 94.005  87.821  170.964 1.00 62.50  ? 391  PRO A CB    1 
ATOM   2872 C  CG    . PRO A 1 391  ? 95.291  88.437  171.395 1.00 62.50  ? 391  PRO A CG    1 
ATOM   2873 C  CD    . PRO A 1 391  ? 96.256  88.207  170.263 1.00 62.50  ? 391  PRO A CD    1 
ATOM   2874 N  N     . SER A 1 392  ? 91.900  89.151  168.869 1.00 66.82  ? 392  SER A N     1 
ATOM   2875 C  CA    . SER A 1 392  ? 91.046  90.263  168.476 1.00 66.82  ? 392  SER A CA    1 
ATOM   2876 C  C     . SER A 1 392  ? 90.895  91.268  169.610 1.00 66.82  ? 392  SER A C     1 
ATOM   2877 O  O     . SER A 1 392  ? 90.839  90.900  170.787 1.00 66.82  ? 392  SER A O     1 
ATOM   2878 C  CB    . SER A 1 392  ? 89.670  89.749  168.053 1.00 66.82  ? 392  SER A CB    1 
ATOM   2879 O  OG    . SER A 1 392  ? 89.005  89.122  169.134 1.00 66.82  ? 392  SER A OG    1 
ATOM   2880 N  N     . GLY A 1 393  ? 90.830  92.547  169.247 1.00 66.15  ? 393  GLY A N     1 
ATOM   2881 C  CA    . GLY A 1 393  ? 90.622  93.597  170.222 1.00 66.15  ? 393  GLY A CA    1 
ATOM   2882 C  C     . GLY A 1 393  ? 91.763  93.805  171.188 1.00 66.15  ? 393  GLY A C     1 
ATOM   2883 O  O     . GLY A 1 393  ? 91.586  94.482  172.203 1.00 66.15  ? 393  GLY A O     1 
ATOM   2884 N  N     . LYS A 1 394  ? 92.933  93.244  170.901 1.00 68.78  ? 394  LYS A N     1 
ATOM   2885 C  CA    . LYS A 1 394  ? 94.092  93.339  171.776 1.00 68.78  ? 394  LYS A CA    1 
ATOM   2886 C  C     . LYS A 1 394  ? 95.218  94.038  171.029 1.00 68.78  ? 394  LYS A C     1 
ATOM   2887 O  O     . LYS A 1 394  ? 95.515  93.691  169.881 1.00 68.78  ? 394  LYS A O     1 
ATOM   2888 C  CB    . LYS A 1 394  ? 94.538  91.951  172.245 1.00 68.78  ? 394  LYS A CB    1 
ATOM   2889 C  CG    . LYS A 1 394  ? 93.432  91.126  172.897 1.00 68.78  ? 394  LYS A CG    1 
ATOM   2890 C  CD    . LYS A 1 394  ? 92.670  91.917  173.950 1.00 68.78  ? 394  LYS A CD    1 
ATOM   2891 C  CE    . LYS A 1 394  ? 93.335  91.819  175.313 1.00 68.78  ? 394  LYS A CE    1 
ATOM   2892 N  NZ    . LYS A 1 394  ? 92.633  92.642  176.335 1.00 68.78  ? 394  LYS A NZ    1 
ATOM   2893 N  N     . THR A 1 395  ? 95.841  95.021  171.680 1.00 73.39  ? 395  THR A N     1 
ATOM   2894 C  CA    . THR A 1 395  ? 96.899  95.817  171.056 1.00 73.39  ? 395  THR A CA    1 
ATOM   2895 C  C     . THR A 1 395  ? 98.226  95.082  171.219 1.00 73.39  ? 395  THR A C     1 
ATOM   2896 O  O     . THR A 1 395  ? 99.048  95.394  172.081 1.00 73.39  ? 395  THR A O     1 
ATOM   2897 C  CB    . THR A 1 395  ? 96.953  97.211  171.666 1.00 73.39  ? 395  THR A CB    1 
ATOM   2898 O  OG1   . THR A 1 395  ? 97.417  97.124  173.019 1.00 73.39  ? 395  THR A OG1   1 
ATOM   2899 C  CG2   . THR A 1 395  ? 95.573  97.848  171.655 1.00 73.39  ? 395  THR A CG2   1 
ATOM   2900 N  N     . VAL A 1 396  ? 98.433  94.087  170.364 1.00 69.37  ? 396  VAL A N     1 
ATOM   2901 C  CA    . VAL A 1 396  ? 99.663  93.303  170.390 1.00 69.37  ? 396  VAL A CA    1 
ATOM   2902 C  C     . VAL A 1 396  ? 100.790 94.123  169.778 1.00 69.37  ? 396  VAL A C     1 
ATOM   2903 O  O     . VAL A 1 396  ? 100.640 94.692  168.691 1.00 69.37  ? 396  VAL A O     1 
ATOM   2904 C  CB    . VAL A 1 396  ? 99.478  91.972  169.647 1.00 69.37  ? 396  VAL A CB    1 
ATOM   2905 C  CG1   . VAL A 1 396  ? 100.670 91.062  169.891 1.00 69.37  ? 396  VAL A CG1   1 
ATOM   2906 C  CG2   . VAL A 1 396  ? 98.190  91.301  170.086 1.00 69.37  ? 396  VAL A CG2   1 
ATOM   2907 N  N     . ALA A 1 397  ? 101.922 94.182  170.472 1.00 73.63  ? 397  ALA A N     1 
ATOM   2908 C  CA    . ALA A 1 397  ? 103.080 94.941  170.028 1.00 73.63  ? 397  ALA A CA    1 
ATOM   2909 C  C     . ALA A 1 397  ? 104.221 94.000  169.667 1.00 73.63  ? 397  ALA A C     1 
ATOM   2910 O  O     . ALA A 1 397  ? 104.388 92.936  170.271 1.00 73.63  ? 397  ALA A O     1 
ATOM   2911 C  CB    . ALA A 1 397  ? 103.541 95.926  171.106 1.00 73.63  ? 397  ALA A CB    1 
ATOM   2912 N  N     . VAL A 1 398  ? 105.005 94.400  168.669 1.00 70.57  ? 398  VAL A N     1 
ATOM   2913 C  CA    . VAL A 1 398  ? 106.140 93.622  168.187 1.00 70.57  ? 398  VAL A CA    1 
ATOM   2914 C  C     . VAL A 1 398  ? 107.398 94.459  168.363 1.00 70.57  ? 398  VAL A C     1 
ATOM   2915 O  O     . VAL A 1 398  ? 107.470 95.593  167.872 1.00 70.57  ? 398  VAL A O     1 
ATOM   2916 C  CB    . VAL A 1 398  ? 105.965 93.206  166.719 1.00 70.57  ? 398  VAL A CB    1 
ATOM   2917 C  CG1   . VAL A 1 398  ? 107.161 92.401  166.260 1.00 70.57  ? 398  VAL A CG1   1 
ATOM   2918 C  CG2   . VAL A 1 398  ? 104.685 92.408  166.545 1.00 70.57  ? 398  VAL A CG2   1 
ATOM   2919 N  N     . VAL A 1 399  ? 108.389 93.902  169.060 1.00 77.07  ? 399  VAL A N     1 
ATOM   2920 C  CA    . VAL A 1 399  ? 109.664 94.566  169.288 1.00 77.07  ? 399  VAL A CA    1 
ATOM   2921 C  C     . VAL A 1 399  ? 110.777 93.554  169.051 1.00 77.07  ? 399  VAL A C     1 
ATOM   2922 O  O     . VAL A 1 399  ? 110.565 92.341  169.098 1.00 77.07  ? 399  VAL A O     1 
ATOM   2923 C  CB    . VAL A 1 399  ? 109.761 95.169  170.711 1.00 77.07  ? 399  VAL A CB    1 
ATOM   2924 C  CG1   . VAL A 1 399  ? 110.023 94.082  171.745 1.00 77.07  ? 399  VAL A CG1   1 
ATOM   2925 C  CG2   . VAL A 1 399  ? 110.818 96.264  170.771 1.00 77.07  ? 399  VAL A CG2   1 
ATOM   2926 N  N     . GLY A 1 400  ? 111.972 94.065  168.778 1.00 73.75  ? 400  GLY A N     1 
ATOM   2927 C  CA    . GLY A 1 400  ? 113.106 93.197  168.540 1.00 73.75  ? 400  GLY A CA    1 
ATOM   2928 C  C     . GLY A 1 400  ? 114.328 93.999  168.141 1.00 73.75  ? 400  GLY A C     1 
ATOM   2929 O  O     . GLY A 1 400  ? 114.367 95.223  168.279 1.00 73.75  ? 400  GLY A O     1 
ATOM   2930 N  N     . GLY A 1 401  ? 115.325 93.276  167.642 1.00 65.48  ? 401  GLY A N     1 
ATOM   2931 C  CA    . GLY A 1 401  ? 116.567 93.884  167.219 1.00 65.48  ? 401  GLY A CA    1 
ATOM   2932 C  C     . GLY A 1 401  ? 116.426 94.614  165.896 1.00 65.48  ? 401  GLY A C     1 
ATOM   2933 O  O     . GLY A 1 401  ? 115.373 94.639  165.258 1.00 65.48  ? 401  GLY A O     1 
ATOM   2934 N  N     . SER A 1 402  ? 117.534 95.227  165.477 1.00 58.37  ? 402  SER A N     1 
ATOM   2935 C  CA    . SER A 1 402  ? 117.566 96.037  164.260 1.00 58.37  ? 402  SER A CA    1 
ATOM   2936 C  C     . SER A 1 402  ? 117.714 95.121  163.048 1.00 58.37  ? 402  SER A C     1 
ATOM   2937 O  O     . SER A 1 402  ? 118.800 94.919  162.501 1.00 58.37  ? 402  SER A O     1 
ATOM   2938 C  CB    . SER A 1 402  ? 118.693 97.059  164.325 1.00 58.37  ? 402  SER A CB    1 
ATOM   2939 O  OG    . SER A 1 402  ? 118.768 97.810  163.126 1.00 58.37  ? 402  SER A OG    1 
ATOM   2940 N  N     . GLY A 1 403  ? 116.588 94.557  162.622 1.00 52.21  ? 403  GLY A N     1 
ATOM   2941 C  CA    . GLY A 1 403  ? 116.564 93.803  161.385 1.00 52.21  ? 403  GLY A CA    1 
ATOM   2942 C  C     . GLY A 1 403  ? 116.373 92.310  161.541 1.00 52.21  ? 403  GLY A C     1 
ATOM   2943 O  O     . GLY A 1 403  ? 116.832 91.538  160.694 1.00 52.21  ? 403  GLY A O     1 
ATOM   2944 N  N     . SER A 1 404  ? 115.705 91.879  162.611 1.00 54.81  ? 404  SER A N     1 
ATOM   2945 C  CA    . SER A 1 404  ? 115.515 90.444  162.816 1.00 54.81  ? 404  SER A CA    1 
ATOM   2946 C  C     . SER A 1 404  ? 114.312 89.914  162.039 1.00 54.81  ? 404  SER A C     1 
ATOM   2947 O  O     . SER A 1 404  ? 114.463 89.139  161.091 1.00 54.81  ? 404  SER A O     1 
ATOM   2948 C  CB    . SER A 1 404  ? 115.369 90.151  164.312 1.00 54.81  ? 404  SER A CB    1 
ATOM   2949 O  OG    . SER A 1 404  ? 114.190 90.741  164.828 1.00 54.81  ? 404  SER A OG    1 
ATOM   2950 N  N     . GLY A 1 405  ? 113.107 90.323  162.430 1.00 54.22  ? 405  GLY A N     1 
ATOM   2951 C  CA    . GLY A 1 405  ? 111.910 89.833  161.772 1.00 54.22  ? 405  GLY A CA    1 
ATOM   2952 C  C     . GLY A 1 405  ? 110.737 90.792  161.738 1.00 54.22  ? 405  GLY A C     1 
ATOM   2953 O  O     . GLY A 1 405  ? 109.631 90.400  161.355 1.00 54.22  ? 405  GLY A O     1 
ATOM   2954 N  N     . LYS A 1 406  ? 110.957 92.046  162.136 1.00 51.93  ? 406  LYS A N     1 
ATOM   2955 C  CA    . LYS A 1 406  ? 109.842 92.933  162.459 1.00 51.93  ? 406  LYS A CA    1 
ATOM   2956 C  C     . LYS A 1 406  ? 108.983 93.237  161.234 1.00 51.93  ? 406  LYS A C     1 
ATOM   2957 O  O     . LYS A 1 406  ? 107.794 92.900  161.199 1.00 51.93  ? 406  LYS A O     1 
ATOM   2958 C  CB    . LYS A 1 406  ? 110.371 94.220  163.091 1.00 51.93  ? 406  LYS A CB    1 
ATOM   2959 C  CG    . LYS A 1 406  ? 111.394 93.973  164.186 1.00 51.93  ? 406  LYS A CG    1 
ATOM   2960 C  CD    . LYS A 1 406  ? 112.122 95.244  164.577 1.00 51.93  ? 406  LYS A CD    1 
ATOM   2961 C  CE    . LYS A 1 406  ? 111.174 96.243  165.214 1.00 51.93  ? 406  LYS A CE    1 
ATOM   2962 N  NZ    . LYS A 1 406  ? 111.899 97.264  166.016 1.00 51.93  ? 406  LYS A NZ    1 
ATOM   2963 N  N     . SER A 1 407  ? 109.564 93.871  160.215 1.00 44.87  ? 407  SER A N     1 
ATOM   2964 C  CA    . SER A 1 407  ? 108.768 94.265  159.057 1.00 44.87  ? 407  SER A CA    1 
ATOM   2965 C  C     . SER A 1 407  ? 108.473 93.098  158.124 1.00 44.87  ? 407  SER A C     1 
ATOM   2966 O  O     . SER A 1 407  ? 107.603 93.224  157.257 1.00 44.87  ? 407  SER A O     1 
ATOM   2967 C  CB    . SER A 1 407  ? 109.467 95.380  158.280 1.00 44.87  ? 407  SER A CB    1 
ATOM   2968 O  OG    . SER A 1 407  ? 109.625 96.537  159.083 1.00 44.87  ? 407  SER A OG    1 
ATOM   2969 N  N     . THR A 1 408  ? 109.178 91.975  158.273 1.00 47.06  ? 408  THR A N     1 
ATOM   2970 C  CA    . THR A 1 408  ? 108.885 90.811  157.443 1.00 47.06  ? 408  THR A CA    1 
ATOM   2971 C  C     . THR A 1 408  ? 107.506 90.240  157.746 1.00 47.06  ? 408  THR A C     1 
ATOM   2972 O  O     . THR A 1 408  ? 106.845 89.707  156.847 1.00 47.06  ? 408  THR A O     1 
ATOM   2973 C  CB    . THR A 1 408  ? 109.955 89.739  157.638 1.00 47.06  ? 408  THR A CB    1 
ATOM   2974 O  OG1   . THR A 1 408  ? 110.048 89.405  159.027 1.00 47.06  ? 408  THR A OG1   1 
ATOM   2975 C  CG2   . THR A 1 408  ? 111.302 90.237  157.148 1.00 47.06  ? 408  THR A CG2   1 
ATOM   2976 N  N     . VAL A 1 409  ? 107.063 90.331  159.001 1.00 45.34  ? 409  VAL A N     1 
ATOM   2977 C  CA    . VAL A 1 409  ? 105.732 89.847  159.363 1.00 45.34  ? 409  VAL A CA    1 
ATOM   2978 C  C     . VAL A 1 409  ? 104.663 90.636  158.619 1.00 45.34  ? 409  VAL A C     1 
ATOM   2979 O  O     . VAL A 1 409  ? 103.702 90.069  158.085 1.00 45.34  ? 409  VAL A O     1 
ATOM   2980 C  CB    . VAL A 1 409  ? 105.531 89.925  160.887 1.00 45.34  ? 409  VAL A CB    1 
ATOM   2981 C  CG1   . VAL A 1 409  ? 104.129 89.481  161.261 1.00 45.34  ? 409  VAL A CG1   1 
ATOM   2982 C  CG2   . VAL A 1 409  ? 106.572 89.083  161.602 1.00 45.34  ? 409  VAL A CG2   1 
ATOM   2983 N  N     . VAL A 1 410  ? 104.817 91.961  158.575 1.00 41.78  ? 410  VAL A N     1 
ATOM   2984 C  CA    . VAL A 1 410  ? 103.858 92.804  157.868 1.00 41.78  ? 410  VAL A CA    1 
ATOM   2985 C  C     . VAL A 1 410  ? 103.850 92.468  156.383 1.00 41.78  ? 410  VAL A C     1 
ATOM   2986 O  O     . VAL A 1 410  ? 102.789 92.410  155.749 1.00 41.78  ? 410  VAL A O     1 
ATOM   2987 C  CB    . VAL A 1 410  ? 104.175 94.290  158.115 1.00 41.78  ? 410  VAL A CB    1 
ATOM   2988 C  CG1   . VAL A 1 410  ? 103.288 95.173  157.263 1.00 41.78  ? 410  VAL A CG1   1 
ATOM   2989 C  CG2   . VAL A 1 410  ? 104.008 94.626  159.588 1.00 41.78  ? 410  VAL A CG2   1 
ATOM   2990 N  N     . SER A 1 411  ? 105.031 92.242  155.805 1.00 39.13  ? 411  SER A N     1 
ATOM   2991 C  CA    . SER A 1 411  ? 105.105 91.873  154.395 1.00 39.13  ? 411  SER A CA    1 
ATOM   2992 C  C     . SER A 1 411  ? 104.414 90.540  154.135 1.00 39.13  ? 411  SER A C     1 
ATOM   2993 O  O     . SER A 1 411  ? 103.719 90.379  153.126 1.00 39.13  ? 411  SER A O     1 
ATOM   2994 C  CB    . SER A 1 411  ? 106.563 91.820  153.944 1.00 39.13  ? 411  SER A CB    1 
ATOM   2995 O  OG    . SER A 1 411  ? 106.655 91.613  152.546 1.00 39.13  ? 411  SER A OG    1 
ATOM   2996 N  N     . LEU A 1 412  ? 104.601 89.567  155.032 1.00 39.69  ? 412  LEU A N     1 
ATOM   2997 C  CA    . LEU A 1 412  ? 103.936 88.277  154.872 1.00 39.69  ? 412  LEU A CA    1 
ATOM   2998 C  C     . LEU A 1 412  ? 102.423 88.416  154.978 1.00 39.69  ? 412  LEU A C     1 
ATOM   2999 O  O     . LEU A 1 412  ? 101.682 87.785  154.215 1.00 39.69  ? 412  LEU A O     1 
ATOM   3000 C  CB    . LEU A 1 412  ? 104.453 87.285  155.913 1.00 39.69  ? 412  LEU A CB    1 
ATOM   3001 C  CG    . LEU A 1 412  ? 105.794 86.613  155.622 1.00 39.69  ? 412  LEU A CG    1 
ATOM   3002 C  CD1   . LEU A 1 412  ? 106.212 85.733  156.786 1.00 39.69  ? 412  LEU A CD1   1 
ATOM   3003 C  CD2   . LEU A 1 412  ? 105.712 85.804  154.342 1.00 39.69  ? 412  LEU A CD2   1 
ATOM   3004 N  N     . ILE A 1 413  ? 101.948 89.230  155.923 1.00 40.11  ? 413  ILE A N     1 
ATOM   3005 C  CA    . ILE A 1 413  ? 100.509 89.407  156.101 1.00 40.11  ? 413  ILE A CA    1 
ATOM   3006 C  C     . ILE A 1 413  ? 99.895  90.076  154.878 1.00 40.11  ? 413  ILE A C     1 
ATOM   3007 O  O     . ILE A 1 413  ? 98.826  89.673  154.403 1.00 40.11  ? 413  ILE A O     1 
ATOM   3008 C  CB    . ILE A 1 413  ? 100.223 90.208  157.385 1.00 40.11  ? 413  ILE A CB    1 
ATOM   3009 C  CG1   . ILE A 1 413  ? 100.588 89.386  158.620 1.00 40.11  ? 413  ILE A CG1   1 
ATOM   3010 C  CG2   . ILE A 1 413  ? 98.764  90.625  157.441 1.00 40.11  ? 413  ILE A CG2   1 
ATOM   3011 C  CD1   . ILE A 1 413  ? 100.206 90.049  159.924 1.00 40.11  ? 413  ILE A CD1   1 
ATOM   3012 N  N     . GLU A 1 414  ? 100.561 91.097  154.341 1.00 43.36  ? 414  GLU A N     1 
ATOM   3013 C  CA    . GLU A 1 414  ? 99.974  91.882  153.263 1.00 43.36  ? 414  GLU A CA    1 
ATOM   3014 C  C     . GLU A 1 414  ? 100.238 91.216  151.915 1.00 43.36  ? 414  GLU A C     1 
ATOM   3015 O  O     . GLU A 1 414  ? 100.625 91.885  150.953 1.00 43.36  ? 414  GLU A O     1 
ATOM   3016 C  CB    . GLU A 1 414  ? 100.554 93.301  153.287 1.00 43.36  ? 414  GLU A CB    1 
ATOM   3017 C  CG    . GLU A 1 414  ? 99.795  94.336  152.477 1.00 43.36  ? 414  GLU A CG    1 
ATOM   3018 C  CD    . GLU A 1 414  ? 98.505  94.748  153.147 1.00 43.36  ? 414  GLU A CD    1 
ATOM   3019 O  OE1   . GLU A 1 414  ? 98.442  94.674  154.391 1.00 43.36  ? 414  GLU A OE1   1 
ATOM   3020 O  OE2   . GLU A 1 414  ? 97.560  95.149  152.437 1.00 43.36  ? 414  GLU A OE2   1 
ATOM   3021 N  N     . ARG A 1 415  ? 100.019 89.899  151.845 1.00 39.76  ? 415  ARG A N     1 
ATOM   3022 C  CA    . ARG A 1 415  ? 100.109 89.097  150.625 1.00 39.76  ? 415  ARG A CA    1 
ATOM   3023 C  C     . ARG A 1 415  ? 101.202 89.547  149.663 1.00 39.76  ? 415  ARG A C     1 
ATOM   3024 O  O     . ARG A 1 415  ? 100.960 89.666  148.458 1.00 39.76  ? 415  ARG A O     1 
ATOM   3025 C  CB    . ARG A 1 415  ? 98.763  89.085  149.899 1.00 39.76  ? 415  ARG A CB    1 
ATOM   3026 C  CG    . ARG A 1 415  ? 97.779  88.076  150.461 1.00 39.76  ? 415  ARG A CG    1 
ATOM   3027 C  CD    . ARG A 1 415  ? 98.432  86.718  150.674 1.00 39.76  ? 415  ARG A CD    1 
ATOM   3028 N  NE    . ARG A 1 415  ? 98.716  86.035  149.415 1.00 39.76  ? 415  ARG A NE    1 
ATOM   3029 C  CZ    . ARG A 1 415  ? 97.795  85.452  148.653 1.00 39.76  ? 415  ARG A CZ    1 
ATOM   3030 N  NH1   . ARG A 1 415  ? 96.522  85.460  149.021 1.00 39.76  ? 415  ARG A NH1   1 
ATOM   3031 N  NH2   . ARG A 1 415  ? 98.149  84.855  147.524 1.00 39.76  ? 415  ARG A NH2   1 
ATOM   3032 N  N     . PHE A 1 416  ? 102.404 89.799  150.175 1.00 35.56  ? 416  PHE A N     1 
ATOM   3033 C  CA    . PHE A 1 416  ? 103.515 90.178  149.312 1.00 35.56  ? 416  PHE A CA    1 
ATOM   3034 C  C     . PHE A 1 416  ? 104.307 88.956  148.863 1.00 35.56  ? 416  PHE A C     1 
ATOM   3035 O  O     . PHE A 1 416  ? 104.647 88.828  147.683 1.00 35.56  ? 416  PHE A O     1 
ATOM   3036 C  CB    . PHE A 1 416  ? 104.430 91.174  150.032 1.00 35.56  ? 416  PHE A CB    1 
ATOM   3037 C  CG    . PHE A 1 416  ? 103.858 92.561  150.135 1.00 35.56  ? 416  PHE A CG    1 
ATOM   3038 C  CD1   . PHE A 1 416  ? 103.123 93.103  149.095 1.00 35.56  ? 416  PHE A CD1   1 
ATOM   3039 C  CD2   . PHE A 1 416  ? 104.059 93.323  151.272 1.00 35.56  ? 416  PHE A CD2   1 
ATOM   3040 C  CE1   . PHE A 1 416  ? 102.599 94.378  149.191 1.00 35.56  ? 416  PHE A CE1   1 
ATOM   3041 C  CE2   . PHE A 1 416  ? 103.536 94.598  151.373 1.00 35.56  ? 416  PHE A CE2   1 
ATOM   3042 C  CZ    . PHE A 1 416  ? 102.805 95.125  150.331 1.00 35.56  ? 416  PHE A CZ    1 
ATOM   3043 N  N     . TYR A 1 417  ? 104.595 88.049  149.791 1.00 33.76  ? 417  TYR A N     1 
ATOM   3044 C  CA    . TYR A 1 417  ? 105.318 86.825  149.496 1.00 33.76  ? 417  TYR A CA    1 
ATOM   3045 C  C     . TYR A 1 417  ? 104.654 85.676  150.237 1.00 33.76  ? 417  TYR A C     1 
ATOM   3046 O  O     . TYR A 1 417  ? 104.270 85.821  151.400 1.00 33.76  ? 417  TYR A O     1 
ATOM   3047 C  CB    . TYR A 1 417  ? 106.787 86.935  149.914 1.00 33.76  ? 417  TYR A CB    1 
ATOM   3048 C  CG    . TYR A 1 417  ? 107.586 87.937  149.114 1.00 33.76  ? 417  TYR A CG    1 
ATOM   3049 C  CD1   . TYR A 1 417  ? 108.086 87.613  147.863 1.00 33.76  ? 417  TYR A CD1   1 
ATOM   3050 C  CD2   . TYR A 1 417  ? 107.845 89.206  149.616 1.00 33.76  ? 417  TYR A CD2   1 
ATOM   3051 C  CE1   . TYR A 1 417  ? 108.818 88.523  147.132 1.00 33.76  ? 417  TYR A CE1   1 
ATOM   3052 C  CE2   . TYR A 1 417  ? 108.577 90.123  148.891 1.00 33.76  ? 417  TYR A CE2   1 
ATOM   3053 C  CZ    . TYR A 1 417  ? 109.060 89.776  147.649 1.00 33.76  ? 417  TYR A CZ    1 
ATOM   3054 O  OH    . TYR A 1 417  ? 109.790 90.684  146.920 1.00 33.76  ? 417  TYR A OH    1 
ATOM   3055 N  N     . ASP A 1 418  ? 104.512 84.550  149.568 1.00 43.00  ? 418  ASP A N     1 
ATOM   3056 C  CA    . ASP A 1 418  ? 103.972 83.404  150.278 1.00 43.00  ? 418  ASP A CA    1 
ATOM   3057 C  C     . ASP A 1 418  ? 105.036 82.756  151.164 1.00 43.00  ? 418  ASP A C     1 
ATOM   3058 O  O     . ASP A 1 418  ? 106.236 82.907  150.919 1.00 43.00  ? 418  ASP A O     1 
ATOM   3059 C  CB    . ASP A 1 418  ? 103.370 82.398  149.284 1.00 43.00  ? 418  ASP A CB    1 
ATOM   3060 C  CG    . ASP A 1 418  ? 104.411 81.523  148.550 1.00 43.00  ? 418  ASP A CG    1 
ATOM   3061 O  OD1   . ASP A 1 418  ? 105.525 81.250  149.039 1.00 43.00  ? 418  ASP A OD1   1 
ATOM   3062 O  OD2   . ASP A 1 418  ? 104.088 81.081  147.429 1.00 43.00  ? 418  ASP A OD2   1 
ATOM   3063 N  N     . PRO A 1 419  ? 104.627 82.064  152.224 1.00 40.49  ? 419  PRO A N     1 
ATOM   3064 C  CA    . PRO A 1 419  ? 105.591 81.271  152.991 1.00 40.49  ? 419  PRO A CA    1 
ATOM   3065 C  C     . PRO A 1 419  ? 105.891 79.963  152.280 1.00 40.49  ? 419  PRO A C     1 
ATOM   3066 O  O     . PRO A 1 419  ? 104.992 79.287  151.774 1.00 40.49  ? 419  PRO A O     1 
ATOM   3067 C  CB    . PRO A 1 419  ? 104.875 81.034  154.325 1.00 40.49  ? 419  PRO A CB    1 
ATOM   3068 C  CG    . PRO A 1 419  ? 103.434 81.101  153.985 1.00 40.49  ? 419  PRO A CG    1 
ATOM   3069 C  CD    . PRO A 1 419  ? 103.300 82.091  152.862 1.00 40.49  ? 419  PRO A CD    1 
ATOM   3070 N  N     . ASN A 1 420  ? 107.177 79.610  152.236 1.00 42.99  ? 420  ASN A N     1 
ATOM   3071 C  CA    . ASN A 1 420  ? 107.571 78.371  151.577 1.00 42.99  ? 420  ASN A CA    1 
ATOM   3072 C  C     . ASN A 1 420  ? 107.114 77.140  152.346 1.00 42.99  ? 420  ASN A C     1 
ATOM   3073 O  O     . ASN A 1 420  ? 107.128 76.037  151.791 1.00 42.99  ? 420  ASN A O     1 
ATOM   3074 C  CB    . ASN A 1 420  ? 109.086 78.338  151.377 1.00 42.99  ? 420  ASN A CB    1 
ATOM   3075 C  CG    . ASN A 1 420  ? 109.847 78.738  152.621 1.00 42.99  ? 420  ASN A CG    1 
ATOM   3076 O  OD1   . ASN A 1 420  ? 109.297 78.756  153.721 1.00 42.99  ? 420  ASN A OD1   1 
ATOM   3077 N  ND2   . ASN A 1 420  ? 111.122 79.065  152.453 1.00 42.99  ? 420  ASN A ND2   1 
ATOM   3078 N  N     . SER A 1 421  ? 106.716 77.302  153.606 1.00 44.63  ? 421  SER A N     1 
ATOM   3079 C  CA    . SER A 1 421  ? 106.168 76.206  154.389 1.00 44.63  ? 421  SER A CA    1 
ATOM   3080 C  C     . SER A 1 421  ? 105.204 76.776  155.418 1.00 44.63  ? 421  SER A C     1 
ATOM   3081 O  O     . SER A 1 421  ? 105.275 77.952  155.780 1.00 44.63  ? 421  SER A O     1 
ATOM   3082 C  CB    . SER A 1 421  ? 107.271 75.390  155.073 1.00 44.63  ? 421  SER A CB    1 
ATOM   3083 O  OG    . SER A 1 421  ? 108.106 74.758  154.118 1.00 44.63  ? 421  SER A OG    1 
ATOM   3084 N  N     . GLY A 1 422  ? 104.298 75.925  155.885 1.00 50.03  ? 422  GLY A N     1 
ATOM   3085 C  CA    . GLY A 1 422  ? 103.315 76.345  156.858 1.00 50.03  ? 422  GLY A CA    1 
ATOM   3086 C  C     . GLY A 1 422  ? 102.203 77.170  156.237 1.00 50.03  ? 422  GLY A C     1 
ATOM   3087 O  O     . GLY A 1 422  ? 102.081 77.304  155.016 1.00 50.03  ? 422  GLY A O     1 
ATOM   3088 N  N     . GLN A 1 423  ? 101.375 77.735  157.112 1.00 51.04  ? 423  GLN A N     1 
ATOM   3089 C  CA    . GLN A 1 423  ? 100.256 78.554  156.671 1.00 51.04  ? 423  GLN A CA    1 
ATOM   3090 C  C     . GLN A 1 423  ? 99.892  79.532  157.776 1.00 51.04  ? 423  GLN A C     1 
ATOM   3091 O  O     . GLN A 1 423  ? 100.259 79.350  158.939 1.00 51.04  ? 423  GLN A O     1 
ATOM   3092 C  CB    . GLN A 1 423  ? 99.046  77.695  156.290 1.00 51.04  ? 423  GLN A CB    1 
ATOM   3093 C  CG    . GLN A 1 423  ? 98.342  77.056  157.473 1.00 51.04  ? 423  GLN A CG    1 
ATOM   3094 C  CD    . GLN A 1 423  ? 98.770  75.621  157.699 1.00 51.04  ? 423  GLN A CD    1 
ATOM   3095 O  OE1   . GLN A 1 423  ? 99.953  75.293  157.611 1.00 51.04  ? 423  GLN A OE1   1 
ATOM   3096 N  NE2   . GLN A 1 423  ? 97.807  74.756  157.990 1.00 51.04  ? 423  GLN A NE2   1 
ATOM   3097 N  N     . ILE A 1 424  ? 99.164  80.577  157.390 1.00 55.43  ? 424  ILE A N     1 
ATOM   3098 C  CA    . ILE A 1 424  ? 98.719  81.620  158.305 1.00 55.43  ? 424  ILE A CA    1 
ATOM   3099 C  C     . ILE A 1 424  ? 97.213  81.795  158.155 1.00 55.43  ? 424  ILE A C     1 
ATOM   3100 O  O     . ILE A 1 424  ? 96.678  81.749  157.041 1.00 55.43  ? 424  ILE A O     1 
ATOM   3101 C  CB    . ILE A 1 424  ? 99.484  82.940  158.066 1.00 55.43  ? 424  ILE A CB    1 
ATOM   3102 C  CG1   . ILE A 1 424  ? 99.241  83.479  156.658 1.00 55.43  ? 424  ILE A CG1   1 
ATOM   3103 C  CG2   . ILE A 1 424  ? 100.968 82.749  158.302 1.00 55.43  ? 424  ILE A CG2   1 
ATOM   3104 C  CD1   . ILE A 1 424  ? 99.784  84.873  156.458 1.00 55.43  ? 424  ILE A CD1   1 
ATOM   3105 N  N     . LEU A 1 425  ? 96.533  81.981  159.283 1.00 61.75  ? 425  LEU A N     1 
ATOM   3106 C  CA    . LEU A 1 425  ? 95.083  81.856  159.375 1.00 61.75  ? 425  LEU A CA    1 
ATOM   3107 C  C     . LEU A 1 425  ? 94.454  83.193  159.746 1.00 61.75  ? 425  LEU A C     1 
ATOM   3108 O  O     . LEU A 1 425  ? 94.904  83.850  160.692 1.00 61.75  ? 425  LEU A O     1 
ATOM   3109 C  CB    . LEU A 1 425  ? 94.693  80.806  160.420 1.00 61.75  ? 425  LEU A CB    1 
ATOM   3110 C  CG    . LEU A 1 425  ? 94.753  79.302  160.127 1.00 61.75  ? 425  LEU A CG    1 
ATOM   3111 C  CD1   . LEU A 1 425  ? 93.785  78.911  159.024 1.00 61.75  ? 425  LEU A CD1   1 
ATOM   3112 C  CD2   . LEU A 1 425  ? 96.166  78.838  159.802 1.00 61.75  ? 425  LEU A CD2   1 
ATOM   3113 N  N     . LEU A 1 426  ? 93.417  83.585  159.008 1.00 63.01  ? 426  LEU A N     1 
ATOM   3114 C  CA    . LEU A 1 426  ? 92.584  84.736  159.366 1.00 63.01  ? 426  LEU A CA    1 
ATOM   3115 C  C     . LEU A 1 426  ? 91.350  84.303  160.159 1.00 63.01  ? 426  LEU A C     1 
ATOM   3116 O  O     . LEU A 1 426  ? 90.214  84.656  159.840 1.00 63.01  ? 426  LEU A O     1 
ATOM   3117 C  CB    . LEU A 1 426  ? 92.195  85.503  158.108 1.00 63.01  ? 426  LEU A CB    1 
ATOM   3118 C  CG    . LEU A 1 426  ? 91.565  86.893  158.251 1.00 63.01  ? 426  LEU A CG    1 
ATOM   3119 C  CD1   . LEU A 1 426  ? 92.487  87.842  158.988 1.00 63.01  ? 426  LEU A CD1   1 
ATOM   3120 C  CD2   . LEU A 1 426  ? 91.199  87.456  156.888 1.00 63.01  ? 426  LEU A CD2   1 
ATOM   3121 N  N     . ASP A 1 427  ? 91.584  83.481  161.183 1.00 69.90  ? 427  ASP A N     1 
ATOM   3122 C  CA    . ASP A 1 427  ? 90.608  83.111  162.207 1.00 69.90  ? 427  ASP A CA    1 
ATOM   3123 C  C     . ASP A 1 427  ? 89.500  82.199  161.688 1.00 69.90  ? 427  ASP A C     1 
ATOM   3124 O  O     . ASP A 1 427  ? 88.758  81.613  162.483 1.00 69.90  ? 427  ASP A O     1 
ATOM   3125 C  CB    . ASP A 1 427  ? 89.987  84.370  162.823 1.00 69.90  ? 427  ASP A CB    1 
ATOM   3126 C  CG    . ASP A 1 427  ? 89.159  84.072  164.057 1.00 69.90  ? 427  ASP A CG    1 
ATOM   3127 O  OD1   . ASP A 1 427  ? 89.456  83.077  164.750 1.00 69.90  ? 427  ASP A OD1   1 
ATOM   3128 O  OD2   . ASP A 1 427  ? 88.207  84.833  164.332 1.00 69.90  ? 427  ASP A OD2   1 
ATOM   3129 N  N     . GLY A 1 428  ? 89.379  82.050  160.373 1.00 70.15  ? 428  GLY A N     1 
ATOM   3130 C  CA    . GLY A 1 428  ? 88.425  81.097  159.844 1.00 70.15  ? 428  GLY A CA    1 
ATOM   3131 C  C     . GLY A 1 428  ? 88.983  80.204  158.759 1.00 70.15  ? 428  GLY A C     1 
ATOM   3132 O  O     . GLY A 1 428  ? 88.474  79.105  158.519 1.00 70.15  ? 428  GLY A O     1 
ATOM   3133 N  N     . VAL A 1 429  ? 90.047  80.668  158.104 1.00 69.05  ? 429  VAL A N     1 
ATOM   3134 C  CA    . VAL A 1 429  ? 90.599  79.982  156.943 1.00 69.05  ? 429  VAL A CA    1 
ATOM   3135 C  C     . VAL A 1 429  ? 91.974  80.566  156.673 1.00 69.05  ? 429  VAL A C     1 
ATOM   3136 O  O     . VAL A 1 429  ? 92.284  81.679  157.114 1.00 69.05  ? 429  VAL A O     1 
ATOM   3137 C  CB    . VAL A 1 429  ? 89.652  80.136  155.722 1.00 69.05  ? 429  VAL A CB    1 
ATOM   3138 C  CG1   . VAL A 1 429  ? 89.763  81.533  155.132 1.00 69.05  ? 429  VAL A CG1   1 
ATOM   3139 C  CG2   . VAL A 1 429  ? 89.941  79.071  154.674 1.00 69.05  ? 429  VAL A CG2   1 
ATOM   3140 N  N     . GLU A 1 430  ? 92.809  79.812  155.964 1.00 69.39  ? 430  GLU A N     1 
ATOM   3141 C  CA    . GLU A 1 430  ? 94.116  80.322  155.580 1.00 69.39  ? 430  GLU A CA    1 
ATOM   3142 C  C     . GLU A 1 430  ? 93.963  81.499  154.622 1.00 69.39  ? 430  GLU A C     1 
ATOM   3143 O  O     . GLU A 1 430  ? 93.059  81.535  153.784 1.00 69.39  ? 430  GLU A O     1 
ATOM   3144 C  CB    . GLU A 1 430  ? 94.954  79.214  154.941 1.00 69.39  ? 430  GLU A CB    1 
ATOM   3145 C  CG    . GLU A 1 430  ? 94.233  78.419  153.868 1.00 69.39  ? 430  GLU A CG    1 
ATOM   3146 C  CD    . GLU A 1 430  ? 94.902  77.086  153.589 1.00 69.39  ? 430  GLU A CD    1 
ATOM   3147 O  OE1   . GLU A 1 430  ? 94.288  76.038  153.879 1.00 69.39  ? 430  GLU A OE1   1 
ATOM   3148 O  OE2   . GLU A 1 430  ? 96.043  77.086  153.082 1.00 69.39  ? 430  GLU A OE2   1 
ATOM   3149 N  N     . ILE A 1 431  ? 94.862  82.476  154.763 1.00 65.97  ? 431  ILE A N     1 
ATOM   3150 C  CA    . ILE A 1 431  ? 94.805  83.681  153.944 1.00 65.97  ? 431  ILE A CA    1 
ATOM   3151 C  C     . ILE A 1 431  ? 95.003  83.366  152.467 1.00 65.97  ? 431  ILE A C     1 
ATOM   3152 O  O     . ILE A 1 431  ? 94.544  84.123  151.604 1.00 65.97  ? 431  ILE A O     1 
ATOM   3153 C  CB    . ILE A 1 431  ? 95.828  84.713  154.473 1.00 65.97  ? 431  ILE A CB    1 
ATOM   3154 C  CG1   . ILE A 1 431  ? 95.439  85.147  155.886 1.00 65.97  ? 431  ILE A CG1   1 
ATOM   3155 C  CG2   . ILE A 1 431  ? 95.929  85.923  153.576 1.00 65.97  ? 431  ILE A CG2   1 
ATOM   3156 C  CD1   . ILE A 1 431  ? 96.482  85.970  156.583 1.00 65.97  ? 431  ILE A CD1   1 
ATOM   3157 N  N     . LYS A 1 432  ? 95.630  82.232  152.153 1.00 68.17  ? 432  LYS A N     1 
ATOM   3158 C  CA    . LYS A 1 432  ? 95.742  81.796  150.767 1.00 68.17  ? 432  LYS A CA    1 
ATOM   3159 C  C     . LYS A 1 432  ? 94.384  81.618  150.101 1.00 68.17  ? 432  LYS A C     1 
ATOM   3160 O  O     . LYS A 1 432  ? 94.304  81.660  148.869 1.00 68.17  ? 432  LYS A O     1 
ATOM   3161 C  CB    . LYS A 1 432  ? 96.523  80.485  150.695 1.00 68.17  ? 432  LYS A CB    1 
ATOM   3162 C  CG    . LYS A 1 432  ? 97.118  80.178  149.336 1.00 68.17  ? 432  LYS A CG    1 
ATOM   3163 C  CD    . LYS A 1 432  ? 98.198  79.118  149.437 1.00 68.17  ? 432  LYS A CD    1 
ATOM   3164 C  CE    . LYS A 1 432  ? 98.688  78.707  148.062 1.00 68.17  ? 432  LYS A CE    1 
ATOM   3165 N  NZ    . LYS A 1 432  ? 99.905  79.457  147.664 1.00 68.17  ? 432  LYS A NZ    1 
ATOM   3166 N  N     . THR A 1 433  ? 93.321  81.420  150.879 1.00 74.60  ? 433  THR A N     1 
ATOM   3167 C  CA    . THR A 1 433  ? 91.964  81.284  150.355 1.00 74.60  ? 433  THR A CA    1 
ATOM   3168 C  C     . THR A 1 433  ? 91.119  82.442  150.883 1.00 74.60  ? 433  THR A C     1 
ATOM   3169 O  O     . THR A 1 433  ? 90.572  82.371  151.987 1.00 74.60  ? 433  THR A O     1 
ATOM   3170 C  CB    . THR A 1 433  ? 91.361  79.937  150.740 1.00 74.60  ? 433  THR A CB    1 
ATOM   3171 O  OG1   . THR A 1 433  ? 92.133  78.884  150.149 1.00 74.60  ? 433  THR A OG1   1 
ATOM   3172 C  CG2   . THR A 1 433  ? 89.933  79.842  150.242 1.00 74.60  ? 433  THR A CG2   1 
ATOM   3173 N  N     . LEU A 1 434  ? 91.004  83.493  150.078 1.00 68.32  ? 434  LEU A N     1 
ATOM   3174 C  CA    . LEU A 1 434  ? 90.252  84.707  150.394 1.00 68.32  ? 434  LEU A CA    1 
ATOM   3175 C  C     . LEU A 1 434  ? 89.866  85.374  149.074 1.00 68.32  ? 434  LEU A C     1 
ATOM   3176 O  O     . LEU A 1 434  ? 89.799  84.714  148.032 1.00 68.32  ? 434  LEU A O     1 
ATOM   3177 C  CB    . LEU A 1 434  ? 91.059  85.647  151.308 1.00 68.32  ? 434  LEU A CB    1 
ATOM   3178 C  CG    . LEU A 1 434  ? 91.405  85.238  152.740 1.00 68.32  ? 434  LEU A CG    1 
ATOM   3179 C  CD1   . LEU A 1 434  ? 92.315  86.261  153.387 1.00 68.32  ? 434  LEU A CD1   1 
ATOM   3180 C  CD2   . LEU A 1 434  ? 90.129  85.084  153.546 1.00 68.32  ? 434  LEU A CD2   1 
ATOM   3181 N  N     . GLN A 1 435  ? 89.532  86.659  149.134 1.00 67.46  ? 435  GLN A N     1 
ATOM   3182 C  CA    . GLN A 1 435  ? 89.470  87.514  147.957 1.00 67.46  ? 435  GLN A CA    1 
ATOM   3183 C  C     . GLN A 1 435  ? 90.503  88.617  148.131 1.00 67.46  ? 435  GLN A C     1 
ATOM   3184 O  O     . GLN A 1 435  ? 90.530  89.283  149.171 1.00 67.46  ? 435  GLN A O     1 
ATOM   3185 C  CB    . GLN A 1 435  ? 88.071  88.106  147.758 1.00 67.46  ? 435  GLN A CB    1 
ATOM   3186 C  CG    . GLN A 1 435  ? 87.175  87.292  146.838 1.00 67.46  ? 435  GLN A CG    1 
ATOM   3187 C  CD    . GLN A 1 435  ? 85.970  88.075  146.355 1.00 67.46  ? 435  GLN A CD    1 
ATOM   3188 O  OE1   . GLN A 1 435  ? 85.714  89.189  146.812 1.00 67.46  ? 435  GLN A OE1   1 
ATOM   3189 N  NE2   . GLN A 1 435  ? 85.220  87.494  145.426 1.00 67.46  ? 435  GLN A NE2   1 
ATOM   3190 N  N     . LEU A 1 436  ? 91.360  88.795  147.122 1.00 55.57  ? 436  LEU A N     1 
ATOM   3191 C  CA    . LEU A 1 436  ? 92.468  89.738  147.249 1.00 55.57  ? 436  LEU A CA    1 
ATOM   3192 C  C     . LEU A 1 436  ? 91.966  91.154  147.497 1.00 55.57  ? 436  LEU A C     1 
ATOM   3193 O  O     . LEU A 1 436  ? 92.471  91.857  148.380 1.00 55.57  ? 436  LEU A O     1 
ATOM   3194 C  CB    . LEU A 1 436  ? 93.345  89.694  145.999 1.00 55.57  ? 436  LEU A CB    1 
ATOM   3195 C  CG    . LEU A 1 436  ? 94.518  88.718  146.045 1.00 55.57  ? 436  LEU A CG    1 
ATOM   3196 C  CD1   . LEU A 1 436  ? 95.200  88.653  144.692 1.00 55.57  ? 436  LEU A CD1   1 
ATOM   3197 C  CD2   . LEU A 1 436  ? 95.503  89.128  147.128 1.00 55.57  ? 436  LEU A CD2   1 
ATOM   3198 N  N     . LYS A 1 437  ? 90.971  91.592  146.726 1.00 54.18  ? 437  LYS A N     1 
ATOM   3199 C  CA    . LYS A 1 437  ? 90.404  92.918  146.947 1.00 54.18  ? 437  LYS A CA    1 
ATOM   3200 C  C     . LYS A 1 437  ? 89.751  93.007  148.320 1.00 54.18  ? 437  LYS A C     1 
ATOM   3201 O  O     . LYS A 1 437  ? 89.862  94.031  149.005 1.00 54.18  ? 437  LYS A O     1 
ATOM   3202 C  CB    . LYS A 1 437  ? 89.396  93.261  145.848 1.00 54.18  ? 437  LYS A CB    1 
ATOM   3203 C  CG    . LYS A 1 437  ? 89.978  93.340  144.438 1.00 54.18  ? 437  LYS A CG    1 
ATOM   3204 C  CD    . LYS A 1 437  ? 90.058  91.978  143.764 1.00 54.18  ? 437  LYS A CD    1 
ATOM   3205 C  CE    . LYS A 1 437  ? 90.920  92.029  142.514 1.00 54.18  ? 437  LYS A CE    1 
ATOM   3206 N  NZ    . LYS A 1 437  ? 91.158  90.671  141.951 1.00 54.18  ? 437  LYS A NZ    1 
ATOM   3207 N  N     . PHE A 1 438  ? 89.065  91.942  148.737 1.00 55.71  ? 438  PHE A N     1 
ATOM   3208 C  CA    . PHE A 1 438  ? 88.451  91.923  150.060 1.00 55.71  ? 438  PHE A CA    1 
ATOM   3209 C  C     . PHE A 1 438  ? 89.501  91.968  151.163 1.00 55.71  ? 438  PHE A C     1 
ATOM   3210 O  O     . PHE A 1 438  ? 89.340  92.689  152.154 1.00 55.71  ? 438  PHE A O     1 
ATOM   3211 C  CB    . PHE A 1 438  ? 87.574  90.680  150.207 1.00 55.71  ? 438  PHE A CB    1 
ATOM   3212 C  CG    . PHE A 1 438  ? 86.989  90.508  151.576 1.00 55.71  ? 438  PHE A CG    1 
ATOM   3213 C  CD1   . PHE A 1 438  ? 86.262  91.527  152.167 1.00 55.71  ? 438  PHE A CD1   1 
ATOM   3214 C  CD2   . PHE A 1 438  ? 87.166  89.326  152.273 1.00 55.71  ? 438  PHE A CD2   1 
ATOM   3215 C  CE1   . PHE A 1 438  ? 85.722  91.368  153.428 1.00 55.71  ? 438  PHE A CE1   1 
ATOM   3216 C  CE2   . PHE A 1 438  ? 86.630  89.163  153.533 1.00 55.71  ? 438  PHE A CE2   1 
ATOM   3217 C  CZ    . PHE A 1 438  ? 85.907  90.185  154.111 1.00 55.71  ? 438  PHE A CZ    1 
ATOM   3218 N  N     . LEU A 1 439  ? 90.582  91.202  151.011 1.00 50.25  ? 439  LEU A N     1 
ATOM   3219 C  CA    . LEU A 1 439  ? 91.575  91.100  152.075 1.00 50.25  ? 439  LEU A CA    1 
ATOM   3220 C  C     . LEU A 1 439  ? 92.304  92.420  152.290 1.00 50.25  ? 439  LEU A C     1 
ATOM   3221 O  O     . LEU A 1 439  ? 92.416  92.902  153.423 1.00 50.25  ? 439  LEU A O     1 
ATOM   3222 C  CB    . LEU A 1 439  ? 92.575  89.993  151.753 1.00 50.25  ? 439  LEU A CB    1 
ATOM   3223 C  CG    . LEU A 1 439  ? 93.826  89.991  152.630 1.00 50.25  ? 439  LEU A CG    1 
ATOM   3224 C  CD1   . LEU A 1 439  ? 93.477  89.788  154.099 1.00 50.25  ? 439  LEU A CD1   1 
ATOM   3225 C  CD2   . LEU A 1 439  ? 94.791  88.938  152.150 1.00 50.25  ? 439  LEU A CD2   1 
ATOM   3226 N  N     . ARG A 1 440  ? 92.814  93.018  151.211 1.00 42.37  ? 440  ARG A N     1 
ATOM   3227 C  CA    . ARG A 1 440  ? 93.596  94.241  151.342 1.00 42.37  ? 440  ARG A CA    1 
ATOM   3228 C  C     . ARG A 1 440  ? 92.768  95.399  151.878 1.00 42.37  ? 440  ARG A C     1 
ATOM   3229 O  O     . ARG A 1 440  ? 93.333  96.341  152.444 1.00 42.37  ? 440  ARG A O     1 
ATOM   3230 C  CB    . ARG A 1 440  ? 94.209  94.616  149.992 1.00 42.37  ? 440  ARG A CB    1 
ATOM   3231 C  CG    . ARG A 1 440  ? 95.042  93.512  149.360 1.00 42.37  ? 440  ARG A CG    1 
ATOM   3232 C  CD    . ARG A 1 440  ? 96.490  93.577  149.808 1.00 42.37  ? 440  ARG A CD    1 
ATOM   3233 N  NE    . ARG A 1 440  ? 97.331  92.627  149.084 1.00 42.37  ? 440  ARG A NE    1 
ATOM   3234 C  CZ    . ARG A 1 440  ? 97.778  92.813  147.847 1.00 42.37  ? 440  ARG A CZ    1 
ATOM   3235 N  NH1   . ARG A 1 440  ? 97.469  93.920  147.186 1.00 42.37  ? 440  ARG A NH1   1 
ATOM   3236 N  NH2   . ARG A 1 440  ? 98.539  91.894  147.270 1.00 42.37  ? 440  ARG A NH2   1 
ATOM   3237 N  N     . GLU A 1 441  ? 91.445  95.351  151.716 1.00 49.86  ? 441  GLU A N     1 
ATOM   3238 C  CA    . GLU A 1 441  ? 90.596  96.433  152.199 1.00 49.86  ? 441  GLU A CA    1 
ATOM   3239 C  C     . GLU A 1 441  ? 90.404  96.373  153.709 1.00 49.86  ? 441  GLU A C     1 
ATOM   3240 O  O     . GLU A 1 441  ? 90.328  97.420  154.359 1.00 49.86  ? 441  GLU A O     1 
ATOM   3241 C  CB    . GLU A 1 441  ? 89.253  96.401  151.453 1.00 49.86  ? 441  GLU A CB    1 
ATOM   3242 C  CG    . GLU A 1 441  ? 88.229  97.496  151.804 1.00 49.86  ? 441  GLU A CG    1 
ATOM   3243 C  CD    . GLU A 1 441  ? 87.521  97.300  153.138 1.00 49.86  ? 441  GLU A CD    1 
ATOM   3244 O  OE1   . GLU A 1 441  ? 86.832  98.241  153.585 1.00 49.86  ? 441  GLU A OE1   1 
ATOM   3245 O  OE2   . GLU A 1 441  ? 87.602  96.194  153.712 1.00 49.86  ? 441  GLU A OE2   1 
ATOM   3246 N  N     . GLN A 1 442  ? 90.324  95.172  154.282 1.00 48.56  ? 442  GLN A N     1 
ATOM   3247 C  CA    . GLN A 1 442  ? 90.057  95.026  155.708 1.00 48.56  ? 442  GLN A CA    1 
ATOM   3248 C  C     . GLN A 1 442  ? 91.255  95.358  156.586 1.00 48.56  ? 442  GLN A C     1 
ATOM   3249 O  O     . GLN A 1 442  ? 91.085  95.503  157.801 1.00 48.56  ? 442  GLN A O     1 
ATOM   3250 C  CB    . GLN A 1 442  ? 89.586  93.603  156.012 1.00 48.56  ? 442  GLN A CB    1 
ATOM   3251 C  CG    . GLN A 1 442  ? 88.407  93.157  155.175 1.00 48.56  ? 442  GLN A CG    1 
ATOM   3252 C  CD    . GLN A 1 442  ? 87.085  93.379  155.879 1.00 48.56  ? 442  GLN A CD    1 
ATOM   3253 O  OE1   . GLN A 1 442  ? 86.902  92.966  157.023 1.00 48.56  ? 442  GLN A OE1   1 
ATOM   3254 N  NE2   . GLN A 1 442  ? 86.156  94.041  155.199 1.00 48.56  ? 442  GLN A NE2   1 
ATOM   3255 N  N     . ILE A 1 443  ? 92.450  95.479  156.018 1.00 45.29  ? 443  ILE A N     1 
ATOM   3256 C  CA    . ILE A 1 443  ? 93.659  95.773  156.776 1.00 45.29  ? 443  ILE A CA    1 
ATOM   3257 C  C     . ILE A 1 443  ? 94.283  97.045  156.221 1.00 45.29  ? 443  ILE A C     1 
ATOM   3258 O  O     . ILE A 1 443  ? 94.473  97.173  155.006 1.00 45.29  ? 443  ILE A O     1 
ATOM   3259 C  CB    . ILE A 1 443  ? 94.652  94.596  156.739 1.00 45.29  ? 443  ILE A CB    1 
ATOM   3260 C  CG1   . ILE A 1 443  ? 94.916  94.145  155.303 1.00 45.29  ? 443  ILE A CG1   1 
ATOM   3261 C  CG2   . ILE A 1 443  ? 94.126  93.431  157.554 1.00 45.29  ? 443  ILE A CG2   1 
ATOM   3262 C  CD1   . ILE A 1 443  ? 95.902  93.007  155.203 1.00 45.29  ? 443  ILE A CD1   1 
ATOM   3263 N  N     . GLY A 1 444  ? 94.582  97.989  157.109 1.00 42.05  ? 444  GLY A N     1 
ATOM   3264 C  CA    . GLY A 1 444  ? 95.172  99.248  156.702 1.00 42.05  ? 444  GLY A CA    1 
ATOM   3265 C  C     . GLY A 1 444  ? 96.637  99.342  157.065 1.00 42.05  ? 444  GLY A C     1 
ATOM   3266 O  O     . GLY A 1 444  ? 96.986  99.486  158.240 1.00 42.05  ? 444  GLY A O     1 
ATOM   3267 N  N     . LEU A 1 445  ? 97.505  99.268  156.062 1.00 40.12  ? 445  LEU A N     1 
ATOM   3268 C  CA    . LEU A 1 445  ? 98.942  99.238  156.286 1.00 40.12  ? 445  LEU A CA    1 
ATOM   3269 C  C     . LEU A 1 445  ? 99.509  100.651 156.297 1.00 40.12  ? 445  LEU A C     1 
ATOM   3270 O  O     . LEU A 1 445  ? 99.113  101.501 155.494 1.00 40.12  ? 445  LEU A O     1 
ATOM   3271 C  CB    . LEU A 1 445  ? 99.628  98.393  155.208 1.00 40.12  ? 445  LEU A CB    1 
ATOM   3272 C  CG    . LEU A 1 445  ? 101.120 98.066  155.325 1.00 40.12  ? 445  LEU A CG    1 
ATOM   3273 C  CD1   . LEU A 1 445  ? 101.407 96.769  154.600 1.00 40.12  ? 445  LEU A CD1   1 
ATOM   3274 C  CD2   . LEU A 1 445  ? 101.989 99.168  154.749 1.00 40.12  ? 445  LEU A CD2   1 
ATOM   3275 N  N     . VAL A 1 446  ? 100.438 100.894 157.216 1.00 37.45  ? 446  VAL A N     1 
ATOM   3276 C  CA    . VAL A 1 446  ? 101.179 102.147 157.293 1.00 37.45  ? 446  VAL A CA    1 
ATOM   3277 C  C     . VAL A 1 446  ? 102.635 101.837 156.981 1.00 37.45  ? 446  VAL A C     1 
ATOM   3278 O  O     . VAL A 1 446  ? 103.249 100.988 157.638 1.00 37.45  ? 446  VAL A O     1 
ATOM   3279 C  CB    . VAL A 1 446  ? 101.037 102.809 158.671 1.00 37.45  ? 446  VAL A CB    1 
ATOM   3280 C  CG1   . VAL A 1 446  ? 101.770 104.140 158.698 1.00 37.45  ? 446  VAL A CG1   1 
ATOM   3281 C  CG2   . VAL A 1 446  ? 99.572  102.993 159.019 1.00 37.45  ? 446  VAL A CG2   1 
ATOM   3282 N  N     . ASN A 1 447  ? 103.185 102.514 155.977 1.00 41.93  ? 447  ASN A N     1 
ATOM   3283 C  CA    . ASN A 1 447  ? 104.557 102.259 155.567 1.00 41.93  ? 447  ASN A CA    1 
ATOM   3284 C  C     . ASN A 1 447  ? 105.540 102.708 156.642 1.00 41.93  ? 447  ASN A C     1 
ATOM   3285 O  O     . ASN A 1 447  ? 105.265 103.620 157.426 1.00 41.93  ? 447  ASN A O     1 
ATOM   3286 C  CB    . ASN A 1 447  ? 104.865 102.977 154.255 1.00 41.93  ? 447  ASN A CB    1 
ATOM   3287 C  CG    . ASN A 1 447  ? 104.706 102.079 153.048 1.00 41.93  ? 447  ASN A CG    1 
ATOM   3288 O  OD1   . ASN A 1 447  ? 103.937 101.119 153.071 1.00 41.93  ? 447  ASN A OD1   1 
ATOM   3289 N  ND2   . ASN A 1 447  ? 105.437 102.384 151.983 1.00 41.93  ? 447  ASN A ND2   1 
ATOM   3290 N  N     . GLN A 1 448  ? 106.697 102.043 156.679 1.00 45.23  ? 448  GLN A N     1 
ATOM   3291 C  CA    . GLN A 1 448  ? 107.771 102.484 157.562 1.00 45.23  ? 448  GLN A CA    1 
ATOM   3292 C  C     . GLN A 1 448  ? 108.240 103.881 157.182 1.00 45.23  ? 448  GLN A C     1 
ATOM   3293 O  O     . GLN A 1 448  ? 108.361 104.767 158.036 1.00 45.23  ? 448  GLN A O     1 
ATOM   3294 C  CB    . GLN A 1 448  ? 108.933 101.492 157.511 1.00 45.23  ? 448  GLN A CB    1 
ATOM   3295 C  CG    . GLN A 1 448  ? 110.268 102.083 157.939 1.00 45.23  ? 448  GLN A CG    1 
ATOM   3296 C  CD    . GLN A 1 448  ? 111.213 101.044 158.510 1.00 45.23  ? 448  GLN A CD    1 
ATOM   3297 O  OE1   . GLN A 1 448  ? 111.224 99.892  158.075 1.00 45.23  ? 448  GLN A OE1   1 
ATOM   3298 N  NE2   . GLN A 1 448  ? 112.009 101.446 159.494 1.00 45.23  ? 448  GLN A NE2   1 
ATOM   3299 N  N     . GLU A 1 449  ? 108.506 104.096 155.900 1.00 43.63  ? 449  GLU A N     1 
ATOM   3300 C  CA    . GLU A 1 449  ? 108.823 105.418 155.365 1.00 43.63  ? 449  GLU A CA    1 
ATOM   3301 C  C     . GLU A 1 449  ? 107.787 105.772 154.311 1.00 43.63  ? 449  GLU A C     1 
ATOM   3302 O  O     . GLU A 1 449  ? 107.816 105.198 153.205 1.00 43.63  ? 449  GLU A O     1 
ATOM   3303 C  CB    . GLU A 1 449  ? 110.231 105.447 154.773 1.00 43.63  ? 449  GLU A CB    1 
ATOM   3304 C  CG    . GLU A 1 449  ? 111.327 105.129 155.775 1.00 43.63  ? 449  GLU A CG    1 
ATOM   3305 C  CD    . GLU A 1 449  ? 111.153 105.872 157.085 1.00 43.63  ? 449  GLU A CD    1 
ATOM   3306 O  OE1   . GLU A 1 449  ? 111.198 105.220 158.149 1.00 43.63  ? 449  GLU A OE1   1 
ATOM   3307 O  OE2   . GLU A 1 449  ? 110.974 107.108 157.053 1.00 43.63  ? 449  GLU A OE2   1 
ATOM   3308 N  N     . PRO A 1 450  ? 106.858 106.683 154.597 1.00 33.86  ? 450  PRO A N     1 
ATOM   3309 C  CA    . PRO A 1 450  ? 105.773 106.955 153.648 1.00 33.86  ? 450  PRO A CA    1 
ATOM   3310 C  C     . PRO A 1 450  ? 106.295 107.467 152.314 1.00 33.86  ? 450  PRO A C     1 
ATOM   3311 O  O     . PRO A 1 450  ? 107.283 108.202 152.244 1.00 33.86  ? 450  PRO A O     1 
ATOM   3312 C  CB    . PRO A 1 450  ? 104.933 108.020 154.364 1.00 33.86  ? 450  PRO A CB    1 
ATOM   3313 C  CG    . PRO A 1 450  ? 105.294 107.887 155.810 1.00 33.86  ? 450  PRO A CG    1 
ATOM   3314 C  CD    . PRO A 1 450  ? 106.731 107.478 155.828 1.00 33.86  ? 450  PRO A CD    1 
ATOM   3315 N  N     . ALA A 1 451  ? 105.614 107.063 151.246 1.00 33.31  ? 451  ALA A N     1 
ATOM   3316 C  CA    . ALA A 1 451  ? 105.968 107.431 149.879 1.00 33.31  ? 451  ALA A CA    1 
ATOM   3317 C  C     . ALA A 1 451  ? 104.788 108.185 149.274 1.00 33.31  ? 451  ALA A C     1 
ATOM   3318 O  O     . ALA A 1 451  ? 103.915 107.589 148.639 1.00 33.31  ? 451  ALA A O     1 
ATOM   3319 C  CB    . ALA A 1 451  ? 106.325 106.198 149.058 1.00 33.31  ? 451  ALA A CB    1 
ATOM   3320 N  N     . LEU A 1 452  ? 104.766 109.498 149.474 1.00 30.84  ? 452  LEU A N     1 
ATOM   3321 C  CA    . LEU A 1 452  ? 103.691 110.317 148.933 1.00 30.84  ? 452  LEU A CA    1 
ATOM   3322 C  C     . LEU A 1 452  ? 103.875 110.504 147.433 1.00 30.84  ? 452  LEU A C     1 
ATOM   3323 O  O     . LEU A 1 452  ? 104.974 110.807 146.963 1.00 30.84  ? 452  LEU A O     1 
ATOM   3324 C  CB    . LEU A 1 452  ? 103.649 111.675 149.632 1.00 30.84  ? 452  LEU A CB    1 
ATOM   3325 C  CG    . LEU A 1 452  ? 102.883 111.775 150.954 1.00 30.84  ? 452  LEU A CG    1 
ATOM   3326 C  CD1   . LEU A 1 452  ? 101.424 111.402 150.743 1.00 30.84  ? 452  LEU A CD1   1 
ATOM   3327 C  CD2   . LEU A 1 452  ? 103.512 110.928 152.051 1.00 30.84  ? 452  LEU A CD2   1 
ATOM   3328 N  N     . PHE A 1 453  ? 102.795 110.321 146.680 1.00 27.87  ? 453  PHE A N     1 
ATOM   3329 C  CA    . PHE A 1 453  ? 102.842 110.523 145.242 1.00 27.87  ? 453  PHE A CA    1 
ATOM   3330 C  C     . PHE A 1 453  ? 102.910 112.016 144.919 1.00 27.87  ? 453  PHE A C     1 
ATOM   3331 O  O     . PHE A 1 453  ? 102.713 112.879 145.779 1.00 27.87  ? 453  PHE A O     1 
ATOM   3332 C  CB    . PHE A 1 453  ? 101.626 109.888 144.570 1.00 27.87  ? 453  PHE A CB    1 
ATOM   3333 C  CG    . PHE A 1 453  ? 101.569 108.389 144.692 1.00 27.87  ? 453  PHE A CG    1 
ATOM   3334 C  CD1   . PHE A 1 453  ? 101.249 107.785 145.896 1.00 27.87  ? 453  PHE A CD1   1 
ATOM   3335 C  CD2   . PHE A 1 453  ? 101.819 107.585 143.595 1.00 27.87  ? 453  PHE A CD2   1 
ATOM   3336 C  CE1   . PHE A 1 453  ? 101.190 106.412 146.005 1.00 27.87  ? 453  PHE A CE1   1 
ATOM   3337 C  CE2   . PHE A 1 453  ? 101.761 106.210 143.699 1.00 27.87  ? 453  PHE A CE2   1 
ATOM   3338 C  CZ    . PHE A 1 453  ? 101.446 105.623 144.906 1.00 27.87  ? 453  PHE A CZ    1 
ATOM   3339 N  N     . ALA A 1 454  ? 103.195 112.319 143.652 1.00 28.06  ? 454  ALA A N     1 
ATOM   3340 C  CA    . ALA A 1 454  ? 103.295 113.703 143.188 1.00 28.06  ? 454  ALA A CA    1 
ATOM   3341 C  C     . ALA A 1 454  ? 101.897 114.206 142.840 1.00 28.06  ? 454  ALA A C     1 
ATOM   3342 O  O     . ALA A 1 454  ? 101.499 114.304 141.676 1.00 28.06  ? 454  ALA A O     1 
ATOM   3343 C  CB    . ALA A 1 454  ? 104.244 113.807 142.001 1.00 28.06  ? 454  ALA A CB    1 
ATOM   3344 N  N     . THR A 1 455  ? 101.138 114.529 143.884 1.00 28.25  ? 455  THR A N     1 
ATOM   3345 C  CA    . THR A 1 455  ? 99.769  115.000 143.734 1.00 28.25  ? 455  THR A CA    1 
ATOM   3346 C  C     . THR A 1 455  ? 99.425  115.786 144.994 1.00 28.25  ? 455  THR A C     1 
ATOM   3347 O  O     . THR A 1 455  ? 100.091 115.652 146.023 1.00 28.25  ? 455  THR A O     1 
ATOM   3348 C  CB    . THR A 1 455  ? 98.805  113.823 143.503 1.00 28.25  ? 455  THR A CB    1 
ATOM   3349 O  OG1   . THR A 1 455  ? 99.192  113.121 142.315 1.00 28.25  ? 455  THR A OG1   1 
ATOM   3350 C  CG2   . THR A 1 455  ? 97.378  114.300 143.294 1.00 28.25  ? 455  THR A CG2   1 
ATOM   3351 N  N     . THR A 1 456  ? 98.389  116.619 144.897 1.00 25.93  ? 456  THR A N     1 
ATOM   3352 C  CA    . THR A 1 456  ? 97.993  117.488 145.997 1.00 25.93  ? 456  THR A CA    1 
ATOM   3353 C  C     . THR A 1 456  ? 97.695  116.686 147.265 1.00 25.93  ? 456  THR A C     1 
ATOM   3354 O  O     . THR A 1 456  ? 97.489  115.471 147.237 1.00 25.93  ? 456  THR A O     1 
ATOM   3355 C  CB    . THR A 1 456  ? 96.765  118.309 145.611 1.00 25.93  ? 456  THR A CB    1 
ATOM   3356 O  OG1   . THR A 1 456  ? 95.592  117.495 145.724 1.00 25.93  ? 456  THR A OG1   1 
ATOM   3357 C  CG2   . THR A 1 456  ? 96.888  118.802 144.180 1.00 25.93  ? 456  THR A CG2   1 
ATOM   3358 N  N     . ILE A 1 457  ? 97.669  117.401 148.393 1.00 22.77  ? 457  ILE A N     1 
ATOM   3359 C  CA    . ILE A 1 457  ? 97.468  116.765 149.693 1.00 22.77  ? 457  ILE A CA    1 
ATOM   3360 C  C     . ILE A 1 457  ? 96.106  116.088 149.761 1.00 22.77  ? 457  ILE A C     1 
ATOM   3361 O  O     . ILE A 1 457  ? 95.980  114.952 150.239 1.00 22.77  ? 457  ILE A O     1 
ATOM   3362 C  CB    . ILE A 1 457  ? 97.633  117.803 150.818 1.00 22.77  ? 457  ILE A CB    1 
ATOM   3363 C  CG1   . ILE A 1 457  ? 99.080  118.287 150.899 1.00 22.77  ? 457  ILE A CG1   1 
ATOM   3364 C  CG2   . ILE A 1 457  ? 97.178  117.228 152.148 1.00 22.77  ? 457  ILE A CG2   1 
ATOM   3365 C  CD1   . ILE A 1 457  ? 99.988  117.360 151.668 1.00 22.77  ? 457  ILE A CD1   1 
ATOM   3366 N  N     . LEU A 1 458  ? 95.063  116.779 149.295 1.00 26.26  ? 458  LEU A N     1 
ATOM   3367 C  CA    . LEU A 1 458  ? 93.709  116.250 149.418 1.00 26.26  ? 458  LEU A CA    1 
ATOM   3368 C  C     . LEU A 1 458  ? 93.552  114.944 148.652 1.00 26.26  ? 458  LEU A C     1 
ATOM   3369 O  O     . LEU A 1 458  ? 92.973  113.981 149.164 1.00 26.26  ? 458  LEU A O     1 
ATOM   3370 C  CB    . LEU A 1 458  ? 92.699  117.288 148.932 1.00 26.26  ? 458  LEU A CB    1 
ATOM   3371 C  CG    . LEU A 1 458  ? 91.223  116.997 149.198 1.00 26.26  ? 458  LEU A CG    1 
ATOM   3372 C  CD1   . LEU A 1 458  ? 90.520  118.254 149.674 1.00 26.26  ? 458  LEU A CD1   1 
ATOM   3373 C  CD2   . LEU A 1 458  ? 90.555  116.461 147.944 1.00 26.26  ? 458  LEU A CD2   1 
ATOM   3374 N  N     . GLU A 1 459  ? 94.076  114.881 147.429 1.00 28.47  ? 459  GLU A N     1 
ATOM   3375 C  CA    . GLU A 1 459  ? 93.974  113.647 146.658 1.00 28.47  ? 459  GLU A CA    1 
ATOM   3376 C  C     . GLU A 1 459  ? 94.822  112.542 147.283 1.00 28.47  ? 459  GLU A C     1 
ATOM   3377 O  O     . GLU A 1 459  ? 94.429  111.365 147.261 1.00 28.47  ? 459  GLU A O     1 
ATOM   3378 C  CB    . GLU A 1 459  ? 94.353  113.943 145.202 1.00 28.47  ? 459  GLU A CB    1 
ATOM   3379 C  CG    . GLU A 1 459  ? 94.056  112.862 144.166 1.00 28.47  ? 459  GLU A CG    1 
ATOM   3380 C  CD    . GLU A 1 459  ? 95.006  111.690 144.207 1.00 28.47  ? 459  GLU A CD    1 
ATOM   3381 O  OE1   . GLU A 1 459  ? 94.717  110.678 143.536 1.00 28.47  ? 459  GLU A OE1   1 
ATOM   3382 O  OE2   . GLU A 1 459  ? 96.064  111.798 144.860 1.00 28.47  ? 459  GLU A OE2   1 
ATOM   3383 N  N     . ASN A 1 460  ? 95.966  112.905 147.873 1.00 27.09  ? 460  ASN A N     1 
ATOM   3384 C  CA    . ASN A 1 460  ? 96.770  111.931 148.605 1.00 27.09  ? 460  ASN A CA    1 
ATOM   3385 C  C     . ASN A 1 460  ? 95.973  111.309 149.743 1.00 27.09  ? 460  ASN A C     1 
ATOM   3386 O  O     . ASN A 1 460  ? 96.040  110.096 149.967 1.00 27.09  ? 460  ASN A O     1 
ATOM   3387 C  CB    . ASN A 1 460  ? 98.036  112.592 149.149 1.00 27.09  ? 460  ASN A CB    1 
ATOM   3388 C  CG    . ASN A 1 460  ? 99.173  112.588 148.153 1.00 27.09  ? 460  ASN A CG    1 
ATOM   3389 O  OD1   . ASN A 1 460  ? 99.731  111.539 147.836 1.00 27.09  ? 460  ASN A OD1   1 
ATOM   3390 N  ND2   . ASN A 1 460  ? 99.525  113.765 147.652 1.00 27.09  ? 460  ASN A ND2   1 
ATOM   3391 N  N     . ILE A 1 461  ? 95.221  112.126 150.481 1.00 25.20  ? 461  ILE A N     1 
ATOM   3392 C  CA    . ILE A 1 461  ? 94.360  111.581 151.526 1.00 25.20  ? 461  ILE A CA    1 
ATOM   3393 C  C     . ILE A 1 461  ? 93.244  110.742 150.912 1.00 25.20  ? 461  ILE A C     1 
ATOM   3394 O  O     . ILE A 1 461  ? 92.846  109.712 151.467 1.00 25.20  ? 461  ILE A O     1 
ATOM   3395 C  CB    . ILE A 1 461  ? 93.806  112.712 152.410 1.00 25.20  ? 461  ILE A CB    1 
ATOM   3396 C  CG1   . ILE A 1 461  ? 94.950  113.531 153.006 1.00 25.20  ? 461  ILE A CG1   1 
ATOM   3397 C  CG2   . ILE A 1 461  ? 92.949  112.146 153.526 1.00 25.20  ? 461  ILE A CG2   1 
ATOM   3398 C  CD1   . ILE A 1 461  ? 94.497  114.799 153.692 1.00 25.20  ? 461  ILE A CD1   1 
ATOM   3399 N  N     . LEU A 1 462  ? 92.732  111.160 149.751 1.00 29.62  ? 462  LEU A N     1 
ATOM   3400 C  CA    . LEU A 1 462  ? 91.673  110.410 149.082 1.00 29.62  ? 462  LEU A CA    1 
ATOM   3401 C  C     . LEU A 1 462  ? 92.155  109.085 148.506 1.00 29.62  ? 462  LEU A C     1 
ATOM   3402 O  O     . LEU A 1 462  ? 91.326  108.300 148.033 1.00 29.62  ? 462  LEU A O     1 
ATOM   3403 C  CB    . LEU A 1 462  ? 91.035  111.245 147.972 1.00 29.62  ? 462  LEU A CB    1 
ATOM   3404 C  CG    . LEU A 1 462  ? 89.742  111.979 148.330 1.00 29.62  ? 462  LEU A CG    1 
ATOM   3405 C  CD1   . LEU A 1 462  ? 89.995  113.132 149.276 1.00 29.62  ? 462  LEU A CD1   1 
ATOM   3406 C  CD2   . LEU A 1 462  ? 89.044  112.463 147.067 1.00 29.62  ? 462  LEU A CD2   1 
ATOM   3407 N  N     . TYR A 1 463  ? 93.463  108.829 148.508 1.00 31.13  ? 463  TYR A N     1 
ATOM   3408 C  CA    . TYR A 1 463  ? 93.958  107.489 148.194 1.00 31.13  ? 463  TYR A CA    1 
ATOM   3409 C  C     . TYR A 1 463  ? 93.266  106.407 149.015 1.00 31.13  ? 463  TYR A C     1 
ATOM   3410 O  O     . TYR A 1 463  ? 92.960  105.331 148.493 1.00 31.13  ? 463  TYR A O     1 
ATOM   3411 C  CB    . TYR A 1 463  ? 95.467  107.403 148.417 1.00 31.13  ? 463  TYR A CB    1 
ATOM   3412 C  CG    . TYR A 1 463  ? 96.280  108.042 147.326 1.00 31.13  ? 463  TYR A CG    1 
ATOM   3413 C  CD1   . TYR A 1 463  ? 95.736  108.249 146.069 1.00 31.13  ? 463  TYR A CD1   1 
ATOM   3414 C  CD2   . TYR A 1 463  ? 97.580  108.463 147.557 1.00 31.13  ? 463  TYR A CD2   1 
ATOM   3415 C  CE1   . TYR A 1 463  ? 96.472  108.826 145.064 1.00 31.13  ? 463  TYR A CE1   1 
ATOM   3416 C  CE2   . TYR A 1 463  ? 98.319  109.057 146.559 1.00 31.13  ? 463  TYR A CE2   1 
ATOM   3417 C  CZ    . TYR A 1 463  ? 97.760  109.237 145.313 1.00 31.13  ? 463  TYR A CZ    1 
ATOM   3418 O  OH    . TYR A 1 463  ? 98.488  109.826 144.307 1.00 31.13  ? 463  TYR A OH    1 
ATOM   3419 N  N     . GLY A 1 464  ? 93.025  106.675 150.296 1.00 32.91  ? 464  GLY A N     1 
ATOM   3420 C  CA    . GLY A 1 464  ? 92.393  105.699 151.162 1.00 32.91  ? 464  GLY A CA    1 
ATOM   3421 C  C     . GLY A 1 464  ? 91.001  105.303 150.716 1.00 32.91  ? 464  GLY A C     1 
ATOM   3422 O  O     . GLY A 1 464  ? 90.776  104.160 150.309 1.00 32.91  ? 464  GLY A O     1 
ATOM   3423 N  N     . LYS A 1 465  ? 90.058  106.238 150.789 1.00 35.26  ? 465  LYS A N     1 
ATOM   3424 C  CA    . LYS A 1 465  ? 88.678  106.004 150.364 1.00 35.26  ? 465  LYS A CA    1 
ATOM   3425 C  C     . LYS A 1 465  ? 88.311  107.012 149.286 1.00 35.26  ? 465  LYS A C     1 
ATOM   3426 O  O     . LYS A 1 465  ? 88.052  108.189 149.597 1.00 35.26  ? 465  LYS A O     1 
ATOM   3427 C  CB    . LYS A 1 465  ? 87.719  106.107 151.547 1.00 35.26  ? 465  LYS A CB    1 
ATOM   3428 C  CG    . LYS A 1 465  ? 86.270  105.812 151.204 1.00 35.26  ? 465  LYS A CG    1 
ATOM   3429 C  CD    . LYS A 1 465  ? 85.523  105.275 152.412 1.00 35.26  ? 465  LYS A CD    1 
ATOM   3430 C  CE    . LYS A 1 465  ? 84.791  106.389 153.143 1.00 35.26  ? 465  LYS A CE    1 
ATOM   3431 N  NZ    . LYS A 1 465  ? 84.389  105.983 154.518 1.00 35.26  ? 465  LYS A NZ    1 
ATOM   3432 N  N     . PRO A 1 466  ? 88.275  106.611 148.013 1.00 36.31  ? 466  PRO A N     1 
ATOM   3433 C  CA    . PRO A 1 466  ? 87.979  107.581 146.946 1.00 36.31  ? 466  PRO A CA    1 
ATOM   3434 C  C     . PRO A 1 466  ? 86.575  108.159 147.007 1.00 36.31  ? 466  PRO A C     1 
ATOM   3435 O  O     . PRO A 1 466  ? 86.322  109.186 146.366 1.00 36.31  ? 466  PRO A O     1 
ATOM   3436 C  CB    . PRO A 1 466  ? 88.191  106.768 145.662 1.00 36.31  ? 466  PRO A CB    1 
ATOM   3437 C  CG    . PRO A 1 466  ? 88.001  105.349 146.077 1.00 36.31  ? 466  PRO A CG    1 
ATOM   3438 C  CD    . PRO A 1 466  ? 88.504  105.256 147.487 1.00 36.31  ? 466  PRO A CD    1 
ATOM   3439 N  N     . ASP A 1 467  ? 85.660  107.545 147.753 1.00 43.20  ? 467  ASP A N     1 
ATOM   3440 C  CA    . ASP A 1 467  ? 84.268  107.987 147.822 1.00 43.20  ? 467  ASP A CA    1 
ATOM   3441 C  C     . ASP A 1 467  ? 83.981  108.769 149.096 1.00 43.20  ? 467  ASP A C     1 
ATOM   3442 O  O     . ASP A 1 467  ? 82.900  108.650 149.680 1.00 43.20  ? 467  ASP A O     1 
ATOM   3443 C  CB    . ASP A 1 467  ? 83.329  106.791 147.705 1.00 43.20  ? 467  ASP A CB    1 
ATOM   3444 C  CG    . ASP A 1 467  ? 83.379  106.141 146.336 1.00 43.20  ? 467  ASP A CG    1 
ATOM   3445 O  OD1   . ASP A 1 467  ? 83.038  106.818 145.343 1.00 43.20  ? 467  ASP A OD1   1 
ATOM   3446 O  OD2   . ASP A 1 467  ? 83.759  104.954 146.252 1.00 43.20  ? 467  ASP A OD2   1 
ATOM   3447 N  N     . ALA A 1 468  ? 84.934  109.576 149.550 1.00 41.89  ? 468  ALA A N     1 
ATOM   3448 C  CA    . ALA A 1 468  ? 84.791  110.367 150.764 1.00 41.89  ? 468  ALA A CA    1 
ATOM   3449 C  C     . ALA A 1 468  ? 84.614  111.833 150.399 1.00 41.89  ? 468  ALA A C     1 
ATOM   3450 O  O     . ALA A 1 468  ? 85.349  112.361 149.558 1.00 41.89  ? 468  ALA A O     1 
ATOM   3451 C  CB    . ALA A 1 468  ? 86.005  110.191 151.678 1.00 41.89  ? 468  ALA A CB    1 
ATOM   3452 N  N     . THR A 1 469  ? 83.639  112.484 151.028 1.00 44.58  ? 469  THR A N     1 
ATOM   3453 C  CA    . THR A 1 469  ? 83.385  113.898 150.789 1.00 44.58  ? 469  THR A CA    1 
ATOM   3454 C  C     . THR A 1 469  ? 84.370  114.735 151.603 1.00 44.58  ? 469  THR A C     1 
ATOM   3455 O  O     . THR A 1 469  ? 85.298  114.217 152.229 1.00 44.58  ? 469  THR A O     1 
ATOM   3456 C  CB    . THR A 1 469  ? 81.935  114.242 151.118 1.00 44.58  ? 469  THR A CB    1 
ATOM   3457 O  OG1   . THR A 1 469  ? 81.682  113.982 152.504 1.00 44.58  ? 469  THR A OG1   1 
ATOM   3458 C  CG2   . THR A 1 469  ? 80.986  113.410 150.271 1.00 44.58  ? 469  THR A CG2   1 
ATOM   3459 N  N     . MET A 1 470  ? 84.172  116.055 151.604 1.00 41.69  ? 470  MET A N     1 
ATOM   3460 C  CA    . MET A 1 470  ? 85.105  116.944 152.287 1.00 41.69  ? 470  MET A CA    1 
ATOM   3461 C  C     . MET A 1 470  ? 85.049  116.780 153.801 1.00 41.69  ? 470  MET A C     1 
ATOM   3462 O  O     . MET A 1 470  ? 86.080  116.900 154.471 1.00 41.69  ? 470  MET A O     1 
ATOM   3463 C  CB    . MET A 1 470  ? 84.819  118.395 151.900 1.00 41.69  ? 470  MET A CB    1 
ATOM   3464 C  CG    . MET A 1 470  ? 85.757  119.410 152.532 1.00 41.69  ? 470  MET A CG    1 
ATOM   3465 S  SD    . MET A 1 470  ? 87.494  119.062 152.200 1.00 41.69  ? 470  MET A SD    1 
ATOM   3466 C  CE    . MET A 1 470  ? 88.276  120.455 153.010 1.00 41.69  ? 470  MET A CE    1 
ATOM   3467 N  N     . VAL A 1 471  ? 83.865  116.511 154.355 1.00 41.93  ? 471  VAL A N     1 
ATOM   3468 C  CA    . VAL A 1 471  ? 83.725  116.428 155.806 1.00 41.93  ? 471  VAL A CA    1 
ATOM   3469 C  C     . VAL A 1 471  ? 84.516  115.249 156.363 1.00 41.93  ? 471  VAL A C     1 
ATOM   3470 O  O     . VAL A 1 471  ? 85.191  115.371 157.393 1.00 41.93  ? 471  VAL A O     1 
ATOM   3471 C  CB    . VAL A 1 471  ? 82.238  116.347 156.194 1.00 41.93  ? 471  VAL A CB    1 
ATOM   3472 C  CG1   . VAL A 1 471  ? 82.089  116.267 157.705 1.00 41.93  ? 471  VAL A CG1   1 
ATOM   3473 C  CG2   . VAL A 1 471  ? 81.483  117.544 155.641 1.00 41.93  ? 471  VAL A CG2   1 
ATOM   3474 N  N     . GLU A 1 472  ? 84.440  114.090 155.703 1.00 41.64  ? 472  GLU A N     1 
ATOM   3475 C  CA    . GLU A 1 472  ? 85.179  112.922 156.176 1.00 41.64  ? 472  GLU A CA    1 
ATOM   3476 C  C     . GLU A 1 472  ? 86.682  113.158 156.119 1.00 41.64  ? 472  GLU A C     1 
ATOM   3477 O  O     . GLU A 1 472  ? 87.413  112.791 157.048 1.00 41.64  ? 472  GLU A O     1 
ATOM   3478 C  CB    . GLU A 1 472  ? 84.800  111.691 155.354 1.00 41.64  ? 472  GLU A CB    1 
ATOM   3479 C  CG    . GLU A 1 472  ? 83.410  111.151 155.645 1.00 41.64  ? 472  GLU A CG    1 
ATOM   3480 C  CD    . GLU A 1 472  ? 82.340  111.814 154.803 1.00 41.64  ? 472  GLU A CD    1 
ATOM   3481 O  OE1   . GLU A 1 472  ? 82.688  112.691 153.985 1.00 41.64  ? 472  GLU A OE1   1 
ATOM   3482 O  OE2   . GLU A 1 472  ? 81.153  111.459 154.958 1.00 41.64  ? 472  GLU A OE2   1 
ATOM   3483 N  N     . VAL A 1 473  ? 87.163  113.768 155.034 1.00 36.62  ? 473  VAL A N     1 
ATOM   3484 C  CA    . VAL A 1 473  ? 88.589  114.054 154.908 1.00 36.62  ? 473  VAL A CA    1 
ATOM   3485 C  C     . VAL A 1 473  ? 89.031  115.038 155.980 1.00 36.62  ? 473  VAL A C     1 
ATOM   3486 O  O     . VAL A 1 473  ? 90.105  114.889 156.575 1.00 36.62  ? 473  VAL A O     1 
ATOM   3487 C  CB    . VAL A 1 473  ? 88.905  114.575 153.495 1.00 36.62  ? 473  VAL A CB    1 
ATOM   3488 C  CG1   . VAL A 1 473  ? 90.390  114.853 153.354 1.00 36.62  ? 473  VAL A CG1   1 
ATOM   3489 C  CG2   . VAL A 1 473  ? 88.449  113.572 152.458 1.00 36.62  ? 473  VAL A CG2   1 
ATOM   3490 N  N     . GLU A 1 474  ? 88.217  116.063 156.240 1.00 36.59  ? 474  GLU A N     1 
ATOM   3491 C  CA    . GLU A 1 474  ? 88.556  117.027 157.280 1.00 36.59  ? 474  GLU A CA    1 
ATOM   3492 C  C     . GLU A 1 474  ? 88.601  116.366 158.651 1.00 36.59  ? 474  GLU A C     1 
ATOM   3493 O  O     . GLU A 1 474  ? 89.495  116.651 159.456 1.00 36.59  ? 474  GLU A O     1 
ATOM   3494 C  CB    . GLU A 1 474  ? 87.556  118.181 157.274 1.00 36.59  ? 474  GLU A CB    1 
ATOM   3495 C  CG    . GLU A 1 474  ? 87.946  119.343 158.174 1.00 36.59  ? 474  GLU A CG    1 
ATOM   3496 C  CD    . GLU A 1 474  ? 89.205  120.048 157.709 1.00 36.59  ? 474  GLU A CD    1 
ATOM   3497 O  OE1   . GLU A 1 474  ? 90.314  119.565 158.021 1.00 36.59  ? 474  GLU A OE1   1 
ATOM   3498 O  OE2   . GLU A 1 474  ? 89.086  121.090 157.031 1.00 36.59  ? 474  GLU A OE2   1 
ATOM   3499 N  N     . ALA A 1 475  ? 87.644  115.479 158.936 1.00 37.31  ? 475  ALA A N     1 
ATOM   3500 C  CA    . ALA A 1 475  ? 87.647  114.775 160.215 1.00 37.31  ? 475  ALA A CA    1 
ATOM   3501 C  C     . ALA A 1 475  ? 88.879  113.891 160.356 1.00 37.31  ? 475  ALA A C     1 
ATOM   3502 O  O     . ALA A 1 475  ? 89.506  113.851 161.422 1.00 37.31  ? 475  ALA A O     1 
ATOM   3503 C  CB    . ALA A 1 475  ? 86.372  113.947 160.361 1.00 37.31  ? 475  ALA A CB    1 
ATOM   3504 N  N     . ALA A 1 476  ? 89.243  113.175 159.289 1.00 35.77  ? 476  ALA A N     1 
ATOM   3505 C  CA    . ALA A 1 476  ? 90.433  112.332 159.336 1.00 35.77  ? 476  ALA A CA    1 
ATOM   3506 C  C     . ALA A 1 476  ? 91.692  113.163 159.544 1.00 35.77  ? 476  ALA A C     1 
ATOM   3507 O  O     . ALA A 1 476  ? 92.572  112.786 160.326 1.00 35.77  ? 476  ALA A O     1 
ATOM   3508 C  CB    . ALA A 1 476  ? 90.542  111.503 158.058 1.00 35.77  ? 476  ALA A CB    1 
ATOM   3509 N  N     . ALA A 1 477  ? 91.797  114.298 158.850 1.00 34.64  ? 477  ALA A N     1 
ATOM   3510 C  CA    . ALA A 1 477  ? 92.963  115.159 159.013 1.00 34.64  ? 477  ALA A CA    1 
ATOM   3511 C  C     . ALA A 1 477  ? 93.038  115.724 160.425 1.00 34.64  ? 477  ALA A C     1 
ATOM   3512 O  O     . ALA A 1 477  ? 94.122  115.799 161.014 1.00 34.64  ? 477  ALA A O     1 
ATOM   3513 C  CB    . ALA A 1 477  ? 92.932  116.287 157.984 1.00 34.64  ? 477  ALA A CB    1 
ATOM   3514 N  N     . SER A 1 478  ? 91.896  116.130 160.983 1.00 36.80  ? 478  SER A N     1 
ATOM   3515 C  CA    . SER A 1 478  ? 91.884  116.663 162.340 1.00 36.80  ? 478  SER A CA    1 
ATOM   3516 C  C     . SER A 1 478  ? 92.233  115.595 163.367 1.00 36.80  ? 478  SER A C     1 
ATOM   3517 O  O     . SER A 1 478  ? 92.868  115.899 164.383 1.00 36.80  ? 478  SER A O     1 
ATOM   3518 C  CB    . SER A 1 478  ? 90.519  117.274 162.652 1.00 36.80  ? 478  SER A CB    1 
ATOM   3519 O  OG    . SER A 1 478  ? 89.497  116.297 162.570 1.00 36.80  ? 478  SER A OG    1 
ATOM   3520 N  N     . ALA A 1 479  ? 91.821  114.348 163.128 1.00 38.56  ? 479  ALA A N     1 
ATOM   3521 C  CA    . ALA A 1 479  ? 92.154  113.271 164.055 1.00 38.56  ? 479  ALA A CA    1 
ATOM   3522 C  C     . ALA A 1 479  ? 93.658  113.031 164.110 1.00 38.56  ? 479  ALA A C     1 
ATOM   3523 O  O     . ALA A 1 479  ? 94.224  112.839 165.192 1.00 38.56  ? 479  ALA A O     1 
ATOM   3524 C  CB    . ALA A 1 479  ? 91.421  111.991 163.658 1.00 38.56  ? 479  ALA A CB    1 
ATOM   3525 N  N     . ALA A 1 480  ? 94.322  113.046 162.957 1.00 39.36  ? 480  ALA A N     1 
ATOM   3526 C  CA    . ALA A 1 480  ? 95.746  112.750 162.872 1.00 39.36  ? 480  ALA A CA    1 
ATOM   3527 C  C     . ALA A 1 480  ? 96.631  113.953 163.181 1.00 39.36  ? 480  ALA A C     1 
ATOM   3528 O  O     . ALA A 1 480  ? 97.830  113.903 162.886 1.00 39.36  ? 480  ALA A O     1 
ATOM   3529 C  CB    . ALA A 1 480  ? 96.086  112.205 161.483 1.00 39.36  ? 480  ALA A CB    1 
ATOM   3530 N  N     . ASN A 1 481  ? 96.077  115.014 163.763 1.00 40.61  ? 481  ASN A N     1 
ATOM   3531 C  CA    . ASN A 1 481  ? 96.822  116.226 164.101 1.00 40.61  ? 481  ASN A CA    1 
ATOM   3532 C  C     . ASN A 1 481  ? 97.533  116.791 162.872 1.00 40.61  ? 481  ASN A C     1 
ATOM   3533 O  O     . ASN A 1 481  ? 98.751  116.973 162.844 1.00 40.61  ? 481  ASN A O     1 
ATOM   3534 C  CB    . ASN A 1 481  ? 97.814  115.963 165.236 1.00 40.61  ? 481  ASN A CB    1 
ATOM   3535 C  CG    . ASN A 1 481  ? 98.344  117.243 165.854 1.00 40.61  ? 481  ASN A CG    1 
ATOM   3536 O  OD1   . ASN A 1 481  ? 97.605  117.988 166.496 1.00 40.61  ? 481  ASN A OD1   1 
ATOM   3537 N  ND2   . ASN A 1 481  ? 99.631  117.504 165.661 1.00 40.61  ? 481  ASN A ND2   1 
ATOM   3538 N  N     . ALA A 1 482  ? 96.739  117.064 161.839 1.00 32.39  ? 482  ALA A N     1 
ATOM   3539 C  CA    . ALA A 1 482  ? 97.258  117.619 160.601 1.00 32.39  ? 482  ALA A CA    1 
ATOM   3540 C  C     . ALA A 1 482  ? 96.481  118.832 160.114 1.00 32.39  ? 482  ALA A C     1 
ATOM   3541 O  O     . ALA A 1 482  ? 96.849  119.407 159.085 1.00 32.39  ? 482  ALA A O     1 
ATOM   3542 C  CB    . ALA A 1 482  ? 97.270  116.551 159.498 1.00 32.39  ? 482  ALA A CB    1 
ATOM   3543 N  N     . HIS A 1 483  ? 95.421  119.235 160.816 1.00 33.21  ? 483  HIS A N     1 
ATOM   3544 C  CA    . HIS A 1 483  ? 94.626  120.373 160.368 1.00 33.21  ? 483  HIS A CA    1 
ATOM   3545 C  C     . HIS A 1 483  ? 95.408  121.676 160.462 1.00 33.21  ? 483  HIS A C     1 
ATOM   3546 O  O     . HIS A 1 483  ? 95.251  122.562 159.614 1.00 33.21  ? 483  HIS A O     1 
ATOM   3547 C  CB    . HIS A 1 483  ? 93.339  120.465 161.184 1.00 33.21  ? 483  HIS A CB    1 
ATOM   3548 C  CG    . HIS A 1 483  ? 92.330  121.410 160.613 1.00 33.21  ? 483  HIS A CG    1 
ATOM   3549 N  ND1   . HIS A 1 483  ? 91.995  121.422 159.277 1.00 33.21  ? 483  HIS A ND1   1 
ATOM   3550 C  CD2   . HIS A 1 483  ? 91.585  122.378 161.197 1.00 33.21  ? 483  HIS A CD2   1 
ATOM   3551 C  CE1   . HIS A 1 483  ? 91.086  122.357 159.062 1.00 33.21  ? 483  HIS A CE1   1 
ATOM   3552 N  NE2   . HIS A 1 483  ? 90.820  122.951 160.211 1.00 33.21  ? 483  HIS A NE2   1 
ATOM   3553 N  N     . SER A 1 484  ? 96.247  121.816 161.490 1.00 31.17  ? 484  SER A N     1 
ATOM   3554 C  CA    . SER A 1 484  ? 96.924  123.086 161.732 1.00 31.17  ? 484  SER A CA    1 
ATOM   3555 C  C     . SER A 1 484  ? 97.864  123.446 160.588 1.00 31.17  ? 484  SER A C     1 
ATOM   3556 O  O     . SER A 1 484  ? 97.795  124.550 160.037 1.00 31.17  ? 484  SER A O     1 
ATOM   3557 C  CB    . SER A 1 484  ? 97.686  123.024 163.056 1.00 31.17  ? 484  SER A CB    1 
ATOM   3558 O  OG    . SER A 1 484  ? 96.798  122.825 164.141 1.00 31.17  ? 484  SER A OG    1 
ATOM   3559 N  N     . PHE A 1 485  ? 98.753  122.524 160.213 1.00 30.28  ? 485  PHE A N     1 
ATOM   3560 C  CA    . PHE A 1 485  ? 99.751  122.849 159.199 1.00 30.28  ? 485  PHE A CA    1 
ATOM   3561 C  C     . PHE A 1 485  ? 99.156  122.861 157.797 1.00 30.28  ? 485  PHE A C     1 
ATOM   3562 O  O     . PHE A 1 485  ? 99.673  123.554 156.915 1.00 30.28  ? 485  PHE A O     1 
ATOM   3563 C  CB    . PHE A 1 485  ? 100.928 121.875 159.288 1.00 30.28  ? 485  PHE A CB    1 
ATOM   3564 C  CG    . PHE A 1 485  ? 100.783 120.654 158.427 1.00 30.28  ? 485  PHE A CG    1 
ATOM   3565 C  CD1   . PHE A 1 485  ? 100.042 119.570 158.861 1.00 30.28  ? 485  PHE A CD1   1 
ATOM   3566 C  CD2   . PHE A 1 485  ? 101.411 120.579 157.195 1.00 30.28  ? 485  PHE A CD2   1 
ATOM   3567 C  CE1   . PHE A 1 485  ? 99.914  118.443 158.075 1.00 30.28  ? 485  PHE A CE1   1 
ATOM   3568 C  CE2   . PHE A 1 485  ? 101.285 119.455 156.405 1.00 30.28  ? 485  PHE A CE2   1 
ATOM   3569 C  CZ    . PHE A 1 485  ? 100.537 118.385 156.846 1.00 30.28  ? 485  PHE A CZ    1 
ATOM   3570 N  N     . ILE A 1 486  ? 98.081  122.105 157.567 1.00 28.51  ? 486  ILE A N     1 
ATOM   3571 C  CA    . ILE A 1 486  ? 97.454  122.102 156.249 1.00 28.51  ? 486  ILE A CA    1 
ATOM   3572 C  C     . ILE A 1 486  ? 96.761  123.432 155.981 1.00 28.51  ? 486  ILE A C     1 
ATOM   3573 O  O     . ILE A 1 486  ? 96.887  124.005 154.892 1.00 28.51  ? 486  ILE A O     1 
ATOM   3574 C  CB    . ILE A 1 486  ? 96.479  120.918 156.121 1.00 28.51  ? 486  ILE A CB    1 
ATOM   3575 C  CG1   . ILE A 1 486  ? 97.246  119.619 155.882 1.00 28.51  ? 486  ILE A CG1   1 
ATOM   3576 C  CG2   . ILE A 1 486  ? 95.496  121.153 154.990 1.00 28.51  ? 486  ILE A CG2   1 
ATOM   3577 C  CD1   . ILE A 1 486  ? 96.378  118.385 155.935 1.00 28.51  ? 486  ILE A CD1   1 
ATOM   3578 N  N     . THR A 1 487  ? 96.027  123.951 156.967 1.00 30.97  ? 487  THR A N     1 
ATOM   3579 C  CA    . THR A 1 487  ? 95.282  125.189 156.776 1.00 30.97  ? 487  THR A CA    1 
ATOM   3580 C  C     . THR A 1 487  ? 96.175  126.422 156.758 1.00 30.97  ? 487  THR A C     1 
ATOM   3581 O  O     . THR A 1 487  ? 95.731  127.483 156.308 1.00 30.97  ? 487  THR A O     1 
ATOM   3582 C  CB    . THR A 1 487  ? 94.218  125.343 157.866 1.00 30.97  ? 487  THR A CB    1 
ATOM   3583 O  OG1   . THR A 1 487  ? 93.247  126.312 157.453 1.00 30.97  ? 487  THR A OG1   1 
ATOM   3584 C  CG2   . THR A 1 487  ? 94.847  125.794 159.174 1.00 30.97  ? 487  THR A CG2   1 
ATOM   3585 N  N     . LEU A 1 488  ? 97.415  126.313 157.235 1.00 30.51  ? 488  LEU A N     1 
ATOM   3586 C  CA    . LEU A 1 488  ? 98.338  127.440 157.204 1.00 30.51  ? 488  LEU A CA    1 
ATOM   3587 C  C     . LEU A 1 488  ? 99.016  127.613 155.853 1.00 30.51  ? 488  LEU A C     1 
ATOM   3588 O  O     . LEU A 1 488  ? 99.612  128.668 155.609 1.00 30.51  ? 488  LEU A O     1 
ATOM   3589 C  CB    . LEU A 1 488  ? 99.400  127.277 158.293 1.00 30.51  ? 488  LEU A CB    1 
ATOM   3590 C  CG    . LEU A 1 488  ? 99.031  127.800 159.682 1.00 30.51  ? 488  LEU A CG    1 
ATOM   3591 C  CD1   . LEU A 1 488  ? 100.267 127.900 160.562 1.00 30.51  ? 488  LEU A CD1   1 
ATOM   3592 C  CD2   . LEU A 1 488  ? 98.329  129.143 159.582 1.00 30.51  ? 488  LEU A CD2   1 
ATOM   3593 N  N     . LEU A 1 489  ? 98.944  126.614 154.979 1.00 30.13  ? 489  LEU A N     1 
ATOM   3594 C  CA    . LEU A 1 489  ? 99.560  126.707 153.670 1.00 30.13  ? 489  LEU A CA    1 
ATOM   3595 C  C     . LEU A 1 489  ? 98.816  127.726 152.810 1.00 30.13  ? 489  LEU A C     1 
ATOM   3596 O  O     . LEU A 1 489  ? 97.637  128.003 153.041 1.00 30.13  ? 489  LEU A O     1 
ATOM   3597 C  CB    . LEU A 1 489  ? 99.565  125.338 152.996 1.00 30.13  ? 489  LEU A CB    1 
ATOM   3598 C  CG    . LEU A 1 489  ? 100.447 124.280 153.664 1.00 30.13  ? 489  LEU A CG    1 
ATOM   3599 C  CD1   . LEU A 1 489  ? 100.580 123.050 152.782 1.00 30.13  ? 489  LEU A CD1   1 
ATOM   3600 C  CD2   . LEU A 1 489  ? 101.814 124.851 154.004 1.00 30.13  ? 489  LEU A CD2   1 
ATOM   3601 N  N     . PRO A 1 490  ? 99.494  128.315 151.814 1.00 30.42  ? 490  PRO A N     1 
ATOM   3602 C  CA    . PRO A 1 490  ? 98.833  129.320 150.969 1.00 30.42  ? 490  PRO A CA    1 
ATOM   3603 C  C     . PRO A 1 490  ? 97.636  128.768 150.211 1.00 30.42  ? 490  PRO A C     1 
ATOM   3604 O  O     . PRO A 1 490  ? 96.529  129.303 150.321 1.00 30.42  ? 490  PRO A O     1 
ATOM   3605 C  CB    . PRO A 1 490  ? 99.947  129.763 150.011 1.00 30.42  ? 490  PRO A CB    1 
ATOM   3606 C  CG    . PRO A 1 490  ? 100.961 128.669 150.057 1.00 30.42  ? 490  PRO A CG    1 
ATOM   3607 C  CD    . PRO A 1 490  ? 100.911 128.144 151.454 1.00 30.42  ? 490  PRO A CD    1 
ATOM   3608 N  N     . LYS A 1 491  ? 97.842  127.701 149.437 1.00 31.63  ? 491  LYS A N     1 
ATOM   3609 C  CA    . LYS A 1 491  ? 96.727  127.107 148.706 1.00 31.63  ? 491  LYS A CA    1 
ATOM   3610 C  C     . LYS A 1 491  ? 95.796  126.344 149.639 1.00 31.63  ? 491  LYS A C     1 
ATOM   3611 O  O     . LYS A 1 491  ? 94.571  126.394 149.480 1.00 31.63  ? 491  LYS A O     1 
ATOM   3612 C  CB    . LYS A 1 491  ? 97.247  126.191 147.600 1.00 31.63  ? 491  LYS A CB    1 
ATOM   3613 C  CG    . LYS A 1 491  ? 97.788  126.924 146.386 1.00 31.63  ? 491  LYS A CG    1 
ATOM   3614 C  CD    . LYS A 1 491  ? 98.168  125.949 145.286 1.00 31.63  ? 491  LYS A CD    1 
ATOM   3615 C  CE    . LYS A 1 491  ? 98.758  126.669 144.088 1.00 31.63  ? 491  LYS A CE    1 
ATOM   3616 N  NZ    . LYS A 1 491  ? 99.184  125.715 143.028 1.00 31.63  ? 491  LYS A NZ    1 
ATOM   3617 N  N     . GLY A 1 492  ? 96.354  125.635 150.616 1.00 30.66  ? 492  GLY A N     1 
ATOM   3618 C  CA    . GLY A 1 492  ? 95.548  124.878 151.552 1.00 30.66  ? 492  GLY A CA    1 
ATOM   3619 C  C     . GLY A 1 492  ? 95.604  123.384 151.315 1.00 30.66  ? 492  GLY A C     1 
ATOM   3620 O  O     . GLY A 1 492  ? 96.629  122.745 151.570 1.00 30.66  ? 492  GLY A O     1 
ATOM   3621 N  N     . TYR A 1 493  ? 94.508  122.815 150.823 1.00 29.20  ? 493  TYR A N     1 
ATOM   3622 C  CA    . TYR A 1 493  ? 94.427  121.388 150.546 1.00 29.20  ? 493  TYR A CA    1 
ATOM   3623 C  C     . TYR A 1 493  ? 94.837  121.037 149.123 1.00 29.20  ? 493  TYR A C     1 
ATOM   3624 O  O     . TYR A 1 493  ? 94.718  119.872 148.731 1.00 29.20  ? 493  TYR A O     1 
ATOM   3625 C  CB    . TYR A 1 493  ? 93.005  120.879 150.803 1.00 29.20  ? 493  TYR A CB    1 
ATOM   3626 C  CG    . TYR A 1 493  ? 92.709  120.571 152.253 1.00 29.20  ? 493  TYR A CG    1 
ATOM   3627 C  CD1   . TYR A 1 493  ? 92.224  121.553 153.106 1.00 29.20  ? 493  TYR A CD1   1 
ATOM   3628 C  CD2   . TYR A 1 493  ? 92.908  119.297 152.767 1.00 29.20  ? 493  TYR A CD2   1 
ATOM   3629 C  CE1   . TYR A 1 493  ? 91.949  121.276 154.430 1.00 29.20  ? 493  TYR A CE1   1 
ATOM   3630 C  CE2   . TYR A 1 493  ? 92.636  119.011 154.090 1.00 29.20  ? 493  TYR A CE2   1 
ATOM   3631 C  CZ    . TYR A 1 493  ? 92.157  120.004 154.916 1.00 29.20  ? 493  TYR A CZ    1 
ATOM   3632 O  OH    . TYR A 1 493  ? 91.885  119.725 156.235 1.00 29.20  ? 493  TYR A OH    1 
ATOM   3633 N  N     . ASP A 1 494  ? 95.304  122.007 148.339 1.00 29.54  ? 494  ASP A N     1 
ATOM   3634 C  CA    . ASP A 1 494  ? 95.675  121.774 146.950 1.00 29.54  ? 494  ASP A CA    1 
ATOM   3635 C  C     . ASP A 1 494  ? 97.167  121.942 146.698 1.00 29.54  ? 494  ASP A C     1 
ATOM   3636 O  O     . ASP A 1 494  ? 97.596  121.905 145.540 1.00 29.54  ? 494  ASP A O     1 
ATOM   3637 C  CB    . ASP A 1 494  ? 94.882  122.703 146.030 1.00 29.54  ? 494  ASP A CB    1 
ATOM   3638 C  CG    . ASP A 1 494  ? 93.387  122.512 146.162 1.00 29.54  ? 494  ASP A CG    1 
ATOM   3639 O  OD1   . ASP A 1 494  ? 92.895  121.419 145.812 1.00 29.54  ? 494  ASP A OD1   1 
ATOM   3640 O  OD2   . ASP A 1 494  ? 92.703  123.453 146.615 1.00 29.54  ? 494  ASP A OD2   1 
ATOM   3641 N  N     . THR A 1 495  ? 97.967  122.131 147.743 1.00 28.21  ? 495  THR A N     1 
ATOM   3642 C  CA    . THR A 1 495  ? 99.405  122.264 147.561 1.00 28.21  ? 495  THR A CA    1 
ATOM   3643 C  C     . THR A 1 495  ? 100.004 120.949 147.083 1.00 28.21  ? 495  THR A C     1 
ATOM   3644 O  O     . THR A 1 495  ? 99.658  119.873 147.577 1.00 28.21  ? 495  THR A O     1 
ATOM   3645 C  CB    . THR A 1 495  ? 100.073 122.694 148.866 1.00 28.21  ? 495  THR A CB    1 
ATOM   3646 O  OG1   . THR A 1 495  ? 100.000 121.626 149.816 1.00 28.21  ? 495  THR A OG1   1 
ATOM   3647 C  CG2   . THR A 1 495  ? 99.380  123.916 149.438 1.00 28.21  ? 495  THR A CG2   1 
ATOM   3648 N  N     . GLN A 1 496  ? 100.906 121.039 146.112 1.00 28.29  ? 496  GLN A N     1 
ATOM   3649 C  CA    . GLN A 1 496  ? 101.589 119.859 145.608 1.00 28.29  ? 496  GLN A CA    1 
ATOM   3650 C  C     . GLN A 1 496  ? 102.778 119.512 146.494 1.00 28.29  ? 496  GLN A C     1 
ATOM   3651 O  O     . GLN A 1 496  ? 103.421 120.387 147.080 1.00 28.29  ? 496  GLN A O     1 
ATOM   3652 C  CB    . GLN A 1 496  ? 102.056 120.079 144.171 1.00 28.29  ? 496  GLN A CB    1 
ATOM   3653 C  CG    . GLN A 1 496  ? 100.997 120.677 143.267 1.00 28.29  ? 496  GLN A CG    1 
ATOM   3654 C  CD    . GLN A 1 496  ? 101.069 120.133 141.858 1.00 28.29  ? 496  GLN A CD    1 
ATOM   3655 O  OE1   . GLN A 1 496  ? 102.100 119.610 141.435 1.00 28.29  ? 496  GLN A OE1   1 
ATOM   3656 N  NE2   . GLN A 1 496  ? 99.971  120.250 141.121 1.00 28.29  ? 496  GLN A NE2   1 
ATOM   3657 N  N     . VAL A 1 497  ? 103.067 118.216 146.590 1.00 29.26  ? 497  VAL A N     1 
ATOM   3658 C  CA    . VAL A 1 497  ? 104.173 117.721 147.401 1.00 29.26  ? 497  VAL A CA    1 
ATOM   3659 C  C     . VAL A 1 497  ? 105.343 117.245 146.561 1.00 29.26  ? 497  VAL A C     1 
ATOM   3660 O  O     . VAL A 1 497  ? 106.370 116.843 147.126 1.00 29.26  ? 497  VAL A O     1 
ATOM   3661 C  CB    . VAL A 1 497  ? 103.713 116.602 148.353 1.00 29.26  ? 497  VAL A CB    1 
ATOM   3662 C  CG1   . VAL A 1 497  ? 102.874 117.179 149.473 1.00 29.26  ? 497  VAL A CG1   1 
ATOM   3663 C  CG2   . VAL A 1 497  ? 102.933 115.552 147.590 1.00 29.26  ? 497  VAL A CG2   1 
ATOM   3664 N  N     . GLY A 1 498  ? 105.228 117.272 145.238 1.00 30.95  ? 498  GLY A N     1 
ATOM   3665 C  CA    . GLY A 1 498  ? 106.338 116.887 144.394 1.00 30.95  ? 498  GLY A CA    1 
ATOM   3666 C  C     . GLY A 1 498  ? 106.615 115.392 144.439 1.00 30.95  ? 498  GLY A C     1 
ATOM   3667 O  O     . GLY A 1 498  ? 105.809 114.583 144.896 1.00 30.95  ? 498  GLY A O     1 
ATOM   3668 N  N     . GLU A 1 499  ? 107.802 115.040 143.956 1.00 33.10  ? 499  GLU A N     1 
ATOM   3669 C  CA    . GLU A 1 499  ? 108.195 113.639 143.864 1.00 33.10  ? 499  GLU A CA    1 
ATOM   3670 C  C     . GLU A 1 499  ? 108.564 113.104 145.242 1.00 33.10  ? 499  GLU A C     1 
ATOM   3671 O  O     . GLU A 1 499  ? 109.519 113.579 145.864 1.00 33.10  ? 499  GLU A O     1 
ATOM   3672 C  CB    . GLU A 1 499  ? 109.365 113.484 142.897 1.00 33.10  ? 499  GLU A CB    1 
ATOM   3673 C  CG    . GLU A 1 499  ? 109.539 112.075 142.357 1.00 33.10  ? 499  GLU A CG    1 
ATOM   3674 C  CD    . GLU A 1 499  ? 108.319 111.588 141.601 1.00 33.10  ? 499  GLU A CD    1 
ATOM   3675 O  OE1   . GLU A 1 499  ? 107.989 110.389 141.712 1.00 33.10  ? 499  GLU A OE1   1 
ATOM   3676 O  OE2   . GLU A 1 499  ? 107.692 112.404 140.893 1.00 33.10  ? 499  GLU A OE2   1 
ATOM   3677 N  N     . ARG A 1 500  ? 107.801 112.117 145.717 1.00 32.72  ? 500  ARG A N     1 
ATOM   3678 C  CA    . ARG A 1 500  ? 108.060 111.442 146.990 1.00 32.72  ? 500  ARG A CA    1 
ATOM   3679 C  C     . ARG A 1 500  ? 108.050 112.410 148.169 1.00 32.72  ? 500  ARG A C     1 
ATOM   3680 O  O     . ARG A 1 500  ? 108.657 112.144 149.208 1.00 32.72  ? 500  ARG A O     1 
ATOM   3681 C  CB    . ARG A 1 500  ? 109.377 110.663 146.949 1.00 32.72  ? 500  ARG A CB    1 
ATOM   3682 C  CG    . ARG A 1 500  ? 109.451 109.648 145.825 1.00 32.72  ? 500  ARG A CG    1 
ATOM   3683 C  CD    . ARG A 1 500  ? 110.276 108.440 146.225 1.00 32.72  ? 500  ARG A CD    1 
ATOM   3684 N  NE    . ARG A 1 500  ? 109.458 107.390 146.825 1.00 32.72  ? 500  ARG A NE    1 
ATOM   3685 C  CZ    . ARG A 1 500  ? 109.863 106.136 146.992 1.00 32.72  ? 500  ARG A CZ    1 
ATOM   3686 N  NH1   . ARG A 1 500  ? 111.074 105.773 146.598 1.00 32.72  ? 500  ARG A NH1   1 
ATOM   3687 N  NH2   . ARG A 1 500  ? 109.057 105.242 147.547 1.00 32.72  ? 500  ARG A NH2   1 
ATOM   3688 N  N     . GLY A 1 501  ? 107.356 113.534 148.021 1.00 29.64  ? 501  GLY A N     1 
ATOM   3689 C  CA    . GLY A 1 501  ? 107.266 114.502 149.102 1.00 29.64  ? 501  GLY A CA    1 
ATOM   3690 C  C     . GLY A 1 501  ? 108.598 115.091 149.512 1.00 29.64  ? 501  GLY A C     1 
ATOM   3691 O  O     . GLY A 1 501  ? 108.814 115.362 150.699 1.00 29.64  ? 501  GLY A O     1 
ATOM   3692 N  N     . VAL A 1 502  ? 109.503 115.294 148.552 1.00 29.14  ? 502  VAL A N     1 
ATOM   3693 C  CA    . VAL A 1 502  ? 110.809 115.855 148.881 1.00 29.14  ? 502  VAL A CA    1 
ATOM   3694 C  C     . VAL A 1 502  ? 110.678 117.299 149.339 1.00 29.14  ? 502  VAL A C     1 
ATOM   3695 O  O     . VAL A 1 502  ? 111.506 117.786 150.119 1.00 29.14  ? 502  VAL A O     1 
ATOM   3696 C  CB    . VAL A 1 502  ? 111.768 115.735 147.683 1.00 29.14  ? 502  VAL A CB    1 
ATOM   3697 C  CG1   . VAL A 1 502  ? 112.194 114.288 147.487 1.00 29.14  ? 502  VAL A CG1   1 
ATOM   3698 C  CG2   . VAL A 1 502  ? 111.120 116.288 146.424 1.00 29.14  ? 502  VAL A CG2   1 
ATOM   3699 N  N     . GLN A 1 503  ? 109.653 118.006 148.872 1.00 32.57  ? 503  GLN A N     1 
ATOM   3700 C  CA    . GLN A 1 503  ? 109.449 119.402 149.227 1.00 32.57  ? 503  GLN A CA    1 
ATOM   3701 C  C     . GLN A 1 503  ? 108.528 119.575 150.427 1.00 32.57  ? 503  GLN A C     1 
ATOM   3702 O  O     . GLN A 1 503  ? 108.070 120.693 150.685 1.00 32.57  ? 503  GLN A O     1 
ATOM   3703 C  CB    . GLN A 1 503  ? 108.899 120.178 148.028 1.00 32.57  ? 503  GLN A CB    1 
ATOM   3704 C  CG    . GLN A 1 503  ? 107.520 119.762 147.578 1.00 32.57  ? 503  GLN A CG    1 
ATOM   3705 C  CD    . GLN A 1 503  ? 107.021 120.605 146.425 1.00 32.57  ? 503  GLN A CD    1 
ATOM   3706 O  OE1   . GLN A 1 503  ? 106.081 121.385 146.572 1.00 32.57  ? 503  GLN A OE1   1 
ATOM   3707 N  NE2   . GLN A 1 503  ? 107.654 120.459 145.268 1.00 32.57  ? 503  GLN A NE2   1 
ATOM   3708 N  N     . LEU A 1 504  ? 108.248 118.502 151.160 1.00 30.15  ? 504  LEU A N     1 
ATOM   3709 C  CA    . LEU A 1 504  ? 107.414 118.550 152.348 1.00 30.15  ? 504  LEU A CA    1 
ATOM   3710 C  C     . LEU A 1 504  ? 108.216 118.047 153.542 1.00 30.15  ? 504  LEU A C     1 
ATOM   3711 O  O     . LEU A 1 504  ? 109.123 117.222 153.394 1.00 30.15  ? 504  LEU A O     1 
ATOM   3712 C  CB    . LEU A 1 504  ? 106.144 117.711 152.158 1.00 30.15  ? 504  LEU A CB    1 
ATOM   3713 C  CG    . LEU A 1 504  ? 105.087 117.743 153.259 1.00 30.15  ? 504  LEU A CG    1 
ATOM   3714 C  CD1   . LEU A 1 504  ? 104.537 119.147 153.402 1.00 30.15  ? 504  LEU A CD1   1 
ATOM   3715 C  CD2   . LEU A 1 504  ? 103.973 116.760 152.955 1.00 30.15  ? 504  LEU A CD2   1 
ATOM   3716 N  N     . SER A 1 505  ? 107.884 118.555 154.725 1.00 36.16  ? 505  SER A N     1 
ATOM   3717 C  CA    . SER A 1 505  ? 108.644 118.229 155.922 1.00 36.16  ? 505  SER A CA    1 
ATOM   3718 C  C     . SER A 1 505  ? 108.503 116.752 156.277 1.00 36.16  ? 505  SER A C     1 
ATOM   3719 O  O     . SER A 1 505  ? 107.529 116.085 155.918 1.00 36.16  ? 505  SER A O     1 
ATOM   3720 C  CB    . SER A 1 505  ? 108.187 119.088 157.099 1.00 36.16  ? 505  SER A CB    1 
ATOM   3721 O  OG    . SER A 1 505  ? 108.838 118.694 158.293 1.00 36.16  ? 505  SER A OG    1 
ATOM   3722 N  N     . GLY A 1 506  ? 109.507 116.240 156.992 1.00 34.07  ? 506  GLY A N     1 
ATOM   3723 C  CA    . GLY A 1 506  ? 109.485 114.838 157.378 1.00 34.07  ? 506  GLY A CA    1 
ATOM   3724 C  C     . GLY A 1 506  ? 108.347 114.512 158.325 1.00 34.07  ? 506  GLY A C     1 
ATOM   3725 O  O     . GLY A 1 506  ? 107.646 113.512 158.156 1.00 34.07  ? 506  GLY A O     1 
ATOM   3726 N  N     . GLY A 1 507  ? 108.149 115.355 159.339 1.00 36.57  ? 507  GLY A N     1 
ATOM   3727 C  CA    . GLY A 1 507  ? 107.053 115.130 160.267 1.00 36.57  ? 507  GLY A CA    1 
ATOM   3728 C  C     . GLY A 1 507  ? 105.695 115.274 159.611 1.00 36.57  ? 507  GLY A C     1 
ATOM   3729 O  O     . GLY A 1 507  ? 104.767 114.518 159.909 1.00 36.57  ? 507  GLY A O     1 
ATOM   3730 N  N     . GLN A 1 508  ? 105.559 116.246 158.709 1.00 32.15  ? 508  GLN A N     1 
ATOM   3731 C  CA    . GLN A 1 508  ? 104.279 116.463 158.045 1.00 32.15  ? 508  GLN A CA    1 
ATOM   3732 C  C     . GLN A 1 508  ? 103.961 115.336 157.071 1.00 32.15  ? 508  GLN A C     1 
ATOM   3733 O  O     . GLN A 1 508  ? 102.789 115.063 156.789 1.00 32.15  ? 508  GLN A O     1 
ATOM   3734 C  CB    . GLN A 1 508  ? 104.287 117.817 157.340 1.00 32.15  ? 508  GLN A CB    1 
ATOM   3735 C  CG    . GLN A 1 508  ? 104.477 118.984 158.297 1.00 32.15  ? 508  GLN A CG    1 
ATOM   3736 C  CD    . GLN A 1 508  ? 104.872 120.268 157.598 1.00 32.15  ? 508  GLN A CD    1 
ATOM   3737 O  OE1   . GLN A 1 508  ? 104.839 120.358 156.373 1.00 32.15  ? 508  GLN A OE1   1 
ATOM   3738 N  NE2   . GLN A 1 508  ? 105.252 121.271 158.380 1.00 32.15  ? 508  GLN A NE2   1 
ATOM   3739 N  N     . LYS A 1 509  ? 104.991 114.676 156.536 1.00 30.90  ? 509  LYS A N     1 
ATOM   3740 C  CA    . LYS A 1 509  ? 104.754 113.521 155.676 1.00 30.90  ? 509  LYS A CA    1 
ATOM   3741 C  C     . LYS A 1 509  ? 104.120 112.374 156.452 1.00 30.90  ? 509  LYS A C     1 
ATOM   3742 O  O     . LYS A 1 509  ? 103.211 111.703 155.951 1.00 30.90  ? 509  LYS A O     1 
ATOM   3743 C  CB    . LYS A 1 509  ? 106.060 113.066 155.026 1.00 30.90  ? 509  LYS A CB    1 
ATOM   3744 C  CG    . LYS A 1 509  ? 106.412 113.805 153.750 1.00 30.90  ? 509  LYS A CG    1 
ATOM   3745 C  CD    . LYS A 1 509  ? 107.711 113.287 153.155 1.00 30.90  ? 509  LYS A CD    1 
ATOM   3746 C  CE    . LYS A 1 509  ? 108.832 113.303 154.180 1.00 30.90  ? 509  LYS A CE    1 
ATOM   3747 N  NZ    . LYS A 1 509  ? 110.172 113.156 153.548 1.00 30.90  ? 509  LYS A NZ    1 
ATOM   3748 N  N     . GLN A 1 510  ? 104.593 112.128 157.676 1.00 36.68  ? 510  GLN A N     1 
ATOM   3749 C  CA    . GLN A 1 510  ? 104.061 111.021 158.464 1.00 36.68  ? 510  GLN A CA    1 
ATOM   3750 C  C     . GLN A 1 510  ? 102.611 111.267 158.859 1.00 36.68  ? 510  GLN A C     1 
ATOM   3751 O  O     . GLN A 1 510  ? 101.809 110.328 158.917 1.00 36.68  ? 510  GLN A O     1 
ATOM   3752 C  CB    . GLN A 1 510  ? 104.924 110.792 159.702 1.00 36.68  ? 510  GLN A CB    1 
ATOM   3753 C  CG    . GLN A 1 510  ? 106.189 110.001 159.429 1.00 36.68  ? 510  GLN A CG    1 
ATOM   3754 C  CD    . GLN A 1 510  ? 106.733 109.329 160.671 1.00 36.68  ? 510  GLN A CD    1 
ATOM   3755 O  OE1   . GLN A 1 510  ? 106.140 109.414 161.745 1.00 36.68  ? 510  GLN A OE1   1 
ATOM   3756 N  NE2   . GLN A 1 510  ? 107.868 108.656 160.532 1.00 36.68  ? 510  GLN A NE2   1 
ATOM   3757 N  N     . ARG A 1 511  ? 102.258 112.522 159.143 1.00 34.53  ? 511  ARG A N     1 
ATOM   3758 C  CA    . ARG A 1 511  ? 100.878 112.835 159.498 1.00 34.53  ? 511  ARG A CA    1 
ATOM   3759 C  C     . ARG A 1 511  ? 99.931  112.542 158.341 1.00 34.53  ? 511  ARG A C     1 
ATOM   3760 O  O     . ARG A 1 511  ? 98.809  112.066 158.553 1.00 34.53  ? 511  ARG A O     1 
ATOM   3761 C  CB    . ARG A 1 511  ? 100.765 114.297 159.925 1.00 34.53  ? 511  ARG A CB    1 
ATOM   3762 C  CG    . ARG A 1 511  ? 101.506 114.630 161.206 1.00 34.53  ? 511  ARG A CG    1 
ATOM   3763 C  CD    . ARG A 1 511  ? 101.788 116.118 161.292 1.00 34.53  ? 511  ARG A CD    1 
ATOM   3764 N  NE    . ARG A 1 511  ? 102.440 116.486 162.543 1.00 34.53  ? 511  ARG A NE    1 
ATOM   3765 C  CZ    . ARG A 1 511  ? 102.703 117.737 162.907 1.00 34.53  ? 511  ARG A CZ    1 
ATOM   3766 N  NH1   . ARG A 1 511  ? 102.367 118.743 162.113 1.00 34.53  ? 511  ARG A NH1   1 
ATOM   3767 N  NH2   . ARG A 1 511  ? 103.301 117.982 164.064 1.00 34.53  ? 511  ARG A NH2   1 
ATOM   3768 N  N     . ILE A 1 512  ? 100.361 112.827 157.110 1.00 29.53  ? 512  ILE A N     1 
ATOM   3769 C  CA    . ILE A 1 512  ? 99.515  112.571 155.947 1.00 29.53  ? 512  ILE A CA    1 
ATOM   3770 C  C     . ILE A 1 512  ? 99.273  111.076 155.778 1.00 29.53  ? 512  ILE A C     1 
ATOM   3771 O  O     . ILE A 1 512  ? 98.153  110.644 155.483 1.00 29.53  ? 512  ILE A O     1 
ATOM   3772 C  CB    . ILE A 1 512  ? 100.141 113.192 154.685 1.00 29.53  ? 512  ILE A CB    1 
ATOM   3773 C  CG1   . ILE A 1 512  ? 100.149 114.716 154.790 1.00 29.53  ? 512  ILE A CG1   1 
ATOM   3774 C  CG2   . ILE A 1 512  ? 99.379  112.762 153.446 1.00 29.53  ? 512  ILE A CG2   1 
ATOM   3775 C  CD1   . ILE A 1 512  ? 98.826  115.304 155.210 1.00 29.53  ? 512  ILE A CD1   1 
ATOM   3776 N  N     . ALA A 1 513  ? 100.318 110.263 155.955 1.00 30.70  ? 513  ALA A N     1 
ATOM   3777 C  CA    . ALA A 1 513  ? 100.157 108.816 155.843 1.00 30.70  ? 513  ALA A CA    1 
ATOM   3778 C  C     . ALA A 1 513  ? 99.221  108.278 156.919 1.00 30.70  ? 513  ALA A C     1 
ATOM   3779 O  O     . ALA A 1 513  ? 98.400  107.390 156.655 1.00 30.70  ? 513  ALA A O     1 
ATOM   3780 C  CB    . ALA A 1 513  ? 101.519 108.128 155.924 1.00 30.70  ? 513  ALA A CB    1 
ATOM   3781 N  N     . ILE A 1 514  ? 99.334  108.802 158.141 1.00 30.73  ? 514  ILE A N     1 
ATOM   3782 C  CA    . ILE A 1 514  ? 98.445  108.379 159.219 1.00 30.73  ? 514  ILE A CA    1 
ATOM   3783 C  C     . ILE A 1 514  ? 97.000  108.726 158.882 1.00 30.73  ? 514  ILE A C     1 
ATOM   3784 O  O     . ILE A 1 514  ? 96.086  107.924 159.105 1.00 30.73  ? 514  ILE A O     1 
ATOM   3785 C  CB    . ILE A 1 514  ? 98.888  109.007 160.552 1.00 30.73  ? 514  ILE A CB    1 
ATOM   3786 C  CG1   . ILE A 1 514  ? 100.147 108.315 161.073 1.00 30.73  ? 514  ILE A CG1   1 
ATOM   3787 C  CG2   . ILE A 1 514  ? 97.780  108.921 161.584 1.00 30.73  ? 514  ILE A CG2   1 
ATOM   3788 C  CD1   . ILE A 1 514  ? 100.682 108.910 162.353 1.00 30.73  ? 514  ILE A CD1   1 
ATOM   3789 N  N     . ALA A 1 515  ? 96.771  109.925 158.341 1.00 32.16  ? 515  ALA A N     1 
ATOM   3790 C  CA    . ALA A 1 515  ? 95.421  110.313 157.944 1.00 32.16  ? 515  ALA A CA    1 
ATOM   3791 C  C     . ALA A 1 515  ? 94.893  109.422 156.827 1.00 32.16  ? 515  ALA A C     1 
ATOM   3792 O  O     . ALA A 1 515  ? 93.712  109.052 156.823 1.00 32.16  ? 515  ALA A O     1 
ATOM   3793 C  CB    . ALA A 1 515  ? 95.402  111.779 157.516 1.00 32.16  ? 515  ALA A CB    1 
ATOM   3794 N  N     . ARG A 1 516  ? 95.749  109.080 155.862 1.00 31.91  ? 516  ARG A N     1 
ATOM   3795 C  CA    . ARG A 1 516  ? 95.330  108.194 154.780 1.00 31.91  ? 516  ARG A CA    1 
ATOM   3796 C  C     . ARG A 1 516  ? 94.942  106.823 155.316 1.00 31.91  ? 516  ARG A C     1 
ATOM   3797 O  O     . ARG A 1 516  ? 93.961  106.224 154.860 1.00 31.91  ? 516  ARG A O     1 
ATOM   3798 C  CB    . ARG A 1 516  ? 96.443  108.067 153.741 1.00 31.91  ? 516  ARG A CB    1 
ATOM   3799 C  CG    . ARG A 1 516  ? 96.081  107.184 152.558 1.00 31.91  ? 516  ARG A CG    1 
ATOM   3800 C  CD    . ARG A 1 516  ? 97.313  106.568 151.912 1.00 31.91  ? 516  ARG A CD    1 
ATOM   3801 N  NE    . ARG A 1 516  ? 98.436  107.499 151.856 1.00 31.91  ? 516  ARG A NE    1 
ATOM   3802 C  CZ    . ARG A 1 516  ? 99.710  107.139 151.968 1.00 31.91  ? 516  ARG A CZ    1 
ATOM   3803 N  NH1   . ARG A 1 516  ? 100.028 105.865 152.143 1.00 31.91  ? 516  ARG A NH1   1 
ATOM   3804 N  NH2   . ARG A 1 516  ? 100.666 108.053 151.905 1.00 31.91  ? 516  ARG A NH2   1 
ATOM   3805 N  N     . ALA A 1 517  ? 95.709  106.305 156.276 1.00 36.45  ? 517  ALA A N     1 
ATOM   3806 C  CA    . ALA A 1 517  ? 95.352  105.035 156.899 1.00 36.45  ? 517  ALA A CA    1 
ATOM   3807 C  C     . ALA A 1 517  ? 94.043  105.145 157.672 1.00 36.45  ? 517  ALA A C     1 
ATOM   3808 O  O     . ALA A 1 517  ? 93.206  104.237 157.626 1.00 36.45  ? 517  ALA A O     1 
ATOM   3809 C  CB    . ALA A 1 517  ? 96.478  104.566 157.818 1.00 36.45  ? 517  ALA A CB    1 
ATOM   3810 N  N     . MET A 1 518  ? 93.852  106.254 158.391 1.00 38.34  ? 518  MET A N     1 
ATOM   3811 C  CA    . MET A 1 518  ? 92.650  106.428 159.200 1.00 38.34  ? 518  MET A CA    1 
ATOM   3812 C  C     . MET A 1 518  ? 91.400  106.511 158.334 1.00 38.34  ? 518  MET A C     1 
ATOM   3813 O  O     . MET A 1 518  ? 90.346  105.982 158.705 1.00 38.34  ? 518  MET A O     1 
ATOM   3814 C  CB    . MET A 1 518  ? 92.780  107.680 160.065 1.00 38.34  ? 518  MET A CB    1 
ATOM   3815 C  CG    . MET A 1 518  ? 92.283  107.506 161.485 1.00 38.34  ? 518  MET A CG    1 
ATOM   3816 S  SD    . MET A 1 518  ? 93.150  106.186 162.350 1.00 38.34  ? 518  MET A SD    1 
ATOM   3817 C  CE    . MET A 1 518  ? 94.700  106.998 162.724 1.00 38.34  ? 518  MET A CE    1 
ATOM   3818 N  N     . LEU A 1 519  ? 91.496  107.181 157.183 1.00 37.87  ? 519  LEU A N     1 
ATOM   3819 C  CA    . LEU A 1 519  ? 90.324  107.354 156.330 1.00 37.87  ? 519  LEU A CA    1 
ATOM   3820 C  C     . LEU A 1 519  ? 89.784  106.022 155.826 1.00 37.87  ? 519  LEU A C     1 
ATOM   3821 O  O     . LEU A 1 519  ? 88.581  105.897 155.574 1.00 37.87  ? 519  LEU A O     1 
ATOM   3822 C  CB    . LEU A 1 519  ? 90.663  108.264 155.151 1.00 37.87  ? 519  LEU A CB    1 
ATOM   3823 C  CG    . LEU A 1 519  ? 89.465  108.851 154.407 1.00 37.87  ? 519  LEU A CG    1 
ATOM   3824 C  CD1   . LEU A 1 519  ? 88.694  109.796 155.309 1.00 37.87  ? 519  LEU A CD1   1 
ATOM   3825 C  CD2   . LEU A 1 519  ? 89.913  109.557 153.141 1.00 37.87  ? 519  LEU A CD2   1 
ATOM   3826 N  N     . LYS A 1 520  ? 90.651  105.018 155.672 1.00 40.85  ? 520  LYS A N     1 
ATOM   3827 C  CA    . LYS A 1 520  ? 90.199  103.721 155.179 1.00 40.85  ? 520  LYS A CA    1 
ATOM   3828 C  C     . LYS A 1 520  ? 89.299  103.016 156.184 1.00 40.85  ? 520  LYS A C     1 
ATOM   3829 O  O     . LYS A 1 520  ? 88.417  102.247 155.788 1.00 40.85  ? 520  LYS A O     1 
ATOM   3830 C  CB    . LYS A 1 520  ? 91.403  102.844 154.839 1.00 40.85  ? 520  LYS A CB    1 
ATOM   3831 C  CG    . LYS A 1 520  ? 91.082  101.649 153.963 1.00 40.85  ? 520  LYS A CG    1 
ATOM   3832 C  CD    . LYS A 1 520  ? 92.349  100.910 153.574 1.00 40.85  ? 520  LYS A CD    1 
ATOM   3833 C  CE    . LYS A 1 520  ? 92.053  99.766  152.625 1.00 40.85  ? 520  LYS A CE    1 
ATOM   3834 N  NZ    . LYS A 1 520  ? 93.280  98.988  152.306 1.00 40.85  ? 520  LYS A NZ    1 
ATOM   3835 N  N     . ASP A 1 521  ? 89.503  103.271 157.479 1.00 48.65  ? 521  ASP A N     1 
ATOM   3836 C  CA    . ASP A 1 521  ? 88.753  102.657 158.571 1.00 48.65  ? 521  ASP A CA    1 
ATOM   3837 C  C     . ASP A 1 521  ? 88.770  101.136 158.463 1.00 48.65  ? 521  ASP A C     1 
ATOM   3838 O  O     . ASP A 1 521  ? 87.741  100.525 158.150 1.00 48.65  ? 521  ASP A O     1 
ATOM   3839 C  CB    . ASP A 1 521  ? 87.312  103.170 158.590 1.00 48.65  ? 521  ASP A CB    1 
ATOM   3840 C  CG    . ASP A 1 521  ? 86.625  102.919 159.916 1.00 48.65  ? 521  ASP A CG    1 
ATOM   3841 O  OD1   . ASP A 1 521  ? 87.214  103.255 160.964 1.00 48.65  ? 521  ASP A OD1   1 
ATOM   3842 O  OD2   . ASP A 1 521  ? 85.496  102.385 159.911 1.00 48.65  ? 521  ASP A OD2   1 
ATOM   3843 N  N     . PRO A 1 522  ? 89.906  100.494 158.709 1.00 50.09  ? 522  PRO A N     1 
ATOM   3844 C  CA    . PRO A 1 522  ? 89.984  99.038  158.600 1.00 50.09  ? 522  PRO A CA    1 
ATOM   3845 C  C     . PRO A 1 522  ? 89.676  98.357  159.929 1.00 50.09  ? 522  PRO A C     1 
ATOM   3846 O  O     . PRO A 1 522  ? 89.609  98.988  160.985 1.00 50.09  ? 522  PRO A O     1 
ATOM   3847 C  CB    . PRO A 1 522  ? 91.447  98.801  158.192 1.00 50.09  ? 522  PRO A CB    1 
ATOM   3848 C  CG    . PRO A 1 522  ? 92.185  100.095 158.542 1.00 50.09  ? 522  PRO A CG    1 
ATOM   3849 C  CD    . PRO A 1 522  ? 91.196  101.071 159.111 1.00 50.09  ? 522  PRO A CD    1 
ATOM   3850 N  N     . LYS A 1 523  ? 89.487  97.041  159.852 1.00 51.83  ? 523  LYS A N     1 
ATOM   3851 C  CA    . LYS A 1 523  ? 89.245  96.238  161.042 1.00 51.83  ? 523  LYS A CA    1 
ATOM   3852 C  C     . LYS A 1 523  ? 90.528  95.788  161.725 1.00 51.83  ? 523  LYS A C     1 
ATOM   3853 O  O     . LYS A 1 523  ? 90.497  95.460  162.916 1.00 51.83  ? 523  LYS A O     1 
ATOM   3854 C  CB    . LYS A 1 523  ? 88.402  95.009  160.691 1.00 51.83  ? 523  LYS A CB    1 
ATOM   3855 C  CG    . LYS A 1 523  ? 86.907  95.269  160.695 1.00 51.83  ? 523  LYS A CG    1 
ATOM   3856 C  CD    . LYS A 1 523  ? 86.419  95.654  162.081 1.00 51.83  ? 523  LYS A CD    1 
ATOM   3857 C  CE    . LYS A 1 523  ? 86.031  94.428  162.892 1.00 51.83  ? 523  LYS A CE    1 
ATOM   3858 N  NZ    . LYS A 1 523  ? 86.000  94.714  164.353 1.00 51.83  ? 523  LYS A NZ    1 
ATOM   3859 N  N     . ILE A 1 524  ? 91.646  95.760  161.005 1.00 48.71  ? 524  ILE A N     1 
ATOM   3860 C  CA    . ILE A 1 524  ? 92.944  95.404  161.565 1.00 48.71  ? 524  ILE A CA    1 
ATOM   3861 C  C     . ILE A 1 524  ? 93.927  96.503  161.191 1.00 48.71  ? 524  ILE A C     1 
ATOM   3862 O  O     . ILE A 1 524  ? 94.075  96.829  160.007 1.00 48.71  ? 524  ILE A O     1 
ATOM   3863 C  CB    . ILE A 1 524  ? 93.441  94.041  161.058 1.00 48.71  ? 524  ILE A CB    1 
ATOM   3864 C  CG1   . ILE A 1 524  ? 92.440  92.941  161.411 1.00 48.71  ? 524  ILE A CG1   1 
ATOM   3865 C  CG2   . ILE A 1 524  ? 94.810  93.726  161.635 1.00 48.71  ? 524  ILE A CG2   1 
ATOM   3866 C  CD1   . ILE A 1 524  ? 92.387  91.820  160.400 1.00 48.71  ? 524  ILE A CD1   1 
ATOM   3867 N  N     . LEU A 1 525  ? 94.597  97.067  162.190 1.00 45.84  ? 525  LEU A N     1 
ATOM   3868 C  CA    . LEU A 1 525  ? 95.557  98.141  161.977 1.00 45.84  ? 525  LEU A CA    1 
ATOM   3869 C  C     . LEU A 1 525  ? 96.972  97.601  162.119 1.00 45.84  ? 525  LEU A C     1 
ATOM   3870 O  O     . LEU A 1 525  ? 97.303  96.970  163.129 1.00 45.84  ? 525  LEU A O     1 
ATOM   3871 C  CB    . LEU A 1 525  ? 95.328  99.284  162.965 1.00 45.84  ? 525  LEU A CB    1 
ATOM   3872 C  CG    . LEU A 1 525  ? 95.786  100.657 162.477 1.00 45.84  ? 525  LEU A CG    1 
ATOM   3873 C  CD1   . LEU A 1 525  ? 94.880  101.160 161.367 1.00 45.84  ? 525  LEU A CD1   1 
ATOM   3874 C  CD2   . LEU A 1 525  ? 95.828  101.645 163.627 1.00 45.84  ? 525  LEU A CD2   1 
ATOM   3875 N  N     . LEU A 1 526  ? 97.800  97.851  161.111 1.00 43.77  ? 526  LEU A N     1 
ATOM   3876 C  CA    . LEU A 1 526  ? 99.194  97.419  161.093 1.00 43.77  ? 526  LEU A CA    1 
ATOM   3877 C  C     . LEU A 1 526  ? 100.068 98.665  161.201 1.00 43.77  ? 526  LEU A C     1 
ATOM   3878 O  O     . LEU A 1 526  ? 100.473 99.247  160.195 1.00 43.77  ? 526  LEU A O     1 
ATOM   3879 C  CB    . LEU A 1 526  ? 99.507  96.624  159.831 1.00 43.77  ? 526  LEU A CB    1 
ATOM   3880 C  CG    . LEU A 1 526  ? 99.031  95.172  159.805 1.00 43.77  ? 526  LEU A CG    1 
ATOM   3881 C  CD1   . LEU A 1 526  ? 98.845  94.698  158.375 1.00 43.77  ? 526  LEU A CD1   1 
ATOM   3882 C  CD2   . LEU A 1 526  ? 100.011 94.280  160.545 1.00 43.77  ? 526  LEU A CD2   1 
ATOM   3883 N  N     . LEU A 1 527  ? 100.355 99.070  162.434 1.00 47.78  ? 527  LEU A N     1 
ATOM   3884 C  CA    . LEU A 1 527  ? 101.205 100.230 162.688 1.00 47.78  ? 527  LEU A CA    1 
ATOM   3885 C  C     . LEU A 1 527  ? 102.659 99.789  162.604 1.00 47.78  ? 527  LEU A C     1 
ATOM   3886 O  O     . LEU A 1 527  ? 103.199 99.200  163.542 1.00 47.78  ? 527  LEU A O     1 
ATOM   3887 C  CB    . LEU A 1 527  ? 100.889 100.845 164.046 1.00 47.78  ? 527  LEU A CB    1 
ATOM   3888 C  CG    . LEU A 1 527  ? 99.795  101.912 164.067 1.00 47.78  ? 527  LEU A CG    1 
ATOM   3889 C  CD1   . LEU A 1 527  ? 99.355  102.197 165.492 1.00 47.78  ? 527  LEU A CD1   1 
ATOM   3890 C  CD2   . LEU A 1 527  ? 100.279 103.182 163.390 1.00 47.78  ? 527  LEU A CD2   1 
ATOM   3891 N  N     . ASP A 1 528  ? 103.298 100.079 161.474 1.00 51.62  ? 528  ASP A N     1 
ATOM   3892 C  CA    . ASP A 1 528  ? 104.708 99.767  161.284 1.00 51.62  ? 528  ASP A CA    1 
ATOM   3893 C  C     . ASP A 1 528  ? 105.550 100.822 161.986 1.00 51.62  ? 528  ASP A C     1 
ATOM   3894 O  O     . ASP A 1 528  ? 105.031 101.583 162.808 1.00 51.62  ? 528  ASP A O     1 
ATOM   3895 C  CB    . ASP A 1 528  ? 105.055 99.691  159.797 1.00 51.62  ? 528  ASP A CB    1 
ATOM   3896 C  CG    . ASP A 1 528  ? 106.181 98.721  159.510 1.00 51.62  ? 528  ASP A CG    1 
ATOM   3897 O  OD1   . ASP A 1 528  ? 106.936 98.395  160.449 1.00 51.62  ? 528  ASP A OD1   1 
ATOM   3898 O  OD2   . ASP A 1 528  ? 106.311 98.285  158.347 1.00 51.62  ? 528  ASP A OD2   1 
ATOM   3899 N  N     . GLU A 1 529  ? 106.843 100.892 161.671 1.00 52.28  ? 529  GLU A N     1 
ATOM   3900 C  CA    . GLU A 1 529  ? 107.717 101.816 162.383 1.00 52.28  ? 529  GLU A CA    1 
ATOM   3901 C  C     . GLU A 1 529  ? 107.437 103.251 161.960 1.00 52.28  ? 529  GLU A C     1 
ATOM   3902 O  O     . GLU A 1 529  ? 108.328 103.951 161.469 1.00 52.28  ? 529  GLU A O     1 
ATOM   3903 C  CB    . GLU A 1 529  ? 109.188 101.471 162.137 1.00 52.28  ? 529  GLU A CB    1 
ATOM   3904 C  CG    . GLU A 1 529  ? 109.614 100.118 162.681 1.00 52.28  ? 529  GLU A CG    1 
ATOM   3905 C  CD    . GLU A 1 529  ? 109.678 99.051  161.607 1.00 52.28  ? 529  GLU A CD    1 
ATOM   3906 O  OE1   . GLU A 1 529  ? 109.541 99.396  160.415 1.00 52.28  ? 529  GLU A OE1   1 
ATOM   3907 O  OE2   . GLU A 1 529  ? 109.866 97.866  161.952 1.00 52.28  ? 529  GLU A OE2   1 
ATOM   3908 N  N     . ALA A 1 530  ? 106.197 103.691 162.151 1.00 50.85  ? 530  ALA A N     1 
ATOM   3909 C  CA    . ALA A 1 530  ? 105.805 105.073 161.938 1.00 50.85  ? 530  ALA A CA    1 
ATOM   3910 C  C     . ALA A 1 530  ? 105.889 105.818 163.268 1.00 50.85  ? 530  ALA A C     1 
ATOM   3911 O  O     . ALA A 1 530  ? 106.428 105.307 164.253 1.00 50.85  ? 530  ALA A O     1 
ATOM   3912 C  CB    . ALA A 1 530  ? 104.408 105.141 161.324 1.00 50.85  ? 530  ALA A CB    1 
ATOM   3913 N  N     . THR A 1 531  ? 105.345 107.033 163.307 1.00 53.10  ? 531  THR A N     1 
ATOM   3914 C  CA    . THR A 1 531  ? 105.348 107.867 164.508 1.00 53.10  ? 531  THR A CA    1 
ATOM   3915 C  C     . THR A 1 531  ? 106.769 108.046 165.041 1.00 53.10  ? 531  THR A C     1 
ATOM   3916 O  O     . THR A 1 531  ? 107.034 107.939 166.240 1.00 53.10  ? 531  THR A O     1 
ATOM   3917 C  CB    . THR A 1 531  ? 104.424 107.289 165.583 1.00 53.10  ? 531  THR A CB    1 
ATOM   3918 O  OG1   . THR A 1 531  ? 104.997 106.090 166.118 1.00 53.10  ? 531  THR A OG1   1 
ATOM   3919 C  CG2   . THR A 1 531  ? 103.060 106.970 164.996 1.00 53.10  ? 531  THR A CG2   1 
ATOM   3920 N  N     . SER A 1 532  ? 107.694 108.311 164.123 1.00 52.60  ? 532  SER A N     1 
ATOM   3921 C  CA    . SER A 1 532  ? 109.099 108.515 164.454 1.00 52.60  ? 532  SER A CA    1 
ATOM   3922 C  C     . SER A 1 532  ? 109.535 109.966 164.358 1.00 52.60  ? 532  SER A C     1 
ATOM   3923 O  O     . SER A 1 532  ? 110.349 110.413 165.168 1.00 52.60  ? 532  SER A O     1 
ATOM   3924 C  CB    . SER A 1 532  ? 109.984 107.663 163.538 1.00 52.60  ? 532  SER A CB    1 
ATOM   3925 O  OG    . SER A 1 532  ? 109.764 107.984 162.176 1.00 52.60  ? 532  SER A OG    1 
ATOM   3926 N  N     . ALA A 1 533  ? 109.018 110.715 163.383 1.00 55.10  ? 533  ALA A N     1 
ATOM   3927 C  CA    . ALA A 1 533  ? 109.392 112.117 163.240 1.00 55.10  ? 533  ALA A CA    1 
ATOM   3928 C  C     . ALA A 1 533  ? 108.700 113.009 164.263 1.00 55.10  ? 533  ALA A C     1 
ATOM   3929 O  O     . ALA A 1 533  ? 109.286 114.003 164.705 1.00 55.10  ? 533  ALA A O     1 
ATOM   3930 C  CB    . ALA A 1 533  ? 109.081 112.600 161.825 1.00 55.10  ? 533  ALA A CB    1 
ATOM   3931 N  N     . LEU A 1 534  ? 107.466 112.681 164.645 1.00 63.41  ? 534  LEU A N     1 
ATOM   3932 C  CA    . LEU A 1 534  ? 106.739 113.480 165.624 1.00 63.41  ? 534  LEU A CA    1 
ATOM   3933 C  C     . LEU A 1 534  ? 107.458 113.440 166.966 1.00 63.41  ? 534  LEU A C     1 
ATOM   3934 O  O     . LEU A 1 534  ? 107.645 112.367 167.547 1.00 63.41  ? 534  LEU A O     1 
ATOM   3935 C  CB    . LEU A 1 534  ? 105.312 112.958 165.762 1.00 63.41  ? 534  LEU A CB    1 
ATOM   3936 C  CG    . LEU A 1 534  ? 104.585 112.654 164.451 1.00 63.41  ? 534  LEU A CG    1 
ATOM   3937 C  CD1   . LEU A 1 534  ? 103.171 112.167 164.722 1.00 63.41  ? 534  LEU A CD1   1 
ATOM   3938 C  CD2   . LEU A 1 534  ? 104.569 113.880 163.555 1.00 63.41  ? 534  LEU A CD2   1 
ATOM   3939 N  N     . ASP A 1 535  ? 107.892 114.606 167.442 1.00 76.30  ? 535  ASP A N     1 
ATOM   3940 C  CA    . ASP A 1 535  ? 108.746 114.658 168.624 1.00 76.30  ? 535  ASP A CA    1 
ATOM   3941 C  C     . ASP A 1 535  ? 108.086 114.215 169.932 1.00 76.30  ? 535  ASP A C     1 
ATOM   3942 O  O     . ASP A 1 535  ? 108.397 113.133 170.441 1.00 76.30  ? 535  ASP A O     1 
ATOM   3943 C  CB    . ASP A 1 535  ? 109.312 116.078 168.760 1.00 76.30  ? 535  ASP A CB    1 
ATOM   3944 C  CG    . ASP A 1 535  ? 108.232 117.127 168.967 1.00 76.30  ? 535  ASP A CG    1 
ATOM   3945 O  OD1   . ASP A 1 535  ? 107.036 116.767 168.964 1.00 76.30  ? 535  ASP A OD1   1 
ATOM   3946 O  OD2   . ASP A 1 535  ? 108.575 118.307 169.152 1.00 76.30  ? 535  ASP A OD2   1 
ATOM   3947 N  N     . ALA A 1 536  ? 107.183 115.025 170.490 1.00 78.21  ? 536  ALA A N     1 
ATOM   3948 C  CA    . ALA A 1 536  ? 106.598 114.705 171.787 1.00 78.21  ? 536  ALA A CA    1 
ATOM   3949 C  C     . ALA A 1 536  ? 105.090 114.921 171.849 1.00 78.21  ? 536  ALA A C     1 
ATOM   3950 O  O     . ALA A 1 536  ? 104.367 114.120 172.450 1.00 78.21  ? 536  ALA A O     1 
ATOM   3951 C  CB    . ALA A 1 536  ? 107.279 115.530 172.880 1.00 78.21  ? 536  ALA A CB    1 
ATOM   3952 N  N     . SER A 1 537  ? 104.607 115.998 171.231 1.00 75.12  ? 537  SER A N     1 
ATOM   3953 C  CA    . SER A 1 537  ? 103.222 116.423 171.408 1.00 75.12  ? 537  SER A CA    1 
ATOM   3954 C  C     . SER A 1 537  ? 102.309 115.840 170.339 1.00 75.12  ? 537  SER A C     1 
ATOM   3955 O  O     . SER A 1 537  ? 101.228 115.322 170.650 1.00 75.12  ? 537  SER A O     1 
ATOM   3956 C  CB    . SER A 1 537  ? 103.139 117.952 171.403 1.00 75.12  ? 537  SER A CB    1 
ATOM   3957 O  OG    . SER A 1 537  ? 103.894 118.496 170.336 1.00 75.12  ? 537  SER A OG    1 
ATOM   3958 N  N     . SER A 1 538  ? 102.728 115.925 169.074 1.00 68.32  ? 538  SER A N     1 
ATOM   3959 C  CA    . SER A 1 538  ? 102.014 115.218 168.022 1.00 68.32  ? 538  SER A CA    1 
ATOM   3960 C  C     . SER A 1 538  ? 101.939 113.731 168.326 1.00 68.32  ? 538  SER A C     1 
ATOM   3961 O  O     . SER A 1 538  ? 100.945 113.079 167.991 1.00 68.32  ? 538  SER A O     1 
ATOM   3962 C  CB    . SER A 1 538  ? 102.689 115.459 166.673 1.00 68.32  ? 538  SER A CB    1 
ATOM   3963 O  OG    . SER A 1 538  ? 102.661 116.833 166.329 1.00 68.32  ? 538  SER A OG    1 
ATOM   3964 N  N     . GLU A 1 539  ? 102.968 113.186 168.980 1.00 66.89  ? 539  GLU A N     1 
ATOM   3965 C  CA    . GLU A 1 539  ? 102.921 111.797 169.418 1.00 66.89  ? 539  GLU A CA    1 
ATOM   3966 C  C     . GLU A 1 539  ? 101.743 111.560 170.351 1.00 66.89  ? 539  GLU A C     1 
ATOM   3967 O  O     . GLU A 1 539  ? 100.960 110.625 170.154 1.00 66.89  ? 539  GLU A O     1 
ATOM   3968 C  CB    . GLU A 1 539  ? 104.229 111.417 170.110 1.00 66.89  ? 539  GLU A CB    1 
ATOM   3969 C  CG    . GLU A 1 539  ? 105.343 111.054 169.160 1.00 66.89  ? 539  GLU A CG    1 
ATOM   3970 C  CD    . GLU A 1 539  ? 104.971 109.921 168.228 1.00 66.89  ? 539  GLU A CD    1 
ATOM   3971 O  OE1   . GLU A 1 539  ? 104.285 108.977 168.672 1.00 66.89  ? 539  GLU A OE1   1 
ATOM   3972 O  OE2   . GLU A 1 539  ? 105.359 109.984 167.044 1.00 66.89  ? 539  GLU A OE2   1 
ATOM   3973 N  N     . SER A 1 540  ? 101.597 112.404 171.373 1.00 71.13  ? 540  SER A N     1 
ATOM   3974 C  CA    . SER A 1 540  ? 100.499 112.231 172.317 1.00 71.13  ? 540  SER A CA    1 
ATOM   3975 C  C     . SER A 1 540  ? 99.151  112.374 171.622 1.00 71.13  ? 540  SER A C     1 
ATOM   3976 O  O     . SER A 1 540  ? 98.221  111.600 171.887 1.00 71.13  ? 540  SER A O     1 
ATOM   3977 C  CB    . SER A 1 540  ? 100.627 113.237 173.459 1.00 71.13  ? 540  SER A CB    1 
ATOM   3978 O  OG    . SER A 1 540  ? 100.111 114.502 173.084 1.00 71.13  ? 540  SER A OG    1 
ATOM   3979 N  N     . ILE A 1 541  ? 99.032  113.348 170.718 1.00 69.99  ? 541  ILE A N     1 
ATOM   3980 C  CA    . ILE A 1 541  ? 97.756  113.574 170.041 1.00 69.99  ? 541  ILE A CA    1 
ATOM   3981 C  C     . ILE A 1 541  ? 97.387  112.371 169.178 1.00 69.99  ? 541  ILE A C     1 
ATOM   3982 O  O     . ILE A 1 541  ? 96.239  111.903 169.189 1.00 69.99  ? 541  ILE A O     1 
ATOM   3983 C  CB    . ILE A 1 541  ? 97.809  114.869 169.213 1.00 69.99  ? 541  ILE A CB    1 
ATOM   3984 C  CG1   . ILE A 1 541  ? 98.124  116.061 170.117 1.00 69.99  ? 541  ILE A CG1   1 
ATOM   3985 C  CG2   . ILE A 1 541  ? 96.488  115.096 168.503 1.00 69.99  ? 541  ILE A CG2   1 
ATOM   3986 C  CD1   . ILE A 1 541  ? 97.092  116.297 171.195 1.00 69.99  ? 541  ILE A CD1   1 
ATOM   3987 N  N     . VAL A 1 542  ? 98.352  111.846 168.417 1.00 70.68  ? 542  VAL A N     1 
ATOM   3988 C  CA    . VAL A 1 542  ? 98.043  110.713 167.551 1.00 70.68  ? 542  VAL A CA    1 
ATOM   3989 C  C     . VAL A 1 542  ? 97.786  109.453 168.368 1.00 70.68  ? 542  VAL A C     1 
ATOM   3990 O  O     . VAL A 1 542  ? 96.959  108.624 167.978 1.00 70.68  ? 542  VAL A O     1 
ATOM   3991 C  CB    . VAL A 1 542  ? 99.144  110.494 166.492 1.00 70.68  ? 542  VAL A CB    1 
ATOM   3992 C  CG1   . VAL A 1 542  ? 99.339  111.751 165.660 1.00 70.68  ? 542  VAL A CG1   1 
ATOM   3993 C  CG2   . VAL A 1 542  ? 100.449 110.053 167.130 1.00 70.68  ? 542  VAL A CG2   1 
ATOM   3994 N  N     . GLN A 1 543  ? 98.467  109.276 169.506 1.00 74.22  ? 543  GLN A N     1 
ATOM   3995 C  CA    . GLN A 1 543  ? 98.157  108.130 170.358 1.00 74.22  ? 543  GLN A CA    1 
ATOM   3996 C  C     . GLN A 1 543  ? 96.751  108.231 170.934 1.00 74.22  ? 543  GLN A C     1 
ATOM   3997 O  O     . GLN A 1 543  ? 96.047  107.221 171.040 1.00 74.22  ? 543  GLN A O     1 
ATOM   3998 C  CB    . GLN A 1 543  ? 99.186  107.987 171.480 1.00 74.22  ? 543  GLN A CB    1 
ATOM   3999 C  CG    . GLN A 1 543  ? 100.612 107.802 171.004 1.00 74.22  ? 543  GLN A CG    1 
ATOM   4000 C  CD    . GLN A 1 543  ? 101.419 106.908 171.918 1.00 74.22  ? 543  GLN A CD    1 
ATOM   4001 O  OE1   . GLN A 1 543  ? 101.070 106.711 173.082 1.00 74.22  ? 543  GLN A OE1   1 
ATOM   4002 N  NE2   . GLN A 1 543  ? 102.509 106.360 171.396 1.00 74.22  ? 543  GLN A NE2   1 
ATOM   4003 N  N     . GLU A 1 544  ? 96.328  109.435 171.328 1.00 75.97  ? 544  GLU A N     1 
ATOM   4004 C  CA    . GLU A 1 544  ? 94.957  109.600 171.798 1.00 75.97  ? 544  GLU A CA    1 
ATOM   4005 C  C     . GLU A 1 544  ? 93.958  109.285 170.692 1.00 75.97  ? 544  GLU A C     1 
ATOM   4006 O  O     . GLU A 1 544  ? 92.976  108.565 170.914 1.00 75.97  ? 544  GLU A O     1 
ATOM   4007 C  CB    . GLU A 1 544  ? 94.747  111.018 172.329 1.00 75.97  ? 544  GLU A CB    1 
ATOM   4008 C  CG    . GLU A 1 544  ? 95.514  111.320 173.605 1.00 75.97  ? 544  GLU A CG    1 
ATOM   4009 C  CD    . GLU A 1 544  ? 94.633  111.291 174.837 1.00 75.97  ? 544  GLU A CD    1 
ATOM   4010 O  OE1   . GLU A 1 544  ? 93.394  111.289 174.683 1.00 75.97  ? 544  GLU A OE1   1 
ATOM   4011 O  OE2   . GLU A 1 544  ? 95.180  111.271 175.960 1.00 75.97  ? 544  GLU A OE2   1 
ATOM   4012 N  N     . ALA A 1 545  ? 94.206  109.789 169.482 1.00 72.57  ? 545  ALA A N     1 
ATOM   4013 C  CA    . ALA A 1 545  ? 93.315  109.480 168.367 1.00 72.57  ? 545  ALA A CA    1 
ATOM   4014 C  C     . ALA A 1 545  ? 93.257  107.978 168.116 1.00 72.57  ? 545  ALA A C     1 
ATOM   4015 O  O     . ALA A 1 545  ? 92.171  107.399 167.972 1.00 72.57  ? 545  ALA A O     1 
ATOM   4016 C  CB    . ALA A 1 545  ? 93.771  110.221 167.111 1.00 72.57  ? 545  ALA A CB    1 
ATOM   4017 N  N     . LEU A 1 546  ? 94.420  107.324 168.098 1.00 76.97  ? 546  LEU A N     1 
ATOM   4018 C  CA    . LEU A 1 546  ? 94.523  105.894 167.847 1.00 76.97  ? 546  LEU A CA    1 
ATOM   4019 C  C     . LEU A 1 546  ? 93.756  105.105 168.896 1.00 76.97  ? 546  LEU A C     1 
ATOM   4020 O  O     . LEU A 1 546  ? 92.791  104.410 168.564 1.00 76.97  ? 546  LEU A O     1 
ATOM   4021 C  CB    . LEU A 1 546  ? 95.991  105.463 167.818 1.00 76.97  ? 546  LEU A CB    1 
ATOM   4022 C  CG    . LEU A 1 546  ? 96.736  105.744 166.511 1.00 76.97  ? 546  LEU A CG    1 
ATOM   4023 C  CD1   . LEU A 1 546  ? 98.232  105.527 166.682 1.00 76.97  ? 546  LEU A CD1   1 
ATOM   4024 C  CD2   . LEU A 1 546  ? 96.190  104.880 165.388 1.00 76.97  ? 546  LEU A CD2   1 
ATOM   4025 N  N     . ASP A 1 547  ? 94.152  105.208 170.165 1.00 77.64  ? 547  ASP A N     1 
ATOM   4026 C  CA    . ASP A 1 547  ? 93.376  104.541 171.206 1.00 77.64  ? 547  ASP A CA    1 
ATOM   4027 C  C     . ASP A 1 547  ? 92.208  105.388 171.688 1.00 77.64  ? 547  ASP A C     1 
ATOM   4028 O  O     . ASP A 1 547  ? 91.928  105.466 172.886 1.00 77.64  ? 547  ASP A O     1 
ATOM   4029 C  CB    . ASP A 1 547  ? 94.297  104.175 172.367 1.00 77.64  ? 547  ASP A CB    1 
ATOM   4030 C  CG    . ASP A 1 547  ? 95.347  103.157 171.976 1.00 77.64  ? 547  ASP A CG    1 
ATOM   4031 O  OD1   . ASP A 1 547  ? 95.081  102.350 171.062 1.00 77.64  ? 547  ASP A OD1   1 
ATOM   4032 O  OD2   . ASP A 1 547  ? 96.439  103.163 172.584 1.00 77.64  ? 547  ASP A OD2   1 
ATOM   4033 N  N     . ARG A 1 548  ? 91.514  106.029 170.751 1.00 76.24  ? 548  ARG A N     1 
ATOM   4034 C  CA    . ARG A 1 548  ? 90.119  106.406 170.918 1.00 76.24  ? 548  ARG A CA    1 
ATOM   4035 C  C     . ARG A 1 548  ? 89.229  105.967 169.765 1.00 76.24  ? 548  ARG A C     1 
ATOM   4036 O  O     . ARG A 1 548  ? 88.022  105.804 169.981 1.00 76.24  ? 548  ARG A O     1 
ATOM   4037 C  CB    . ARG A 1 548  ? 89.977  107.925 171.096 1.00 76.24  ? 548  ARG A CB    1 
ATOM   4038 C  CG    . ARG A 1 548  ? 90.250  108.419 172.505 1.00 76.24  ? 548  ARG A CG    1 
ATOM   4039 C  CD    . ARG A 1 548  ? 90.130  109.931 172.580 1.00 76.24  ? 548  ARG A CD    1 
ATOM   4040 N  NE    . ARG A 1 548  ? 91.156  110.602 171.788 1.00 76.24  ? 548  ARG A NE    1 
ATOM   4041 C  CZ    . ARG A 1 548  ? 91.150  111.901 171.507 1.00 76.24  ? 548  ARG A CZ    1 
ATOM   4042 N  NH1   . ARG A 1 548  ? 92.124  112.429 170.777 1.00 76.24  ? 548  ARG A NH1   1 
ATOM   4043 N  NH2   . ARG A 1 548  ? 90.169  112.673 171.954 1.00 76.24  ? 548  ARG A NH2   1 
ATOM   4044 N  N     . VAL A 1 549  ? 89.765  105.767 168.559 1.00 74.54  ? 549  VAL A N     1 
ATOM   4045 C  CA    . VAL A 1 549  ? 88.960  105.287 167.446 1.00 74.54  ? 549  VAL A CA    1 
ATOM   4046 C  C     . VAL A 1 549  ? 89.287  103.846 167.059 1.00 74.54  ? 549  VAL A C     1 
ATOM   4047 O  O     . VAL A 1 549  ? 88.430  103.167 166.481 1.00 74.54  ? 549  VAL A O     1 
ATOM   4048 C  CB    . VAL A 1 549  ? 89.079  106.214 166.218 1.00 74.54  ? 549  VAL A CB    1 
ATOM   4049 C  CG1   . VAL A 1 549  ? 88.569  107.609 166.548 1.00 74.54  ? 549  VAL A CG1   1 
ATOM   4050 C  CG2   . VAL A 1 549  ? 90.503  106.249 165.693 1.00 74.54  ? 549  VAL A CG2   1 
ATOM   4051 N  N     . MET A 1 550  ? 90.490  103.357 167.355 1.00 74.28  ? 550  MET A N     1 
ATOM   4052 C  CA    . MET A 1 550  ? 90.888  102.001 166.998 1.00 74.28  ? 550  MET A CA    1 
ATOM   4053 C  C     . MET A 1 550  ? 90.648  100.994 168.115 1.00 74.28  ? 550  MET A C     1 
ATOM   4054 O  O     . MET A 1 550  ? 91.071  99.840  167.991 1.00 74.28  ? 550  MET A O     1 
ATOM   4055 C  CB    . MET A 1 550  ? 92.362  101.973 166.583 1.00 74.28  ? 550  MET A CB    1 
ATOM   4056 C  CG    . MET A 1 550  ? 92.676  102.744 165.310 1.00 74.28  ? 550  MET A CG    1 
ATOM   4057 S  SD    . MET A 1 550  ? 91.820  102.093 163.859 1.00 74.28  ? 550  MET A SD    1 
ATOM   4058 C  CE    . MET A 1 550  ? 90.486  103.271 163.661 1.00 74.28  ? 550  MET A CE    1 
ATOM   4059 N  N     . VAL A 1 551  ? 89.991  101.401 169.201 1.00 71.67  ? 551  VAL A N     1 
ATOM   4060 C  CA    . VAL A 1 551  ? 89.669  100.469 170.273 1.00 71.67  ? 551  VAL A CA    1 
ATOM   4061 C  C     . VAL A 1 551  ? 88.648  99.454  169.775 1.00 71.67  ? 551  VAL A C     1 
ATOM   4062 O  O     . VAL A 1 551  ? 87.735  99.785  169.006 1.00 71.67  ? 551  VAL A O     1 
ATOM   4063 C  CB    . VAL A 1 551  ? 89.158  101.230 171.510 1.00 71.67  ? 551  VAL A CB    1 
ATOM   4064 C  CG1   . VAL A 1 551  ? 87.921  102.049 171.169 1.00 71.67  ? 551  VAL A CG1   1 
ATOM   4065 C  CG2   . VAL A 1 551  ? 88.875  100.269 172.656 1.00 71.67  ? 551  VAL A CG2   1 
ATOM   4066 N  N     . GLY A 1 552  ? 88.809  98.203  170.198 1.00 66.12  ? 552  GLY A N     1 
ATOM   4067 C  CA    . GLY A 1 552  ? 87.919  97.141  169.784 1.00 66.12  ? 552  GLY A CA    1 
ATOM   4068 C  C     . GLY A 1 552  ? 88.265  96.481  168.469 1.00 66.12  ? 552  GLY A C     1 
ATOM   4069 O  O     . GLY A 1 552  ? 87.458  95.693  167.962 1.00 66.12  ? 552  GLY A O     1 
ATOM   4070 N  N     . ARG A 1 553  ? 89.432  96.773  167.901 1.00 59.84  ? 553  ARG A N     1 
ATOM   4071 C  CA    . ARG A 1 553  ? 89.865  96.184  166.644 1.00 59.84  ? 553  ARG A CA    1 
ATOM   4072 C  C     . ARG A 1 553  ? 91.276  95.638  166.800 1.00 59.84  ? 553  ARG A C     1 
ATOM   4073 O  O     . ARG A 1 553  ? 92.055  96.121  167.627 1.00 59.84  ? 553  ARG A O     1 
ATOM   4074 C  CB    . ARG A 1 553  ? 89.822  97.206  165.501 1.00 59.84  ? 553  ARG A CB    1 
ATOM   4075 C  CG    . ARG A 1 553  ? 88.456  97.832  165.280 1.00 59.84  ? 553  ARG A CG    1 
ATOM   4076 C  CD    . ARG A 1 553  ? 88.384  98.539  163.938 1.00 59.84  ? 553  ARG A CD    1 
ATOM   4077 N  NE    . ARG A 1 553  ? 87.015  98.893  163.577 1.00 59.84  ? 553  ARG A NE    1 
ATOM   4078 C  CZ    . ARG A 1 553  ? 86.690  99.663  162.545 1.00 59.84  ? 553  ARG A CZ    1 
ATOM   4079 N  NH1   . ARG A 1 553  ? 85.417  99.933  162.292 1.00 59.84  ? 553  ARG A NH1   1 
ATOM   4080 N  NH2   . ARG A 1 553  ? 87.637  100.164 161.764 1.00 59.84  ? 553  ARG A NH2   1 
ATOM   4081 N  N     . THR A 1 554  ? 91.594  94.621  166.002 1.00 58.54  ? 554  THR A N     1 
ATOM   4082 C  CA    . THR A 1 554  ? 92.915  94.009  166.065 1.00 58.54  ? 554  THR A CA    1 
ATOM   4083 C  C     . THR A 1 554  ? 93.990  95.034  165.728 1.00 58.54  ? 554  THR A C     1 
ATOM   4084 O  O     . THR A 1 554  ? 93.889  95.763  164.738 1.00 58.54  ? 554  THR A O     1 
ATOM   4085 C  CB    . THR A 1 554  ? 92.998  92.823  165.104 1.00 58.54  ? 554  THR A CB    1 
ATOM   4086 O  OG1   . THR A 1 554  ? 91.825  92.011  165.241 1.00 58.54  ? 554  THR A OG1   1 
ATOM   4087 C  CG2   . THR A 1 554  ? 94.227  91.981  165.406 1.00 58.54  ? 554  THR A CG2   1 
ATOM   4088 N  N     . THR A 1 555  ? 95.026  95.087  166.561 1.00 59.52  ? 555  THR A N     1 
ATOM   4089 C  CA    . THR A 1 555  ? 96.068  96.097  166.447 1.00 59.52  ? 555  THR A CA    1 
ATOM   4090 C  C     . THR A 1 555  ? 97.435  95.434  166.519 1.00 59.52  ? 555  THR A C     1 
ATOM   4091 O  O     . THR A 1 555  ? 97.700  94.650  167.436 1.00 59.52  ? 555  THR A O     1 
ATOM   4092 C  CB    . THR A 1 555  ? 95.933  97.150  167.553 1.00 59.52  ? 555  THR A CB    1 
ATOM   4093 O  OG1   . THR A 1 555  ? 94.738  97.912  167.346 1.00 59.52  ? 555  THR A OG1   1 
ATOM   4094 C  CG2   . THR A 1 555  ? 97.127  98.088  167.548 1.00 59.52  ? 555  THR A CG2   1 
ATOM   4095 N  N     . VAL A 1 556  ? 98.297  95.752  165.556 1.00 53.64  ? 556  VAL A N     1 
ATOM   4096 C  CA    . VAL A 1 556  ? 99.679  95.285  165.534 1.00 53.64  ? 556  VAL A CA    1 
ATOM   4097 C  C     . VAL A 1 556  ? 100.565 96.519  165.465 1.00 53.64  ? 556  VAL A C     1 
ATOM   4098 O  O     . VAL A 1 556  ? 100.480 97.295  164.505 1.00 53.64  ? 556  VAL A O     1 
ATOM   4099 C  CB    . VAL A 1 556  ? 99.959  94.345  164.355 1.00 53.64  ? 556  VAL A CB    1 
ATOM   4100 C  CG1   . VAL A 1 556  ? 101.447 94.058  164.252 1.00 53.64  ? 556  VAL A CG1   1 
ATOM   4101 C  CG2   . VAL A 1 556  ? 99.172  93.055  164.507 1.00 53.64  ? 556  VAL A CG2   1 
ATOM   4102 N  N     . VAL A 1 557  ? 101.414 96.703  166.471 1.00 57.00  ? 557  VAL A N     1 
ATOM   4103 C  CA    . VAL A 1 557  ? 102.265 97.882  166.583 1.00 57.00  ? 557  VAL A CA    1 
ATOM   4104 C  C     . VAL A 1 557  ? 103.717 97.430  166.543 1.00 57.00  ? 557  VAL A C     1 
ATOM   4105 O  O     . VAL A 1 557  ? 104.127 96.569  167.331 1.00 57.00  ? 557  VAL A O     1 
ATOM   4106 C  CB    . VAL A 1 557  ? 101.976 98.675  167.867 1.00 57.00  ? 557  VAL A CB    1 
ATOM   4107 C  CG1   . VAL A 1 557  ? 103.033 99.744  168.076 1.00 57.00  ? 557  VAL A CG1   1 
ATOM   4108 C  CG2   . VAL A 1 557  ? 100.594 99.297  167.802 1.00 57.00  ? 557  VAL A CG2   1 
ATOM   4109 N  N     . VAL A 1 558  ? 104.488 98.008  165.631 1.00 56.23  ? 558  VAL A N     1 
ATOM   4110 C  CA    . VAL A 1 558  ? 105.917 97.727  165.501 1.00 56.23  ? 558  VAL A CA    1 
ATOM   4111 C  C     . VAL A 1 558  ? 106.635 99.050  165.739 1.00 56.23  ? 558  VAL A C     1 
ATOM   4112 O  O     . VAL A 1 558  ? 106.827 99.849  164.819 1.00 56.23  ? 558  VAL A O     1 
ATOM   4113 C  CB    . VAL A 1 558  ? 106.273 97.133  164.137 1.00 56.23  ? 558  VAL A CB    1 
ATOM   4114 C  CG1   . VAL A 1 558  ? 107.714 96.659  164.127 1.00 56.23  ? 558  VAL A CG1   1 
ATOM   4115 C  CG2   . VAL A 1 558  ? 105.328 95.993  163.787 1.00 56.23  ? 558  VAL A CG2   1 
ATOM   4116 N  N     . ALA A 1 559  ? 107.043 99.293  166.981 1.00 68.41  ? 559  ALA A N     1 
ATOM   4117 C  CA    . ALA A 1 559  ? 107.634 100.563 167.373 1.00 68.41  ? 559  ALA A CA    1 
ATOM   4118 C  C     . ALA A 1 559  ? 109.022 100.345 167.956 1.00 68.41  ? 559  ALA A C     1 
ATOM   4119 O  O     . ALA A 1 559  ? 109.241 99.411  168.734 1.00 68.41  ? 559  ALA A O     1 
ATOM   4120 C  CB    . ALA A 1 559  ? 106.751 101.291 168.391 1.00 68.41  ? 559  ALA A CB    1 
ATOM   4121 N  N     . HIS A 1 560  ? 109.957 101.216 167.576 1.00 76.63  ? 560  HIS A N     1 
ATOM   4122 C  CA    . HIS A 1 560  ? 111.312 101.144 168.112 1.00 76.63  ? 560  HIS A CA    1 
ATOM   4123 C  C     . HIS A 1 560  ? 111.384 101.719 169.521 1.00 76.63  ? 560  HIS A C     1 
ATOM   4124 O  O     . HIS A 1 560  ? 111.781 101.026 170.463 1.00 76.63  ? 560  HIS A O     1 
ATOM   4125 C  CB    . HIS A 1 560  ? 112.288 101.865 167.181 1.00 76.63  ? 560  HIS A CB    1 
ATOM   4126 C  CG    . HIS A 1 560  ? 112.627 101.088 165.950 1.00 76.63  ? 560  HIS A CG    1 
ATOM   4127 N  ND1   . HIS A 1 560  ? 113.466 99.995  165.972 1.00 76.63  ? 560  HIS A ND1   1 
ATOM   4128 C  CD2   . HIS A 1 560  ? 112.237 101.238 164.662 1.00 76.63  ? 560  HIS A CD2   1 
ATOM   4129 C  CE1   . HIS A 1 560  ? 113.584 99.509  164.750 1.00 76.63  ? 560  HIS A CE1   1 
ATOM   4130 N  NE2   . HIS A 1 560  ? 112.846 100.243 163.937 1.00 76.63  ? 560  HIS A NE2   1 
ATOM   4131 N  N     . ARG A 1 561  ? 111.011 102.988 169.683 1.00 89.28  ? 561  ARG A N     1 
ATOM   4132 C  CA    . ARG A 1 561  ? 111.023 103.596 171.006 1.00 89.28  ? 561  ARG A CA    1 
ATOM   4133 C  C     . ARG A 1 561  ? 110.060 102.860 171.930 1.00 89.28  ? 561  ARG A C     1 
ATOM   4134 O  O     . ARG A 1 561  ? 108.910 102.598 171.568 1.00 89.28  ? 561  ARG A O     1 
ATOM   4135 C  CB    . ARG A 1 561  ? 110.657 105.079 170.917 1.00 89.28  ? 561  ARG A CB    1 
ATOM   4136 C  CG    . ARG A 1 561  ? 110.896 105.847 172.209 1.00 89.28  ? 561  ARG A CG    1 
ATOM   4137 C  CD    . ARG A 1 561  ? 110.422 107.289 172.114 1.00 89.28  ? 561  ARG A CD    1 
ATOM   4138 N  NE    . ARG A 1 561  ? 111.133 108.048 171.089 1.00 89.28  ? 561  ARG A NE    1 
ATOM   4139 C  CZ    . ARG A 1 561  ? 110.782 109.266 170.689 1.00 89.28  ? 561  ARG A CZ    1 
ATOM   4140 N  NH1   . ARG A 1 561  ? 109.723 109.858 171.221 1.00 89.28  ? 561  ARG A NH1   1 
ATOM   4141 N  NH2   . ARG A 1 561  ? 111.486 109.890 169.753 1.00 89.28  ? 561  ARG A NH2   1 
ATOM   4142 N  N     . LEU A 1 562  ? 110.539 102.527 173.129 1.00 98.17  ? 562  LEU A N     1 
ATOM   4143 C  CA    . LEU A 1 562  ? 109.796 101.679 174.052 1.00 98.17  ? 562  LEU A CA    1 
ATOM   4144 C  C     . LEU A 1 562  ? 108.698 102.420 174.802 1.00 98.17  ? 562  LEU A C     1 
ATOM   4145 O  O     . LEU A 1 562  ? 107.832 101.769 175.397 1.00 98.17  ? 562  LEU A O     1 
ATOM   4146 C  CB    . LEU A 1 562  ? 110.752 101.044 175.068 1.00 98.17  ? 562  LEU A CB    1 
ATOM   4147 C  CG    . LEU A 1 562  ? 111.530 99.782  174.680 1.00 98.17  ? 562  LEU A CG    1 
ATOM   4148 C  CD1   . LEU A 1 562  ? 110.576 98.645  174.400 1.00 98.17  ? 562  LEU A CD1   1 
ATOM   4149 C  CD2   . LEU A 1 562  ? 112.452 100.001 173.490 1.00 98.17  ? 562  LEU A CD2   1 
ATOM   4150 N  N     . CYS A 1 563  ? 108.714 103.754 174.792 1.00 104.65 ? 563  CYS A N     1 
ATOM   4151 C  CA    . CYS A 1 563  ? 107.734 104.516 175.558 1.00 104.65 ? 563  CYS A CA    1 
ATOM   4152 C  C     . CYS A 1 563  ? 106.363 104.491 174.896 1.00 104.65 ? 563  CYS A C     1 
ATOM   4153 O  O     . CYS A 1 563  ? 105.335 104.520 175.583 1.00 104.65 ? 563  CYS A O     1 
ATOM   4154 C  CB    . CYS A 1 563  ? 108.217 105.953 175.735 1.00 104.65 ? 563  CYS A CB    1 
ATOM   4155 S  SG    . CYS A 1 563  ? 109.949 106.092 176.218 1.00 104.65 ? 563  CYS A SG    1 
ATOM   4156 N  N     . THR A 1 564  ? 106.328 104.456 173.562 1.00 99.19  ? 564  THR A N     1 
ATOM   4157 C  CA    . THR A 1 564  ? 105.055 104.464 172.851 1.00 99.19  ? 564  THR A CA    1 
ATOM   4158 C  C     . THR A 1 564  ? 104.236 103.213 173.139 1.00 99.19  ? 564  THR A C     1 
ATOM   4159 O  O     . THR A 1 564  ? 103.002 103.274 173.170 1.00 99.19  ? 564  THR A O     1 
ATOM   4160 C  CB    . THR A 1 564  ? 105.296 104.600 171.347 1.00 99.19  ? 564  THR A CB    1 
ATOM   4161 O  OG1   . THR A 1 564  ? 106.224 103.596 170.916 1.00 99.19  ? 564  THR A OG1   1 
ATOM   4162 C  CG2   . THR A 1 564  ? 105.858 105.977 171.023 1.00 99.19  ? 564  THR A CG2   1 
ATOM   4163 N  N     . ILE A 1 565  ? 104.897 102.082 173.361 1.00 100.02 ? 565  ILE A N     1 
ATOM   4164 C  CA    . ILE A 1 565  ? 104.220 100.816 173.588 1.00 100.02 ? 565  ILE A CA    1 
ATOM   4165 C  C     . ILE A 1 565  ? 104.191 100.452 175.074 1.00 100.02 ? 565  ILE A C     1 
ATOM   4166 O  O     . ILE A 1 565  ? 104.079 99.277  175.421 1.00 100.02 ? 565  ILE A O     1 
ATOM   4167 C  CB    . ILE A 1 565  ? 104.844 99.689  172.751 1.00 100.02 ? 565  ILE A CB    1 
ATOM   4168 C  CG1   . ILE A 1 565  ? 106.305 99.470  173.148 1.00 100.02 ? 565  ILE A CG1   1 
ATOM   4169 C  CG2   . ILE A 1 565  ? 104.748 100.016 171.273 1.00 100.02 ? 565  ILE A CG2   1 
ATOM   4170 C  CD1   . ILE A 1 565  ? 106.920 98.230  172.536 1.00 100.02 ? 565  ILE A CD1   1 
ATOM   4171 N  N     . ARG A 1 566  ? 104.299 101.446 175.959 1.00 104.77 ? 566  ARG A N     1 
ATOM   4172 C  CA    . ARG A 1 566  ? 104.266 101.169 177.392 1.00 104.77 ? 566  ARG A CA    1 
ATOM   4173 C  C     . ARG A 1 566  ? 102.925 100.580 177.815 1.00 104.77 ? 566  ARG A C     1 
ATOM   4174 O  O     . ARG A 1 566  ? 102.877 99.632  178.608 1.00 104.77 ? 566  ARG A O     1 
ATOM   4175 C  CB    . ARG A 1 566  ? 104.563 102.446 178.178 1.00 104.77 ? 566  ARG A CB    1 
ATOM   4176 C  CG    . ARG A 1 566  ? 104.543 102.269 179.686 1.00 104.77 ? 566  ARG A CG    1 
ATOM   4177 C  CD    . ARG A 1 566  ? 104.715 103.600 180.395 1.00 104.77 ? 566  ARG A CD    1 
ATOM   4178 N  NE    . ARG A 1 566  ? 103.611 104.513 180.116 1.00 104.77 ? 566  ARG A NE    1 
ATOM   4179 C  CZ    . ARG A 1 566  ? 103.713 105.595 179.352 1.00 104.77 ? 566  ARG A CZ    1 
ATOM   4180 N  NH1   . ARG A 1 566  ? 104.871 105.900 178.785 1.00 104.77 ? 566  ARG A NH1   1 
ATOM   4181 N  NH2   . ARG A 1 566  ? 102.656 106.370 179.153 1.00 104.77 ? 566  ARG A NH2   1 
ATOM   4182 N  N     . ASN A 1 567  ? 101.825 101.126 177.297 1.00 101.29 ? 567  ASN A N     1 
ATOM   4183 C  CA    . ASN A 1 567  ? 100.484 100.654 177.648 1.00 101.29 ? 567  ASN A CA    1 
ATOM   4184 C  C     . ASN A 1 567  ? 100.024 99.610  176.629 1.00 101.29 ? 567  ASN A C     1 
ATOM   4185 O  O     . ASN A 1 567  ? 99.109  99.819  175.831 1.00 101.29 ? 567  ASN A O     1 
ATOM   4186 C  CB    . ASN A 1 567  ? 99.513  101.825 177.730 1.00 101.29 ? 567  ASN A CB    1 
ATOM   4187 C  CG    . ASN A 1 567  ? 99.814  102.749 178.890 1.00 101.29 ? 567  ASN A CG    1 
ATOM   4188 O  OD1   . ASN A 1 567  ? 100.179 102.301 179.976 1.00 101.29 ? 567  ASN A OD1   1 
ATOM   4189 N  ND2   . ASN A 1 567  ? 99.662  104.049 178.666 1.00 101.29 ? 567  ASN A ND2   1 
ATOM   4190 N  N     . VAL A 1 568  ? 100.691 98.460  176.673 1.00 96.60  ? 568  VAL A N     1 
ATOM   4191 C  CA    . VAL A 1 568  ? 100.405 97.346  175.778 1.00 96.60  ? 568  VAL A CA    1 
ATOM   4192 C  C     . VAL A 1 568  ? 100.153 96.101  176.616 1.00 96.60  ? 568  VAL A C     1 
ATOM   4193 O  O     . VAL A 1 568  ? 100.940 95.781  177.514 1.00 96.60  ? 568  VAL A O     1 
ATOM   4194 C  CB    . VAL A 1 568  ? 101.550 97.110  174.775 1.00 96.60  ? 568  VAL A CB    1 
ATOM   4195 C  CG1   . VAL A 1 568  ? 101.396 95.762  174.099 1.00 96.60  ? 568  VAL A CG1   1 
ATOM   4196 C  CG2   . VAL A 1 568  ? 101.568 98.219  173.737 1.00 96.60  ? 568  VAL A CG2   1 
ATOM   4197 N  N     . ASP A 1 569  ? 99.052  95.406  176.322 1.00 88.47  ? 569  ASP A N     1 
ATOM   4198 C  CA    . ASP A 1 569  ? 98.673  94.232  177.102 1.00 88.47  ? 569  ASP A CA    1 
ATOM   4199 C  C     . ASP A 1 569  ? 99.681  93.098  176.949 1.00 88.47  ? 569  ASP A C     1 
ATOM   4200 O  O     . ASP A 1 569  ? 100.064 92.464  177.939 1.00 88.47  ? 569  ASP A O     1 
ATOM   4201 C  CB    . ASP A 1 569  ? 97.281  93.768  176.683 1.00 88.47  ? 569  ASP A CB    1 
ATOM   4202 C  CG    . ASP A 1 569  ? 97.150  93.617  175.182 1.00 88.47  ? 569  ASP A CG    1 
ATOM   4203 O  OD1   . ASP A 1 569  ? 98.123  93.931  174.465 1.00 88.47  ? 569  ASP A OD1   1 
ATOM   4204 O  OD2   . ASP A 1 569  ? 96.078  93.186  174.717 1.00 88.47  ? 569  ASP A OD2   1 
ATOM   4205 N  N     . SER A 1 570  ? 100.117 92.821  175.721 1.00 92.37  ? 570  SER A N     1 
ATOM   4206 C  CA    . SER A 1 570  ? 101.003 91.693  175.451 1.00 92.37  ? 570  SER A CA    1 
ATOM   4207 C  C     . SER A 1 570  ? 102.050 92.113  174.433 1.00 92.37  ? 570  SER A C     1 
ATOM   4208 O  O     . SER A 1 570  ? 101.709 92.510  173.315 1.00 92.37  ? 570  SER A O     1 
ATOM   4209 C  CB    . SER A 1 570  ? 100.215 90.478  174.949 1.00 92.37  ? 570  SER A CB    1 
ATOM   4210 O  OG    . SER A 1 570  ? 99.662  90.714  173.667 1.00 92.37  ? 570  SER A OG    1 
ATOM   4211 N  N     . ILE A 1 571  ? 103.316 92.017  174.823 1.00 96.33  ? 571  ILE A N     1 
ATOM   4212 C  CA    . ILE A 1 571  ? 104.443 92.437  173.999 1.00 96.33  ? 571  ILE A CA    1 
ATOM   4213 C  C     . ILE A 1 571  ? 105.164 91.168  173.556 1.00 96.33  ? 571  ILE A C     1 
ATOM   4214 O  O     . ILE A 1 571  ? 105.903 90.558  174.333 1.00 96.33  ? 571  ILE A O     1 
ATOM   4215 C  CB    . ILE A 1 571  ? 105.373 93.378  174.768 1.00 96.33  ? 571  ILE A CB    1 
ATOM   4216 C  CG1   . ILE A 1 571  ? 104.631 94.661  175.148 1.00 96.33  ? 571  ILE A CG1   1 
ATOM   4217 C  CG2   . ILE A 1 571  ? 106.596 93.704  173.935 1.00 96.33  ? 571  ILE A CG2   1 
ATOM   4218 C  CD1   . ILE A 1 571  ? 105.377 95.538  176.127 1.00 96.33  ? 571  ILE A CD1   1 
ATOM   4219 N  N     . ALA A 1 572  ? 104.949 90.759  172.307 1.00 87.62  ? 572  ALA A N     1 
ATOM   4220 C  CA    . ALA A 1 572  ? 105.569 89.548  171.767 1.00 87.62  ? 572  ALA A CA    1 
ATOM   4221 C  C     . ALA A 1 572  ? 106.858 89.938  171.056 1.00 87.62  ? 572  ALA A C     1 
ATOM   4222 O  O     . ALA A 1 572  ? 106.833 90.438  169.929 1.00 87.62  ? 572  ALA A O     1 
ATOM   4223 C  CB    . ALA A 1 572  ? 104.614 88.822  170.827 1.00 87.62  ? 572  ALA A CB    1 
ATOM   4224 N  N     . VAL A 1 573  ? 107.994 89.709  171.717 1.00 83.74  ? 573  VAL A N     1 
ATOM   4225 C  CA    . VAL A 1 573  ? 109.284 90.013  171.112 1.00 83.74  ? 573  VAL A CA    1 
ATOM   4226 C  C     . VAL A 1 573  ? 109.588 88.998  170.017 1.00 83.74  ? 573  VAL A C     1 
ATOM   4227 O  O     . VAL A 1 573  ? 109.278 87.805  170.141 1.00 83.74  ? 573  VAL A O     1 
ATOM   4228 C  CB    . VAL A 1 573  ? 110.389 90.038  172.184 1.00 83.74  ? 573  VAL A CB    1 
ATOM   4229 C  CG1   . VAL A 1 573  ? 110.567 88.665  172.811 1.00 83.74  ? 573  VAL A CG1   1 
ATOM   4230 C  CG2   . VAL A 1 573  ? 111.701 90.534  171.593 1.00 83.74  ? 573  VAL A CG2   1 
ATOM   4231 N  N     . ILE A 1 574  ? 110.179 89.474  168.923 1.00 74.54  ? 574  ILE A N     1 
ATOM   4232 C  CA    . ILE A 1 574  ? 110.541 88.636  167.786 1.00 74.54  ? 574  ILE A CA    1 
ATOM   4233 C  C     . ILE A 1 574  ? 112.055 88.640  167.647 1.00 74.54  ? 574  ILE A C     1 
ATOM   4234 O  O     . ILE A 1 574  ? 112.673 89.707  167.556 1.00 74.54  ? 574  ILE A O     1 
ATOM   4235 C  CB    . ILE A 1 574  ? 109.875 89.118  166.484 1.00 74.54  ? 574  ILE A CB    1 
ATOM   4236 C  CG1   . ILE A 1 574  ? 108.392 88.753  166.477 1.00 74.54  ? 574  ILE A CG1   1 
ATOM   4237 C  CG2   . ILE A 1 574  ? 110.574 88.518  165.274 1.00 74.54  ? 574  ILE A CG2   1 
ATOM   4238 C  CD1   . ILE A 1 574  ? 107.710 89.017  165.155 1.00 74.54  ? 574  ILE A CD1   1 
ATOM   4239 N  N     . GLN A 1 575  ? 112.646 87.448  167.628 1.00 77.19  ? 575  GLN A N     1 
ATOM   4240 C  CA    . GLN A 1 575  ? 114.079 87.302  167.410 1.00 77.19  ? 575  GLN A CA    1 
ATOM   4241 C  C     . GLN A 1 575  ? 114.322 86.350  166.249 1.00 77.19  ? 575  GLN A C     1 
ATOM   4242 O  O     . GLN A 1 575  ? 113.384 85.996  165.527 1.00 77.19  ? 575  GLN A O     1 
ATOM   4243 C  CB    . GLN A 1 575  ? 114.775 86.802  168.677 1.00 77.19  ? 575  GLN A CB    1 
ATOM   4244 C  CG    . GLN A 1 575  ? 114.962 87.870  169.738 1.00 77.19  ? 575  GLN A CG    1 
ATOM   4245 C  CD    . GLN A 1 575  ? 115.762 89.053  169.234 1.00 77.19  ? 575  GLN A CD    1 
ATOM   4246 O  OE1   . GLN A 1 575  ? 115.238 90.158  169.097 1.00 77.19  ? 575  GLN A OE1   1 
ATOM   4247 N  NE2   . GLN A 1 575  ? 117.039 88.827  168.953 1.00 77.19  ? 575  GLN A NE2   1 
ATOM   4248 N  N     . GLN A 1 576  ? 115.574 85.944  166.051 1.00 83.99  ? 576  GLN A N     1 
ATOM   4249 C  CA    . GLN A 1 576  ? 115.889 85.011  164.979 1.00 83.99  ? 576  GLN A CA    1 
ATOM   4250 C  C     . GLN A 1 576  ? 115.113 83.711  165.159 1.00 83.99  ? 576  GLN A C     1 
ATOM   4251 O  O     . GLN A 1 576  ? 115.023 83.167  166.263 1.00 83.99  ? 576  GLN A O     1 
ATOM   4252 C  CB    . GLN A 1 576  ? 117.393 84.733  164.944 1.00 83.99  ? 576  GLN A CB    1 
ATOM   4253 C  CG    . GLN A 1 576  ? 117.982 84.301  166.277 1.00 83.99  ? 576  GLN A CG    1 
ATOM   4254 C  CD    . GLN A 1 576  ? 118.042 82.794  166.427 1.00 83.99  ? 576  GLN A CD    1 
ATOM   4255 O  OE1   . GLN A 1 576  ? 118.263 82.071  165.456 1.00 83.99  ? 576  GLN A OE1   1 
ATOM   4256 N  NE2   . GLN A 1 576  ? 117.838 82.312  167.646 1.00 83.99  ? 576  GLN A NE2   1 
ATOM   4257 N  N     . GLY A 1 577  ? 114.536 83.224  164.064 1.00 71.92  ? 577  GLY A N     1 
ATOM   4258 C  CA    . GLY A 1 577  ? 113.777 81.991  164.102 1.00 71.92  ? 577  GLY A CA    1 
ATOM   4259 C  C     . GLY A 1 577  ? 112.336 82.166  164.534 1.00 71.92  ? 577  GLY A C     1 
ATOM   4260 O  O     . GLY A 1 577  ? 111.422 82.060  163.711 1.00 71.92  ? 577  GLY A O     1 
ATOM   4261 N  N     . GLN A 1 578  ? 112.115 82.434  165.819 1.00 77.13  ? 578  GLN A N     1 
ATOM   4262 C  CA    . GLN A 1 578  ? 110.768 82.513  166.364 1.00 77.13  ? 578  GLN A CA    1 
ATOM   4263 C  C     . GLN A 1 578  ? 110.751 83.515  167.513 1.00 77.13  ? 578  GLN A C     1 
ATOM   4264 O  O     . GLN A 1 578  ? 111.770 84.123  167.852 1.00 77.13  ? 578  GLN A O     1 
ATOM   4265 C  CB    . GLN A 1 578  ? 110.282 81.134  166.822 1.00 77.13  ? 578  GLN A CB    1 
ATOM   4266 C  CG    . GLN A 1 578  ? 110.935 80.621  168.104 1.00 77.13  ? 578  GLN A CG    1 
ATOM   4267 C  CD    . GLN A 1 578  ? 112.351 80.106  167.897 1.00 77.13  ? 578  GLN A CD    1 
ATOM   4268 O  OE1   . GLN A 1 578  ? 113.192 80.775  167.295 1.00 77.13  ? 578  GLN A OE1   1 
ATOM   4269 N  NE2   . GLN A 1 578  ? 112.621 78.907  168.401 1.00 77.13  ? 578  GLN A NE2   1 
ATOM   4270 N  N     . VAL A 1 579  ? 109.572 83.679  168.114 1.00 84.55  ? 579  VAL A N     1 
ATOM   4271 C  CA    . VAL A 1 579  ? 109.383 84.591  169.236 1.00 84.55  ? 579  VAL A CA    1 
ATOM   4272 C  C     . VAL A 1 579  ? 109.991 83.982  170.492 1.00 84.55  ? 579  VAL A C     1 
ATOM   4273 O  O     . VAL A 1 579  ? 110.339 82.797  170.516 1.00 84.55  ? 579  VAL A O     1 
ATOM   4274 C  CB    . VAL A 1 579  ? 107.894 84.913  169.454 1.00 84.55  ? 579  VAL A CB    1 
ATOM   4275 C  CG1   . VAL A 1 579  ? 107.315 85.607  168.236 1.00 84.55  ? 579  VAL A CG1   1 
ATOM   4276 C  CG2   . VAL A 1 579  ? 107.121 83.645  169.771 1.00 84.55  ? 579  VAL A CG2   1 
ATOM   4277 N  N     . VAL A 1 580  ? 110.122 84.789  171.541 1.00 96.48  ? 580  VAL A N     1 
ATOM   4278 C  CA    . VAL A 1 580  ? 110.678 84.347  172.818 1.00 96.48  ? 580  VAL A CA    1 
ATOM   4279 C  C     . VAL A 1 580  ? 109.619 84.367  173.918 1.00 96.48  ? 580  VAL A C     1 
ATOM   4280 O  O     . VAL A 1 580  ? 109.348 83.343  174.548 1.00 96.48  ? 580  VAL A O     1 
ATOM   4281 C  CB    . VAL A 1 580  ? 111.909 85.193  173.211 1.00 96.48  ? 580  VAL A CB    1 
ATOM   4282 C  CG1   . VAL A 1 580  ? 112.411 84.791  174.588 1.00 96.48  ? 580  VAL A CG1   1 
ATOM   4283 C  CG2   . VAL A 1 580  ? 113.009 85.046  172.172 1.00 96.48  ? 580  VAL A CG2   1 
ATOM   4284 N  N     . GLU A 1 581  ? 109.006 85.524  174.158 1.00 110.01 ? 581  GLU A N     1 
ATOM   4285 C  CA    . GLU A 1 581  ? 108.069 85.694  175.259 1.00 110.01 ? 581  GLU A CA    1 
ATOM   4286 C  C     . GLU A 1 581  ? 106.895 86.549  174.806 1.00 110.01 ? 581  GLU A C     1 
ATOM   4287 O  O     . GLU A 1 581  ? 107.024 87.377  173.902 1.00 110.01 ? 581  GLU A O     1 
ATOM   4288 C  CB    . GLU A 1 581  ? 108.756 86.334  176.470 1.00 110.01 ? 581  GLU A CB    1 
ATOM   4289 C  CG    . GLU A 1 581  ? 109.616 87.534  176.114 1.00 110.01 ? 581  GLU A CG    1 
ATOM   4290 C  CD    . GLU A 1 581  ? 110.595 87.897  177.210 1.00 110.01 ? 581  GLU A CD    1 
ATOM   4291 O  OE1   . GLU A 1 581  ? 110.620 87.195  178.241 1.00 110.01 ? 581  GLU A OE1   1 
ATOM   4292 O  OE2   . GLU A 1 581  ? 111.341 88.884  177.039 1.00 110.01 ? 581  GLU A OE2   1 
ATOM   4293 N  N     . THR A 1 582  ? 105.746 86.340  175.446 1.00 110.17 ? 582  THR A N     1 
ATOM   4294 C  CA    . THR A 1 582  ? 104.504 87.037  175.118 1.00 110.17 ? 582  THR A CA    1 
ATOM   4295 C  C     . THR A 1 582  ? 103.818 87.536  176.385 1.00 110.17 ? 582  THR A C     1 
ATOM   4296 O  O     . THR A 1 582  ? 102.612 87.369  176.577 1.00 110.17 ? 582  THR A O     1 
ATOM   4297 C  CB    . THR A 1 582  ? 103.553 86.140  174.326 1.00 110.17 ? 582  THR A CB    1 
ATOM   4298 O  OG1   . THR A 1 582  ? 103.268 84.955  175.081 1.00 110.17 ? 582  THR A OG1   1 
ATOM   4299 C  CG2   . THR A 1 582  ? 104.161 85.751  172.984 1.00 110.17 ? 582  THR A CG2   1 
ATOM   4300 N  N     . GLY A 1 583  ? 104.588 88.164  177.275 1.00 116.81 ? 583  GLY A N     1 
ATOM   4301 C  CA    . GLY A 1 583  ? 104.061 88.696  178.511 1.00 116.81 ? 583  GLY A CA    1 
ATOM   4302 C  C     . GLY A 1 583  ? 103.729 90.180  178.420 1.00 116.81 ? 583  GLY A C     1 
ATOM   4303 O  O     . GLY A 1 583  ? 103.847 90.819  177.378 1.00 116.81 ? 583  GLY A O     1 
ATOM   4304 N  N     . THR A 1 584  ? 103.302 90.724  179.557 1.00 121.87 ? 584  THR A N     1 
ATOM   4305 C  CA    . THR A 1 584  ? 102.972 92.137  179.660 1.00 121.87 ? 584  THR A CA    1 
ATOM   4306 C  C     . THR A 1 584  ? 104.226 92.929  180.029 1.00 121.87 ? 584  THR A C     1 
ATOM   4307 O  O     . THR A 1 584  ? 105.344 92.410  180.005 1.00 121.87 ? 584  THR A O     1 
ATOM   4308 C  CB    . THR A 1 584  ? 101.841 92.351  180.666 1.00 121.87 ? 584  THR A CB    1 
ATOM   4309 O  OG1   . THR A 1 584  ? 101.389 93.710  180.597 1.00 121.87 ? 584  THR A OG1   1 
ATOM   4310 C  CG2   . THR A 1 584  ? 102.311 92.054  182.081 1.00 121.87 ? 584  THR A CG2   1 
ATOM   4311 N  N     . HIS A 1 585  ? 104.051 94.207  180.371 1.00 131.32 ? 585  HIS A N     1 
ATOM   4312 C  CA    . HIS A 1 585  ? 105.193 95.060  180.683 1.00 131.32 ? 585  HIS A CA    1 
ATOM   4313 C  C     . HIS A 1 585  ? 105.913 94.583  181.940 1.00 131.32 ? 585  HIS A C     1 
ATOM   4314 O  O     . HIS A 1 585  ? 107.114 94.293  181.912 1.00 131.32 ? 585  HIS A O     1 
ATOM   4315 C  CB    . HIS A 1 585  ? 104.733 96.510  180.840 1.00 131.32 ? 585  HIS A CB    1 
ATOM   4316 C  CG    . HIS A 1 585  ? 105.782 97.419  181.400 1.00 131.32 ? 585  HIS A CG    1 
ATOM   4317 N  ND1   . HIS A 1 585  ? 106.758 98.000  180.620 1.00 131.32 ? 585  HIS A ND1   1 
ATOM   4318 C  CD2   . HIS A 1 585  ? 106.007 97.849  182.665 1.00 131.32 ? 585  HIS A CD2   1 
ATOM   4319 C  CE1   . HIS A 1 585  ? 107.540 98.748  181.379 1.00 131.32 ? 585  HIS A CE1   1 
ATOM   4320 N  NE2   . HIS A 1 585  ? 107.105 98.673  182.624 1.00 131.32 ? 585  HIS A NE2   1 
ATOM   4321 N  N     . GLU A 1 586  ? 105.189 94.495  183.057 1.00 135.21 ? 586  GLU A N     1 
ATOM   4322 C  CA    . GLU A 1 586  ? 105.826 94.143  184.323 1.00 135.21 ? 586  GLU A CA    1 
ATOM   4323 C  C     . GLU A 1 586  ? 106.243 92.678  184.354 1.00 135.21 ? 586  GLU A C     1 
ATOM   4324 O  O     . GLU A 1 586  ? 107.278 92.333  184.938 1.00 135.21 ? 586  GLU A O     1 
ATOM   4325 C  CB    . GLU A 1 586  ? 104.889 94.459  185.489 1.00 135.21 ? 586  GLU A CB    1 
ATOM   4326 C  CG    . GLU A 1 586  ? 105.596 94.637  186.824 1.00 135.21 ? 586  GLU A CG    1 
ATOM   4327 C  CD    . GLU A 1 586  ? 106.786 95.575  186.736 1.00 135.21 ? 586  GLU A CD    1 
ATOM   4328 O  OE1   . GLU A 1 586  ? 106.579 96.805  186.791 1.00 135.21 ? 586  GLU A OE1   1 
ATOM   4329 O  OE2   . GLU A 1 586  ? 107.927 95.082  186.617 1.00 135.21 ? 586  GLU A OE2   1 
ATOM   4330 N  N     . GLU A 1 587  ? 105.447 91.799  183.740 1.00 133.45 ? 587  GLU A N     1 
ATOM   4331 C  CA    . GLU A 1 587  ? 105.742 90.369  183.795 1.00 133.45 ? 587  GLU A CA    1 
ATOM   4332 C  C     . GLU A 1 587  ? 107.067 90.047  183.113 1.00 133.45 ? 587  GLU A C     1 
ATOM   4333 O  O     . GLU A 1 587  ? 107.852 89.236  183.619 1.00 133.45 ? 587  GLU A O     1 
ATOM   4334 C  CB    . GLU A 1 587  ? 104.600 89.574  183.162 1.00 133.45 ? 587  GLU A CB    1 
ATOM   4335 C  CG    . GLU A 1 587  ? 104.959 88.149  182.777 1.00 133.45 ? 587  GLU A CG    1 
ATOM   4336 C  CD    . GLU A 1 587  ? 103.795 87.405  182.152 1.00 133.45 ? 587  GLU A CD    1 
ATOM   4337 O  OE1   . GLU A 1 587  ? 102.670 87.949  182.153 1.00 133.45 ? 587  GLU A OE1   1 
ATOM   4338 O  OE2   . GLU A 1 587  ? 104.003 86.276  181.661 1.00 133.45 ? 587  GLU A OE2   1 
ATOM   4339 N  N     . LEU A 1 588  ? 107.337 90.673  181.966 1.00 129.80 ? 588  LEU A N     1 
ATOM   4340 C  CA    . LEU A 1 588  ? 108.586 90.405  181.261 1.00 129.80 ? 588  LEU A CA    1 
ATOM   4341 C  C     . LEU A 1 588  ? 109.786 90.986  181.997 1.00 129.80 ? 588  LEU A C     1 
ATOM   4342 O  O     . LEU A 1 588  ? 110.904 90.477  181.856 1.00 129.80 ? 588  LEU A O     1 
ATOM   4343 C  CB    . LEU A 1 588  ? 108.517 90.954  179.837 1.00 129.80 ? 588  LEU A CB    1 
ATOM   4344 C  CG    . LEU A 1 588  ? 107.474 90.294  178.934 1.00 129.80 ? 588  LEU A CG    1 
ATOM   4345 C  CD1   . LEU A 1 588  ? 107.522 90.876  177.530 1.00 129.80 ? 588  LEU A CD1   1 
ATOM   4346 C  CD2   . LEU A 1 588  ? 107.662 88.788  178.911 1.00 129.80 ? 588  LEU A CD2   1 
ATOM   4347 N  N     . ILE A 1 589  ? 109.581 92.050  182.776 1.00 135.83 ? 589  ILE A N     1 
ATOM   4348 C  CA    . ILE A 1 589  ? 110.675 92.626  183.552 1.00 135.83 ? 589  ILE A CA    1 
ATOM   4349 C  C     . ILE A 1 589  ? 111.118 91.665  184.649 1.00 135.83 ? 589  ILE A C     1 
ATOM   4350 O  O     . ILE A 1 589  ? 112.311 91.574  184.968 1.00 135.83 ? 589  ILE A O     1 
ATOM   4351 C  CB    . ILE A 1 589  ? 110.257 93.994  184.125 1.00 135.83 ? 589  ILE A CB    1 
ATOM   4352 C  CG1   . ILE A 1 589  ? 110.033 94.997  182.993 1.00 135.83 ? 589  ILE A CG1   1 
ATOM   4353 C  CG2   . ILE A 1 589  ? 111.305 94.524  185.090 1.00 135.83 ? 589  ILE A CG2   1 
ATOM   4354 C  CD1   . ILE A 1 589  ? 109.410 96.297  183.447 1.00 135.83 ? 589  ILE A CD1   1 
ATOM   4355 N  N     . ALA A 1 590  ? 110.171 90.928  185.237 1.00 141.09 ? 590  ALA A N     1 
ATOM   4356 C  CA    . ALA A 1 590  ? 110.494 90.037  186.349 1.00 141.09 ? 590  ALA A CA    1 
ATOM   4357 C  C     . ALA A 1 590  ? 111.528 88.993  185.943 1.00 141.09 ? 590  ALA A C     1 
ATOM   4358 O  O     . ALA A 1 590  ? 112.555 88.827  186.612 1.00 141.09 ? 590  ALA A O     1 
ATOM   4359 C  CB    . ALA A 1 590  ? 109.221 89.365  186.865 1.00 141.09 ? 590  ALA A CB    1 
ATOM   4360 N  N     . LYS A 1 591  ? 111.277 88.280  184.845 1.00 137.83 ? 591  LYS A N     1 
ATOM   4361 C  CA    . LYS A 1 591  ? 112.248 87.325  184.326 1.00 137.83 ? 591  LYS A CA    1 
ATOM   4362 C  C     . LYS A 1 591  ? 113.377 87.998  183.561 1.00 137.83 ? 591  LYS A C     1 
ATOM   4363 O  O     . LYS A 1 591  ? 114.391 87.347  183.283 1.00 137.83 ? 591  LYS A O     1 
ATOM   4364 C  CB    . LYS A 1 591  ? 111.551 86.308  183.419 1.00 137.83 ? 591  LYS A CB    1 
ATOM   4365 C  CG    . LYS A 1 591  ? 111.042 86.895  182.110 1.00 137.83 ? 591  LYS A CG    1 
ATOM   4366 C  CD    . LYS A 1 591  ? 110.195 85.892  181.345 1.00 137.83 ? 591  LYS A CD    1 
ATOM   4367 C  CE    . LYS A 1 591  ? 108.803 85.775  181.943 1.00 137.83 ? 591  LYS A CE    1 
ATOM   4368 N  NZ    . LYS A 1 591  ? 108.049 87.056  181.852 1.00 137.83 ? 591  LYS A NZ    1 
ATOM   4369 N  N     . SER A 1 592  ? 113.193 89.266  183.187 1.00 136.19 ? 592  SER A N     1 
ATOM   4370 C  CA    . SER A 1 592  ? 114.150 90.105  182.471 1.00 136.19 ? 592  SER A CA    1 
ATOM   4371 C  C     . SER A 1 592  ? 114.298 89.672  181.018 1.00 136.19 ? 592  SER A C     1 
ATOM   4372 O  O     . SER A 1 592  ? 114.862 90.415  180.208 1.00 136.19 ? 592  SER A O     1 
ATOM   4373 C  CB    . SER A 1 592  ? 115.515 90.101  183.168 1.00 136.19 ? 592  SER A CB    1 
ATOM   4374 O  OG    . SER A 1 592  ? 115.409 90.579  184.497 1.00 136.19 ? 592  SER A OG    1 
ATOM   4375 N  N     . GLY A 1 593  ? 113.782 88.484  180.686 1.00 132.95 ? 593  GLY A N     1 
ATOM   4376 C  CA    . GLY A 1 593  ? 113.548 88.035  179.324 1.00 132.95 ? 593  GLY A CA    1 
ATOM   4377 C  C     . GLY A 1 593  ? 114.530 88.516  178.278 1.00 132.95 ? 593  GLY A C     1 
ATOM   4378 O  O     . GLY A 1 593  ? 115.748 88.371  178.415 1.00 132.95 ? 593  GLY A O     1 
ATOM   4379 N  N     . ALA A 1 594  ? 113.978 89.101  177.218 1.00 126.36 ? 594  ALA A N     1 
ATOM   4380 C  CA    . ALA A 1 594  ? 114.726 89.913  176.271 1.00 126.36 ? 594  ALA A CA    1 
ATOM   4381 C  C     . ALA A 1 594  ? 114.109 91.285  176.053 1.00 126.36 ? 594  ALA A C     1 
ATOM   4382 O  O     . ALA A 1 594  ? 114.810 92.188  175.579 1.00 126.36 ? 594  ALA A O     1 
ATOM   4383 C  CB    . ALA A 1 594  ? 114.849 89.197  174.918 1.00 126.36 ? 594  ALA A CB    1 
ATOM   4384 N  N     . TYR A 1 595  ? 112.824 91.468  176.372 1.00 121.54 ? 595  TYR A N     1 
ATOM   4385 C  CA    . TYR A 1 595  ? 112.210 92.791  176.337 1.00 121.54 ? 595  TYR A CA    1 
ATOM   4386 C  C     . TYR A 1 595  ? 112.838 93.725  177.362 1.00 121.54 ? 595  TYR A C     1 
ATOM   4387 O  O     . TYR A 1 595  ? 113.106 94.895  177.064 1.00 121.54 ? 595  TYR A O     1 
ATOM   4388 C  CB    . TYR A 1 595  ? 110.709 92.669  176.596 1.00 121.54 ? 595  TYR A CB    1 
ATOM   4389 C  CG    . TYR A 1 595  ? 109.971 93.985  176.546 1.00 121.54 ? 595  TYR A CG    1 
ATOM   4390 C  CD1   . TYR A 1 595  ? 109.685 94.596  175.336 1.00 121.54 ? 595  TYR A CD1   1 
ATOM   4391 C  CD2   . TYR A 1 595  ? 109.588 94.631  177.715 1.00 121.54 ? 595  TYR A CD2   1 
ATOM   4392 C  CE1   . TYR A 1 595  ? 109.012 95.800  175.290 1.00 121.54 ? 595  TYR A CE1   1 
ATOM   4393 C  CE2   . TYR A 1 595  ? 108.922 95.839  177.678 1.00 121.54 ? 595  TYR A CE2   1 
ATOM   4394 C  CZ    . TYR A 1 595  ? 108.640 96.421  176.462 1.00 121.54 ? 595  TYR A CZ    1 
ATOM   4395 O  OH    . TYR A 1 595  ? 107.974 97.623  176.417 1.00 121.54 ? 595  TYR A OH    1 
ATOM   4396 N  N     . ALA A 1 596  ? 113.066 93.231  178.581 1.00 124.37 ? 596  ALA A N     1 
ATOM   4397 C  CA    . ALA A 1 596  ? 113.674 94.062  179.614 1.00 124.37 ? 596  ALA A CA    1 
ATOM   4398 C  C     . ALA A 1 596  ? 115.120 94.396  179.282 1.00 124.37 ? 596  ALA A C     1 
ATOM   4399 O  O     . ALA A 1 596  ? 115.655 95.395  179.779 1.00 124.37 ? 596  ALA A O     1 
ATOM   4400 C  CB    . ALA A 1 596  ? 113.586 93.366  180.971 1.00 124.37 ? 596  ALA A CB    1 
ATOM   4401 N  N     . SER A 1 597  ? 115.769 93.567  178.462 1.00 125.44 ? 597  SER A N     1 
ATOM   4402 C  CA    . SER A 1 597  ? 117.116 93.889  178.004 1.00 125.44 ? 597  SER A CA    1 
ATOM   4403 C  C     . SER A 1 597  ? 117.124 95.191  177.216 1.00 125.44 ? 597  SER A C     1 
ATOM   4404 O  O     . SER A 1 597  ? 117.998 96.043  177.416 1.00 125.44 ? 597  SER A O     1 
ATOM   4405 C  CB    . SER A 1 597  ? 117.671 92.741  177.161 1.00 125.44 ? 597  SER A CB    1 
ATOM   4406 O  OG    . SER A 1 597  ? 117.129 92.763  175.852 1.00 125.44 ? 597  SER A OG    1 
ATOM   4407 N  N     . LEU A 1 598  ? 116.141 95.371  176.331 1.00 120.21 ? 598  LEU A N     1 
ATOM   4408 C  CA    . LEU A 1 598  ? 116.021 96.627  175.601 1.00 120.21 ? 598  LEU A CA    1 
ATOM   4409 C  C     . LEU A 1 598  ? 115.757 97.789  176.549 1.00 120.21 ? 598  LEU A C     1 
ATOM   4410 O  O     . LEU A 1 598  ? 116.263 98.897  176.339 1.00 120.21 ? 598  LEU A O     1 
ATOM   4411 C  CB    . LEU A 1 598  ? 114.909 96.522  174.558 1.00 120.21 ? 598  LEU A CB    1 
ATOM   4412 C  CG    . LEU A 1 598  ? 115.148 95.514  173.434 1.00 120.21 ? 598  LEU A CG    1 
ATOM   4413 C  CD1   . LEU A 1 598  ? 113.877 95.295  172.631 1.00 120.21 ? 598  LEU A CD1   1 
ATOM   4414 C  CD2   . LEU A 1 598  ? 116.277 95.985  172.534 1.00 120.21 ? 598  LEU A CD2   1 
ATOM   4415 N  N     . ILE A 1 599  ? 114.968 97.556  177.599 1.00 124.59 ? 599  ILE A N     1 
ATOM   4416 C  CA    . ILE A 1 599  ? 114.665 98.618  178.556 1.00 124.59 ? 599  ILE A CA    1 
ATOM   4417 C  C     . ILE A 1 599  ? 115.932 99.069  179.273 1.00 124.59 ? 599  ILE A C     1 
ATOM   4418 O  O     . ILE A 1 599  ? 116.220 100.269 179.369 1.00 124.59 ? 599  ILE A O     1 
ATOM   4419 C  CB    . ILE A 1 599  ? 113.588 98.149  179.551 1.00 124.59 ? 599  ILE A CB    1 
ATOM   4420 C  CG1   . ILE A 1 599  ? 112.207 98.181  178.894 1.00 124.59 ? 599  ILE A CG1   1 
ATOM   4421 C  CG2   . ILE A 1 599  ? 113.602 99.012  180.803 1.00 124.59 ? 599  ILE A CG2   1 
ATOM   4422 C  CD1   . ILE A 1 599  ? 111.077 97.815  179.828 1.00 124.59 ? 599  ILE A CD1   1 
ATOM   4423 N  N     . ARG A 1 600  ? 116.717 98.112  179.779 1.00 122.81 ? 600  ARG A N     1 
ATOM   4424 C  CA    . ARG A 1 600  ? 117.934 98.490  180.490 1.00 122.81 ? 600  ARG A CA    1 
ATOM   4425 C  C     . ARG A 1 600  ? 118.979 99.065  179.543 1.00 122.81 ? 600  ARG A C     1 
ATOM   4426 O  O     . ARG A 1 600  ? 119.801 99.889  179.960 1.00 122.81 ? 600  ARG A O     1 
ATOM   4427 C  CB    . ARG A 1 600  ? 118.511 97.302  181.264 1.00 122.81 ? 600  ARG A CB    1 
ATOM   4428 C  CG    . ARG A 1 600  ? 119.208 96.246  180.424 1.00 122.81 ? 600  ARG A CG    1 
ATOM   4429 C  CD    . ARG A 1 600  ? 118.884 94.846  180.925 1.00 122.81 ? 600  ARG A CD    1 
ATOM   4430 N  NE    . ARG A 1 600  ? 119.558 93.806  180.151 1.00 122.81 ? 600  ARG A NE    1 
ATOM   4431 C  CZ    . ARG A 1 600  ? 120.865 93.559  180.192 1.00 122.81 ? 600  ARG A CZ    1 
ATOM   4432 N  NH1   . ARG A 1 600  ? 121.658 94.272  180.980 1.00 122.81 ? 600  ARG A NH1   1 
ATOM   4433 N  NH2   . ARG A 1 600  ? 121.378 92.589  179.448 1.00 122.81 ? 600  ARG A NH2   1 
ATOM   4434 N  N     . PHE A 1 601  ? 118.970 98.650  178.273 1.00 117.23 ? 601  PHE A N     1 
ATOM   4435 C  CA    . PHE A 1 601  ? 119.856 99.274  177.298 1.00 117.23 ? 601  PHE A CA    1 
ATOM   4436 C  C     . PHE A 1 601  ? 119.459 100.722 177.046 1.00 117.23 ? 601  PHE A C     1 
ATOM   4437 O  O     . PHE A 1 601  ? 120.319 101.606 176.968 1.00 117.23 ? 601  PHE A O     1 
ATOM   4438 C  CB    . PHE A 1 601  ? 119.848 98.479  175.993 1.00 117.23 ? 601  PHE A CB    1 
ATOM   4439 C  CG    . PHE A 1 601  ? 120.849 98.963  174.987 1.00 117.23 ? 601  PHE A CG    1 
ATOM   4440 C  CD1   . PHE A 1 601  ? 122.152 98.495  175.006 1.00 117.23 ? 601  PHE A CD1   1 
ATOM   4441 C  CD2   . PHE A 1 601  ? 120.489 99.892  174.025 1.00 117.23 ? 601  PHE A CD2   1 
ATOM   4442 C  CE1   . PHE A 1 601  ? 123.075 98.943  174.083 1.00 117.23 ? 601  PHE A CE1   1 
ATOM   4443 C  CE2   . PHE A 1 601  ? 121.409 100.345 173.101 1.00 117.23 ? 601  PHE A CE2   1 
ATOM   4444 C  CZ    . PHE A 1 601  ? 122.702 99.870  173.130 1.00 117.23 ? 601  PHE A CZ    1 
ATOM   4445 N  N     . GLN A 1 602  ? 118.157 100.984 176.916 1.00 125.02 ? 602  GLN A N     1 
ATOM   4446 C  CA    . GLN A 1 602  ? 117.691 102.348 176.697 1.00 125.02 ? 602  GLN A CA    1 
ATOM   4447 C  C     . GLN A 1 602  ? 117.994 103.230 177.899 1.00 125.02 ? 602  GLN A C     1 
ATOM   4448 O  O     . GLN A 1 602  ? 118.324 104.412 177.744 1.00 125.02 ? 602  GLN A O     1 
ATOM   4449 C  CB    . GLN A 1 602  ? 116.192 102.350 176.395 1.00 125.02 ? 602  GLN A CB    1 
ATOM   4450 C  CG    . GLN A 1 602  ? 115.645 103.703 175.972 1.00 125.02 ? 602  GLN A CG    1 
ATOM   4451 C  CD    . GLN A 1 602  ? 115.086 104.496 177.137 1.00 125.02 ? 602  GLN A CD    1 
ATOM   4452 O  OE1   . GLN A 1 602  ? 114.098 104.101 177.755 1.00 125.02 ? 602  GLN A OE1   1 
ATOM   4453 N  NE2   . GLN A 1 602  ? 115.720 105.622 177.444 1.00 125.02 ? 602  GLN A NE2   1 
ATOM   4454 N  N     . GLU A 1 603  ? 117.876 102.676 179.108 1.00 126.74 ? 603  GLU A N     1 
ATOM   4455 C  CA    . GLU A 1 603  ? 118.155 103.462 180.304 1.00 126.74 ? 603  GLU A CA    1 
ATOM   4456 C  C     . GLU A 1 603  ? 119.612 103.909 180.352 1.00 126.74 ? 603  GLU A C     1 
ATOM   4457 O  O     . GLU A 1 603  ? 119.902 105.063 180.689 1.00 126.74 ? 603  GLU A O     1 
ATOM   4458 C  CB    . GLU A 1 603  ? 117.799 102.661 181.556 1.00 126.74 ? 603  GLU A CB    1 
ATOM   4459 C  CG    . GLU A 1 603  ? 117.881 103.466 182.842 1.00 126.74 ? 603  GLU A CG    1 
ATOM   4460 C  CD    . GLU A 1 603  ? 117.133 104.783 182.754 1.00 126.74 ? 603  GLU A CD    1 
ATOM   4461 O  OE1   . GLU A 1 603  ? 117.788 105.830 182.567 1.00 126.74 ? 603  GLU A OE1   1 
ATOM   4462 O  OE2   . GLU A 1 603  ? 115.890 104.771 182.871 1.00 126.74 ? 603  GLU A OE2   1 
ATOM   4463 N  N     . MET A 1 604  ? 120.544 103.014 180.013 1.00 125.01 ? 604  MET A N     1 
ATOM   4464 C  CA    . MET A 1 604  ? 121.958 103.360 180.116 1.00 125.01 ? 604  MET A CA    1 
ATOM   4465 C  C     . MET A 1 604  ? 122.403 104.285 178.987 1.00 125.01 ? 604  MET A C     1 
ATOM   4466 O  O     . MET A 1 604  ? 123.321 105.090 179.178 1.00 125.01 ? 604  MET A O     1 
ATOM   4467 C  CB    . MET A 1 604  ? 122.812 102.088 180.166 1.00 125.01 ? 604  MET A CB    1 
ATOM   4468 C  CG    . MET A 1 604  ? 122.727 101.169 178.952 1.00 125.01 ? 604  MET A CG    1 
ATOM   4469 S  SD    . MET A 1 604  ? 123.708 101.697 177.533 1.00 125.01 ? 604  MET A SD    1 
ATOM   4470 C  CE    . MET A 1 604  ? 125.366 101.389 178.134 1.00 125.01 ? 604  MET A CE    1 
ATOM   4471 N  N     . VAL A 1 605  ? 121.780 104.183 177.810 1.00 126.62 ? 605  VAL A N     1 
ATOM   4472 C  CA    . VAL A 1 605  ? 122.077 105.130 176.738 1.00 126.62 ? 605  VAL A CA    1 
ATOM   4473 C  C     . VAL A 1 605  ? 121.649 106.537 177.136 1.00 126.62 ? 605  VAL A C     1 
ATOM   4474 O  O     . VAL A 1 605  ? 122.373 107.512 176.899 1.00 126.62 ? 605  VAL A O     1 
ATOM   4475 C  CB    . VAL A 1 605  ? 121.412 104.688 175.421 1.00 126.62 ? 605  VAL A CB    1 
ATOM   4476 C  CG1   . VAL A 1 605  ? 121.617 105.740 174.344 1.00 126.62 ? 605  VAL A CG1   1 
ATOM   4477 C  CG2   . VAL A 1 605  ? 121.984 103.363 174.957 1.00 126.62 ? 605  VAL A CG2   1 
ATOM   4478 N  N     . GLY A 1 606  ? 120.468 106.667 177.744 1.00 132.24 ? 606  GLY A N     1 
ATOM   4479 C  CA    . GLY A 1 606  ? 120.003 107.978 178.167 1.00 132.24 ? 606  GLY A CA    1 
ATOM   4480 C  C     . GLY A 1 606  ? 120.916 108.621 179.193 1.00 132.24 ? 606  GLY A C     1 
ATOM   4481 O  O     . GLY A 1 606  ? 121.143 109.833 179.163 1.00 132.24 ? 606  GLY A O     1 
ATOM   4482 N  N     . THR A 1 607  ? 121.447 107.823 180.114 1.00 133.98 ? 607  THR A N     1 
ATOM   4483 C  CA    . THR A 1 607  ? 122.371 108.327 181.123 1.00 133.98 ? 607  THR A CA    1 
ATOM   4484 C  C     . THR A 1 607  ? 123.722 108.670 180.504 1.00 133.98 ? 607  THR A C     1 
ATOM   4485 O  O     . THR A 1 607  ? 124.019 109.837 180.247 1.00 133.98 ? 607  THR A O     1 
ATOM   4486 C  CB    . THR A 1 607  ? 122.582 107.308 182.258 1.00 133.98 ? 607  THR A CB    1 
ATOM   4487 O  OG1   . THR A 1 607  ? 123.121 106.094 181.719 1.00 133.98 ? 607  THR A OG1   1 
ATOM   4488 C  CG2   . THR A 1 607  ? 121.267 107.010 182.960 1.00 133.98 ? 607  THR A CG2   1 
ATOM   4489 N  N     . GLU A 1 670  ? 114.290 130.487 116.918 1.00 79.54  ? 670  GLU A N     1 
ATOM   4490 C  CA    . GLU A 1 670  ? 114.417 130.637 115.473 1.00 79.54  ? 670  GLU A CA    1 
ATOM   4491 C  C     . GLU A 1 670  ? 115.870 130.502 115.032 1.00 79.54  ? 670  GLU A C     1 
ATOM   4492 O  O     . GLU A 1 670  ? 116.789 130.825 115.787 1.00 79.54  ? 670  GLU A O     1 
ATOM   4493 C  CB    . GLU A 1 670  ? 113.849 131.985 115.024 1.00 79.54  ? 670  GLU A CB    1 
ATOM   4494 C  CG    . GLU A 1 670  ? 114.532 133.194 115.647 1.00 79.54  ? 670  GLU A CG    1 
ATOM   4495 C  CD    . GLU A 1 670  ? 115.645 133.751 114.780 1.00 79.54  ? 670  GLU A CD    1 
ATOM   4496 O  OE1   . GLU A 1 670  ? 115.636 133.492 113.558 1.00 79.54  ? 670  GLU A OE1   1 
ATOM   4497 O  OE2   . GLU A 1 670  ? 116.529 134.448 115.321 1.00 79.54  ? 670  GLU A OE2   1 
ATOM   4498 N  N     . ASN A 1 671  ? 116.063 130.024 113.802 1.00 73.96  ? 671  ASN A N     1 
ATOM   4499 C  CA    . ASN A 1 671  ? 117.389 129.827 113.218 1.00 73.96  ? 671  ASN A CA    1 
ATOM   4500 C  C     . ASN A 1 671  ? 118.257 128.940 114.109 1.00 73.96  ? 671  ASN A C     1 
ATOM   4501 O  O     . ASN A 1 671  ? 119.441 129.202 114.333 1.00 73.96  ? 671  ASN A O     1 
ATOM   4502 C  CB    . ASN A 1 671  ? 118.072 131.169 112.945 1.00 73.96  ? 671  ASN A CB    1 
ATOM   4503 C  CG    . ASN A 1 671  ? 119.230 131.047 111.972 1.00 73.96  ? 671  ASN A CG    1 
ATOM   4504 O  OD1   . ASN A 1 671  ? 119.521 129.962 111.469 1.00 73.96  ? 671  ASN A OD1   1 
ATOM   4505 N  ND2   . ASN A 1 671  ? 119.897 132.164 111.702 1.00 73.96  ? 671  ASN A ND2   1 
ATOM   4506 N  N     . TYR A 1 672  ? 117.649 127.874 114.629 1.00 69.93  ? 672  TYR A N     1 
ATOM   4507 C  CA    . TYR A 1 672  ? 118.371 126.912 115.449 1.00 69.93  ? 672  TYR A CA    1 
ATOM   4508 C  C     . TYR A 1 672  ? 118.808 125.672 114.681 1.00 69.93  ? 672  TYR A C     1 
ATOM   4509 O  O     . TYR A 1 672  ? 119.727 124.982 115.130 1.00 69.93  ? 672  TYR A O     1 
ATOM   4510 C  CB    . TYR A 1 672  ? 117.521 126.492 116.656 1.00 69.93  ? 672  TYR A CB    1 
ATOM   4511 C  CG    . TYR A 1 672  ? 116.062 126.249 116.344 1.00 69.93  ? 672  TYR A CG    1 
ATOM   4512 C  CD1   . TYR A 1 672  ? 115.659 125.133 115.622 1.00 69.93  ? 672  TYR A CD1   1 
ATOM   4513 C  CD2   . TYR A 1 672  ? 115.084 127.132 116.781 1.00 69.93  ? 672  TYR A CD2   1 
ATOM   4514 C  CE1   . TYR A 1 672  ? 114.325 124.908 115.339 1.00 69.93  ? 672  TYR A CE1   1 
ATOM   4515 C  CE2   . TYR A 1 672  ? 113.748 126.916 116.503 1.00 69.93  ? 672  TYR A CE2   1 
ATOM   4516 C  CZ    . TYR A 1 672  ? 113.375 125.802 115.782 1.00 69.93  ? 672  TYR A CZ    1 
ATOM   4517 O  OH    . TYR A 1 672  ? 112.045 125.582 115.503 1.00 69.93  ? 672  TYR A OH    1 
ATOM   4518 N  N     . PHE A 1 673  ? 118.176 125.373 113.544 1.00 67.53  ? 673  PHE A N     1 
ATOM   4519 C  CA    . PHE A 1 673  ? 118.620 124.252 112.721 1.00 67.53  ? 673  PHE A CA    1 
ATOM   4520 C  C     . PHE A 1 673  ? 120.019 124.501 112.166 1.00 67.53  ? 673  PHE A C     1 
ATOM   4521 O  O     . PHE A 1 673  ? 120.871 123.601 112.166 1.00 67.53  ? 673  PHE A O     1 
ATOM   4522 C  CB    . PHE A 1 673  ? 117.618 124.021 111.590 1.00 67.53  ? 673  PHE A CB    1 
ATOM   4523 C  CG    . PHE A 1 673  ? 117.952 122.860 110.701 1.00 67.53  ? 673  PHE A CG    1 
ATOM   4524 C  CD1   . PHE A 1 673  ? 117.738 121.561 111.127 1.00 67.53  ? 673  PHE A CD1   1 
ATOM   4525 C  CD2   . PHE A 1 673  ? 118.462 123.068 109.430 1.00 67.53  ? 673  PHE A CD2   1 
ATOM   4526 C  CE1   . PHE A 1 673  ? 118.036 120.490 110.307 1.00 67.53  ? 673  PHE A CE1   1 
ATOM   4527 C  CE2   . PHE A 1 673  ? 118.762 122.001 108.605 1.00 67.53  ? 673  PHE A CE2   1 
ATOM   4528 C  CZ    . PHE A 1 673  ? 118.548 120.710 109.044 1.00 67.53  ? 673  PHE A CZ    1 
ATOM   4529 N  N     . TYR A 1 674  ? 120.275 125.723 111.695 1.00 70.12  ? 674  TYR A N     1 
ATOM   4530 C  CA    . TYR A 1 674  ? 121.609 126.068 111.221 1.00 70.12  ? 674  TYR A CA    1 
ATOM   4531 C  C     . TYR A 1 674  ? 122.626 125.991 112.352 1.00 70.12  ? 674  TYR A C     1 
ATOM   4532 O  O     . TYR A 1 674  ? 123.763 125.555 112.145 1.00 70.12  ? 674  TYR A O     1 
ATOM   4533 C  CB    . TYR A 1 674  ? 121.598 127.463 110.595 1.00 70.12  ? 674  TYR A CB    1 
ATOM   4534 C  CG    . TYR A 1 674  ? 122.968 128.082 110.443 1.00 70.12  ? 674  TYR A CG    1 
ATOM   4535 C  CD1   . TYR A 1 674  ? 123.849 127.633 109.469 1.00 70.12  ? 674  TYR A CD1   1 
ATOM   4536 C  CD2   . TYR A 1 674  ? 123.379 129.120 111.270 1.00 70.12  ? 674  TYR A CD2   1 
ATOM   4537 C  CE1   . TYR A 1 674  ? 125.102 128.197 109.324 1.00 70.12  ? 674  TYR A CE1   1 
ATOM   4538 C  CE2   . TYR A 1 674  ? 124.629 129.690 111.133 1.00 70.12  ? 674  TYR A CE2   1 
ATOM   4539 C  CZ    . TYR A 1 674  ? 125.486 129.225 110.158 1.00 70.12  ? 674  TYR A CZ    1 
ATOM   4540 O  OH    . TYR A 1 674  ? 126.733 129.790 110.017 1.00 70.12  ? 674  TYR A OH    1 
ATOM   4541 N  N     . ARG A 1 675  ? 122.232 126.406 113.558 1.00 64.99  ? 675  ARG A N     1 
ATOM   4542 C  CA    . ARG A 1 675  ? 123.123 126.283 114.707 1.00 64.99  ? 675  ARG A CA    1 
ATOM   4543 C  C     . ARG A 1 675  ? 123.409 124.821 115.028 1.00 64.99  ? 675  ARG A C     1 
ATOM   4544 O  O     . ARG A 1 675  ? 124.530 124.469 115.410 1.00 64.99  ? 675  ARG A O     1 
ATOM   4545 C  CB    . ARG A 1 675  ? 122.518 126.993 115.917 1.00 64.99  ? 675  ARG A CB    1 
ATOM   4546 C  CG    . ARG A 1 675  ? 123.457 127.100 117.105 1.00 64.99  ? 675  ARG A CG    1 
ATOM   4547 C  CD    . ARG A 1 675  ? 122.689 127.270 118.404 1.00 64.99  ? 675  ARG A CD    1 
ATOM   4548 N  NE    . ARG A 1 675  ? 121.572 128.199 118.263 1.00 64.99  ? 675  ARG A NE    1 
ATOM   4549 C  CZ    . ARG A 1 675  ? 120.897 128.716 119.284 1.00 64.99  ? 675  ARG A CZ    1 
ATOM   4550 N  NH1   . ARG A 1 675  ? 119.894 129.555 119.062 1.00 64.99  ? 675  ARG A NH1   1 
ATOM   4551 N  NH2   . ARG A 1 675  ? 121.224 128.395 120.529 1.00 64.99  ? 675  ARG A NH2   1 
ATOM   4552 N  N     . LEU A 1 676  ? 122.402 123.957 114.884 1.00 59.72  ? 676  LEU A N     1 
ATOM   4553 C  CA    . LEU A 1 676  ? 122.605 122.532 115.124 1.00 59.72  ? 676  LEU A CA    1 
ATOM   4554 C  C     . LEU A 1 676  ? 123.585 121.938 114.120 1.00 59.72  ? 676  LEU A C     1 
ATOM   4555 O  O     . LEU A 1 676  ? 124.449 121.134 114.486 1.00 59.72  ? 676  LEU A O     1 
ATOM   4556 C  CB    . LEU A 1 676  ? 121.268 121.795 115.066 1.00 59.72  ? 676  LEU A CB    1 
ATOM   4557 C  CG    . LEU A 1 676  ? 121.320 120.288 115.316 1.00 59.72  ? 676  LEU A CG    1 
ATOM   4558 C  CD1   . LEU A 1 676  ? 121.790 120.000 116.731 1.00 59.72  ? 676  LEU A CD1   1 
ATOM   4559 C  CD2   . LEU A 1 676  ? 119.962 119.658 115.061 1.00 59.72  ? 676  LEU A CD2   1 
ATOM   4560 N  N     . LEU A 1 677  ? 123.457 122.313 112.846 1.00 62.02  ? 677  LEU A N     1 
ATOM   4561 C  CA    . LEU A 1 677  ? 124.438 121.867 111.857 1.00 62.02  ? 677  LEU A CA    1 
ATOM   4562 C  C     . LEU A 1 677  ? 125.825 122.422 112.161 1.00 62.02  ? 677  LEU A C     1 
ATOM   4563 O  O     . LEU A 1 677  ? 126.831 121.726 111.986 1.00 62.02  ? 677  LEU A O     1 
ATOM   4564 C  CB    . LEU A 1 677  ? 124.000 122.248 110.442 1.00 62.02  ? 677  LEU A CB    1 
ATOM   4565 C  CG    . LEU A 1 677  ? 123.016 121.319 109.720 1.00 62.02  ? 677  LEU A CG    1 
ATOM   4566 C  CD1   . LEU A 1 677  ? 123.665 119.961 109.495 1.00 62.02  ? 677  LEU A CD1   1 
ATOM   4567 C  CD2   . LEU A 1 677  ? 121.705 121.153 110.461 1.00 62.02  ? 677  LEU A CD2   1 
ATOM   4568 N  N     . LYS A 1 678  ? 125.899 123.676 112.613 1.00 62.87  ? 678  LYS A N     1 
ATOM   4569 C  CA    . LYS A 1 678  ? 127.178 124.245 113.025 1.00 62.87  ? 678  LYS A CA    1 
ATOM   4570 C  C     . LYS A 1 678  ? 127.782 123.472 114.190 1.00 62.87  ? 678  LYS A C     1 
ATOM   4571 O  O     . LYS A 1 678  ? 129.010 123.387 114.312 1.00 62.87  ? 678  LYS A O     1 
ATOM   4572 C  CB    . LYS A 1 678  ? 126.996 125.716 113.403 1.00 62.87  ? 678  LYS A CB    1 
ATOM   4573 C  CG    . LYS A 1 678  ? 128.287 126.450 113.728 1.00 62.87  ? 678  LYS A CG    1 
ATOM   4574 C  CD    . LYS A 1 678  ? 128.011 127.883 114.158 1.00 62.87  ? 678  LYS A CD    1 
ATOM   4575 C  CE    . LYS A 1 678  ? 127.609 128.748 112.975 1.00 62.87  ? 678  LYS A CE    1 
ATOM   4576 N  NZ    . LYS A 1 678  ? 127.448 130.178 113.357 1.00 62.87  ? 678  LYS A NZ    1 
ATOM   4577 N  N     . LEU A 1 679  ? 126.937 122.901 115.050 1.00 58.78  ? 679  LEU A N     1 
ATOM   4578 C  CA    . LEU A 1 679  ? 127.415 122.143 116.201 1.00 58.78  ? 679  LEU A CA    1 
ATOM   4579 C  C     . LEU A 1 679  ? 128.169 120.883 115.796 1.00 58.78  ? 679  LEU A C     1 
ATOM   4580 O  O     . LEU A 1 679  ? 128.902 120.321 116.617 1.00 58.78  ? 679  LEU A O     1 
ATOM   4581 C  CB    . LEU A 1 679  ? 126.232 121.780 117.100 1.00 58.78  ? 679  LEU A CB    1 
ATOM   4582 C  CG    . LEU A 1 679  ? 126.503 121.275 118.517 1.00 58.78  ? 679  LEU A CG    1 
ATOM   4583 C  CD1   . LEU A 1 679  ? 127.446 122.209 119.255 1.00 58.78  ? 679  LEU A CD1   1 
ATOM   4584 C  CD2   . LEU A 1 679  ? 125.191 121.127 119.265 1.00 58.78  ? 679  LEU A CD2   1 
ATOM   4585 N  N     . ASN A 1 680  ? 128.013 120.431 114.554 1.00 53.20  ? 680  ASN A N     1 
ATOM   4586 C  CA    . ASN A 1 680  ? 128.638 119.203 114.069 1.00 53.20  ? 680  ASN A CA    1 
ATOM   4587 C  C     . ASN A 1 680  ? 129.904 119.498 113.272 1.00 53.20  ? 680  ASN A C     1 
ATOM   4588 O  O     . ASN A 1 680  ? 130.214 118.817 112.291 1.00 53.20  ? 680  ASN A O     1 
ATOM   4589 C  CB    . ASN A 1 680  ? 127.643 118.407 113.231 1.00 53.20  ? 680  ASN A CB    1 
ATOM   4590 C  CG    . ASN A 1 680  ? 128.049 116.962 113.066 1.00 53.20  ? 680  ASN A CG    1 
ATOM   4591 O  OD1   . ASN A 1 680  ? 128.888 116.459 113.811 1.00 53.20  ? 680  ASN A OD1   1 
ATOM   4592 N  ND2   . ASN A 1 680  ? 127.458 116.284 112.088 1.00 53.20  ? 680  ASN A ND2   1 
ATOM   4593 N  N     . SER A 1 681  ? 130.643 120.527 113.680 1.00 56.38  ? 681  SER A N     1 
ATOM   4594 C  CA    . SER A 1 681  ? 131.821 120.959 112.929 1.00 56.38  ? 681  SER A CA    1 
ATOM   4595 C  C     . SER A 1 681  ? 132.919 119.905 112.817 1.00 56.38  ? 681  SER A C     1 
ATOM   4596 O  O     . SER A 1 681  ? 133.439 119.715 111.704 1.00 56.38  ? 681  SER A O     1 
ATOM   4597 C  CB    . SER A 1 681  ? 132.368 122.250 113.547 1.00 56.38  ? 681  SER A CB    1 
ATOM   4598 O  OG    . SER A 1 681  ? 133.588 122.630 112.934 1.00 56.38  ? 681  SER A OG    1 
ATOM   4599 N  N     . PRO A 1 682  ? 133.334 119.209 113.889 1.00 51.74  ? 682  PRO A N     1 
ATOM   4600 C  CA    . PRO A 1 682  ? 134.576 118.413 113.794 1.00 51.74  ? 682  PRO A CA    1 
ATOM   4601 C  C     . PRO A 1 682  ? 134.586 117.374 112.686 1.00 51.74  ? 682  PRO A C     1 
ATOM   4602 O  O     . PRO A 1 682  ? 135.626 117.180 112.044 1.00 51.74  ? 682  PRO A O     1 
ATOM   4603 C  CB    . PRO A 1 682  ? 134.670 117.757 115.178 1.00 51.74  ? 682  PRO A CB    1 
ATOM   4604 C  CG    . PRO A 1 682  ? 133.931 118.672 116.071 1.00 51.74  ? 682  PRO A CG    1 
ATOM   4605 C  CD    . PRO A 1 682  ? 132.780 119.165 115.254 1.00 51.74  ? 682  PRO A CD    1 
ATOM   4606 N  N     . GLU A 1 683  ? 133.468 116.696 112.438 1.00 49.82  ? 683  GLU A N     1 
ATOM   4607 C  CA    . GLU A 1 683  ? 133.420 115.654 111.412 1.00 49.82  ? 683  GLU A CA    1 
ATOM   4608 C  C     . GLU A 1 683  ? 132.878 116.212 110.094 1.00 49.82  ? 683  GLU A C     1 
ATOM   4609 O  O     . GLU A 1 683  ? 131.880 115.748 109.544 1.00 49.82  ? 683  GLU A O     1 
ATOM   4610 C  CB    . GLU A 1 683  ? 132.591 114.472 111.899 1.00 49.82  ? 683  GLU A CB    1 
ATOM   4611 C  CG    . GLU A 1 683  ? 131.246 114.861 112.476 1.00 49.82  ? 683  GLU A CG    1 
ATOM   4612 C  CD    . GLU A 1 683  ? 130.273 113.705 112.514 1.00 49.82  ? 683  GLU A CD    1 
ATOM   4613 O  OE1   . GLU A 1 683  ? 129.060 113.957 112.661 1.00 49.82  ? 683  GLU A OE1   1 
ATOM   4614 O  OE2   . GLU A 1 683  ? 130.720 112.545 112.397 1.00 49.82  ? 683  GLU A OE2   1 
ATOM   4615 N  N     . TRP A 1 684  ? 133.567 117.228 109.582 1.00 53.90  ? 684  TRP A N     1 
ATOM   4616 C  CA    . TRP A 1 684  ? 133.155 117.819 108.314 1.00 53.90  ? 684  TRP A CA    1 
ATOM   4617 C  C     . TRP A 1 684  ? 133.506 116.954 107.099 1.00 53.90  ? 684  TRP A C     1 
ATOM   4618 O  O     . TRP A 1 684  ? 132.725 116.945 106.139 1.00 53.90  ? 684  TRP A O     1 
ATOM   4619 C  CB    . TRP A 1 684  ? 133.727 119.237 108.165 1.00 53.90  ? 684  TRP A CB    1 
ATOM   4620 C  CG    . TRP A 1 684  ? 135.209 119.366 107.924 1.00 53.90  ? 684  TRP A CG    1 
ATOM   4621 C  CD1   . TRP A 1 684  ? 135.896 119.008 106.799 1.00 53.90  ? 684  TRP A CD1   1 
ATOM   4622 C  CD2   . TRP A 1 684  ? 136.179 119.904 108.830 1.00 53.90  ? 684  TRP A CD2   1 
ATOM   4623 N  NE1   . TRP A 1 684  ? 137.233 119.283 106.952 1.00 53.90  ? 684  TRP A NE1   1 
ATOM   4624 C  CE2   . TRP A 1 684  ? 137.432 119.835 108.190 1.00 53.90  ? 684  TRP A CE2   1 
ATOM   4625 C  CE3   . TRP A 1 684  ? 136.110 120.436 110.121 1.00 53.90  ? 684  TRP A CE3   1 
ATOM   4626 C  CZ2   . TRP A 1 684  ? 138.605 120.276 108.796 1.00 53.90  ? 684  TRP A CZ2   1 
ATOM   4627 C  CZ3   . TRP A 1 684  ? 137.276 120.873 110.721 1.00 53.90  ? 684  TRP A CZ3   1 
ATOM   4628 C  CH2   . TRP A 1 684  ? 138.506 120.790 110.059 1.00 53.90  ? 684  TRP A CH2   1 
ATOM   4629 N  N     . PRO A 1 685  ? 134.639 116.227 107.062 1.00 52.61  ? 685  PRO A N     1 
ATOM   4630 C  CA    . PRO A 1 685  ? 134.915 115.429 105.851 1.00 52.61  ? 685  PRO A CA    1 
ATOM   4631 C  C     . PRO A 1 685  ? 133.857 114.377 105.570 1.00 52.61  ? 685  PRO A C     1 
ATOM   4632 O  O     . PRO A 1 685  ? 133.513 114.140 104.403 1.00 52.61  ? 685  PRO A O     1 
ATOM   4633 C  CB    . PRO A 1 685  ? 136.282 114.793 106.150 1.00 52.61  ? 685  PRO A CB    1 
ATOM   4634 C  CG    . PRO A 1 685  ? 136.868 115.620 107.227 1.00 52.61  ? 685  PRO A CG    1 
ATOM   4635 C  CD    . PRO A 1 685  ? 135.708 116.030 108.060 1.00 52.61  ? 685  PRO A CD    1 
ATOM   4636 N  N     . TYR A 1 686  ? 133.324 113.742 106.616 1.00 51.77  ? 686  TYR A N     1 
ATOM   4637 C  CA    . TYR A 1 686  ? 132.274 112.750 106.419 1.00 51.77  ? 686  TYR A CA    1 
ATOM   4638 C  C     . TYR A 1 686  ? 131.031 113.384 105.814 1.00 51.77  ? 686  TYR A C     1 
ATOM   4639 O  O     . TYR A 1 686  ? 130.428 112.826 104.891 1.00 51.77  ? 686  TYR A O     1 
ATOM   4640 C  CB    . TYR A 1 686  ? 131.939 112.070 107.745 1.00 51.77  ? 686  TYR A CB    1 
ATOM   4641 C  CG    . TYR A 1 686  ? 133.065 111.231 108.298 1.00 51.77  ? 686  TYR A CG    1 
ATOM   4642 C  CD1   . TYR A 1 686  ? 133.742 110.329 107.492 1.00 51.77  ? 686  TYR A CD1   1 
ATOM   4643 C  CD2   . TYR A 1 686  ? 133.453 111.341 109.626 1.00 51.77  ? 686  TYR A CD2   1 
ATOM   4644 C  CE1   . TYR A 1 686  ? 134.772 109.559 107.990 1.00 51.77  ? 686  TYR A CE1   1 
ATOM   4645 C  CE2   . TYR A 1 686  ? 134.483 110.575 110.134 1.00 51.77  ? 686  TYR A CE2   1 
ATOM   4646 C  CZ    . TYR A 1 686  ? 135.138 109.685 109.311 1.00 51.77  ? 686  TYR A CZ    1 
ATOM   4647 O  OH    . TYR A 1 686  ? 136.166 108.918 109.809 1.00 51.77  ? 686  TYR A OH    1 
ATOM   4648 N  N     . SER A 1 687  ? 130.641 114.558 106.314 1.00 51.65  ? 687  SER A N     1 
ATOM   4649 C  CA    . SER A 1 687  ? 129.480 115.247 105.762 1.00 51.65  ? 687  SER A CA    1 
ATOM   4650 C  C     . SER A 1 687  ? 129.711 115.641 104.309 1.00 51.65  ? 687  SER A C     1 
ATOM   4651 O  O     . SER A 1 687  ? 128.808 115.515 103.476 1.00 51.65  ? 687  SER A O     1 
ATOM   4652 C  CB    . SER A 1 687  ? 129.151 116.479 106.603 1.00 51.65  ? 687  SER A CB    1 
ATOM   4653 O  OG    . SER A 1 687  ? 128.120 117.241 106.001 1.00 51.65  ? 687  SER A OG    1 
ATOM   4654 N  N     . ILE A 1 688  ? 130.914 116.121 103.987 1.00 53.16  ? 688  ILE A N     1 
ATOM   4655 C  CA    . ILE A 1 688  ? 131.207 116.529 102.615 1.00 53.16  ? 688  ILE A CA    1 
ATOM   4656 C  C     . ILE A 1 688  ? 131.130 115.333 101.674 1.00 53.16  ? 688  ILE A C     1 
ATOM   4657 O  O     . ILE A 1 688  ? 130.515 115.403 100.603 1.00 53.16  ? 688  ILE A O     1 
ATOM   4658 C  CB    . ILE A 1 688  ? 132.579 117.223 102.540 1.00 53.16  ? 688  ILE A CB    1 
ATOM   4659 C  CG1   . ILE A 1 688  ? 132.567 118.508 103.370 1.00 53.16  ? 688  ILE A CG1   1 
ATOM   4660 C  CG2   . ILE A 1 688  ? 132.950 117.519 101.097 1.00 53.16  ? 688  ILE A CG2   1 
ATOM   4661 C  CD1   . ILE A 1 688  ? 133.933 119.122 103.570 1.00 53.16  ? 688  ILE A CD1   1 
ATOM   4662 N  N     . MET A 1 689  ? 131.736 114.208 102.066 1.00 53.52  ? 689  MET A N     1 
ATOM   4663 C  CA    . MET A 1 689  ? 131.726 113.043 101.186 1.00 53.52  ? 689  MET A CA    1 
ATOM   4664 C  C     . MET A 1 689  ? 130.329 112.442 101.078 1.00 53.52  ? 689  MET A C     1 
ATOM   4665 O  O     . MET A 1 689  ? 129.942 111.945 100.015 1.00 53.52  ? 689  MET A O     1 
ATOM   4666 C  CB    . MET A 1 689  ? 132.732 111.999 101.672 1.00 53.52  ? 689  MET A CB    1 
ATOM   4667 C  CG    . MET A 1 689  ? 133.201 111.053 100.574 1.00 53.52  ? 689  MET A CG    1 
ATOM   4668 S  SD    . MET A 1 689  ? 134.673 110.110 101.019 1.00 53.52  ? 689  MET A SD    1 
ATOM   4669 C  CE    . MET A 1 689  ? 135.020 109.272 99.473  1.00 53.52  ? 689  MET A CE    1 
ATOM   4670 N  N     . GLY A 1 690  ? 129.549 112.497 102.160 1.00 48.94  ? 690  GLY A N     1 
ATOM   4671 C  CA    . GLY A 1 690  ? 128.174 112.035 102.086 1.00 48.94  ? 690  GLY A CA    1 
ATOM   4672 C  C     . GLY A 1 690  ? 127.312 112.901 101.189 1.00 48.94  ? 690  GLY A C     1 
ATOM   4673 O  O     . GLY A 1 690  ? 126.476 112.394 100.442 1.00 48.94  ? 690  GLY A O     1 
ATOM   4674 N  N     . ALA A 1 691  ? 127.497 114.222 101.257 1.00 51.63  ? 691  ALA A N     1 
ATOM   4675 C  CA    . ALA A 1 691  ? 126.778 115.113 100.353 1.00 51.63  ? 691  ALA A CA    1 
ATOM   4676 C  C     . ALA A 1 691  ? 127.187 114.863 98.908  1.00 51.63  ? 691  ALA A C     1 
ATOM   4677 O  O     . ALA A 1 691  ? 126.350 114.912 97.995  1.00 51.63  ? 691  ALA A O     1 
ATOM   4678 C  CB    . ALA A 1 691  ? 127.026 116.570 100.746 1.00 51.63  ? 691  ALA A CB    1 
ATOM   4679 N  N     . VAL A 1 692  ? 128.472 114.585 98.684  1.00 53.67  ? 692  VAL A N     1 
ATOM   4680 C  CA    . VAL A 1 692  ? 128.935 114.232 97.345  1.00 53.67  ? 692  VAL A CA    1 
ATOM   4681 C  C     . VAL A 1 692  ? 128.239 112.964 96.861  1.00 53.67  ? 692  VAL A C     1 
ATOM   4682 O  O     . VAL A 1 692  ? 127.755 112.896 95.726  1.00 53.67  ? 692  VAL A O     1 
ATOM   4683 C  CB    . VAL A 1 692  ? 130.467 114.085 97.330  1.00 53.67  ? 692  VAL A CB    1 
ATOM   4684 C  CG1   . VAL A 1 692  ? 130.926 113.403 96.057  1.00 53.67  ? 692  VAL A CG1   1 
ATOM   4685 C  CG2   . VAL A 1 692  ? 131.122 115.450 97.455  1.00 53.67  ? 692  VAL A CG2   1 
ATOM   4686 N  N     . GLY A 1 693  ? 128.161 111.949 97.723  1.00 52.19  ? 693  GLY A N     1 
ATOM   4687 C  CA    . GLY A 1 693  ? 127.486 110.717 97.341  1.00 52.19  ? 693  GLY A CA    1 
ATOM   4688 C  C     . GLY A 1 693  ? 126.003 110.913 97.086  1.00 52.19  ? 693  GLY A C     1 
ATOM   4689 O  O     . GLY A 1 693  ? 125.439 110.320 96.164  1.00 52.19  ? 693  GLY A O     1 
ATOM   4690 N  N     . SER A 1 694  ? 125.351 111.745 97.901  1.00 52.84  ? 694  SER A N     1 
ATOM   4691 C  CA    . SER A 1 694  ? 123.926 112.006 97.717  1.00 52.84  ? 694  SER A CA    1 
ATOM   4692 C  C     . SER A 1 694  ? 123.651 112.707 96.395  1.00 52.84  ? 694  SER A C     1 
ATOM   4693 O  O     . SER A 1 694  ? 122.748 112.307 95.652  1.00 52.84  ? 694  SER A O     1 
ATOM   4694 C  CB    . SER A 1 694  ? 123.386 112.827 98.885  1.00 52.84  ? 694  SER A CB    1 
ATOM   4695 O  OG    . SER A 1 694  ? 123.807 112.263 100.107 1.00 52.84  ? 694  SER A OG    1 
ATOM   4696 N  N     . ILE A 1 695  ? 124.433 113.740 96.068  1.00 56.08  ? 695  ILE A N     1 
ATOM   4697 C  CA    . ILE A 1 695  ? 124.280 114.394 94.769  1.00 56.08  ? 695  ILE A CA    1 
ATOM   4698 C  C     . ILE A 1 695  ? 124.557 113.395 93.648  1.00 56.08  ? 695  ILE A C     1 
ATOM   4699 O  O     . ILE A 1 695  ? 123.810 113.314 92.658  1.00 56.08  ? 695  ILE A O     1 
ATOM   4700 C  CB    . ILE A 1 695  ? 125.209 115.625 94.685  1.00 56.08  ? 695  ILE A CB    1 
ATOM   4701 C  CG1   . ILE A 1 695  ? 124.810 116.688 95.715  1.00 56.08  ? 695  ILE A CG1   1 
ATOM   4702 C  CG2   . ILE A 1 695  ? 125.208 116.248 93.271  1.00 56.08  ? 695  ILE A CG2   1 
ATOM   4703 C  CD1   . ILE A 1 695  ? 125.818 117.815 95.830  1.00 56.08  ? 695  ILE A CD1   1 
ATOM   4704 N  N     . LEU A 1 696  ? 125.617 112.593 93.803  1.00 56.33  ? 696  LEU A N     1 
ATOM   4705 C  CA    . LEU A 1 696  ? 126.064 111.725 92.722  1.00 56.33  ? 696  LEU A CA    1 
ATOM   4706 C  C     . LEU A 1 696  ? 125.040 110.633 92.434  1.00 56.33  ? 696  LEU A C     1 
ATOM   4707 O  O     . LEU A 1 696  ? 124.829 110.259 91.274  1.00 56.33  ? 696  LEU A O     1 
ATOM   4708 C  CB    . LEU A 1 696  ? 127.413 111.101 93.069  1.00 56.33  ? 696  LEU A CB    1 
ATOM   4709 C  CG    . LEU A 1 696  ? 128.587 111.970 92.595  1.00 56.33  ? 696  LEU A CG    1 
ATOM   4710 C  CD1   . LEU A 1 696  ? 129.935 111.518 93.188  1.00 56.33  ? 696  LEU A CD1   1 
ATOM   4711 C  CD2   . LEU A 1 696  ? 128.637 112.241 91.088  1.00 56.33  ? 696  LEU A CD2   1 
ATOM   4712 N  N     . SER A 1 697  ? 124.420 110.084 93.484  1.00 53.00  ? 697  SER A N     1 
ATOM   4713 C  CA    . SER A 1 697  ? 123.270 109.204 93.298  1.00 53.00  ? 697  SER A CA    1 
ATOM   4714 C  C     . SER A 1 697  ? 122.063 109.979 92.789  1.00 53.00  ? 697  SER A C     1 
ATOM   4715 O  O     . SER A 1 697  ? 121.156 109.393 92.191  1.00 53.00  ? 697  SER A O     1 
ATOM   4716 C  CB    . SER A 1 697  ? 122.922 108.488 94.604  1.00 53.00  ? 697  SER A CB    1 
ATOM   4717 O  OG    . SER A 1 697  ? 122.471 109.405 95.587  1.00 53.00  ? 697  SER A OG    1 
ATOM   4718 N  N     . GLY A 1 698  ? 122.018 111.287 93.045  1.00 57.10  ? 698  GLY A N     1 
ATOM   4719 C  CA    . GLY A 1 698  ? 120.965 112.108 92.471  1.00 57.10  ? 698  GLY A CA    1 
ATOM   4720 C  C     . GLY A 1 698  ? 121.020 112.177 90.956  1.00 57.10  ? 698  GLY A C     1 
ATOM   4721 O  O     . GLY A 1 698  ? 119.983 112.281 90.295  1.00 57.10  ? 698  GLY A O     1 
ATOM   4722 N  N     . PHE A 1 699  ? 122.229 112.144 90.383  1.00 60.44  ? 699  PHE A N     1 
ATOM   4723 C  CA    . PHE A 1 699  ? 122.340 112.139 88.921  1.00 60.44  ? 699  PHE A CA    1 
ATOM   4724 C  C     . PHE A 1 699  ? 121.662 110.929 88.289  1.00 60.44  ? 699  PHE A C     1 
ATOM   4725 O  O     . PHE A 1 699  ? 121.000 111.057 87.252  1.00 60.44  ? 699  PHE A O     1 
ATOM   4726 C  CB    . PHE A 1 699  ? 123.800 112.189 88.469  1.00 60.44  ? 699  PHE A CB    1 
ATOM   4727 C  CG    . PHE A 1 699  ? 124.488 113.475 88.772  1.00 60.44  ? 699  PHE A CG    1 
ATOM   4728 C  CD1   . PHE A 1 699  ? 124.307 114.563 87.940  1.00 60.44  ? 699  PHE A CD1   1 
ATOM   4729 C  CD2   . PHE A 1 699  ? 125.301 113.610 89.881  1.00 60.44  ? 699  PHE A CD2   1 
ATOM   4730 C  CE1   . PHE A 1 699  ? 124.935 115.758 88.199  1.00 60.44  ? 699  PHE A CE1   1 
ATOM   4731 C  CE2   . PHE A 1 699  ? 125.930 114.811 90.149  1.00 60.44  ? 699  PHE A CE2   1 
ATOM   4732 C  CZ    . PHE A 1 699  ? 125.745 115.886 89.307  1.00 60.44  ? 699  PHE A CZ    1 
ATOM   4733 N  N     . ILE A 1 700  ? 121.820 109.744 88.883  1.00 63.55  ? 700  ILE A N     1 
ATOM   4734 C  CA    . ILE A 1 700  ? 121.449 108.515 88.188  1.00 63.55  ? 700  ILE A CA    1 
ATOM   4735 C  C     . ILE A 1 700  ? 119.943 108.364 88.008  1.00 63.55  ? 700  ILE A C     1 
ATOM   4736 O  O     . ILE A 1 700  ? 119.504 107.567 87.169  1.00 63.55  ? 700  ILE A O     1 
ATOM   4737 C  CB    . ILE A 1 700  ? 122.044 107.294 88.925  1.00 63.55  ? 700  ILE A CB    1 
ATOM   4738 C  CG1   . ILE A 1 700  ? 121.905 106.028 88.083  1.00 63.55  ? 700  ILE A CG1   1 
ATOM   4739 C  CG2   . ILE A 1 700  ? 121.334 107.055 90.241  1.00 63.55  ? 700  ILE A CG2   1 
ATOM   4740 C  CD1   . ILE A 1 700  ? 122.737 104.874 88.581  1.00 63.55  ? 700  ILE A CD1   1 
ATOM   4741 N  N     . GLY A 1 701  ? 119.138 109.134 88.739  1.00 62.67  ? 701  GLY A N     1 
ATOM   4742 C  CA    . GLY A 1 701  ? 117.698 109.057 88.637  1.00 62.67  ? 701  GLY A CA    1 
ATOM   4743 C  C     . GLY A 1 701  ? 117.170 109.262 87.228  1.00 62.67  ? 701  GLY A C     1 
ATOM   4744 O  O     . GLY A 1 701  ? 116.639 108.338 86.604  1.00 62.67  ? 701  GLY A O     1 
ATOM   4745 N  N     . PRO A 1 702  ? 117.307 110.480 86.694  1.00 62.06  ? 702  PRO A N     1 
ATOM   4746 C  CA    . PRO A 1 702  ? 116.779 110.755 85.347  1.00 62.06  ? 702  PRO A CA    1 
ATOM   4747 C  C     . PRO A 1 702  ? 117.591 110.137 84.217  1.00 62.06  ? 702  PRO A C     1 
ATOM   4748 O  O     . PRO A 1 702  ? 117.112 110.131 83.073  1.00 62.06  ? 702  PRO A O     1 
ATOM   4749 C  CB    . PRO A 1 702  ? 116.800 112.286 85.271  1.00 62.06  ? 702  PRO A CB    1 
ATOM   4750 C  CG    . PRO A 1 702  ? 117.867 112.692 86.221  1.00 62.06  ? 702  PRO A CG    1 
ATOM   4751 C  CD    . PRO A 1 702  ? 117.834 111.694 87.341  1.00 62.06  ? 702  PRO A CD    1 
ATOM   4752 N  N     . THR A 1 703  ? 118.794 109.623 84.489  1.00 62.89  ? 703  THR A N     1 
ATOM   4753 C  CA    . THR A 1 703  ? 119.575 108.990 83.431  1.00 62.89  ? 703  THR A CA    1 
ATOM   4754 C  C     . THR A 1 703  ? 118.873 107.747 82.901  1.00 62.89  ? 703  THR A C     1 
ATOM   4755 O  O     . THR A 1 703  ? 118.958 107.438 81.706  1.00 62.89  ? 703  THR A O     1 
ATOM   4756 C  CB    . THR A 1 703  ? 120.974 108.639 83.933  1.00 62.89  ? 703  THR A CB    1 
ATOM   4757 O  OG1   . THR A 1 703  ? 120.873 107.876 85.140  1.00 62.89  ? 703  THR A OG1   1 
ATOM   4758 C  CG2   . THR A 1 703  ? 121.772 109.904 84.203  1.00 62.89  ? 703  THR A CG2   1 
ATOM   4759 N  N     . PHE A 1 704  ? 118.183 107.015 83.778  1.00 64.96  ? 704  PHE A N     1 
ATOM   4760 C  CA    . PHE A 1 704  ? 117.404 105.865 83.333  1.00 64.96  ? 704  PHE A CA    1 
ATOM   4761 C  C     . PHE A 1 704  ? 116.344 106.285 82.324  1.00 64.96  ? 704  PHE A C     1 
ATOM   4762 O  O     . PHE A 1 704  ? 116.172 105.643 81.281  1.00 64.96  ? 704  PHE A O     1 
ATOM   4763 C  CB    . PHE A 1 704  ? 116.757 105.175 84.534  1.00 64.96  ? 704  PHE A CB    1 
ATOM   4764 C  CG    . PHE A 1 704  ? 117.720 104.387 85.374  1.00 64.96  ? 704  PHE A CG    1 
ATOM   4765 C  CD1   . PHE A 1 704  ? 118.795 103.736 84.795  1.00 64.96  ? 704  PHE A CD1   1 
ATOM   4766 C  CD2   . PHE A 1 704  ? 117.545 104.292 86.743  1.00 64.96  ? 704  PHE A CD2   1 
ATOM   4767 C  CE1   . PHE A 1 704  ? 119.679 103.008 85.567  1.00 64.96  ? 704  PHE A CE1   1 
ATOM   4768 C  CE2   . PHE A 1 704  ? 118.425 103.566 87.519  1.00 64.96  ? 704  PHE A CE2   1 
ATOM   4769 C  CZ    . PHE A 1 704  ? 119.493 102.923 86.930  1.00 64.96  ? 704  PHE A CZ    1 
ATOM   4770 N  N     . ALA A 1 705  ? 115.627 107.372 82.617  1.00 66.54  ? 705  ALA A N     1 
ATOM   4771 C  CA    . ALA A 1 705  ? 114.611 107.863 81.692  1.00 66.54  ? 705  ALA A CA    1 
ATOM   4772 C  C     . ALA A 1 705  ? 115.233 108.328 80.382  1.00 66.54  ? 705  ALA A C     1 
ATOM   4773 O  O     . ALA A 1 705  ? 114.680 108.085 79.303  1.00 66.54  ? 705  ALA A O     1 
ATOM   4774 C  CB    . ALA A 1 705  ? 113.815 108.994 82.341  1.00 66.54  ? 705  ALA A CB    1 
ATOM   4775 N  N     . ILE A 1 706  ? 116.381 109.004 80.458  1.00 68.61  ? 706  ILE A N     1 
ATOM   4776 C  CA    . ILE A 1 706  ? 117.057 109.467 79.247  1.00 68.61  ? 706  ILE A CA    1 
ATOM   4777 C  C     . ILE A 1 706  ? 117.425 108.284 78.359  1.00 68.61  ? 706  ILE A C     1 
ATOM   4778 O  O     . ILE A 1 706  ? 117.162 108.280 77.147  1.00 68.61  ? 706  ILE A O     1 
ATOM   4779 C  CB    . ILE A 1 706  ? 118.303 110.291 79.614  1.00 68.61  ? 706  ILE A CB    1 
ATOM   4780 C  CG1   . ILE A 1 706  ? 117.908 111.566 80.359  1.00 68.61  ? 706  ILE A CG1   1 
ATOM   4781 C  CG2   . ILE A 1 706  ? 119.118 110.610 78.369  1.00 68.61  ? 706  ILE A CG2   1 
ATOM   4782 C  CD1   . ILE A 1 706  ? 119.011 112.586 80.405  1.00 68.61  ? 706  ILE A CD1   1 
ATOM   4783 N  N     . VAL A 1 707  ? 118.036 107.259 78.956  1.00 72.03  ? 707  VAL A N     1 
ATOM   4784 C  CA    . VAL A 1 707  ? 118.468 106.099 78.186  1.00 72.03  ? 707  VAL A CA    1 
ATOM   4785 C  C     . VAL A 1 707  ? 117.268 105.346 77.629  1.00 72.03  ? 707  VAL A C     1 
ATOM   4786 O  O     . VAL A 1 707  ? 117.302 104.861 76.496  1.00 72.03  ? 707  VAL A O     1 
ATOM   4787 C  CB    . VAL A 1 707  ? 119.366 105.191 79.044  1.00 72.03  ? 707  VAL A CB    1 
ATOM   4788 C  CG1   . VAL A 1 707  ? 119.735 103.933 78.278  1.00 72.03  ? 707  VAL A CG1   1 
ATOM   4789 C  CG2   . VAL A 1 707  ? 120.622 105.937 79.456  1.00 72.03  ? 707  VAL A CG2   1 
ATOM   4790 N  N     . MET A 1 708  ? 116.186 105.243 78.404  1.00 74.69  ? 708  MET A N     1 
ATOM   4791 C  CA    . MET A 1 708  ? 114.993 104.564 77.907  1.00 74.69  ? 708  MET A CA    1 
ATOM   4792 C  C     . MET A 1 708  ? 114.372 105.318 76.737  1.00 74.69  ? 708  MET A C     1 
ATOM   4793 O  O     . MET A 1 708  ? 113.908 104.702 75.769  1.00 74.69  ? 708  MET A O     1 
ATOM   4794 C  CB    . MET A 1 708  ? 113.981 104.390 79.038  1.00 74.69  ? 708  MET A CB    1 
ATOM   4795 C  CG    . MET A 1 708  ? 113.088 103.169 78.884  1.00 74.69  ? 708  MET A CG    1 
ATOM   4796 S  SD    . MET A 1 708  ? 111.779 103.371 77.663  1.00 74.69  ? 708  MET A SD    1 
ATOM   4797 C  CE    . MET A 1 708  ? 110.482 104.056 78.686  1.00 74.69  ? 708  MET A CE    1 
ATOM   4798 N  N     . SER A 1 709  ? 114.335 106.650 76.815  1.00 77.68  ? 709  SER A N     1 
ATOM   4799 C  CA    . SER A 1 709  ? 113.802 107.438 75.709  1.00 77.68  ? 709  SER A CA    1 
ATOM   4800 C  C     . SER A 1 709  ? 114.647 107.265 74.454  1.00 77.68  ? 709  SER A C     1 
ATOM   4801 O  O     . SER A 1 709  ? 114.112 107.098 73.351  1.00 77.68  ? 709  SER A O     1 
ATOM   4802 C  CB    . SER A 1 709  ? 113.722 108.911 76.108  1.00 77.68  ? 709  SER A CB    1 
ATOM   4803 O  OG    . SER A 1 709  ? 112.946 109.076 77.282  1.00 77.68  ? 709  SER A OG    1 
ATOM   4804 N  N     . ASN A 1 710  ? 115.974 107.288 74.602  1.00 81.75  ? 710  ASN A N     1 
ATOM   4805 C  CA    . ASN A 1 710  ? 116.833 107.044 73.447  1.00 81.75  ? 710  ASN A CA    1 
ATOM   4806 C  C     . ASN A 1 710  ? 116.626 105.635 72.901  1.00 81.75  ? 710  ASN A C     1 
ATOM   4807 O  O     . ASN A 1 710  ? 116.635 105.421 71.681  1.00 81.75  ? 710  ASN A O     1 
ATOM   4808 C  CB    . ASN A 1 710  ? 118.296 107.271 73.821  1.00 81.75  ? 710  ASN A CB    1 
ATOM   4809 C  CG    . ASN A 1 710  ? 118.571 108.700 74.241  1.00 81.75  ? 710  ASN A CG    1 
ATOM   4810 O  OD1   . ASN A 1 710  ? 117.652 109.509 74.361  1.00 81.75  ? 710  ASN A OD1   1 
ATOM   4811 N  ND2   . ASN A 1 710  ? 119.841 109.021 74.460  1.00 81.75  ? 710  ASN A ND2   1 
ATOM   4812 N  N     . MET A 1 711  ? 116.435 104.662 73.794  1.00 86.07  ? 711  MET A N     1 
ATOM   4813 C  CA    . MET A 1 711  ? 116.213 103.285 73.372  1.00 86.07  ? 711  MET A CA    1 
ATOM   4814 C  C     . MET A 1 711  ? 114.940 103.159 72.551  1.00 86.07  ? 711  MET A C     1 
ATOM   4815 O  O     . MET A 1 711  ? 114.932 102.507 71.503  1.00 86.07  ? 711  MET A O     1 
ATOM   4816 C  CB    . MET A 1 711  ? 116.147 102.365 74.594  1.00 86.07  ? 711  MET A CB    1 
ATOM   4817 C  CG    . MET A 1 711  ? 117.487 101.973 75.234  1.00 86.07  ? 711  MET A CG    1 
ATOM   4818 S  SD    . MET A 1 711  ? 118.962 101.710 74.217  1.00 86.07  ? 711  MET A SD    1 
ATOM   4819 C  CE    . MET A 1 711  ? 118.358 100.769 72.816  1.00 86.07  ? 711  MET A CE    1 
ATOM   4820 N  N     . ILE A 1 712  ? 113.851 103.777 73.006  1.00 89.01  ? 712  ILE A N     1 
ATOM   4821 C  CA    . ILE A 1 712  ? 112.602 103.674 72.255  1.00 89.01  ? 712  ILE A CA    1 
ATOM   4822 C  C     . ILE A 1 712  ? 112.703 104.447 70.945  1.00 89.01  ? 712  ILE A C     1 
ATOM   4823 O  O     . ILE A 1 712  ? 112.134 104.040 69.923  1.00 89.01  ? 712  ILE A O     1 
ATOM   4824 C  CB    . ILE A 1 712  ? 111.402 104.124 73.112  1.00 89.01  ? 712  ILE A CB    1 
ATOM   4825 C  CG1   . ILE A 1 712  ? 110.096 103.715 72.430  1.00 89.01  ? 712  ILE A CG1   1 
ATOM   4826 C  CG2   . ILE A 1 712  ? 111.419 105.619 73.364  1.00 89.01  ? 712  ILE A CG2   1 
ATOM   4827 C  CD1   . ILE A 1 712  ? 109.899 102.217 72.346  1.00 89.01  ? 712  ILE A CD1   1 
ATOM   4828 N  N     . GLU A 1 713  ? 113.434 105.567 70.945  1.00 91.67  ? 713  GLU A N     1 
ATOM   4829 C  CA    . GLU A 1 713  ? 113.642 106.312 69.707  1.00 91.67  ? 713  GLU A CA    1 
ATOM   4830 C  C     . GLU A 1 713  ? 114.368 105.463 68.671  1.00 91.67  ? 713  GLU A C     1 
ATOM   4831 O  O     . GLU A 1 713  ? 113.987 105.439 67.494  1.00 91.67  ? 713  GLU A O     1 
ATOM   4832 C  CB    . GLU A 1 713  ? 114.420 107.598 69.988  1.00 91.67  ? 713  GLU A CB    1 
ATOM   4833 C  CG    . GLU A 1 713  ? 114.778 108.406 68.741  1.00 91.67  ? 713  GLU A CG    1 
ATOM   4834 C  CD    . GLU A 1 713  ? 113.656 109.314 68.266  1.00 91.67  ? 713  GLU A CD    1 
ATOM   4835 O  OE1   . GLU A 1 713  ? 112.474 108.979 68.485  1.00 91.67  ? 713  GLU A OE1   1 
ATOM   4836 O  OE2   . GLU A 1 713  ? 113.961 110.368 67.666  1.00 91.67  ? 713  GLU A OE2   1 
ATOM   4837 N  N     . VAL A 1 714  ? 115.423 104.758 69.088  1.00 96.01  ? 714  VAL A N     1 
ATOM   4838 C  CA    . VAL A 1 714  ? 116.152 103.933 68.128  1.00 96.01  ? 714  VAL A CA    1 
ATOM   4839 C  C     . VAL A 1 714  ? 115.351 102.684 67.771  1.00 96.01  ? 714  VAL A C     1 
ATOM   4840 O  O     . VAL A 1 714  ? 115.501 102.137 66.671  1.00 96.01  ? 714  VAL A O     1 
ATOM   4841 C  CB    . VAL A 1 714  ? 117.560 103.590 68.655  1.00 96.01  ? 714  VAL A CB    1 
ATOM   4842 C  CG1   . VAL A 1 714  ? 117.489 102.631 69.821  1.00 96.01  ? 714  VAL A CG1   1 
ATOM   4843 C  CG2   . VAL A 1 714  ? 118.425 103.018 67.540  1.00 96.01  ? 714  VAL A CG2   1 
ATOM   4844 N  N     . PHE A 1 715  ? 114.491 102.211 68.679  1.00 91.18  ? 715  PHE A N     1 
ATOM   4845 C  CA    . PHE A 1 715  ? 113.606 101.097 68.352  1.00 91.18  ? 715  PHE A CA    1 
ATOM   4846 C  C     . PHE A 1 715  ? 112.624 101.473 67.253  1.00 91.18  ? 715  PHE A C     1 
ATOM   4847 O  O     . PHE A 1 715  ? 112.366 100.677 66.342  1.00 91.18  ? 715  PHE A O     1 
ATOM   4848 C  CB    . PHE A 1 715  ? 112.844 100.635 69.596  1.00 91.18  ? 715  PHE A CB    1 
ATOM   4849 C  CG    . PHE A 1 715  ? 113.706 99.983  70.639  1.00 91.18  ? 715  PHE A CG    1 
ATOM   4850 C  CD1   . PHE A 1 715  ? 114.989 99.560  70.339  1.00 91.18  ? 715  PHE A CD1   1 
ATOM   4851 C  CD2   . PHE A 1 715  ? 113.227 99.795  71.924  1.00 91.18  ? 715  PHE A CD2   1 
ATOM   4852 C  CE1   . PHE A 1 715  ? 115.776 98.959  71.302  1.00 91.18  ? 715  PHE A CE1   1 
ATOM   4853 C  CE2   . PHE A 1 715  ? 114.010 99.196  72.890  1.00 91.18  ? 715  PHE A CE2   1 
ATOM   4854 C  CZ    . PHE A 1 715  ? 115.286 98.779  72.579  1.00 91.18  ? 715  PHE A CZ    1 
ATOM   4855 N  N     . TYR A 1 716  ? 112.052 102.677 67.328  1.00 99.24  ? 716  TYR A N     1 
ATOM   4856 C  CA    . TYR A 1 716  ? 111.060 103.072 66.334  1.00 99.24  ? 716  TYR A CA    1 
ATOM   4857 C  C     . TYR A 1 716  ? 111.703 103.386 64.990  1.00 99.24  ? 716  TYR A C     1 
ATOM   4858 O  O     . TYR A 1 716  ? 111.060 103.228 63.946  1.00 99.24  ? 716  TYR A O     1 
ATOM   4859 C  CB    . TYR A 1 716  ? 110.251 104.261 66.847  1.00 99.24  ? 716  TYR A CB    1 
ATOM   4860 C  CG    . TYR A 1 716  ? 109.230 103.867 67.889  1.00 99.24  ? 716  TYR A CG    1 
ATOM   4861 C  CD1   . TYR A 1 716  ? 108.698 102.584 67.913  1.00 99.24  ? 716  TYR A CD1   1 
ATOM   4862 C  CD2   . TYR A 1 716  ? 108.808 104.769 68.856  1.00 99.24  ? 716  TYR A CD2   1 
ATOM   4863 C  CE1   . TYR A 1 716  ? 107.767 102.213 68.863  1.00 99.24  ? 716  TYR A CE1   1 
ATOM   4864 C  CE2   . TYR A 1 716  ? 107.878 104.407 69.811  1.00 99.24  ? 716  TYR A CE2   1 
ATOM   4865 C  CZ    . TYR A 1 716  ? 107.361 103.128 69.811  1.00 99.24  ? 716  TYR A CZ    1 
ATOM   4866 O  OH    . TYR A 1 716  ? 106.434 102.763 70.761  1.00 99.24  ? 716  TYR A OH    1 
ATOM   4867 N  N     . TYR A 1 717  ? 112.961 103.832 64.992  1.00 104.13 ? 717  TYR A N     1 
ATOM   4868 C  CA    . TYR A 1 717  ? 113.715 103.914 63.745  1.00 104.13 ? 717  TYR A CA    1 
ATOM   4869 C  C     . TYR A 1 717  ? 114.002 102.527 63.185  1.00 104.13 ? 717  TYR A C     1 
ATOM   4870 O  O     . TYR A 1 717  ? 114.151 102.367 61.967  1.00 104.13 ? 717  TYR A O     1 
ATOM   4871 C  CB    . TYR A 1 717  ? 115.017 104.682 63.974  1.00 104.13 ? 717  TYR A CB    1 
ATOM   4872 C  CG    . TYR A 1 717  ? 115.837 104.906 62.725  1.00 104.13 ? 717  TYR A CG    1 
ATOM   4873 C  CD1   . TYR A 1 717  ? 115.388 105.748 61.716  1.00 104.13 ? 717  TYR A CD1   1 
ATOM   4874 C  CD2   . TYR A 1 717  ? 117.063 104.278 62.556  1.00 104.13 ? 717  TYR A CD2   1 
ATOM   4875 C  CE1   . TYR A 1 717  ? 116.137 105.956 60.573  1.00 104.13 ? 717  TYR A CE1   1 
ATOM   4876 C  CE2   . TYR A 1 717  ? 117.819 104.478 61.417  1.00 104.13 ? 717  TYR A CE2   1 
ATOM   4877 C  CZ    . TYR A 1 717  ? 117.352 105.318 60.429  1.00 104.13 ? 717  TYR A CZ    1 
ATOM   4878 O  OH    . TYR A 1 717  ? 118.102 105.521 59.294  1.00 104.13 ? 717  TYR A OH    1 
ATOM   4879 N  N     . THR A 1 718  ? 114.123 101.534 64.070  1.00 107.07 ? 718  THR A N     1 
ATOM   4880 C  CA    . THR A 1 718  ? 114.278 100.111 63.778  1.00 107.07 ? 718  THR A CA    1 
ATOM   4881 C  C     . THR A 1 718  ? 115.680 99.809  63.253  1.00 107.07 ? 718  THR A C     1 
ATOM   4882 O  O     . THR A 1 718  ? 116.097 98.646  63.227  1.00 107.07 ? 718  THR A O     1 
ATOM   4883 C  CB    . THR A 1 718  ? 113.199 99.651  62.784  1.00 107.07 ? 718  THR A CB    1 
ATOM   4884 O  OG1   . THR A 1 718  ? 111.911 100.054 63.265  1.00 107.07 ? 718  THR A OG1   1 
ATOM   4885 C  CG2   . THR A 1 718  ? 113.195 98.136  62.629  1.00 107.07 ? 718  THR A CG2   1 
ATOM   4886 N  N     . ASP A 1 719  ? 116.419 100.857 62.877  1.00 106.21 ? 719  ASP A N     1 
ATOM   4887 C  CA    . ASP A 1 719  ? 117.875 100.869 62.745  1.00 106.21 ? 719  ASP A CA    1 
ATOM   4888 C  C     . ASP A 1 719  ? 118.488 99.546  62.296  1.00 106.21 ? 719  ASP A C     1 
ATOM   4889 O  O     . ASP A 1 719  ? 119.332 98.989  63.004  1.00 106.21 ? 719  ASP A O     1 
ATOM   4890 C  CB    . ASP A 1 719  ? 118.511 101.301 64.068  1.00 106.21 ? 719  ASP A CB    1 
ATOM   4891 C  CG    . ASP A 1 719  ? 119.931 101.805 63.894  1.00 106.21 ? 719  ASP A CG    1 
ATOM   4892 O  OD1   . ASP A 1 719  ? 120.102 102.945 63.413  1.00 106.21 ? 719  ASP A OD1   1 
ATOM   4893 O  OD2   . ASP A 1 719  ? 120.875 101.062 64.232  1.00 106.21 ? 719  ASP A OD2   1 
ATOM   4894 N  N     . TYR A 1 720  ? 118.088 99.022  61.137  1.00 108.38 ? 720  TYR A N     1 
ATOM   4895 C  CA    . TYR A 1 720  ? 118.654 97.744  60.721  1.00 108.38 ? 720  TYR A CA    1 
ATOM   4896 C  C     . TYR A 1 720  ? 120.018 97.936  60.070  1.00 108.38 ? 720  TYR A C     1 
ATOM   4897 O  O     . TYR A 1 720  ? 120.286 97.371  59.005  1.00 108.38 ? 720  TYR A O     1 
ATOM   4898 C  CB    . TYR A 1 720  ? 117.715 97.027  59.746  1.00 108.38 ? 720  TYR A CB    1 
ATOM   4899 C  CG    . TYR A 1 720  ? 116.545 96.320  60.392  1.00 108.38 ? 720  TYR A CG    1 
ATOM   4900 C  CD1   . TYR A 1 720  ? 116.576 95.962  61.733  1.00 108.38 ? 720  TYR A CD1   1 
ATOM   4901 C  CD2   . TYR A 1 720  ? 115.410 96.005  59.656  1.00 108.38 ? 720  TYR A CD2   1 
ATOM   4902 C  CE1   . TYR A 1 720  ? 115.506 95.313  62.323  1.00 108.38 ? 720  TYR A CE1   1 
ATOM   4903 C  CE2   . TYR A 1 720  ? 114.338 95.357  60.236  1.00 108.38 ? 720  TYR A CE2   1 
ATOM   4904 C  CZ    . TYR A 1 720  ? 114.390 95.013  61.570  1.00 108.38 ? 720  TYR A CZ    1 
ATOM   4905 O  OH    . TYR A 1 720  ? 113.323 94.368  62.151  1.00 108.38 ? 720  TYR A OH    1 
ATOM   4906 N  N     . ASP A 1 721  ? 120.886 98.730  60.699  1.00 109.97 ? 721  ASP A N     1 
ATOM   4907 C  CA    . ASP A 1 721  ? 122.279 98.813  60.282  1.00 109.97 ? 721  ASP A CA    1 
ATOM   4908 C  C     . ASP A 1 721  ? 123.224 98.530  61.445  1.00 109.97 ? 721  ASP A C     1 
ATOM   4909 O  O     . ASP A 1 721  ? 124.126 97.693  61.333  1.00 109.97 ? 721  ASP A O     1 
ATOM   4910 C  CB    . ASP A 1 721  ? 122.574 100.187 59.678  1.00 109.97 ? 721  ASP A CB    1 
ATOM   4911 C  CG    . ASP A 1 721  ? 123.807 100.182 58.795  1.00 109.97 ? 721  ASP A CG    1 
ATOM   4912 O  OD1   . ASP A 1 721  ? 124.428 99.109  58.646  1.00 109.97 ? 721  ASP A OD1   1 
ATOM   4913 O  OD2   . ASP A 1 721  ? 124.153 101.250 58.248  1.00 109.97 ? 721  ASP A OD2   1 
ATOM   4914 N  N     . SER A 1 722  ? 123.013 99.224  62.573  1.00 105.27 ? 722  SER A N     1 
ATOM   4915 C  CA    . SER A 1 722  ? 123.931 99.148  63.704  1.00 105.27 ? 722  SER A CA    1 
ATOM   4916 C  C     . SER A 1 722  ? 123.205 99.125  65.047  1.00 105.27 ? 722  SER A C     1 
ATOM   4917 O  O     . SER A 1 722  ? 123.791 99.516  66.069  1.00 105.27 ? 722  SER A O     1 
ATOM   4918 C  CB    . SER A 1 722  ? 124.920 100.319 63.678  1.00 105.27 ? 722  SER A CB    1 
ATOM   4919 O  OG    . SER A 1 722  ? 125.770 100.246 62.546  1.00 105.27 ? 722  SER A OG    1 
ATOM   4920 N  N     . MET A 1 723  ? 121.942 98.695  65.072  1.00 100.42 ? 723  MET A N     1 
ATOM   4921 C  CA    . MET A 1 723  ? 121.230 98.594  66.338  1.00 100.42 ? 723  MET A CA    1 
ATOM   4922 C  C     . MET A 1 723  ? 121.877 97.584  67.275  1.00 100.42 ? 723  MET A C     1 
ATOM   4923 O  O     . MET A 1 723  ? 121.754 97.730  68.493  1.00 100.42 ? 723  MET A O     1 
ATOM   4924 C  CB    . MET A 1 723  ? 119.760 98.252  66.089  1.00 100.42 ? 723  MET A CB    1 
ATOM   4925 C  CG    . MET A 1 723  ? 119.520 96.871  65.520  1.00 100.42 ? 723  MET A CG    1 
ATOM   4926 S  SD    . MET A 1 723  ? 117.787 96.593  65.102  1.00 100.42 ? 723  MET A SD    1 
ATOM   4927 C  CE    . MET A 1 723  ? 116.971 97.300  66.530  1.00 100.42 ? 723  MET A CE    1 
ATOM   4928 N  N     . GLU A 1 724  ? 122.579 96.580  66.742  1.00 99.19  ? 724  GLU A N     1 
ATOM   4929 C  CA    . GLU A 1 724  ? 123.403 95.723  67.590  1.00 99.19  ? 724  GLU A CA    1 
ATOM   4930 C  C     . GLU A 1 724  ? 124.417 96.545  68.374  1.00 99.19  ? 724  GLU A C     1 
ATOM   4931 O  O     . GLU A 1 724  ? 124.541 96.402  69.598  1.00 99.19  ? 724  GLU A O     1 
ATOM   4932 C  CB    . GLU A 1 724  ? 124.116 94.670  66.739  1.00 99.19  ? 724  GLU A CB    1 
ATOM   4933 C  CG    . GLU A 1 724  ? 123.193 93.791  65.925  1.00 99.19  ? 724  GLU A CG    1 
ATOM   4934 C  CD    . GLU A 1 724  ? 122.400 92.843  66.799  1.00 99.19  ? 724  GLU A CD    1 
ATOM   4935 O  OE1   . GLU A 1 724  ? 121.185 93.055  66.961  1.00 99.19  ? 724  GLU A OE1   1 
ATOM   4936 O  OE2   . GLU A 1 724  ? 122.997 91.880  67.324  1.00 99.19  ? 724  GLU A OE2   1 
ATOM   4937 N  N     . ARG A 1 725  ? 125.153 97.415  67.678  1.00 95.98  ? 725  ARG A N     1 
ATOM   4938 C  CA    . ARG A 1 725  ? 126.140 98.255  68.344  1.00 95.98  ? 725  ARG A CA    1 
ATOM   4939 C  C     . ARG A 1 725  ? 125.477 99.180  69.354  1.00 95.98  ? 725  ARG A C     1 
ATOM   4940 O  O     . ARG A 1 725  ? 125.969 99.343  70.479  1.00 95.98  ? 725  ARG A O     1 
ATOM   4941 C  CB    . ARG A 1 725  ? 126.923 99.060  67.307  1.00 95.98  ? 725  ARG A CB    1 
ATOM   4942 C  CG    . ARG A 1 725  ? 128.111 99.816  67.870  1.00 95.98  ? 725  ARG A CG    1 
ATOM   4943 C  CD    . ARG A 1 725  ? 128.788 100.647 66.793  1.00 95.98  ? 725  ARG A CD    1 
ATOM   4944 N  NE    . ARG A 1 725  ? 129.211 99.830  65.659  1.00 95.98  ? 725  ARG A NE    1 
ATOM   4945 C  CZ    . ARG A 1 725  ? 130.328 99.110  65.631  1.00 95.98  ? 725  ARG A CZ    1 
ATOM   4946 N  NH1   . ARG A 1 725  ? 131.141 99.100  66.678  1.00 95.98  ? 725  ARG A NH1   1 
ATOM   4947 N  NH2   . ARG A 1 725  ? 130.631 98.396  64.556  1.00 95.98  ? 725  ARG A NH2   1 
ATOM   4948 N  N     . LYS A 1 726  ? 124.350 99.783  68.972  1.00 92.59  ? 726  LYS A N     1 
ATOM   4949 C  CA    . LYS A 1 726  ? 123.646 100.678 69.888  1.00 92.59  ? 726  LYS A CA    1 
ATOM   4950 C  C     . LYS A 1 726  ? 123.244 99.948  71.166  1.00 92.59  ? 726  LYS A C     1 
ATOM   4951 O  O     . LYS A 1 726  ? 123.516 100.418 72.278  1.00 92.59  ? 726  LYS A O     1 
ATOM   4952 C  CB    . LYS A 1 726  ? 122.417 101.280 69.205  1.00 92.59  ? 726  LYS A CB    1 
ATOM   4953 C  CG    . LYS A 1 726  ? 122.668 101.816 67.808  1.00 92.59  ? 726  LYS A CG    1 
ATOM   4954 C  CD    . LYS A 1 726  ? 123.141 103.259 67.838  1.00 92.59  ? 726  LYS A CD    1 
ATOM   4955 C  CE    . LYS A 1 726  ? 124.025 103.571 66.641  1.00 92.59  ? 726  LYS A CE    1 
ATOM   4956 N  NZ    . LYS A 1 726  ? 124.743 104.865 66.798  1.00 92.59  ? 726  LYS A NZ    1 
ATOM   4957 N  N     . THR A 1 727  ? 122.605 98.784  71.023  1.00 92.83  ? 727  THR A N     1 
ATOM   4958 C  CA    . THR A 1 727  ? 122.130 98.044  72.185  1.00 92.83  ? 727  THR A CA    1 
ATOM   4959 C  C     . THR A 1 727  ? 123.280 97.555  73.056  1.00 92.83  ? 727  THR A C     1 
ATOM   4960 O  O     . THR A 1 727  ? 123.181 97.593  74.286  1.00 92.83  ? 727  THR A O     1 
ATOM   4961 C  CB    . THR A 1 727  ? 121.250 96.871  71.748  1.00 92.83  ? 727  THR A CB    1 
ATOM   4962 O  OG1   . THR A 1 727  ? 122.003 95.986  70.909  1.00 92.83  ? 727  THR A OG1   1 
ATOM   4963 C  CG2   . THR A 1 727  ? 120.010 97.365  71.014  1.00 92.83  ? 727  THR A CG2   1 
ATOM   4964 N  N     . LYS A 1 728  ? 124.374 97.079  72.452  1.00 90.96  ? 728  LYS A N     1 
ATOM   4965 C  CA    . LYS A 1 728  ? 125.477 96.602  73.282  1.00 90.96  ? 728  LYS A CA    1 
ATOM   4966 C  C     . LYS A 1 728  ? 126.148 97.755  74.022  1.00 90.96  ? 728  LYS A C     1 
ATOM   4967 O  O     . LYS A 1 728  ? 126.504 97.619  75.202  1.00 90.96  ? 728  LYS A O     1 
ATOM   4968 C  CB    . LYS A 1 728  ? 126.485 95.807  72.447  1.00 90.96  ? 728  LYS A CB    1 
ATOM   4969 C  CG    . LYS A 1 728  ? 127.255 96.588  71.404  1.00 90.96  ? 728  LYS A CG    1 
ATOM   4970 C  CD    . LYS A 1 728  ? 127.644 95.686  70.241  1.00 90.96  ? 728  LYS A CD    1 
ATOM   4971 C  CE    . LYS A 1 728  ? 128.861 94.840  70.569  1.00 90.96  ? 728  LYS A CE    1 
ATOM   4972 N  NZ    . LYS A 1 728  ? 129.099 93.800  69.531  1.00 90.96  ? 728  LYS A NZ    1 
ATOM   4973 N  N     . GLU A 1 729  ? 126.292 98.912  73.370  1.00 90.80  ? 729  GLU A N     1 
ATOM   4974 C  CA    . GLU A 1 729  ? 126.831 100.072 74.072  1.00 90.80  ? 729  GLU A CA    1 
ATOM   4975 C  C     . GLU A 1 729  ? 125.921 100.484 75.223  1.00 90.80  ? 729  GLU A C     1 
ATOM   4976 O  O     . GLU A 1 729  ? 126.397 100.798 76.322  1.00 90.80  ? 729  GLU A O     1 
ATOM   4977 C  CB    . GLU A 1 729  ? 127.030 101.233 73.097  1.00 90.80  ? 729  GLU A CB    1 
ATOM   4978 C  CG    . GLU A 1 729  ? 128.151 101.016 72.090  1.00 90.80  ? 729  GLU A CG    1 
ATOM   4979 C  CD    . GLU A 1 729  ? 129.517 100.915 72.741  1.00 90.80  ? 729  GLU A CD    1 
ATOM   4980 O  OE1   . GLU A 1 729  ? 129.744 101.598 73.762  1.00 90.80  ? 729  GLU A OE1   1 
ATOM   4981 O  OE2   . GLU A 1 729  ? 130.364 100.152 72.230  1.00 90.80  ? 729  GLU A OE2   1 
ATOM   4982 N  N     . TYR A 1 730  ? 124.605 100.459 75.004  1.00 86.20  ? 730  TYR A N     1 
ATOM   4983 C  CA    . TYR A 1 730  ? 123.692 100.898 76.055  1.00 86.20  ? 730  TYR A CA    1 
ATOM   4984 C  C     . TYR A 1 730  ? 123.608 99.894  77.202  1.00 86.20  ? 730  TYR A C     1 
ATOM   4985 O  O     . TYR A 1 730  ? 123.433 100.297 78.357  1.00 86.20  ? 730  TYR A O     1 
ATOM   4986 C  CB    . TYR A 1 730  ? 122.312 101.180 75.463  1.00 86.20  ? 730  TYR A CB    1 
ATOM   4987 C  CG    . TYR A 1 730  ? 122.193 102.578 74.892  1.00 86.20  ? 730  TYR A CG    1 
ATOM   4988 C  CD1   . TYR A 1 730  ? 122.215 103.691 75.722  1.00 86.20  ? 730  TYR A CD1   1 
ATOM   4989 C  CD2   . TYR A 1 730  ? 122.073 102.785 73.524  1.00 86.20  ? 730  TYR A CD2   1 
ATOM   4990 C  CE1   . TYR A 1 730  ? 122.112 104.969 75.208  1.00 86.20  ? 730  TYR A CE1   1 
ATOM   4991 C  CE2   . TYR A 1 730  ? 121.967 104.060 73.001  1.00 86.20  ? 730  TYR A CE2   1 
ATOM   4992 C  CZ    . TYR A 1 730  ? 121.989 105.148 73.847  1.00 86.20  ? 730  TYR A CZ    1 
ATOM   4993 O  OH    . TYR A 1 730  ? 121.886 106.419 73.332  1.00 86.20  ? 730  TYR A OH    1 
ATOM   4994 N  N     . VAL A 1 731  ? 123.737 98.594  76.925  1.00 77.99  ? 731  VAL A N     1 
ATOM   4995 C  CA    . VAL A 1 731  ? 123.766 97.642  78.034  1.00 77.99  ? 731  VAL A CA    1 
ATOM   4996 C  C     . VAL A 1 731  ? 125.078 97.758  78.802  1.00 77.99  ? 731  VAL A C     1 
ATOM   4997 O  O     . VAL A 1 731  ? 125.107 97.558  80.024  1.00 77.99  ? 731  VAL A O     1 
ATOM   4998 C  CB    . VAL A 1 731  ? 123.504 96.199  77.557  1.00 77.99  ? 731  VAL A CB    1 
ATOM   4999 C  CG1   . VAL A 1 731  ? 122.162 96.106  76.845  1.00 77.99  ? 731  VAL A CG1   1 
ATOM   5000 C  CG2   . VAL A 1 731  ? 124.625 95.688  76.678  1.00 77.99  ? 731  VAL A CG2   1 
ATOM   5001 N  N     . PHE A 1 732  ? 126.178 98.096  78.120  1.00 75.56  ? 732  PHE A N     1 
ATOM   5002 C  CA    . PHE A 1 732  ? 127.398 98.429  78.851  1.00 75.56  ? 732  PHE A CA    1 
ATOM   5003 C  C     . PHE A 1 732  ? 127.176 99.638  79.750  1.00 75.56  ? 732  PHE A C     1 
ATOM   5004 O  O     . PHE A 1 732  ? 127.649 99.673  80.896  1.00 75.56  ? 732  PHE A O     1 
ATOM   5005 C  CB    . PHE A 1 732  ? 128.546 98.685  77.876  1.00 75.56  ? 732  PHE A CB    1 
ATOM   5006 C  CG    . PHE A 1 732  ? 129.193 97.433  77.361  1.00 75.56  ? 732  PHE A CG    1 
ATOM   5007 C  CD1   . PHE A 1 732  ? 128.981 96.219  77.992  1.00 75.56  ? 732  PHE A CD1   1 
ATOM   5008 C  CD2   . PHE A 1 732  ? 130.020 97.470  76.252  1.00 75.56  ? 732  PHE A CD2   1 
ATOM   5009 C  CE1   . PHE A 1 732  ? 129.577 95.064  77.525  1.00 75.56  ? 732  PHE A CE1   1 
ATOM   5010 C  CE2   . PHE A 1 732  ? 130.619 96.318  75.779  1.00 75.56  ? 732  PHE A CE2   1 
ATOM   5011 C  CZ    . PHE A 1 732  ? 130.397 95.114  76.417  1.00 75.56  ? 732  PHE A CZ    1 
ATOM   5012 N  N     . ILE A 1 733  ? 126.452 100.639 79.243  1.00 75.16  ? 733  ILE A N     1 
ATOM   5013 C  CA    . ILE A 1 733  ? 126.103 101.801 80.057  1.00 75.16  ? 733  ILE A CA    1 
ATOM   5014 C  C     . ILE A 1 733  ? 125.298 101.373 81.279  1.00 75.16  ? 733  ILE A C     1 
ATOM   5015 O  O     . ILE A 1 733  ? 125.515 101.871 82.389  1.00 75.16  ? 733  ILE A O     1 
ATOM   5016 C  CB    . ILE A 1 733  ? 125.338 102.835 79.210  1.00 75.16  ? 733  ILE A CB    1 
ATOM   5017 C  CG1   . ILE A 1 733  ? 126.222 103.360 78.078  1.00 75.16  ? 733  ILE A CG1   1 
ATOM   5018 C  CG2   . ILE A 1 733  ? 124.855 103.987 80.078  1.00 75.16  ? 733  ILE A CG2   1 
ATOM   5019 C  CD1   . ILE A 1 733  ? 125.477 104.179 77.048  1.00 75.16  ? 733  ILE A CD1   1 
ATOM   5020 N  N     . TYR A 1 734  ? 124.353 100.449 81.091  1.00 68.84  ? 734  TYR A N     1 
ATOM   5021 C  CA    . TYR A 1 734  ? 123.542 99.968  82.207  1.00 68.84  ? 734  TYR A CA    1 
ATOM   5022 C  C     . TYR A 1 734  ? 124.388 99.263  83.260  1.00 68.84  ? 734  TYR A C     1 
ATOM   5023 O  O     . TYR A 1 734  ? 124.184 99.460  84.462  1.00 68.84  ? 734  TYR A O     1 
ATOM   5024 C  CB    . TYR A 1 734  ? 122.449 99.030  81.702  1.00 68.84  ? 734  TYR A CB    1 
ATOM   5025 C  CG    . TYR A 1 734  ? 121.121 99.707  81.500  1.00 68.84  ? 734  TYR A CG    1 
ATOM   5026 C  CD1   . TYR A 1 734  ? 120.471 100.326 82.558  1.00 68.84  ? 734  TYR A CD1   1 
ATOM   5027 C  CD2   . TYR A 1 734  ? 120.515 99.730  80.256  1.00 68.84  ? 734  TYR A CD2   1 
ATOM   5028 C  CE1   . TYR A 1 734  ? 119.253 100.946 82.382  1.00 68.84  ? 734  TYR A CE1   1 
ATOM   5029 C  CE2   . TYR A 1 734  ? 119.304 100.350 80.072  1.00 68.84  ? 734  TYR A CE2   1 
ATOM   5030 C  CZ    . TYR A 1 734  ? 118.673 100.955 81.136  1.00 68.84  ? 734  TYR A CZ    1 
ATOM   5031 O  OH    . TYR A 1 734  ? 117.459 101.574 80.952  1.00 68.84  ? 734  TYR A OH    1 
ATOM   5032 N  N     . ILE A 1 735  ? 125.327 98.420  82.828  1.00 66.39  ? 735  ILE A N     1 
ATOM   5033 C  CA    . ILE A 1 735  ? 126.186 97.717  83.781  1.00 66.39  ? 735  ILE A CA    1 
ATOM   5034 C  C     . ILE A 1 735  ? 127.021 98.716  84.574  1.00 66.39  ? 735  ILE A C     1 
ATOM   5035 O  O     . ILE A 1 735  ? 127.136 98.631  85.811  1.00 66.39  ? 735  ILE A O     1 
ATOM   5036 C  CB    . ILE A 1 735  ? 127.075 96.698  83.047  1.00 66.39  ? 735  ILE A CB    1 
ATOM   5037 C  CG1   . ILE A 1 735  ? 126.214 95.683  82.294  1.00 66.39  ? 735  ILE A CG1   1 
ATOM   5038 C  CG2   . ILE A 1 735  ? 128.009 96.002  84.023  1.00 66.39  ? 735  ILE A CG2   1 
ATOM   5039 C  CD1   . ILE A 1 735  ? 125.310 94.875  83.187  1.00 66.39  ? 735  ILE A CD1   1 
ATOM   5040 N  N     . GLY A 1 736  ? 127.619 99.679  83.868  1.00 66.17  ? 736  GLY A N     1 
ATOM   5041 C  CA    . GLY A 1 736  ? 128.388 100.707 84.547  1.00 66.17  ? 736  GLY A CA    1 
ATOM   5042 C  C     . GLY A 1 736  ? 127.550 101.495 85.534  1.00 66.17  ? 736  GLY A C     1 
ATOM   5043 O  O     . GLY A 1 736  ? 127.991 101.775 86.649  1.00 66.17  ? 736  GLY A O     1 
ATOM   5044 N  N     . ALA A 1 737  ? 126.321 101.842 85.143  1.00 63.01  ? 737  ALA A N     1 
ATOM   5045 C  CA    . ALA A 1 737  ? 125.433 102.585 86.029  1.00 63.01  ? 737  ALA A CA    1 
ATOM   5046 C  C     . ALA A 1 737  ? 125.058 101.765 87.255  1.00 63.01  ? 737  ALA A C     1 
ATOM   5047 O  O     . ALA A 1 737  ? 124.921 102.310 88.353  1.00 63.01  ? 737  ALA A O     1 
ATOM   5048 C  CB    . ALA A 1 737  ? 124.179 103.017 85.270  1.00 63.01  ? 737  ALA A CB    1 
ATOM   5049 N  N     . GLY A 1 738  ? 124.861 100.458 87.085  1.00 57.31  ? 738  GLY A N     1 
ATOM   5050 C  CA    . GLY A 1 738  ? 124.539 99.621  88.231  1.00 57.31  ? 738  GLY A CA    1 
ATOM   5051 C  C     . GLY A 1 738  ? 125.663 99.577  89.248  1.00 57.31  ? 738  GLY A C     1 
ATOM   5052 O  O     . GLY A 1 738  ? 125.446 99.791  90.448  1.00 57.31  ? 738  GLY A O     1 
ATOM   5053 N  N     . LEU A 1 739  ? 126.889 99.330  88.779  1.00 58.30  ? 739  LEU A N     1 
ATOM   5054 C  CA    . LEU A 1 739  ? 128.025 99.337  89.701  1.00 58.30  ? 739  LEU A CA    1 
ATOM   5055 C  C     . LEU A 1 739  ? 128.200 100.716 90.338  1.00 58.30  ? 739  LEU A C     1 
ATOM   5056 O  O     . LEU A 1 739  ? 128.481 100.837 91.542  1.00 58.30  ? 739  LEU A O     1 
ATOM   5057 C  CB    . LEU A 1 739  ? 129.298 98.921  88.966  1.00 58.30  ? 739  LEU A CB    1 
ATOM   5058 C  CG    . LEU A 1 739  ? 129.248 97.585  88.224  1.00 58.30  ? 739  LEU A CG    1 
ATOM   5059 C  CD1   . LEU A 1 739  ? 130.559 97.341  87.514  1.00 58.30  ? 739  LEU A CD1   1 
ATOM   5060 C  CD2   . LEU A 1 739  ? 128.938 96.440  89.146  1.00 58.30  ? 739  LEU A CD2   1 
ATOM   5061 N  N     . TYR A 1 740  ? 128.021 101.765 89.535  1.00 59.91  ? 740  TYR A N     1 
ATOM   5062 C  CA    . TYR A 1 740  ? 128.127 103.139 90.004  1.00 59.91  ? 740  TYR A CA    1 
ATOM   5063 C  C     . TYR A 1 740  ? 127.120 103.425 91.110  1.00 59.91  ? 740  TYR A C     1 
ATOM   5064 O  O     . TYR A 1 740  ? 127.457 104.042 92.128  1.00 59.91  ? 740  TYR A O     1 
ATOM   5065 C  CB    . TYR A 1 740  ? 127.907 104.049 88.798  1.00 59.91  ? 740  TYR A CB    1 
ATOM   5066 C  CG    . TYR A 1 740  ? 128.013 105.520 89.049  1.00 59.91  ? 740  TYR A CG    1 
ATOM   5067 C  CD1   . TYR A 1 740  ? 129.249 106.122 89.211  1.00 59.91  ? 740  TYR A CD1   1 
ATOM   5068 C  CD2   . TYR A 1 740  ? 126.878 106.317 89.091  1.00 59.91  ? 740  TYR A CD2   1 
ATOM   5069 C  CE1   . TYR A 1 740  ? 129.353 107.469 89.427  1.00 59.91  ? 740  TYR A CE1   1 
ATOM   5070 C  CE2   . TYR A 1 740  ? 126.973 107.669 89.310  1.00 59.91  ? 740  TYR A CE2   1 
ATOM   5071 C  CZ    . TYR A 1 740  ? 128.211 108.239 89.475  1.00 59.91  ? 740  TYR A CZ    1 
ATOM   5072 O  OH    . TYR A 1 740  ? 128.291 109.591 89.685  1.00 59.91  ? 740  TYR A OH    1 
ATOM   5073 N  N     . ALA A 1 741  ? 125.881 102.965 90.934  1.00 54.70  ? 741  ALA A N     1 
ATOM   5074 C  CA    . ALA A 1 741  ? 124.852 103.174 91.943  1.00 54.70  ? 741  ALA A CA    1 
ATOM   5075 C  C     . ALA A 1 741  ? 125.171 102.409 93.218  1.00 54.70  ? 741  ALA A C     1 
ATOM   5076 O  O     . ALA A 1 741  ? 124.945 102.915 94.324  1.00 54.70  ? 741  ALA A O     1 
ATOM   5077 C  CB    . ALA A 1 741  ? 123.487 102.767 91.392  1.00 54.70  ? 741  ALA A CB    1 
ATOM   5078 N  N     . VAL A 1 742  ? 125.698 101.188 93.084  1.00 50.02  ? 742  VAL A N     1 
ATOM   5079 C  CA    . VAL A 1 742  ? 126.114 100.438 94.267  1.00 50.02  ? 742  VAL A CA    1 
ATOM   5080 C  C     . VAL A 1 742  ? 127.117 101.250 95.073  1.00 50.02  ? 742  VAL A C     1 
ATOM   5081 O  O     . VAL A 1 742  ? 126.947 101.470 96.284  1.00 50.02  ? 742  VAL A O     1 
ATOM   5082 C  CB    . VAL A 1 742  ? 126.705 99.075  93.863  1.00 50.02  ? 742  VAL A CB    1 
ATOM   5083 C  CG1   . VAL A 1 742  ? 127.248 98.347  95.087  1.00 50.02  ? 742  VAL A CG1   1 
ATOM   5084 C  CG2   . VAL A 1 742  ? 125.668 98.229  93.160  1.00 50.02  ? 742  VAL A CG2   1 
ATOM   5085 N  N     . GLY A 1 743  ? 128.157 101.745 94.399  1.00 50.82  ? 743  GLY A N     1 
ATOM   5086 C  CA    . GLY A 1 743  ? 129.174 102.513 95.100  1.00 50.82  ? 743  GLY A CA    1 
ATOM   5087 C  C     . GLY A 1 743  ? 128.617 103.768 95.745  1.00 50.82  ? 743  GLY A C     1 
ATOM   5088 O  O     . GLY A 1 743  ? 128.886 104.057 96.919  1.00 50.82  ? 743  GLY A O     1 
ATOM   5089 N  N     . ALA A 1 744  ? 127.818 104.527 94.989  1.00 48.27  ? 744  ALA A N     1 
ATOM   5090 C  CA    . ALA A 1 744  ? 127.307 105.796 95.497  1.00 48.27  ? 744  ALA A CA    1 
ATOM   5091 C  C     . ALA A 1 744  ? 126.388 105.589 96.694  1.00 48.27  ? 744  ALA A C     1 
ATOM   5092 O  O     . ALA A 1 744  ? 126.501 106.300 97.701  1.00 48.27  ? 744  ALA A O     1 
ATOM   5093 C  CB    . ALA A 1 744  ? 126.582 106.553 94.385  1.00 48.27  ? 744  ALA A CB    1 
ATOM   5094 N  N     . TYR A 1 745  ? 125.470 104.621 96.605  1.00 46.32  ? 745  TYR A N     1 
ATOM   5095 C  CA    . TYR A 1 745  ? 124.553 104.371 97.711  1.00 46.32  ? 745  TYR A CA    1 
ATOM   5096 C  C     . TYR A 1 745  ? 125.301 103.913 98.953  1.00 46.32  ? 745  TYR A C     1 
ATOM   5097 O  O     . TYR A 1 745  ? 125.010 104.376 100.066 1.00 46.32  ? 745  TYR A O     1 
ATOM   5098 C  CB    . TYR A 1 745  ? 123.505 103.336 97.305  1.00 46.32  ? 745  TYR A CB    1 
ATOM   5099 C  CG    . TYR A 1 745  ? 122.248 103.944 96.729  1.00 46.32  ? 745  TYR A CG    1 
ATOM   5100 C  CD1   . TYR A 1 745  ? 121.307 104.548 97.549  1.00 46.32  ? 745  TYR A CD1   1 
ATOM   5101 C  CD2   . TYR A 1 745  ? 122.006 103.916 95.364  1.00 46.32  ? 745  TYR A CD2   1 
ATOM   5102 C  CE1   . TYR A 1 745  ? 120.158 105.107 97.025  1.00 46.32  ? 745  TYR A CE1   1 
ATOM   5103 C  CE2   . TYR A 1 745  ? 120.861 104.472 94.831  1.00 46.32  ? 745  TYR A CE2   1 
ATOM   5104 C  CZ    . TYR A 1 745  ? 119.941 105.066 95.665  1.00 46.32  ? 745  TYR A CZ    1 
ATOM   5105 O  OH    . TYR A 1 745  ? 118.800 105.620 95.136  1.00 46.32  ? 745  TYR A OH    1 
ATOM   5106 N  N     . LEU A 1 746  ? 126.274 103.010 98.788  1.00 43.25  ? 746  LEU A N     1 
ATOM   5107 C  CA    . LEU A 1 746  ? 127.042 102.557 99.943  1.00 43.25  ? 746  LEU A CA    1 
ATOM   5108 C  C     . LEU A 1 746  ? 127.746 103.726 100.619 1.00 43.25  ? 746  LEU A C     1 
ATOM   5109 O  O     . LEU A 1 746  ? 127.656 103.897 101.844 1.00 43.25  ? 746  LEU A O     1 
ATOM   5110 C  CB    . LEU A 1 746  ? 128.050 101.490 99.516  1.00 43.25  ? 746  LEU A CB    1 
ATOM   5111 C  CG    . LEU A 1 746  ? 129.020 101.004 100.593 1.00 43.25  ? 746  LEU A CG    1 
ATOM   5112 C  CD1   . LEU A 1 746  ? 128.261 100.519 101.812 1.00 43.25  ? 746  LEU A CD1   1 
ATOM   5113 C  CD2   . LEU A 1 746  ? 129.912 99.904  100.047 1.00 43.25  ? 746  LEU A CD2   1 
ATOM   5114 N  N     . ILE A 1 747  ? 128.428 104.561 99.829  1.00 45.28  ? 747  ILE A N     1 
ATOM   5115 C  CA    . ILE A 1 747  ? 129.172 105.684 100.398 1.00 45.28  ? 747  ILE A CA    1 
ATOM   5116 C  C     . ILE A 1 747  ? 128.230 106.630 101.136 1.00 45.28  ? 747  ILE A C     1 
ATOM   5117 O  O     . ILE A 1 747  ? 128.464 106.992 102.300 1.00 45.28  ? 747  ILE A O     1 
ATOM   5118 C  CB    . ILE A 1 747  ? 129.954 106.416 99.292  1.00 45.28  ? 747  ILE A CB    1 
ATOM   5119 C  CG1   . ILE A 1 747  ? 131.222 105.640 98.933  1.00 45.28  ? 747  ILE A CG1   1 
ATOM   5120 C  CG2   . ILE A 1 747  ? 130.287 107.837 99.712  1.00 45.28  ? 747  ILE A CG2   1 
ATOM   5121 C  CD1   . ILE A 1 747  ? 131.846 106.066 97.624  1.00 45.28  ? 747  ILE A CD1   1 
ATOM   5122 N  N     . GLN A 1 748  ? 127.141 107.026 100.472 1.00 45.92  ? 748  GLN A N     1 
ATOM   5123 C  CA    . GLN A 1 748  ? 126.205 107.980 101.059 1.00 45.92  ? 748  GLN A CA    1 
ATOM   5124 C  C     . GLN A 1 748  ? 125.638 107.465 102.374 1.00 45.92  ? 748  GLN A C     1 
ATOM   5125 O  O     . GLN A 1 748  ? 125.679 108.161 103.400 1.00 45.92  ? 748  GLN A O     1 
ATOM   5126 C  CB    . GLN A 1 748  ? 125.081 108.262 100.063 1.00 45.92  ? 748  GLN A CB    1 
ATOM   5127 C  CG    . GLN A 1 748  ? 123.765 108.672 100.694 1.00 45.92  ? 748  GLN A CG    1 
ATOM   5128 C  CD    . GLN A 1 748  ? 122.635 108.701 99.688  1.00 45.92  ? 748  GLN A CD    1 
ATOM   5129 O  OE1   . GLN A 1 748  ? 122.198 107.658 99.205  1.00 45.92  ? 748  GLN A OE1   1 
ATOM   5130 N  NE2   . GLN A 1 748  ? 122.139 109.891 99.383  1.00 45.92  ? 748  GLN A NE2   1 
ATOM   5131 N  N     . HIS A 1 749  ? 125.101 106.241 102.365 1.00 42.13  ? 749  HIS A N     1 
ATOM   5132 C  CA    . HIS A 1 749  ? 124.445 105.732 103.561 1.00 42.13  ? 749  HIS A CA    1 
ATOM   5133 C  C     . HIS A 1 749  ? 125.437 105.539 104.699 1.00 42.13  ? 749  HIS A C     1 
ATOM   5134 O  O     . HIS A 1 749  ? 125.143 105.900 105.845 1.00 42.13  ? 749  HIS A O     1 
ATOM   5135 C  CB    . HIS A 1 749  ? 123.708 104.433 103.243 1.00 42.13  ? 749  HIS A CB    1 
ATOM   5136 C  CG    . HIS A 1 749  ? 122.364 104.646 102.621 1.00 42.13  ? 749  HIS A CG    1 
ATOM   5137 N  ND1   . HIS A 1 749  ? 121.443 105.537 103.129 1.00 42.13  ? 749  HIS A ND1   1 
ATOM   5138 C  CD2   . HIS A 1 749  ? 121.787 104.092 101.529 1.00 42.13  ? 749  HIS A CD2   1 
ATOM   5139 C  CE1   . HIS A 1 749  ? 120.356 105.519 102.379 1.00 42.13  ? 749  HIS A CE1   1 
ATOM   5140 N  NE2   . HIS A 1 749  ? 120.539 104.651 101.401 1.00 42.13  ? 749  HIS A NE2   1 
ATOM   5141 N  N     . TYR A 1 750  ? 126.626 105.000 104.409 1.00 42.79  ? 750  TYR A N     1 
ATOM   5142 C  CA    . TYR A 1 750  ? 127.601 104.789 105.474 1.00 42.79  ? 750  TYR A CA    1 
ATOM   5143 C  C     . TYR A 1 750  ? 128.018 106.109 106.113 1.00 42.79  ? 750  TYR A C     1 
ATOM   5144 O  O     . TYR A 1 750  ? 128.073 106.224 107.349 1.00 42.79  ? 750  TYR A O     1 
ATOM   5145 C  CB    . TYR A 1 750  ? 128.817 104.042 104.926 1.00 42.79  ? 750  TYR A CB    1 
ATOM   5146 C  CG    . TYR A 1 750  ? 129.919 103.824 105.938 1.00 42.79  ? 750  TYR A CG    1 
ATOM   5147 C  CD1   . TYR A 1 750  ? 129.633 103.380 107.220 1.00 42.79  ? 750  TYR A CD1   1 
ATOM   5148 C  CD2   . TYR A 1 750  ? 131.247 104.051 105.606 1.00 42.79  ? 750  TYR A CD2   1 
ATOM   5149 C  CE1   . TYR A 1 750  ? 130.636 103.177 108.147 1.00 42.79  ? 750  TYR A CE1   1 
ATOM   5150 C  CE2   . TYR A 1 750  ? 132.257 103.850 106.526 1.00 42.79  ? 750  TYR A CE2   1 
ATOM   5151 C  CZ    . TYR A 1 750  ? 131.946 103.413 107.794 1.00 42.79  ? 750  TYR A CZ    1 
ATOM   5152 O  OH    . TYR A 1 750  ? 132.948 103.211 108.715 1.00 42.79  ? 750  TYR A OH    1 
ATOM   5153 N  N     . PHE A 1 751  ? 128.288 107.130 105.294 1.00 44.25  ? 751  PHE A N     1 
ATOM   5154 C  CA    . PHE A 1 751  ? 128.808 108.366 105.868 1.00 44.25  ? 751  PHE A CA    1 
ATOM   5155 C  C     . PHE A 1 751  ? 127.723 109.148 106.602 1.00 44.25  ? 751  PHE A C     1 
ATOM   5156 O  O     . PHE A 1 751  ? 127.992 109.749 107.652 1.00 44.25  ? 751  PHE A O     1 
ATOM   5157 C  CB    . PHE A 1 751  ? 129.480 109.206 104.785 1.00 44.25  ? 751  PHE A CB    1 
ATOM   5158 C  CG    . PHE A 1 751  ? 130.825 108.678 104.376 1.00 44.25  ? 751  PHE A CG    1 
ATOM   5159 C  CD1   . PHE A 1 751  ? 131.824 108.503 105.317 1.00 44.25  ? 751  PHE A CD1   1 
ATOM   5160 C  CD2   . PHE A 1 751  ? 131.092 108.349 103.061 1.00 44.25  ? 751  PHE A CD2   1 
ATOM   5161 C  CE1   . PHE A 1 751  ? 133.062 108.012 104.953 1.00 44.25  ? 751  PHE A CE1   1 
ATOM   5162 C  CE2   . PHE A 1 751  ? 132.329 107.857 102.690 1.00 44.25  ? 751  PHE A CE2   1 
ATOM   5163 C  CZ    . PHE A 1 751  ? 133.315 107.690 103.637 1.00 44.25  ? 751  PHE A CZ    1 
ATOM   5164 N  N     . PHE A 1 752  ? 126.486 109.138 106.098 1.00 44.55  ? 752  PHE A N     1 
ATOM   5165 C  CA    . PHE A 1 752  ? 125.416 109.747 106.883 1.00 44.55  ? 752  PHE A CA    1 
ATOM   5166 C  C     . PHE A 1 752  ? 125.166 108.992 108.182 1.00 44.55  ? 752  PHE A C     1 
ATOM   5167 O  O     . PHE A 1 752  ? 124.894 109.612 109.217 1.00 44.55  ? 752  PHE A O     1 
ATOM   5168 C  CB    . PHE A 1 752  ? 124.137 109.890 106.064 1.00 44.55  ? 752  PHE A CB    1 
ATOM   5169 C  CG    . PHE A 1 752  ? 124.236 110.909 104.971 1.00 44.55  ? 752  PHE A CG    1 
ATOM   5170 C  CD1   . PHE A 1 752  ? 125.273 111.828 104.957 1.00 44.55  ? 752  PHE A CD1   1 
ATOM   5171 C  CD2   . PHE A 1 752  ? 123.275 110.982 103.988 1.00 44.55  ? 752  PHE A CD2   1 
ATOM   5172 C  CE1   . PHE A 1 752  ? 125.356 112.781 103.965 1.00 44.55  ? 752  PHE A CE1   1 
ATOM   5173 C  CE2   . PHE A 1 752  ? 123.349 111.931 102.999 1.00 44.55  ? 752  PHE A CE2   1 
ATOM   5174 C  CZ    . PHE A 1 752  ? 124.394 112.832 102.985 1.00 44.55  ? 752  PHE A CZ    1 
ATOM   5175 N  N     . SER A 1 753  ? 125.272 107.661 108.165 1.00 38.90  ? 753  SER A N     1 
ATOM   5176 C  CA    . SER A 1 753  ? 125.130 106.912 109.408 1.00 38.90  ? 753  SER A CA    1 
ATOM   5177 C  C     . SER A 1 753  ? 126.158 107.368 110.434 1.00 38.90  ? 753  SER A C     1 
ATOM   5178 O  O     . SER A 1 753  ? 125.813 107.672 111.585 1.00 38.90  ? 753  SER A O     1 
ATOM   5179 C  CB    . SER A 1 753  ? 125.267 105.414 109.142 1.00 38.90  ? 753  SER A CB    1 
ATOM   5180 O  OG    . SER A 1 753  ? 126.624 105.055 108.952 1.00 38.90  ? 753  SER A OG    1 
ATOM   5181 N  N     . ILE A 1 754  ? 127.429 107.446 110.028 1.00 40.95  ? 754  ILE A N     1 
ATOM   5182 C  CA    . ILE A 1 754  ? 128.463 107.789 111.002 1.00 40.95  ? 754  ILE A CA    1 
ATOM   5183 C  C     . ILE A 1 754  ? 128.285 109.219 111.509 1.00 40.95  ? 754  ILE A C     1 
ATOM   5184 O  O     . ILE A 1 754  ? 128.409 109.478 112.717 1.00 40.95  ? 754  ILE A O     1 
ATOM   5185 C  CB    . ILE A 1 754  ? 129.875 107.542 110.433 1.00 40.95  ? 754  ILE A CB    1 
ATOM   5186 C  CG1   . ILE A 1 754  ? 130.938 107.906 111.468 1.00 40.95  ? 754  ILE A CG1   1 
ATOM   5187 C  CG2   . ILE A 1 754  ? 130.125 108.329 109.180 1.00 40.95  ? 754  ILE A CG2   1 
ATOM   5188 C  CD1   . ILE A 1 754  ? 132.312 107.387 111.125 1.00 40.95  ? 754  ILE A CD1   1 
ATOM   5189 N  N     . MET A 1 755  ? 127.978 110.172 110.615 1.00 44.77  ? 755  MET A N     1 
ATOM   5190 C  CA    . MET A 1 755  ? 127.826 111.546 111.093 1.00 44.77  ? 755  MET A CA    1 
ATOM   5191 C  C     . MET A 1 755  ? 126.627 111.669 112.026 1.00 44.77  ? 755  MET A C     1 
ATOM   5192 O  O     . MET A 1 755  ? 126.692 112.378 113.040 1.00 44.77  ? 755  MET A O     1 
ATOM   5193 C  CB    . MET A 1 755  ? 127.697 112.538 109.936 1.00 44.77  ? 755  MET A CB    1 
ATOM   5194 C  CG    . MET A 1 755  ? 126.651 112.210 108.904 1.00 44.77  ? 755  MET A CG    1 
ATOM   5195 S  SD    . MET A 1 755  ? 125.864 113.687 108.231 1.00 44.77  ? 755  MET A SD    1 
ATOM   5196 C  CE    . MET A 1 755  ? 124.859 114.203 109.620 1.00 44.77  ? 755  MET A CE    1 
ATOM   5197 N  N     . GLY A 1 756  ? 125.527 110.980 111.708 1.00 39.19  ? 756  GLY A N     1 
ATOM   5198 C  CA    . GLY A 1 756  ? 124.361 111.038 112.569 1.00 39.19  ? 756  GLY A CA    1 
ATOM   5199 C  C     . GLY A 1 756  ? 124.628 110.478 113.951 1.00 39.19  ? 756  GLY A C     1 
ATOM   5200 O  O     . GLY A 1 756  ? 124.220 111.066 114.956 1.00 39.19  ? 756  GLY A O     1 
ATOM   5201 N  N     . GLU A 1 757  ? 125.316 109.335 114.025 1.00 35.73  ? 757  GLU A N     1 
ATOM   5202 C  CA    . GLU A 1 757  ? 125.611 108.765 115.338 1.00 35.73  ? 757  GLU A CA    1 
ATOM   5203 C  C     . GLU A 1 757  ? 126.552 109.657 116.143 1.00 35.73  ? 757  GLU A C     1 
ATOM   5204 O  O     . GLU A 1 757  ? 126.352 109.839 117.352 1.00 35.73  ? 757  GLU A O     1 
ATOM   5205 C  CB    . GLU A 1 757  ? 126.168 107.351 115.196 1.00 35.73  ? 757  GLU A CB    1 
ATOM   5206 C  CG    . GLU A 1 757  ? 125.328 106.492 114.279 1.00 35.73  ? 757  GLU A CG    1 
ATOM   5207 C  CD    . GLU A 1 757  ? 124.474 105.500 115.030 1.00 35.73  ? 757  GLU A CD    1 
ATOM   5208 O  OE1   . GLU A 1 757  ? 124.400 105.600 116.271 1.00 35.73  ? 757  GLU A OE1   1 
ATOM   5209 O  OE2   . GLU A 1 757  ? 123.848 104.644 114.374 1.00 35.73  ? 757  GLU A OE2   1 
ATOM   5210 N  N     . ASN A 1 758  ? 127.577 110.229 115.500 1.00 35.93  ? 758  ASN A N     1 
ATOM   5211 C  CA    . ASN A 1 758  ? 128.450 111.147 116.230 1.00 35.93  ? 758  ASN A CA    1 
ATOM   5212 C  C     . ASN A 1 758  ? 127.669 112.341 116.768 1.00 35.93  ? 758  ASN A C     1 
ATOM   5213 O  O     . ASN A 1 758  ? 127.826 112.723 117.938 1.00 35.93  ? 758  ASN A O     1 
ATOM   5214 C  CB    . ASN A 1 758  ? 129.596 111.623 115.339 1.00 35.93  ? 758  ASN A CB    1 
ATOM   5215 C  CG    . ASN A 1 758  ? 130.737 110.631 115.276 1.00 35.93  ? 758  ASN A CG    1 
ATOM   5216 O  OD1   . ASN A 1 758  ? 131.063 109.983 116.269 1.00 35.93  ? 758  ASN A OD1   1 
ATOM   5217 N  ND2   . ASN A 1 758  ? 131.365 110.523 114.112 1.00 35.93  ? 758  ASN A ND2   1 
ATOM   5218 N  N     . LEU A 1 759  ? 126.807 112.931 115.933 1.00 35.50  ? 759  LEU A N     1 
ATOM   5219 C  CA    . LEU A 1 759  ? 126.020 114.078 116.372 1.00 35.50  ? 759  LEU A CA    1 
ATOM   5220 C  C     . LEU A 1 759  ? 125.100 113.709 117.529 1.00 35.50  ? 759  LEU A C     1 
ATOM   5221 O  O     . LEU A 1 759  ? 124.984 114.463 118.506 1.00 35.50  ? 759  LEU A O     1 
ATOM   5222 C  CB    . LEU A 1 759  ? 125.210 114.631 115.199 1.00 35.50  ? 759  LEU A CB    1 
ATOM   5223 C  CG    . LEU A 1 759  ? 124.088 115.608 115.546 1.00 35.50  ? 759  LEU A CG    1 
ATOM   5224 C  CD1   . LEU A 1 759  ? 124.665 116.906 116.084 1.00 35.50  ? 759  LEU A CD1   1 
ATOM   5225 C  CD2   . LEU A 1 759  ? 123.206 115.865 114.336 1.00 35.50  ? 759  LEU A CD2   1 
ATOM   5226 N  N     . THR A 1 760  ? 124.438 112.553 117.437 1.00 32.87  ? 760  THR A N     1 
ATOM   5227 C  CA    . THR A 1 760  ? 123.515 112.138 118.488 1.00 32.87  ? 760  THR A CA    1 
ATOM   5228 C  C     . THR A 1 760  ? 124.241 111.920 119.808 1.00 32.87  ? 760  THR A C     1 
ATOM   5229 O  O     . THR A 1 760  ? 123.772 112.366 120.864 1.00 32.87  ? 760  THR A O     1 
ATOM   5230 C  CB    . THR A 1 760  ? 122.777 110.868 118.065 1.00 32.87  ? 760  THR A CB    1 
ATOM   5231 O  OG1   . THR A 1 760  ? 122.064 111.112 116.847 1.00 32.87  ? 760  THR A OG1   1 
ATOM   5232 C  CG2   . THR A 1 760  ? 121.794 110.440 119.138 1.00 32.87  ? 760  THR A CG2   1 
ATOM   5233 N  N     . THR A 1 761  ? 125.392 111.244 119.773 1.00 30.84  ? 761  THR A N     1 
ATOM   5234 C  CA    . THR A 1 761  ? 126.140 111.024 121.006 1.00 30.84  ? 761  THR A CA    1 
ATOM   5235 C  C     . THR A 1 761  ? 126.599 112.343 121.617 1.00 30.84  ? 761  THR A C     1 
ATOM   5236 O  O     . THR A 1 761  ? 126.483 112.549 122.835 1.00 30.84  ? 761  THR A O     1 
ATOM   5237 C  CB    . THR A 1 761  ? 127.336 110.111 120.741 1.00 30.84  ? 761  THR A CB    1 
ATOM   5238 O  OG1   . THR A 1 761  ? 126.873 108.853 120.234 1.00 30.84  ? 761  THR A OG1   1 
ATOM   5239 C  CG2   . THR A 1 761  ? 128.120 109.878 122.022 1.00 30.84  ? 761  THR A CG2   1 
ATOM   5240 N  N     . ARG A 1 762  ? 127.107 113.258 120.784 1.00 31.25  ? 762  ARG A N     1 
ATOM   5241 C  CA    . ARG A 1 762  ? 127.573 114.537 121.309 1.00 31.25  ? 762  ARG A CA    1 
ATOM   5242 C  C     . ARG A 1 762  ? 126.432 115.326 121.943 1.00 31.25  ? 762  ARG A C     1 
ATOM   5243 O  O     . ARG A 1 762  ? 126.587 115.888 123.037 1.00 31.25  ? 762  ARG A O     1 
ATOM   5244 C  CB    . ARG A 1 762  ? 128.236 115.351 120.200 1.00 31.25  ? 762  ARG A CB    1 
ATOM   5245 C  CG    . ARG A 1 762  ? 129.162 116.447 120.706 1.00 31.25  ? 762  ARG A CG    1 
ATOM   5246 C  CD    . ARG A 1 762  ? 129.938 117.093 119.569 1.00 31.25  ? 762  ARG A CD    1 
ATOM   5247 N  NE    . ARG A 1 762  ? 130.906 116.176 118.977 1.00 31.25  ? 762  ARG A NE    1 
ATOM   5248 C  CZ    . ARG A 1 762  ? 130.731 115.552 117.817 1.00 31.25  ? 762  ARG A CZ    1 
ATOM   5249 N  NH1   . ARG A 1 762  ? 131.665 114.734 117.354 1.00 31.25  ? 762  ARG A NH1   1 
ATOM   5250 N  NH2   . ARG A 1 762  ? 129.619 115.743 117.122 1.00 31.25  ? 762  ARG A NH2   1 
ATOM   5251 N  N     . VAL A 1 763  ? 125.276 115.375 121.276 1.00 28.55  ? 763  VAL A N     1 
ATOM   5252 C  CA    . VAL A 1 763  ? 124.171 116.164 121.811 1.00 28.55  ? 763  VAL A CA    1 
ATOM   5253 C  C     . VAL A 1 763  ? 123.624 115.527 123.084 1.00 28.55  ? 763  VAL A C     1 
ATOM   5254 O  O     . VAL A 1 763  ? 123.234 116.233 124.019 1.00 28.55  ? 763  VAL A O     1 
ATOM   5255 C  CB    . VAL A 1 763  ? 123.075 116.376 120.747 1.00 28.55  ? 763  VAL A CB    1 
ATOM   5256 C  CG1   . VAL A 1 763  ? 122.365 115.081 120.406 1.00 28.55  ? 763  VAL A CG1   1 
ATOM   5257 C  CG2   . VAL A 1 763  ? 122.081 117.425 121.219 1.00 28.55  ? 763  VAL A CG2   1 
ATOM   5258 N  N     . ARG A 1 764  ? 123.605 114.191 123.156 1.00 25.85  ? 764  ARG A N     1 
ATOM   5259 C  CA    . ARG A 1 764  ? 123.185 113.530 124.390 1.00 25.85  ? 764  ARG A CA    1 
ATOM   5260 C  C     . ARG A 1 764  ? 124.102 113.901 125.547 1.00 25.85  ? 764  ARG A C     1 
ATOM   5261 O  O     . ARG A 1 764  ? 123.637 114.246 126.643 1.00 25.85  ? 764  ARG A O     1 
ATOM   5262 C  CB    . ARG A 1 764  ? 123.168 112.014 124.198 1.00 25.85  ? 764  ARG A CB    1 
ATOM   5263 C  CG    . ARG A 1 764  ? 121.863 111.443 123.681 1.00 25.85  ? 764  ARG A CG    1 
ATOM   5264 C  CD    . ARG A 1 764  ? 122.000 109.947 123.461 1.00 25.85  ? 764  ARG A CD    1 
ATOM   5265 N  NE    . ARG A 1 764  ? 120.757 109.332 123.009 1.00 25.85  ? 764  ARG A NE    1 
ATOM   5266 C  CZ    . ARG A 1 764  ? 119.923 108.670 123.802 1.00 25.85  ? 764  ARG A CZ    1 
ATOM   5267 N  NH1   . ARG A 1 764  ? 118.815 108.138 123.306 1.00 25.85  ? 764  ARG A NH1   1 
ATOM   5268 N  NH2   . ARG A 1 764  ? 120.196 108.540 125.093 1.00 25.85  ? 764  ARG A NH2   1 
ATOM   5269 N  N     . ARG A 1 765  ? 125.416 113.837 125.317 1.00 27.88  ? 765  ARG A N     1 
ATOM   5270 C  CA    . ARG A 1 765  ? 126.364 114.160 126.378 1.00 27.88  ? 765  ARG A CA    1 
ATOM   5271 C  C     . ARG A 1 765  ? 126.197 115.602 126.843 1.00 27.88  ? 765  ARG A C     1 
ATOM   5272 O  O     . ARG A 1 765  ? 126.149 115.879 128.051 1.00 27.88  ? 765  ARG A O     1 
ATOM   5273 C  CB    . ARG A 1 765  ? 127.791 113.909 125.894 1.00 27.88  ? 765  ARG A CB    1 
ATOM   5274 C  CG    . ARG A 1 765  ? 128.866 114.363 126.862 1.00 27.88  ? 765  ARG A CG    1 
ATOM   5275 C  CD    . ARG A 1 765  ? 128.945 113.453 128.072 1.00 27.88  ? 765  ARG A CD    1 
ATOM   5276 N  NE    . ARG A 1 765  ? 130.015 113.857 128.978 1.00 27.88  ? 765  ARG A NE    1 
ATOM   5277 C  CZ    . ARG A 1 765  ? 131.276 113.452 128.873 1.00 27.88  ? 765  ARG A CZ    1 
ATOM   5278 N  NH1   . ARG A 1 765  ? 132.185 113.872 129.742 1.00 27.88  ? 765  ARG A NH1   1 
ATOM   5279 N  NH2   . ARG A 1 765  ? 131.629 112.627 127.897 1.00 27.88  ? 765  ARG A NH2   1 
ATOM   5280 N  N     . MET A 1 766  ? 126.085 116.538 125.896 1.00 29.58  ? 766  MET A N     1 
ATOM   5281 C  CA    . MET A 1 766  ? 125.959 117.941 126.283 1.00 29.58  ? 766  MET A CA    1 
ATOM   5282 C  C     . MET A 1 766  ? 124.639 118.210 126.997 1.00 29.58  ? 766  MET A C     1 
ATOM   5283 O  O     . MET A 1 766  ? 124.598 118.995 127.950 1.00 29.58  ? 766  MET A O     1 
ATOM   5284 C  CB    . MET A 1 766  ? 126.110 118.855 125.068 1.00 29.58  ? 766  MET A CB    1 
ATOM   5285 C  CG    . MET A 1 766  ? 127.434 118.707 124.340 1.00 29.58  ? 766  MET A CG    1 
ATOM   5286 S  SD    . MET A 1 766  ? 127.267 118.933 122.563 1.00 29.58  ? 766  MET A SD    1 
ATOM   5287 C  CE    . MET A 1 766  ? 126.569 120.580 122.522 1.00 29.58  ? 766  MET A CE    1 
ATOM   5288 N  N     . MET A 1 767  ? 123.550 117.574 126.554 1.00 25.97  ? 767  MET A N     1 
ATOM   5289 C  CA    . MET A 1 767  ? 122.266 117.762 127.219 1.00 25.97  ? 767  MET A CA    1 
ATOM   5290 C  C     . MET A 1 767  ? 122.308 117.257 128.654 1.00 25.97  ? 767  MET A C     1 
ATOM   5291 O  O     . MET A 1 767  ? 121.808 117.924 129.570 1.00 25.97  ? 767  MET A O     1 
ATOM   5292 C  CB    . MET A 1 767  ? 121.162 117.049 126.439 1.00 25.97  ? 767  MET A CB    1 
ATOM   5293 C  CG    . MET A 1 767  ? 119.767 117.573 126.719 1.00 25.97  ? 767  MET A CG    1 
ATOM   5294 S  SD    . MET A 1 767  ? 118.520 116.793 125.679 1.00 25.97  ? 767  MET A SD    1 
ATOM   5295 C  CE    . MET A 1 767  ? 119.462 116.495 124.187 1.00 25.97  ? 767  MET A CE    1 
ATOM   5296 N  N     . LEU A 1 768  ? 122.899 116.079 128.873 1.00 24.47  ? 768  LEU A N     1 
ATOM   5297 C  CA    . LEU A 1 768  ? 122.991 115.564 130.235 1.00 24.47  ? 768  LEU A CA    1 
ATOM   5298 C  C     . LEU A 1 768  ? 123.858 116.464 131.106 1.00 24.47  ? 768  LEU A C     1 
ATOM   5299 O  O     . LEU A 1 768  ? 123.528 116.716 132.272 1.00 24.47  ? 768  LEU A O     1 
ATOM   5300 C  CB    . LEU A 1 768  ? 123.535 114.138 130.236 1.00 24.47  ? 768  LEU A CB    1 
ATOM   5301 C  CG    . LEU A 1 768  ? 123.372 113.433 131.585 1.00 24.47  ? 768  LEU A CG    1 
ATOM   5302 C  CD1   . LEU A 1 768  ? 121.937 113.536 132.067 1.00 24.47  ? 768  LEU A CD1   1 
ATOM   5303 C  CD2   . LEU A 1 768  ? 123.804 111.986 131.498 1.00 24.47  ? 768  LEU A CD2   1 
ATOM   5304 N  N     . SER A 1 769  ? 124.973 116.959 130.560 1.00 25.56  ? 769  SER A N     1 
ATOM   5305 C  CA    . SER A 1 769  ? 125.816 117.866 131.333 1.00 25.56  ? 769  SER A CA    1 
ATOM   5306 C  C     . SER A 1 769  ? 125.066 119.143 131.694 1.00 25.56  ? 769  SER A C     1 
ATOM   5307 O  O     . SER A 1 769  ? 125.149 119.623 132.832 1.00 25.56  ? 769  SER A O     1 
ATOM   5308 C  CB    . SER A 1 769  ? 127.088 118.194 130.554 1.00 25.56  ? 769  SER A CB    1 
ATOM   5309 O  OG    . SER A 1 769  ? 128.078 118.737 131.408 1.00 25.56  ? 769  SER A OG    1 
ATOM   5310 N  N     . ALA A 1 770  ? 124.318 119.702 130.740 1.00 24.16  ? 770  ALA A N     1 
ATOM   5311 C  CA    . ALA A 1 770  ? 123.564 120.922 131.006 1.00 24.16  ? 770  ALA A CA    1 
ATOM   5312 C  C     . ALA A 1 770  ? 122.499 120.695 132.069 1.00 24.16  ? 770  ALA A C     1 
ATOM   5313 O  O     . ALA A 1 770  ? 122.290 121.549 132.938 1.00 24.16  ? 770  ALA A O     1 
ATOM   5314 C  CB    . ALA A 1 770  ? 122.932 121.442 129.717 1.00 24.16  ? 770  ALA A CB    1 
ATOM   5315 N  N     . ILE A 1 771  ? 121.807 119.553 132.015 1.00 21.59  ? 771  ILE A N     1 
ATOM   5316 C  CA    . ILE A 1 771  ? 120.795 119.265 133.028 1.00 21.59  ? 771  ILE A CA    1 
ATOM   5317 C  C     . ILE A 1 771  ? 121.437 119.122 134.401 1.00 21.59  ? 771  ILE A C     1 
ATOM   5318 O  O     . ILE A 1 771  ? 120.943 119.674 135.392 1.00 21.59  ? 771  ILE A O     1 
ATOM   5319 C  CB    . ILE A 1 771  ? 119.984 118.015 132.647 1.00 21.59  ? 771  ILE A CB    1 
ATOM   5320 C  CG1   . ILE A 1 771  ? 118.887 118.385 131.653 1.00 21.59  ? 771  ILE A CG1   1 
ATOM   5321 C  CG2   . ILE A 1 771  ? 119.376 117.374 133.880 1.00 21.59  ? 771  ILE A CG2   1 
ATOM   5322 C  CD1   . ILE A 1 771  ? 118.046 117.219 131.226 1.00 21.59  ? 771  ILE A CD1   1 
ATOM   5323 N  N     . LEU A 1 772  ? 122.551 118.392 134.485 1.00 23.27  ? 772  LEU A N     1 
ATOM   5324 C  CA    . LEU A 1 772  ? 123.242 118.263 135.764 1.00 23.27  ? 772  LEU A CA    1 
ATOM   5325 C  C     . LEU A 1 772  ? 123.805 119.589 136.256 1.00 23.27  ? 772  LEU A C     1 
ATOM   5326 O  O     . LEU A 1 772  ? 124.065 119.730 137.455 1.00 23.27  ? 772  LEU A O     1 
ATOM   5327 C  CB    . LEU A 1 772  ? 124.365 117.229 135.666 1.00 23.27  ? 772  LEU A CB    1 
ATOM   5328 C  CG    . LEU A 1 772  ? 124.032 115.779 136.031 1.00 23.27  ? 772  LEU A CG    1 
ATOM   5329 C  CD1   . LEU A 1 772  ? 123.674 115.676 137.504 1.00 23.27  ? 772  LEU A CD1   1 
ATOM   5330 C  CD2   . LEU A 1 772  ? 122.915 115.220 135.166 1.00 23.27  ? 772  LEU A CD2   1 
ATOM   5331 N  N     . ARG A 1 773  ? 124.000 120.561 135.362 1.00 28.26  ? 773  ARG A N     1 
ATOM   5332 C  CA    . ARG A 1 773  ? 124.529 121.856 135.773 1.00 28.26  ? 773  ARG A CA    1 
ATOM   5333 C  C     . ARG A 1 773  ? 123.499 122.710 136.507 1.00 28.26  ? 773  ARG A C     1 
ATOM   5334 O  O     . ARG A 1 773  ? 123.885 123.582 137.293 1.00 28.26  ? 773  ARG A O     1 
ATOM   5335 C  CB    . ARG A 1 773  ? 125.059 122.607 134.549 1.00 28.26  ? 773  ARG A CB    1 
ATOM   5336 C  CG    . ARG A 1 773  ? 125.856 123.860 134.865 1.00 28.26  ? 773  ARG A CG    1 
ATOM   5337 C  CD    . ARG A 1 773  ? 126.460 124.454 133.605 1.00 28.26  ? 773  ARG A CD    1 
ATOM   5338 N  NE    . ARG A 1 773  ? 127.095 125.744 133.854 1.00 28.26  ? 773  ARG A NE    1 
ATOM   5339 C  CZ    . ARG A 1 773  ? 128.337 125.891 134.302 1.00 28.26  ? 773  ARG A CZ    1 
ATOM   5340 N  NH1   . ARG A 1 773  ? 128.834 127.105 134.498 1.00 28.26  ? 773  ARG A NH1   1 
ATOM   5341 N  NH2   . ARG A 1 773  ? 129.084 124.826 134.558 1.00 28.26  ? 773  ARG A NH2   1 
ATOM   5342 N  N     . ASN A 1 774  ? 122.208 122.476 136.282 1.00 25.27  ? 774  ASN A N     1 
ATOM   5343 C  CA    . ASN A 1 774  ? 121.172 123.322 136.857 1.00 25.27  ? 774  ASN A CA    1 
ATOM   5344 C  C     . ASN A 1 774  ? 121.118 123.174 138.375 1.00 25.27  ? 774  ASN A C     1 
ATOM   5345 O  O     . ASN A 1 774  ? 121.580 122.186 138.951 1.00 25.27  ? 774  ASN A O     1 
ATOM   5346 C  CB    . ASN A 1 774  ? 119.807 122.980 136.261 1.00 25.27  ? 774  ASN A CB    1 
ATOM   5347 C  CG    . ASN A 1 774  ? 119.618 123.551 134.874 1.00 25.27  ? 774  ASN A CG    1 
ATOM   5348 O  OD1   . ASN A 1 774  ? 120.568 124.013 134.245 1.00 25.27  ? 774  ASN A OD1   1 
ATOM   5349 N  ND2   . ASN A 1 774  ? 118.384 123.522 134.387 1.00 25.27  ? 774  ASN A ND2   1 
ATOM   5350 N  N     . GLU A 1 775  ? 120.540 124.182 139.024 1.00 26.21  ? 775  GLU A N     1 
ATOM   5351 C  CA    . GLU A 1 775  ? 120.383 124.169 140.468 1.00 26.21  ? 775  GLU A CA    1 
ATOM   5352 C  C     . GLU A 1 775  ? 119.176 123.321 140.866 1.00 26.21  ? 775  GLU A C     1 
ATOM   5353 O  O     . GLU A 1 775  ? 118.393 122.869 140.026 1.00 26.21  ? 775  GLU A O     1 
ATOM   5354 C  CB    . GLU A 1 775  ? 120.242 125.592 141.005 1.00 26.21  ? 775  GLU A CB    1 
ATOM   5355 C  CG    . GLU A 1 775  ? 118.838 126.163 140.912 1.00 26.21  ? 775  GLU A CG    1 
ATOM   5356 C  CD    . GLU A 1 775  ? 118.577 126.864 139.594 1.00 26.21  ? 775  GLU A CD    1 
ATOM   5357 O  OE1   . GLU A 1 775  ? 119.251 126.534 138.597 1.00 26.21  ? 775  GLU A OE1   1 
ATOM   5358 O  OE2   . GLU A 1 775  ? 117.698 127.751 139.555 1.00 26.21  ? 775  GLU A OE2   1 
ATOM   5359 N  N     . VAL A 1 776  ? 119.032 123.102 142.176 1.00 26.30  ? 776  VAL A N     1 
ATOM   5360 C  CA    . VAL A 1 776  ? 117.975 122.223 142.666 1.00 26.30  ? 776  VAL A CA    1 
ATOM   5361 C  C     . VAL A 1 776  ? 116.599 122.848 142.468 1.00 26.30  ? 776  VAL A C     1 
ATOM   5362 O  O     . VAL A 1 776  ? 115.612 122.131 142.259 1.00 26.30  ? 776  VAL A O     1 
ATOM   5363 C  CB    . VAL A 1 776  ? 118.221 121.856 144.141 1.00 26.30  ? 776  VAL A CB    1 
ATOM   5364 C  CG1   . VAL A 1 776  ? 119.624 121.308 144.323 1.00 26.30  ? 776  VAL A CG1   1 
ATOM   5365 C  CG2   . VAL A 1 776  ? 117.997 123.055 145.037 1.00 26.30  ? 776  VAL A CG2   1 
ATOM   5366 N  N     . GLY A 1 777  ? 116.502 124.179 142.527 1.00 26.00  ? 777  GLY A N     1 
ATOM   5367 C  CA    . GLY A 1 777  ? 115.209 124.826 142.387 1.00 26.00  ? 777  GLY A CA    1 
ATOM   5368 C  C     . GLY A 1 777  ? 114.546 124.544 141.055 1.00 26.00  ? 777  GLY A C     1 
ATOM   5369 O  O     . GLY A 1 777  ? 113.326 124.371 140.989 1.00 26.00  ? 777  GLY A O     1 
ATOM   5370 N  N     . TRP A 1 778  ? 115.336 124.483 139.982 1.00 24.87  ? 778  TRP A N     1 
ATOM   5371 C  CA    . TRP A 1 778  ? 114.786 124.152 138.672 1.00 24.87  ? 778  TRP A CA    1 
ATOM   5372 C  C     . TRP A 1 778  ? 114.134 122.776 138.683 1.00 24.87  ? 778  TRP A C     1 
ATOM   5373 O  O     . TRP A 1 778  ? 113.199 122.517 137.918 1.00 24.87  ? 778  TRP A O     1 
ATOM   5374 C  CB    . TRP A 1 778  ? 115.887 124.219 137.615 1.00 24.87  ? 778  TRP A CB    1 
ATOM   5375 C  CG    . TRP A 1 778  ? 115.419 123.891 136.239 1.00 24.87  ? 778  TRP A CG    1 
ATOM   5376 C  CD1   . TRP A 1 778  ? 114.811 124.736 135.360 1.00 24.87  ? 778  TRP A CD1   1 
ATOM   5377 C  CD2   . TRP A 1 778  ? 115.524 122.628 135.574 1.00 24.87  ? 778  TRP A CD2   1 
ATOM   5378 N  NE1   . TRP A 1 778  ? 114.530 124.078 134.188 1.00 24.87  ? 778  TRP A NE1   1 
ATOM   5379 C  CE2   . TRP A 1 778  ? 114.956 122.781 134.296 1.00 24.87  ? 778  TRP A CE2   1 
ATOM   5380 C  CE3   . TRP A 1 778  ? 116.041 121.382 135.937 1.00 24.87  ? 778  TRP A CE3   1 
ATOM   5381 C  CZ2   . TRP A 1 778  ? 114.892 121.737 133.379 1.00 24.87  ? 778  TRP A CZ2   1 
ATOM   5382 C  CZ3   . TRP A 1 778  ? 115.976 120.348 135.026 1.00 24.87  ? 778  TRP A CZ3   1 
ATOM   5383 C  CH2   . TRP A 1 778  ? 115.406 120.530 133.762 1.00 24.87  ? 778  TRP A CH2   1 
ATOM   5384 N  N     . PHE A 1 779  ? 114.618 121.877 139.543 1.00 24.52  ? 779  PHE A N     1 
ATOM   5385 C  CA    . PHE A 1 779  ? 113.994 120.565 139.664 1.00 24.52  ? 779  PHE A CA    1 
ATOM   5386 C  C     . PHE A 1 779  ? 112.673 120.649 140.418 1.00 24.52  ? 779  PHE A C     1 
ATOM   5387 O  O     . PHE A 1 779  ? 111.748 119.875 140.146 1.00 24.52  ? 779  PHE A O     1 
ATOM   5388 C  CB    . PHE A 1 779  ? 114.947 119.591 140.355 1.00 24.52  ? 779  PHE A CB    1 
ATOM   5389 C  CG    . PHE A 1 779  ? 116.165 119.257 139.543 1.00 24.52  ? 779  PHE A CG    1 
ATOM   5390 C  CD1   . PHE A 1 779  ? 116.077 118.403 138.459 1.00 24.52  ? 779  PHE A CD1   1 
ATOM   5391 C  CD2   . PHE A 1 779  ? 117.397 119.798 139.865 1.00 24.52  ? 779  PHE A CD2   1 
ATOM   5392 C  CE1   . PHE A 1 779  ? 117.192 118.096 137.710 1.00 24.52  ? 779  PHE A CE1   1 
ATOM   5393 C  CE2   . PHE A 1 779  ? 118.516 119.494 139.119 1.00 24.52  ? 779  PHE A CE2   1 
ATOM   5394 C  CZ    . PHE A 1 779  ? 118.413 118.642 138.041 1.00 24.52  ? 779  PHE A CZ    1 
ATOM   5395 N  N     . ASP A 1 780  ? 112.564 121.582 141.365 1.00 28.23  ? 780  ASP A N     1 
ATOM   5396 C  CA    . ASP A 1 780  ? 111.365 121.710 142.195 1.00 28.23  ? 780  ASP A CA    1 
ATOM   5397 C  C     . ASP A 1 780  ? 110.310 122.497 141.424 1.00 28.23  ? 780  ASP A C     1 
ATOM   5398 O  O     . ASP A 1 780  ? 110.056 123.679 141.669 1.00 28.23  ? 780  ASP A O     1 
ATOM   5399 C  CB    . ASP A 1 780  ? 111.699 122.372 143.525 1.00 28.23  ? 780  ASP A CB    1 
ATOM   5400 C  CG    . ASP A 1 780  ? 112.237 121.390 144.544 1.00 28.23  ? 780  ASP A CG    1 
ATOM   5401 O  OD1   . ASP A 1 780  ? 112.579 120.254 144.152 1.00 28.23  ? 780  ASP A OD1   1 
ATOM   5402 O  OD2   . ASP A 1 780  ? 112.320 121.754 145.735 1.00 28.23  ? 780  ASP A OD2   1 
ATOM   5403 N  N     . GLU A 1 781  ? 109.681 121.816 140.472 1.00 31.76  ? 781  GLU A N     1 
ATOM   5404 C  CA    . GLU A 1 781  ? 108.608 122.398 139.678 1.00 31.76  ? 781  GLU A CA    1 
ATOM   5405 C  C     . GLU A 1 781  ? 107.609 121.294 139.354 1.00 31.76  ? 781  GLU A C     1 
ATOM   5406 O  O     . GLU A 1 781  ? 107.720 120.168 139.848 1.00 31.76  ? 781  GLU A O     1 
ATOM   5407 C  CB    . GLU A 1 781  ? 109.166 123.071 138.418 1.00 31.76  ? 781  GLU A CB    1 
ATOM   5408 C  CG    . GLU A 1 781  ? 109.526 124.537 138.607 1.00 31.76  ? 781  GLU A CG    1 
ATOM   5409 C  CD    . GLU A 1 781  ? 109.686 125.275 137.292 1.00 31.76  ? 781  GLU A CD    1 
ATOM   5410 O  OE1   . GLU A 1 781  ? 110.201 126.413 137.306 1.00 31.76  ? 781  GLU A OE1   1 
ATOM   5411 O  OE2   . GLU A 1 781  ? 109.293 124.719 136.246 1.00 31.76  ? 781  GLU A OE2   1 
ATOM   5412 N  N     . ASP A 1 782  ? 106.625 121.618 138.516 1.00 35.33  ? 782  ASP A N     1 
ATOM   5413 C  CA    . ASP A 1 782  ? 105.583 120.662 138.165 1.00 35.33  ? 782  ASP A CA    1 
ATOM   5414 C  C     . ASP A 1 782  ? 105.950 119.817 136.952 1.00 35.33  ? 782  ASP A C     1 
ATOM   5415 O  O     . ASP A 1 782  ? 105.674 118.613 136.930 1.00 35.33  ? 782  ASP A O     1 
ATOM   5416 C  CB    . ASP A 1 782  ? 104.264 121.395 137.906 1.00 35.33  ? 782  ASP A CB    1 
ATOM   5417 C  CG    . ASP A 1 782  ? 103.138 120.453 137.530 1.00 35.33  ? 782  ASP A CG    1 
ATOM   5418 O  OD1   . ASP A 1 782  ? 103.059 119.354 138.116 1.00 35.33  ? 782  ASP A OD1   1 
ATOM   5419 O  OD2   . ASP A 1 782  ? 102.331 120.812 136.647 1.00 35.33  ? 782  ASP A OD2   1 
ATOM   5420 N  N     . GLU A 1 783  ? 106.569 120.425 135.941 1.00 34.97  ? 783  GLU A N     1 
ATOM   5421 C  CA    . GLU A 1 783  ? 106.916 119.735 134.708 1.00 34.97  ? 783  GLU A CA    1 
ATOM   5422 C  C     . GLU A 1 783  ? 108.320 119.138 134.738 1.00 34.97  ? 783  GLU A C     1 
ATOM   5423 O  O     . GLU A 1 783  ? 108.657 118.332 133.864 1.00 34.97  ? 783  GLU A O     1 
ATOM   5424 C  CB    . GLU A 1 783  ? 106.774 120.706 133.523 1.00 34.97  ? 783  GLU A CB    1 
ATOM   5425 C  CG    . GLU A 1 783  ? 107.022 120.114 132.142 1.00 34.97  ? 783  GLU A CG    1 
ATOM   5426 C  CD    . GLU A 1 783  ? 106.813 121.122 131.030 1.00 34.97  ? 783  GLU A CD    1 
ATOM   5427 O  OE1   . GLU A 1 783  ? 106.494 122.289 131.337 1.00 34.97  ? 783  GLU A OE1   1 
ATOM   5428 O  OE2   . GLU A 1 783  ? 106.977 120.748 129.850 1.00 34.97  ? 783  GLU A OE2   1 
ATOM   5429 N  N     . HIS A 1 784  ? 109.132 119.482 135.736 1.00 27.65  ? 784  HIS A N     1 
ATOM   5430 C  CA    . HIS A 1 784  ? 110.505 118.990 135.829 1.00 27.65  ? 784  HIS A CA    1 
ATOM   5431 C  C     . HIS A 1 784  ? 110.540 117.813 136.800 1.00 27.65  ? 784  HIS A C     1 
ATOM   5432 O  O     . HIS A 1 784  ? 110.957 117.925 137.952 1.00 27.65  ? 784  HIS A O     1 
ATOM   5433 C  CB    . HIS A 1 784  ? 111.442 120.113 136.252 1.00 27.65  ? 784  HIS A CB    1 
ATOM   5434 C  CG    . HIS A 1 784  ? 111.403 121.298 135.339 1.00 27.65  ? 784  HIS A CG    1 
ATOM   5435 N  ND1   . HIS A 1 784  ? 111.709 122.573 135.760 1.00 27.65  ? 784  HIS A ND1   1 
ATOM   5436 C  CD2   . HIS A 1 784  ? 111.087 121.400 134.027 1.00 27.65  ? 784  HIS A CD2   1 
ATOM   5437 C  CE1   . HIS A 1 784  ? 111.585 123.410 134.745 1.00 27.65  ? 784  HIS A CE1   1 
ATOM   5438 N  NE2   . HIS A 1 784  ? 111.210 122.723 133.682 1.00 27.65  ? 784  HIS A NE2   1 
ATOM   5439 N  N     . ASN A 1 785  ? 110.088 116.663 136.311 1.00 26.56  ? 785  ASN A N     1 
ATOM   5440 C  CA    . ASN A 1 785  ? 110.074 115.425 137.072 1.00 26.56  ? 785  ASN A CA    1 
ATOM   5441 C  C     . ASN A 1 785  ? 111.127 114.470 136.525 1.00 26.56  ? 785  ASN A C     1 
ATOM   5442 O  O     . ASN A 1 785  ? 111.524 114.551 135.359 1.00 26.56  ? 785  ASN A O     1 
ATOM   5443 C  CB    . ASN A 1 785  ? 108.692 114.768 137.025 1.00 26.56  ? 785  ASN A CB    1 
ATOM   5444 C  CG    . ASN A 1 785  ? 108.493 113.756 138.129 1.00 26.56  ? 785  ASN A CG    1 
ATOM   5445 O  OD1   . ASN A 1 785  ? 108.976 112.627 138.046 1.00 26.56  ? 785  ASN A OD1   1 
ATOM   5446 N  ND2   . ASN A 1 785  ? 107.776 114.152 139.173 1.00 26.56  ? 785  ASN A ND2   1 
ATOM   5447 N  N     . SER A 1 786  ? 111.581 113.560 137.389 1.00 25.28  ? 786  SER A N     1 
ATOM   5448 C  CA    . SER A 1 786  ? 112.635 112.628 136.999 1.00 25.28  ? 786  SER A CA    1 
ATOM   5449 C  C     . SER A 1 786  ? 112.192 111.752 135.835 1.00 25.28  ? 786  SER A C     1 
ATOM   5450 O  O     . SER A 1 786  ? 112.921 111.594 134.848 1.00 25.28  ? 786  SER A O     1 
ATOM   5451 C  CB    . SER A 1 786  ? 113.040 111.768 138.194 1.00 25.28  ? 786  SER A CB    1 
ATOM   5452 O  OG    . SER A 1 786  ? 113.592 112.564 139.226 1.00 25.28  ? 786  SER A OG    1 
ATOM   5453 N  N     . SER A 1 787  ? 110.992 111.177 135.929 1.00 25.79  ? 787  SER A N     1 
ATOM   5454 C  CA    . SER A 1 787  ? 110.482 110.366 134.830 1.00 25.79  ? 787  SER A CA    1 
ATOM   5455 C  C     . SER A 1 787  ? 110.236 111.215 133.590 1.00 25.79  ? 787  SER A C     1 
ATOM   5456 O  O     . SER A 1 787  ? 110.505 110.776 132.466 1.00 25.79  ? 787  SER A O     1 
ATOM   5457 C  CB    . SER A 1 787  ? 109.203 109.646 135.253 1.00 25.79  ? 787  SER A CB    1 
ATOM   5458 O  OG    . SER A 1 787  ? 108.582 109.031 134.139 1.00 25.79  ? 787  SER A OG    1 
ATOM   5459 N  N     . LEU A 1 788  ? 109.726 112.435 133.774 1.00 24.87  ? 788  LEU A N     1 
ATOM   5460 C  CA    . LEU A 1 788  ? 109.511 113.329 132.640 1.00 24.87  ? 788  LEU A CA    1 
ATOM   5461 C  C     . LEU A 1 788  ? 110.823 113.650 131.938 1.00 24.87  ? 788  LEU A C     1 
ATOM   5462 O  O     . LEU A 1 788  ? 110.907 113.612 130.706 1.00 24.87  ? 788  LEU A O     1 
ATOM   5463 C  CB    . LEU A 1 788  ? 108.826 114.613 133.105 1.00 24.87  ? 788  LEU A CB    1 
ATOM   5464 C  CG    . LEU A 1 788  ? 107.304 114.554 133.220 1.00 24.87  ? 788  LEU A CG    1 
ATOM   5465 C  CD1   . LEU A 1 788  ? 106.754 115.800 133.888 1.00 24.87  ? 788  LEU A CD1   1 
ATOM   5466 C  CD2   . LEU A 1 788  ? 106.691 114.375 131.848 1.00 24.87  ? 788  LEU A CD2   1 
ATOM   5467 N  N     . ILE A 1 789  ? 111.864 113.962 132.710 1.00 23.21  ? 789  ILE A N     1 
ATOM   5468 C  CA    . ILE A 1 789  ? 113.153 114.298 132.115 1.00 23.21  ? 789  ILE A CA    1 
ATOM   5469 C  C     . ILE A 1 789  ? 113.757 113.084 131.420 1.00 23.21  ? 789  ILE A C     1 
ATOM   5470 O  O     . ILE A 1 789  ? 114.320 113.197 130.324 1.00 23.21  ? 789  ILE A O     1 
ATOM   5471 C  CB    . ILE A 1 789  ? 114.095 114.876 133.184 1.00 23.21  ? 789  ILE A CB    1 
ATOM   5472 C  CG1   . ILE A 1 789  ? 113.640 116.281 133.578 1.00 23.21  ? 789  ILE A CG1   1 
ATOM   5473 C  CG2   . ILE A 1 789  ? 115.524 114.907 132.680 1.00 23.21  ? 789  ILE A CG2   1 
ATOM   5474 C  CD1   . ILE A 1 789  ? 114.520 116.938 134.610 1.00 23.21  ? 789  ILE A CD1   1 
ATOM   5475 N  N     . ALA A 1 790  ? 113.652 111.906 132.039 1.00 22.72  ? 790  ALA A N     1 
ATOM   5476 C  CA    . ALA A 1 790  ? 114.182 110.698 131.415 1.00 22.72  ? 790  ALA A CA    1 
ATOM   5477 C  C     . ALA A 1 790  ? 113.466 110.399 130.103 1.00 22.72  ? 790  ALA A C     1 
ATOM   5478 O  O     . ALA A 1 790  ? 114.100 110.054 129.099 1.00 22.72  ? 790  ALA A O     1 
ATOM   5479 C  CB    . ALA A 1 790  ? 114.066 109.516 132.376 1.00 22.72  ? 790  ALA A CB    1 
ATOM   5480 N  N     . ALA A 1 791  ? 112.137 110.536 130.090 1.00 26.68  ? 791  ALA A N     1 
ATOM   5481 C  CA    . ALA A 1 791  ? 111.383 110.306 128.863 1.00 26.68  ? 791  ALA A CA    1 
ATOM   5482 C  C     . ALA A 1 791  ? 111.737 111.333 127.796 1.00 26.68  ? 791  ALA A C     1 
ATOM   5483 O  O     . ALA A 1 791  ? 111.847 110.996 126.612 1.00 26.68  ? 791  ALA A O     1 
ATOM   5484 C  CB    . ALA A 1 791  ? 109.884 110.330 129.156 1.00 26.68  ? 791  ALA A CB    1 
ATOM   5485 N  N     . ARG A 1 792  ? 111.911 112.594 128.195 1.00 29.64  ? 792  ARG A N     1 
ATOM   5486 C  CA    . ARG A 1 792  ? 112.269 113.632 127.235 1.00 29.64  ? 792  ARG A CA    1 
ATOM   5487 C  C     . ARG A 1 792  ? 113.636 113.361 126.618 1.00 29.64  ? 792  ARG A C     1 
ATOM   5488 O  O     . ARG A 1 792  ? 113.823 113.510 125.406 1.00 29.64  ? 792  ARG A O     1 
ATOM   5489 C  CB    . ARG A 1 792  ? 112.240 115.001 127.915 1.00 29.64  ? 792  ARG A CB    1 
ATOM   5490 C  CG    . ARG A 1 792  ? 112.354 116.171 126.959 1.00 29.64  ? 792  ARG A CG    1 
ATOM   5491 C  CD    . ARG A 1 792  ? 111.567 117.365 127.469 1.00 29.64  ? 792  ARG A CD    1 
ATOM   5492 N  NE    . ARG A 1 792  ? 110.175 117.023 127.740 1.00 29.64  ? 792  ARG A NE    1 
ATOM   5493 C  CZ    . ARG A 1 792  ? 109.220 116.987 126.816 1.00 29.64  ? 792  ARG A CZ    1 
ATOM   5494 N  NH1   . ARG A 1 792  ? 109.504 117.277 125.554 1.00 29.64  ? 792  ARG A NH1   1 
ATOM   5495 N  NH2   . ARG A 1 792  ? 107.980 116.664 127.154 1.00 29.64  ? 792  ARG A NH2   1 
ATOM   5496 N  N     . LEU A 1 793  ? 114.607 112.958 127.440 1.00 27.44  ? 793  LEU A N     1 
ATOM   5497 C  CA    . LEU A 1 793  ? 115.934 112.640 126.922 1.00 27.44  ? 793  LEU A CA    1 
ATOM   5498 C  C     . LEU A 1 793  ? 115.891 111.426 126.004 1.00 27.44  ? 793  LEU A C     1 
ATOM   5499 O  O     . LEU A 1 793  ? 116.530 111.410 124.946 1.00 27.44  ? 793  LEU A O     1 
ATOM   5500 C  CB    . LEU A 1 793  ? 116.908 112.404 128.075 1.00 27.44  ? 793  LEU A CB    1 
ATOM   5501 C  CG    . LEU A 1 793  ? 117.781 113.595 128.462 1.00 27.44  ? 793  LEU A CG    1 
ATOM   5502 C  CD1   . LEU A 1 793  ? 116.915 114.738 128.950 1.00 27.44  ? 793  LEU A CD1   1 
ATOM   5503 C  CD2   . LEU A 1 793  ? 118.795 113.190 129.522 1.00 27.44  ? 793  LEU A CD2   1 
ATOM   5504 N  N     . ALA A 1 794  ? 115.145 110.394 126.399 1.00 30.08  ? 794  ALA A N     1 
ATOM   5505 C  CA    . ALA A 1 794  ? 115.057 109.190 125.579 1.00 30.08  ? 794  ALA A CA    1 
ATOM   5506 C  C     . ALA A 1 794  ? 114.364 109.475 124.253 1.00 30.08  ? 794  ALA A C     1 
ATOM   5507 O  O     . ALA A 1 794  ? 114.775 108.969 123.203 1.00 30.08  ? 794  ALA A O     1 
ATOM   5508 C  CB    . ALA A 1 794  ? 114.327 108.087 126.346 1.00 30.08  ? 794  ALA A CB    1 
ATOM   5509 N  N     . THR A 1 795  ? 113.302 110.280 124.280 1.00 32.59  ? 795  THR A N     1 
ATOM   5510 C  CA    . THR A 1 795  ? 112.538 110.517 123.060 1.00 32.59  ? 795  THR A CA    1 
ATOM   5511 C  C     . THR A 1 795  ? 113.250 111.489 122.125 1.00 32.59  ? 795  THR A C     1 
ATOM   5512 O  O     . THR A 1 795  ? 113.357 111.232 120.921 1.00 32.59  ? 795  THR A O     1 
ATOM   5513 C  CB    . THR A 1 795  ? 111.144 111.035 123.408 1.00 32.59  ? 795  THR A CB    1 
ATOM   5514 O  OG1   . THR A 1 795  ? 111.247 112.078 124.384 1.00 32.59  ? 795  THR A OG1   1 
ATOM   5515 C  CG2   . THR A 1 795  ? 110.290 109.912 123.966 1.00 32.59  ? 795  THR A CG2   1 
ATOM   5516 N  N     . ASP A 1 796  ? 113.772 112.594 122.665 1.00 38.53  ? 796  ASP A N     1 
ATOM   5517 C  CA    . ASP A 1 796  ? 114.238 113.692 121.819 1.00 38.53  ? 796  ASP A CA    1 
ATOM   5518 C  C     . ASP A 1 796  ? 115.417 113.276 120.947 1.00 38.53  ? 796  ASP A C     1 
ATOM   5519 O  O     . ASP A 1 796  ? 115.344 113.364 119.714 1.00 38.53  ? 796  ASP A O     1 
ATOM   5520 C  CB    . ASP A 1 796  ? 114.610 114.894 122.688 1.00 38.53  ? 796  ASP A CB    1 
ATOM   5521 C  CG    . ASP A 1 796  ? 113.396 115.678 123.143 1.00 38.53  ? 796  ASP A CG    1 
ATOM   5522 O  OD1   . ASP A 1 796  ? 112.304 115.079 123.241 1.00 38.53  ? 796  ASP A OD1   1 
ATOM   5523 O  OD2   . ASP A 1 796  ? 113.533 116.891 123.408 1.00 38.53  ? 796  ASP A OD2   1 
ATOM   5524 N  N     . ALA A 1 797  ? 116.499 112.800 121.568 1.00 34.39  ? 797  ALA A N     1 
ATOM   5525 C  CA    . ALA A 1 797  ? 117.706 112.466 120.818 1.00 34.39  ? 797  ALA A CA    1 
ATOM   5526 C  C     . ALA A 1 797  ? 117.398 111.497 119.686 1.00 34.39  ? 797  ALA A C     1 
ATOM   5527 O  O     . ALA A 1 797  ? 117.883 111.667 118.560 1.00 34.39  ? 797  ALA A O     1 
ATOM   5528 C  CB    . ALA A 1 797  ? 118.764 111.884 121.755 1.00 34.39  ? 797  ALA A CB    1 
ATOM   5529 N  N     . ALA A 1 798  ? 116.559 110.494 119.957 1.00 35.82  ? 798  ALA A N     1 
ATOM   5530 C  CA    . ALA A 1 798  ? 116.186 109.541 118.919 1.00 35.82  ? 798  ALA A CA    1 
ATOM   5531 C  C     . ALA A 1 798  ? 115.650 110.259 117.688 1.00 35.82  ? 798  ALA A C     1 
ATOM   5532 O  O     . ALA A 1 798  ? 116.170 110.080 116.580 1.00 35.82  ? 798  ALA A O     1 
ATOM   5533 C  CB    . ALA A 1 798  ? 115.153 108.552 119.459 1.00 35.82  ? 798  ALA A CB    1 
ATOM   5534 N  N     . ASP A 1 799  ? 114.653 111.132 117.870 1.00 38.85  ? 799  ASP A N     1 
ATOM   5535 C  CA    . ASP A 1 799  ? 114.147 111.873 116.718 1.00 38.85  ? 799  ASP A CA    1 
ATOM   5536 C  C     . ASP A 1 799  ? 115.234 112.762 116.138 1.00 38.85  ? 799  ASP A C     1 
ATOM   5537 O  O     . ASP A 1 799  ? 115.370 112.869 114.913 1.00 38.85  ? 799  ASP A O     1 
ATOM   5538 C  CB    . ASP A 1 799  ? 112.911 112.696 117.081 1.00 38.85  ? 799  ASP A CB    1 
ATOM   5539 C  CG    . ASP A 1 799  ? 111.886 111.903 117.865 1.00 38.85  ? 799  ASP A CG    1 
ATOM   5540 O  OD1   . ASP A 1 799  ? 111.736 112.160 119.075 1.00 38.85  ? 799  ASP A OD1   1 
ATOM   5541 O  OD2   . ASP A 1 799  ? 111.246 111.006 117.277 1.00 38.85  ? 799  ASP A OD2   1 
ATOM   5542 N  N     . VAL A 1 800  ? 116.044 113.372 117.007 1.00 39.11  ? 800  VAL A N     1 
ATOM   5543 C  CA    . VAL A 1 800  ? 117.147 114.211 116.547 1.00 39.11  ? 800  VAL A CA    1 
ATOM   5544 C  C     . VAL A 1 800  ? 118.038 113.423 115.596 1.00 39.11  ? 800  VAL A C     1 
ATOM   5545 O  O     . VAL A 1 800  ? 118.567 113.963 114.619 1.00 39.11  ? 800  VAL A O     1 
ATOM   5546 C  CB    . VAL A 1 800  ? 117.935 114.761 117.750 1.00 39.11  ? 800  VAL A CB    1 
ATOM   5547 C  CG1   . VAL A 1 800  ? 119.303 115.259 117.324 1.00 39.11  ? 800  VAL A CG1   1 
ATOM   5548 C  CG2   . VAL A 1 800  ? 117.148 115.868 118.430 1.00 39.11  ? 800  VAL A CG2   1 
ATOM   5549 N  N     . LYS A 1 801  ? 118.192 112.124 115.850 1.00 41.51  ? 801  LYS A N     1 
ATOM   5550 C  CA    . LYS A 1 801  ? 118.880 111.282 114.881 1.00 41.51  ? 801  LYS A CA    1 
ATOM   5551 C  C     . LYS A 1 801  ? 118.019 111.082 113.641 1.00 41.51  ? 801  LYS A C     1 
ATOM   5552 O  O     . LYS A 1 801  ? 118.411 111.457 112.529 1.00 41.51  ? 801  LYS A O     1 
ATOM   5553 C  CB    . LYS A 1 801  ? 119.244 109.940 115.514 1.00 41.51  ? 801  LYS A CB    1 
ATOM   5554 C  CG    . LYS A 1 801  ? 119.875 108.952 114.549 1.00 41.51  ? 801  LYS A CG    1 
ATOM   5555 C  CD    . LYS A 1 801  ? 120.155 107.615 115.221 1.00 41.51  ? 801  LYS A CD    1 
ATOM   5556 C  CE    . LYS A 1 801  ? 120.493 107.784 116.696 1.00 41.51  ? 801  LYS A CE    1 
ATOM   5557 N  NZ    . LYS A 1 801  ? 120.832 106.487 117.345 1.00 41.51  ? 801  LYS A NZ    1 
ATOM   5558 N  N     . SER A 1 802  ? 116.812 110.540 113.828 1.00 47.45  ? 802  SER A N     1 
ATOM   5559 C  CA    . SER A 1 802  ? 115.991 110.122 112.696 1.00 47.45  ? 802  SER A CA    1 
ATOM   5560 C  C     . SER A 1 802  ? 115.644 111.302 111.798 1.00 47.45  ? 802  SER A C     1 
ATOM   5561 O  O     . SER A 1 802  ? 115.503 111.150 110.579 1.00 47.45  ? 802  SER A O     1 
ATOM   5562 C  CB    . SER A 1 802  ? 114.723 109.431 113.199 1.00 47.45  ? 802  SER A CB    1 
ATOM   5563 O  OG    . SER A 1 802  ? 113.874 109.070 112.124 1.00 47.45  ? 802  SER A OG    1 
ATOM   5564 N  N     . ALA A 1 803  ? 115.499 112.491 112.384 1.00 49.04  ? 803  ALA A N     1 
ATOM   5565 C  CA    . ALA A 1 803  ? 115.245 113.678 111.576 1.00 49.04  ? 803  ALA A CA    1 
ATOM   5566 C  C     . ALA A 1 803  ? 116.470 114.052 110.753 1.00 49.04  ? 803  ALA A C     1 
ATOM   5567 O  O     . ALA A 1 803  ? 116.363 114.331 109.554 1.00 49.04  ? 803  ALA A O     1 
ATOM   5568 C  CB    . ALA A 1 803  ? 114.817 114.843 112.469 1.00 49.04  ? 803  ALA A CB    1 
ATOM   5569 N  N     . ILE A 1 804  ? 117.649 114.063 111.379 1.00 51.43  ? 804  ILE A N     1 
ATOM   5570 C  CA    . ILE A 1 804  ? 118.847 114.527 110.681 1.00 51.43  ? 804  ILE A CA    1 
ATOM   5571 C  C     . ILE A 1 804  ? 119.283 113.512 109.630 1.00 51.43  ? 804  ILE A C     1 
ATOM   5572 O  O     . ILE A 1 804  ? 119.648 113.874 108.505 1.00 51.43  ? 804  ILE A O     1 
ATOM   5573 C  CB    . ILE A 1 804  ? 119.974 114.831 111.683 1.00 51.43  ? 804  ILE A CB    1 
ATOM   5574 C  CG1   . ILE A 1 804  ? 119.608 116.046 112.540 1.00 51.43  ? 804  ILE A CG1   1 
ATOM   5575 C  CG2   . ILE A 1 804  ? 121.288 115.074 110.957 1.00 51.43  ? 804  ILE A CG2   1 
ATOM   5576 C  CD1   . ILE A 1 804  ? 119.409 117.318 111.746 1.00 51.43  ? 804  ILE A CD1   1 
ATOM   5577 N  N     . ALA A 1 805  ? 119.252 112.225 109.981 1.00 52.25  ? 805  ALA A N     1 
ATOM   5578 C  CA    . ALA A 1 805  ? 119.740 111.197 109.067 1.00 52.25  ? 805  ALA A CA    1 
ATOM   5579 C  C     . ALA A 1 805  ? 118.845 111.070 107.839 1.00 52.25  ? 805  ALA A C     1 
ATOM   5580 O  O     . ALA A 1 805  ? 119.334 110.993 106.706 1.00 52.25  ? 805  ALA A O     1 
ATOM   5581 C  CB    . ALA A 1 805  ? 119.848 109.858 109.795 1.00 52.25  ? 805  ALA A CB    1 
ATOM   5582 N  N     . GLU A 1 806  ? 117.527 111.042 108.043 1.00 56.27  ? 806  GLU A N     1 
ATOM   5583 C  CA    . GLU A 1 806  ? 116.619 110.744 106.939 1.00 56.27  ? 806  GLU A CA    1 
ATOM   5584 C  C     . GLU A 1 806  ? 116.345 111.975 106.081 1.00 56.27  ? 806  GLU A C     1 
ATOM   5585 O  O     . GLU A 1 806  ? 116.388 111.902 104.848 1.00 56.27  ? 806  GLU A O     1 
ATOM   5586 C  CB    . GLU A 1 806  ? 115.313 110.159 107.476 1.00 56.27  ? 806  GLU A CB    1 
ATOM   5587 C  CG    . GLU A 1 806  ? 115.403 108.684 107.832 1.00 56.27  ? 806  GLU A CG    1 
ATOM   5588 C  CD    . GLU A 1 806  ? 115.479 107.791 106.607 1.00 56.27  ? 806  GLU A CD    1 
ATOM   5589 O  OE1   . GLU A 1 806  ? 115.858 106.611 106.754 1.00 56.27  ? 806  GLU A OE1   1 
ATOM   5590 O  OE2   . GLU A 1 806  ? 115.155 108.267 105.498 1.00 56.27  ? 806  GLU A OE2   1 
ATOM   5591 N  N     . ARG A 1 807  ? 116.047 113.114 106.712 1.00 59.62  ? 807  ARG A N     1 
ATOM   5592 C  CA    . ARG A 1 807  ? 115.659 114.298 105.950 1.00 59.62  ? 807  ARG A CA    1 
ATOM   5593 C  C     . ARG A 1 807  ? 116.790 114.769 105.044 1.00 59.62  ? 807  ARG A C     1 
ATOM   5594 O  O     . ARG A 1 807  ? 116.564 115.113 103.879 1.00 59.62  ? 807  ARG A O     1 
ATOM   5595 C  CB    . ARG A 1 807  ? 115.225 115.420 106.896 1.00 59.62  ? 807  ARG A CB    1 
ATOM   5596 C  CG    . ARG A 1 807  ? 115.219 116.807 106.264 1.00 59.62  ? 807  ARG A CG    1 
ATOM   5597 C  CD    . ARG A 1 807  ? 115.319 117.905 107.317 1.00 59.62  ? 807  ARG A CD    1 
ATOM   5598 N  NE    . ARG A 1 807  ? 114.109 118.011 108.128 1.00 59.62  ? 807  ARG A NE    1 
ATOM   5599 C  CZ    . ARG A 1 807  ? 113.087 118.811 107.845 1.00 59.62  ? 807  ARG A CZ    1 
ATOM   5600 N  NH1   . ARG A 1 807  ? 112.027 118.841 108.640 1.00 59.62  ? 807  ARG A NH1   1 
ATOM   5601 N  NH2   . ARG A 1 807  ? 113.125 119.586 106.770 1.00 59.62  ? 807  ARG A NH2   1 
ATOM   5602 N  N     . ILE A 1 808  ? 118.019 114.779 105.560 1.00 56.16  ? 808  ILE A N     1 
ATOM   5603 C  CA    . ILE A 1 808  ? 119.147 115.288 104.784 1.00 56.16  ? 808  ILE A CA    1 
ATOM   5604 C  C     . ILE A 1 808  ? 119.374 114.431 103.542 1.00 56.16  ? 808  ILE A C     1 
ATOM   5605 O  O     . ILE A 1 808  ? 119.630 114.949 102.449 1.00 56.16  ? 808  ILE A O     1 
ATOM   5606 C  CB    . ILE A 1 808  ? 120.407 115.371 105.663 1.00 56.16  ? 808  ILE A CB    1 
ATOM   5607 C  CG1   . ILE A 1 808  ? 120.274 116.524 106.659 1.00 56.16  ? 808  ILE A CG1   1 
ATOM   5608 C  CG2   . ILE A 1 808  ? 121.652 115.544 104.811 1.00 56.16  ? 808  ILE A CG2   1 
ATOM   5609 C  CD1   . ILE A 1 808  ? 120.120 117.875 106.000 1.00 56.16  ? 808  ILE A CD1   1 
ATOM   5610 N  N     . SER A 1 809  ? 119.278 113.108 103.688 1.00 55.63  ? 809  SER A N     1 
ATOM   5611 C  CA    . SER A 1 809  ? 119.499 112.219 102.549 1.00 55.63  ? 809  SER A CA    1 
ATOM   5612 C  C     . SER A 1 809  ? 118.481 112.473 101.443 1.00 55.63  ? 809  SER A C     1 
ATOM   5613 O  O     . SER A 1 809  ? 118.844 112.762 100.292 1.00 55.63  ? 809  SER A O     1 
ATOM   5614 C  CB    . SER A 1 809  ? 119.416 110.762 103.005 1.00 55.63  ? 809  SER A CB    1 
ATOM   5615 O  OG    . SER A 1 809  ? 120.437 110.438 103.925 1.00 55.63  ? 809  SER A OG    1 
ATOM   5616 N  N     . VAL A 1 810  ? 117.194 112.396 101.786 1.00 56.44  ? 810  VAL A N     1 
ATOM   5617 C  CA    . VAL A 1 810  ? 116.153 112.459 100.769 1.00 56.44  ? 810  VAL A CA    1 
ATOM   5618 C  C     . VAL A 1 810  ? 116.092 113.845 100.145 1.00 56.44  ? 810  VAL A C     1 
ATOM   5619 O  O     . VAL A 1 810  ? 115.856 113.981 98.941  1.00 56.44  ? 810  VAL A O     1 
ATOM   5620 C  CB    . VAL A 1 810  ? 114.795 112.032 101.357 1.00 56.44  ? 810  VAL A CB    1 
ATOM   5621 C  CG1   . VAL A 1 810  ? 114.878 110.610 101.882 1.00 56.44  ? 810  VAL A CG1   1 
ATOM   5622 C  CG2   . VAL A 1 810  ? 114.356 112.982 102.461 1.00 56.44  ? 810  VAL A CG2   1 
ATOM   5623 N  N     . ILE A 1 811  ? 116.311 114.892 100.940 1.00 57.01  ? 811  ILE A N     1 
ATOM   5624 C  CA    . ILE A 1 811  ? 116.228 116.248 100.405 1.00 57.01  ? 811  ILE A CA    1 
ATOM   5625 C  C     . ILE A 1 811  ? 117.304 116.466 99.349  1.00 57.01  ? 811  ILE A C     1 
ATOM   5626 O  O     . ILE A 1 811  ? 117.020 116.919 98.235  1.00 57.01  ? 811  ILE A O     1 
ATOM   5627 C  CB    . ILE A 1 811  ? 116.325 117.282 101.541 1.00 57.01  ? 811  ILE A CB    1 
ATOM   5628 C  CG1   . ILE A 1 811  ? 115.000 117.352 102.299 1.00 57.01  ? 811  ILE A CG1   1 
ATOM   5629 C  CG2   . ILE A 1 811  ? 116.690 118.648 100.992 1.00 57.01  ? 811  ILE A CG2   1 
ATOM   5630 C  CD1   . ILE A 1 811  ? 113.832 117.758 101.437 1.00 57.01  ? 811  ILE A CD1   1 
ATOM   5631 N  N     . LEU A 1 812  ? 118.554 116.130 99.677  1.00 54.69  ? 812  LEU A N     1 
ATOM   5632 C  CA    . LEU A 1 812  ? 119.635 116.286 98.709  1.00 54.69  ? 812  LEU A CA    1 
ATOM   5633 C  C     . LEU A 1 812  ? 119.393 115.437 97.468  1.00 54.69  ? 812  LEU A C     1 
ATOM   5634 O  O     . LEU A 1 812  ? 119.527 115.925 96.338  1.00 54.69  ? 812  LEU A O     1 
ATOM   5635 C  CB    . LEU A 1 812  ? 120.984 115.951 99.349  1.00 54.69  ? 812  LEU A CB    1 
ATOM   5636 C  CG    . LEU A 1 812  ? 121.706 117.039 100.160 1.00 54.69  ? 812  LEU A CG    1 
ATOM   5637 C  CD1   . LEU A 1 812  ? 122.086 118.202 99.252  1.00 54.69  ? 812  LEU A CD1   1 
ATOM   5638 C  CD2   . LEU A 1 812  ? 120.910 117.549 101.353 1.00 54.69  ? 812  LEU A CD2   1 
ATOM   5639 N  N     . GLN A 1 813  ? 119.007 114.168 97.653  1.00 55.46  ? 813  GLN A N     1 
ATOM   5640 C  CA    . GLN A 1 813  ? 118.777 113.304 96.496  1.00 55.46  ? 813  GLN A CA    1 
ATOM   5641 C  C     . GLN A 1 813  ? 117.682 113.863 95.594  1.00 55.46  ? 813  GLN A C     1 
ATOM   5642 O  O     . GLN A 1 813  ? 117.839 113.923 94.368  1.00 55.46  ? 813  GLN A O     1 
ATOM   5643 C  CB    . GLN A 1 813  ? 118.412 111.892 96.948  1.00 55.46  ? 813  GLN A CB    1 
ATOM   5644 C  CG    . GLN A 1 813  ? 119.541 111.106 97.569  1.00 55.46  ? 813  GLN A CG    1 
ATOM   5645 C  CD    . GLN A 1 813  ? 119.088 109.735 98.021  1.00 55.46  ? 813  GLN A CD    1 
ATOM   5646 O  OE1   . GLN A 1 813  ? 119.878 108.941 98.524  1.00 55.46  ? 813  GLN A OE1   1 
ATOM   5647 N  NE2   . GLN A 1 813  ? 117.804 109.450 97.842  1.00 55.46  ? 813  GLN A NE2   1 
ATOM   5648 N  N     . ASN A 1 814  ? 116.567 114.294 96.187  1.00 60.12  ? 814  ASN A N     1 
ATOM   5649 C  CA    . ASN A 1 814  ? 115.424 114.721 95.392  1.00 60.12  ? 814  ASN A CA    1 
ATOM   5650 C  C     . ASN A 1 814  ? 115.687 116.048 94.697  1.00 60.12  ? 814  ASN A C     1 
ATOM   5651 O  O     . ASN A 1 814  ? 115.344 116.208 93.521  1.00 60.12  ? 814  ASN A O     1 
ATOM   5652 C  CB    . ASN A 1 814  ? 114.181 114.802 96.275  1.00 60.12  ? 814  ASN A CB    1 
ATOM   5653 C  CG    . ASN A 1 814  ? 113.745 113.443 96.781  1.00 60.12  ? 814  ASN A CG    1 
ATOM   5654 O  OD1   . ASN A 1 814  ? 114.440 112.446 96.588  1.00 60.12  ? 814  ASN A OD1   1 
ATOM   5655 N  ND2   . ASN A 1 814  ? 112.593 113.395 97.437  1.00 60.12  ? 814  ASN A ND2   1 
ATOM   5656 N  N     . MET A 1 815  ? 116.289 117.017 95.395  1.00 59.44  ? 815  MET A N     1 
ATOM   5657 C  CA    . MET A 1 815  ? 116.617 118.273 94.728  1.00 59.44  ? 815  MET A CA    1 
ATOM   5658 C  C     . MET A 1 815  ? 117.627 118.057 93.609  1.00 59.44  ? 815  MET A C     1 
ATOM   5659 O  O     . MET A 1 815  ? 117.502 118.658 92.536  1.00 59.44  ? 815  MET A O     1 
ATOM   5660 C  CB    . MET A 1 815  ? 117.127 119.314 95.726  1.00 59.44  ? 815  MET A CB    1 
ATOM   5661 C  CG    . MET A 1 815  ? 116.262 119.485 96.961  1.00 59.44  ? 815  MET A CG    1 
ATOM   5662 S  SD    . MET A 1 815  ? 114.891 120.628 96.708  1.00 59.44  ? 815  MET A SD    1 
ATOM   5663 C  CE    . MET A 1 815  ? 113.567 119.750 97.535  1.00 59.44  ? 815  MET A CE    1 
ATOM   5664 N  N     . THR A 1 816  ? 118.629 117.199 93.828  1.00 54.35  ? 816  THR A N     1 
ATOM   5665 C  CA    . THR A 1 816  ? 119.598 116.936 92.769  1.00 54.35  ? 816  THR A CA    1 
ATOM   5666 C  C     . THR A 1 816  ? 118.937 116.290 91.557  1.00 54.35  ? 816  THR A C     1 
ATOM   5667 O  O     . THR A 1 816  ? 119.194 116.690 90.413  1.00 54.35  ? 816  THR A O     1 
ATOM   5668 C  CB    . THR A 1 816  ? 120.727 116.054 93.298  1.00 54.35  ? 816  THR A CB    1 
ATOM   5669 O  OG1   . THR A 1 816  ? 121.285 116.649 94.476  1.00 54.35  ? 816  THR A OG1   1 
ATOM   5670 C  CG2   . THR A 1 816  ? 121.813 115.905 92.250  1.00 54.35  ? 816  THR A CG2   1 
ATOM   5671 N  N     . SER A 1 817  ? 118.073 115.296 91.784  1.00 56.54  ? 817  SER A N     1 
ATOM   5672 C  CA    . SER A 1 817  ? 117.403 114.641 90.665  1.00 56.54  ? 817  SER A CA    1 
ATOM   5673 C  C     . SER A 1 817  ? 116.481 115.605 89.927  1.00 56.54  ? 817  SER A C     1 
ATOM   5674 O  O     . SER A 1 817  ? 116.431 115.604 88.690  1.00 56.54  ? 817  SER A O     1 
ATOM   5675 C  CB    . SER A 1 817  ? 116.625 113.423 91.160  1.00 56.54  ? 817  SER A CB    1 
ATOM   5676 O  OG    . SER A 1 817  ? 115.352 113.801 91.648  1.00 56.54  ? 817  SER A OG    1 
ATOM   5677 N  N     . LEU A 1 818  ? 115.744 116.437 90.668  1.00 56.80  ? 818  LEU A N     1 
ATOM   5678 C  CA    . LEU A 1 818  ? 114.853 117.402 90.033  1.00 56.80  ? 818  LEU A CA    1 
ATOM   5679 C  C     . LEU A 1 818  ? 115.635 118.417 89.210  1.00 56.80  ? 818  LEU A C     1 
ATOM   5680 O  O     . LEU A 1 818  ? 115.234 118.761 88.092  1.00 56.80  ? 818  LEU A O     1 
ATOM   5681 C  CB    . LEU A 1 818  ? 114.006 118.107 91.091  1.00 56.80  ? 818  LEU A CB    1 
ATOM   5682 C  CG    . LEU A 1 818  ? 112.772 117.349 91.582  1.00 56.80  ? 818  LEU A CG    1 
ATOM   5683 C  CD1   . LEU A 1 818  ? 112.044 118.147 92.652  1.00 56.80  ? 818  LEU A CD1   1 
ATOM   5684 C  CD2   . LEU A 1 818  ? 111.844 117.025 90.423  1.00 56.80  ? 818  LEU A CD2   1 
ATOM   5685 N  N     . LEU A 1 819  ? 116.753 118.911 89.747  1.00 55.66  ? 819  LEU A N     1 
ATOM   5686 C  CA    . LEU A 1 819  ? 117.571 119.859 89.000  1.00 55.66  ? 819  LEU A CA    1 
ATOM   5687 C  C     . LEU A 1 819  ? 118.140 119.222 87.741  1.00 55.66  ? 819  LEU A C     1 
ATOM   5688 O  O     . LEU A 1 819  ? 118.160 119.850 86.675  1.00 55.66  ? 819  LEU A O     1 
ATOM   5689 C  CB    . LEU A 1 819  ? 118.695 120.395 89.886  1.00 55.66  ? 819  LEU A CB    1 
ATOM   5690 C  CG    . LEU A 1 819  ? 119.755 121.242 89.181  1.00 55.66  ? 819  LEU A CG    1 
ATOM   5691 C  CD1   . LEU A 1 819  ? 119.195 122.609 88.825  1.00 55.66  ? 819  LEU A CD1   1 
ATOM   5692 C  CD2   . LEU A 1 819  ? 121.001 121.374 90.042  1.00 55.66  ? 819  LEU A CD2   1 
ATOM   5693 N  N     . THR A 1 820  ? 118.609 117.975 87.840  1.00 56.70  ? 820  THR A N     1 
ATOM   5694 C  CA    . THR A 1 820  ? 119.136 117.296 86.661  1.00 56.70  ? 820  THR A CA    1 
ATOM   5695 C  C     . THR A 1 820  ? 118.056 117.116 85.601  1.00 56.70  ? 820  THR A C     1 
ATOM   5696 O  O     . THR A 1 820  ? 118.295 117.353 84.410  1.00 56.70  ? 820  THR A O     1 
ATOM   5697 C  CB    . THR A 1 820  ? 119.733 115.945 87.052  1.00 56.70  ? 820  THR A CB    1 
ATOM   5698 O  OG1   . THR A 1 820  ? 120.728 116.137 88.064  1.00 56.70  ? 820  THR A OG1   1 
ATOM   5699 C  CG2   . THR A 1 820  ? 120.376 115.281 85.845  1.00 56.70  ? 820  THR A CG2   1 
ATOM   5700 N  N     . SER A 1 821  ? 116.853 116.711 86.017  1.00 57.64  ? 821  SER A N     1 
ATOM   5701 C  CA    . SER A 1 821  ? 115.762 116.544 85.063  1.00 57.64  ? 821  SER A CA    1 
ATOM   5702 C  C     . SER A 1 821  ? 115.381 117.870 84.418  1.00 57.64  ? 821  SER A C     1 
ATOM   5703 O  O     . SER A 1 821  ? 115.084 117.923 83.219  1.00 57.64  ? 821  SER A O     1 
ATOM   5704 C  CB    . SER A 1 821  ? 114.553 115.920 85.754  1.00 57.64  ? 821  SER A CB    1 
ATOM   5705 O  OG    . SER A 1 821  ? 113.472 115.780 84.851  1.00 57.64  ? 821  SER A OG    1 
ATOM   5706 N  N     . PHE A 1 822  ? 115.373 118.953 85.197  1.00 61.23  ? 822  PHE A N     1 
ATOM   5707 C  CA    . PHE A 1 822  ? 115.039 120.259 84.639  1.00 61.23  ? 822  PHE A CA    1 
ATOM   5708 C  C     . PHE A 1 822  ? 116.095 120.721 83.642  1.00 61.23  ? 822  PHE A C     1 
ATOM   5709 O  O     . PHE A 1 822  ? 115.764 121.309 82.605  1.00 61.23  ? 822  PHE A O     1 
ATOM   5710 C  CB    . PHE A 1 822  ? 114.868 121.280 85.764  1.00 61.23  ? 822  PHE A CB    1 
ATOM   5711 C  CG    . PHE A 1 822  ? 113.578 121.134 86.522  1.00 61.23  ? 822  PHE A CG    1 
ATOM   5712 C  CD1   . PHE A 1 822  ? 112.608 120.239 86.101  1.00 61.23  ? 822  PHE A CD1   1 
ATOM   5713 C  CD2   . PHE A 1 822  ? 113.338 121.886 87.659  1.00 61.23  ? 822  PHE A CD2   1 
ATOM   5714 C  CE1   . PHE A 1 822  ? 111.423 120.100 86.797  1.00 61.23  ? 822  PHE A CE1   1 
ATOM   5715 C  CE2   . PHE A 1 822  ? 112.154 121.752 88.359  1.00 61.23  ? 822  PHE A CE2   1 
ATOM   5716 C  CZ    . PHE A 1 822  ? 111.196 120.858 87.927  1.00 61.23  ? 822  PHE A CZ    1 
ATOM   5717 N  N     . ILE A 1 823  ? 117.372 120.464 83.934  1.00 59.32  ? 823  ILE A N     1 
ATOM   5718 C  CA    . ILE A 1 823  ? 118.428 120.793 82.980  1.00 59.32  ? 823  ILE A CA    1 
ATOM   5719 C  C     . ILE A 1 823  ? 118.258 119.984 81.700  1.00 59.32  ? 823  ILE A C     1 
ATOM   5720 O  O     . ILE A 1 823  ? 118.418 120.506 80.589  1.00 59.32  ? 823  ILE A O     1 
ATOM   5721 C  CB    . ILE A 1 823  ? 119.814 120.573 83.614  1.00 59.32  ? 823  ILE A CB    1 
ATOM   5722 C  CG1   . ILE A 1 823  ? 120.021 121.526 84.792  1.00 59.32  ? 823  ILE A CG1   1 
ATOM   5723 C  CG2   . ILE A 1 823  ? 120.913 120.764 82.583  1.00 59.32  ? 823  ILE A CG2   1 
ATOM   5724 C  CD1   . ILE A 1 823  ? 119.619 122.953 84.503  1.00 59.32  ? 823  ILE A CD1   1 
ATOM   5725 N  N     . VAL A 1 824  ? 117.927 118.698 81.834  1.00 63.06  ? 824  VAL A N     1 
ATOM   5726 C  CA    . VAL A 1 824  ? 117.700 117.865 80.654  1.00 63.06  ? 824  VAL A CA    1 
ATOM   5727 C  C     . VAL A 1 824  ? 116.531 118.400 79.838  1.00 63.06  ? 824  VAL A C     1 
ATOM   5728 O  O     . VAL A 1 824  ? 116.569 118.414 78.602  1.00 63.06  ? 824  VAL A O     1 
ATOM   5729 C  CB    . VAL A 1 824  ? 117.480 116.399 81.069  1.00 63.06  ? 824  VAL A CB    1 
ATOM   5730 C  CG1   . VAL A 1 824  ? 117.063 115.560 79.867  1.00 63.06  ? 824  VAL A CG1   1 
ATOM   5731 C  CG2   . VAL A 1 824  ? 118.748 115.845 81.699  1.00 63.06  ? 824  VAL A CG2   1 
ATOM   5732 N  N     . ALA A 1 825  ? 115.473 118.849 80.517  1.00 63.68  ? 825  ALA A N     1 
ATOM   5733 C  CA    . ALA A 1 825  ? 114.344 119.452 79.817  1.00 63.68  ? 825  ALA A CA    1 
ATOM   5734 C  C     . ALA A 1 825  ? 114.766 120.721 79.086  1.00 63.68  ? 825  ALA A C     1 
ATOM   5735 O  O     . ALA A 1 825  ? 114.330 120.967 77.956  1.00 63.68  ? 825  ALA A O     1 
ATOM   5736 C  CB    . ALA A 1 825  ? 113.214 119.742 80.802  1.00 63.68  ? 825  ALA A CB    1 
ATOM   5737 N  N     . PHE A 1 826  ? 115.614 121.538 79.719  1.00 66.99  ? 826  PHE A N     1 
ATOM   5738 C  CA    . PHE A 1 826  ? 116.178 122.706 79.044  1.00 66.99  ? 826  PHE A CA    1 
ATOM   5739 C  C     . PHE A 1 826  ? 116.934 122.312 77.782  1.00 66.99  ? 826  PHE A C     1 
ATOM   5740 O  O     . PHE A 1 826  ? 116.876 123.018 76.769  1.00 66.99  ? 826  PHE A O     1 
ATOM   5741 C  CB    . PHE A 1 826  ? 117.110 123.472 79.983  1.00 66.99  ? 826  PHE A CB    1 
ATOM   5742 C  CG    . PHE A 1 826  ? 116.404 124.250 81.051  1.00 66.99  ? 826  PHE A CG    1 
ATOM   5743 C  CD1   . PHE A 1 826  ? 115.054 124.525 80.949  1.00 66.99  ? 826  PHE A CD1   1 
ATOM   5744 C  CD2   . PHE A 1 826  ? 117.098 124.718 82.154  1.00 66.99  ? 826  PHE A CD2   1 
ATOM   5745 C  CE1   . PHE A 1 826  ? 114.405 125.247 81.930  1.00 66.99  ? 826  PHE A CE1   1 
ATOM   5746 C  CE2   . PHE A 1 826  ? 116.455 125.439 83.138  1.00 66.99  ? 826  PHE A CE2   1 
ATOM   5747 C  CZ    . PHE A 1 826  ? 115.107 125.704 83.025  1.00 66.99  ? 826  PHE A CZ    1 
ATOM   5748 N  N     . ILE A 1 827  ? 117.666 121.198 77.834  1.00 60.99  ? 827  ILE A N     1 
ATOM   5749 C  CA    . ILE A 1 827  ? 118.509 120.806 76.703  1.00 60.99  ? 827  ILE A CA    1 
ATOM   5750 C  C     . ILE A 1 827  ? 117.666 120.584 75.452  1.00 60.99  ? 827  ILE A C     1 
ATOM   5751 O  O     . ILE A 1 827  ? 118.017 121.039 74.357  1.00 60.99  ? 827  ILE A O     1 
ATOM   5752 C  CB    . ILE A 1 827  ? 119.337 119.555 77.050  1.00 60.99  ? 827  ILE A CB    1 
ATOM   5753 C  CG1   . ILE A 1 827  ? 120.285 119.840 78.215  1.00 60.99  ? 827  ILE A CG1   1 
ATOM   5754 C  CG2   . ILE A 1 827  ? 120.115 119.077 75.835  1.00 60.99  ? 827  ILE A CG2   1 
ATOM   5755 C  CD1   . ILE A 1 827  ? 121.037 121.147 78.090  1.00 60.99  ? 827  ILE A CD1   1 
ATOM   5756 N  N     . VAL A 1 828  ? 116.539 119.892 75.594  1.00 64.02  ? 828  VAL A N     1 
ATOM   5757 C  CA    . VAL A 1 828  ? 115.740 119.534 74.427  1.00 64.02  ? 828  VAL A CA    1 
ATOM   5758 C  C     . VAL A 1 828  ? 114.686 120.588 74.084  1.00 64.02  ? 828  VAL A C     1 
ATOM   5759 O  O     . VAL A 1 828  ? 114.320 120.731 72.913  1.00 64.02  ? 828  VAL A O     1 
ATOM   5760 C  CB    . VAL A 1 828  ? 115.095 118.156 74.637  1.00 64.02  ? 828  VAL A CB    1 
ATOM   5761 C  CG1   . VAL A 1 828  ? 116.146 117.065 74.547  1.00 64.02  ? 828  VAL A CG1   1 
ATOM   5762 C  CG2   . VAL A 1 828  ? 114.407 118.105 75.984  1.00 64.02  ? 828  VAL A CG2   1 
ATOM   5763 N  N     . GLU A 1 829  ? 114.188 121.330 75.071  1.00 71.53  ? 829  GLU A N     1 
ATOM   5764 C  CA    . GLU A 1 829  ? 113.179 122.352 74.831  1.00 71.53  ? 829  GLU A CA    1 
ATOM   5765 C  C     . GLU A 1 829  ? 113.406 123.520 75.779  1.00 71.53  ? 829  GLU A C     1 
ATOM   5766 O  O     . GLU A 1 829  ? 114.030 123.378 76.832  1.00 71.53  ? 829  GLU A O     1 
ATOM   5767 C  CB    . GLU A 1 829  ? 111.760 121.798 75.007  1.00 71.53  ? 829  GLU A CB    1 
ATOM   5768 C  CG    . GLU A 1 829  ? 111.188 121.175 73.752  1.00 71.53  ? 829  GLU A CG    1 
ATOM   5769 C  CD    . GLU A 1 829  ? 111.102 122.165 72.611  1.00 71.53  ? 829  GLU A CD    1 
ATOM   5770 O  OE1   . GLU A 1 829  ? 110.680 123.314 72.852  1.00 71.53  ? 829  GLU A OE1   1 
ATOM   5771 O  OE2   . GLU A 1 829  ? 111.462 121.795 71.474  1.00 71.53  ? 829  GLU A OE2   1 
ATOM   5772 N  N     . TRP A 1 830  ? 112.895 124.686 75.395  1.00 71.56  ? 830  TRP A N     1 
ATOM   5773 C  CA    . TRP A 1 830  ? 113.028 125.873 76.231  1.00 71.56  ? 830  TRP A CA    1 
ATOM   5774 C  C     . TRP A 1 830  ? 111.687 126.447 76.659  1.00 71.56  ? 830  TRP A C     1 
ATOM   5775 O  O     . TRP A 1 830  ? 111.488 126.713 77.850  1.00 71.56  ? 830  TRP A O     1 
ATOM   5776 C  CB    . TRP A 1 830  ? 113.864 126.946 75.512  1.00 71.56  ? 830  TRP A CB    1 
ATOM   5777 C  CG    . TRP A 1 830  ? 113.391 127.298 74.134  1.00 71.56  ? 830  TRP A CG    1 
ATOM   5778 C  CD1   . TRP A 1 830  ? 113.401 126.496 73.029  1.00 71.56  ? 830  TRP A CD1   1 
ATOM   5779 C  CD2   . TRP A 1 830  ? 112.848 128.554 73.713  1.00 71.56  ? 830  TRP A CD2   1 
ATOM   5780 N  NE1   . TRP A 1 830  ? 112.893 127.174 71.948  1.00 71.56  ? 830  TRP A NE1   1 
ATOM   5781 C  CE2   . TRP A 1 830  ? 112.547 128.439 72.341  1.00 71.56  ? 830  TRP A CE2   1 
ATOM   5782 C  CE3   . TRP A 1 830  ? 112.586 129.763 74.362  1.00 71.56  ? 830  TRP A CE3   1 
ATOM   5783 C  CZ2   . TRP A 1 830  ? 111.996 129.487 71.609  1.00 71.56  ? 830  TRP A CZ2   1 
ATOM   5784 C  CZ3   . TRP A 1 830  ? 112.040 130.802 73.634  1.00 71.56  ? 830  TRP A CZ3   1 
ATOM   5785 C  CH2   . TRP A 1 830  ? 111.750 130.658 72.272  1.00 71.56  ? 830  TRP A CH2   1 
ATOM   5786 N  N     . ARG A 1 831  ? 110.756 126.650 75.724  1.00 71.77  ? 831  ARG A N     1 
ATOM   5787 C  CA    . ARG A 1 831  ? 109.459 127.208 76.095  1.00 71.77  ? 831  ARG A CA    1 
ATOM   5788 C  C     . ARG A 1 831  ? 108.676 126.256 76.989  1.00 71.77  ? 831  ARG A C     1 
ATOM   5789 O  O     . ARG A 1 831  ? 108.062 126.684 77.973  1.00 71.77  ? 831  ARG A O     1 
ATOM   5790 C  CB    . ARG A 1 831  ? 108.654 127.550 74.843  1.00 71.77  ? 831  ARG A CB    1 
ATOM   5791 C  CG    . ARG A 1 831  ? 109.175 128.755 74.084  1.00 71.77  ? 831  ARG A CG    1 
ATOM   5792 C  CD    . ARG A 1 831  ? 108.103 129.825 73.960  1.00 71.77  ? 831  ARG A CD    1 
ATOM   5793 N  NE    . ARG A 1 831  ? 108.658 131.115 73.562  1.00 71.77  ? 831  ARG A NE    1 
ATOM   5794 C  CZ    . ARG A 1 831  ? 107.971 132.252 73.555  1.00 71.77  ? 831  ARG A CZ    1 
ATOM   5795 N  NH1   . ARG A 1 831  ? 106.699 132.262 73.929  1.00 71.77  ? 831  ARG A NH1   1 
ATOM   5796 N  NH2   . ARG A 1 831  ? 108.556 133.380 73.177  1.00 71.77  ? 831  ARG A NH2   1 
ATOM   5797 N  N     . VAL A 1 832  ? 108.680 124.963 76.661  1.00 70.39  ? 832  VAL A N     1 
ATOM   5798 C  CA    . VAL A 1 832  ? 107.930 123.993 77.453  1.00 70.39  ? 832  VAL A CA    1 
ATOM   5799 C  C     . VAL A 1 832  ? 108.520 123.874 78.852  1.00 70.39  ? 832  VAL A C     1 
ATOM   5800 O  O     . VAL A 1 832  ? 107.789 123.819 79.849  1.00 70.39  ? 832  VAL A O     1 
ATOM   5801 C  CB    . VAL A 1 832  ? 107.893 122.631 76.734  1.00 70.39  ? 832  VAL A CB    1 
ATOM   5802 C  CG1   . VAL A 1 832  ? 107.053 121.638 77.518  1.00 70.39  ? 832  VAL A CG1   1 
ATOM   5803 C  CG2   . VAL A 1 832  ? 107.351 122.792 75.324  1.00 70.39  ? 832  VAL A CG2   1 
ATOM   5804 N  N     . SER A 1 833  ? 109.850 123.837 78.951  1.00 74.28  ? 833  SER A N     1 
ATOM   5805 C  CA    . SER A 1 833  ? 110.487 123.664 80.251  1.00 74.28  ? 833  SER A CA    1 
ATOM   5806 C  C     . SER A 1 833  ? 110.312 124.892 81.139  1.00 74.28  ? 833  SER A C     1 
ATOM   5807 O  O     . SER A 1 833  ? 110.258 124.765 82.368  1.00 74.28  ? 833  SER A O     1 
ATOM   5808 C  CB    . SER A 1 833  ? 111.966 123.341 80.068  1.00 74.28  ? 833  SER A CB    1 
ATOM   5809 O  OG    . SER A 1 833  ? 112.518 122.827 81.265  1.00 74.28  ? 833  SER A OG    1 
ATOM   5810 N  N     . LEU A 1 834  ? 110.229 126.085 80.547  1.00 75.27  ? 834  LEU A N     1 
ATOM   5811 C  CA    . LEU A 1 834  ? 109.914 127.265 81.344  1.00 75.27  ? 834  LEU A CA    1 
ATOM   5812 C  C     . LEU A 1 834  ? 108.540 127.127 81.986  1.00 75.27  ? 834  LEU A C     1 
ATOM   5813 O  O     . LEU A 1 834  ? 108.332 127.546 83.131  1.00 75.27  ? 834  LEU A O     1 
ATOM   5814 C  CB    . LEU A 1 834  ? 109.983 128.522 80.477  1.00 75.27  ? 834  LEU A CB    1 
ATOM   5815 C  CG    . LEU A 1 834  ? 111.386 129.067 80.202  1.00 75.27  ? 834  LEU A CG    1 
ATOM   5816 C  CD1   . LEU A 1 834  ? 111.316 130.393 79.461  1.00 75.27  ? 834  LEU A CD1   1 
ATOM   5817 C  CD2   . LEU A 1 834  ? 112.171 129.208 81.496  1.00 75.27  ? 834  LEU A CD2   1 
ATOM   5818 N  N     . LEU A 1 835  ? 107.594 126.523 81.264  1.00 72.97  ? 835  LEU A N     1 
ATOM   5819 C  CA    . LEU A 1 835  ? 106.268 126.288 81.822  1.00 72.97  ? 835  LEU A CA    1 
ATOM   5820 C  C     . LEU A 1 835  ? 106.327 125.341 83.017  1.00 72.97  ? 835  LEU A C     1 
ATOM   5821 O  O     . LEU A 1 835  ? 105.667 125.578 84.035  1.00 72.97  ? 835  LEU A O     1 
ATOM   5822 C  CB    . LEU A 1 835  ? 105.339 125.737 80.740  1.00 72.97  ? 835  LEU A CB    1 
ATOM   5823 C  CG    . LEU A 1 835  ? 103.865 125.563 81.105  1.00 72.97  ? 835  LEU A CG    1 
ATOM   5824 C  CD1   . LEU A 1 835  ? 103.247 126.901 81.467  1.00 72.97  ? 835  LEU A CD1   1 
ATOM   5825 C  CD2   . LEU A 1 835  ? 103.110 124.921 79.956  1.00 72.97  ? 835  LEU A CD2   1 
ATOM   5826 N  N     . ILE A 1 836  ? 107.111 124.264 82.916  1.00 73.96  ? 836  ILE A N     1 
ATOM   5827 C  CA    . ILE A 1 836  ? 107.180 123.315 84.024  1.00 73.96  ? 836  ILE A CA    1 
ATOM   5828 C  C     . ILE A 1 836  ? 107.896 123.932 85.219  1.00 73.96  ? 836  ILE A C     1 
ATOM   5829 O  O     . ILE A 1 836  ? 107.540 123.664 86.372  1.00 73.96  ? 836  ILE A O     1 
ATOM   5830 C  CB    . ILE A 1 836  ? 107.825 121.984 83.587  1.00 73.96  ? 836  ILE A CB    1 
ATOM   5831 C  CG1   . ILE A 1 836  ? 107.542 120.910 84.635  1.00 73.96  ? 836  ILE A CG1   1 
ATOM   5832 C  CG2   . ILE A 1 836  ? 109.321 122.102 83.401  1.00 73.96  ? 836  ILE A CG2   1 
ATOM   5833 C  CD1   . ILE A 1 836  ? 106.090 120.775 84.990  1.00 73.96  ? 836  ILE A CD1   1 
ATOM   5834 N  N     . LEU A 1 837  ? 108.910 124.768 84.975  1.00 75.48  ? 837  LEU A N     1 
ATOM   5835 C  CA    . LEU A 1 837  ? 109.521 125.478 86.093  1.00 75.48  ? 837  LEU A CA    1 
ATOM   5836 C  C     . LEU A 1 837  ? 108.627 126.591 86.622  1.00 75.48  ? 837  LEU A C     1 
ATOM   5837 O  O     . LEU A 1 837  ? 108.887 127.114 87.711  1.00 75.48  ? 837  LEU A O     1 
ATOM   5838 C  CB    . LEU A 1 837  ? 110.889 126.040 85.705  1.00 75.48  ? 837  LEU A CB    1 
ATOM   5839 C  CG    . LEU A 1 837  ? 112.074 125.092 85.923  1.00 75.48  ? 837  LEU A CG    1 
ATOM   5840 C  CD1   . LEU A 1 837  ? 112.133 123.989 84.874  1.00 75.48  ? 837  LEU A CD1   1 
ATOM   5841 C  CD2   . LEU A 1 837  ? 113.385 125.861 85.990  1.00 75.48  ? 837  LEU A CD2   1 
ATOM   5842 N  N     . GLY A 1 838  ? 107.585 126.963 85.881  1.00 77.38  ? 838  GLY A N     1 
ATOM   5843 C  CA    . GLY A 1 838  ? 106.570 127.855 86.394  1.00 77.38  ? 838  GLY A CA    1 
ATOM   5844 C  C     . GLY A 1 838  ? 105.521 127.196 87.259  1.00 77.38  ? 838  GLY A C     1 
ATOM   5845 O  O     . GLY A 1 838  ? 104.626 127.878 87.764  1.00 77.38  ? 838  GLY A O     1 
ATOM   5846 N  N     . THR A 1 839  ? 105.607 125.878 87.449  1.00 75.54  ? 839  THR A N     1 
ATOM   5847 C  CA    . THR A 1 839  ? 104.651 125.128 88.252  1.00 75.54  ? 839  THR A CA    1 
ATOM   5848 C  C     . THR A 1 839  ? 105.201 124.756 89.626  1.00 75.54  ? 839  THR A C     1 
ATOM   5849 O  O     . THR A 1 839  ? 104.417 124.477 90.540  1.00 75.54  ? 839  THR A O     1 
ATOM   5850 C  CB    . THR A 1 839  ? 104.225 123.861 87.490  1.00 75.54  ? 839  THR A CB    1 
ATOM   5851 O  OG1   . THR A 1 839  ? 103.621 124.238 86.247  1.00 75.54  ? 839  THR A OG1   1 
ATOM   5852 C  CG2   . THR A 1 839  ? 103.216 123.047 88.282  1.00 75.54  ? 839  THR A CG2   1 
ATOM   5853 N  N     . PHE A 1 840  ? 106.519 124.807 89.803  1.00 76.99  ? 840  PHE A N     1 
ATOM   5854 C  CA    . PHE A 1 840  ? 107.130 124.491 91.092  1.00 76.99  ? 840  PHE A CA    1 
ATOM   5855 C  C     . PHE A 1 840  ? 106.542 125.257 92.275  1.00 76.99  ? 840  PHE A C     1 
ATOM   5856 O  O     . PHE A 1 840  ? 106.418 124.653 93.357  1.00 76.99  ? 840  PHE A O     1 
ATOM   5857 C  CB    . PHE A 1 840  ? 108.645 124.725 91.001  1.00 76.99  ? 840  PHE A CB    1 
ATOM   5858 C  CG    . PHE A 1 840  ? 109.389 124.391 92.263  1.00 76.99  ? 840  PHE A CG    1 
ATOM   5859 C  CD1   . PHE A 1 840  ? 109.633 123.074 92.612  1.00 76.99  ? 840  PHE A CD1   1 
ATOM   5860 C  CD2   . PHE A 1 840  ? 109.852 125.397 93.096  1.00 76.99  ? 840  PHE A CD2   1 
ATOM   5861 C  CE1   . PHE A 1 840  ? 110.321 122.765 93.773  1.00 76.99  ? 840  PHE A CE1   1 
ATOM   5862 C  CE2   . PHE A 1 840  ? 110.541 125.095 94.258  1.00 76.99  ? 840  PHE A CE2   1 
ATOM   5863 C  CZ    . PHE A 1 840  ? 110.775 123.778 94.597  1.00 76.99  ? 840  PHE A CZ    1 
ATOM   5864 N  N     . PRO A 1 841  ? 106.197 126.564 92.172  1.00 75.99  ? 841  PRO A N     1 
ATOM   5865 C  CA    . PRO A 1 841  ? 105.595 127.249 93.326  1.00 75.99  ? 841  PRO A CA    1 
ATOM   5866 C  C     . PRO A 1 841  ? 104.355 126.560 93.877  1.00 75.99  ? 841  PRO A C     1 
ATOM   5867 O  O     . PRO A 1 841  ? 104.176 126.514 95.096  1.00 75.99  ? 841  PRO A O     1 
ATOM   5868 C  CB    . PRO A 1 841  ? 105.261 128.641 92.775  1.00 75.99  ? 841  PRO A CB    1 
ATOM   5869 C  CG    . PRO A 1 841  ? 106.236 128.851 91.689  1.00 75.99  ? 841  PRO A CG    1 
ATOM   5870 C  CD    . PRO A 1 841  ? 106.480 127.509 91.074  1.00 75.99  ? 841  PRO A CD    1 
ATOM   5871 N  N     . LEU A 1 842  ? 103.503 126.009 93.010  1.00 75.71  ? 842  LEU A N     1 
ATOM   5872 C  CA    . LEU A 1 842  ? 102.311 125.313 93.481  1.00 75.71  ? 842  LEU A CA    1 
ATOM   5873 C  C     . LEU A 1 842  ? 102.669 124.125 94.370  1.00 75.71  ? 842  LEU A C     1 
ATOM   5874 O  O     . LEU A 1 842  ? 102.136 123.970 95.477  1.00 75.71  ? 842  LEU A O     1 
ATOM   5875 C  CB    . LEU A 1 842  ? 101.466 124.854 92.287  1.00 75.71  ? 842  LEU A CB    1 
ATOM   5876 C  CG    . LEU A 1 842  ? 100.519 125.869 91.641  1.00 75.71  ? 842  LEU A CG    1 
ATOM   5877 C  CD1   . LEU A 1 842  ? 101.278 126.859 90.769  1.00 75.71  ? 842  LEU A CD1   1 
ATOM   5878 C  CD2   . LEU A 1 842  ? 99.443  125.154 90.835  1.00 75.71  ? 842  LEU A CD2   1 
ATOM   5879 N  N     . LEU A 1 843  ? 103.586 123.280 93.895  1.00 70.70  ? 843  LEU A N     1 
ATOM   5880 C  CA    . LEU A 1 843  ? 103.972 122.095 94.654  1.00 70.70  ? 843  LEU A CA    1 
ATOM   5881 C  C     . LEU A 1 843  ? 104.665 122.472 95.957  1.00 70.70  ? 843  LEU A C     1 
ATOM   5882 O  O     . LEU A 1 843  ? 104.405 121.873 97.009  1.00 70.70  ? 843  LEU A O     1 
ATOM   5883 C  CB    . LEU A 1 843  ? 104.870 121.192 93.806  1.00 70.70  ? 843  LEU A CB    1 
ATOM   5884 C  CG    . LEU A 1 843  ? 104.210 120.224 92.818  1.00 70.70  ? 843  LEU A CG    1 
ATOM   5885 C  CD1   . LEU A 1 843  ? 103.371 119.196 93.564  1.00 70.70  ? 843  LEU A CD1   1 
ATOM   5886 C  CD2   . LEU A 1 843  ? 103.377 120.940 91.762  1.00 70.70  ? 843  LEU A CD2   1 
ATOM   5887 N  N     . VAL A 1 844  ? 105.562 123.461 95.909  1.00 72.34  ? 844  VAL A N     1 
ATOM   5888 C  CA    . VAL A 1 844  ? 106.288 123.835 97.120  1.00 72.34  ? 844  VAL A CA    1 
ATOM   5889 C  C     . VAL A 1 844  ? 105.339 124.463 98.135  1.00 72.34  ? 844  VAL A C     1 
ATOM   5890 O  O     . VAL A 1 844  ? 105.482 124.264 99.346  1.00 72.34  ? 844  VAL A O     1 
ATOM   5891 C  CB    . VAL A 1 844  ? 107.481 124.754 96.790  1.00 72.34  ? 844  VAL A CB    1 
ATOM   5892 C  CG1   . VAL A 1 844  ? 107.024 126.132 96.362  1.00 72.34  ? 844  VAL A CG1   1 
ATOM   5893 C  CG2   . VAL A 1 844  ? 108.418 124.849 97.985  1.00 72.34  ? 844  VAL A CG2   1 
ATOM   5894 N  N     . LEU A 1 845  ? 104.334 125.206 97.660  1.00 71.66  ? 845  LEU A N     1 
ATOM   5895 C  CA    . LEU A 1 845  ? 103.354 125.781 98.575  1.00 71.66  ? 845  LEU A CA    1 
ATOM   5896 C  C     . LEU A 1 845  ? 102.476 124.698 99.186  1.00 71.66  ? 845  LEU A C     1 
ATOM   5897 O  O     . LEU A 1 845  ? 102.115 124.774 100.365 1.00 71.66  ? 845  LEU A O     1 
ATOM   5898 C  CB    . LEU A 1 845  ? 102.509 126.828 97.848  1.00 71.66  ? 845  LEU A CB    1 
ATOM   5899 C  CG    . LEU A 1 845  ? 101.624 127.749 98.695  1.00 71.66  ? 845  LEU A CG    1 
ATOM   5900 C  CD1   . LEU A 1 845  ? 101.519 129.117 98.042  1.00 71.66  ? 845  LEU A CD1   1 
ATOM   5901 C  CD2   . LEU A 1 845  ? 100.236 127.161 98.908  1.00 71.66  ? 845  LEU A CD2   1 
ATOM   5902 N  N     . ALA A 1 846  ? 102.120 123.678 98.400  1.00 69.18  ? 846  ALA A N     1 
ATOM   5903 C  CA    . ALA A 1 846  ? 101.353 122.562 98.948  1.00 69.18  ? 846  ALA A CA    1 
ATOM   5904 C  C     . ALA A 1 846  ? 102.147 121.834 100.029 1.00 69.18  ? 846  ALA A C     1 
ATOM   5905 O  O     . ALA A 1 846  ? 101.613 121.498 101.095 1.00 69.18  ? 846  ALA A O     1 
ATOM   5906 C  CB    . ALA A 1 846  ? 100.952 121.602 97.829  1.00 69.18  ? 846  ALA A CB    1 
ATOM   5907 N  N     . ASN A 1 847  ? 103.434 121.591 99.771  1.00 66.65  ? 847  ASN A N     1 
ATOM   5908 C  CA    . ASN A 1 847  ? 104.275 120.940 100.771 1.00 66.65  ? 847  ASN A CA    1 
ATOM   5909 C  C     . ASN A 1 847  ? 104.447 121.812 102.010 1.00 66.65  ? 847  ASN A C     1 
ATOM   5910 O  O     . ASN A 1 847  ? 104.488 121.304 103.136 1.00 66.65  ? 847  ASN A O     1 
ATOM   5911 C  CB    . ASN A 1 847  ? 105.633 120.585 100.166 1.00 66.65  ? 847  ASN A CB    1 
ATOM   5912 C  CG    . ASN A 1 847  ? 105.518 119.595 99.026  1.00 66.65  ? 847  ASN A CG    1 
ATOM   5913 O  OD1   . ASN A 1 847  ? 104.423 119.149 98.688  1.00 66.65  ? 847  ASN A OD1   1 
ATOM   5914 N  ND2   . ASN A 1 847  ? 106.651 119.243 98.430  1.00 66.65  ? 847  ASN A ND2   1 
ATOM   5915 N  N     . PHE A 1 848  ? 104.552 123.129 101.824 1.00 71.44  ? 848  PHE A N     1 
ATOM   5916 C  CA    . PHE A 1 848  ? 104.645 124.033 102.965 1.00 71.44  ? 848  PHE A CA    1 
ATOM   5917 C  C     . PHE A 1 848  ? 103.369 124.005 103.795 1.00 71.44  ? 848  PHE A C     1 
ATOM   5918 O  O     . PHE A 1 848  ? 103.417 124.046 105.028 1.00 71.44  ? 848  PHE A O     1 
ATOM   5919 C  CB    . PHE A 1 848  ? 104.954 125.452 102.489 1.00 71.44  ? 848  PHE A CB    1 
ATOM   5920 C  CG    . PHE A 1 848  ? 106.394 125.666 102.126 1.00 71.44  ? 848  PHE A CG    1 
ATOM   5921 C  CD1   . PHE A 1 848  ? 107.363 124.762 102.528 1.00 71.44  ? 848  PHE A CD1   1 
ATOM   5922 C  CD2   . PHE A 1 848  ? 106.781 126.772 101.388 1.00 71.44  ? 848  PHE A CD2   1 
ATOM   5923 C  CE1   . PHE A 1 848  ? 108.691 124.955 102.200 1.00 71.44  ? 848  PHE A CE1   1 
ATOM   5924 C  CE2   . PHE A 1 848  ? 108.109 126.970 101.055 1.00 71.44  ? 848  PHE A CE2   1 
ATOM   5925 C  CZ    . PHE A 1 848  ? 109.064 126.060 101.463 1.00 71.44  ? 848  PHE A CZ    1 
ATOM   5926 N  N     . ALA A 1 849  ? 102.212 123.946 103.133 1.00 70.40  ? 849  ALA A N     1 
ATOM   5927 C  CA    . ALA A 1 849  ? 100.951 123.828 103.857 1.00 70.40  ? 849  ALA A CA    1 
ATOM   5928 C  C     . ALA A 1 849  ? 100.903 122.529 104.652 1.00 70.40  ? 849  ALA A C     1 
ATOM   5929 O  O     . ALA A 1 849  ? 100.473 122.508 105.813 1.00 70.40  ? 849  ALA A O     1 
ATOM   5930 C  CB    . ALA A 1 849  ? 99.776  123.909 102.881 1.00 70.40  ? 849  ALA A CB    1 
ATOM   5931 N  N     . GLN A 1 850  ? 101.348 121.431 104.035 1.00 65.78  ? 850  GLN A N     1 
ATOM   5932 C  CA    . GLN A 1 850  ? 101.448 120.158 104.744 1.00 65.78  ? 850  GLN A CA    1 
ATOM   5933 C  C     . GLN A 1 850  ? 102.317 120.290 105.988 1.00 65.78  ? 850  GLN A C     1 
ATOM   5934 O  O     . GLN A 1 850  ? 101.939 119.858 107.082 1.00 65.78  ? 850  GLN A O     1 
ATOM   5935 C  CB    . GLN A 1 850  ? 102.024 119.085 103.821 1.00 65.78  ? 850  GLN A CB    1 
ATOM   5936 C  CG    . GLN A 1 850  ? 101.134 118.665 102.677 1.00 65.78  ? 850  GLN A CG    1 
ATOM   5937 C  CD    . GLN A 1 850  ? 101.190 117.171 102.453 1.00 65.78  ? 850  GLN A CD    1 
ATOM   5938 O  OE1   . GLN A 1 850  ? 102.075 116.491 102.970 1.00 65.78  ? 850  GLN A OE1   1 
ATOM   5939 N  NE2   . GLN A 1 850  ? 100.254 116.653 101.674 1.00 65.78  ? 850  GLN A NE2   1 
ATOM   5940 N  N     . GLN A 1 851  ? 103.499 120.884 105.826 1.00 71.47  ? 851  GLN A N     1 
ATOM   5941 C  CA    . GLN A 1 851  ? 104.465 120.982 106.912 1.00 71.47  ? 851  GLN A CA    1 
ATOM   5942 C  C     . GLN A 1 851  ? 103.949 121.877 108.035 1.00 71.47  ? 851  GLN A C     1 
ATOM   5943 O  O     . GLN A 1 851  ? 104.212 121.630 109.217 1.00 71.47  ? 851  GLN A O     1 
ATOM   5944 C  CB    . GLN A 1 851  ? 105.798 121.496 106.353 1.00 71.47  ? 851  GLN A CB    1 
ATOM   5945 C  CG    . GLN A 1 851  ? 106.970 121.422 107.315 1.00 71.47  ? 851  GLN A CG    1 
ATOM   5946 C  CD    . GLN A 1 851  ? 107.242 122.730 108.028 1.00 71.47  ? 851  GLN A CD    1 
ATOM   5947 O  OE1   . GLN A 1 851  ? 106.413 123.637 108.026 1.00 71.47  ? 851  GLN A OE1   1 
ATOM   5948 N  NE2   . GLN A 1 851  ? 108.415 122.835 108.642 1.00 71.47  ? 851  GLN A NE2   1 
ATOM   5949 N  N     . LEU A 1 852  ? 103.206 122.925 107.675 1.00 72.50  ? 852  LEU A N     1 
ATOM   5950 C  CA    . LEU A 1 852  ? 102.654 123.834 108.674 1.00 72.50  ? 852  LEU A CA    1 
ATOM   5951 C  C     . LEU A 1 852  ? 101.518 123.180 109.453 1.00 72.50  ? 852  LEU A C     1 
ATOM   5952 O  O     . LEU A 1 852  ? 101.450 123.281 110.683 1.00 72.50  ? 852  LEU A O     1 
ATOM   5953 C  CB    . LEU A 1 852  ? 102.166 125.118 107.999 1.00 72.50  ? 852  LEU A CB    1 
ATOM   5954 C  CG    . LEU A 1 852  ? 103.065 126.356 108.050 1.00 72.50  ? 852  LEU A CG    1 
ATOM   5955 C  CD1   . LEU A 1 852  ? 104.462 126.040 107.553 1.00 72.50  ? 852  LEU A CD1   1 
ATOM   5956 C  CD2   . LEU A 1 852  ? 102.455 127.496 107.249 1.00 72.50  ? 852  LEU A CD2   1 
ATOM   5957 N  N     . SER A 1 853  ? 100.609 122.506 108.744 1.00 71.66  ? 853  SER A N     1 
ATOM   5958 C  CA    . SER A 1 853  ? 99.378  122.031 109.372 1.00 71.66  ? 853  SER A CA    1 
ATOM   5959 C  C     . SER A 1 853  ? 99.656  120.981 110.445 1.00 71.66  ? 853  SER A C     1 
ATOM   5960 O  O     . SER A 1 853  ? 99.069  121.020 111.533 1.00 71.66  ? 853  SER A O     1 
ATOM   5961 C  CB    . SER A 1 853  ? 98.431  121.481 108.305 1.00 71.66  ? 853  SER A CB    1 
ATOM   5962 O  OG    . SER A 1 853  ? 98.897  120.248 107.791 1.00 71.66  ? 853  SER A OG    1 
ATOM   5963 N  N     . LEU A 1 854  ? 100.552 120.035 110.161 1.00 68.95  ? 854  LEU A N     1 
ATOM   5964 C  CA    . LEU A 1 854  ? 100.782 118.931 111.089 1.00 68.95  ? 854  LEU A CA    1 
ATOM   5965 C  C     . LEU A 1 854  ? 101.572 119.379 112.314 1.00 68.95  ? 854  LEU A C     1 
ATOM   5966 O  O     . LEU A 1 854  ? 101.437 118.802 113.399 1.00 68.95  ? 854  LEU A O     1 
ATOM   5967 C  CB    . LEU A 1 854  ? 101.505 117.783 110.379 1.00 68.95  ? 854  LEU A CB    1 
ATOM   5968 C  CG    . LEU A 1 854  ? 100.656 116.769 109.606 1.00 68.95  ? 854  LEU A CG    1 
ATOM   5969 C  CD1   . LEU A 1 854  ? 100.084 117.362 108.330 1.00 68.95  ? 854  LEU A CD1   1 
ATOM   5970 C  CD2   . LEU A 1 854  ? 101.469 115.523 109.299 1.00 68.95  ? 854  LEU A CD2   1 
ATOM   5971 N  N     . LYS A 1 855  ? 102.410 120.404 112.155 1.00 69.17  ? 855  LYS A N     1 
ATOM   5972 C  CA    . LYS A 1 855  ? 103.320 120.805 113.224 1.00 69.17  ? 855  LYS A CA    1 
ATOM   5973 C  C     . LYS A 1 855  ? 102.568 121.300 114.456 1.00 69.17  ? 855  LYS A C     1 
ATOM   5974 O  O     . LYS A 1 855  ? 102.946 120.999 115.593 1.00 69.17  ? 855  LYS A O     1 
ATOM   5975 C  CB    . LYS A 1 855  ? 104.281 121.881 112.715 1.00 69.17  ? 855  LYS A CB    1 
ATOM   5976 C  CG    . LYS A 1 855  ? 105.581 121.334 112.153 1.00 69.17  ? 855  LYS A CG    1 
ATOM   5977 C  CD    . LYS A 1 855  ? 106.518 122.459 111.754 1.00 69.17  ? 855  LYS A CD    1 
ATOM   5978 C  CE    . LYS A 1 855  ? 107.420 122.856 112.910 1.00 69.17  ? 855  LYS A CE    1 
ATOM   5979 N  NZ    . LYS A 1 855  ? 107.803 124.293 112.849 1.00 69.17  ? 855  LYS A NZ    1 
ATOM   5980 N  N     . GLY A 1 856  ? 101.501 122.073 114.244 1.00 62.19  ? 856  GLY A N     1 
ATOM   5981 C  CA    . GLY A 1 856  ? 100.833 122.719 115.365 1.00 62.19  ? 856  GLY A CA    1 
ATOM   5982 C  C     . GLY A 1 856  ? 100.255 121.739 116.366 1.00 62.19  ? 856  GLY A C     1 
ATOM   5983 O  O     . GLY A 1 856  ? 100.393 121.914 117.579 1.00 62.19  ? 856  GLY A O     1 
ATOM   5984 N  N     . PHE A 1 857  ? 99.598  120.688 115.873 1.00 58.79  ? 857  PHE A N     1 
ATOM   5985 C  CA    . PHE A 1 857  ? 98.940  119.751 116.777 1.00 58.79  ? 857  PHE A CA    1 
ATOM   5986 C  C     . PHE A 1 857  ? 99.884  118.652 117.245 1.00 58.79  ? 857  PHE A C     1 
ATOM   5987 O  O     . PHE A 1 857  ? 99.559  117.917 118.185 1.00 58.79  ? 857  PHE A O     1 
ATOM   5988 C  CB    . PHE A 1 857  ? 97.709  119.156 116.100 1.00 58.79  ? 857  PHE A CB    1 
ATOM   5989 C  CG    . PHE A 1 857  ? 96.517  120.067 116.116 1.00 58.79  ? 857  PHE A CG    1 
ATOM   5990 C  CD1   . PHE A 1 857  ? 95.628  120.050 117.175 1.00 58.79  ? 857  PHE A CD1   1 
ATOM   5991 C  CD2   . PHE A 1 857  ? 96.297  120.955 115.077 1.00 58.79  ? 857  PHE A CD2   1 
ATOM   5992 C  CE1   . PHE A 1 857  ? 94.534  120.894 117.194 1.00 58.79  ? 857  PHE A CE1   1 
ATOM   5993 C  CE2   . PHE A 1 857  ? 95.206  121.802 115.090 1.00 58.79  ? 857  PHE A CE2   1 
ATOM   5994 C  CZ    . PHE A 1 857  ? 94.323  121.771 116.150 1.00 58.79  ? 857  PHE A CZ    1 
ATOM   5995 N  N     . ALA A 1 858  ? 101.049 118.519 116.608 1.00 55.94  ? 858  ALA A N     1 
ATOM   5996 C  CA    . ALA A 1 858  ? 102.013 117.503 117.019 1.00 55.94  ? 858  ALA A CA    1 
ATOM   5997 C  C     . ALA A 1 858  ? 102.641 117.851 118.363 1.00 55.94  ? 858  ALA A C     1 
ATOM   5998 O  O     . ALA A 1 858  ? 102.959 116.963 119.163 1.00 55.94  ? 858  ALA A O     1 
ATOM   5999 C  CB    . ALA A 1 858  ? 103.090 117.339 115.947 1.00 55.94  ? 858  ALA A CB    1 
ATOM   6000 N  N     . GLY A 1 859  ? 102.837 119.145 118.623 1.00 50.19  ? 859  GLY A N     1 
ATOM   6001 C  CA    . GLY A 1 859  ? 103.455 119.554 119.875 1.00 50.19  ? 859  GLY A CA    1 
ATOM   6002 C  C     . GLY A 1 859  ? 102.603 119.234 121.086 1.00 50.19  ? 859  GLY A C     1 
ATOM   6003 O  O     . GLY A 1 859  ? 103.117 118.895 122.154 1.00 50.19  ? 859  GLY A O     1 
ATOM   6004 N  N     . ASP A 1 860  ? 101.282 119.345 120.937 1.00 43.39  ? 860  ASP A N     1 
ATOM   6005 C  CA    . ASP A 1 860  ? 100.380 119.087 122.055 1.00 43.39  ? 860  ASP A CA    1 
ATOM   6006 C  C     . ASP A 1 860  ? 100.445 117.629 122.494 1.00 43.39  ? 860  ASP A C     1 
ATOM   6007 O  O     . ASP A 1 860  ? 100.421 117.327 123.693 1.00 43.39  ? 860  ASP A O     1 
ATOM   6008 C  CB    . ASP A 1 860  ? 98.951  119.473 121.669 1.00 43.39  ? 860  ASP A CB    1 
ATOM   6009 C  CG    . ASP A 1 860  ? 98.069  119.722 122.875 1.00 43.39  ? 860  ASP A CG    1 
ATOM   6010 O  OD1   . ASP A 1 860  ? 98.551  119.548 124.014 1.00 43.39  ? 860  ASP A OD1   1 
ATOM   6011 O  OD2   . ASP A 1 860  ? 96.893  120.096 122.684 1.00 43.39  ? 860  ASP A OD2   1 
ATOM   6012 N  N     . THR A 1 861  ? 100.526 116.706 121.533 1.00 40.75  ? 861  THR A N     1 
ATOM   6013 C  CA    . THR A 1 861  ? 100.512 115.285 121.868 1.00 40.75  ? 861  THR A CA    1 
ATOM   6014 C  C     . THR A 1 861  ? 101.786 114.852 122.582 1.00 40.75  ? 861  THR A C     1 
ATOM   6015 O  O     . THR A 1 861  ? 101.753 113.921 123.396 1.00 40.75  ? 861  THR A O     1 
ATOM   6016 C  CB    . THR A 1 861  ? 100.308 114.448 120.605 1.00 40.75  ? 861  THR A CB    1 
ATOM   6017 O  OG1   . THR A 1 861  ? 101.221 114.883 119.590 1.00 40.75  ? 861  THR A OG1   1 
ATOM   6018 C  CG2   . THR A 1 861  ? 98.884  114.595 120.097 1.00 40.75  ? 861  THR A CG2   1 
ATOM   6019 N  N     . ALA A 1 862  ? 102.915 115.500 122.288 1.00 38.90  ? 862  ALA A N     1 
ATOM   6020 C  CA    . ALA A 1 862  ? 104.177 115.119 122.915 1.00 38.90  ? 862  ALA A CA    1 
ATOM   6021 C  C     . ALA A 1 862  ? 104.120 115.319 124.425 1.00 38.90  ? 862  ALA A C     1 
ATOM   6022 O  O     . ALA A 1 862  ? 104.559 114.459 125.200 1.00 38.90  ? 862  ALA A O     1 
ATOM   6023 C  CB    . ALA A 1 862  ? 105.327 115.921 122.305 1.00 38.90  ? 862  ALA A CB    1 
ATOM   6024 N  N     . LYS A 1 863  ? 103.569 116.454 124.860 1.00 36.46  ? 863  LYS A N     1 
ATOM   6025 C  CA    . LYS A 1 863  ? 103.442 116.715 126.290 1.00 36.46  ? 863  LYS A CA    1 
ATOM   6026 C  C     . LYS A 1 863  ? 102.521 115.701 126.953 1.00 36.46  ? 863  LYS A C     1 
ATOM   6027 O  O     . LYS A 1 863  ? 102.791 115.239 128.068 1.00 36.46  ? 863  LYS A O     1 
ATOM   6028 C  CB    . LYS A 1 863  ? 102.934 118.138 126.519 1.00 36.46  ? 863  LYS A CB    1 
ATOM   6029 C  CG    . LYS A 1 863  ? 102.898 118.551 127.979 1.00 36.46  ? 863  LYS A CG    1 
ATOM   6030 C  CD    . LYS A 1 863  ? 102.331 119.951 128.146 1.00 36.46  ? 863  LYS A CD    1 
ATOM   6031 C  CE    . LYS A 1 863  ? 103.324 121.007 127.689 1.00 36.46  ? 863  LYS A CE    1 
ATOM   6032 N  NZ    . LYS A 1 863  ? 102.832 122.386 127.956 1.00 36.46  ? 863  LYS A NZ    1 
ATOM   6033 N  N     . ALA A 1 864  ? 101.426 115.341 126.280 1.00 33.95  ? 864  ALA A N     1 
ATOM   6034 C  CA    . ALA A 1 864  ? 100.510 114.348 126.830 1.00 33.95  ? 864  ALA A CA    1 
ATOM   6035 C  C     . ALA A 1 864  ? 101.195 112.997 126.989 1.00 33.95  ? 864  ALA A C     1 
ATOM   6036 O  O     . ALA A 1 864  ? 101.055 112.336 128.024 1.00 33.95  ? 864  ALA A O     1 
ATOM   6037 C  CB    . ALA A 1 864  ? 99.276  114.224 125.937 1.00 33.95  ? 864  ALA A CB    1 
ATOM   6038 N  N     . HIS A 1 865  ? 101.947 112.571 125.971 1.00 29.39  ? 865  HIS A N     1 
ATOM   6039 C  CA    . HIS A 1 865  ? 102.643 111.290 126.056 1.00 29.39  ? 865  HIS A CA    1 
ATOM   6040 C  C     . HIS A 1 865  ? 103.690 111.307 127.162 1.00 29.39  ? 865  HIS A C     1 
ATOM   6041 O  O     . HIS A 1 865  ? 103.858 110.316 127.887 1.00 29.39  ? 865  HIS A O     1 
ATOM   6042 C  CB    . HIS A 1 865  ? 103.281 110.949 124.711 1.00 29.39  ? 865  HIS A CB    1 
ATOM   6043 C  CG    . HIS A 1 865  ? 102.287 110.655 123.631 1.00 29.39  ? 865  HIS A CG    1 
ATOM   6044 N  ND1   . HIS A 1 865  ? 100.993 110.261 123.898 1.00 29.39  ? 865  HIS A ND1   1 
ATOM   6045 C  CD2   . HIS A 1 865  ? 102.396 110.699 122.283 1.00 29.39  ? 865  HIS A CD2   1 
ATOM   6046 C  CE1   . HIS A 1 865  ? 100.349 110.073 122.760 1.00 29.39  ? 865  HIS A CE1   1 
ATOM   6047 N  NE2   . HIS A 1 865  ? 101.178 110.332 121.765 1.00 29.39  ? 865  HIS A NE2   1 
ATOM   6048 N  N     . ALA A 1 866  ? 104.397 112.428 127.316 1.00 26.81  ? 866  ALA A N     1 
ATOM   6049 C  CA    . ALA A 1 866  ? 105.351 112.553 128.412 1.00 26.81  ? 866  ALA A CA    1 
ATOM   6050 C  C     . ALA A 1 866  ? 104.648 112.453 129.761 1.00 26.81  ? 866  ALA A C     1 
ATOM   6051 O  O     . ALA A 1 866  ? 105.156 111.822 130.695 1.00 26.81  ? 866  ALA A O     1 
ATOM   6052 C  CB    . ALA A 1 866  ? 106.116 113.870 128.293 1.00 26.81  ? 866  ALA A CB    1 
ATOM   6053 N  N     . LYS A 1 867  ? 103.473 113.076 129.881 1.00 27.41  ? 867  LYS A N     1 
ATOM   6054 C  CA    . LYS A 1 867  ? 102.721 113.005 131.131 1.00 27.41  ? 867  LYS A CA    1 
ATOM   6055 C  C     . LYS A 1 867  ? 102.286 111.577 131.441 1.00 27.41  ? 867  LYS A C     1 
ATOM   6056 O  O     . LYS A 1 867  ? 102.357 111.136 132.594 1.00 27.41  ? 867  LYS A O     1 
ATOM   6057 C  CB    . LYS A 1 867  ? 101.508 113.930 131.064 1.00 27.41  ? 867  LYS A CB    1 
ATOM   6058 C  CG    . LYS A 1 867  ? 100.703 113.981 132.348 1.00 27.41  ? 867  LYS A CG    1 
ATOM   6059 C  CD    . LYS A 1 867  ? 101.546 114.498 133.499 1.00 27.41  ? 867  LYS A CD    1 
ATOM   6060 C  CE    . LYS A 1 867  ? 101.872 115.970 133.322 1.00 27.41  ? 867  LYS A CE    1 
ATOM   6061 N  NZ    . LYS A 1 867  ? 102.699 116.492 134.443 1.00 27.41  ? 867  LYS A NZ    1 
ATOM   6062 N  N     . THR A 1 868  ? 101.819 110.844 130.428 1.00 24.91  ? 868  THR A N     1 
ATOM   6063 C  CA    . THR A 1 868  ? 101.450 109.447 130.652 1.00 24.91  ? 868  THR A CA    1 
ATOM   6064 C  C     . THR A 1 868  ? 102.655 108.616 131.076 1.00 24.91  ? 868  THR A C     1 
ATOM   6065 O  O     . THR A 1 868  ? 102.550 107.766 131.971 1.00 24.91  ? 868  THR A O     1 
ATOM   6066 C  CB    . THR A 1 868  ? 100.799 108.845 129.404 1.00 24.91  ? 868  THR A CB    1 
ATOM   6067 O  OG1   . THR A 1 868  ? 101.803 108.536 128.428 1.00 24.91  ? 868  THR A OG1   1 
ATOM   6068 C  CG2   . THR A 1 868  ? 99.748  109.770 128.821 1.00 24.91  ? 868  THR A CG2   1 
ATOM   6069 N  N     . SER A 1 869  ? 103.810 108.846 130.446 1.00 23.79  ? 869  SER A N     1 
ATOM   6070 C  CA    . SER A 1 869  ? 105.014 108.128 130.854 1.00 23.79  ? 869  SER A CA    1 
ATOM   6071 C  C     . SER A 1 869  ? 105.381 108.449 132.298 1.00 23.79  ? 869  SER A C     1 
ATOM   6072 O  O     . SER A 1 869  ? 105.773 107.557 133.061 1.00 23.79  ? 869  SER A O     1 
ATOM   6073 C  CB    . SER A 1 869  ? 106.173 108.468 129.919 1.00 23.79  ? 869  SER A CB    1 
ATOM   6074 O  OG    . SER A 1 869  ? 107.410 108.099 130.500 1.00 23.79  ? 869  SER A OG    1 
ATOM   6075 N  N     . MET A 1 870  ? 105.255 109.718 132.689 1.00 25.44  ? 870  MET A N     1 
ATOM   6076 C  CA    . MET A 1 870  ? 105.542 110.115 134.064 1.00 25.44  ? 870  MET A CA    1 
ATOM   6077 C  C     . MET A 1 870  ? 104.599 109.421 135.038 1.00 25.44  ? 870  MET A C     1 
ATOM   6078 O  O     . MET A 1 870  ? 105.014 108.966 136.108 1.00 25.44  ? 870  MET A O     1 
ATOM   6079 C  CB    . MET A 1 870  ? 105.444 111.639 134.190 1.00 25.44  ? 870  MET A CB    1 
ATOM   6080 C  CG    . MET A 1 870  ? 105.748 112.228 135.572 1.00 25.44  ? 870  MET A CG    1 
ATOM   6081 S  SD    . MET A 1 870  ? 104.470 112.025 136.830 1.00 25.44  ? 870  MET A SD    1 
ATOM   6082 C  CE    . MET A 1 870  ? 103.739 113.658 136.830 1.00 25.44  ? 870  MET A CE    1 
ATOM   6083 N  N     . ILE A 1 871  ? 103.314 109.348 134.685 1.00 23.54  ? 871  ILE A N     1 
ATOM   6084 C  CA    . ILE A 1 871  ? 102.339 108.697 135.557 1.00 23.54  ? 871  ILE A CA    1 
ATOM   6085 C  C     . ILE A 1 871  ? 102.677 107.223 135.725 1.00 23.54  ? 871  ILE A C     1 
ATOM   6086 O  O     . ILE A 1 871  ? 102.632 106.681 136.837 1.00 23.54  ? 871  ILE A O     1 
ATOM   6087 C  CB    . ILE A 1 871  ? 100.913 108.893 135.008 1.00 23.54  ? 871  ILE A CB    1 
ATOM   6088 C  CG1   . ILE A 1 871  ? 100.441 110.326 135.257 1.00 23.54  ? 871  ILE A CG1   1 
ATOM   6089 C  CG2   . ILE A 1 871  ? 99.957  107.899 135.640 1.00 23.54  ? 871  ILE A CG2   1 
ATOM   6090 C  CD1   . ILE A 1 871  ? 99.112  110.650 134.616 1.00 23.54  ? 871  ILE A CD1   1 
ATOM   6091 N  N     . ALA A 1 872  ? 103.026 106.553 134.624 1.00 23.86  ? 872  ALA A N     1 
ATOM   6092 C  CA    . ALA A 1 872  ? 103.391 105.141 134.710 1.00 23.86  ? 872  ALA A CA    1 
ATOM   6093 C  C     . ALA A 1 872  ? 104.629 104.939 135.576 1.00 23.86  ? 872  ALA A C     1 
ATOM   6094 O  O     . ALA A 1 872  ? 104.674 104.022 136.406 1.00 23.86  ? 872  ALA A O     1 
ATOM   6095 C  CB    . ALA A 1 872  ? 103.615 104.567 133.311 1.00 23.86  ? 872  ALA A CB    1 
ATOM   6096 N  N     . GLY A 1 873  ? 105.643 105.790 135.401 1.00 23.41  ? 873  GLY A N     1 
ATOM   6097 C  CA    . GLY A 1 873  ? 106.845 105.662 136.210 1.00 23.41  ? 873  GLY A CA    1 
ATOM   6098 C  C     . GLY A 1 873  ? 106.584 105.902 137.684 1.00 23.41  ? 873  GLY A C     1 
ATOM   6099 O  O     . GLY A 1 873  ? 107.107 105.187 138.544 1.00 23.41  ? 873  GLY A O     1 
ATOM   6100 N  N     . GLU A 1 874  ? 105.767 106.911 137.996 1.00 27.50  ? 874  GLU A N     1 
ATOM   6101 C  CA    . GLU A 1 874  ? 105.411 107.182 139.385 1.00 27.50  ? 874  GLU A CA    1 
ATOM   6102 C  C     . GLU A 1 874  ? 104.641 106.017 139.992 1.00 27.50  ? 874  GLU A C     1 
ATOM   6103 O  O     . GLU A 1 874  ? 104.859 105.659 141.155 1.00 27.50  ? 874  GLU A O     1 
ATOM   6104 C  CB    . GLU A 1 874  ? 104.595 108.471 139.468 1.00 27.50  ? 874  GLU A CB    1 
ATOM   6105 C  CG    . GLU A 1 874  ? 104.230 108.900 140.877 1.00 27.50  ? 874  GLU A CG    1 
ATOM   6106 C  CD    . GLU A 1 874  ? 102.973 109.749 140.914 1.00 27.50  ? 874  GLU A CD    1 
ATOM   6107 O  OE1   . GLU A 1 874  ? 103.093 110.992 140.927 1.00 27.50  ? 874  GLU A OE1   1 
ATOM   6108 O  OE2   . GLU A 1 874  ? 101.865 109.174 140.924 1.00 27.50  ? 874  GLU A OE2   1 
ATOM   6109 N  N     . GLY A 1 875  ? 103.730 105.419 139.223 1.00 23.80  ? 875  GLY A N     1 
ATOM   6110 C  CA    . GLY A 1 875  ? 103.005 104.263 139.723 1.00 23.80  ? 875  GLY A CA    1 
ATOM   6111 C  C     . GLY A 1 875  ? 103.910 103.076 139.993 1.00 23.80  ? 875  GLY A C     1 
ATOM   6112 O  O     . GLY A 1 875  ? 103.770 102.397 141.012 1.00 23.80  ? 875  GLY A O     1 
ATOM   6113 N  N     . VAL A 1 876  ? 104.850 102.811 139.085 1.00 22.99  ? 876  VAL A N     1 
ATOM   6114 C  CA    . VAL A 1 876  ? 105.744 101.668 139.261 1.00 22.99  ? 876  VAL A CA    1 
ATOM   6115 C  C     . VAL A 1 876  ? 106.691 101.894 140.435 1.00 22.99  ? 876  VAL A C     1 
ATOM   6116 O  O     . VAL A 1 876  ? 107.016 100.958 141.175 1.00 22.99  ? 876  VAL A O     1 
ATOM   6117 C  CB    . VAL A 1 876  ? 106.511 101.381 137.958 1.00 22.99  ? 876  VAL A CB    1 
ATOM   6118 C  CG1   . VAL A 1 876  ? 107.519 100.266 138.167 1.00 22.99  ? 876  VAL A CG1   1 
ATOM   6119 C  CG2   . VAL A 1 876  ? 105.543 101.004 136.852 1.00 22.99  ? 876  VAL A CG2   1 
ATOM   6120 N  N     . SER A 1 877  ? 107.147 103.135 140.630 1.00 26.26  ? 877  SER A N     1 
ATOM   6121 C  CA    . SER A 1 877  ? 108.158 103.402 141.649 1.00 26.26  ? 877  SER A CA    1 
ATOM   6122 C  C     . SER A 1 877  ? 107.663 103.143 143.068 1.00 26.26  ? 877  SER A C     1 
ATOM   6123 O  O     . SER A 1 877  ? 108.484 102.910 143.961 1.00 26.26  ? 877  SER A O     1 
ATOM   6124 C  CB    . SER A 1 877  ? 108.648 104.846 141.533 1.00 26.26  ? 877  SER A CB    1 
ATOM   6125 O  OG    . SER A 1 877  ? 109.607 105.136 142.534 1.00 26.26  ? 877  SER A OG    1 
ATOM   6126 N  N     . ASN A 1 878  ? 106.352 103.176 143.300 1.00 28.52  ? 878  ASN A N     1 
ATOM   6127 C  CA    . ASN A 1 878  ? 105.809 103.007 144.644 1.00 28.52  ? 878  ASN A CA    1 
ATOM   6128 C  C     . ASN A 1 878  ? 104.868 101.812 144.715 1.00 28.52  ? 878  ASN A C     1 
ATOM   6129 O  O     . ASN A 1 878  ? 103.757 101.923 145.242 1.00 28.52  ? 878  ASN A O     1 
ATOM   6130 C  CB    . ASN A 1 878  ? 105.082 104.275 145.094 1.00 28.52  ? 878  ASN A CB    1 
ATOM   6131 C  CG    . ASN A 1 878  ? 105.989 105.485 145.126 1.00 28.52  ? 878  ASN A CG    1 
ATOM   6132 O  OD1   . ASN A 1 878  ? 107.086 105.437 145.680 1.00 28.52  ? 878  ASN A OD1   1 
ATOM   6133 N  ND2   . ASN A 1 878  ? 105.534 106.582 144.532 1.00 28.52  ? 878  ASN A ND2   1 
ATOM   6134 N  N     . ILE A 1 879  ? 105.303 100.668 144.180 1.00 24.48  ? 879  ILE A N     1 
ATOM   6135 C  CA    . ILE A 1 879  ? 104.433 99.497  144.091 1.00 24.48  ? 879  ILE A CA    1 
ATOM   6136 C  C     . ILE A 1 879  ? 103.995 99.018  145.470 1.00 24.48  ? 879  ILE A C     1 
ATOM   6137 O  O     . ILE A 1 879  ? 102.926 98.413  145.612 1.00 24.48  ? 879  ILE A O     1 
ATOM   6138 C  CB    . ILE A 1 879  ? 105.136 98.378  143.298 1.00 24.48  ? 879  ILE A CB    1 
ATOM   6139 C  CG1   . ILE A 1 879  ? 104.135 97.293  142.900 1.00 24.48  ? 879  ILE A CG1   1 
ATOM   6140 C  CG2   . ILE A 1 879  ? 106.287 97.790  144.096 1.00 24.48  ? 879  ILE A CG2   1 
ATOM   6141 C  CD1   . ILE A 1 879  ? 103.157 97.728  141.835 1.00 24.48  ? 879  ILE A CD1   1 
ATOM   6142 N  N     . ARG A 1 880  ? 104.799 99.277  146.505 1.00 27.46  ? 880  ARG A N     1 
ATOM   6143 C  CA    . ARG A 1 880  ? 104.425 98.861  147.854 1.00 27.46  ? 880  ARG A CA    1 
ATOM   6144 C  C     . ARG A 1 880  ? 103.157 99.569  148.318 1.00 27.46  ? 880  ARG A C     1 
ATOM   6145 O  O     . ARG A 1 880  ? 102.269 98.950  148.914 1.00 27.46  ? 880  ARG A O     1 
ATOM   6146 C  CB    . ARG A 1 880  ? 105.575 99.128  148.824 1.00 27.46  ? 880  ARG A CB    1 
ATOM   6147 C  CG    . ARG A 1 880  ? 106.439 97.913  149.110 1.00 27.46  ? 880  ARG A CG    1 
ATOM   6148 C  CD    . ARG A 1 880  ? 107.916 98.254  149.024 1.00 27.46  ? 880  ARG A CD    1 
ATOM   6149 N  NE    . ARG A 1 880  ? 108.759 97.095  149.299 1.00 27.46  ? 880  ARG A NE    1 
ATOM   6150 C  CZ    . ARG A 1 880  ? 109.230 96.276  148.366 1.00 27.46  ? 880  ARG A CZ    1 
ATOM   6151 N  NH1   . ARG A 1 880  ? 108.942 96.486  147.089 1.00 27.46  ? 880  ARG A NH1   1 
ATOM   6152 N  NH2   . ARG A 1 880  ? 109.991 95.246  148.708 1.00 27.46  ? 880  ARG A NH2   1 
ATOM   6153 N  N     . THR A 1 881  ? 103.058 100.873 148.056 1.00 27.27  ? 881  THR A N     1 
ATOM   6154 C  CA    . THR A 1 881  ? 101.861 101.614 148.443 1.00 27.27  ? 881  THR A CA    1 
ATOM   6155 C  C     . THR A 1 881  ? 100.684 101.272 147.538 1.00 27.27  ? 881  THR A C     1 
ATOM   6156 O  O     . THR A 1 881  ? 99.535  101.226 147.993 1.00 27.27  ? 881  THR A O     1 
ATOM   6157 C  CB    . THR A 1 881  ? 102.145 103.115 148.417 1.00 27.27  ? 881  THR A CB    1 
ATOM   6158 O  OG1   . THR A 1 881  ? 103.268 103.403 149.259 1.00 27.27  ? 881  THR A OG1   1 
ATOM   6159 C  CG2   . THR A 1 881  ? 100.942 103.898 148.914 1.00 27.27  ? 881  THR A CG2   1 
ATOM   6160 N  N     . VAL A 1 882  ? 100.948 101.029 146.252 1.00 24.75  ? 882  VAL A N     1 
ATOM   6161 C  CA    . VAL A 1 882  ? 99.875  100.698 145.319 1.00 24.75  ? 882  VAL A CA    1 
ATOM   6162 C  C     . VAL A 1 882  ? 99.239  99.363  145.685 1.00 24.75  ? 882  VAL A C     1 
ATOM   6163 O  O     . VAL A 1 882  ? 98.012  99.211  145.647 1.00 24.75  ? 882  VAL A O     1 
ATOM   6164 C  CB    . VAL A 1 882  ? 100.406 100.699 143.874 1.00 24.75  ? 882  VAL A CB    1 
ATOM   6165 C  CG1   . VAL A 1 882  ? 99.363  100.141 142.922 1.00 24.75  ? 882  VAL A CG1   1 
ATOM   6166 C  CG2   . VAL A 1 882  ? 100.807 102.104 143.463 1.00 24.75  ? 882  VAL A CG2   1 
ATOM   6167 N  N     . ALA A 1 883  ? 100.058 98.371  146.036 1.00 26.67  ? 883  ALA A N     1 
ATOM   6168 C  CA    . ALA A 1 883  ? 99.516  97.066  146.398 1.00 26.67  ? 883  ALA A CA    1 
ATOM   6169 C  C     . ALA A 1 883  ? 98.713  97.134  147.692 1.00 26.67  ? 883  ALA A C     1 
ATOM   6170 O  O     . ALA A 1 883  ? 97.629  96.548  147.785 1.00 26.67  ? 883  ALA A O     1 
ATOM   6171 C  CB    . ALA A 1 883  ? 100.645 96.044  146.520 1.00 26.67  ? 883  ALA A CB    1 
ATOM   6172 N  N     . ALA A 1 884  ? 99.228  97.839  148.701 1.00 28.52  ? 884  ALA A N     1 
ATOM   6173 C  CA    . ALA A 1 884  ? 98.535  97.927  149.983 1.00 28.52  ? 884  ALA A CA    1 
ATOM   6174 C  C     . ALA A 1 884  ? 97.194  98.635  149.834 1.00 28.52  ? 884  ALA A C     1 
ATOM   6175 O  O     . ALA A 1 884  ? 96.133  98.042  150.058 1.00 28.52  ? 884  ALA A O     1 
ATOM   6176 C  CB    . ALA A 1 884  ? 99.416  98.642  151.007 1.00 28.52  ? 884  ALA A CB    1 
ATOM   6177 N  N     . PHE A 1 885  ? 97.223  99.909  149.453 1.00 27.77  ? 885  PHE A N     1 
ATOM   6178 C  CA    . PHE A 1 885  ? 96.010  100.669 149.174 1.00 27.77  ? 885  PHE A CA    1 
ATOM   6179 C  C     . PHE A 1 885  ? 95.638  100.433 147.717 1.00 27.77  ? 885  PHE A C     1 
ATOM   6180 O  O     . PHE A 1 885  ? 96.269  100.994 146.816 1.00 27.77  ? 885  PHE A O     1 
ATOM   6181 C  CB    . PHE A 1 885  ? 96.222  102.155 149.447 1.00 27.77  ? 885  PHE A CB    1 
ATOM   6182 C  CG    . PHE A 1 885  ? 96.597  102.465 150.864 1.00 27.77  ? 885  PHE A CG    1 
ATOM   6183 C  CD1   . PHE A 1 885  ? 95.667  102.350 151.881 1.00 27.77  ? 885  PHE A CD1   1 
ATOM   6184 C  CD2   . PHE A 1 885  ? 97.879  102.876 151.179 1.00 27.77  ? 885  PHE A CD2   1 
ATOM   6185 C  CE1   . PHE A 1 885  ? 96.011  102.639 153.187 1.00 27.77  ? 885  PHE A CE1   1 
ATOM   6186 C  CE2   . PHE A 1 885  ? 98.228  103.164 152.483 1.00 27.77  ? 885  PHE A CE2   1 
ATOM   6187 C  CZ    . PHE A 1 885  ? 97.293  103.046 153.487 1.00 27.77  ? 885  PHE A CZ    1 
ATOM   6188 N  N     . ASN A 1 886  ? 94.617  99.608  147.485 1.00 30.63  ? 886  ASN A N     1 
ATOM   6189 C  CA    . ASN A 1 886  ? 94.241  99.238  146.126 1.00 30.63  ? 886  ASN A CA    1 
ATOM   6190 C  C     . ASN A 1 886  ? 93.910  100.475 145.303 1.00 30.63  ? 886  ASN A C     1 
ATOM   6191 O  O     . ASN A 1 886  ? 92.893  101.134 145.539 1.00 30.63  ? 886  ASN A O     1 
ATOM   6192 C  CB    . ASN A 1 886  ? 93.054  98.275  146.143 1.00 30.63  ? 886  ASN A CB    1 
ATOM   6193 C  CG    . ASN A 1 886  ? 92.787  97.661  144.786 1.00 30.63  ? 886  ASN A CG    1 
ATOM   6194 O  OD1   . ASN A 1 886  ? 93.714  97.360  144.036 1.00 30.63  ? 886  ASN A OD1   1 
ATOM   6195 N  ND2   . ASN A 1 886  ? 91.513  97.475  144.462 1.00 30.63  ? 886  ASN A ND2   1 
ATOM   6196 N  N     . ALA A 1 887  ? 94.767  100.795 144.328 1.00 27.72  ? 887  ALA A N     1 
ATOM   6197 C  CA    . ALA A 1 887  ? 94.621  102.041 143.586 1.00 27.72  ? 887  ALA A CA    1 
ATOM   6198 C  C     . ALA A 1 887  ? 94.924  101.882 142.100 1.00 27.72  ? 887  ALA A C     1 
ATOM   6199 O  O     . ALA A 1 887  ? 95.229  102.877 141.433 1.00 27.72  ? 887  ALA A O     1 
ATOM   6200 C  CB    . ALA A 1 887  ? 95.522  103.129 144.178 1.00 27.72  ? 887  ALA A CB    1 
ATOM   6201 N  N     . GLN A 1 888  ? 94.854  100.663 141.563 1.00 28.63  ? 888  GLN A N     1 
ATOM   6202 C  CA    . GLN A 1 888  ? 95.078  100.482 140.133 1.00 28.63  ? 888  GLN A CA    1 
ATOM   6203 C  C     . GLN A 1 888  ? 94.004  101.179 139.309 1.00 28.63  ? 888  GLN A C     1 
ATOM   6204 O  O     . GLN A 1 888  ? 94.285  101.680 138.212 1.00 28.63  ? 888  GLN A O     1 
ATOM   6205 C  CB    . GLN A 1 888  ? 95.129  98.993  139.798 1.00 28.63  ? 888  GLN A CB    1 
ATOM   6206 C  CG    . GLN A 1 888  ? 96.008  98.186  140.738 1.00 28.63  ? 888  GLN A CG    1 
ATOM   6207 C  CD    . GLN A 1 888  ? 95.753  96.696  140.641 1.00 28.63  ? 888  GLN A CD    1 
ATOM   6208 O  OE1   . GLN A 1 888  ? 94.925  96.246  139.848 1.00 28.63  ? 888  GLN A OE1   1 
ATOM   6209 N  NE2   . GLN A 1 888  ? 96.462  95.920  141.452 1.00 28.63  ? 888  GLN A NE2   1 
ATOM   6210 N  N     . SER A 1 889  ? 92.773  101.226 139.824 1.00 28.56  ? 889  SER A N     1 
ATOM   6211 C  CA    . SER A 1 889  ? 91.691  101.887 139.103 1.00 28.56  ? 889  SER A CA    1 
ATOM   6212 C  C     . SER A 1 889  ? 91.972  103.373 138.926 1.00 28.56  ? 889  SER A C     1 
ATOM   6213 O  O     . SER A 1 889  ? 91.713  103.935 137.857 1.00 28.56  ? 889  SER A O     1 
ATOM   6214 C  CB    . SER A 1 889  ? 90.368  101.675 139.837 1.00 28.56  ? 889  SER A CB    1 
ATOM   6215 O  OG    . SER A 1 889  ? 90.398  102.273 141.121 1.00 28.56  ? 889  SER A OG    1 
ATOM   6216 N  N     . LYS A 1 890  ? 92.498  104.028 139.963 1.00 26.05  ? 890  LYS A N     1 
ATOM   6217 C  CA    . LYS A 1 890  ? 92.819  105.447 139.850 1.00 26.05  ? 890  LYS A CA    1 
ATOM   6218 C  C     . LYS A 1 890  ? 93.902  105.688 138.806 1.00 26.05  ? 890  LYS A C     1 
ATOM   6219 O  O     . LYS A 1 890  ? 93.815  106.639 138.017 1.00 26.05  ? 890  LYS A O     1 
ATOM   6220 C  CB    . LYS A 1 890  ? 93.253  105.998 141.207 1.00 26.05  ? 890  LYS A CB    1 
ATOM   6221 C  CG    . LYS A 1 890  ? 92.115  106.554 142.042 1.00 26.05  ? 890  LYS A CG    1 
ATOM   6222 C  CD    . LYS A 1 890  ? 92.638  107.266 143.277 1.00 26.05  ? 890  LYS A CD    1 
ATOM   6223 C  CE    . LYS A 1 890  ? 91.527  108.016 143.991 1.00 26.05  ? 890  LYS A CE    1 
ATOM   6224 N  NZ    . LYS A 1 890  ? 92.055  109.132 144.823 1.00 26.05  ? 890  LYS A NZ    1 
ATOM   6225 N  N     . ILE A 1 891  ? 94.933  104.842 138.789 1.00 24.55  ? 891  ILE A N     1 
ATOM   6226 C  CA    . ILE A 1 891  ? 96.008  105.003 137.814 1.00 24.55  ? 891  ILE A CA    1 
ATOM   6227 C  C     . ILE A 1 891  ? 95.477  104.814 136.399 1.00 24.55  ? 891  ILE A C     1 
ATOM   6228 O  O     . ILE A 1 891  ? 95.811  105.581 135.488 1.00 24.55  ? 891  ILE A O     1 
ATOM   6229 C  CB    . ILE A 1 891  ? 97.161  104.032 138.123 1.00 24.55  ? 891  ILE A CB    1 
ATOM   6230 C  CG1   . ILE A 1 891  ? 97.592  104.164 139.584 1.00 24.55  ? 891  ILE A CG1   1 
ATOM   6231 C  CG2   . ILE A 1 891  ? 98.334  104.291 137.197 1.00 24.55  ? 891  ILE A CG2   1 
ATOM   6232 C  CD1   . ILE A 1 891  ? 98.076  105.545 139.959 1.00 24.55  ? 891  ILE A CD1   1 
ATOM   6233 N  N     . LEU A 1 892  ? 94.640  103.794 136.193 1.00 26.72  ? 892  LEU A N     1 
ATOM   6234 C  CA    . LEU A 1 892  ? 94.062  103.579 134.869 1.00 26.72  ? 892  LEU A CA    1 
ATOM   6235 C  C     . LEU A 1 892  ? 93.165  104.741 134.457 1.00 26.72  ? 892  LEU A C     1 
ATOM   6236 O  O     . LEU A 1 892  ? 93.157  105.144 133.288 1.00 26.72  ? 892  LEU A O     1 
ATOM   6237 C  CB    . LEU A 1 892  ? 93.287  102.264 134.838 1.00 26.72  ? 892  LEU A CB    1 
ATOM   6238 C  CG    . LEU A 1 892  ? 94.127  101.021 134.553 1.00 26.72  ? 892  LEU A CG    1 
ATOM   6239 C  CD1   . LEU A 1 892  ? 93.237  99.798  134.402 1.00 26.72  ? 892  LEU A CD1   1 
ATOM   6240 C  CD2   . LEU A 1 892  ? 94.973  101.230 133.310 1.00 26.72  ? 892  LEU A CD2   1 
ATOM   6241 N  N     . SER A 1 893  ? 92.394  105.285 135.402 1.00 27.83  ? 893  SER A N     1 
ATOM   6242 C  CA    . SER A 1 893  ? 91.541  106.426 135.092 1.00 27.83  ? 893  SER A CA    1 
ATOM   6243 C  C     . SER A 1 893  ? 92.368  107.637 134.685 1.00 27.83  ? 893  SER A C     1 
ATOM   6244 O  O     . SER A 1 893  ? 92.032  108.331 133.717 1.00 27.83  ? 893  SER A O     1 
ATOM   6245 C  CB    . SER A 1 893  ? 90.656  106.758 136.293 1.00 27.83  ? 893  SER A CB    1 
ATOM   6246 O  OG    . SER A 1 893  ? 89.887  107.922 136.052 1.00 27.83  ? 893  SER A OG    1 
ATOM   6247 N  N     . LEU A 1 894  ? 93.457  107.905 135.410 1.00 26.81  ? 894  LEU A N     1 
ATOM   6248 C  CA    . LEU A 1 894  ? 94.331  109.015 135.042 1.00 26.81  ? 894  LEU A CA    1 
ATOM   6249 C  C     . LEU A 1 894  ? 94.951  108.792 133.669 1.00 26.81  ? 894  LEU A C     1 
ATOM   6250 O  O     . LEU A 1 894  ? 95.045  109.724 132.860 1.00 26.81  ? 894  LEU A O     1 
ATOM   6251 C  CB    . LEU A 1 894  ? 95.421  109.201 136.097 1.00 26.81  ? 894  LEU A CB    1 
ATOM   6252 C  CG    . LEU A 1 894  ? 94.989  109.782 137.442 1.00 26.81  ? 894  LEU A CG    1 
ATOM   6253 C  CD1   . LEU A 1 894  ? 96.136  109.737 138.438 1.00 26.81  ? 894  LEU A CD1   1 
ATOM   6254 C  CD2   . LEU A 1 894  ? 94.485  111.203 137.267 1.00 26.81  ? 894  LEU A CD2   1 
ATOM   6255 N  N     . PHE A 1 895  ? 95.375  107.559 133.388 1.00 27.05  ? 895  PHE A N     1 
ATOM   6256 C  CA    . PHE A 1 895  ? 95.963  107.244 132.091 1.00 27.05  ? 895  PHE A CA    1 
ATOM   6257 C  C     . PHE A 1 895  ? 94.968  107.499 130.964 1.00 27.05  ? 895  PHE A C     1 
ATOM   6258 O  O     . PHE A 1 895  ? 95.300  108.130 129.953 1.00 27.05  ? 895  PHE A O     1 
ATOM   6259 C  CB    . PHE A 1 895  ? 96.424  105.788 132.088 1.00 27.05  ? 895  PHE A CB    1 
ATOM   6260 C  CG    . PHE A 1 895  ? 97.564  105.507 131.159 1.00 27.05  ? 895  PHE A CG    1 
ATOM   6261 C  CD1   . PHE A 1 895  ? 98.813  106.047 131.394 1.00 27.05  ? 895  PHE A CD1   1 
ATOM   6262 C  CD2   . PHE A 1 895  ? 97.391  104.682 130.062 1.00 27.05  ? 895  PHE A CD2   1 
ATOM   6263 C  CE1   . PHE A 1 895  ? 99.868  105.775 130.550 1.00 27.05  ? 895  PHE A CE1   1 
ATOM   6264 C  CE2   . PHE A 1 895  ? 98.442  104.411 129.211 1.00 27.05  ? 895  PHE A CE2   1 
ATOM   6265 C  CZ    . PHE A 1 895  ? 99.682  104.960 129.455 1.00 27.05  ? 895  PHE A CZ    1 
ATOM   6266 N  N     . CYS A 1 896  ? 93.731  107.022 131.131 1.00 31.31  ? 896  CYS A N     1 
ATOM   6267 C  CA    . CYS A 1 896  ? 92.714  107.217 130.102 1.00 31.31  ? 896  CYS A CA    1 
ATOM   6268 C  C     . CYS A 1 896  ? 92.378  108.693 129.927 1.00 31.31  ? 896  CYS A C     1 
ATOM   6269 O  O     . CYS A 1 896  ? 92.200  109.168 128.798 1.00 31.31  ? 896  CYS A O     1 
ATOM   6270 C  CB    . CYS A 1 896  ? 91.457  106.420 130.446 1.00 31.31  ? 896  CYS A CB    1 
ATOM   6271 S  SG    . CYS A 1 896  ? 91.667  104.628 130.370 1.00 31.31  ? 896  CYS A SG    1 
ATOM   6272 N  N     . HIS A 1 897  ? 92.277  109.434 131.034 1.00 32.08  ? 897  HIS A N     1 
ATOM   6273 C  CA    . HIS A 1 897  ? 91.972  110.857 130.938 1.00 32.08  ? 897  HIS A CA    1 
ATOM   6274 C  C     . HIS A 1 897  ? 93.078  111.607 130.209 1.00 32.08  ? 897  HIS A C     1 
ATOM   6275 O  O     . HIS A 1 897  ? 92.804  112.519 129.420 1.00 32.08  ? 897  HIS A O     1 
ATOM   6276 C  CB    . HIS A 1 897  ? 91.752  111.441 132.332 1.00 32.08  ? 897  HIS A CB    1 
ATOM   6277 C  CG    . HIS A 1 897  ? 90.408  111.127 132.909 1.00 32.08  ? 897  HIS A CG    1 
ATOM   6278 N  ND1   . HIS A 1 897  ? 89.805  111.915 133.866 1.00 32.08  ? 897  HIS A ND1   1 
ATOM   6279 C  CD2   . HIS A 1 897  ? 89.548  110.110 132.663 1.00 32.08  ? 897  HIS A CD2   1 
ATOM   6280 C  CE1   . HIS A 1 897  ? 88.633  111.396 134.185 1.00 32.08  ? 897  HIS A CE1   1 
ATOM   6281 N  NE2   . HIS A 1 897  ? 88.453  110.301 133.470 1.00 32.08  ? 897  HIS A NE2   1 
ATOM   6282 N  N     . GLU A 1 898  ? 94.335  111.238 130.459 1.00 31.91  ? 898  GLU A N     1 
ATOM   6283 C  CA    . GLU A 1 898  ? 95.438  111.886 129.759 1.00 31.91  ? 898  GLU A CA    1 
ATOM   6284 C  C     . GLU A 1 898  ? 95.461  111.510 128.282 1.00 31.91  ? 898  GLU A C     1 
ATOM   6285 O  O     . GLU A 1 898  ? 95.802  112.339 127.431 1.00 31.91  ? 898  GLU A O     1 
ATOM   6286 C  CB    . GLU A 1 898  ? 96.765  111.527 130.424 1.00 31.91  ? 898  GLU A CB    1 
ATOM   6287 C  CG    . GLU A 1 898  ? 97.807  112.623 130.334 1.00 31.91  ? 898  GLU A CG    1 
ATOM   6288 C  CD    . GLU A 1 898  ? 97.293  113.949 130.853 1.00 31.91  ? 898  GLU A CD    1 
ATOM   6289 O  OE1   . GLU A 1 898  ? 96.917  114.017 132.042 1.00 31.91  ? 898  GLU A OE1   1 
ATOM   6290 O  OE2   . GLU A 1 898  ? 97.260  114.922 130.072 1.00 31.91  ? 898  GLU A OE2   1 
ATOM   6291 N  N     . LEU A 1 899  ? 95.103  110.269 127.956 1.00 31.97  ? 899  LEU A N     1 
ATOM   6292 C  CA    . LEU A 1 899  ? 95.200  109.792 126.582 1.00 31.97  ? 899  LEU A CA    1 
ATOM   6293 C  C     . LEU A 1 899  ? 93.961  110.079 125.741 1.00 31.97  ? 899  LEU A C     1 
ATOM   6294 O  O     . LEU A 1 899  ? 93.978  109.802 124.537 1.00 31.97  ? 899  LEU A O     1 
ATOM   6295 C  CB    . LEU A 1 899  ? 95.475  108.285 126.570 1.00 31.97  ? 899  LEU A CB    1 
ATOM   6296 C  CG    . LEU A 1 899  ? 96.940  107.856 126.650 1.00 31.97  ? 899  LEU A CG    1 
ATOM   6297 C  CD1   . LEU A 1 899  ? 97.087  106.397 126.255 1.00 31.97  ? 899  LEU A CD1   1 
ATOM   6298 C  CD2   . LEU A 1 899  ? 97.812  108.741 125.777 1.00 31.97  ? 899  LEU A CD2   1 
ATOM   6299 N  N     . ARG A 1 900  ? 92.887  110.601 126.338 1.00 37.39  ? 900  ARG A N     1 
ATOM   6300 C  CA    . ARG A 1 900  ? 91.657  110.830 125.579 1.00 37.39  ? 900  ARG A CA    1 
ATOM   6301 C  C     . ARG A 1 900  ? 91.860  111.841 124.452 1.00 37.39  ? 900  ARG A C     1 
ATOM   6302 O  O     . ARG A 1 900  ? 91.432  111.611 123.315 1.00 37.39  ? 900  ARG A O     1 
ATOM   6303 C  CB    . ARG A 1 900  ? 90.546  111.293 126.522 1.00 37.39  ? 900  ARG A CB    1 
ATOM   6304 C  CG    . ARG A 1 900  ? 89.189  111.443 125.856 1.00 37.39  ? 900  ARG A CG    1 
ATOM   6305 C  CD    . ARG A 1 900  ? 88.687  110.113 125.316 1.00 37.39  ? 900  ARG A CD    1 
ATOM   6306 N  NE    . ARG A 1 900  ? 88.553  109.107 126.366 1.00 37.39  ? 900  ARG A NE    1 
ATOM   6307 C  CZ    . ARG A 1 900  ? 87.479  108.970 127.138 1.00 37.39  ? 900  ARG A CZ    1 
ATOM   6308 N  NH1   . ARG A 1 900  ? 86.439  109.777 126.979 1.00 37.39  ? 900  ARG A NH1   1 
ATOM   6309 N  NH2   . ARG A 1 900  ? 87.444  108.026 128.068 1.00 37.39  ? 900  ARG A NH2   1 
ATOM   6310 N  N     . VAL A 1 901  ? 92.504  112.972 124.751 1.00 36.92  ? 901  VAL A N     1 
ATOM   6311 C  CA    . VAL A 1 901  ? 92.614  114.053 123.763 1.00 36.92  ? 901  VAL A CA    1 
ATOM   6312 C  C     . VAL A 1 901  ? 93.392  113.644 122.516 1.00 36.92  ? 901  VAL A C     1 
ATOM   6313 O  O     . VAL A 1 901  ? 92.938  113.961 121.400 1.00 36.92  ? 901  VAL A O     1 
ATOM   6314 C  CB    . VAL A 1 901  ? 93.194  115.315 124.429 1.00 36.92  ? 901  VAL A CB    1 
ATOM   6315 C  CG1   . VAL A 1 901  ? 93.413  116.410 123.398 1.00 36.92  ? 901  VAL A CG1   1 
ATOM   6316 C  CG2   . VAL A 1 901  ? 92.278  115.794 125.543 1.00 36.92  ? 901  VAL A CG2   1 
ATOM   6317 N  N     . PRO A 1 902  ? 94.550  112.975 122.611 1.00 37.31  ? 902  PRO A N     1 
ATOM   6318 C  CA    . PRO A 1 902  ? 95.312  112.674 121.389 1.00 37.31  ? 902  PRO A CA    1 
ATOM   6319 C  C     . PRO A 1 902  ? 94.538  111.891 120.346 1.00 37.31  ? 902  PRO A C     1 
ATOM   6320 O  O     . PRO A 1 902  ? 94.801  112.074 119.156 1.00 37.31  ? 902  PRO A O     1 
ATOM   6321 C  CB    . PRO A 1 902  ? 96.511  111.878 121.917 1.00 37.31  ? 902  PRO A CB    1 
ATOM   6322 C  CG    . PRO A 1 902  ? 96.725  112.421 123.267 1.00 37.31  ? 902  PRO A CG    1 
ATOM   6323 C  CD    . PRO A 1 902  ? 95.349  112.672 123.815 1.00 37.31  ? 902  PRO A CD    1 
ATOM   6324 N  N     . GLN A 1 903  ? 93.593  111.033 120.735 1.00 39.50  ? 903  GLN A N     1 
ATOM   6325 C  CA    . GLN A 1 903  ? 92.802  110.318 119.735 1.00 39.50  ? 903  GLN A CA    1 
ATOM   6326 C  C     . GLN A 1 903  ? 91.947  111.283 118.919 1.00 39.50  ? 903  GLN A C     1 
ATOM   6327 O  O     . GLN A 1 903  ? 91.903  111.211 117.679 1.00 39.50  ? 903  GLN A O     1 
ATOM   6328 C  CB    . GLN A 1 903  ? 91.925  109.267 120.417 1.00 39.50  ? 903  GLN A CB    1 
ATOM   6329 C  CG    . GLN A 1 903  ? 92.530  108.663 121.677 1.00 39.50  ? 903  GLN A CG    1 
ATOM   6330 C  CD    . GLN A 1 903  ? 93.903  108.066 121.440 1.00 39.50  ? 903  GLN A CD    1 
ATOM   6331 O  OE1   . GLN A 1 903  ? 94.902  108.547 121.976 1.00 39.50  ? 903  GLN A OE1   1 
ATOM   6332 N  NE2   . GLN A 1 903  ? 93.959  107.014 120.634 1.00 39.50  ? 903  GLN A NE2   1 
ATOM   6333 N  N     . LYS A 1 904  ? 91.261  112.201 119.605 1.00 38.64  ? 904  LYS A N     1 
ATOM   6334 C  CA    . LYS A 1 904  ? 90.430  113.180 118.913 1.00 38.64  ? 904  LYS A CA    1 
ATOM   6335 C  C     . LYS A 1 904  ? 91.272  114.073 118.015 1.00 38.64  ? 904  LYS A C     1 
ATOM   6336 O  O     . LYS A 1 904  ? 90.867  114.392 116.891 1.00 38.64  ? 904  LYS A O     1 
ATOM   6337 C  CB    . LYS A 1 904  ? 89.654  114.022 119.925 1.00 38.64  ? 904  LYS A CB    1 
ATOM   6338 C  CG    . LYS A 1 904  ? 89.200  113.258 121.156 1.00 38.64  ? 904  LYS A CG    1 
ATOM   6339 C  CD    . LYS A 1 904  ? 88.093  113.999 121.891 1.00 38.64  ? 904  LYS A CD    1 
ATOM   6340 C  CE    . LYS A 1 904  ? 88.460  115.456 122.135 1.00 38.64  ? 904  LYS A CE    1 
ATOM   6341 N  NZ    . LYS A 1 904  ? 89.756  115.600 122.853 1.00 38.64  ? 904  LYS A NZ    1 
ATOM   6342 N  N     . ARG A 1 905  ? 92.446  114.490 118.491 1.00 40.56  ? 905  ARG A N     1 
ATOM   6343 C  CA    . ARG A 1 905  ? 93.312  115.307 117.645 1.00 40.56  ? 905  ARG A CA    1 
ATOM   6344 C  C     . ARG A 1 905  ? 93.844  114.511 116.457 1.00 40.56  ? 905  ARG A C     1 
ATOM   6345 O  O     . ARG A 1 905  ? 93.956  115.043 115.345 1.00 40.56  ? 905  ARG A O     1 
ATOM   6346 C  CB    . ARG A 1 905  ? 94.456  115.888 118.473 1.00 40.56  ? 905  ARG A CB    1 
ATOM   6347 C  CG    . ARG A 1 905  ? 94.011  116.964 119.453 1.00 40.56  ? 905  ARG A CG    1 
ATOM   6348 C  CD    . ARG A 1 905  ? 93.217  118.059 118.751 1.00 40.56  ? 905  ARG A CD    1 
ATOM   6349 N  NE    . ARG A 1 905  ? 91.773  117.843 118.807 1.00 40.56  ? 905  ARG A NE    1 
ATOM   6350 C  CZ    . ARG A 1 905  ? 90.904  118.389 117.961 1.00 40.56  ? 905  ARG A CZ    1 
ATOM   6351 N  NH1   . ARG A 1 905  ? 89.608  118.138 118.085 1.00 40.56  ? 905  ARG A NH1   1 
ATOM   6352 N  NH2   . ARG A 1 905  ? 91.330  119.185 116.990 1.00 40.56  ? 905  ARG A NH2   1 
ATOM   6353 N  N     . SER A 1 906  ? 94.158  113.232 116.669 1.00 38.95  ? 906  SER A N     1 
ATOM   6354 C  CA    . SER A 1 906  ? 94.735  112.408 115.616 1.00 38.95  ? 906  SER A CA    1 
ATOM   6355 C  C     . SER A 1 906  ? 93.736  112.125 114.508 1.00 38.95  ? 906  SER A C     1 
ATOM   6356 O  O     . SER A 1 906  ? 94.134  111.984 113.348 1.00 38.95  ? 906  SER A O     1 
ATOM   6357 C  CB    . SER A 1 906  ? 95.250  111.096 116.202 1.00 38.95  ? 906  SER A CB    1 
ATOM   6358 O  OG    . SER A 1 906  ? 94.176  110.211 116.467 1.00 38.95  ? 906  SER A OG    1 
ATOM   6359 N  N     . LEU A 1 907  ? 92.447  112.018 114.837 1.00 35.35  ? 907  LEU A N     1 
ATOM   6360 C  CA    . LEU A 1 907  ? 91.450  111.838 113.783 1.00 35.35  ? 907  LEU A CA    1 
ATOM   6361 C  C     . LEU A 1 907  ? 91.518  112.974 112.763 1.00 35.35  ? 907  LEU A C     1 
ATOM   6362 O  O     . LEU A 1 907  ? 91.666  112.740 111.553 1.00 35.35  ? 907  LEU A O     1 
ATOM   6363 C  CB    . LEU A 1 907  ? 90.052  111.750 114.394 1.00 35.35  ? 907  LEU A CB    1 
ATOM   6364 C  CG    . LEU A 1 907  ? 88.891  111.879 113.408 1.00 35.35  ? 907  LEU A CG    1 
ATOM   6365 C  CD1   . LEU A 1 907  ? 88.859  110.699 112.454 1.00 35.35  ? 907  LEU A CD1   1 
ATOM   6366 C  CD2   . LEU A 1 907  ? 87.573  112.006 114.151 1.00 35.35  ? 907  LEU A CD2   1 
ATOM   6367 N  N     . TYR A 1 908  ? 91.448  114.216 113.243 1.00 39.23  ? 908  TYR A N     1 
ATOM   6368 C  CA    . TYR A 1 908  ? 91.497  115.361 112.343 1.00 39.23  ? 908  TYR A CA    1 
ATOM   6369 C  C     . TYR A 1 908  ? 92.864  115.490 111.685 1.00 39.23  ? 908  TYR A C     1 
ATOM   6370 O  O     . TYR A 1 908  ? 92.958  115.890 110.519 1.00 39.23  ? 908  TYR A O     1 
ATOM   6371 C  CB    . TYR A 1 908  ? 91.137  116.640 113.096 1.00 39.23  ? 908  TYR A CB    1 
ATOM   6372 C  CG    . TYR A 1 908  ? 89.649  116.876 113.217 1.00 39.23  ? 908  TYR A CG    1 
ATOM   6373 C  CD1   . TYR A 1 908  ? 88.824  115.936 113.820 1.00 39.23  ? 908  TYR A CD1   1 
ATOM   6374 C  CD2   . TYR A 1 908  ? 89.069  118.036 112.724 1.00 39.23  ? 908  TYR A CD2   1 
ATOM   6375 C  CE1   . TYR A 1 908  ? 87.464  116.147 113.933 1.00 39.23  ? 908  TYR A CE1   1 
ATOM   6376 C  CE2   . TYR A 1 908  ? 87.709  118.256 112.832 1.00 39.23  ? 908  TYR A CE2   1 
ATOM   6377 C  CZ    . TYR A 1 908  ? 86.912  117.308 113.437 1.00 39.23  ? 908  TYR A CZ    1 
ATOM   6378 O  OH    . TYR A 1 908  ? 85.557  117.521 113.546 1.00 39.23  ? 908  TYR A OH    1 
ATOM   6379 N  N     . ARG A 1 909  ? 93.935  115.159 112.413 1.00 43.29  ? 909  ARG A N     1 
ATOM   6380 C  CA    . ARG A 1 909  ? 95.267  115.205 111.817 1.00 43.29  ? 909  ARG A CA    1 
ATOM   6381 C  C     . ARG A 1 909  ? 95.365  114.261 110.626 1.00 43.29  ? 909  ARG A C     1 
ATOM   6382 O  O     . ARG A 1 909  ? 95.872  114.634 109.562 1.00 43.29  ? 909  ARG A O     1 
ATOM   6383 C  CB    . ARG A 1 909  ? 96.325  114.855 112.863 1.00 43.29  ? 909  ARG A CB    1 
ATOM   6384 C  CG    . ARG A 1 909  ? 97.729  114.760 112.293 1.00 43.29  ? 909  ARG A CG    1 
ATOM   6385 C  CD    . ARG A 1 909  ? 98.693  114.105 113.269 1.00 43.29  ? 909  ARG A CD    1 
ATOM   6386 N  NE    . ARG A 1 909  ? 98.841  114.877 114.498 1.00 43.29  ? 909  ARG A NE    1 
ATOM   6387 C  CZ    . ARG A 1 909  ? 98.508  114.431 115.705 1.00 43.29  ? 909  ARG A CZ    1 
ATOM   6388 N  NH1   . ARG A 1 909  ? 98.678  115.202 116.769 1.00 43.29  ? 909  ARG A NH1   1 
ATOM   6389 N  NH2   . ARG A 1 909  ? 98.007  113.212 115.848 1.00 43.29  ? 909  ARG A NH2   1 
ATOM   6390 N  N     . SER A 1 910  ? 94.873  113.031 110.787 1.00 35.89  ? 910  SER A N     1 
ATOM   6391 C  CA    . SER A 1 910  ? 94.916  112.064 109.697 1.00 35.89  ? 910  SER A CA    1 
ATOM   6392 C  C     . SER A 1 910  ? 94.062  112.518 108.523 1.00 35.89  ? 910  SER A C     1 
ATOM   6393 O  O     . SER A 1 910  ? 94.480  112.404 107.364 1.00 35.89  ? 910  SER A O     1 
ATOM   6394 C  CB    . SER A 1 910  ? 94.457  110.695 110.194 1.00 35.89  ? 910  SER A CB    1 
ATOM   6395 O  OG    . SER A 1 910  ? 93.047  110.584 110.133 1.00 35.89  ? 910  SER A OG    1 
ATOM   6396 N  N     . GLN A 1 911  ? 92.861  113.034 108.800 1.00 34.87  ? 911  GLN A N     1 
ATOM   6397 C  CA    . GLN A 1 911  ? 92.001  113.489 107.709 1.00 34.87  ? 911  GLN A CA    1 
ATOM   6398 C  C     . GLN A 1 911  ? 92.655  114.626 106.928 1.00 34.87  ? 911  GLN A C     1 
ATOM   6399 O  O     . GLN A 1 911  ? 92.665  114.623 105.688 1.00 34.87  ? 911  GLN A O     1 
ATOM   6400 C  CB    . GLN A 1 911  ? 90.639  113.918 108.253 1.00 34.87  ? 911  GLN A CB    1 
ATOM   6401 C  CG    . GLN A 1 911  ? 89.850  112.792 108.895 1.00 34.87  ? 911  GLN A CG    1 
ATOM   6402 C  CD    . GLN A 1 911  ? 89.357  111.775 107.886 1.00 34.87  ? 911  GLN A CD    1 
ATOM   6403 O  OE1   . GLN A 1 911  ? 89.309  112.045 106.687 1.00 34.87  ? 911  GLN A OE1   1 
ATOM   6404 N  NE2   . GLN A 1 911  ? 88.988  110.595 108.369 1.00 34.87  ? 911  GLN A NE2   1 
ATOM   6405 N  N     . THR A 1 912  ? 93.223  115.602 107.639 1.00 36.89  ? 912  THR A N     1 
ATOM   6406 C  CA    . THR A 1 912  ? 93.872  116.724 106.971 1.00 36.89  ? 912  THR A CA    1 
ATOM   6407 C  C     . THR A 1 912  ? 95.089  116.268 106.176 1.00 36.89  ? 912  THR A C     1 
ATOM   6408 O  O     . THR A 1 912  ? 95.308  116.731 105.051 1.00 36.89  ? 912  THR A O     1 
ATOM   6409 C  CB    . THR A 1 912  ? 94.266  117.787 107.996 1.00 36.89  ? 912  THR A CB    1 
ATOM   6410 O  OG1   . THR A 1 912  ? 93.091  118.262 108.664 1.00 36.89  ? 912  THR A OG1   1 
ATOM   6411 C  CG2   . THR A 1 912  ? 94.959  118.956 107.316 1.00 36.89  ? 912  THR A CG2   1 
ATOM   6412 N  N     . SER A 1 913  ? 95.892  115.362 106.741 1.00 35.88  ? 913  SER A N     1 
ATOM   6413 C  CA    . SER A 1 913  ? 97.065  114.875 106.022 1.00 35.88  ? 913  SER A CA    1 
ATOM   6414 C  C     . SER A 1 913  ? 96.663  114.149 104.747 1.00 35.88  ? 913  SER A C     1 
ATOM   6415 O  O     . SER A 1 913  ? 97.275  114.349 103.691 1.00 35.88  ? 913  SER A O     1 
ATOM   6416 C  CB    . SER A 1 913  ? 97.891  113.957 106.920 1.00 35.88  ? 913  SER A CB    1 
ATOM   6417 O  OG    . SER A 1 913  ? 97.316  112.664 106.982 1.00 35.88  ? 913  SER A OG    1 
ATOM   6418 N  N     . GLY A 1 914  ? 95.630  113.307 104.823 1.00 38.25  ? 914  GLY A N     1 
ATOM   6419 C  CA    . GLY A 1 914  ? 95.170  112.616 103.630 1.00 38.25  ? 914  GLY A CA    1 
ATOM   6420 C  C     . GLY A 1 914  ? 94.654  113.566 102.568 1.00 38.25  ? 914  GLY A C     1 
ATOM   6421 O  O     . GLY A 1 914  ? 94.959  113.413 101.380 1.00 38.25  ? 914  GLY A O     1 
ATOM   6422 N  N     . PHE A 1 915  ? 93.865  114.565 102.978 1.00 42.33  ? 915  PHE A N     1 
ATOM   6423 C  CA    . PHE A 1 915  ? 93.348  115.527 102.009 1.00 42.33  ? 915  PHE A CA    1 
ATOM   6424 C  C     . PHE A 1 915  ? 94.474  116.314 101.352 1.00 42.33  ? 915  PHE A C     1 
ATOM   6425 O  O     . PHE A 1 915  ? 94.463  116.531 100.134 1.00 42.33  ? 915  PHE A O     1 
ATOM   6426 C  CB    . PHE A 1 915  ? 92.355  116.473 102.680 1.00 42.33  ? 915  PHE A CB    1 
ATOM   6427 C  CG    . PHE A 1 915  ? 91.407  117.128 101.719 1.00 42.33  ? 915  PHE A CG    1 
ATOM   6428 C  CD1   . PHE A 1 915  ? 90.610  116.363 100.884 1.00 42.33  ? 915  PHE A CD1   1 
ATOM   6429 C  CD2   . PHE A 1 915  ? 91.316  118.507 101.647 1.00 42.33  ? 915  PHE A CD2   1 
ATOM   6430 C  CE1   . PHE A 1 915  ? 89.738  116.962 99.996  1.00 42.33  ? 915  PHE A CE1   1 
ATOM   6431 C  CE2   . PHE A 1 915  ? 90.446  119.112 100.761 1.00 42.33  ? 915  PHE A CE2   1 
ATOM   6432 C  CZ    . PHE A 1 915  ? 89.655  118.338 99.935  1.00 42.33  ? 915  PHE A CZ    1 
ATOM   6433 N  N     . LEU A 1 916  ? 95.456  116.753 102.143 1.00 43.24  ? 916  LEU A N     1 
ATOM   6434 C  CA    . LEU A 1 916  ? 96.573  117.502 101.578 1.00 43.24  ? 916  LEU A CA    1 
ATOM   6435 C  C     . LEU A 1 916  ? 97.395  116.640 100.629 1.00 43.24  ? 916  LEU A C     1 
ATOM   6436 O  O     . LEU A 1 916  ? 97.847  117.118 99.583  1.00 43.24  ? 916  LEU A O     1 
ATOM   6437 C  CB    . LEU A 1 916  ? 97.449  118.067 102.695 1.00 43.24  ? 916  LEU A CB    1 
ATOM   6438 C  CG    . LEU A 1 916  ? 97.139  119.493 103.158 1.00 43.24  ? 916  LEU A CG    1 
ATOM   6439 C  CD1   . LEU A 1 916  ? 97.424  120.483 102.042 1.00 43.24  ? 916  LEU A CD1   1 
ATOM   6440 C  CD2   . LEU A 1 916  ? 95.703  119.629 103.636 1.00 43.24  ? 916  LEU A CD2   1 
ATOM   6441 N  N     . PHE A 1 917  ? 97.606  115.368 100.977 1.00 45.64  ? 917  PHE A N     1 
ATOM   6442 C  CA    . PHE A 1 917  ? 98.347  114.476 100.090 1.00 45.64  ? 917  PHE A CA    1 
ATOM   6443 C  C     . PHE A 1 917  ? 97.608  114.284 98.771  1.00 45.64  ? 917  PHE A C     1 
ATOM   6444 O  O     . PHE A 1 917  ? 98.216  114.310 97.692  1.00 45.64  ? 917  PHE A O     1 
ATOM   6445 C  CB    . PHE A 1 917  ? 98.585  113.133 100.780 1.00 45.64  ? 917  PHE A CB    1 
ATOM   6446 C  CG    . PHE A 1 917  ? 99.777  112.386 100.259 1.00 45.64  ? 917  PHE A CG    1 
ATOM   6447 C  CD1   . PHE A 1 917  ? 101.052 112.709 100.685 1.00 45.64  ? 917  PHE A CD1   1 
ATOM   6448 C  CD2   . PHE A 1 917  ? 99.623  111.362 99.342  1.00 45.64  ? 917  PHE A CD2   1 
ATOM   6449 C  CE1   . PHE A 1 917  ? 102.152 112.024 100.208 1.00 45.64  ? 917  PHE A CE1   1 
ATOM   6450 C  CE2   . PHE A 1 917  ? 100.719 110.673 98.861  1.00 45.64  ? 917  PHE A CE2   1 
ATOM   6451 C  CZ    . PHE A 1 917  ? 101.985 111.006 99.295  1.00 45.64  ? 917  PHE A CZ    1 
ATOM   6452 N  N     . GLY A 1 918  ? 96.289  114.094 98.839  1.00 41.95  ? 918  GLY A N     1 
ATOM   6453 C  CA    . GLY A 1 918  ? 95.512  113.969 97.617  1.00 41.95  ? 918  GLY A CA    1 
ATOM   6454 C  C     . GLY A 1 918  ? 95.575  115.217 96.756  1.00 41.95  ? 918  GLY A C     1 
ATOM   6455 O  O     . GLY A 1 918  ? 95.727  115.135 95.533  1.00 41.95  ? 918  GLY A O     1 
ATOM   6456 N  N     . LEU A 1 919  ? 95.462  116.391 97.383  1.00 44.39  ? 919  LEU A N     1 
ATOM   6457 C  CA    . LEU A 1 919  ? 95.545  117.638 96.631  1.00 44.39  ? 919  LEU A CA    1 
ATOM   6458 C  C     . LEU A 1 919  ? 96.915  117.803 95.985  1.00 44.39  ? 919  LEU A C     1 
ATOM   6459 O  O     . LEU A 1 919  ? 97.017  118.247 94.835  1.00 44.39  ? 919  LEU A O     1 
ATOM   6460 C  CB    . LEU A 1 919  ? 95.237  118.825 97.542  1.00 44.39  ? 919  LEU A CB    1 
ATOM   6461 C  CG    . LEU A 1 919  ? 93.757  119.128 97.784  1.00 44.39  ? 919  LEU A CG    1 
ATOM   6462 C  CD1   . LEU A 1 919  ? 93.586  120.512 98.391  1.00 44.39  ? 919  LEU A CD1   1 
ATOM   6463 C  CD2   . LEU A 1 919  ? 92.963  118.999 96.492  1.00 44.39  ? 919  LEU A CD2   1 
ATOM   6464 N  N     . SER A 1 920  ? 97.980  117.455 96.711  1.00 47.13  ? 920  SER A N     1 
ATOM   6465 C  CA    . SER A 1 920  ? 99.322  117.555 96.148  1.00 47.13  ? 920  SER A CA    1 
ATOM   6466 C  C     . SER A 1 920  ? 99.489  116.628 94.953  1.00 47.13  ? 920  SER A C     1 
ATOM   6467 O  O     . SER A 1 920  ? 100.062 117.021 93.930  1.00 47.13  ? 920  SER A O     1 
ATOM   6468 C  CB    . SER A 1 920  ? 100.366 117.240 97.218  1.00 47.13  ? 920  SER A CB    1 
ATOM   6469 O  OG    . SER A 1 920  ? 101.675 117.300 96.681  1.00 47.13  ? 920  SER A OG    1 
ATOM   6470 N  N     . GLN A 1 921  ? 98.994  115.392 95.059  1.00 48.39  ? 921  GLN A N     1 
ATOM   6471 C  CA    . GLN A 1 921  ? 99.091  114.467 93.932  1.00 48.39  ? 921  GLN A CA    1 
ATOM   6472 C  C     . GLN A 1 921  ? 98.306  114.977 92.729  1.00 48.39  ? 921  GLN A C     1 
ATOM   6473 O  O     . GLN A 1 921  ? 98.785  114.907 91.589  1.00 48.39  ? 921  GLN A O     1 
ATOM   6474 C  CB    . GLN A 1 921  ? 98.603  113.079 94.342  1.00 48.39  ? 921  GLN A CB    1 
ATOM   6475 C  CG    . GLN A 1 921  ? 99.443  112.427 95.424  1.00 48.39  ? 921  GLN A CG    1 
ATOM   6476 C  CD    . GLN A 1 921  ? 100.868 112.176 94.980  1.00 48.39  ? 921  GLN A CD    1 
ATOM   6477 O  OE1   . GLN A 1 921  ? 101.123 111.328 94.126  1.00 48.39  ? 921  GLN A OE1   1 
ATOM   6478 N  NE2   . GLN A 1 921  ? 101.806 112.916 95.558  1.00 48.39  ? 921  GLN A NE2   1 
ATOM   6479 N  N     . LEU A 1 922  ? 97.097  115.498 92.963  1.00 45.26  ? 922  LEU A N     1 
ATOM   6480 C  CA    . LEU A 1 922  ? 96.296  116.018 91.860  1.00 45.26  ? 922  LEU A CA    1 
ATOM   6481 C  C     . LEU A 1 922  ? 96.977  117.207 91.194  1.00 45.26  ? 922  LEU A C     1 
ATOM   6482 O  O     . LEU A 1 922  ? 96.967  117.328 89.963  1.00 45.26  ? 922  LEU A O     1 
ATOM   6483 C  CB    . LEU A 1 922  ? 94.904  116.409 92.354  1.00 45.26  ? 922  LEU A CB    1 
ATOM   6484 C  CG    . LEU A 1 922  ? 93.873  116.712 91.264  1.00 45.26  ? 922  LEU A CG    1 
ATOM   6485 C  CD1   . LEU A 1 922  ? 93.999  115.728 90.111  1.00 45.26  ? 922  LEU A CD1   1 
ATOM   6486 C  CD2   . LEU A 1 922  ? 92.463  116.699 91.832  1.00 45.26  ? 922  LEU A CD2   1 
ATOM   6487 N  N     . ALA A 1 923  ? 97.568  118.099 91.991  1.00 45.80  ? 923  ALA A N     1 
ATOM   6488 C  CA    . ALA A 1 923  ? 98.285  119.235 91.422  1.00 45.80  ? 923  ALA A CA    1 
ATOM   6489 C  C     . ALA A 1 923  ? 99.502  118.778 90.631  1.00 45.80  ? 923  ALA A C     1 
ATOM   6490 O  O     . ALA A 1 923  ? 99.825  119.354 89.586  1.00 45.80  ? 923  ALA A O     1 
ATOM   6491 C  CB    . ALA A 1 923  ? 98.695  120.205 92.529  1.00 45.80  ? 923  ALA A CB    1 
ATOM   6492 N  N     . LEU A 1 924  ? 100.198 117.749 91.120  1.00 48.05  ? 924  LEU A N     1 
ATOM   6493 C  CA    . LEU A 1 924  ? 101.373 117.249 90.415  1.00 48.05  ? 924  LEU A CA    1 
ATOM   6494 C  C     . LEU A 1 924  ? 100.991 116.642 89.070  1.00 48.05  ? 924  LEU A C     1 
ATOM   6495 O  O     . LEU A 1 924  ? 101.663 116.874 88.059  1.00 48.05  ? 924  LEU A O     1 
ATOM   6496 C  CB    . LEU A 1 924  ? 102.111 116.233 91.291  1.00 48.05  ? 924  LEU A CB    1 
ATOM   6497 C  CG    . LEU A 1 924  ? 103.475 115.702 90.845  1.00 48.05  ? 924  LEU A CG    1 
ATOM   6498 C  CD1   . LEU A 1 924  ? 104.313 115.359 92.061  1.00 48.05  ? 924  LEU A CD1   1 
ATOM   6499 C  CD2   . LEU A 1 924  ? 103.330 114.474 89.969  1.00 48.05  ? 924  LEU A CD2   1 
ATOM   6500 N  N     . TYR A 1 925  ? 99.910  115.856 89.036  1.00 50.51  ? 925  TYR A N     1 
ATOM   6501 C  CA    . TYR A 1 925  ? 99.496  115.249 87.772  1.00 50.51  ? 925  TYR A CA    1 
ATOM   6502 C  C     . TYR A 1 925  ? 98.911  116.281 86.817  1.00 50.51  ? 925  TYR A C     1 
ATOM   6503 O  O     . TYR A 1 925  ? 99.155  116.223 85.607  1.00 50.51  ? 925  TYR A O     1 
ATOM   6504 C  CB    . TYR A 1 925  ? 98.499  114.117 88.019  1.00 50.51  ? 925  TYR A CB    1 
ATOM   6505 C  CG    . TYR A 1 925  ? 99.099  112.911 88.702  1.00 50.51  ? 925  TYR A CG    1 
ATOM   6506 C  CD1   . TYR A 1 925  ? 100.475 112.747 88.781  1.00 50.51  ? 925  TYR A CD1   1 
ATOM   6507 C  CD2   . TYR A 1 925  ? 98.292  111.927 89.252  1.00 50.51  ? 925  TYR A CD2   1 
ATOM   6508 C  CE1   . TYR A 1 925  ? 101.029 111.644 89.399  1.00 50.51  ? 925  TYR A CE1   1 
ATOM   6509 C  CE2   . TYR A 1 925  ? 98.836  110.821 89.870  1.00 50.51  ? 925  TYR A CE2   1 
ATOM   6510 C  CZ    . TYR A 1 925  ? 100.205 110.684 89.942  1.00 50.51  ? 925  TYR A CZ    1 
ATOM   6511 O  OH    . TYR A 1 925  ? 100.751 109.583 90.559  1.00 50.51  ? 925  TYR A OH    1 
ATOM   6512 N  N     . GLY A 1 926  ? 98.135  117.233 87.336  1.00 50.82  ? 926  GLY A N     1 
ATOM   6513 C  CA    . GLY A 1 926  ? 97.538  118.233 86.466  1.00 50.82  ? 926  GLY A CA    1 
ATOM   6514 C  C     . GLY A 1 926  ? 98.573  119.077 85.747  1.00 50.82  ? 926  GLY A C     1 
ATOM   6515 O  O     . GLY A 1 926  ? 98.312  119.609 84.665  1.00 50.82  ? 926  GLY A O     1 
ATOM   6516 N  N     . SER A 1 927  ? 99.761  119.210 86.337  1.00 52.04  ? 927  SER A N     1 
ATOM   6517 C  CA    . SER A 1 927  ? 100.828 119.976 85.703  1.00 52.04  ? 927  SER A CA    1 
ATOM   6518 C  C     . SER A 1 927  ? 101.308 119.304 84.421  1.00 52.04  ? 927  SER A C     1 
ATOM   6519 O  O     . SER A 1 927  ? 101.524 119.968 83.402  1.00 52.04  ? 927  SER A O     1 
ATOM   6520 C  CB    . SER A 1 927  ? 101.988 120.154 86.678  1.00 52.04  ? 927  SER A CB    1 
ATOM   6521 O  OG    . SER A 1 927  ? 103.138 120.618 86.000  1.00 52.04  ? 927  SER A OG    1 
ATOM   6522 N  N     . GLU A 1 928  ? 101.494 117.983 84.460  1.00 53.79  ? 928  GLU A N     1 
ATOM   6523 C  CA    . GLU A 1 928  ? 102.034 117.275 83.302  1.00 53.79  ? 928  GLU A CA    1 
ATOM   6524 C  C     . GLU A 1 928  ? 101.052 117.278 82.139  1.00 53.79  ? 928  GLU A C     1 
ATOM   6525 O  O     . GLU A 1 928  ? 101.459 117.342 80.972  1.00 53.79  ? 928  GLU A O     1 
ATOM   6526 C  CB    . GLU A 1 928  ? 102.406 115.846 83.693  1.00 53.79  ? 928  GLU A CB    1 
ATOM   6527 C  CG    . GLU A 1 928  ? 103.393 115.768 84.843  1.00 53.79  ? 928  GLU A CG    1 
ATOM   6528 C  CD    . GLU A 1 928  ? 103.377 114.423 85.537  1.00 53.79  ? 928  GLU A CD    1 
ATOM   6529 O  OE1   . GLU A 1 928  ? 103.363 114.402 86.784  1.00 53.79  ? 928  GLU A OE1   1 
ATOM   6530 O  OE2   . GLU A 1 928  ? 103.372 113.389 84.839  1.00 53.79  ? 928  GLU A OE2   1 
ATOM   6531 N  N     . ALA A 1 929  ? 99.754  117.200 82.435  1.00 52.75  ? 929  ALA A N     1 
ATOM   6532 C  CA    . ALA A 1 929  ? 98.753  117.262 81.376  1.00 52.75  ? 929  ALA A CA    1 
ATOM   6533 C  C     . ALA A 1 929  ? 98.808  118.599 80.650  1.00 52.75  ? 929  ALA A C     1 
ATOM   6534 O  O     . ALA A 1 929  ? 98.693  118.653 79.420  1.00 52.75  ? 929  ALA A O     1 
ATOM   6535 C  CB    . ALA A 1 929  ? 97.362  117.020 81.957  1.00 52.75  ? 929  ALA A CB    1 
ATOM   6536 N  N     . LEU A 1 930  ? 98.985  119.691 81.397  1.00 57.56  ? 930  LEU A N     1 
ATOM   6537 C  CA    . LEU A 1 930  ? 99.125  121.000 80.770  1.00 57.56  ? 930  LEU A CA    1 
ATOM   6538 C  C     . LEU A 1 930  ? 100.385 121.066 79.918  1.00 57.56  ? 930  LEU A C     1 
ATOM   6539 O  O     . LEU A 1 930  ? 100.386 121.680 78.845  1.00 57.56  ? 930  LEU A O     1 
ATOM   6540 C  CB    . LEU A 1 930  ? 99.137  122.093 81.837  1.00 57.56  ? 930  LEU A CB    1 
ATOM   6541 C  CG    . LEU A 1 930  ? 99.213  123.534 81.335  1.00 57.56  ? 930  LEU A CG    1 
ATOM   6542 C  CD1   . LEU A 1 930  ? 97.989  123.874 80.502  1.00 57.56  ? 930  LEU A CD1   1 
ATOM   6543 C  CD2   . LEU A 1 930  ? 99.356  124.498 82.501  1.00 57.56  ? 930  LEU A CD2   1 
ATOM   6544 N  N     . ILE A 1 931  ? 101.468 120.437 80.380  1.00 58.93  ? 931  ILE A N     1 
ATOM   6545 C  CA    . ILE A 1 931  ? 102.703 120.400 79.600  1.00 58.93  ? 931  ILE A CA    1 
ATOM   6546 C  C     . ILE A 1 931  ? 102.467 119.690 78.274  1.00 58.93  ? 931  ILE A C     1 
ATOM   6547 O  O     . ILE A 1 931  ? 102.877 120.169 77.208  1.00 58.93  ? 931  ILE A O     1 
ATOM   6548 C  CB    . ILE A 1 931  ? 103.825 119.723 80.408  1.00 58.93  ? 931  ILE A CB    1 
ATOM   6549 C  CG1   . ILE A 1 931  ? 104.360 120.668 81.486  1.00 58.93  ? 931  ILE A CG1   1 
ATOM   6550 C  CG2   . ILE A 1 931  ? 104.944 119.260 79.488  1.00 58.93  ? 931  ILE A CG2   1 
ATOM   6551 C  CD1   . ILE A 1 931  ? 105.000 121.922 80.942  1.00 58.93  ? 931  ILE A CD1   1 
ATOM   6552 N  N     . LEU A 1 932  ? 101.796 118.538 78.321  1.00 59.01  ? 932  LEU A N     1 
ATOM   6553 C  CA    . LEU A 1 932  ? 101.526 117.793 77.095  1.00 59.01  ? 932  LEU A CA    1 
ATOM   6554 C  C     . LEU A 1 932  ? 100.602 118.570 76.164  1.00 59.01  ? 932  LEU A C     1 
ATOM   6555 O  O     . LEU A 1 932  ? 100.796 118.561 74.944  1.00 59.01  ? 932  LEU A O     1 
ATOM   6556 C  CB    . LEU A 1 932  ? 100.930 116.427 77.427  1.00 59.01  ? 932  LEU A CB    1 
ATOM   6557 C  CG    . LEU A 1 932  ? 100.845 115.448 76.255  1.00 59.01  ? 932  LEU A CG    1 
ATOM   6558 C  CD1   . LEU A 1 932  ? 102.209 115.268 75.616  1.00 59.01  ? 932  LEU A CD1   1 
ATOM   6559 C  CD2   . LEU A 1 932  ? 100.291 114.113 76.714  1.00 59.01  ? 932  LEU A CD2   1 
ATOM   6560 N  N     . TRP A 1 933  ? 99.592  119.246 76.718  1.00 59.33  ? 933  TRP A N     1 
ATOM   6561 C  CA    . TRP A 1 933  ? 98.689  120.035 75.884  1.00 59.33  ? 933  TRP A CA    1 
ATOM   6562 C  C     . TRP A 1 933  ? 99.419  121.194 75.213  1.00 59.33  ? 933  TRP A C     1 
ATOM   6563 O  O     . TRP A 1 933  ? 99.199  121.475 74.028  1.00 59.33  ? 933  TRP A O     1 
ATOM   6564 C  CB    . TRP A 1 933  ? 97.520  120.549 76.723  1.00 59.33  ? 933  TRP A CB    1 
ATOM   6565 C  CG    . TRP A 1 933  ? 96.525  121.342 75.940  1.00 59.33  ? 933  TRP A CG    1 
ATOM   6566 C  CD1   . TRP A 1 933  ? 95.513  120.853 75.168  1.00 59.33  ? 933  TRP A CD1   1 
ATOM   6567 C  CD2   . TRP A 1 933  ? 96.441  122.769 75.856  1.00 59.33  ? 933  TRP A CD2   1 
ATOM   6568 N  NE1   . TRP A 1 933  ? 94.805  121.886 74.605  1.00 59.33  ? 933  TRP A NE1   1 
ATOM   6569 C  CE2   . TRP A 1 933  ? 95.354  123.073 75.012  1.00 59.33  ? 933  TRP A CE2   1 
ATOM   6570 C  CE3   . TRP A 1 933  ? 97.178  123.818 76.410  1.00 59.33  ? 933  TRP A CE3   1 
ATOM   6571 C  CZ2   . TRP A 1 933  ? 94.988  124.382 74.710  1.00 59.33  ? 933  TRP A CZ2   1 
ATOM   6572 C  CZ3   . TRP A 1 933  ? 96.813  125.117 76.109  1.00 59.33  ? 933  TRP A CZ3   1 
ATOM   6573 C  CH2   . TRP A 1 933  ? 95.728  125.387 75.267  1.00 59.33  ? 933  TRP A CH2   1 
ATOM   6574 N  N     . TYR A 1 934  ? 100.288 121.881 75.958  1.00 65.26  ? 934  TYR A N     1 
ATOM   6575 C  CA    . TYR A 1 934  ? 101.063 122.975 75.382  1.00 65.26  ? 934  TYR A CA    1 
ATOM   6576 C  C     . TYR A 1 934  ? 101.996 122.462 74.291  1.00 65.26  ? 934  TYR A C     1 
ATOM   6577 O  O     . TYR A 1 934  ? 102.136 123.092 73.235  1.00 65.26  ? 934  TYR A O     1 
ATOM   6578 C  CB    . TYR A 1 934  ? 101.842 123.688 76.490  1.00 65.26  ? 934  TYR A CB    1 
ATOM   6579 C  CG    . TYR A 1 934  ? 102.574 124.951 76.078  1.00 65.26  ? 934  TYR A CG    1 
ATOM   6580 C  CD1   . TYR A 1 934  ? 103.692 124.906 75.255  1.00 65.26  ? 934  TYR A CD1   1 
ATOM   6581 C  CD2   . TYR A 1 934  ? 102.144 126.193 76.525  1.00 65.26  ? 934  TYR A CD2   1 
ATOM   6582 C  CE1   . TYR A 1 934  ? 104.355 126.060 74.887  1.00 65.26  ? 934  TYR A CE1   1 
ATOM   6583 C  CE2   . TYR A 1 934  ? 102.801 127.352 76.162  1.00 65.26  ? 934  TYR A CE2   1 
ATOM   6584 C  CZ    . TYR A 1 934  ? 103.906 127.280 75.343  1.00 65.26  ? 934  TYR A CZ    1 
ATOM   6585 O  OH    . TYR A 1 934  ? 104.563 128.432 74.980  1.00 65.26  ? 934  TYR A OH    1 
ATOM   6586 N  N     . GLY A 1 935  ? 102.644 121.320 74.530  1.00 65.69  ? 935  GLY A N     1 
ATOM   6587 C  CA    . GLY A 1 935  ? 103.488 120.735 73.501  1.00 65.69  ? 935  GLY A CA    1 
ATOM   6588 C  C     . GLY A 1 935  ? 102.705 120.350 72.262  1.00 65.69  ? 935  GLY A C     1 
ATOM   6589 O  O     . GLY A 1 935  ? 103.178 120.523 71.138  1.00 65.69  ? 935  GLY A O     1 
ATOM   6590 N  N     . ALA A 1 936  ? 101.494 119.827 72.452  1.00 65.14  ? 936  ALA A N     1 
ATOM   6591 C  CA    . ALA A 1 936  ? 100.636 119.503 71.318  1.00 65.14  ? 936  ALA A CA    1 
ATOM   6592 C  C     . ALA A 1 936  ? 100.277 120.748 70.522  1.00 65.14  ? 936  ALA A C     1 
ATOM   6593 O  O     . ALA A 1 936  ? 100.305 120.737 69.285  1.00 65.14  ? 936  ALA A O     1 
ATOM   6594 C  CB    . ALA A 1 936  ? 99.369  118.816 71.813  1.00 65.14  ? 936  ALA A CB    1 
ATOM   6595 N  N     . HIS A 1 937  ? 99.923  121.829 71.218  1.00 69.21  ? 937  HIS A N     1 
ATOM   6596 C  CA    . HIS A 1 937  ? 99.590  123.069 70.528  1.00 69.21  ? 937  HIS A CA    1 
ATOM   6597 C  C     . HIS A 1 937  ? 100.791 123.600 69.758  1.00 69.21  ? 937  HIS A C     1 
ATOM   6598 O  O     . HIS A 1 937  ? 100.646 124.112 68.641  1.00 69.21  ? 937  HIS A O     1 
ATOM   6599 C  CB    . HIS A 1 937  ? 99.084  124.106 71.529  1.00 69.21  ? 937  HIS A CB    1 
ATOM   6600 C  CG    . HIS A 1 937  ? 98.531  125.341 70.891  1.00 69.21  ? 937  HIS A CG    1 
ATOM   6601 N  ND1   . HIS A 1 937  ? 99.077  126.590 71.090  1.00 69.21  ? 937  HIS A ND1   1 
ATOM   6602 C  CD2   . HIS A 1 937  ? 97.479  125.518 70.057  1.00 69.21  ? 937  HIS A CD2   1 
ATOM   6603 C  CE1   . HIS A 1 937  ? 98.385  127.484 70.406  1.00 69.21  ? 937  HIS A CE1   1 
ATOM   6604 N  NE2   . HIS A 1 937  ? 97.411  126.860 69.771  1.00 69.21  ? 937  HIS A NE2   1 
ATOM   6605 N  N     . LEU A 1 938  ? 101.988 123.486 70.340  1.00 70.49  ? 938  LEU A N     1 
ATOM   6606 C  CA    . LEU A 1 938  ? 103.198 123.880 69.624  1.00 70.49  ? 938  LEU A CA    1 
ATOM   6607 C  C     . LEU A 1 938  ? 103.420 123.010 68.392  1.00 70.49  ? 938  LEU A C     1 
ATOM   6608 O  O     . LEU A 1 938  ? 103.850 123.505 67.344  1.00 70.49  ? 938  LEU A O     1 
ATOM   6609 C  CB    . LEU A 1 938  ? 104.408 123.811 70.554  1.00 70.49  ? 938  LEU A CB    1 
ATOM   6610 C  CG    . LEU A 1 938  ? 104.718 125.083 71.342  1.00 70.49  ? 938  LEU A CG    1 
ATOM   6611 C  CD1   . LEU A 1 938  ? 106.116 125.016 71.936  1.00 70.49  ? 938  LEU A CD1   1 
ATOM   6612 C  CD2   . LEU A 1 938  ? 104.565 126.308 70.456  1.00 70.49  ? 938  LEU A CD2   1 
ATOM   6613 N  N     . VAL A 1 939  ? 103.146 121.708 68.504  1.00 73.25  ? 939  VAL A N     1 
ATOM   6614 C  CA    . VAL A 1 939  ? 103.267 120.818 67.351  1.00 73.25  ? 939  VAL A CA    1 
ATOM   6615 C  C     . VAL A 1 939  ? 102.317 121.255 66.245  1.00 73.25  ? 939  VAL A C     1 
ATOM   6616 O  O     . VAL A 1 939  ? 102.683 121.278 65.063  1.00 73.25  ? 939  VAL A O     1 
ATOM   6617 C  CB    . VAL A 1 939  ? 103.011 119.358 67.769  1.00 73.25  ? 939  VAL A CB    1 
ATOM   6618 C  CG1   . VAL A 1 939  ? 102.824 118.477 66.543  1.00 73.25  ? 939  VAL A CG1   1 
ATOM   6619 C  CG2   . VAL A 1 939  ? 104.153 118.839 68.619  1.00 73.25  ? 939  VAL A CG2   1 
ATOM   6620 N  N     . SER A 1 940  ? 101.082 121.609 66.611  1.00 76.54  ? 940  SER A N     1 
ATOM   6621 C  CA    . SER A 1 940  ? 100.122 122.078 65.616  1.00 76.54  ? 940  SER A CA    1 
ATOM   6622 C  C     . SER A 1 940  ? 100.609 123.339 64.918  1.00 76.54  ? 940  SER A C     1 
ATOM   6623 O  O     . SER A 1 940  ? 100.314 123.548 63.736  1.00 76.54  ? 940  SER A O     1 
ATOM   6624 C  CB    . SER A 1 940  ? 98.765  122.329 66.272  1.00 76.54  ? 940  SER A CB    1 
ATOM   6625 O  OG    . SER A 1 940  ? 97.838  122.861 65.341  1.00 76.54  ? 940  SER A OG    1 
ATOM   6626 N  N     . LYS A 1 941  ? 101.352 124.189 65.626  1.00 75.74  ? 941  LYS A N     1 
ATOM   6627 C  CA    . LYS A 1 941  ? 101.853 125.425 65.042  1.00 75.74  ? 941  LYS A CA    1 
ATOM   6628 C  C     . LYS A 1 941  ? 103.118 125.216 64.216  1.00 75.74  ? 941  LYS A C     1 
ATOM   6629 O  O     . LYS A 1 941  ? 103.467 126.089 63.414  1.00 75.74  ? 941  LYS A O     1 
ATOM   6630 C  CB    . LYS A 1 941  ? 102.103 126.451 66.155  1.00 75.74  ? 941  LYS A CB    1 
ATOM   6631 C  CG    . LYS A 1 941  ? 102.349 127.882 65.688  1.00 75.74  ? 941  LYS A CG    1 
ATOM   6632 C  CD    . LYS A 1 941  ? 103.833 128.219 65.651  1.00 75.74  ? 941  LYS A CD    1 
ATOM   6633 C  CE    . LYS A 1 941  ? 104.083 129.539 64.939  1.00 75.74  ? 941  LYS A CE    1 
ATOM   6634 N  NZ    . LYS A 1 941  ? 105.519 129.719 64.588  1.00 75.74  ? 941  LYS A NZ    1 
ATOM   6635 N  N     . GLY A 1 942  ? 103.785 124.071 64.349  1.00 78.96  ? 942  GLY A N     1 
ATOM   6636 C  CA    . GLY A 1 942  ? 105.065 123.900 63.688  1.00 78.96  ? 942  GLY A CA    1 
ATOM   6637 C  C     . GLY A 1 942  ? 106.145 123.242 64.524  1.00 78.96  ? 942  GLY A C     1 
ATOM   6638 O  O     . GLY A 1 942  ? 106.031 122.067 64.885  1.00 78.96  ? 942  GLY A O     1 
ATOM   6639 N  N     . VAL A 1 943  ? 107.202 123.994 64.829  1.00 78.58  ? 943  VAL A N     1 
ATOM   6640 C  CA    . VAL A 1 943  ? 108.436 123.467 65.409  1.00 78.58  ? 943  VAL A CA    1 
ATOM   6641 C  C     . VAL A 1 943  ? 108.182 122.839 66.774  1.00 78.58  ? 943  VAL A C     1 
ATOM   6642 O  O     . VAL A 1 943  ? 107.097 122.988 67.346  1.00 78.58  ? 943  VAL A O     1 
ATOM   6643 C  CB    . VAL A 1 943  ? 109.504 124.571 65.512  1.00 78.58  ? 943  VAL A CB    1 
ATOM   6644 C  CG1   . VAL A 1 943  ? 109.832 125.123 64.135  1.00 78.58  ? 943  VAL A CG1   1 
ATOM   6645 C  CG2   . VAL A 1 943  ? 109.028 125.680 66.436  1.00 78.58  ? 943  VAL A CG2   1 
ATOM   6646 N  N     . SER A 1 944  ? 109.186 122.122 67.290  1.00 79.40  ? 944  SER A N     1 
ATOM   6647 C  CA    . SER A 1 944  ? 109.073 121.327 68.516  1.00 79.40  ? 944  SER A CA    1 
ATOM   6648 C  C     . SER A 1 944  ? 108.040 120.213 68.334  1.00 79.40  ? 944  SER A C     1 
ATOM   6649 O  O     . SER A 1 944  ? 107.003 120.165 68.997  1.00 79.40  ? 944  SER A O     1 
ATOM   6650 C  CB    . SER A 1 944  ? 108.744 122.206 69.728  1.00 79.40  ? 944  SER A CB    1 
ATOM   6651 O  OG    . SER A 1 944  ? 108.386 121.416 70.848  1.00 79.40  ? 944  SER A OG    1 
ATOM   6652 N  N     . THR A 1 945  ? 108.360 119.308 67.415  1.00 78.54  ? 945  THR A N     1 
ATOM   6653 C  CA    . THR A 1 945  ? 107.422 118.310 66.920  1.00 78.54  ? 945  THR A CA    1 
ATOM   6654 C  C     . THR A 1 945  ? 107.272 117.153 67.909  1.00 78.54  ? 945  THR A C     1 
ATOM   6655 O  O     . THR A 1 945  ? 107.653 117.237 69.080  1.00 78.54  ? 945  THR A O     1 
ATOM   6656 C  CB    . THR A 1 945  ? 107.866 117.808 65.548  1.00 78.54  ? 945  THR A CB    1 
ATOM   6657 O  OG1   . THR A 1 945  ? 106.989 116.761 65.115  1.00 78.54  ? 945  THR A OG1   1 
ATOM   6658 C  CG2   . THR A 1 945  ? 109.289 117.276 65.614  1.00 78.54  ? 945  THR A CG2   1 
ATOM   6659 N  N     . PHE A 1 946  ? 106.688 116.058 67.415  1.00 79.93  ? 946  PHE A N     1 
ATOM   6660 C  CA    . PHE A 1 946  ? 106.326 114.881 68.198  1.00 79.93  ? 946  PHE A CA    1 
ATOM   6661 C  C     . PHE A 1 946  ? 107.430 114.406 69.140  1.00 79.93  ? 946  PHE A C     1 
ATOM   6662 O  O     . PHE A 1 946  ? 107.186 114.156 70.326  1.00 79.93  ? 946  PHE A O     1 
ATOM   6663 C  CB    . PHE A 1 946  ? 105.929 113.771 67.212  1.00 79.93  ? 946  PHE A CB    1 
ATOM   6664 C  CG    . PHE A 1 946  ? 105.518 112.473 67.855  1.00 79.93  ? 946  PHE A CG    1 
ATOM   6665 C  CD1   . PHE A 1 946  ? 106.467 111.534 68.232  1.00 79.93  ? 946  PHE A CD1   1 
ATOM   6666 C  CD2   . PHE A 1 946  ? 104.180 112.177 68.051  1.00 79.93  ? 946  PHE A CD2   1 
ATOM   6667 C  CE1   . PHE A 1 946  ? 106.090 110.336 68.810  1.00 79.93  ? 946  PHE A CE1   1 
ATOM   6668 C  CE2   . PHE A 1 946  ? 103.796 110.980 68.627  1.00 79.93  ? 946  PHE A CE2   1 
ATOM   6669 C  CZ    . PHE A 1 946  ? 104.753 110.058 69.005  1.00 79.93  ? 946  PHE A CZ    1 
ATOM   6670 N  N     . SER A 1 947  ? 108.653 114.271 68.624  1.00 72.35  ? 947  SER A N     1 
ATOM   6671 C  CA    . SER A 1 947  ? 109.709 113.604 69.382  1.00 72.35  ? 947  SER A CA    1 
ATOM   6672 C  C     . SER A 1 947  ? 110.095 114.390 70.631  1.00 72.35  ? 947  SER A C     1 
ATOM   6673 O  O     . SER A 1 947  ? 110.222 113.819 71.720  1.00 72.35  ? 947  SER A O     1 
ATOM   6674 C  CB    . SER A 1 947  ? 110.928 113.383 68.487  1.00 72.35  ? 947  SER A CB    1 
ATOM   6675 O  OG    . SER A 1 947  ? 110.543 112.880 67.220  1.00 72.35  ? 947  SER A OG    1 
ATOM   6676 N  N     . LYS A 1 948  ? 110.290 115.703 70.493  1.00 68.04  ? 948  LYS A N     1 
ATOM   6677 C  CA    . LYS A 1 948  ? 110.839 116.491 71.594  1.00 68.04  ? 948  LYS A CA    1 
ATOM   6678 C  C     . LYS A 1 948  ? 109.877 116.561 72.776  1.00 68.04  ? 948  LYS A C     1 
ATOM   6679 O  O     . LYS A 1 948  ? 110.291 116.441 73.934  1.00 68.04  ? 948  LYS A O     1 
ATOM   6680 C  CB    . LYS A 1 948  ? 111.194 117.896 71.106  1.00 68.04  ? 948  LYS A CB    1 
ATOM   6681 C  CG    . LYS A 1 948  ? 112.144 117.919 69.921  1.00 68.04  ? 948  LYS A CG    1 
ATOM   6682 C  CD    . LYS A 1 948  ? 113.378 117.073 70.191  1.00 68.04  ? 948  LYS A CD    1 
ATOM   6683 C  CE    . LYS A 1 948  ? 114.457 117.326 69.152  1.00 68.04  ? 948  LYS A CE    1 
ATOM   6684 N  NZ    . LYS A 1 948  ? 114.762 118.776 69.015  1.00 68.04  ? 948  LYS A NZ    1 
ATOM   6685 N  N     . VAL A 1 949  ? 108.586 116.763 72.504  1.00 61.99  ? 949  VAL A N     1 
ATOM   6686 C  CA    . VAL A 1 949  ? 107.633 116.990 73.587  1.00 61.99  ? 949  VAL A CA    1 
ATOM   6687 C  C     . VAL A 1 949  ? 107.397 115.713 74.388  1.00 61.99  ? 949  VAL A C     1 
ATOM   6688 O  O     . VAL A 1 949  ? 107.310 115.748 75.622  1.00 61.99  ? 949  VAL A O     1 
ATOM   6689 C  CB    . VAL A 1 949  ? 106.320 117.571 73.030  1.00 61.99  ? 949  VAL A CB    1 
ATOM   6690 C  CG1   . VAL A 1 949  ? 106.550 118.983 72.519  1.00 61.99  ? 949  VAL A CG1   1 
ATOM   6691 C  CG2   . VAL A 1 949  ? 105.770 116.693 71.919  1.00 61.99  ? 949  VAL A CG2   1 
ATOM   6692 N  N     . ILE A 1 950  ? 107.288 114.569 73.709  1.00 59.18  ? 950  ILE A N     1 
ATOM   6693 C  CA    . ILE A 1 950  ? 106.983 113.326 74.413  1.00 59.18  ? 950  ILE A CA    1 
ATOM   6694 C  C     . ILE A 1 950  ? 108.182 112.842 75.219  1.00 59.18  ? 950  ILE A C     1 
ATOM   6695 O  O     . ILE A 1 950  ? 108.017 112.254 76.296  1.00 59.18  ? 950  ILE A O     1 
ATOM   6696 C  CB    . ILE A 1 950  ? 106.480 112.268 73.415  1.00 59.18  ? 950  ILE A CB    1 
ATOM   6697 C  CG1   . ILE A 1 950  ? 105.051 112.606 72.993  1.00 59.18  ? 950  ILE A CG1   1 
ATOM   6698 C  CG2   . ILE A 1 950  ? 106.531 110.875 74.016  1.00 59.18  ? 950  ILE A CG2   1 
ATOM   6699 C  CD1   . ILE A 1 950  ? 104.444 111.612 72.048  1.00 59.18  ? 950  ILE A CD1   1 
ATOM   6700 N  N     . LYS A 1 951  ? 109.401 113.078 74.731  1.00 57.99  ? 951  LYS A N     1 
ATOM   6701 C  CA    . LYS A 1 951  ? 110.580 112.778 75.537  1.00 57.99  ? 951  LYS A CA    1 
ATOM   6702 C  C     . LYS A 1 951  ? 110.569 113.579 76.832  1.00 57.99  ? 951  LYS A C     1 
ATOM   6703 O  O     . LYS A 1 951  ? 110.857 113.042 77.911  1.00 57.99  ? 951  LYS A O     1 
ATOM   6704 C  CB    . LYS A 1 951  ? 111.850 113.068 74.738  1.00 57.99  ? 951  LYS A CB    1 
ATOM   6705 C  CG    . LYS A 1 951  ? 113.128 113.021 75.559  1.00 57.99  ? 951  LYS A CG    1 
ATOM   6706 C  CD    . LYS A 1 951  ? 114.350 113.257 74.687  1.00 57.99  ? 951  LYS A CD    1 
ATOM   6707 C  CE    . LYS A 1 951  ? 114.419 112.251 73.549  1.00 57.99  ? 951  LYS A CE    1 
ATOM   6708 N  NZ    . LYS A 1 951  ? 115.080 112.821 72.344  1.00 57.99  ? 951  LYS A NZ    1 
ATOM   6709 N  N     . VAL A 1 952  ? 110.222 114.865 76.743  1.00 54.30  ? 952  VAL A N     1 
ATOM   6710 C  CA    . VAL A 1 952  ? 110.076 115.689 77.938  1.00 54.30  ? 952  VAL A CA    1 
ATOM   6711 C  C     . VAL A 1 952  ? 109.007 115.109 78.853  1.00 54.30  ? 952  VAL A C     1 
ATOM   6712 O  O     . VAL A 1 952  ? 109.199 115.006 80.069  1.00 54.30  ? 952  VAL A O     1 
ATOM   6713 C  CB    . VAL A 1 952  ? 109.760 117.144 77.543  1.00 54.30  ? 952  VAL A CB    1 
ATOM   6714 C  CG1   . VAL A 1 952  ? 109.115 117.888 78.693  1.00 54.30  ? 952  VAL A CG1   1 
ATOM   6715 C  CG2   . VAL A 1 952  ? 111.021 117.854 77.106  1.00 54.30  ? 952  VAL A CG2   1 
ATOM   6716 N  N     . PHE A 1 953  ? 107.868 114.713 78.284  1.00 54.03  ? 953  PHE A N     1 
ATOM   6717 C  CA    . PHE A 1 953  ? 106.786 114.174 79.100  1.00 54.03  ? 953  PHE A CA    1 
ATOM   6718 C  C     . PHE A 1 953  ? 107.242 112.934 79.862  1.00 54.03  ? 953  PHE A C     1 
ATOM   6719 O  O     . PHE A 1 953  ? 106.982 112.798 81.063  1.00 54.03  ? 953  PHE A O     1 
ATOM   6720 C  CB    . PHE A 1 953  ? 105.580 113.857 78.217  1.00 54.03  ? 953  PHE A CB    1 
ATOM   6721 C  CG    . PHE A 1 953  ? 104.399 113.327 78.972  1.00 54.03  ? 953  PHE A CG    1 
ATOM   6722 C  CD1   . PHE A 1 953  ? 103.568 114.184 79.670  1.00 54.03  ? 953  PHE A CD1   1 
ATOM   6723 C  CD2   . PHE A 1 953  ? 104.115 111.973 78.979  1.00 54.03  ? 953  PHE A CD2   1 
ATOM   6724 C  CE1   . PHE A 1 953  ? 102.478 113.701 80.364  1.00 54.03  ? 953  PHE A CE1   1 
ATOM   6725 C  CE2   . PHE A 1 953  ? 103.027 111.485 79.673  1.00 54.03  ? 953  PHE A CE2   1 
ATOM   6726 C  CZ    . PHE A 1 953  ? 102.208 112.349 80.365  1.00 54.03  ? 953  PHE A CZ    1 
ATOM   6727 N  N     . VAL A 1 954  ? 107.947 112.031 79.180  1.00 51.79  ? 954  VAL A N     1 
ATOM   6728 C  CA    . VAL A 1 954  ? 108.406 110.799 79.815  1.00 51.79  ? 954  VAL A CA    1 
ATOM   6729 C  C     . VAL A 1 954  ? 109.429 111.098 80.908  1.00 51.79  ? 954  VAL A C     1 
ATOM   6730 O  O     . VAL A 1 954  ? 109.377 110.518 82.002  1.00 51.79  ? 954  VAL A O     1 
ATOM   6731 C  CB    . VAL A 1 954  ? 108.969 109.835 78.755  1.00 51.79  ? 954  VAL A CB    1 
ATOM   6732 C  CG1   . VAL A 1 954  ? 109.816 108.758 79.406  1.00 51.79  ? 954  VAL A CG1   1 
ATOM   6733 C  CG2   . VAL A 1 954  ? 107.837 109.213 77.956  1.00 51.79  ? 954  VAL A CG2   1 
ATOM   6734 N  N     . VAL A 1 955  ? 110.380 111.996 80.630  1.00 52.27  ? 955  VAL A N     1 
ATOM   6735 C  CA    . VAL A 1 955  ? 111.402 112.318 81.624  1.00 52.27  ? 955  VAL A CA    1 
ATOM   6736 C  C     . VAL A 1 955  ? 110.768 112.929 82.866  1.00 52.27  ? 955  VAL A C     1 
ATOM   6737 O  O     . VAL A 1 955  ? 111.107 112.564 84.000  1.00 52.27  ? 955  VAL A O     1 
ATOM   6738 C  CB    . VAL A 1 955  ? 112.468 113.247 81.016  1.00 52.27  ? 955  VAL A CB    1 
ATOM   6739 C  CG1   . VAL A 1 955  ? 113.334 113.845 82.109  1.00 52.27  ? 955  VAL A CG1   1 
ATOM   6740 C  CG2   . VAL A 1 955  ? 113.323 112.486 80.020  1.00 52.27  ? 955  VAL A CG2   1 
ATOM   6741 N  N     . LEU A 1 956  ? 109.838 113.867 82.673  1.00 51.76  ? 956  LEU A N     1 
ATOM   6742 C  CA    . LEU A 1 956  ? 109.124 114.450 83.804  1.00 51.76  ? 956  LEU A CA    1 
ATOM   6743 C  C     . LEU A 1 956  ? 108.312 113.411 84.566  1.00 51.76  ? 956  LEU A C     1 
ATOM   6744 O  O     . LEU A 1 956  ? 108.265 113.447 85.798  1.00 51.76  ? 956  LEU A O     1 
ATOM   6745 C  CB    . LEU A 1 956  ? 108.237 115.600 83.330  1.00 51.76  ? 956  LEU A CB    1 
ATOM   6746 C  CG    . LEU A 1 956  ? 108.886 116.978 83.170  1.00 51.76  ? 956  LEU A CG    1 
ATOM   6747 C  CD1   . LEU A 1 956  ? 109.892 117.080 82.053  1.00 51.76  ? 956  LEU A CD1   1 
ATOM   6748 C  CD2   . LEU A 1 956  ? 107.762 117.954 82.913  1.00 51.76  ? 956  LEU A CD2   1 
ATOM   6749 N  N     . VAL A 1 957  ? 107.666 112.480 83.862  1.00 49.57  ? 957  VAL A N     1 
ATOM   6750 C  CA    . VAL A 1 957  ? 106.894 111.448 84.552  1.00 49.57  ? 957  VAL A CA    1 
ATOM   6751 C  C     . VAL A 1 957  ? 107.804 110.620 85.451  1.00 49.57  ? 957  VAL A C     1 
ATOM   6752 O  O     . VAL A 1 957  ? 107.512 110.401 86.635  1.00 49.57  ? 957  VAL A O     1 
ATOM   6753 C  CB    . VAL A 1 957  ? 106.149 110.563 83.537  1.00 49.57  ? 957  VAL A CB    1 
ATOM   6754 C  CG1   . VAL A 1 957  ? 105.782 109.229 84.163  1.00 49.57  ? 957  VAL A CG1   1 
ATOM   6755 C  CG2   . VAL A 1 957  ? 104.911 111.269 83.025  1.00 49.57  ? 957  VAL A CG2   1 
ATOM   6756 N  N     . ILE A 1 958  ? 108.938 110.172 84.905  1.00 49.46  ? 958  ILE A N     1 
ATOM   6757 C  CA    . ILE A 1 958  ? 109.855 109.333 85.675  1.00 49.46  ? 958  ILE A CA    1 
ATOM   6758 C  C     . ILE A 1 958  ? 110.407 110.101 86.870  1.00 49.46  ? 958  ILE A C     1 
ATOM   6759 O  O     . ILE A 1 958  ? 110.451 109.586 87.995  1.00 49.46  ? 958  ILE A O     1 
ATOM   6760 C  CB    . ILE A 1 958  ? 110.985 108.803 84.774  1.00 49.46  ? 958  ILE A CB    1 
ATOM   6761 C  CG1   . ILE A 1 958  ? 110.445 107.742 83.816  1.00 49.46  ? 958  ILE A CG1   1 
ATOM   6762 C  CG2   . ILE A 1 958  ? 112.117 108.235 85.616  1.00 49.46  ? 958  ILE A CG2   1 
ATOM   6763 C  CD1   . ILE A 1 958  ? 109.964 106.495 84.512  1.00 49.46  ? 958  ILE A CD1   1 
ATOM   6764 N  N     . THR A 1 959  ? 110.837 111.345 86.647  1.00 51.82  ? 959  THR A N     1 
ATOM   6765 C  CA    . THR A 1 959  ? 111.419 112.120 87.736  1.00 51.82  ? 959  THR A CA    1 
ATOM   6766 C  C     . THR A 1 959  ? 110.392 112.421 88.821  1.00 51.82  ? 959  THR A C     1 
ATOM   6767 O  O     . THR A 1 959  ? 110.705 112.347 90.014  1.00 51.82  ? 959  THR A O     1 
ATOM   6768 C  CB    . THR A 1 959  ? 112.024 113.415 87.200  1.00 51.82  ? 959  THR A CB    1 
ATOM   6769 O  OG1   . THR A 1 959  ? 112.925 113.113 86.128  1.00 51.82  ? 959  THR A OG1   1 
ATOM   6770 C  CG2   . THR A 1 959  ? 112.785 114.135 88.304  1.00 51.82  ? 959  THR A CG2   1 
ATOM   6771 N  N     . ALA A 1 960  ? 109.163 112.768 88.431  1.00 51.95  ? 960  ALA A N     1 
ATOM   6772 C  CA    . ALA A 1 960  ? 108.124 113.033 89.419  1.00 51.95  ? 960  ALA A CA    1 
ATOM   6773 C  C     . ALA A 1 960  ? 107.811 111.786 90.228  1.00 51.95  ? 960  ALA A C     1 
ATOM   6774 O  O     . ALA A 1 960  ? 107.628 111.859 91.449  1.00 51.95  ? 960  ALA A O     1 
ATOM   6775 C  CB    . ALA A 1 960  ? 106.866 113.562 88.731  1.00 51.95  ? 960  ALA A CB    1 
ATOM   6776 N  N     . ASN A 1 961  ? 107.751 110.626 89.569  1.00 55.21  ? 961  ASN A N     1 
ATOM   6777 C  CA    . ASN A 1 961  ? 107.516 109.388 90.302  1.00 55.21  ? 961  ASN A CA    1 
ATOM   6778 C  C     . ASN A 1 961  ? 108.657 109.110 91.275  1.00 55.21  ? 961  ASN A C     1 
ATOM   6779 O  O     . ASN A 1 961  ? 108.426 108.654 92.401  1.00 55.21  ? 961  ASN A O     1 
ATOM   6780 C  CB    . ASN A 1 961  ? 107.334 108.229 89.321  1.00 55.21  ? 961  ASN A CB    1 
ATOM   6781 C  CG    . ASN A 1 961  ? 106.876 106.947 89.997  1.00 55.21  ? 961  ASN A CG    1 
ATOM   6782 O  OD1   . ASN A 1 961  ? 106.710 106.892 91.215  1.00 55.21  ? 961  ASN A OD1   1 
ATOM   6783 N  ND2   . ASN A 1 961  ? 106.669 105.906 89.201  1.00 55.21  ? 961  ASN A ND2   1 
ATOM   6784 N  N     . SER A 1 962  ? 109.897 109.383 90.861  1.00 55.30  ? 962  SER A N     1 
ATOM   6785 C  CA    . SER A 1 962  ? 111.037 109.158 91.747  1.00 55.30  ? 962  SER A CA    1 
ATOM   6786 C  C     . SER A 1 962  ? 110.999 110.083 92.957  1.00 55.30  ? 962  SER A C     1 
ATOM   6787 O  O     . SER A 1 962  ? 111.285 109.656 94.081  1.00 55.30  ? 962  SER A O     1 
ATOM   6788 C  CB    . SER A 1 962  ? 112.346 109.336 90.977  1.00 55.30  ? 962  SER A CB    1 
ATOM   6789 O  OG    . SER A 1 962  ? 112.720 110.701 90.914  1.00 55.30  ? 962  SER A OG    1 
ATOM   6790 N  N     . VAL A 1 963  ? 110.646 111.354 92.748  1.00 58.22  ? 963  VAL A N     1 
ATOM   6791 C  CA    . VAL A 1 963  ? 110.661 112.326 93.840  1.00 58.22  ? 963  VAL A CA    1 
ATOM   6792 C  C     . VAL A 1 963  ? 109.407 112.266 94.699  1.00 58.22  ? 963  VAL A C     1 
ATOM   6793 O  O     . VAL A 1 963  ? 109.409 112.794 95.818  1.00 58.22  ? 963  VAL A O     1 
ATOM   6794 C  CB    . VAL A 1 963  ? 110.883 113.739 93.261  1.00 58.22  ? 963  VAL A CB    1 
ATOM   6795 C  CG1   . VAL A 1 963  ? 111.054 114.775 94.364  1.00 58.22  ? 963  VAL A CG1   1 
ATOM   6796 C  CG2   . VAL A 1 963  ? 112.109 113.748 92.370  1.00 58.22  ? 963  VAL A CG2   1 
ATOM   6797 N  N     . ALA A 1 964  ? 108.350 111.588 94.246  1.00 61.73  ? 964  ALA A N     1 
ATOM   6798 C  CA    . ALA A 1 964  ? 107.106 111.528 95.013  1.00 61.73  ? 964  ALA A CA    1 
ATOM   6799 C  C     . ALA A 1 964  ? 107.250 110.593 96.218  1.00 61.73  ? 964  ALA A C     1 
ATOM   6800 O  O     . ALA A 1 964  ? 106.524 109.614 96.388  1.00 61.73  ? 964  ALA A O     1 
ATOM   6801 C  CB    . ALA A 1 964  ? 105.954 111.101 94.114  1.00 61.73  ? 964  ALA A CB    1 
ATOM   6802 N  N     . GLU A 1 965  ? 108.224 110.924 97.065  1.00 63.26  ? 965  GLU A N     1 
ATOM   6803 C  CA    . GLU A 1 965  ? 108.397 110.276 98.362  1.00 63.26  ? 965  GLU A CA    1 
ATOM   6804 C  C     . GLU A 1 965  ? 108.668 111.247 99.499  1.00 63.26  ? 965  GLU A C     1 
ATOM   6805 O  O     . GLU A 1 965  ? 108.437 110.881 100.657 1.00 63.26  ? 965  GLU A O     1 
ATOM   6806 C  CB    . GLU A 1 965  ? 109.536 109.251 98.304  1.00 63.26  ? 965  GLU A CB    1 
ATOM   6807 C  CG    . GLU A 1 965  ? 110.846 109.807 97.778  1.00 63.26  ? 965  GLU A CG    1 
ATOM   6808 C  CD    . GLU A 1 965  ? 111.764 110.279 98.886  1.00 63.26  ? 965  GLU A CD    1 
ATOM   6809 O  OE1   . GLU A 1 965  ? 112.680 111.079 98.602  1.00 63.26  ? 965  GLU A OE1   1 
ATOM   6810 O  OE2   . GLU A 1 965  ? 111.569 109.850 100.042 1.00 63.26  ? 965  GLU A OE2   1 
ATOM   6811 N  N     . THR A 1 966  ? 109.149 112.462 99.224  1.00 69.14  ? 966  THR A N     1 
ATOM   6812 C  CA    . THR A 1 966  ? 109.407 113.427 100.289 1.00 69.14  ? 966  THR A CA    1 
ATOM   6813 C  C     . THR A 1 966  ? 108.118 113.836 100.988 1.00 69.14  ? 966  THR A C     1 
ATOM   6814 O  O     . THR A 1 966  ? 108.090 113.997 102.214 1.00 69.14  ? 966  THR A O     1 
ATOM   6815 C  CB    . THR A 1 966  ? 110.119 114.656 99.720  1.00 69.14  ? 966  THR A CB    1 
ATOM   6816 O  OG1   . THR A 1 966  ? 111.347 114.255 99.103  1.00 69.14  ? 966  THR A OG1   1 
ATOM   6817 C  CG2   . THR A 1 966  ? 110.420 115.661 100.821 1.00 69.14  ? 966  THR A CG2   1 
ATOM   6818 N  N     . VAL A 1 967  ? 107.039 114.011 100.223 1.00 68.29  ? 967  VAL A N     1 
ATOM   6819 C  CA    . VAL A 1 967  ? 105.757 114.378 100.817 1.00 68.29  ? 967  VAL A CA    1 
ATOM   6820 C  C     . VAL A 1 967  ? 105.283 113.285 101.766 1.00 68.29  ? 967  VAL A C     1 
ATOM   6821 O  O     . VAL A 1 967  ? 104.787 113.567 102.864 1.00 68.29  ? 967  VAL A O     1 
ATOM   6822 C  CB    . VAL A 1 967  ? 104.721 114.662 99.713  1.00 68.29  ? 967  VAL A CB    1 
ATOM   6823 C  CG1   . VAL A 1 967  ? 103.489 115.332 100.297 1.00 68.29  ? 967  VAL A CG1   1 
ATOM   6824 C  CG2   . VAL A 1 967  ? 105.336 115.520 98.616  1.00 68.29  ? 967  VAL A CG2   1 
ATOM   6825 N  N     . SER A 1 968  ? 105.428 112.022 101.358 1.00 68.51  ? 968  SER A N     1 
ATOM   6826 C  CA    . SER A 1 968  ? 105.051 110.913 102.227 1.00 68.51  ? 968  SER A CA    1 
ATOM   6827 C  C     . SER A 1 968  ? 105.956 110.833 103.451 1.00 68.51  ? 968  SER A C     1 
ATOM   6828 O  O     . SER A 1 968  ? 105.499 110.486 104.546 1.00 68.51  ? 968  SER A O     1 
ATOM   6829 C  CB    . SER A 1 968  ? 105.090 109.601 101.445 1.00 68.51  ? 968  SER A CB    1 
ATOM   6830 O  OG    . SER A 1 968  ? 106.400 109.326 100.982 1.00 68.51  ? 968  SER A OG    1 
ATOM   6831 N  N     . LEU A 1 969  ? 107.242 111.143 103.284 1.00 71.22  ? 969  LEU A N     1 
ATOM   6832 C  CA    . LEU A 1 969  ? 108.194 111.097 104.386 1.00 71.22  ? 969  LEU A CA    1 
ATOM   6833 C  C     . LEU A 1 969  ? 108.153 112.343 105.262 1.00 71.22  ? 969  LEU A C     1 
ATOM   6834 O  O     . LEU A 1 969  ? 108.787 112.354 106.322 1.00 71.22  ? 969  LEU A O     1 
ATOM   6835 C  CB    . LEU A 1 969  ? 109.612 110.902 103.842 1.00 71.22  ? 969  LEU A CB    1 
ATOM   6836 C  CG    . LEU A 1 969  ? 110.601 110.133 104.719 1.00 71.22  ? 969  LEU A CG    1 
ATOM   6837 C  CD1   . LEU A 1 969  ? 110.208 108.669 104.815 1.00 71.22  ? 969  LEU A CD1   1 
ATOM   6838 C  CD2   . LEU A 1 969  ? 112.012 110.273 104.175 1.00 71.22  ? 969  LEU A CD2   1 
ATOM   6839 N  N     . ALA A 1 970  ? 107.431 113.382 104.845 1.00 72.93  ? 970  ALA A N     1 
ATOM   6840 C  CA    . ALA A 1 970  ? 107.395 114.629 105.607 1.00 72.93  ? 970  ALA A CA    1 
ATOM   6841 C  C     . ALA A 1 970  ? 106.831 114.477 107.017 1.00 72.93  ? 970  ALA A C     1 
ATOM   6842 O  O     . ALA A 1 970  ? 107.438 115.022 107.956 1.00 72.93  ? 970  ALA A O     1 
ATOM   6843 C  CB    . ALA A 1 970  ? 106.620 115.688 104.814 1.00 72.93  ? 970  ALA A CB    1 
ATOM   6844 N  N     . PRO A 1 971  ? 105.701 113.790 107.249 1.00 72.08  ? 971  PRO A N     1 
ATOM   6845 C  CA    . PRO A 1 971  ? 105.113 113.816 108.604 1.00 72.08  ? 971  PRO A CA    1 
ATOM   6846 C  C     . PRO A 1 971  ? 106.020 113.266 109.693 1.00 72.08  ? 971  PRO A C     1 
ATOM   6847 O  O     . PRO A 1 971  ? 106.280 113.959 110.686 1.00 72.08  ? 971  PRO A O     1 
ATOM   6848 C  CB    . PRO A 1 971  ? 103.840 112.972 108.442 1.00 72.08  ? 971  PRO A CB    1 
ATOM   6849 C  CG    . PRO A 1 971  ? 103.508 113.065 107.002 1.00 72.08  ? 971  PRO A CG    1 
ATOM   6850 C  CD    . PRO A 1 971  ? 104.828 113.068 106.305 1.00 72.08  ? 971  PRO A CD    1 
ATOM   6851 N  N     . GLU A 1 972  ? 106.510 112.033 109.542 1.00 67.34  ? 972  GLU A N     1 
ATOM   6852 C  CA    . GLU A 1 972  ? 107.313 111.429 110.600 1.00 67.34  ? 972  GLU A CA    1 
ATOM   6853 C  C     . GLU A 1 972  ? 108.625 112.172 110.816 1.00 67.34  ? 972  GLU A C     1 
ATOM   6854 O  O     . GLU A 1 972  ? 109.196 112.111 111.911 1.00 67.34  ? 972  GLU A O     1 
ATOM   6855 C  CB    . GLU A 1 972  ? 107.573 109.956 110.287 1.00 67.34  ? 972  GLU A CB    1 
ATOM   6856 C  CG    . GLU A 1 972  ? 108.262 109.707 108.958 1.00 67.34  ? 972  GLU A CG    1 
ATOM   6857 C  CD    . GLU A 1 972  ? 107.280 109.586 107.809 1.00 67.34  ? 972  GLU A CD    1 
ATOM   6858 O  OE1   . GLU A 1 972  ? 106.138 110.075 107.943 1.00 67.34  ? 972  GLU A OE1   1 
ATOM   6859 O  OE2   . GLU A 1 972  ? 107.646 108.992 106.774 1.00 67.34  ? 972  GLU A OE2   1 
ATOM   6860 N  N     . ILE A 1 973  ? 109.127 112.864 109.793 1.00 68.77  ? 973  ILE A N     1 
ATOM   6861 C  CA    . ILE A 1 973  ? 110.301 113.709 109.986 1.00 68.77  ? 973  ILE A CA    1 
ATOM   6862 C  C     . ILE A 1 973  ? 109.924 114.993 110.714 1.00 68.77  ? 973  ILE A C     1 
ATOM   6863 O  O     . ILE A 1 973  ? 110.634 115.439 111.623 1.00 68.77  ? 973  ILE A O     1 
ATOM   6864 C  CB    . ILE A 1 973  ? 110.983 114.001 108.637 1.00 68.77  ? 973  ILE A CB    1 
ATOM   6865 C  CG1   . ILE A 1 973  ? 111.535 112.712 108.026 1.00 68.77  ? 973  ILE A CG1   1 
ATOM   6866 C  CG2   . ILE A 1 973  ? 112.091 115.029 108.809 1.00 68.77  ? 973  ILE A CG2   1 
ATOM   6867 C  CD1   . ILE A 1 973  ? 112.234 112.920 106.700 1.00 68.77  ? 973  ILE A CD1   1 
ATOM   6868 N  N     . ILE A 1 974  ? 108.798 115.603 110.334 1.00 68.27  ? 974  ILE A N     1 
ATOM   6869 C  CA    . ILE A 1 974  ? 108.454 116.918 110.861 1.00 68.27  ? 974  ILE A CA    1 
ATOM   6870 C  C     . ILE A 1 974  ? 107.947 116.860 112.296 1.00 68.27  ? 974  ILE A C     1 
ATOM   6871 O  O     . ILE A 1 974  ? 107.881 117.899 112.964 1.00 68.27  ? 974  ILE A O     1 
ATOM   6872 C  CB    . ILE A 1 974  ? 107.424 117.609 109.949 1.00 68.27  ? 974  ILE A CB    1 
ATOM   6873 C  CG1   . ILE A 1 974  ? 107.590 119.126 110.034 1.00 68.27  ? 974  ILE A CG1   1 
ATOM   6874 C  CG2   . ILE A 1 974  ? 106.009 117.199 110.326 1.00 68.27  ? 974  ILE A CG2   1 
ATOM   6875 C  CD1   . ILE A 1 974  ? 108.958 119.607 109.605 1.00 68.27  ? 974  ILE A CD1   1 
ATOM   6876 N  N     . ARG A 1 975  ? 107.586 115.678 112.799 1.00 60.60  ? 975  ARG A N     1 
ATOM   6877 C  CA    . ARG A 1 975  ? 107.177 115.581 114.194 1.00 60.60  ? 975  ARG A CA    1 
ATOM   6878 C  C     . ARG A 1 975  ? 108.330 115.832 115.156 1.00 60.60  ? 975  ARG A C     1 
ATOM   6879 O  O     . ARG A 1 975  ? 108.081 116.110 116.334 1.00 60.60  ? 975  ARG A O     1 
ATOM   6880 C  CB    . ARG A 1 975  ? 106.561 114.211 114.479 1.00 60.60  ? 975  ARG A CB    1 
ATOM   6881 C  CG    . ARG A 1 975  ? 107.546 113.060 114.429 1.00 60.60  ? 975  ARG A CG    1 
ATOM   6882 C  CD    . ARG A 1 975  ? 106.825 111.725 114.380 1.00 60.60  ? 975  ARG A CD    1 
ATOM   6883 N  NE    . ARG A 1 975  ? 107.624 110.648 114.954 1.00 60.60  ? 975  ARG A NE    1 
ATOM   6884 C  CZ    . ARG A 1 975  ? 107.113 109.554 115.507 1.00 60.60  ? 975  ARG A CZ    1 
ATOM   6885 N  NH1   . ARG A 1 975  ? 107.915 108.623 116.004 1.00 60.60  ? 975  ARG A NH1   1 
ATOM   6886 N  NH2   . ARG A 1 975  ? 105.798 109.389 115.563 1.00 60.60  ? 975  ARG A NH2   1 
ATOM   6887 N  N     . GLY A 1 976  ? 109.572 115.740 114.689 1.00 58.61  ? 976  GLY A N     1 
ATOM   6888 C  CA    . GLY A 1 976  ? 110.735 116.044 115.489 1.00 58.61  ? 976  GLY A CA    1 
ATOM   6889 C  C     . GLY A 1 976  ? 111.149 117.495 115.492 1.00 58.61  ? 976  GLY A C     1 
ATOM   6890 O  O     . GLY A 1 976  ? 112.162 117.839 116.110 1.00 58.61  ? 976  GLY A O     1 
ATOM   6891 N  N     . GLY A 1 977  ? 110.397 118.364 114.814 1.00 55.33  ? 977  GLY A N     1 
ATOM   6892 C  CA    . GLY A 1 977  ? 110.735 119.778 114.817 1.00 55.33  ? 977  GLY A CA    1 
ATOM   6893 C  C     . GLY A 1 977  ? 110.618 120.401 116.194 1.00 55.33  ? 977  GLY A C     1 
ATOM   6894 O  O     . GLY A 1 977  ? 111.480 121.180 116.609 1.00 55.33  ? 977  GLY A O     1 
ATOM   6895 N  N     . GLU A 1 978  ? 109.550 120.069 116.921 1.00 55.99  ? 978  GLU A N     1 
ATOM   6896 C  CA    . GLU A 1 978  ? 109.412 120.564 118.285 1.00 55.99  ? 978  GLU A CA    1 
ATOM   6897 C  C     . GLU A 1 978  ? 110.370 119.856 119.234 1.00 55.99  ? 978  GLU A C     1 
ATOM   6898 O  O     . GLU A 1 978  ? 110.711 120.402 120.289 1.00 55.99  ? 978  GLU A O     1 
ATOM   6899 C  CB    . GLU A 1 978  ? 107.969 120.405 118.760 1.00 55.99  ? 978  GLU A CB    1 
ATOM   6900 C  CG    . GLU A 1 978  ? 106.956 121.127 117.885 1.00 55.99  ? 978  GLU A CG    1 
ATOM   6901 C  CD    . GLU A 1 978  ? 105.808 121.715 118.680 1.00 55.99  ? 978  GLU A CD    1 
ATOM   6902 O  OE1   . GLU A 1 978  ? 105.906 121.760 119.924 1.00 55.99  ? 978  GLU A OE1   1 
ATOM   6903 O  OE2   . GLU A 1 978  ? 104.806 122.132 118.062 1.00 55.99  ? 978  GLU A OE2   1 
ATOM   6904 N  N     . ALA A 1 979  ? 110.806 118.644 118.882 1.00 49.00  ? 979  ALA A N     1 
ATOM   6905 C  CA    . ALA A 1 979  ? 111.807 117.956 119.691 1.00 49.00  ? 979  ALA A CA    1 
ATOM   6906 C  C     . ALA A 1 979  ? 113.126 118.717 119.697 1.00 49.00  ? 979  ALA A C     1 
ATOM   6907 O  O     . ALA A 1 979  ? 113.773 118.844 120.744 1.00 49.00  ? 979  ALA A O     1 
ATOM   6908 C  CB    . ALA A 1 979  ? 112.010 116.532 119.175 1.00 49.00  ? 979  ALA A CB    1 
ATOM   6909 N  N     . VAL A 1 980  ? 113.541 119.230 118.537 1.00 49.38  ? 980  VAL A N     1 
ATOM   6910 C  CA    . VAL A 1 980  ? 114.779 120.001 118.459 1.00 49.38  ? 980  VAL A CA    1 
ATOM   6911 C  C     . VAL A 1 980  ? 114.670 121.269 119.295 1.00 49.38  ? 980  VAL A C     1 
ATOM   6912 O  O     . VAL A 1 980  ? 115.613 121.650 119.999 1.00 49.38  ? 980  VAL A O     1 
ATOM   6913 C  CB    . VAL A 1 980  ? 115.121 120.315 116.991 1.00 49.38  ? 980  VAL A CB    1 
ATOM   6914 C  CG1   . VAL A 1 980  ? 116.177 121.404 116.909 1.00 49.38  ? 980  VAL A CG1   1 
ATOM   6915 C  CG2   . VAL A 1 980  ? 115.589 119.058 116.279 1.00 49.38  ? 980  VAL A CG2   1 
ATOM   6916 N  N     . GLY A 1 981  ? 113.518 121.940 119.234 1.00 47.29  ? 981  GLY A N     1 
ATOM   6917 C  CA    . GLY A 1 981  ? 113.329 123.136 120.038 1.00 47.29  ? 981  GLY A CA    1 
ATOM   6918 C  C     . GLY A 1 981  ? 113.432 122.861 121.525 1.00 47.29  ? 981  GLY A C     1 
ATOM   6919 O  O     . GLY A 1 981  ? 113.923 123.695 122.289 1.00 47.29  ? 981  GLY A O     1 
ATOM   6920 N  N     . SER A 1 982  ? 112.968 121.687 121.957 1.00 43.77  ? 982  SER A N     1 
ATOM   6921 C  CA    . SER A 1 982  ? 113.111 121.309 123.359 1.00 43.77  ? 982  SER A CA    1 
ATOM   6922 C  C     . SER A 1 982  ? 114.573 121.080 123.722 1.00 43.77  ? 982  SER A C     1 
ATOM   6923 O  O     . SER A 1 982  ? 115.000 121.398 124.838 1.00 43.77  ? 982  SER A O     1 
ATOM   6924 C  CB    . SER A 1 982  ? 112.283 120.059 123.651 1.00 43.77  ? 982  SER A CB    1 
ATOM   6925 O  OG    . SER A 1 982  ? 112.719 118.967 122.861 1.00 43.77  ? 982  SER A OG    1 
ATOM   6926 N  N     . VAL A 1 983  ? 115.353 120.519 122.795 1.00 39.13  ? 983  VAL A N     1 
ATOM   6927 C  CA    . VAL A 1 983  ? 116.765 120.254 123.065 1.00 39.13  ? 983  VAL A CA    1 
ATOM   6928 C  C     . VAL A 1 983  ? 117.520 121.558 123.285 1.00 39.13  ? 983  VAL A C     1 
ATOM   6929 O  O     . VAL A 1 983  ? 118.307 121.691 124.229 1.00 39.13  ? 983  VAL A O     1 
ATOM   6930 C  CB    . VAL A 1 983  ? 117.383 119.431 121.921 1.00 39.13  ? 983  VAL A CB    1 
ATOM   6931 C  CG1   . VAL A 1 983  ? 118.898 119.433 122.022 1.00 39.13  ? 983  VAL A CG1   1 
ATOM   6932 C  CG2   . VAL A 1 983  ? 116.847 118.011 121.943 1.00 39.13  ? 983  VAL A CG2   1 
ATOM   6933 N  N     . PHE A 1 984  ? 117.287 122.544 122.417 1.00 43.89  ? 984  PHE A N     1 
ATOM   6934 C  CA    . PHE A 1 984  ? 118.003 123.809 122.532 1.00 43.89  ? 984  PHE A CA    1 
ATOM   6935 C  C     . PHE A 1 984  ? 117.511 124.631 123.713 1.00 43.89  ? 984  PHE A C     1 
ATOM   6936 O  O     . PHE A 1 984  ? 118.273 125.430 124.267 1.00 43.89  ? 984  PHE A O     1 
ATOM   6937 C  CB    . PHE A 1 984  ? 117.873 124.601 121.233 1.00 43.89  ? 984  PHE A CB    1 
ATOM   6938 C  CG    . PHE A 1 984  ? 118.828 124.163 120.164 1.00 43.89  ? 984  PHE A CG    1 
ATOM   6939 C  CD1   . PHE A 1 984  ? 120.162 123.945 120.458 1.00 43.89  ? 984  PHE A CD1   1 
ATOM   6940 C  CD2   . PHE A 1 984  ? 118.388 123.945 118.872 1.00 43.89  ? 984  PHE A CD2   1 
ATOM   6941 C  CE1   . PHE A 1 984  ? 121.042 123.536 119.479 1.00 43.89  ? 984  PHE A CE1   1 
ATOM   6942 C  CE2   . PHE A 1 984  ? 119.263 123.534 117.890 1.00 43.89  ? 984  PHE A CE2   1 
ATOM   6943 C  CZ    . PHE A 1 984  ? 120.592 123.329 118.194 1.00 43.89  ? 984  PHE A CZ    1 
ATOM   6944 N  N     . SER A 1 985  ? 116.248 124.458 124.108 1.00 38.69  ? 985  SER A N     1 
ATOM   6945 C  CA    . SER A 1 985  ? 115.737 125.169 125.276 1.00 38.69  ? 985  SER A CA    1 
ATOM   6946 C  C     . SER A 1 985  ? 116.474 124.749 126.541 1.00 38.69  ? 985  SER A C     1 
ATOM   6947 O  O     . SER A 1 985  ? 116.779 125.589 127.396 1.00 38.69  ? 985  SER A O     1 
ATOM   6948 C  CB    . SER A 1 985  ? 114.235 124.928 125.421 1.00 38.69  ? 985  SER A CB    1 
ATOM   6949 O  OG    . SER A 1 985  ? 113.974 123.635 125.935 1.00 38.69  ? 985  SER A OG    1 
ATOM   6950 N  N     . VAL A 1 986  ? 116.759 123.453 126.683 1.00 37.21  ? 986  VAL A N     1 
ATOM   6951 C  CA    . VAL A 1 986  ? 117.510 122.975 127.841 1.00 37.21  ? 986  VAL A CA    1 
ATOM   6952 C  C     . VAL A 1 986  ? 118.929 123.529 127.823 1.00 37.21  ? 986  VAL A C     1 
ATOM   6953 O  O     . VAL A 1 986  ? 119.455 123.964 128.854 1.00 37.21  ? 986  VAL A O     1 
ATOM   6954 C  CB    . VAL A 1 986  ? 117.503 121.436 127.883 1.00 37.21  ? 986  VAL A CB    1 
ATOM   6955 C  CG1   . VAL A 1 986  ? 118.387 120.934 129.007 1.00 37.21  ? 986  VAL A CG1   1 
ATOM   6956 C  CG2   . VAL A 1 986  ? 116.085 120.919 128.048 1.00 37.21  ? 986  VAL A CG2   1 
ATOM   6957 N  N     . LEU A 1 987  ? 119.570 123.521 126.652 1.00 35.61  ? 987  LEU A N     1 
ATOM   6958 C  CA    . LEU A 1 987  ? 120.941 124.014 126.550 1.00 35.61  ? 987  LEU A CA    1 
ATOM   6959 C  C     . LEU A 1 987  ? 121.018 125.523 126.744 1.00 35.61  ? 987  LEU A C     1 
ATOM   6960 O  O     . LEU A 1 987  ? 122.015 126.028 127.272 1.00 35.61  ? 987  LEU A O     1 
ATOM   6961 C  CB    . LEU A 1 987  ? 121.534 123.627 125.196 1.00 35.61  ? 987  LEU A CB    1 
ATOM   6962 C  CG    . LEU A 1 987  ? 121.853 122.147 124.982 1.00 35.61  ? 987  LEU A CG    1 
ATOM   6963 C  CD1   . LEU A 1 987  ? 122.075 121.858 123.510 1.00 35.61  ? 987  LEU A CD1   1 
ATOM   6964 C  CD2   . LEU A 1 987  ? 123.067 121.744 125.795 1.00 35.61  ? 987  LEU A CD2   1 
ATOM   6965 N  N     . ASP A 1 988  ? 119.987 126.255 126.321 1.00 39.61  ? 988  ASP A N     1 
ATOM   6966 C  CA    . ASP A 1 988  ? 120.010 127.712 126.392 1.00 39.61  ? 988  ASP A CA    1 
ATOM   6967 C  C     . ASP A 1 988  ? 119.952 128.196 127.838 1.00 39.61  ? 988  ASP A C     1 
ATOM   6968 O  O     . ASP A 1 988  ? 120.649 129.150 128.202 1.00 39.61  ? 988  ASP A O     1 
ATOM   6969 C  CB    . ASP A 1 988  ? 118.842 128.278 125.575 1.00 39.61  ? 988  ASP A CB    1 
ATOM   6970 C  CG    . ASP A 1 988  ? 118.810 129.803 125.529 1.00 39.61  ? 988  ASP A CG    1 
ATOM   6971 O  OD1   . ASP A 1 988  ? 117.942 130.342 124.810 1.00 39.61  ? 988  ASP A OD1   1 
ATOM   6972 O  OD2   . ASP A 1 988  ? 119.654 130.471 126.159 1.00 39.61  ? 988  ASP A OD2   1 
ATOM   6973 N  N     . ARG A 1 989  ? 119.150 127.537 128.673 1.00 34.31  ? 989  ARG A N     1 
ATOM   6974 C  CA    . ARG A 1 989  ? 118.913 128.007 130.034 1.00 34.31  ? 989  ARG A CA    1 
ATOM   6975 C  C     . ARG A 1 989  ? 120.219 128.140 130.805 1.00 34.31  ? 989  ARG A C     1 
ATOM   6976 O  O     . ARG A 1 989  ? 121.064 127.241 130.785 1.00 34.31  ? 989  ARG A O     1 
ATOM   6977 C  CB    . ARG A 1 989  ? 117.970 127.049 130.761 1.00 34.31  ? 989  ARG A CB    1 
ATOM   6978 C  CG    . ARG A 1 989  ? 117.144 127.699 131.857 1.00 34.31  ? 989  ARG A CG    1 
ATOM   6979 C  CD    . ARG A 1 989  ? 117.790 127.515 133.220 1.00 34.31  ? 989  ARG A CD    1 
ATOM   6980 N  NE    . ARG A 1 989  ? 116.839 127.721 134.309 1.00 34.31  ? 989  ARG A NE    1 
ATOM   6981 C  CZ    . ARG A 1 989  ? 117.162 127.690 135.597 1.00 34.31  ? 989  ARG A CZ    1 
ATOM   6982 N  NH1   . ARG A 1 989  ? 116.232 127.889 136.521 1.00 34.31  ? 989  ARG A NH1   1 
ATOM   6983 N  NH2   . ARG A 1 989  ? 118.415 127.462 135.964 1.00 34.31  ? 989  ARG A NH2   1 
ATOM   6984 N  N     . GLN A 1 990  ? 120.379 129.270 131.486 1.00 37.60  ? 990  GLN A N     1 
ATOM   6985 C  CA    . GLN A 1 990  ? 121.563 129.547 132.286 1.00 37.60  ? 990  GLN A CA    1 
ATOM   6986 C  C     . GLN A 1 990  ? 121.223 129.388 133.761 1.00 37.60  ? 990  GLN A C     1 
ATOM   6987 O  O     . GLN A 1 990  ? 120.282 130.014 134.258 1.00 37.60  ? 990  GLN A O     1 
ATOM   6988 C  CB    . GLN A 1 990  ? 122.090 130.956 132.012 1.00 37.60  ? 990  GLN A CB    1 
ATOM   6989 C  CG    . GLN A 1 990  ? 122.865 131.082 130.713 1.00 37.60  ? 990  GLN A CG    1 
ATOM   6990 C  CD    . GLN A 1 990  ? 123.144 132.524 130.342 1.00 37.60  ? 990  GLN A CD    1 
ATOM   6991 O  OE1   . GLN A 1 990  ? 122.525 133.445 130.875 1.00 37.60  ? 990  GLN A OE1   1 
ATOM   6992 N  NE2   . GLN A 1 990  ? 124.081 132.728 129.424 1.00 37.60  ? 990  GLN A NE2   1 
ATOM   6993 N  N     . THR A 1 991  ? 121.991 128.552 134.454 1.00 34.45  ? 991  THR A N     1 
ATOM   6994 C  CA    . THR A 1 991  ? 121.719 128.273 135.854 1.00 34.45  ? 991  THR A CA    1 
ATOM   6995 C  C     . THR A 1 991  ? 121.986 129.500 136.718 1.00 34.45  ? 991  THR A C     1 
ATOM   6996 O  O     . THR A 1 991  ? 122.898 130.290 136.459 1.00 34.45  ? 991  THR A O     1 
ATOM   6997 C  CB    . THR A 1 991  ? 122.568 127.097 136.339 1.00 34.45  ? 991  THR A CB    1 
ATOM   6998 O  OG1   . THR A 1 991  ? 122.260 126.815 137.709 1.00 34.45  ? 991  THR A OG1   1 
ATOM   6999 C  CG2   . THR A 1 991  ? 124.051 127.408 136.208 1.00 34.45  ? 991  THR A CG2   1 
ATOM   7000 N  N     . ARG A 1 992  ? 121.156 129.666 137.748 1.00 36.91  ? 992  ARG A N     1 
ATOM   7001 C  CA    . ARG A 1 992  ? 121.371 130.741 138.708 1.00 36.91  ? 992  ARG A CA    1 
ATOM   7002 C  C     . ARG A 1 992  ? 122.518 130.428 139.657 1.00 36.91  ? 992  ARG A C     1 
ATOM   7003 O  O     . ARG A 1 992  ? 123.153 131.349 140.181 1.00 36.91  ? 992  ARG A O     1 
ATOM   7004 C  CB    . ARG A 1 992  ? 120.091 131.006 139.500 1.00 36.91  ? 992  ARG A CB    1 
ATOM   7005 C  CG    . ARG A 1 992  ? 118.964 131.589 138.670 1.00 36.91  ? 992  ARG A CG    1 
ATOM   7006 C  CD    . ARG A 1 992  ? 117.666 131.629 139.454 1.00 36.91  ? 992  ARG A CD    1 
ATOM   7007 N  NE    . ARG A 1 992  ? 117.039 132.945 139.397 1.00 36.91  ? 992  ARG A NE    1 
ATOM   7008 C  CZ    . ARG A 1 992  ? 116.188 133.324 138.449 1.00 36.91  ? 992  ARG A CZ    1 
ATOM   7009 N  NH1   . ARG A 1 992  ? 115.665 134.542 138.475 1.00 36.91  ? 992  ARG A NH1   1 
ATOM   7010 N  NH2   . ARG A 1 992  ? 115.861 132.487 137.475 1.00 36.91  ? 992  ARG A NH2   1 
ATOM   7011 N  N     . ILE A 1 993  ? 122.792 129.150 139.889 1.00 34.86  ? 993  ILE A N     1 
ATOM   7012 C  CA    . ILE A 1 993  ? 123.874 128.711 140.761 1.00 34.86  ? 993  ILE A CA    1 
ATOM   7013 C  C     . ILE A 1 993  ? 124.946 128.104 139.864 1.00 34.86  ? 993  ILE A C     1 
ATOM   7014 O  O     . ILE A 1 993  ? 124.819 126.962 139.408 1.00 34.86  ? 993  ILE A O     1 
ATOM   7015 C  CB    . ILE A 1 993  ? 123.389 127.711 141.816 1.00 34.86  ? 993  ILE A CB    1 
ATOM   7016 C  CG1   . ILE A 1 993  ? 122.213 128.292 142.598 1.00 34.86  ? 993  ILE A CG1   1 
ATOM   7017 C  CG2   . ILE A 1 993  ? 124.510 127.364 142.769 1.00 34.86  ? 993  ILE A CG2   1 
ATOM   7018 C  CD1   . ILE A 1 993  ? 122.573 129.517 143.397 1.00 34.86  ? 993  ILE A CD1   1 
ATOM   7019 N  N     . ASP A 1 994  ? 126.003 128.864 139.607 1.00 38.19  ? 994  ASP A N     1 
ATOM   7020 C  CA    . ASP A 1 994  ? 127.088 128.384 138.761 1.00 38.19  ? 994  ASP A CA    1 
ATOM   7021 C  C     . ASP A 1 994  ? 127.952 127.413 139.556 1.00 38.19  ? 994  ASP A C     1 
ATOM   7022 O  O     . ASP A 1 994  ? 128.519 127.805 140.582 1.00 38.19  ? 994  ASP A O     1 
ATOM   7023 C  CB    . ASP A 1 994  ? 127.921 129.556 138.259 1.00 38.19  ? 994  ASP A CB    1 
ATOM   7024 C  CG    . ASP A 1 994  ? 128.742 129.209 137.034 1.00 38.19  ? 994  ASP A CG    1 
ATOM   7025 O  OD1   . ASP A 1 994  ? 128.724 128.035 136.613 1.00 38.19  ? 994  ASP A OD1   1 
ATOM   7026 O  OD2   . ASP A 1 994  ? 129.398 130.117 136.483 1.00 38.19  ? 994  ASP A OD2   1 
ATOM   7027 N  N     . PRO A 1 995  ? 128.068 126.149 139.135 1.00 36.83  ? 995  PRO A N     1 
ATOM   7028 C  CA    . PRO A 1 995  ? 128.783 125.166 139.969 1.00 36.83  ? 995  PRO A CA    1 
ATOM   7029 C  C     . PRO A 1 995  ? 130.233 125.519 140.255 1.00 36.83  ? 995  PRO A C     1 
ATOM   7030 O  O     . PRO A 1 995  ? 130.703 125.296 141.377 1.00 36.83  ? 995  PRO A O     1 
ATOM   7031 C  CB    . PRO A 1 995  ? 128.667 123.872 139.150 1.00 36.83  ? 995  PRO A CB    1 
ATOM   7032 C  CG    . PRO A 1 995  ? 127.456 124.065 138.306 1.00 36.83  ? 995  PRO A CG    1 
ATOM   7033 C  CD    . PRO A 1 995  ? 127.427 125.524 137.966 1.00 36.83  ? 995  PRO A CD    1 
ATOM   7034 N  N     . ASP A 1 996  ? 130.964 126.058 139.280 1.00 43.81  ? 996  ASP A N     1 
ATOM   7035 C  CA    . ASP A 1 996  ? 132.381 126.327 139.494 1.00 43.81  ? 996  ASP A CA    1 
ATOM   7036 C  C     . ASP A 1 996  ? 132.765 127.753 139.122 1.00 43.81  ? 996  ASP A C     1 
ATOM   7037 O  O     . ASP A 1 996  ? 133.617 128.360 139.779 1.00 43.81  ? 996  ASP A O     1 
ATOM   7038 C  CB    . ASP A 1 996  ? 133.230 125.333 138.699 1.00 43.81  ? 996  ASP A CB    1 
ATOM   7039 C  CG    . ASP A 1 996  ? 134.524 124.977 139.403 1.00 43.81  ? 996  ASP A CG    1 
ATOM   7040 O  OD1   . ASP A 1 996  ? 134.600 125.154 140.636 1.00 43.81  ? 996  ASP A OD1   1 
ATOM   7041 O  OD2   . ASP A 1 996  ? 135.465 124.518 138.723 1.00 43.81  ? 996  ASP A OD2   1 
ATOM   7042 N  N     . ASP A 1 997  ? 132.168 128.272 138.046 1.00 44.32  ? 997  ASP A N     1 
ATOM   7043 C  CA    . ASP A 1 997  ? 132.430 129.609 137.513 1.00 44.32  ? 997  ASP A CA    1 
ATOM   7044 C  C     . ASP A 1 997  ? 133.837 129.716 136.930 1.00 44.32  ? 997  ASP A C     1 
ATOM   7045 O  O     . ASP A 1 997  ? 134.192 130.744 136.344 1.00 44.32  ? 997  ASP A O     1 
ATOM   7046 C  CB    . ASP A 1 997  ? 132.216 130.678 138.591 1.00 44.32  ? 997  ASP A CB    1 
ATOM   7047 C  CG    . ASP A 1 997  ? 131.656 131.970 138.029 1.00 44.32  ? 997  ASP A CG    1 
ATOM   7048 O  OD1   . ASP A 1 997  ? 131.758 132.182 136.803 1.00 44.32  ? 997  ASP A OD1   1 
ATOM   7049 O  OD2   . ASP A 1 997  ? 131.115 132.774 138.817 1.00 44.32  ? 997  ASP A OD2   1 
ATOM   7050 N  N     . ALA A 1 998  ? 134.645 128.668 137.107 1.00 46.58  ? 998  ALA A N     1 
ATOM   7051 C  CA    . ALA A 1 998  ? 135.940 128.493 136.455 1.00 46.58  ? 998  ALA A CA    1 
ATOM   7052 C  C     . ALA A 1 998  ? 136.986 129.517 136.888 1.00 46.58  ? 998  ALA A C     1 
ATOM   7053 O  O     . ALA A 1 998  ? 138.156 129.404 136.510 1.00 46.58  ? 998  ALA A O     1 
ATOM   7054 C  CB    . ALA A 1 998  ? 135.778 128.530 134.932 1.00 46.58  ? 998  ALA A CB    1 
ATOM   7055 N  N     . ASP A 1 999  ? 136.587 130.520 137.674 1.00 51.12  ? 999  ASP A N     1 
ATOM   7056 C  CA    . ASP A 1 999  ? 137.540 131.509 138.163 1.00 51.12  ? 999  ASP A CA    1 
ATOM   7057 C  C     . ASP A 1 999  ? 137.240 131.974 139.583 1.00 51.12  ? 999  ASP A C     1 
ATOM   7058 O  O     . ASP A 1 999  ? 137.886 132.918 140.055 1.00 51.12  ? 999  ASP A O     1 
ATOM   7059 C  CB    . ASP A 1 999  ? 137.589 132.723 137.225 1.00 51.12  ? 999  ASP A CB    1 
ATOM   7060 C  CG    . ASP A 1 999  ? 136.270 133.467 137.161 1.00 51.12  ? 999  ASP A CG    1 
ATOM   7061 O  OD1   . ASP A 1 999  ? 136.028 134.325 138.036 1.00 51.12  ? 999  ASP A OD1   1 
ATOM   7062 O  OD2   . ASP A 1 999  ? 135.480 133.202 136.233 1.00 51.12  ? 999  ASP A OD2   1 
ATOM   7063 N  N     . ALA A 1 1000 ? 136.287 131.354 140.275 1.00 51.52  ? 1000 ALA A N     1 
ATOM   7064 C  CA    . ALA A 1 1000 ? 135.752 131.898 141.523 1.00 51.52  ? 1000 ALA A CA    1 
ATOM   7065 C  C     . ALA A 1 1000 ? 136.542 131.364 142.712 1.00 51.52  ? 1000 ALA A C     1 
ATOM   7066 O  O     . ALA A 1 1000 ? 136.121 130.429 143.395 1.00 51.52  ? 1000 ALA A O     1 
ATOM   7067 C  CB    . ALA A 1 1000 ? 134.270 131.571 141.645 1.00 51.52  ? 1000 ALA A CB    1 
ATOM   7068 N  N     . ASP A 1 1001 ? 137.702 131.982 142.967 1.00 56.51  ? 1001 ASP A N     1 
ATOM   7069 C  CA    . ASP A 1 1001 ? 138.495 131.807 144.182 1.00 56.51  ? 1001 ASP A CA    1 
ATOM   7070 C  C     . ASP A 1 1001 ? 138.700 130.345 144.565 1.00 56.51  ? 1001 ASP A C     1 
ATOM   7071 O  O     . ASP A 1 1001 ? 138.077 129.863 145.519 1.00 56.51  ? 1001 ASP A O     1 
ATOM   7072 C  CB    . ASP A 1 1001 ? 137.839 132.554 145.345 1.00 56.51  ? 1001 ASP A CB    1 
ATOM   7073 C  CG    . ASP A 1 1001 ? 137.815 134.054 145.132 1.00 56.51  ? 1001 ASP A CG    1 
ATOM   7074 O  OD1   . ASP A 1 1001 ? 138.226 134.506 144.043 1.00 56.51  ? 1001 ASP A OD1   1 
ATOM   7075 O  OD2   . ASP A 1 1001 ? 137.387 134.781 146.052 1.00 56.51  ? 1001 ASP A OD2   1 
ATOM   7076 N  N     . PRO A 1 1002 ? 139.557 129.609 143.858 1.00 57.43  ? 1002 PRO A N     1 
ATOM   7077 C  CA    . PRO A 1 1002 ? 139.789 128.204 144.223 1.00 57.43  ? 1002 PRO A CA    1 
ATOM   7078 C  C     . PRO A 1 1002 ? 140.575 128.072 145.518 1.00 57.43  ? 1002 PRO A C     1 
ATOM   7079 O  O     . PRO A 1 1002 ? 141.791 127.855 145.496 1.00 57.43  ? 1002 PRO A O     1 
ATOM   7080 C  CB    . PRO A 1 1002 ? 140.581 127.650 143.028 1.00 57.43  ? 1002 PRO A CB    1 
ATOM   7081 C  CG    . PRO A 1 1002 ? 140.544 128.726 141.970 1.00 57.43  ? 1002 PRO A CG    1 
ATOM   7082 C  CD    . PRO A 1 1002 ? 140.354 130.014 142.692 1.00 57.43  ? 1002 PRO A CD    1 
ATOM   7083 N  N     . VAL A 1 1003 ? 139.890 128.202 146.651 1.00 59.47  ? 1003 VAL A N     1 
ATOM   7084 C  CA    . VAL A 1 1003 ? 140.511 128.160 147.970 1.00 59.47  ? 1003 VAL A CA    1 
ATOM   7085 C  C     . VAL A 1 1003 ? 140.144 126.842 148.637 1.00 59.47  ? 1003 VAL A C     1 
ATOM   7086 O  O     . VAL A 1 1003 ? 138.963 126.477 148.699 1.00 59.47  ? 1003 VAL A O     1 
ATOM   7087 C  CB    . VAL A 1 1003 ? 140.075 129.355 148.835 1.00 59.47  ? 1003 VAL A CB    1 
ATOM   7088 C  CG1   . VAL A 1 1003 ? 140.709 129.272 150.215 1.00 59.47  ? 1003 VAL A CG1   1 
ATOM   7089 C  CG2   . VAL A 1 1003 ? 140.441 130.664 148.151 1.00 59.47  ? 1003 VAL A CG2   1 
ATOM   7090 N  N     . GLU A 1 1004 ? 141.156 126.131 149.137 1.00 67.65  ? 1004 GLU A N     1 
ATOM   7091 C  CA    . GLU A 1 1004 ? 140.965 124.834 149.768 1.00 67.65  ? 1004 GLU A CA    1 
ATOM   7092 C  C     . GLU A 1 1004 ? 141.219 124.841 151.269 1.00 67.65  ? 1004 GLU A C     1 
ATOM   7093 O  O     . GLU A 1 1004 ? 140.865 123.866 151.941 1.00 67.65  ? 1004 GLU A O     1 
ATOM   7094 C  CB    . GLU A 1 1004 ? 141.880 123.788 149.114 1.00 67.65  ? 1004 GLU A CB    1 
ATOM   7095 C  CG    . GLU A 1 1004 ? 143.357 124.136 149.181 1.00 67.65  ? 1004 GLU A CG    1 
ATOM   7096 C  CD    . GLU A 1 1004 ? 143.822 124.942 147.985 1.00 67.65  ? 1004 GLU A CD    1 
ATOM   7097 O  OE1   . GLU A 1 1004 ? 142.962 125.379 147.191 1.00 67.65  ? 1004 GLU A OE1   1 
ATOM   7098 O  OE2   . GLU A 1 1004 ? 145.046 125.143 147.841 1.00 67.65  ? 1004 GLU A OE2   1 
ATOM   7099 N  N     . THR A 1 1005 ? 141.820 125.900 151.810 1.00 66.17  ? 1005 THR A N     1 
ATOM   7100 C  CA    . THR A 1 1005 ? 142.121 125.982 153.240 1.00 66.17  ? 1005 THR A CA    1 
ATOM   7101 C  C     . THR A 1 1005 ? 140.870 126.454 153.976 1.00 66.17  ? 1005 THR A C     1 
ATOM   7102 O  O     . THR A 1 1005 ? 140.660 127.643 154.229 1.00 66.17  ? 1005 THR A O     1 
ATOM   7103 C  CB    . THR A 1 1005 ? 143.302 126.911 153.490 1.00 66.17  ? 1005 THR A CB    1 
ATOM   7104 O  OG1   . THR A 1 1005 ? 143.025 128.200 152.929 1.00 66.17  ? 1005 THR A OG1   1 
ATOM   7105 C  CG2   . THR A 1 1005 ? 144.565 126.347 152.857 1.00 66.17  ? 1005 THR A CG2   1 
ATOM   7106 N  N     . ILE A 1 1006 ? 140.023 125.492 154.324 1.00 56.40  ? 1006 ILE A N     1 
ATOM   7107 C  CA    . ILE A 1 1006 ? 138.777 125.785 155.022 1.00 56.40  ? 1006 ILE A CA    1 
ATOM   7108 C  C     . ILE A 1 1006 ? 139.048 125.911 156.515 1.00 56.40  ? 1006 ILE A C     1 
ATOM   7109 O  O     . ILE A 1 1006 ? 139.892 125.201 157.077 1.00 56.40  ? 1006 ILE A O     1 
ATOM   7110 C  CB    . ILE A 1 1006 ? 137.723 124.703 154.722 1.00 56.40  ? 1006 ILE A CB    1 
ATOM   7111 C  CG1   . ILE A 1 1006 ? 136.347 125.131 155.237 1.00 56.40  ? 1006 ILE A CG1   1 
ATOM   7112 C  CG2   . ILE A 1 1006 ? 138.137 123.359 155.304 1.00 56.40  ? 1006 ILE A CG2   1 
ATOM   7113 C  CD1   . ILE A 1 1006 ? 135.211 124.287 154.707 1.00 56.40  ? 1006 ILE A CD1   1 
ATOM   7114 N  N     . ARG A 1 1007 ? 138.346 126.841 157.161 1.00 56.83  ? 1007 ARG A N     1 
ATOM   7115 C  CA    . ARG A 1 1007 ? 138.461 127.054 158.600 1.00 56.83  ? 1007 ARG A CA    1 
ATOM   7116 C  C     . ARG A 1 1007 ? 137.389 126.291 159.370 1.00 56.83  ? 1007 ARG A C     1 
ATOM   7117 O  O     . ARG A 1 1007 ? 137.706 125.466 160.232 1.00 56.83  ? 1007 ARG A O     1 
ATOM   7118 C  CB    . ARG A 1 1007 ? 138.383 128.554 158.915 1.00 56.83  ? 1007 ARG A CB    1 
ATOM   7119 C  CG    . ARG A 1 1007 ? 139.685 129.305 158.691 1.00 56.83  ? 1007 ARG A CG    1 
ATOM   7120 C  CD    . ARG A 1 1007 ? 140.763 128.844 159.658 1.00 56.83  ? 1007 ARG A CD    1 
ATOM   7121 N  NE    . ARG A 1 1007 ? 140.309 128.892 161.045 1.00 56.83  ? 1007 ARG A NE    1 
ATOM   7122 C  CZ    . ARG A 1 1007 ? 140.223 127.830 161.839 1.00 56.83  ? 1007 ARG A CZ    1 
ATOM   7123 N  NH1   . ARG A 1 1007 ? 139.800 127.967 163.088 1.00 56.83  ? 1007 ARG A NH1   1 
ATOM   7124 N  NH2   . ARG A 1 1007 ? 140.558 126.631 161.384 1.00 56.83  ? 1007 ARG A NH2   1 
ATOM   7125 N  N     . GLY A 1 1008 ? 136.120 126.549 159.068 1.00 55.99  ? 1008 GLY A N     1 
ATOM   7126 C  CA    . GLY A 1 1008 ? 135.015 125.896 159.737 1.00 55.99  ? 1008 GLY A CA    1 
ATOM   7127 C  C     . GLY A 1 1008 ? 134.175 126.777 160.639 1.00 55.99  ? 1008 GLY A C     1 
ATOM   7128 O  O     . GLY A 1 1008 ? 133.303 126.253 161.342 1.00 55.99  ? 1008 GLY A O     1 
ATOM   7129 N  N     . ASP A 1 1009 ? 134.403 128.090 160.647 1.00 52.23  ? 1009 ASP A N     1 
ATOM   7130 C  CA    . ASP A 1 1009 ? 133.638 129.004 161.497 1.00 52.23  ? 1009 ASP A CA    1 
ATOM   7131 C  C     . ASP A 1 1009 ? 132.480 129.606 160.698 1.00 52.23  ? 1009 ASP A C     1 
ATOM   7132 O  O     . ASP A 1 1009 ? 132.549 130.708 160.152 1.00 52.23  ? 1009 ASP A O     1 
ATOM   7133 C  CB    . ASP A 1 1009 ? 134.551 130.078 162.076 1.00 52.23  ? 1009 ASP A CB    1 
ATOM   7134 C  CG    . ASP A 1 1009 ? 135.422 130.736 161.024 1.00 52.23  ? 1009 ASP A CG    1 
ATOM   7135 O  OD1   . ASP A 1 1009 ? 135.403 130.279 159.862 1.00 52.23  ? 1009 ASP A OD1   1 
ATOM   7136 O  OD2   . ASP A 1 1009 ? 136.127 131.711 161.360 1.00 52.23  ? 1009 ASP A OD2   1 
ATOM   7137 N  N     . ILE A 1 1010 ? 131.387 128.845 160.648 1.00 48.49  ? 1010 ILE A N     1 
ATOM   7138 C  CA    . ILE A 1 1010 ? 130.220 129.256 159.878 1.00 48.49  ? 1010 ILE A CA    1 
ATOM   7139 C  C     . ILE A 1 1010 ? 129.476 130.354 160.627 1.00 48.49  ? 1010 ILE A C     1 
ATOM   7140 O  O     . ILE A 1 1010 ? 129.457 130.381 161.863 1.00 48.49  ? 1010 ILE A O     1 
ATOM   7141 C  CB    . ILE A 1 1010 ? 129.314 128.042 159.607 1.00 48.49  ? 1010 ILE A CB    1 
ATOM   7142 C  CG1   . ILE A 1 1010 ? 130.079 126.975 158.823 1.00 48.49  ? 1010 ILE A CG1   1 
ATOM   7143 C  CG2   . ILE A 1 1010 ? 128.069 128.445 158.840 1.00 48.49  ? 1010 ILE A CG2   1 
ATOM   7144 C  CD1   . ILE A 1 1010 ? 130.469 125.773 159.649 1.00 48.49  ? 1010 ILE A CD1   1 
ATOM   7145 N  N     . GLU A 1 1011 ? 128.871 131.280 159.886 1.00 49.53  ? 1011 GLU A N     1 
ATOM   7146 C  CA    . GLU A 1 1011 ? 128.048 132.312 160.500 1.00 49.53  ? 1011 GLU A CA    1 
ATOM   7147 C  C     . GLU A 1 1011 ? 126.938 132.727 159.546 1.00 49.53  ? 1011 GLU A C     1 
ATOM   7148 O  O     . GLU A 1 1011 ? 127.086 132.658 158.324 1.00 49.53  ? 1011 GLU A O     1 
ATOM   7149 C  CB    . GLU A 1 1011 ? 128.879 133.537 160.905 1.00 49.53  ? 1011 GLU A CB    1 
ATOM   7150 C  CG    . GLU A 1 1011 ? 129.526 134.269 159.745 1.00 49.53  ? 1011 GLU A CG    1 
ATOM   7151 C  CD    . GLU A 1 1011 ? 130.174 135.571 160.172 1.00 49.53  ? 1011 GLU A CD    1 
ATOM   7152 O  OE1   . GLU A 1 1011 ? 129.441 136.557 160.393 1.00 49.53  ? 1011 GLU A OE1   1 
ATOM   7153 O  OE2   . GLU A 1 1011 ? 131.417 135.609 160.285 1.00 49.53  ? 1011 GLU A OE2   1 
ATOM   7154 N  N     . PHE A 1 1012 ? 125.822 133.157 160.127 1.00 43.63  ? 1012 PHE A N     1 
ATOM   7155 C  CA    . PHE A 1 1012 ? 124.685 133.686 159.392 1.00 43.63  ? 1012 PHE A CA    1 
ATOM   7156 C  C     . PHE A 1 1012 ? 124.496 135.147 159.773 1.00 43.63  ? 1012 PHE A C     1 
ATOM   7157 O  O     . PHE A 1 1012 ? 124.810 135.554 160.895 1.00 43.63  ? 1012 PHE A O     1 
ATOM   7158 C  CB    . PHE A 1 1012 ? 123.402 132.904 159.700 1.00 43.63  ? 1012 PHE A CB    1 
ATOM   7159 C  CG    . PHE A 1 1012 ? 123.275 131.613 158.942 1.00 43.63  ? 1012 PHE A CG    1 
ATOM   7160 C  CD1   . PHE A 1 1012 ? 124.193 130.595 159.123 1.00 43.63  ? 1012 PHE A CD1   1 
ATOM   7161 C  CD2   . PHE A 1 1012 ? 122.228 131.413 158.059 1.00 43.63  ? 1012 PHE A CD2   1 
ATOM   7162 C  CE1   . PHE A 1 1012 ? 124.073 129.408 158.432 1.00 43.63  ? 1012 PHE A CE1   1 
ATOM   7163 C  CE2   . PHE A 1 1012 ? 122.104 130.227 157.365 1.00 43.63  ? 1012 PHE A CE2   1 
ATOM   7164 C  CZ    . PHE A 1 1012 ? 123.028 129.224 157.552 1.00 43.63  ? 1012 PHE A CZ    1 
ATOM   7165 N  N     . ARG A 1 1013 ? 123.985 135.940 158.833 1.00 45.86  ? 1013 ARG A N     1 
ATOM   7166 C  CA    . ARG A 1 1013 ? 123.782 137.370 159.068 1.00 45.86  ? 1013 ARG A CA    1 
ATOM   7167 C  C     . ARG A 1 1013 ? 122.513 137.813 158.347 1.00 45.86  ? 1013 ARG A C     1 
ATOM   7168 O  O     . ARG A 1 1013 ? 122.531 138.037 157.134 1.00 45.86  ? 1013 ARG A O     1 
ATOM   7169 C  CB    . ARG A 1 1013 ? 124.989 138.180 158.611 1.00 45.86  ? 1013 ARG A CB    1 
ATOM   7170 C  CG    . ARG A 1 1013 ? 126.115 138.233 159.628 1.00 45.86  ? 1013 ARG A CG    1 
ATOM   7171 C  CD    . ARG A 1 1013 ? 127.289 139.045 159.115 1.00 45.86  ? 1013 ARG A CD    1 
ATOM   7172 N  NE    . ARG A 1 1013 ? 126.915 140.426 158.826 1.00 45.86  ? 1013 ARG A NE    1 
ATOM   7173 C  CZ    . ARG A 1 1013 ? 127.693 141.289 158.182 1.00 45.86  ? 1013 ARG A CZ    1 
ATOM   7174 N  NH1   . ARG A 1 1013 ? 127.273 142.528 157.963 1.00 45.86  ? 1013 ARG A NH1   1 
ATOM   7175 N  NH2   . ARG A 1 1013 ? 128.892 140.915 157.757 1.00 45.86  ? 1013 ARG A NH2   1 
ATOM   7176 N  N     . HIS A 1 1014 ? 121.422 137.941 159.104 1.00 42.48  ? 1014 HIS A N     1 
ATOM   7177 C  CA    . HIS A 1 1014 ? 120.166 138.506 158.608 1.00 42.48  ? 1014 HIS A CA    1 
ATOM   7178 C  C     . HIS A 1 1014 ? 119.668 137.766 157.367 1.00 42.48  ? 1014 HIS A C     1 
ATOM   7179 O  O     . HIS A 1 1014 ? 119.286 138.372 156.364 1.00 42.48  ? 1014 HIS A O     1 
ATOM   7180 C  CB    . HIS A 1 1014 ? 120.320 140.002 158.329 1.00 42.48  ? 1014 HIS A CB    1 
ATOM   7181 C  CG    . HIS A 1 1014 ? 120.839 140.780 159.497 1.00 42.48  ? 1014 HIS A CG    1 
ATOM   7182 N  ND1   . HIS A 1 1014 ? 120.016 141.503 160.334 1.00 42.48  ? 1014 HIS A ND1   1 
ATOM   7183 C  CD2   . HIS A 1 1014 ? 122.096 140.946 159.970 1.00 42.48  ? 1014 HIS A CD2   1 
ATOM   7184 C  CE1   . HIS A 1 1014 ? 120.745 142.082 161.271 1.00 42.48  ? 1014 HIS A CE1   1 
ATOM   7185 N  NE2   . HIS A 1 1014 ? 122.010 141.760 161.073 1.00 42.48  ? 1014 HIS A NE2   1 
ATOM   7186 N  N     . VAL A 1 1015 ? 119.671 136.440 157.442 1.00 37.73  ? 1015 VAL A N     1 
ATOM   7187 C  CA    . VAL A 1 1015 ? 119.247 135.615 156.317 1.00 37.73  ? 1015 VAL A CA    1 
ATOM   7188 C  C     . VAL A 1 1015 ? 117.728 135.529 156.307 1.00 37.73  ? 1015 VAL A C     1 
ATOM   7189 O  O     . VAL A 1 1015 ? 117.115 135.063 157.273 1.00 37.73  ? 1015 VAL A O     1 
ATOM   7190 C  CB    . VAL A 1 1015 ? 119.878 134.219 156.386 1.00 37.73  ? 1015 VAL A CB    1 
ATOM   7191 C  CG1   . VAL A 1 1015 ? 119.341 133.345 155.268 1.00 37.73  ? 1015 VAL A CG1   1 
ATOM   7192 C  CG2   . VAL A 1 1015 ? 121.387 134.324 156.300 1.00 37.73  ? 1015 VAL A CG2   1 
ATOM   7193 N  N     . ASP A 1 1016 ? 117.119 135.980 155.216 1.00 39.58  ? 1016 ASP A N     1 
ATOM   7194 C  CA    . ASP A 1 1016 ? 115.688 135.844 154.989 1.00 39.58  ? 1016 ASP A CA    1 
ATOM   7195 C  C     . ASP A 1 1016 ? 115.477 134.954 153.774 1.00 39.58  ? 1016 ASP A C     1 
ATOM   7196 O  O     . ASP A 1 1016 ? 116.036 135.218 152.705 1.00 39.58  ? 1016 ASP A O     1 
ATOM   7197 C  CB    . ASP A 1 1016 ? 115.032 137.208 154.772 1.00 39.58  ? 1016 ASP A CB    1 
ATOM   7198 C  CG    . ASP A 1 1016 ? 115.146 138.105 155.984 1.00 39.58  ? 1016 ASP A CG    1 
ATOM   7199 O  OD1   . ASP A 1 1016 ? 115.250 137.574 157.109 1.00 39.58  ? 1016 ASP A OD1   1 
ATOM   7200 O  OD2   . ASP A 1 1016 ? 115.129 139.342 155.814 1.00 39.58  ? 1016 ASP A OD2   1 
ATOM   7201 N  N     . PHE A 1 1017 ? 114.678 133.903 153.936 1.00 31.73  ? 1017 PHE A N     1 
ATOM   7202 C  CA    . PHE A 1 1017 ? 114.520 132.914 152.883 1.00 31.73  ? 1017 PHE A CA    1 
ATOM   7203 C  C     . PHE A 1 1017 ? 113.064 132.502 152.747 1.00 31.73  ? 1017 PHE A C     1 
ATOM   7204 O  O     . PHE A 1 1017 ? 112.314 132.462 153.725 1.00 31.73  ? 1017 PHE A O     1 
ATOM   7205 C  CB    . PHE A 1 1017 ? 115.386 131.679 153.147 1.00 31.73  ? 1017 PHE A CB    1 
ATOM   7206 C  CG    . PHE A 1 1017 ? 115.223 130.600 152.122 1.00 31.73  ? 1017 PHE A CG    1 
ATOM   7207 C  CD1   . PHE A 1 1017 ? 115.701 130.772 150.837 1.00 31.73  ? 1017 PHE A CD1   1 
ATOM   7208 C  CD2   . PHE A 1 1017 ? 114.603 129.409 152.446 1.00 31.73  ? 1017 PHE A CD2   1 
ATOM   7209 C  CE1   . PHE A 1 1017 ? 115.552 129.783 149.892 1.00 31.73  ? 1017 PHE A CE1   1 
ATOM   7210 C  CE2   . PHE A 1 1017 ? 114.454 128.414 151.505 1.00 31.73  ? 1017 PHE A CE2   1 
ATOM   7211 C  CZ    . PHE A 1 1017 ? 114.929 128.601 150.227 1.00 31.73  ? 1017 PHE A CZ    1 
ATOM   7212 N  N     . ALA A 1 1018 ? 112.677 132.199 151.510 1.00 31.09  ? 1018 ALA A N     1 
ATOM   7213 C  CA    . ALA A 1 1018 ? 111.371 131.635 151.201 1.00 31.09  ? 1018 ALA A CA    1 
ATOM   7214 C  C     . ALA A 1 1018 ? 111.545 130.670 150.041 1.00 31.09  ? 1018 ALA A C     1 
ATOM   7215 O  O     . ALA A 1 1018 ? 112.207 131.004 149.054 1.00 31.09  ? 1018 ALA A O     1 
ATOM   7216 C  CB    . ALA A 1 1018 ? 110.357 132.727 150.848 1.00 31.09  ? 1018 ALA A CB    1 
ATOM   7217 N  N     . TYR A 1 1019 ? 110.965 129.483 150.164 1.00 31.80  ? 1019 TYR A N     1 
ATOM   7218 C  CA    . TYR A 1 1019 ? 111.140 128.471 149.134 1.00 31.80  ? 1019 TYR A CA    1 
ATOM   7219 C  C     . TYR A 1 1019 ? 110.488 128.926 147.830 1.00 31.80  ? 1019 TYR A C     1 
ATOM   7220 O  O     . TYR A 1 1019 ? 109.386 129.481 147.847 1.00 31.80  ? 1019 TYR A O     1 
ATOM   7221 C  CB    . TYR A 1 1019 ? 110.543 127.140 149.584 1.00 31.80  ? 1019 TYR A CB    1 
ATOM   7222 C  CG    . TYR A 1 1019 ? 111.476 126.321 150.444 1.00 31.80  ? 1019 TYR A CG    1 
ATOM   7223 C  CD1   . TYR A 1 1019 ? 112.451 125.518 149.873 1.00 31.80  ? 1019 TYR A CD1   1 
ATOM   7224 C  CD2   . TYR A 1 1019 ? 111.387 126.358 151.827 1.00 31.80  ? 1019 TYR A CD2   1 
ATOM   7225 C  CE1   . TYR A 1 1019 ? 113.307 124.770 150.654 1.00 31.80  ? 1019 TYR A CE1   1 
ATOM   7226 C  CE2   . TYR A 1 1019 ? 112.240 125.615 152.616 1.00 31.80  ? 1019 TYR A CE2   1 
ATOM   7227 C  CZ    . TYR A 1 1019 ? 113.197 124.823 152.025 1.00 31.80  ? 1019 TYR A CZ    1 
ATOM   7228 O  OH    . TYR A 1 1019 ? 114.049 124.080 152.810 1.00 31.80  ? 1019 TYR A OH    1 
ATOM   7229 N  N     . PRO A 1 1020 ? 111.150 128.718 146.690 1.00 29.32  ? 1020 PRO A N     1 
ATOM   7230 C  CA    . PRO A 1 1020 ? 110.567 129.162 145.413 1.00 29.32  ? 1020 PRO A CA    1 
ATOM   7231 C  C     . PRO A 1 1020 ? 109.233 128.514 145.091 1.00 29.32  ? 1020 PRO A C     1 
ATOM   7232 O  O     . PRO A 1 1020 ? 108.416 129.123 144.390 1.00 29.32  ? 1020 PRO A O     1 
ATOM   7233 C  CB    . PRO A 1 1020 ? 111.641 128.776 144.387 1.00 29.32  ? 1020 PRO A CB    1 
ATOM   7234 C  CG    . PRO A 1 1020 ? 112.902 128.667 145.174 1.00 29.32  ? 1020 PRO A CG    1 
ATOM   7235 C  CD    . PRO A 1 1020 ? 112.497 128.153 146.518 1.00 29.32  ? 1020 PRO A CD    1 
ATOM   7236 N  N     . SER A 1 1021 ? 108.991 127.291 145.570 1.00 31.50  ? 1021 SER A N     1 
ATOM   7237 C  CA    . SER A 1 1021 ? 107.732 126.617 145.268 1.00 31.50  ? 1021 SER A CA    1 
ATOM   7238 C  C     . SER A 1 1021 ? 106.542 127.371 145.849 1.00 31.50  ? 1021 SER A C     1 
ATOM   7239 O  O     . SER A 1 1021 ? 105.521 127.550 145.174 1.00 31.50  ? 1021 SER A O     1 
ATOM   7240 C  CB    . SER A 1 1021 ? 107.765 125.182 145.792 1.00 31.50  ? 1021 SER A CB    1 
ATOM   7241 O  OG    . SER A 1 1021 ? 106.666 124.436 145.300 1.00 31.50  ? 1021 SER A OG    1 
ATOM   7242 N  N     . ARG A 1 1022 ? 106.652 127.822 147.098 1.00 29.15  ? 1022 ARG A N     1 
ATOM   7243 C  CA    . ARG A 1 1022 ? 105.600 128.592 147.763 1.00 29.15  ? 1022 ARG A CA    1 
ATOM   7244 C  C     . ARG A 1 1022 ? 106.221 129.849 148.363 1.00 29.15  ? 1022 ARG A C     1 
ATOM   7245 O  O     . ARG A 1 1022 ? 106.440 129.939 149.578 1.00 29.15  ? 1022 ARG A O     1 
ATOM   7246 C  CB    . ARG A 1 1022 ? 104.867 127.739 148.805 1.00 29.15  ? 1022 ARG A CB    1 
ATOM   7247 C  CG    . ARG A 1 1022 ? 105.737 127.108 149.889 1.00 29.15  ? 1022 ARG A CG    1 
ATOM   7248 C  CD    . ARG A 1 1022 ? 104.887 126.388 150.925 1.00 29.15  ? 1022 ARG A CD    1 
ATOM   7249 N  NE    . ARG A 1 1022 ? 104.261 125.185 150.389 1.00 29.15  ? 1022 ARG A NE    1 
ATOM   7250 C  CZ    . ARG A 1 1022 ? 104.804 123.974 150.452 1.00 29.15  ? 1022 ARG A CZ    1 
ATOM   7251 N  NH1   . ARG A 1 1022 ? 105.978 123.806 151.042 1.00 29.15  ? 1022 ARG A NH1   1 
ATOM   7252 N  NH2   . ARG A 1 1022 ? 104.169 122.931 149.937 1.00 29.15  ? 1022 ARG A NH2   1 
ATOM   7253 N  N     . PRO A 1 1023 ? 106.505 130.859 147.534 1.00 27.08  ? 1023 PRO A N     1 
ATOM   7254 C  CA    . PRO A 1 1023 ? 107.202 132.066 147.996 1.00 27.08  ? 1023 PRO A CA    1 
ATOM   7255 C  C     . PRO A 1 1023 ? 106.309 133.040 148.763 1.00 27.08  ? 1023 PRO A C     1 
ATOM   7256 O  O     . PRO A 1 1023 ? 106.356 134.253 148.553 1.00 27.08  ? 1023 PRO A O     1 
ATOM   7257 C  CB    . PRO A 1 1023 ? 107.711 132.680 146.690 1.00 27.08  ? 1023 PRO A CB    1 
ATOM   7258 C  CG    . PRO A 1 1023 ? 106.693 132.279 145.681 1.00 27.08  ? 1023 PRO A CG    1 
ATOM   7259 C  CD    . PRO A 1 1023 ? 106.168 130.930 146.101 1.00 27.08  ? 1023 PRO A CD    1 
ATOM   7260 N  N     . ASP A 1 1024 ? 105.487 132.502 149.667 1.00 30.44  ? 1024 ASP A N     1 
ATOM   7261 C  CA    . ASP A 1 1024 ? 104.603 133.328 150.480 1.00 30.44  ? 1024 ASP A CA    1 
ATOM   7262 C  C     . ASP A 1 1024 ? 104.532 132.832 151.919 1.00 30.44  ? 1024 ASP A C     1 
ATOM   7263 O  O     . ASP A 1 1024 ? 103.523 133.046 152.600 1.00 30.44  ? 1024 ASP A O     1 
ATOM   7264 C  CB    . ASP A 1 1024 ? 103.196 133.379 149.883 1.00 30.44  ? 1024 ASP A CB    1 
ATOM   7265 C  CG    . ASP A 1 1024 ? 103.051 134.451 148.824 1.00 30.44  ? 1024 ASP A CG    1 
ATOM   7266 O  OD1   . ASP A 1 1024 ? 103.714 135.501 148.948 1.00 30.44  ? 1024 ASP A OD1   1 
ATOM   7267 O  OD2   . ASP A 1 1024 ? 102.273 134.245 147.869 1.00 30.44  ? 1024 ASP A OD2   1 
ATOM   7268 N  N     . VAL A 1 1025 ? 105.583 132.171 152.404 1.00 29.84  ? 1025 VAL A N     1 
ATOM   7269 C  CA    . VAL A 1 1025 ? 105.540 131.585 153.739 1.00 29.84  ? 1025 VAL A CA    1 
ATOM   7270 C  C     . VAL A 1 1025 ? 106.614 132.191 154.632 1.00 29.84  ? 1025 VAL A C     1 
ATOM   7271 O  O     . VAL A 1 1025 ? 106.435 132.280 155.852 1.00 29.84  ? 1025 VAL A O     1 
ATOM   7272 C  CB    . VAL A 1 1025 ? 105.683 130.054 153.673 1.00 29.84  ? 1025 VAL A CB    1 
ATOM   7273 C  CG1   . VAL A 1 1025 ? 104.389 129.424 153.182 1.00 29.84  ? 1025 VAL A CG1   1 
ATOM   7274 C  CG2   . VAL A 1 1025 ? 106.846 129.666 152.776 1.00 29.84  ? 1025 VAL A CG2   1 
ATOM   7275 N  N     . MET A 1 1026 ? 107.725 132.621 154.036 1.00 34.06  ? 1026 MET A N     1 
ATOM   7276 C  CA    . MET A 1 1026 ? 108.832 133.242 154.766 1.00 34.06  ? 1026 MET A CA    1 
ATOM   7277 C  C     . MET A 1 1026 ? 109.294 132.350 155.922 1.00 34.06  ? 1026 MET A C     1 
ATOM   7278 O  O     . MET A 1 1026 ? 109.131 132.663 157.101 1.00 34.06  ? 1026 MET A O     1 
ATOM   7279 C  CB    . MET A 1 1026 ? 108.439 134.638 155.261 1.00 34.06  ? 1026 MET A CB    1 
ATOM   7280 C  CG    . MET A 1 1026 ? 109.603 135.466 155.790 1.00 34.06  ? 1026 MET A CG    1 
ATOM   7281 S  SD    . MET A 1 1026 ? 110.300 136.573 154.551 1.00 34.06  ? 1026 MET A SD    1 
ATOM   7282 C  CE    . MET A 1 1026 ? 109.263 138.016 154.768 1.00 34.06  ? 1026 MET A CE    1 
ATOM   7283 N  N     . VAL A 1 1027 ? 109.861 131.201 155.542 1.00 32.61  ? 1027 VAL A N     1 
ATOM   7284 C  CA    . VAL A 1 1027 ? 110.296 130.214 156.525 1.00 32.61  ? 1027 VAL A CA    1 
ATOM   7285 C  C     . VAL A 1 1027 ? 111.359 130.767 157.463 1.00 32.61  ? 1027 VAL A C     1 
ATOM   7286 O  O     . VAL A 1 1027 ? 111.511 130.267 158.583 1.00 32.61  ? 1027 VAL A O     1 
ATOM   7287 C  CB    . VAL A 1 1027 ? 110.805 128.937 155.823 1.00 32.61  ? 1027 VAL A CB    1 
ATOM   7288 C  CG1   . VAL A 1 1027 ? 109.724 128.355 154.931 1.00 32.61  ? 1027 VAL A CG1   1 
ATOM   7289 C  CG2   . VAL A 1 1027 ? 112.060 129.229 155.024 1.00 32.61  ? 1027 VAL A CG2   1 
ATOM   7290 N  N     . PHE A 1 1028 ? 112.105 131.785 157.041 1.00 39.60  ? 1028 PHE A N     1 
ATOM   7291 C  CA    . PHE A 1 1028 ? 113.149 132.381 157.862 1.00 39.60  ? 1028 PHE A CA    1 
ATOM   7292 C  C     . PHE A 1 1028 ? 112.910 133.876 158.018 1.00 39.60  ? 1028 PHE A C     1 
ATOM   7293 O  O     . PHE A 1 1028 ? 112.601 134.573 157.047 1.00 39.60  ? 1028 PHE A O     1 
ATOM   7294 C  CB    . PHE A 1 1028 ? 114.536 132.138 157.262 1.00 39.60  ? 1028 PHE A CB    1 
ATOM   7295 C  CG    . PHE A 1 1028 ? 115.103 130.783 157.575 1.00 39.60  ? 1028 PHE A CG    1 
ATOM   7296 C  CD1   . PHE A 1 1028 ? 115.088 130.293 158.868 1.00 39.60  ? 1028 PHE A CD1   1 
ATOM   7297 C  CD2   . PHE A 1 1028 ? 115.663 130.005 156.577 1.00 39.60  ? 1028 PHE A CD2   1 
ATOM   7298 C  CE1   . PHE A 1 1028 ? 115.613 129.051 159.160 1.00 39.60  ? 1028 PHE A CE1   1 
ATOM   7299 C  CE2   . PHE A 1 1028 ? 116.190 128.762 156.863 1.00 39.60  ? 1028 PHE A CE2   1 
ATOM   7300 C  CZ    . PHE A 1 1028 ? 116.164 128.284 158.156 1.00 39.60  ? 1028 PHE A CZ    1 
ATOM   7301 N  N     . ARG A 1 1029 ? 113.054 134.357 159.247 1.00 48.48  ? 1029 ARG A N     1 
ATOM   7302 C  CA    . ARG A 1 1029 ? 112.947 135.764 159.591 1.00 48.48  ? 1029 ARG A CA    1 
ATOM   7303 C  C     . ARG A 1 1029 ? 114.367 136.315 159.764 1.00 48.48  ? 1029 ARG A C     1 
ATOM   7304 O  O     . ARG A 1 1029 ? 115.354 135.631 159.482 1.00 48.48  ? 1029 ARG A O     1 
ATOM   7305 C  CB    . ARG A 1 1029 ? 112.053 135.897 160.834 1.00 48.48  ? 1029 ARG A CB    1 
ATOM   7306 C  CG    . ARG A 1 1029 ? 111.774 137.305 161.368 1.00 48.48  ? 1029 ARG A CG    1 
ATOM   7307 C  CD    . ARG A 1 1029 ? 110.890 138.120 160.436 1.00 48.48  ? 1029 ARG A CD    1 
ATOM   7308 N  NE    . ARG A 1 1029 ? 111.666 138.835 159.427 1.00 48.48  ? 1029 ARG A NE    1 
ATOM   7309 C  CZ    . ARG A 1 1029 ? 111.133 139.501 158.407 1.00 48.48  ? 1029 ARG A CZ    1 
ATOM   7310 N  NH1   . ARG A 1 1029 ? 109.817 139.548 158.259 1.00 48.48  ? 1029 ARG A NH1   1 
ATOM   7311 N  NH2   . ARG A 1 1029 ? 111.917 140.124 157.538 1.00 48.48  ? 1029 ARG A NH2   1 
ATOM   7312 N  N     . ASP A 1 1030 ? 114.485 137.560 160.219 1.00 51.51  ? 1030 ASP A N     1 
ATOM   7313 C  CA    . ASP A 1 1030 ? 115.792 138.167 160.430 1.00 51.51  ? 1030 ASP A CA    1 
ATOM   7314 C  C     . ASP A 1 1030 ? 116.489 137.518 161.620 1.00 51.51  ? 1030 ASP A C     1 
ATOM   7315 O  O     . ASP A 1 1030 ? 116.283 137.927 162.766 1.00 51.51  ? 1030 ASP A O     1 
ATOM   7316 C  CB    . ASP A 1 1030 ? 115.649 139.674 160.652 1.00 51.51  ? 1030 ASP A CB    1 
ATOM   7317 C  CG    . ASP A 1 1030 ? 116.982 140.390 160.680 1.00 51.51  ? 1030 ASP A CG    1 
ATOM   7318 O  OD1   . ASP A 1 1030 ? 117.491 140.741 159.596 1.00 51.51  ? 1030 ASP A OD1   1 
ATOM   7319 O  OD2   . ASP A 1 1030 ? 117.521 140.602 161.787 1.00 51.51  ? 1030 ASP A OD2   1 
ATOM   7320 N  N     . PHE A 1 1031 ? 117.317 136.510 161.355 1.00 48.85  ? 1031 PHE A N     1 
ATOM   7321 C  CA    . PHE A 1 1031 ? 117.972 135.740 162.401 1.00 48.85  ? 1031 PHE A CA    1 
ATOM   7322 C  C     . PHE A 1 1031 ? 119.430 135.505 162.036 1.00 48.85  ? 1031 PHE A C     1 
ATOM   7323 O  O     . PHE A 1 1031 ? 119.812 135.532 160.864 1.00 48.85  ? 1031 PHE A O     1 
ATOM   7324 C  CB    . PHE A 1 1031 ? 117.271 134.395 162.630 1.00 48.85  ? 1031 PHE A CB    1 
ATOM   7325 C  CG    . PHE A 1 1031 ? 117.687 133.321 161.664 1.00 48.85  ? 1031 PHE A CG    1 
ATOM   7326 C  CD1   . PHE A 1 1031 ? 117.266 133.354 160.348 1.00 48.85  ? 1031 PHE A CD1   1 
ATOM   7327 C  CD2   . PHE A 1 1031 ? 118.484 132.268 162.079 1.00 48.85  ? 1031 PHE A CD2   1 
ATOM   7328 C  CE1   . PHE A 1 1031 ? 117.643 132.368 159.461 1.00 48.85  ? 1031 PHE A CE1   1 
ATOM   7329 C  CE2   . PHE A 1 1031 ? 118.861 131.277 161.196 1.00 48.85  ? 1031 PHE A CE2   1 
ATOM   7330 C  CZ    . PHE A 1 1031 ? 118.439 131.327 159.886 1.00 48.85  ? 1031 PHE A CZ    1 
ATOM   7331 N  N     . ASN A 1 1032 ? 120.243 135.268 163.063 1.00 51.81  ? 1032 ASN A N     1 
ATOM   7332 C  CA    . ASN A 1 1032 ? 121.664 135.009 162.886 1.00 51.81  ? 1032 ASN A CA    1 
ATOM   7333 C  C     . ASN A 1 1032 ? 122.138 133.977 163.898 1.00 51.81  ? 1032 ASN A C     1 
ATOM   7334 O  O     . ASN A 1 1032 ? 121.694 133.971 165.049 1.00 51.81  ? 1032 ASN A O     1 
ATOM   7335 C  CB    . ASN A 1 1032 ? 122.484 136.302 163.008 1.00 51.81  ? 1032 ASN A CB    1 
ATOM   7336 C  CG    . ASN A 1 1032 ? 122.194 137.069 164.287 1.00 51.81  ? 1032 ASN A CG    1 
ATOM   7337 O  OD1   . ASN A 1 1032 ? 121.397 136.641 165.120 1.00 51.81  ? 1032 ASN A OD1   1 
ATOM   7338 N  ND2   . ASN A 1 1032 ? 122.846 138.214 164.445 1.00 51.81  ? 1032 ASN A ND2   1 
ATOM   7339 N  N     . LEU A 1 1033 ? 123.032 133.096 163.455 1.00 55.70  ? 1033 LEU A N     1 
ATOM   7340 C  CA    . LEU A 1 1033 ? 123.625 132.079 164.310 1.00 55.70  ? 1033 LEU A CA    1 
ATOM   7341 C  C     . LEU A 1 1033 ? 125.048 131.812 163.845 1.00 55.70  ? 1033 LEU A C     1 
ATOM   7342 O  O     . LEU A 1 1033 ? 125.338 131.834 162.647 1.00 55.70  ? 1033 LEU A O     1 
ATOM   7343 C  CB    . LEU A 1 1033 ? 122.800 130.781 164.303 1.00 55.70  ? 1033 LEU A CB    1 
ATOM   7344 C  CG    . LEU A 1 1033 ? 122.565 130.033 162.985 1.00 55.70  ? 1033 LEU A CG    1 
ATOM   7345 C  CD1   . LEU A 1 1033 ? 123.663 129.017 162.696 1.00 55.70  ? 1033 LEU A CD1   1 
ATOM   7346 C  CD2   . LEU A 1 1033 ? 121.207 129.354 163.002 1.00 55.70  ? 1033 LEU A CD2   1 
ATOM   7347 N  N     . ARG A 1 1034 ? 125.936 131.560 164.801 1.00 57.63  ? 1034 ARG A N     1 
ATOM   7348 C  CA    . ARG A 1 1034 ? 127.339 131.319 164.497 1.00 57.63  ? 1034 ARG A CA    1 
ATOM   7349 C  C     . ARG A 1 1034 ? 127.781 129.992 165.095 1.00 57.63  ? 1034 ARG A C     1 
ATOM   7350 O  O     . ARG A 1 1034 ? 127.420 129.655 166.227 1.00 57.63  ? 1034 ARG A O     1 
ATOM   7351 C  CB    . ARG A 1 1034 ? 128.223 132.464 165.013 1.00 57.63  ? 1034 ARG A CB    1 
ATOM   7352 C  CG    . ARG A 1 1034 ? 128.224 132.643 166.521 1.00 57.63  ? 1034 ARG A CG    1 
ATOM   7353 C  CD    . ARG A 1 1034 ? 128.991 133.892 166.921 1.00 57.63  ? 1034 ARG A CD    1 
ATOM   7354 N  NE    . ARG A 1 1034 ? 130.247 134.017 166.187 1.00 57.63  ? 1034 ARG A NE    1 
ATOM   7355 C  CZ    . ARG A 1 1034 ? 131.358 133.350 166.484 1.00 57.63  ? 1034 ARG A CZ    1 
ATOM   7356 N  NH1   . ARG A 1 1034 ? 131.377 132.506 167.506 1.00 57.63  ? 1034 ARG A NH1   1 
ATOM   7357 N  NH2   . ARG A 1 1034 ? 132.452 133.529 165.757 1.00 57.63  ? 1034 ARG A NH2   1 
ATOM   7358 N  N     . ILE A 1 1035 ? 128.551 129.235 164.317 1.00 56.06  ? 1035 ILE A N     1 
ATOM   7359 C  CA    . ILE A 1 1035 ? 129.121 127.961 164.736 1.00 56.06  ? 1035 ILE A CA    1 
ATOM   7360 C  C     . ILE A 1 1035 ? 130.630 128.101 164.588 1.00 56.06  ? 1035 ILE A C     1 
ATOM   7361 O  O     . ILE A 1 1035 ? 131.159 128.064 163.470 1.00 56.06  ? 1035 ILE A O     1 
ATOM   7362 C  CB    . ILE A 1 1035 ? 128.594 126.782 163.913 1.00 56.06  ? 1035 ILE A CB    1 
ATOM   7363 C  CG1   . ILE A 1 1035 ? 127.090 126.924 163.678 1.00 56.06  ? 1035 ILE A CG1   1 
ATOM   7364 C  CG2   . ILE A 1 1035 ? 128.896 125.473 164.614 1.00 56.06  ? 1035 ILE A CG2   1 
ATOM   7365 C  CD1   . ILE A 1 1035 ? 126.569 126.065 162.552 1.00 56.06  ? 1035 ILE A CD1   1 
ATOM   7366 N  N     . ARG A 1 1036 ? 131.324 128.282 165.708 1.00 59.16  ? 1036 ARG A N     1 
ATOM   7367 C  CA    . ARG A 1 1036 ? 132.777 128.355 165.689 1.00 59.16  ? 1036 ARG A CA    1 
ATOM   7368 C  C     . ARG A 1 1036 ? 133.364 126.976 165.411 1.00 59.16  ? 1036 ARG A C     1 
ATOM   7369 O  O     . ARG A 1 1036 ? 132.814 125.955 165.834 1.00 59.16  ? 1036 ARG A O     1 
ATOM   7370 C  CB    . ARG A 1 1036 ? 133.292 128.903 167.021 1.00 59.16  ? 1036 ARG A CB    1 
ATOM   7371 C  CG    . ARG A 1 1036 ? 134.804 128.890 167.182 1.00 59.16  ? 1036 ARG A CG    1 
ATOM   7372 C  CD    . ARG A 1 1036 ? 135.489 129.738 166.122 1.00 59.16  ? 1036 ARG A CD    1 
ATOM   7373 N  NE    . ARG A 1 1036 ? 135.275 131.166 166.334 1.00 59.16  ? 1036 ARG A NE    1 
ATOM   7374 C  CZ    . ARG A 1 1036 ? 135.667 132.111 165.485 1.00 59.16  ? 1036 ARG A CZ    1 
ATOM   7375 N  NH1   . ARG A 1 1036 ? 135.433 133.388 165.757 1.00 59.16  ? 1036 ARG A NH1   1 
ATOM   7376 N  NH2   . ARG A 1 1036 ? 136.295 131.781 164.366 1.00 59.16  ? 1036 ARG A NH2   1 
ATOM   7377 N  N     . ALA A 1 1037 ? 134.477 126.950 164.680 1.00 59.56  ? 1037 ALA A N     1 
ATOM   7378 C  CA    . ALA A 1 1037 ? 135.138 125.690 164.367 1.00 59.56  ? 1037 ALA A CA    1 
ATOM   7379 C  C     . ALA A 1 1037 ? 135.536 124.963 165.644 1.00 59.56  ? 1037 ALA A C     1 
ATOM   7380 O  O     . ALA A 1 1037 ? 136.053 125.565 166.589 1.00 59.56  ? 1037 ALA A O     1 
ATOM   7381 C  CB    . ALA A 1 1037 ? 136.369 125.940 163.496 1.00 59.56  ? 1037 ALA A CB    1 
ATOM   7382 N  N     . GLY A 1 1038 ? 135.292 123.656 165.668 1.00 62.95  ? 1038 GLY A N     1 
ATOM   7383 C  CA    . GLY A 1 1038 ? 135.542 122.856 166.847 1.00 62.95  ? 1038 GLY A CA    1 
ATOM   7384 C  C     . GLY A 1 1038 ? 134.382 122.748 167.810 1.00 62.95  ? 1038 GLY A C     1 
ATOM   7385 O  O     . GLY A 1 1038 ? 134.583 122.300 168.945 1.00 62.95  ? 1038 GLY A O     1 
ATOM   7386 N  N     . HIS A 1 1039 ? 133.182 123.139 167.401 1.00 66.54  ? 1039 HIS A N     1 
ATOM   7387 C  CA    . HIS A 1 1039 ? 131.990 123.069 168.234 1.00 66.54  ? 1039 HIS A CA    1 
ATOM   7388 C  C     . HIS A 1 1039 ? 130.914 122.266 167.503 1.00 66.54  ? 1039 HIS A C     1 
ATOM   7389 O  O     . HIS A 1 1039 ? 131.167 121.653 166.463 1.00 66.54  ? 1039 HIS A O     1 
ATOM   7390 C  CB    . HIS A 1 1039 ? 131.508 124.474 168.600 1.00 66.54  ? 1039 HIS A CB    1 
ATOM   7391 C  CG    . HIS A 1 1039 ? 132.503 125.263 169.392 1.00 66.54  ? 1039 HIS A CG    1 
ATOM   7392 N  ND1   . HIS A 1 1039 ? 133.651 125.786 168.836 1.00 66.54  ? 1039 HIS A ND1   1 
ATOM   7393 C  CD2   . HIS A 1 1039 ? 132.523 125.618 170.698 1.00 66.54  ? 1039 HIS A CD2   1 
ATOM   7394 C  CE1   . HIS A 1 1039 ? 134.334 126.429 169.766 1.00 66.54  ? 1039 HIS A CE1   1 
ATOM   7395 N  NE2   . HIS A 1 1039 ? 133.672 126.342 170.905 1.00 66.54  ? 1039 HIS A NE2   1 
ATOM   7396 N  N     . SER A 1 1040 ? 129.704 122.271 168.056 1.00 71.01  ? 1040 SER A N     1 
ATOM   7397 C  CA    . SER A 1 1040 ? 128.622 121.474 167.497 1.00 71.01  ? 1040 SER A CA    1 
ATOM   7398 C  C     . SER A 1 1040 ? 127.294 122.186 167.713 1.00 71.01  ? 1040 SER A C     1 
ATOM   7399 O  O     . SER A 1 1040 ? 127.174 123.096 168.537 1.00 71.01  ? 1040 SER A O     1 
ATOM   7400 C  CB    . SER A 1 1040 ? 128.592 120.072 168.111 1.00 71.01  ? 1040 SER A CB    1 
ATOM   7401 O  OG    . SER A 1 1040 ? 129.514 119.217 167.458 1.00 71.01  ? 1040 SER A OG    1 
ATOM   7402 N  N     . GLN A 1 1041 ? 126.294 121.757 166.947 1.00 73.34  ? 1041 GLN A N     1 
ATOM   7403 C  CA    . GLN A 1 1041 ? 124.939 122.277 167.034 1.00 73.34  ? 1041 GLN A CA    1 
ATOM   7404 C  C     . GLN A 1 1041 ? 123.994 121.153 167.434 1.00 73.34  ? 1041 GLN A C     1 
ATOM   7405 O  O     . GLN A 1 1041 ? 124.255 119.977 167.166 1.00 73.34  ? 1041 GLN A O     1 
ATOM   7406 C  CB    . GLN A 1 1041 ? 124.475 122.867 165.697 1.00 73.34  ? 1041 GLN A CB    1 
ATOM   7407 C  CG    . GLN A 1 1041 ? 124.983 124.263 165.385 1.00 73.34  ? 1041 GLN A CG    1 
ATOM   7408 C  CD    . GLN A 1 1041 ? 125.129 125.130 166.612 1.00 73.34  ? 1041 GLN A CD    1 
ATOM   7409 O  OE1   . GLN A 1 1041 ? 126.240 125.482 167.001 1.00 73.34  ? 1041 GLN A OE1   1 
ATOM   7410 N  NE2   . GLN A 1 1041 ? 124.007 125.489 167.225 1.00 73.34  ? 1041 GLN A NE2   1 
ATOM   7411 N  N     . ALA A 1 1042 ? 122.888 121.521 168.077 1.00 77.95  ? 1042 ALA A N     1 
ATOM   7412 C  CA    . ALA A 1 1042 ? 121.812 120.581 168.362 1.00 77.95  ? 1042 ALA A CA    1 
ATOM   7413 C  C     . ALA A 1 1042 ? 120.547 120.898 167.582 1.00 77.95  ? 1042 ALA A C     1 
ATOM   7414 O  O     . ALA A 1 1042 ? 119.952 119.999 166.981 1.00 77.95  ? 1042 ALA A O     1 
ATOM   7415 C  CB    . ALA A 1 1042 ? 121.507 120.551 169.865 1.00 77.95  ? 1042 ALA A CB    1 
ATOM   7416 N  N     . LEU A 1 1043 ? 120.118 122.160 167.583 1.00 74.51  ? 1043 LEU A N     1 
ATOM   7417 C  CA    . LEU A 1 1043 ? 119.034 122.640 166.725 1.00 74.51  ? 1043 LEU A CA    1 
ATOM   7418 C  C     . LEU A 1 1043 ? 117.749 121.839 166.946 1.00 74.51  ? 1043 LEU A C     1 
ATOM   7419 O  O     . LEU A 1 1043 ? 117.241 121.169 166.045 1.00 74.51  ? 1043 LEU A O     1 
ATOM   7420 C  CB    . LEU A 1 1043 ? 119.457 122.602 165.253 1.00 74.51  ? 1043 LEU A CB    1 
ATOM   7421 C  CG    . LEU A 1 1043 ? 120.640 123.474 164.832 1.00 74.51  ? 1043 LEU A CG    1 
ATOM   7422 C  CD1   . LEU A 1 1043 ? 120.868 123.369 163.334 1.00 74.51  ? 1043 LEU A CD1   1 
ATOM   7423 C  CD2   . LEU A 1 1043 ? 120.430 124.918 165.243 1.00 74.51  ? 1043 LEU A CD2   1 
ATOM   7424 N  N     . VAL A 1 1044 ? 117.227 121.914 168.170 1.00 76.57  ? 1044 VAL A N     1 
ATOM   7425 C  CA    . VAL A 1 1044 ? 115.968 121.243 168.471 1.00 76.57  ? 1044 VAL A CA    1 
ATOM   7426 C  C     . VAL A 1 1044 ? 114.833 121.958 167.748 1.00 76.57  ? 1044 VAL A C     1 
ATOM   7427 O  O     . VAL A 1 1044 ? 114.660 123.178 167.871 1.00 76.57  ? 1044 VAL A O     1 
ATOM   7428 C  CB    . VAL A 1 1044 ? 115.738 121.170 169.988 1.00 76.57  ? 1044 VAL A CB    1 
ATOM   7429 C  CG1   . VAL A 1 1044 ? 116.718 120.193 170.613 1.00 76.57  ? 1044 VAL A CG1   1 
ATOM   7430 C  CG2   . VAL A 1 1044 ? 115.908 122.531 170.625 1.00 76.57  ? 1044 VAL A CG2   1 
ATOM   7431 N  N     . GLY A 1 1045 ? 114.059 121.196 166.982 1.00 60.88  ? 1045 GLY A N     1 
ATOM   7432 C  CA    . GLY A 1 1045 ? 113.132 121.742 166.010 1.00 60.88  ? 1045 GLY A CA    1 
ATOM   7433 C  C     . GLY A 1 1045 ? 111.695 121.302 166.193 1.00 60.88  ? 1045 GLY A C     1 
ATOM   7434 O  O     . GLY A 1 1045 ? 111.041 120.928 165.216 1.00 60.88  ? 1045 GLY A O     1 
ATOM   7435 N  N     . ALA A 1 1046 ? 111.209 121.335 167.437 1.00 58.03  ? 1046 ALA A N     1 
ATOM   7436 C  CA    . ALA A 1 1046 ? 109.951 120.720 167.857 1.00 58.03  ? 1046 ALA A CA    1 
ATOM   7437 C  C     . ALA A 1 1046 ? 108.858 120.760 166.796 1.00 58.03  ? 1046 ALA A C     1 
ATOM   7438 O  O     . ALA A 1 1046 ? 108.293 119.719 166.444 1.00 58.03  ? 1046 ALA A O     1 
ATOM   7439 C  CB    . ALA A 1 1046 ? 109.444 121.401 169.131 1.00 58.03  ? 1046 ALA A CB    1 
ATOM   7440 N  N     . SER A 1 1047 ? 108.558 121.942 166.274 1.00 54.56  ? 1047 SER A N     1 
ATOM   7441 C  CA    . SER A 1 1047 ? 107.698 122.084 165.110 1.00 54.56  ? 1047 SER A CA    1 
ATOM   7442 C  C     . SER A 1 1047 ? 108.574 122.365 163.899 1.00 54.56  ? 1047 SER A C     1 
ATOM   7443 O  O     . SER A 1 1047 ? 109.479 123.204 163.964 1.00 54.56  ? 1047 SER A O     1 
ATOM   7444 C  CB    . SER A 1 1047 ? 106.676 123.209 165.301 1.00 54.56  ? 1047 SER A CB    1 
ATOM   7445 O  OG    . SER A 1 1047 ? 105.671 122.834 166.226 1.00 54.56  ? 1047 SER A OG    1 
ATOM   7446 N  N     . GLY A 1 1048 ? 108.321 121.650 162.805 1.00 49.59  ? 1048 GLY A N     1 
ATOM   7447 C  CA    . GLY A 1 1048 ? 109.194 121.771 161.656 1.00 49.59  ? 1048 GLY A CA    1 
ATOM   7448 C  C     . GLY A 1 1048 ? 109.259 123.182 161.116 1.00 49.59  ? 1048 GLY A C     1 
ATOM   7449 O  O     . GLY A 1 1048 ? 108.342 123.639 160.427 1.00 49.59  ? 1048 GLY A O     1 
ATOM   7450 N  N     . SER A 1 1049 ? 110.349 123.884 161.428 1.00 47.93  ? 1049 SER A N     1 
ATOM   7451 C  CA    . SER A 1 1049 ? 110.564 125.238 160.933 1.00 47.93  ? 1049 SER A CA    1 
ATOM   7452 C  C     . SER A 1 1049 ? 111.829 125.352 160.095 1.00 47.93  ? 1049 SER A C     1 
ATOM   7453 O  O     . SER A 1 1049 ? 111.757 125.751 158.929 1.00 47.93  ? 1049 SER A O     1 
ATOM   7454 C  CB    . SER A 1 1049 ? 110.609 126.215 162.114 1.00 47.93  ? 1049 SER A CB    1 
ATOM   7455 O  OG    . SER A 1 1049 ? 109.512 126.006 162.984 1.00 47.93  ? 1049 SER A OG    1 
ATOM   7456 N  N     . GLY A 1 1050 ? 112.988 125.012 160.653 1.00 44.96  ? 1050 GLY A N     1 
ATOM   7457 C  CA    . GLY A 1 1050 ? 114.241 125.177 159.944 1.00 44.96  ? 1050 GLY A CA    1 
ATOM   7458 C  C     . GLY A 1 1050 ? 115.289 124.130 160.258 1.00 44.96  ? 1050 GLY A C     1 
ATOM   7459 O  O     . GLY A 1 1050 ? 116.481 124.365 160.037 1.00 44.96  ? 1050 GLY A O     1 
ATOM   7460 N  N     . LYS A 1 1051 ? 114.868 122.980 160.788 1.00 47.16  ? 1051 LYS A N     1 
ATOM   7461 C  CA    . LYS A 1 1051 ? 115.827 121.948 161.170 1.00 47.16  ? 1051 LYS A CA    1 
ATOM   7462 C  C     . LYS A 1 1051 ? 116.653 121.493 159.974 1.00 47.16  ? 1051 LYS A C     1 
ATOM   7463 O  O     . LYS A 1 1051 ? 117.888 121.479 160.027 1.00 47.16  ? 1051 LYS A O     1 
ATOM   7464 C  CB    . LYS A 1 1051 ? 115.098 120.761 161.795 1.00 47.16  ? 1051 LYS A CB    1 
ATOM   7465 C  CG    . LYS A 1 1051 ? 115.242 120.649 163.297 1.00 47.16  ? 1051 LYS A CG    1 
ATOM   7466 C  CD    . LYS A 1 1051 ? 114.602 119.365 163.794 1.00 47.16  ? 1051 LYS A CD    1 
ATOM   7467 C  CE    . LYS A 1 1051 ? 115.320 118.823 165.015 1.00 47.16  ? 1051 LYS A CE    1 
ATOM   7468 N  NZ    . LYS A 1 1051 ? 114.829 117.468 165.384 1.00 47.16  ? 1051 LYS A NZ    1 
ATOM   7469 N  N     . SER A 1 1052 ? 115.989 121.117 158.884 1.00 39.66  ? 1052 SER A N     1 
ATOM   7470 C  CA    . SER A 1 1052 ? 116.681 120.679 157.681 1.00 39.66  ? 1052 SER A CA    1 
ATOM   7471 C  C     . SER A 1 1052 ? 116.925 121.807 156.690 1.00 39.66  ? 1052 SER A C     1 
ATOM   7472 O  O     . SER A 1 1052 ? 117.635 121.597 155.701 1.00 39.66  ? 1052 SER A O     1 
ATOM   7473 C  CB    . SER A 1 1052 ? 115.888 119.562 156.994 1.00 39.66  ? 1052 SER A CB    1 
ATOM   7474 O  OG    . SER A 1 1052 ? 115.738 118.443 157.851 1.00 39.66  ? 1052 SER A OG    1 
ATOM   7475 N  N     . SER A 1 1053 ? 116.358 122.990 156.926 1.00 37.57  ? 1053 SER A N     1 
ATOM   7476 C  CA    . SER A 1 1053 ? 116.556 124.103 156.005 1.00 37.57  ? 1053 SER A CA    1 
ATOM   7477 C  C     . SER A 1 1053 ? 117.932 124.735 156.174 1.00 37.57  ? 1053 SER A C     1 
ATOM   7478 O  O     . SER A 1 1053 ? 118.536 125.180 155.192 1.00 37.57  ? 1053 SER A O     1 
ATOM   7479 C  CB    . SER A 1 1053 ? 115.460 125.148 156.203 1.00 37.57  ? 1053 SER A CB    1 
ATOM   7480 O  OG    . SER A 1 1053 ? 115.460 126.086 155.143 1.00 37.57  ? 1053 SER A OG    1 
ATOM   7481 N  N     . VAL A 1 1054 ? 118.440 124.789 157.408 1.00 37.96  ? 1054 VAL A N     1 
ATOM   7482 C  CA    . VAL A 1 1054 ? 119.760 125.366 157.646 1.00 37.96  ? 1054 VAL A CA    1 
ATOM   7483 C  C     . VAL A 1 1054 ? 120.843 124.526 156.987 1.00 37.96  ? 1054 VAL A C     1 
ATOM   7484 O  O     . VAL A 1 1054 ? 121.859 125.059 156.526 1.00 37.96  ? 1054 VAL A O     1 
ATOM   7485 C  CB    . VAL A 1 1054 ? 120.015 125.531 159.157 1.00 37.96  ? 1054 VAL A CB    1 
ATOM   7486 C  CG1   . VAL A 1 1054 ? 119.155 126.648 159.719 1.00 37.96  ? 1054 VAL A CG1   1 
ATOM   7487 C  CG2   . VAL A 1 1054 ? 119.746 124.230 159.888 1.00 37.96  ? 1054 VAL A CG2   1 
ATOM   7488 N  N     . ILE A 1 1055 ? 120.657 123.205 156.944 1.00 39.66  ? 1055 ILE A N     1 
ATOM   7489 C  CA    . ILE A 1 1055 ? 121.624 122.335 156.281 1.00 39.66  ? 1055 ILE A CA    1 
ATOM   7490 C  C     . ILE A 1 1055 ? 121.688 122.649 154.792 1.00 39.66  ? 1055 ILE A C     1 
ATOM   7491 O  O     . ILE A 1 1055 ? 122.762 122.611 154.179 1.00 39.66  ? 1055 ILE A O     1 
ATOM   7492 C  CB    . ILE A 1 1055 ? 121.277 120.858 156.539 1.00 39.66  ? 1055 ILE A CB    1 
ATOM   7493 C  CG1   . ILE A 1 1055 ? 121.258 120.579 158.042 1.00 39.66  ? 1055 ILE A CG1   1 
ATOM   7494 C  CG2   . ILE A 1 1055 ? 122.266 119.943 155.837 1.00 39.66  ? 1055 ILE A CG2   1 
ATOM   7495 C  CD1   . ILE A 1 1055 ? 121.161 119.115 158.389 1.00 39.66  ? 1055 ILE A CD1   1 
ATOM   7496 N  N     . ALA A 1 1056 ? 120.542 122.965 154.186 1.00 36.21  ? 1056 ALA A N     1 
ATOM   7497 C  CA    . ALA A 1 1056 ? 120.538 123.355 152.780 1.00 36.21  ? 1056 ALA A CA    1 
ATOM   7498 C  C     . ALA A 1 1056 ? 121.282 124.664 152.555 1.00 36.21  ? 1056 ALA A C     1 
ATOM   7499 O  O     . ALA A 1 1056 ? 121.764 124.917 151.447 1.00 36.21  ? 1056 ALA A O     1 
ATOM   7500 C  CB    . ALA A 1 1056 ? 119.103 123.468 152.268 1.00 36.21  ? 1056 ALA A CB    1 
ATOM   7501 N  N     . MET A 1 1057 ? 121.379 125.509 153.584 1.00 37.26  ? 1057 MET A N     1 
ATOM   7502 C  CA    . MET A 1 1057 ? 122.091 126.774 153.433 1.00 37.26  ? 1057 MET A CA    1 
ATOM   7503 C  C     . MET A 1 1057 ? 123.599 126.565 153.371 1.00 37.26  ? 1057 MET A C     1 
ATOM   7504 O  O     . MET A 1 1057 ? 124.279 127.171 152.536 1.00 37.26  ? 1057 MET A O     1 
ATOM   7505 C  CB    . MET A 1 1057 ? 121.730 127.720 154.577 1.00 37.26  ? 1057 MET A CB    1 
ATOM   7506 C  CG    . MET A 1 1057 ? 120.317 128.264 154.503 1.00 37.26  ? 1057 MET A CG    1 
ATOM   7507 S  SD    . MET A 1 1057 ? 120.027 129.228 153.011 1.00 37.26  ? 1057 MET A SD    1 
ATOM   7508 C  CE    . MET A 1 1057 ? 118.240 129.290 153.006 1.00 37.26  ? 1057 MET A CE    1 
ATOM   7509 N  N     . ILE A 1 1058 ? 124.140 125.718 154.251 1.00 35.82  ? 1058 ILE A N     1 
ATOM   7510 C  CA    . ILE A 1 1058 ? 125.587 125.514 154.296 1.00 35.82  ? 1058 ILE A CA    1 
ATOM   7511 C  C     . ILE A 1 1058 ? 126.076 124.908 152.987 1.00 35.82  ? 1058 ILE A C     1 
ATOM   7512 O  O     . ILE A 1 1058 ? 127.022 125.404 152.365 1.00 35.82  ? 1058 ILE A O     1 
ATOM   7513 C  CB    . ILE A 1 1058 ? 125.969 124.635 155.499 1.00 35.82  ? 1058 ILE A CB    1 
ATOM   7514 C  CG1   . ILE A 1 1058 ? 125.164 125.041 156.732 1.00 35.82  ? 1058 ILE A CG1   1 
ATOM   7515 C  CG2   . ILE A 1 1058 ? 127.453 124.747 155.785 1.00 35.82  ? 1058 ILE A CG2   1 
ATOM   7516 C  CD1   . ILE A 1 1058 ? 125.474 126.428 157.220 1.00 35.82  ? 1058 ILE A CD1   1 
ATOM   7517 N  N     . GLU A 1 1059 ? 125.436 123.825 152.551 1.00 37.79  ? 1059 GLU A N     1 
ATOM   7518 C  CA    . GLU A 1 1059 ? 125.666 123.268 151.220 1.00 37.79  ? 1059 GLU A CA    1 
ATOM   7519 C  C     . GLU A 1 1059 ? 124.652 123.921 150.290 1.00 37.79  ? 1059 GLU A C     1 
ATOM   7520 O  O     . GLU A 1 1059 ? 123.618 123.347 149.944 1.00 37.79  ? 1059 GLU A O     1 
ATOM   7521 C  CB    . GLU A 1 1059 ? 125.532 121.751 151.236 1.00 37.79  ? 1059 GLU A CB    1 
ATOM   7522 C  CG    . GLU A 1 1059 ? 126.774 121.016 151.701 1.00 37.79  ? 1059 GLU A CG    1 
ATOM   7523 C  CD    . GLU A 1 1059 ? 126.854 119.611 151.141 1.00 37.79  ? 1059 GLU A CD    1 
ATOM   7524 O  OE1   . GLU A 1 1059 ? 127.808 118.882 151.481 1.00 37.79  ? 1059 GLU A OE1   1 
ATOM   7525 O  OE2   . GLU A 1 1059 ? 125.956 119.237 150.358 1.00 37.79  ? 1059 GLU A OE2   1 
ATOM   7526 N  N     . ARG A 1 1060 ? 124.967 125.152 149.883 1.00 35.32  ? 1060 ARG A N     1 
ATOM   7527 C  CA    . ARG A 1 1060 ? 123.975 126.044 149.293 1.00 35.32  ? 1060 ARG A CA    1 
ATOM   7528 C  C     . ARG A 1 1060 ? 123.249 125.415 148.111 1.00 35.32  ? 1060 ARG A C     1 
ATOM   7529 O  O     . ARG A 1 1060 ? 123.844 125.143 147.063 1.00 35.32  ? 1060 ARG A O     1 
ATOM   7530 C  CB    . ARG A 1 1060 ? 124.624 127.370 148.882 1.00 35.32  ? 1060 ARG A CB    1 
ATOM   7531 C  CG    . ARG A 1 1060 ? 125.857 127.250 148.006 1.00 35.32  ? 1060 ARG A CG    1 
ATOM   7532 C  CD    . ARG A 1 1060 ? 126.566 128.588 147.887 1.00 35.32  ? 1060 ARG A CD    1 
ATOM   7533 N  NE    . ARG A 1 1060 ? 125.703 129.624 147.329 1.00 35.32  ? 1060 ARG A NE    1 
ATOM   7534 C  CZ    . ARG A 1 1060 ? 125.578 129.874 146.030 1.00 35.32  ? 1060 ARG A CZ    1 
ATOM   7535 N  NH1   . ARG A 1 1060 ? 126.263 129.162 145.146 1.00 35.32  ? 1060 ARG A NH1   1 
ATOM   7536 N  NH2   . ARG A 1 1060 ? 124.769 130.838 145.613 1.00 35.32  ? 1060 ARG A NH2   1 
ATOM   7537 N  N     . PHE A 1 1061 ? 121.956 125.166 148.294 1.00 31.98  ? 1061 PHE A N     1 
ATOM   7538 C  CA    . PHE A 1 1061 ? 121.078 124.705 147.230 1.00 31.98  ? 1061 PHE A CA    1 
ATOM   7539 C  C     . PHE A 1 1061 ? 120.179 125.810 146.700 1.00 31.98  ? 1061 PHE A C     1 
ATOM   7540 O  O     . PHE A 1 1061 ? 119.802 125.780 145.524 1.00 31.98  ? 1061 PHE A O     1 
ATOM   7541 C  CB    . PHE A 1 1061 ? 120.207 123.545 147.724 1.00 31.98  ? 1061 PHE A CB    1 
ATOM   7542 C  CG    . PHE A 1 1061 ? 120.984 122.323 148.122 1.00 31.98  ? 1061 PHE A CG    1 
ATOM   7543 C  CD1   . PHE A 1 1061 ? 121.738 121.630 147.193 1.00 31.98  ? 1061 PHE A CD1   1 
ATOM   7544 C  CD2   . PHE A 1 1061 ? 120.947 121.858 149.426 1.00 31.98  ? 1061 PHE A CD2   1 
ATOM   7545 C  CE1   . PHE A 1 1061 ? 122.449 120.503 147.558 1.00 31.98  ? 1061 PHE A CE1   1 
ATOM   7546 C  CE2   . PHE A 1 1061 ? 121.657 120.732 149.796 1.00 31.98  ? 1061 PHE A CE2   1 
ATOM   7547 C  CZ    . PHE A 1 1061 ? 122.409 120.054 148.861 1.00 31.98  ? 1061 PHE A CZ    1 
ATOM   7548 N  N     . TYR A 1 1062 ? 119.834 126.778 147.541 1.00 29.55  ? 1062 TYR A N     1 
ATOM   7549 C  CA    . TYR A 1 1062 ? 119.051 127.945 147.169 1.00 29.55  ? 1062 TYR A CA    1 
ATOM   7550 C  C     . TYR A 1 1062 ? 119.833 129.207 147.523 1.00 29.55  ? 1062 TYR A C     1 
ATOM   7551 O  O     . TYR A 1 1062 ? 120.965 129.148 148.007 1.00 29.55  ? 1062 TYR A O     1 
ATOM   7552 C  CB    . TYR A 1 1062 ? 117.687 127.933 147.863 1.00 29.55  ? 1062 TYR A CB    1 
ATOM   7553 C  CG    . TYR A 1 1062 ? 116.972 126.603 147.813 1.00 29.55  ? 1062 TYR A CG    1 
ATOM   7554 C  CD1   . TYR A 1 1062 ? 116.169 126.265 146.734 1.00 29.55  ? 1062 TYR A CD1   1 
ATOM   7555 C  CD2   . TYR A 1 1062 ? 117.092 125.688 148.849 1.00 29.55  ? 1062 TYR A CD2   1 
ATOM   7556 C  CE1   . TYR A 1 1062 ? 115.510 125.053 146.686 1.00 29.55  ? 1062 TYR A CE1   1 
ATOM   7557 C  CE2   . TYR A 1 1062 ? 116.438 124.474 148.809 1.00 29.55  ? 1062 TYR A CE2   1 
ATOM   7558 C  CZ    . TYR A 1 1062 ? 115.649 124.162 147.726 1.00 29.55  ? 1062 TYR A CZ    1 
ATOM   7559 O  OH    . TYR A 1 1062 ? 114.995 122.953 147.682 1.00 29.55  ? 1062 TYR A OH    1 
ATOM   7560 N  N     . ASP A 1 1063 ? 119.215 130.360 147.284 1.00 34.67  ? 1063 ASP A N     1 
ATOM   7561 C  CA    . ASP A 1 1063 ? 119.846 131.642 147.533 1.00 34.67  ? 1063 ASP A CA    1 
ATOM   7562 C  C     . ASP A 1 1063 ? 119.054 132.426 148.570 1.00 34.67  ? 1063 ASP A C     1 
ATOM   7563 O  O     . ASP A 1 1063 ? 117.837 132.596 148.412 1.00 34.67  ? 1063 ASP A O     1 
ATOM   7564 C  CB    . ASP A 1 1063 ? 119.954 132.461 146.238 1.00 34.67  ? 1063 ASP A CB    1 
ATOM   7565 C  CG    . ASP A 1 1063 ? 121.147 132.064 145.394 1.00 34.67  ? 1063 ASP A CG    1 
ATOM   7566 O  OD1   . ASP A 1 1063 ? 122.127 131.535 145.959 1.00 34.67  ? 1063 ASP A OD1   1 
ATOM   7567 O  OD2   . ASP A 1 1063 ? 121.107 132.288 144.166 1.00 34.67  ? 1063 ASP A OD2   1 
ATOM   7568 N  N     . PRO A 1 1064 ? 119.691 132.907 149.637 1.00 31.62  ? 1064 PRO A N     1 
ATOM   7569 C  CA    . PRO A 1 1064 ? 118.983 133.769 150.590 1.00 31.62  ? 1064 PRO A CA    1 
ATOM   7570 C  C     . PRO A 1 1064 ? 118.494 135.043 149.918 1.00 31.62  ? 1064 PRO A C     1 
ATOM   7571 O  O     . PRO A 1 1064 ? 119.169 135.612 149.058 1.00 31.62  ? 1064 PRO A O     1 
ATOM   7572 C  CB    . PRO A 1 1064 ? 120.042 134.066 151.657 1.00 31.62  ? 1064 PRO A CB    1 
ATOM   7573 C  CG    . PRO A 1 1064 ? 121.058 132.985 151.505 1.00 31.62  ? 1064 PRO A CG    1 
ATOM   7574 C  CD    . PRO A 1 1064 ? 121.078 132.645 150.051 1.00 31.62  ? 1064 PRO A CD    1 
ATOM   7575 N  N     . LEU A 1 1065 ? 117.302 135.489 150.319 1.00 31.90  ? 1065 LEU A N     1 
ATOM   7576 C  CA    . LEU A 1 1065 ? 116.729 136.697 149.737 1.00 31.90  ? 1065 LEU A CA    1 
ATOM   7577 C  C     . LEU A 1 1065 ? 117.375 137.961 150.287 1.00 31.90  ? 1065 LEU A C     1 
ATOM   7578 O  O     . LEU A 1 1065 ? 117.386 138.992 149.606 1.00 31.90  ? 1065 LEU A O     1 
ATOM   7579 C  CB    . LEU A 1 1065 ? 115.219 136.731 149.972 1.00 31.90  ? 1065 LEU A CB    1 
ATOM   7580 C  CG    . LEU A 1 1065 ? 114.389 135.672 149.244 1.00 31.90  ? 1065 LEU A CG    1 
ATOM   7581 C  CD1   . LEU A 1 1065 ? 112.961 136.155 149.057 1.00 31.90  ? 1065 LEU A CD1   1 
ATOM   7582 C  CD2   . LEU A 1 1065 ? 115.011 135.307 147.905 1.00 31.90  ? 1065 LEU A CD2   1 
ATOM   7583 N  N     . ALA A 1 1066 ? 117.910 137.906 151.503 1.00 33.61  ? 1066 ALA A N     1 
ATOM   7584 C  CA    . ALA A 1 1066 ? 118.554 139.053 152.122 1.00 33.61  ? 1066 ALA A CA    1 
ATOM   7585 C  C     . ALA A 1 1066 ? 119.682 138.562 153.016 1.00 33.61  ? 1066 ALA A C     1 
ATOM   7586 O  O     . ALA A 1 1066 ? 119.763 137.380 153.358 1.00 33.61  ? 1066 ALA A O     1 
ATOM   7587 C  CB    . ALA A 1 1066 ? 117.556 139.898 152.922 1.00 33.61  ? 1066 ALA A CB    1 
ATOM   7588 N  N     . GLY A 1 1067 ? 120.562 139.485 153.389 1.00 36.94  ? 1067 GLY A N     1 
ATOM   7589 C  CA    . GLY A 1 1067 ? 121.678 139.107 154.227 1.00 36.94  ? 1067 GLY A CA    1 
ATOM   7590 C  C     . GLY A 1 1067 ? 122.693 138.267 153.467 1.00 36.94  ? 1067 GLY A C     1 
ATOM   7591 O  O     . GLY A 1 1067 ? 122.708 138.208 152.235 1.00 36.94  ? 1067 GLY A O     1 
ATOM   7592 N  N     . LYS A 1 1068 ? 123.553 137.602 154.233 1.00 42.98  ? 1068 LYS A N     1 
ATOM   7593 C  CA    . LYS A 1 1068 ? 124.599 136.777 153.648 1.00 42.98  ? 1068 LYS A CA    1 
ATOM   7594 C  C     . LYS A 1 1068 ? 125.022 135.723 154.658 1.00 42.98  ? 1068 LYS A C     1 
ATOM   7595 O  O     . LYS A 1 1068 ? 124.796 135.862 155.862 1.00 42.98  ? 1068 LYS A O     1 
ATOM   7596 C  CB    . LYS A 1 1068 ? 125.800 137.623 153.214 1.00 42.98  ? 1068 LYS A CB    1 
ATOM   7597 C  CG    . LYS A 1 1068 ? 126.413 138.441 154.336 1.00 42.98  ? 1068 LYS A CG    1 
ATOM   7598 C  CD    . LYS A 1 1068 ? 127.618 139.228 153.851 1.00 42.98  ? 1068 LYS A CD    1 
ATOM   7599 C  CE    . LYS A 1 1068 ? 127.201 140.364 152.933 1.00 42.98  ? 1068 LYS A CE    1 
ATOM   7600 N  NZ    . LYS A 1 1068 ? 126.240 141.286 153.598 1.00 42.98  ? 1068 LYS A NZ    1 
ATOM   7601 N  N     . VAL A 1 1069 ? 125.641 134.662 154.144 1.00 41.39  ? 1069 VAL A N     1 
ATOM   7602 C  CA    . VAL A 1 1069 ? 126.150 133.563 154.955 1.00 41.39  ? 1069 VAL A CA    1 
ATOM   7603 C  C     . VAL A 1 1069 ? 127.613 133.339 154.594 1.00 41.39  ? 1069 VAL A C     1 
ATOM   7604 O  O     . VAL A 1 1069 ? 127.978 133.359 153.414 1.00 41.39  ? 1069 VAL A O     1 
ATOM   7605 C  CB    . VAL A 1 1069 ? 125.318 132.278 154.762 1.00 41.39  ? 1069 VAL A CB    1 
ATOM   7606 C  CG1   . VAL A 1 1069 ? 125.408 131.770 153.332 1.00 41.39  ? 1069 VAL A CG1   1 
ATOM   7607 C  CG2   . VAL A 1 1069 ? 125.770 131.203 155.734 1.00 41.39  ? 1069 VAL A CG2   1 
ATOM   7608 N  N     . MET A 1 1070 ? 128.454 133.163 155.610 1.00 48.60  ? 1070 MET A N     1 
ATOM   7609 C  CA    . MET A 1 1070 ? 129.887 132.995 155.420 1.00 48.60  ? 1070 MET A CA    1 
ATOM   7610 C  C     . MET A 1 1070 ? 130.363 131.739 156.132 1.00 48.60  ? 1070 MET A C     1 
ATOM   7611 O  O     . MET A 1 1070 ? 129.870 131.403 157.214 1.00 48.60  ? 1070 MET A O     1 
ATOM   7612 C  CB    . MET A 1 1070 ? 130.662 134.208 155.940 1.00 48.60  ? 1070 MET A CB    1 
ATOM   7613 C  CG    . MET A 1 1070 ? 130.452 135.468 155.125 1.00 48.60  ? 1070 MET A CG    1 
ATOM   7614 S  SD    . MET A 1 1070 ? 128.989 136.377 155.641 1.00 48.60  ? 1070 MET A SD    1 
ATOM   7615 C  CE    . MET A 1 1070 ? 129.605 137.169 157.122 1.00 48.60  ? 1070 MET A CE    1 
ATOM   7616 N  N     . ILE A 1 1071 ? 131.322 131.049 155.522 1.00 48.52  ? 1071 ILE A N     1 
ATOM   7617 C  CA    . ILE A 1 1071 ? 131.898 129.830 156.073 1.00 48.52  ? 1071 ILE A CA    1 
ATOM   7618 C  C     . ILE A 1 1071 ? 133.307 130.068 156.605 1.00 48.52  ? 1071 ILE A C     1 
ATOM   7619 O  O     . ILE A 1 1071 ? 133.635 129.664 157.721 1.00 48.52  ? 1071 ILE A O     1 
ATOM   7620 C  CB    . ILE A 1 1071 ? 131.879 128.689 155.031 1.00 48.52  ? 1071 ILE A CB    1 
ATOM   7621 C  CG1   . ILE A 1 1071 ? 130.506 128.017 155.017 1.00 48.52  ? 1071 ILE A CG1   1 
ATOM   7622 C  CG2   . ILE A 1 1071 ? 132.964 127.667 155.324 1.00 48.52  ? 1071 ILE A CG2   1 
ATOM   7623 C  CD1   . ILE A 1 1071 ? 130.385 126.897 154.015 1.00 48.52  ? 1071 ILE A CD1   1 
ATOM   7624 N  N     . ASP A 1 1072 ? 134.152 130.730 155.822 1.00 53.44  ? 1072 ASP A N     1 
ATOM   7625 C  CA    . ASP A 1 1072 ? 135.528 131.012 156.209 1.00 53.44  ? 1072 ASP A CA    1 
ATOM   7626 C  C     . ASP A 1 1072 ? 135.781 132.512 156.269 1.00 53.44  ? 1072 ASP A C     1 
ATOM   7627 O  O     . ASP A 1 1072 ? 136.840 133.000 155.868 1.00 53.44  ? 1072 ASP A O     1 
ATOM   7628 C  CB    . ASP A 1 1072 ? 136.511 130.340 155.254 1.00 53.44  ? 1072 ASP A CB    1 
ATOM   7629 C  CG    . ASP A 1 1072 ? 136.361 128.834 155.229 1.00 53.44  ? 1072 ASP A CG    1 
ATOM   7630 O  OD1   . ASP A 1 1072 ? 136.055 128.250 156.289 1.00 53.44  ? 1072 ASP A OD1   1 
ATOM   7631 O  OD2   . ASP A 1 1072 ? 136.552 128.234 154.151 1.00 53.44  ? 1072 ASP A OD2   1 
ATOM   7632 N  N     . GLY A 1 1073 ? 134.808 133.264 156.775 1.00 49.12  ? 1073 GLY A N     1 
ATOM   7633 C  CA    . GLY A 1 1073 ? 134.916 134.704 156.826 1.00 49.12  ? 1073 GLY A CA    1 
ATOM   7634 C  C     . GLY A 1 1073 ? 134.622 135.412 155.523 1.00 49.12  ? 1073 GLY A C     1 
ATOM   7635 O  O     . GLY A 1 1073 ? 134.749 136.641 155.463 1.00 49.12  ? 1073 GLY A O     1 
ATOM   7636 N  N     . LYS A 1 1074 ? 134.238 134.680 154.480 1.00 46.07  ? 1074 LYS A N     1 
ATOM   7637 C  CA    . LYS A 1 1074 ? 133.907 135.257 153.187 1.00 46.07  ? 1074 LYS A CA    1 
ATOM   7638 C  C     . LYS A 1 1074 ? 132.616 134.633 152.679 1.00 46.07  ? 1074 LYS A C     1 
ATOM   7639 O  O     . LYS A 1 1074 ? 132.278 133.500 153.031 1.00 46.07  ? 1074 LYS A O     1 
ATOM   7640 C  CB    . LYS A 1 1074 ? 135.034 135.038 152.169 1.00 46.07  ? 1074 LYS A CB    1 
ATOM   7641 C  CG    . LYS A 1 1074 ? 135.056 136.051 151.037 1.00 46.07  ? 1074 LYS A CG    1 
ATOM   7642 C  CD    . LYS A 1 1074 ? 135.963 137.227 151.365 1.00 46.07  ? 1074 LYS A CD    1 
ATOM   7643 C  CE    . LYS A 1 1074 ? 135.782 138.360 150.369 1.00 46.07  ? 1074 LYS A CE    1 
ATOM   7644 N  NZ    . LYS A 1 1074 ? 136.863 139.378 150.486 1.00 46.07  ? 1074 LYS A NZ    1 
ATOM   7645 N  N     . ASP A 1 1075 ? 131.893 135.390 151.858 1.00 43.05  ? 1075 ASP A N     1 
ATOM   7646 C  CA    . ASP A 1 1075 ? 130.630 134.910 151.314 1.00 43.05  ? 1075 ASP A CA    1 
ATOM   7647 C  C     . ASP A 1 1075 ? 130.853 133.660 150.473 1.00 43.05  ? 1075 ASP A C     1 
ATOM   7648 O  O     . ASP A 1 1075 ? 131.788 133.594 149.672 1.00 43.05  ? 1075 ASP A O     1 
ATOM   7649 C  CB    . ASP A 1 1075 ? 129.970 136.004 150.474 1.00 43.05  ? 1075 ASP A CB    1 
ATOM   7650 C  CG    . ASP A 1 1075 ? 128.611 135.593 149.936 1.00 43.05  ? 1075 ASP A CG    1 
ATOM   7651 O  OD1   . ASP A 1 1075 ? 128.073 134.556 150.380 1.00 43.05  ? 1075 ASP A OD1   1 
ATOM   7652 O  OD2   . ASP A 1 1075 ? 128.076 136.312 149.066 1.00 43.05  ? 1075 ASP A OD2   1 
ATOM   7653 N  N     . ILE A 1 1076 ? 129.984 132.661 150.661 1.00 40.39  ? 1076 ILE A N     1 
ATOM   7654 C  CA    . ILE A 1 1076 ? 130.087 131.422 149.893 1.00 40.39  ? 1076 ILE A CA    1 
ATOM   7655 C  C     . ILE A 1 1076 ? 129.475 131.540 148.509 1.00 40.39  ? 1076 ILE A C     1 
ATOM   7656 O  O     . ILE A 1 1076 ? 129.499 130.564 147.748 1.00 40.39  ? 1076 ILE A O     1 
ATOM   7657 C  CB    . ILE A 1 1076 ? 129.430 130.247 150.643 1.00 40.39  ? 1076 ILE A CB    1 
ATOM   7658 C  CG1   . ILE A 1 1076 ? 127.938 130.503 150.846 1.00 40.39  ? 1076 ILE A CG1   1 
ATOM   7659 C  CG2   . ILE A 1 1076 ? 130.116 130.023 151.976 1.00 40.39  ? 1076 ILE A CG2   1 
ATOM   7660 C  CD1   . ILE A 1 1076 ? 127.188 129.298 151.364 1.00 40.39  ? 1076 ILE A CD1   1 
ATOM   7661 N  N     . ARG A 1 1077 ? 128.919 132.701 148.159 1.00 40.21  ? 1077 ARG A N     1 
ATOM   7662 C  CA    . ARG A 1 1077 ? 128.432 132.900 146.800 1.00 40.21  ? 1077 ARG A CA    1 
ATOM   7663 C  C     . ARG A 1 1077 ? 129.579 133.117 145.822 1.00 40.21  ? 1077 ARG A C     1 
ATOM   7664 O  O     . ARG A 1 1077 ? 129.440 132.819 144.631 1.00 40.21  ? 1077 ARG A O     1 
ATOM   7665 C  CB    . ARG A 1 1077 ? 127.464 134.082 146.754 1.00 40.21  ? 1077 ARG A CB    1 
ATOM   7666 C  CG    . ARG A 1 1077 ? 126.037 133.728 147.130 1.00 40.21  ? 1077 ARG A CG    1 
ATOM   7667 C  CD    . ARG A 1 1077 ? 125.081 134.861 146.797 1.00 40.21  ? 1077 ARG A CD    1 
ATOM   7668 N  NE    . ARG A 1 1077 ? 125.338 136.049 147.605 1.00 40.21  ? 1077 ARG A NE    1 
ATOM   7669 C  CZ    . ARG A 1 1077 ? 124.946 136.198 148.866 1.00 40.21  ? 1077 ARG A CZ    1 
ATOM   7670 N  NH1   . ARG A 1 1077 ? 125.226 137.315 149.522 1.00 40.21  ? 1077 ARG A NH1   1 
ATOM   7671 N  NH2   . ARG A 1 1077 ? 124.273 135.230 149.473 1.00 40.21  ? 1077 ARG A NH2   1 
ATOM   7672 N  N     . ARG A 1 1078 ? 130.712 133.632 146.301 1.00 45.14  ? 1078 ARG A N     1 
ATOM   7673 C  CA    . ARG A 1 1078 ? 131.856 133.894 145.439 1.00 45.14  ? 1078 ARG A CA    1 
ATOM   7674 C  C     . ARG A 1 1078 ? 132.869 132.759 145.421 1.00 45.14  ? 1078 ARG A C     1 
ATOM   7675 O  O     . ARG A 1 1078 ? 133.705 132.712 144.513 1.00 45.14  ? 1078 ARG A O     1 
ATOM   7676 C  CB    . ARG A 1 1078 ? 132.554 135.189 145.864 1.00 45.14  ? 1078 ARG A CB    1 
ATOM   7677 C  CG    . ARG A 1 1078 ? 133.240 135.114 147.214 1.00 45.14  ? 1078 ARG A CG    1 
ATOM   7678 C  CD    . ARG A 1 1078 ? 134.014 136.388 147.498 1.00 45.14  ? 1078 ARG A CD    1 
ATOM   7679 N  NE    . ARG A 1 1078 ? 133.374 137.553 146.895 1.00 45.14  ? 1078 ARG A NE    1 
ATOM   7680 C  CZ    . ARG A 1 1078 ? 132.465 138.305 147.506 1.00 45.14  ? 1078 ARG A CZ    1 
ATOM   7681 N  NH1   . ARG A 1 1078 ? 131.933 139.345 146.881 1.00 45.14  ? 1078 ARG A NH1   1 
ATOM   7682 N  NH2   . ARG A 1 1078 ? 132.087 138.017 148.744 1.00 45.14  ? 1078 ARG A NH2   1 
ATOM   7683 N  N     . LEU A 1 1079 ? 132.830 131.858 146.399 1.00 42.78  ? 1079 LEU A N     1 
ATOM   7684 C  CA    . LEU A 1 1079 ? 133.709 130.697 146.390 1.00 42.78  ? 1079 LEU A CA    1 
ATOM   7685 C  C     . LEU A 1 1079 ? 133.134 129.613 145.490 1.00 42.78  ? 1079 LEU A C     1 
ATOM   7686 O  O     . LEU A 1 1079 ? 131.923 129.376 145.476 1.00 42.78  ? 1079 LEU A O     1 
ATOM   7687 C  CB    . LEU A 1 1079 ? 133.900 130.154 147.806 1.00 42.78  ? 1079 LEU A CB    1 
ATOM   7688 C  CG    . LEU A 1 1079 ? 134.317 131.153 148.887 1.00 42.78  ? 1079 LEU A CG    1 
ATOM   7689 C  CD1   . LEU A 1 1079 ? 134.566 130.438 150.204 1.00 42.78  ? 1079 LEU A CD1   1 
ATOM   7690 C  CD2   . LEU A 1 1079 ? 135.549 131.931 148.458 1.00 42.78  ? 1079 LEU A CD2   1 
ATOM   7691 N  N     . ASN A 1 1080 ? 134.009 128.957 144.730 1.00 43.91  ? 1080 ASN A N     1 
ATOM   7692 C  CA    . ASN A 1 1080 ? 133.561 127.890 143.846 1.00 43.91  ? 1080 ASN A CA    1 
ATOM   7693 C  C     . ASN A 1 1080 ? 133.002 126.732 144.661 1.00 43.91  ? 1080 ASN A C     1 
ATOM   7694 O  O     . ASN A 1 1080 ? 133.531 126.380 145.718 1.00 43.91  ? 1080 ASN A O     1 
ATOM   7695 C  CB    . ASN A 1 1080 ? 134.709 127.410 142.960 1.00 43.91  ? 1080 ASN A CB    1 
ATOM   7696 C  CG    . ASN A 1 1080 ? 135.979 127.160 143.739 1.00 43.91  ? 1080 ASN A CG    1 
ATOM   7697 O  OD1   . ASN A 1 1080 ? 136.068 127.483 144.922 1.00 43.91  ? 1080 ASN A OD1   1 
ATOM   7698 N  ND2   . ASN A 1 1080 ? 136.973 126.579 143.078 1.00 43.91  ? 1080 ASN A ND2   1 
ATOM   7699 N  N     . LEU A 1 1081 ? 131.918 126.138 144.160 1.00 37.52  ? 1081 LEU A N     1 
ATOM   7700 C  CA    . LEU A 1 1081 ? 131.193 125.140 144.936 1.00 37.52  ? 1081 LEU A CA    1 
ATOM   7701 C  C     . LEU A 1 1081 ? 131.917 123.805 145.005 1.00 37.52  ? 1081 LEU A C     1 
ATOM   7702 O  O     . LEU A 1 1081 ? 131.720 123.057 145.967 1.00 37.52  ? 1081 LEU A O     1 
ATOM   7703 C  CB    . LEU A 1 1081 ? 129.798 124.932 144.355 1.00 37.52  ? 1081 LEU A CB    1 
ATOM   7704 C  CG    . LEU A 1 1081 ? 128.944 126.188 144.233 1.00 37.52  ? 1081 LEU A CG    1 
ATOM   7705 C  CD1   . LEU A 1 1081 ? 127.658 125.865 143.508 1.00 37.52  ? 1081 LEU A CD1   1 
ATOM   7706 C  CD2   . LEU A 1 1081 ? 128.664 126.759 145.608 1.00 37.52  ? 1081 LEU A CD2   1 
ATOM   7707 N  N     . LYS A 1 1082 ? 132.737 123.474 144.006 1.00 34.23  ? 1082 LYS A N     1 
ATOM   7708 C  CA    . LYS A 1 1082 ? 133.368 122.158 143.985 1.00 34.23  ? 1082 LYS A CA    1 
ATOM   7709 C  C     . LYS A 1 1082 ? 134.288 121.969 145.185 1.00 34.23  ? 1082 LYS A C     1 
ATOM   7710 O  O     . LYS A 1 1082 ? 134.206 120.956 145.890 1.00 34.23  ? 1082 LYS A O     1 
ATOM   7711 C  CB    . LYS A 1 1082 ? 134.133 121.966 142.676 1.00 34.23  ? 1082 LYS A CB    1 
ATOM   7712 C  CG    . LYS A 1 1082 ? 133.238 121.869 141.454 1.00 34.23  ? 1082 LYS A CG    1 
ATOM   7713 C  CD    . LYS A 1 1082 ? 132.054 120.952 141.710 1.00 34.23  ? 1082 LYS A CD    1 
ATOM   7714 C  CE    . LYS A 1 1082 ? 131.341 120.596 140.418 1.00 34.23  ? 1082 LYS A CE    1 
ATOM   7715 N  NZ    . LYS A 1 1082 ? 132.298 120.210 139.345 1.00 34.23  ? 1082 LYS A NZ    1 
ATOM   7716 N  N     . SER A 1 1083 ? 135.159 122.946 145.446 1.00 35.31  ? 1083 SER A N     1 
ATOM   7717 C  CA    . SER A 1 1083 ? 136.070 122.837 146.581 1.00 35.31  ? 1083 SER A CA    1 
ATOM   7718 C  C     . SER A 1 1083 ? 135.310 122.802 147.901 1.00 35.31  ? 1083 SER A C     1 
ATOM   7719 O  O     . SER A 1 1083 ? 135.623 121.995 148.786 1.00 35.31  ? 1083 SER A O     1 
ATOM   7720 C  CB    . SER A 1 1083 ? 137.064 123.997 146.568 1.00 35.31  ? 1083 SER A CB    1 
ATOM   7721 O  OG    . SER A 1 1083 ? 138.128 123.746 145.668 1.00 35.31  ? 1083 SER A OG    1 
ATOM   7722 N  N     . LEU A 1 1084 ? 134.304 123.665 148.049 1.00 34.52  ? 1084 LEU A N     1 
ATOM   7723 C  CA    . LEU A 1 1084 ? 133.555 123.723 149.300 1.00 34.52  ? 1084 LEU A CA    1 
ATOM   7724 C  C     . LEU A 1 1084 ? 132.821 122.414 149.563 1.00 34.52  ? 1084 LEU A C     1 
ATOM   7725 O  O     . LEU A 1 1084 ? 132.842 121.892 150.683 1.00 34.52  ? 1084 LEU A O     1 
ATOM   7726 C  CB    . LEU A 1 1084 ? 132.575 124.894 149.268 1.00 34.52  ? 1084 LEU A CB    1 
ATOM   7727 C  CG    . LEU A 1 1084 ? 132.096 125.392 150.630 1.00 34.52  ? 1084 LEU A CG    1 
ATOM   7728 C  CD1   . LEU A 1 1084 ? 133.222 126.098 151.364 1.00 34.52  ? 1084 LEU A CD1   1 
ATOM   7729 C  CD2   . LEU A 1 1084 ? 130.899 126.310 150.463 1.00 34.52  ? 1084 LEU A CD2   1 
ATOM   7730 N  N     . ARG A 1 1085 ? 132.170 121.865 148.537 1.00 28.38  ? 1085 ARG A N     1 
ATOM   7731 C  CA    . ARG A 1 1085 ? 131.458 120.605 148.695 1.00 28.38  ? 1085 ARG A CA    1 
ATOM   7732 C  C     . ARG A 1 1085 ? 132.406 119.425 148.849 1.00 28.38  ? 1085 ARG A C     1 
ATOM   7733 O  O     . ARG A 1 1085 ? 132.002 118.390 149.388 1.00 28.38  ? 1085 ARG A O     1 
ATOM   7734 C  CB    . ARG A 1 1085 ? 130.521 120.379 147.508 1.00 28.38  ? 1085 ARG A CB    1 
ATOM   7735 C  CG    . ARG A 1 1085 ? 129.392 121.393 147.421 1.00 28.38  ? 1085 ARG A CG    1 
ATOM   7736 C  CD    . ARG A 1 1085 ? 128.139 120.781 146.827 1.00 28.38  ? 1085 ARG A CD    1 
ATOM   7737 N  NE    . ARG A 1 1085 ? 127.202 121.796 146.355 1.00 28.38  ? 1085 ARG A NE    1 
ATOM   7738 C  CZ    . ARG A 1 1085 ? 126.822 121.927 145.089 1.00 28.38  ? 1085 ARG A CZ    1 
ATOM   7739 N  NH1   . ARG A 1 1085 ? 125.965 122.878 144.745 1.00 28.38  ? 1085 ARG A NH1   1 
ATOM   7740 N  NH2   . ARG A 1 1085 ? 127.296 121.104 144.165 1.00 28.38  ? 1085 ARG A NH2   1 
ATOM   7741 N  N     . LEU A 1 1086 ? 133.650 119.549 148.383 1.00 31.92  ? 1086 LEU A N     1 
ATOM   7742 C  CA    . LEU A 1 1086 ? 134.637 118.513 148.662 1.00 31.92  ? 1086 LEU A CA    1 
ATOM   7743 C  C     . LEU A 1 1086 ? 135.112 118.582 150.107 1.00 31.92  ? 1086 LEU A C     1 
ATOM   7744 O  O     . LEU A 1 1086 ? 135.396 117.548 150.723 1.00 31.92  ? 1086 LEU A O     1 
ATOM   7745 C  CB    . LEU A 1 1086 ? 135.816 118.636 147.699 1.00 31.92  ? 1086 LEU A CB    1 
ATOM   7746 C  CG    . LEU A 1 1086 ? 135.707 117.825 146.409 1.00 31.92  ? 1086 LEU A CG    1 
ATOM   7747 C  CD1   . LEU A 1 1086 ? 136.938 118.024 145.545 1.00 31.92  ? 1086 LEU A CD1   1 
ATOM   7748 C  CD2   . LEU A 1 1086 ? 135.514 116.355 146.732 1.00 31.92  ? 1086 LEU A CD2   1 
ATOM   7749 N  N     . LYS A 1 1087 ? 135.206 119.790 150.665 1.00 37.64  ? 1087 LYS A N     1 
ATOM   7750 C  CA    . LYS A 1 1087 ? 135.671 119.942 152.038 1.00 37.64  ? 1087 LYS A CA    1 
ATOM   7751 C  C     . LYS A 1 1087 ? 134.579 119.691 153.069 1.00 37.64  ? 1087 LYS A C     1 
ATOM   7752 O  O     . LYS A 1 1087 ? 134.881 119.636 154.265 1.00 37.64  ? 1087 LYS A O     1 
ATOM   7753 C  CB    . LYS A 1 1087 ? 136.255 121.340 152.251 1.00 37.64  ? 1087 LYS A CB    1 
ATOM   7754 C  CG    . LYS A 1 1087 ? 137.451 121.657 151.372 1.00 37.64  ? 1087 LYS A CG    1 
ATOM   7755 C  CD    . LYS A 1 1087 ? 138.566 120.647 151.567 1.00 37.64  ? 1087 LYS A CD    1 
ATOM   7756 C  CE    . LYS A 1 1087 ? 139.717 120.916 150.613 1.00 37.64  ? 1087 LYS A CE    1 
ATOM   7757 N  NZ    . LYS A 1 1087 ? 139.323 120.696 149.194 1.00 37.64  ? 1087 LYS A NZ    1 
ATOM   7758 N  N     . ILE A 1 1088 ? 133.328 119.539 152.643 1.00 37.09  ? 1088 ILE A N     1 
ATOM   7759 C  CA    . ILE A 1 1088 ? 132.208 119.373 153.561 1.00 37.09  ? 1088 ILE A CA    1 
ATOM   7760 C  C     . ILE A 1 1088 ? 131.412 118.141 153.156 1.00 37.09  ? 1088 ILE A C     1 
ATOM   7761 O  O     . ILE A 1 1088 ? 131.439 117.711 151.998 1.00 37.09  ? 1088 ILE A O     1 
ATOM   7762 C  CB    . ILE A 1 1088 ? 131.313 120.632 153.591 1.00 37.09  ? 1088 ILE A CB    1 
ATOM   7763 C  CG1   . ILE A 1 1088 ? 130.541 120.718 154.906 1.00 37.09  ? 1088 ILE A CG1   1 
ATOM   7764 C  CG2   . ILE A 1 1088 ? 130.353 120.643 152.416 1.00 37.09  ? 1088 ILE A CG2   1 
ATOM   7765 C  CD1   . ILE A 1 1088 ? 130.013 122.100 155.203 1.00 37.09  ? 1088 ILE A CD1   1 
ATOM   7766 N  N     . GLY A 1 1089 ? 130.711 117.563 154.121 1.00 40.17  ? 1089 GLY A N     1 
ATOM   7767 C  CA    . GLY A 1 1089 ? 129.921 116.370 153.869 1.00 40.17  ? 1089 GLY A CA    1 
ATOM   7768 C  C     . GLY A 1 1089 ? 128.775 116.268 154.848 1.00 40.17  ? 1089 GLY A C     1 
ATOM   7769 O  O     . GLY A 1 1089 ? 128.869 116.724 155.992 1.00 40.17  ? 1089 GLY A O     1 
ATOM   7770 N  N     . LEU A 1 1090 ? 127.683 115.656 154.395 1.00 40.39  ? 1090 LEU A N     1 
ATOM   7771 C  CA    . LEU A 1 1090 ? 126.482 115.524 155.204 1.00 40.39  ? 1090 LEU A CA    1 
ATOM   7772 C  C     . LEU A 1 1090 ? 125.859 114.155 154.978 1.00 40.39  ? 1090 LEU A C     1 
ATOM   7773 O  O     . LEU A 1 1090 ? 126.226 113.420 154.057 1.00 40.39  ? 1090 LEU A O     1 
ATOM   7774 C  CB    . LEU A 1 1090 ? 125.469 116.639 154.896 1.00 40.39  ? 1090 LEU A CB    1 
ATOM   7775 C  CG    . LEU A 1 1090 ? 124.866 116.794 153.495 1.00 40.39  ? 1090 LEU A CG    1 
ATOM   7776 C  CD1   . LEU A 1 1090 ? 123.675 115.872 153.254 1.00 40.39  ? 1090 LEU A CD1   1 
ATOM   7777 C  CD2   . LEU A 1 1090 ? 124.466 118.242 153.267 1.00 40.39  ? 1090 LEU A CD2   1 
ATOM   7778 N  N     . VAL A 1 1091 ? 124.902 113.822 155.840 1.00 42.58  ? 1091 VAL A N     1 
ATOM   7779 C  CA    . VAL A 1 1091 ? 124.094 112.617 155.714 1.00 42.58  ? 1091 VAL A CA    1 
ATOM   7780 C  C     . VAL A 1 1091 ? 122.628 113.029 155.723 1.00 42.58  ? 1091 VAL A C     1 
ATOM   7781 O  O     . VAL A 1 1091 ? 122.230 113.924 156.476 1.00 42.58  ? 1091 VAL A O     1 
ATOM   7782 C  CB    . VAL A 1 1091 ? 124.401 111.602 156.837 1.00 42.58  ? 1091 VAL A CB    1 
ATOM   7783 C  CG1   . VAL A 1 1091 ? 124.128 112.204 158.202 1.00 42.58  ? 1091 VAL A CG1   1 
ATOM   7784 C  CG2   . VAL A 1 1091 ? 123.594 110.329 156.641 1.00 42.58  ? 1091 VAL A CG2   1 
ATOM   7785 N  N     . GLN A 1 1092 ? 121.834 112.406 154.859 1.00 41.82  ? 1092 GLN A N     1 
ATOM   7786 C  CA    . GLN A 1 1092 ? 120.430 112.760 154.739 1.00 41.82  ? 1092 GLN A CA    1 
ATOM   7787 C  C     . GLN A 1 1092 ? 119.631 112.217 155.921 1.00 41.82  ? 1092 GLN A C     1 
ATOM   7788 O  O     . GLN A 1 1092 ? 120.030 111.261 156.590 1.00 41.82  ? 1092 GLN A O     1 
ATOM   7789 C  CB    . GLN A 1 1092 ? 119.854 112.226 153.428 1.00 41.82  ? 1092 GLN A CB    1 
ATOM   7790 C  CG    . GLN A 1 1092 ? 120.511 112.800 152.185 1.00 41.82  ? 1092 GLN A CG    1 
ATOM   7791 C  CD    . GLN A 1 1092 ? 119.643 113.825 151.488 1.00 41.82  ? 1092 GLN A CD    1 
ATOM   7792 O  OE1   . GLN A 1 1092 ? 118.557 113.508 151.002 1.00 41.82  ? 1092 GLN A OE1   1 
ATOM   7793 N  NE2   . GLN A 1 1092 ? 120.116 115.064 151.434 1.00 41.82  ? 1092 GLN A NE2   1 
ATOM   7794 N  N     . GLN A 1 1093 ? 118.484 112.854 156.179 1.00 42.04  ? 1093 GLN A N     1 
ATOM   7795 C  CA    . GLN A 1 1093 ? 117.585 112.359 157.217 1.00 42.04  ? 1093 GLN A CA    1 
ATOM   7796 C  C     . GLN A 1 1093 ? 116.938 111.041 156.813 1.00 42.04  ? 1093 GLN A C     1 
ATOM   7797 O  O     . GLN A 1 1093 ? 116.656 110.200 157.673 1.00 42.04  ? 1093 GLN A O     1 
ATOM   7798 C  CB    . GLN A 1 1093 ? 116.513 113.402 157.536 1.00 42.04  ? 1093 GLN A CB    1 
ATOM   7799 C  CG    . GLN A 1 1093 ? 115.570 113.710 156.384 1.00 42.04  ? 1093 GLN A CG    1 
ATOM   7800 C  CD    . GLN A 1 1093 ? 114.380 114.548 156.811 1.00 42.04  ? 1093 GLN A CD    1 
ATOM   7801 O  OE1   . GLN A 1 1093 ? 114.161 114.777 158.000 1.00 42.04  ? 1093 GLN A OE1   1 
ATOM   7802 N  NE2   . GLN A 1 1093 ? 113.605 115.012 155.838 1.00 42.04  ? 1093 GLN A NE2   1 
ATOM   7803 N  N     . GLU A 1 1094 ? 116.694 110.846 155.518 1.00 41.97  ? 1094 GLU A N     1 
ATOM   7804 C  CA    . GLU A 1 1094 ? 116.128 109.609 154.985 1.00 41.97  ? 1094 GLU A CA    1 
ATOM   7805 C  C     . GLU A 1 1094 ? 117.062 109.124 153.887 1.00 41.97  ? 1094 GLU A C     1 
ATOM   7806 O  O     . GLU A 1 1094 ? 116.881 109.460 152.709 1.00 41.97  ? 1094 GLU A O     1 
ATOM   7807 C  CB    . GLU A 1 1094 ? 114.711 109.825 154.461 1.00 41.97  ? 1094 GLU A CB    1 
ATOM   7808 C  CG    . GLU A 1 1094 ? 113.634 109.687 155.521 1.00 41.97  ? 1094 GLU A CG    1 
ATOM   7809 C  CD    . GLU A 1 1094 ? 112.302 109.260 154.941 1.00 41.97  ? 1094 GLU A CD    1 
ATOM   7810 O  OE1   . GLU A 1 1094 ? 112.141 108.058 154.649 1.00 41.97  ? 1094 GLU A OE1   1 
ATOM   7811 O  OE2   . GLU A 1 1094 ? 111.416 110.125 154.780 1.00 41.97  ? 1094 GLU A OE2   1 
ATOM   7812 N  N     . PRO A 1 1095 ? 118.084 108.344 154.240 1.00 34.27  ? 1095 PRO A N     1 
ATOM   7813 C  CA    . PRO A 1 1095 ? 119.089 107.949 153.247 1.00 34.27  ? 1095 PRO A CA    1 
ATOM   7814 C  C     . PRO A 1 1095 ? 118.475 107.154 152.105 1.00 34.27  ? 1095 PRO A C     1 
ATOM   7815 O  O     . PRO A 1 1095 ? 117.550 106.363 152.298 1.00 34.27  ? 1095 PRO A O     1 
ATOM   7816 C  CB    . PRO A 1 1095 ? 120.074 107.099 154.058 1.00 34.27  ? 1095 PRO A CB    1 
ATOM   7817 C  CG    . PRO A 1 1095 ? 119.846 107.498 155.481 1.00 34.27  ? 1095 PRO A CG    1 
ATOM   7818 C  CD    . PRO A 1 1095 ? 118.389 107.817 155.578 1.00 34.27  ? 1095 PRO A CD    1 
ATOM   7819 N  N     . ALA A 1 1096 ? 119.004 107.376 150.904 1.00 30.19  ? 1096 ALA A N     1 
ATOM   7820 C  CA    . ALA A 1 1096 ? 118.547 106.701 149.692 1.00 30.19  ? 1096 ALA A CA    1 
ATOM   7821 C  C     . ALA A 1 1096 ? 119.770 106.105 149.004 1.00 30.19  ? 1096 ALA A C     1 
ATOM   7822 O  O     . ALA A 1 1096 ? 120.547 106.824 148.369 1.00 30.19  ? 1096 ALA A O     1 
ATOM   7823 C  CB    . ALA A 1 1096 ? 117.803 107.661 148.772 1.00 30.19  ? 1096 ALA A CB    1 
ATOM   7824 N  N     . LEU A 1 1097 ? 119.938 104.794 149.134 1.00 28.33  ? 1097 LEU A N     1 
ATOM   7825 C  CA    . LEU A 1 1097 ? 121.104 104.118 148.589 1.00 28.33  ? 1097 LEU A CA    1 
ATOM   7826 C  C     . LEU A 1 1097 ? 120.968 103.918 147.084 1.00 28.33  ? 1097 LEU A C     1 
ATOM   7827 O  O     . LEU A 1 1097 ? 119.871 103.724 146.555 1.00 28.33  ? 1097 LEU A O     1 
ATOM   7828 C  CB    . LEU A 1 1097 ? 121.317 102.770 149.278 1.00 28.33  ? 1097 LEU A CB    1 
ATOM   7829 C  CG    . LEU A 1 1097 ? 122.059 102.777 150.618 1.00 28.33  ? 1097 LEU A CG    1 
ATOM   7830 C  CD1   . LEU A 1 1097 ? 123.475 103.268 150.405 1.00 28.33  ? 1097 LEU A CD1   1 
ATOM   7831 C  CD2   . LEU A 1 1097 ? 121.359 103.603 151.686 1.00 28.33  ? 1097 LEU A CD2   1 
ATOM   7832 N  N     . PHE A 1 1098 ? 122.105 103.969 146.396 1.00 27.05  ? 1098 PHE A N     1 
ATOM   7833 C  CA    . PHE A 1 1098 ? 122.126 103.730 144.962 1.00 27.05  ? 1098 PHE A CA    1 
ATOM   7834 C  C     . PHE A 1 1098 ? 121.947 102.246 144.668 1.00 27.05  ? 1098 PHE A C     1 
ATOM   7835 O  O     . PHE A 1 1098 ? 122.265 101.383 145.489 1.00 27.05  ? 1098 PHE A O     1 
ATOM   7836 C  CB    . PHE A 1 1098 ? 123.438 104.228 144.355 1.00 27.05  ? 1098 PHE A CB    1 
ATOM   7837 C  CG    . PHE A 1 1098 ? 123.555 105.723 144.307 1.00 27.05  ? 1098 PHE A CG    1 
ATOM   7838 C  CD1   . PHE A 1 1098 ? 123.938 106.438 145.427 1.00 27.05  ? 1098 PHE A CD1   1 
ATOM   7839 C  CD2   . PHE A 1 1098 ? 123.281 106.414 143.140 1.00 27.05  ? 1098 PHE A CD2   1 
ATOM   7840 C  CE1   . PHE A 1 1098 ? 124.045 107.812 145.385 1.00 27.05  ? 1098 PHE A CE1   1 
ATOM   7841 C  CE2   . PHE A 1 1098 ? 123.387 107.789 143.091 1.00 27.05  ? 1098 PHE A CE2   1 
ATOM   7842 C  CZ    . PHE A 1 1098 ? 123.769 108.489 144.215 1.00 27.05  ? 1098 PHE A CZ    1 
ATOM   7843 N  N     . ALA A 1 1099 ? 121.433 101.951 143.473 1.00 29.40  ? 1099 ALA A N     1 
ATOM   7844 C  CA    . ALA A 1 1099 ? 121.176 100.573 143.055 1.00 29.40  ? 1099 ALA A CA    1 
ATOM   7845 C  C     . ALA A 1 1099 ? 122.495 99.930  142.639 1.00 29.40  ? 1099 ALA A C     1 
ATOM   7846 O  O     . ALA A 1 1099 ? 122.819 99.789  141.457 1.00 29.40  ? 1099 ALA A O     1 
ATOM   7847 C  CB    . ALA A 1 1099 ? 120.152 100.535 141.929 1.00 29.40  ? 1099 ALA A CB    1 
ATOM   7848 N  N     . ALA A 1 1100 ? 123.268 99.525  143.641 1.00 31.10  ? 1100 ALA A N     1 
ATOM   7849 C  CA    . ALA A 1 1100 ? 124.558 98.882  143.421 1.00 31.10  ? 1100 ALA A CA    1 
ATOM   7850 C  C     . ALA A 1 1100 ? 124.905 98.073  144.666 1.00 31.10  ? 1100 ALA A C     1 
ATOM   7851 O  O     . ALA A 1 1100 ? 124.064 97.866  145.546 1.00 31.10  ? 1100 ALA A O     1 
ATOM   7852 C  CB    . ALA A 1 1100 ? 125.635 99.918  143.086 1.00 31.10  ? 1100 ALA A CB    1 
ATOM   7853 N  N     . THR A 1 1101 ? 126.151 97.614  144.740 1.00 32.39  ? 1101 THR A N     1 
ATOM   7854 C  CA    . THR A 1 1101 ? 126.601 96.835  145.881 1.00 32.39  ? 1101 THR A CA    1 
ATOM   7855 C  C     . THR A 1 1101 ? 126.821 97.738  147.094 1.00 32.39  ? 1101 THR A C     1 
ATOM   7856 O  O     . THR A 1 1101 ? 126.838 98.968  146.995 1.00 32.39  ? 1101 THR A O     1 
ATOM   7857 C  CB    . THR A 1 1101 ? 127.891 96.091  145.544 1.00 32.39  ? 1101 THR A CB    1 
ATOM   7858 O  OG1   . THR A 1 1101 ? 128.973 97.026  145.472 1.00 32.39  ? 1101 THR A OG1   1 
ATOM   7859 C  CG2   . THR A 1 1101 ? 127.758 95.380  144.209 1.00 32.39  ? 1101 THR A CG2   1 
ATOM   7860 N  N     . ILE A 1 1102 ? 126.984 97.106  148.259 1.00 30.69  ? 1102 ILE A N     1 
ATOM   7861 C  CA    . ILE A 1 1102 ? 127.301 97.862  149.468 1.00 30.69  ? 1102 ILE A CA    1 
ATOM   7862 C  C     . ILE A 1 1102 ? 128.651 98.550  149.323 1.00 30.69  ? 1102 ILE A C     1 
ATOM   7863 O  O     . ILE A 1 1102 ? 128.822 99.707  149.724 1.00 30.69  ? 1102 ILE A O     1 
ATOM   7864 C  CB    . ILE A 1 1102 ? 127.266 96.954  150.713 1.00 30.69  ? 1102 ILE A CB    1 
ATOM   7865 C  CG1   . ILE A 1 1102 ? 125.863 96.395  150.963 1.00 30.69  ? 1102 ILE A CG1   1 
ATOM   7866 C  CG2   . ILE A 1 1102 ? 127.749 97.708  151.938 1.00 30.69  ? 1102 ILE A CG2   1 
ATOM   7867 C  CD1   . ILE A 1 1102 ? 125.586 95.082  150.289 1.00 30.69  ? 1102 ILE A CD1   1 
ATOM   7868 N  N     . PHE A 1 1103 ? 129.632 97.850  148.748 1.00 37.16  ? 1103 PHE A N     1 
ATOM   7869 C  CA    . PHE A 1 1103 ? 130.964 98.428  148.599 1.00 37.16  ? 1103 PHE A CA    1 
ATOM   7870 C  C     . PHE A 1 1103 ? 130.941 99.656  147.698 1.00 37.16  ? 1103 PHE A C     1 
ATOM   7871 O  O     . PHE A 1 1103 ? 131.604 100.658 147.988 1.00 37.16  ? 1103 PHE A O     1 
ATOM   7872 C  CB    . PHE A 1 1103 ? 131.931 97.382  148.051 1.00 37.16  ? 1103 PHE A CB    1 
ATOM   7873 C  CG    . PHE A 1 1103 ? 133.188 97.963  147.477 1.00 37.16  ? 1103 PHE A CG    1 
ATOM   7874 C  CD1   . PHE A 1 1103 ? 134.116 98.583  148.295 1.00 37.16  ? 1103 PHE A CD1   1 
ATOM   7875 C  CD2   . PHE A 1 1103 ? 133.441 97.890  146.119 1.00 37.16  ? 1103 PHE A CD2   1 
ATOM   7876 C  CE1   . PHE A 1 1103 ? 135.273 99.119  147.768 1.00 37.16  ? 1103 PHE A CE1   1 
ATOM   7877 C  CE2   . PHE A 1 1103 ? 134.597 98.425  145.586 1.00 37.16  ? 1103 PHE A CE2   1 
ATOM   7878 C  CZ    . PHE A 1 1103 ? 135.514 99.041  146.413 1.00 37.16  ? 1103 PHE A CZ    1 
ATOM   7879 N  N     . ASP A 1 1104 ? 130.191 99.597  146.596 1.00 32.87  ? 1104 ASP A N     1 
ATOM   7880 C  CA    . ASP A 1 1104 ? 130.096 100.755 145.713 1.00 32.87  ? 1104 ASP A CA    1 
ATOM   7881 C  C     . ASP A 1 1104 ? 129.409 101.924 146.407 1.00 32.87  ? 1104 ASP A C     1 
ATOM   7882 O  O     . ASP A 1 1104 ? 129.827 103.077 146.256 1.00 32.87  ? 1104 ASP A O     1 
ATOM   7883 C  CB    . ASP A 1 1104 ? 129.355 100.384 144.431 1.00 32.87  ? 1104 ASP A CB    1 
ATOM   7884 C  CG    . ASP A 1 1104 ? 129.327 101.519 143.430 1.00 32.87  ? 1104 ASP A CG    1 
ATOM   7885 O  OD1   . ASP A 1 1104 ? 130.228 102.381 143.485 1.00 32.87  ? 1104 ASP A OD1   1 
ATOM   7886 O  OD2   . ASP A 1 1104 ? 128.405 101.553 142.589 1.00 32.87  ? 1104 ASP A OD2   1 
ATOM   7887 N  N     . ASN A 1 1105 ? 128.346 101.646 147.166 1.00 28.35  ? 1105 ASN A N     1 
ATOM   7888 C  CA    . ASN A 1 1105 ? 127.645 102.709 147.877 1.00 28.35  ? 1105 ASN A CA    1 
ATOM   7889 C  C     . ASN A 1 1105 ? 128.542 103.367 148.917 1.00 28.35  ? 1105 ASN A C     1 
ATOM   7890 O  O     . ASN A 1 1105 ? 128.539 104.595 149.061 1.00 28.35  ? 1105 ASN A O     1 
ATOM   7891 C  CB    . ASN A 1 1105 ? 126.383 102.156 148.536 1.00 28.35  ? 1105 ASN A CB    1 
ATOM   7892 C  CG    . ASN A 1 1105 ? 125.237 102.008 147.562 1.00 28.35  ? 1105 ASN A CG    1 
ATOM   7893 O  OD1   . ASN A 1 1105 ? 124.638 102.994 147.138 1.00 28.35  ? 1105 ASN A OD1   1 
ATOM   7894 N  ND2   . ASN A 1 1105 ? 124.922 100.770 147.201 1.00 28.35  ? 1105 ASN A ND2   1 
ATOM   7895 N  N     . ILE A 1 1106 ? 129.309 102.566 149.658 1.00 29.96  ? 1106 ILE A N     1 
ATOM   7896 C  CA    . ILE A 1 1106 ? 130.200 103.125 150.670 1.00 29.96  ? 1106 ILE A CA    1 
ATOM   7897 C  C     . ILE A 1 1106 ? 131.307 103.943 150.017 1.00 29.96  ? 1106 ILE A C     1 
ATOM   7898 O  O     . ILE A 1 1106 ? 131.636 105.044 150.475 1.00 29.96  ? 1106 ILE A O     1 
ATOM   7899 C  CB    . ILE A 1 1106 ? 130.772 102.006 151.558 1.00 29.96  ? 1106 ILE A CB    1 
ATOM   7900 C  CG1   . ILE A 1 1106 ? 129.662 101.368 152.392 1.00 29.96  ? 1106 ILE A CG1   1 
ATOM   7901 C  CG2   . ILE A 1 1106 ? 131.857 102.550 152.468 1.00 29.96  ? 1106 ILE A CG2   1 
ATOM   7902 C  CD1   . ILE A 1 1106 ? 130.137 100.225 153.257 1.00 29.96  ? 1106 ILE A CD1   1 
ATOM   7903 N  N     . ALA A 1 1107 ? 131.887 103.433 148.935 1.00 29.56  ? 1107 ALA A N     1 
ATOM   7904 C  CA    . ALA A 1 1107 ? 133.008 104.088 148.275 1.00 29.56  ? 1107 ALA A CA    1 
ATOM   7905 C  C     . ALA A 1 1107 ? 132.588 105.257 147.391 1.00 29.56  ? 1107 ALA A C     1 
ATOM   7906 O  O     . ALA A 1 1107 ? 133.409 105.734 146.601 1.00 29.56  ? 1107 ALA A O     1 
ATOM   7907 C  CB    . ALA A 1 1107 ? 133.795 103.072 147.444 1.00 29.56  ? 1107 ALA A CB    1 
ATOM   7908 N  N     . TYR A 1 1108 ? 131.340 105.721 147.493 1.00 26.71  ? 1108 TYR A N     1 
ATOM   7909 C  CA    . TYR A 1 1108 ? 130.917 106.868 146.696 1.00 26.71  ? 1108 TYR A CA    1 
ATOM   7910 C  C     . TYR A 1 1108 ? 131.681 108.124 147.091 1.00 26.71  ? 1108 TYR A C     1 
ATOM   7911 O  O     . TYR A 1 1108 ? 132.081 108.913 146.228 1.00 26.71  ? 1108 TYR A O     1 
ATOM   7912 C  CB    . TYR A 1 1108 ? 129.413 107.086 146.843 1.00 26.71  ? 1108 TYR A CB    1 
ATOM   7913 C  CG    . TYR A 1 1108 ? 128.776 107.742 145.641 1.00 26.71  ? 1108 TYR A CG    1 
ATOM   7914 C  CD1   . TYR A 1 1108 ? 128.334 106.983 144.568 1.00 26.71  ? 1108 TYR A CD1   1 
ATOM   7915 C  CD2   . TYR A 1 1108 ? 128.616 109.119 145.578 1.00 26.71  ? 1108 TYR A CD2   1 
ATOM   7916 C  CE1   . TYR A 1 1108 ? 127.751 107.575 143.467 1.00 26.71  ? 1108 TYR A CE1   1 
ATOM   7917 C  CE2   . TYR A 1 1108 ? 128.034 109.720 144.481 1.00 26.71  ? 1108 TYR A CE2   1 
ATOM   7918 C  CZ    . TYR A 1 1108 ? 127.604 108.943 143.428 1.00 26.71  ? 1108 TYR A CZ    1 
ATOM   7919 O  OH    . TYR A 1 1108 ? 127.023 109.532 142.329 1.00 26.71  ? 1108 TYR A OH    1 
ATOM   7920 N  N     . GLY A 1 1109 ? 131.886 108.331 148.389 1.00 28.73  ? 1109 GLY A N     1 
ATOM   7921 C  CA    . GLY A 1 1109 ? 132.688 109.455 148.841 1.00 28.73  ? 1109 GLY A CA    1 
ATOM   7922 C  C     . GLY A 1 1109 ? 134.170 109.115 148.816 1.00 28.73  ? 1109 GLY A C     1 
ATOM   7923 O  O     . GLY A 1 1109 ? 134.580 108.004 149.152 1.00 28.73  ? 1109 GLY A O     1 
ATOM   7924 N  N     . LYS A 1 1110 ? 134.976 110.097 148.408 1.00 33.29  ? 1110 LYS A N     1 
ATOM   7925 C  CA    . LYS A 1 1110 ? 136.429 109.958 148.310 1.00 33.29  ? 1110 LYS A CA    1 
ATOM   7926 C  C     . LYS A 1 1110 ? 136.797 108.793 147.386 1.00 33.29  ? 1110 LYS A C     1 
ATOM   7927 O  O     . LYS A 1 1110 ? 137.348 107.771 147.799 1.00 33.29  ? 1110 LYS A O     1 
ATOM   7928 C  CB    . LYS A 1 1110 ? 137.060 109.791 149.698 1.00 33.29  ? 1110 LYS A CB    1 
ATOM   7929 C  CG    . LYS A 1 1110 ? 138.545 110.104 149.743 1.00 33.29  ? 1110 LYS A CG    1 
ATOM   7930 C  CD    . LYS A 1 1110 ? 139.103 109.924 151.144 1.00 33.29  ? 1110 LYS A CD    1 
ATOM   7931 C  CE    . LYS A 1 1110 ? 140.603 110.153 151.172 1.00 33.29  ? 1110 LYS A CE    1 
ATOM   7932 N  NZ    . LYS A 1 1110 ? 141.176 109.886 152.519 1.00 33.29  ? 1110 LYS A NZ    1 
ATOM   7933 N  N     . ASP A 1 1111 ? 136.456 108.980 146.113 1.00 37.18  ? 1111 ASP A N     1 
ATOM   7934 C  CA    . ASP A 1 1111 ? 136.664 107.937 145.118 1.00 37.18  ? 1111 ASP A CA    1 
ATOM   7935 C  C     . ASP A 1 1111 ? 138.144 107.589 144.989 1.00 37.18  ? 1111 ASP A C     1 
ATOM   7936 O  O     . ASP A 1 1111 ? 139.027 108.415 145.235 1.00 37.18  ? 1111 ASP A O     1 
ATOM   7937 C  CB    . ASP A 1 1111 ? 136.070 108.370 143.771 1.00 37.18  ? 1111 ASP A CB    1 
ATOM   7938 C  CG    . ASP A 1 1111 ? 136.734 109.613 143.191 1.00 37.18  ? 1111 ASP A CG    1 
ATOM   7939 O  OD1   . ASP A 1 1111 ? 135.993 110.530 142.778 1.00 37.18  ? 1111 ASP A OD1   1 
ATOM   7940 O  OD2   . ASP A 1 1111 ? 137.977 109.676 143.105 1.00 37.18  ? 1111 ASP A OD2   1 
ATOM   7941 N  N     . GLY A 1 1112 ? 138.408 106.337 144.625 1.00 37.89  ? 1112 GLY A N     1 
ATOM   7942 C  CA    . GLY A 1 1112 ? 139.766 105.834 144.577 1.00 37.89  ? 1112 GLY A CA    1 
ATOM   7943 C  C     . GLY A 1 1112 ? 140.221 105.310 145.923 1.00 37.89  ? 1112 GLY A C     1 
ATOM   7944 O  O     . GLY A 1 1112 ? 141.297 105.671 146.408 1.00 37.89  ? 1112 GLY A O     1 
ATOM   7945 N  N     . ALA A 1 1113 ? 139.404 104.459 146.539 1.00 39.13  ? 1113 ALA A N     1 
ATOM   7946 C  CA    . ALA A 1 1113 ? 139.655 103.951 147.880 1.00 39.13  ? 1113 ALA A CA    1 
ATOM   7947 C  C     . ALA A 1 1113 ? 139.888 102.449 147.829 1.00 39.13  ? 1113 ALA A C     1 
ATOM   7948 O  O     . ALA A 1 1113 ? 139.123 101.717 147.192 1.00 39.13  ? 1113 ALA A O     1 
ATOM   7949 C  CB    . ALA A 1 1113 ? 138.486 104.271 148.815 1.00 39.13  ? 1113 ALA A CB    1 
ATOM   7950 N  N     . THR A 1 1114 ? 140.943 101.998 148.501 1.00 44.88  ? 1114 THR A N     1 
ATOM   7951 C  CA    . THR A 1 1114 ? 141.238 100.576 148.587 1.00 44.88  ? 1114 THR A CA    1 
ATOM   7952 C  C     . THR A 1 1114 ? 140.210 99.886  149.481 1.00 44.88  ? 1114 THR A C     1 
ATOM   7953 O  O     . THR A 1 1114 ? 139.613 100.503 150.367 1.00 44.88  ? 1114 THR A O     1 
ATOM   7954 C  CB    . THR A 1 1114 ? 142.664 100.378 149.121 1.00 44.88  ? 1114 THR A CB    1 
ATOM   7955 O  OG1   . THR A 1 1114 ? 143.599 100.913 148.178 1.00 44.88  ? 1114 THR A OG1   1 
ATOM   7956 C  CG2   . THR A 1 1114 ? 142.996 98.905  149.337 1.00 44.88  ? 1114 THR A CG2   1 
ATOM   7957 N  N     . GLU A 1 1115 ? 139.994 98.590  149.228 1.00 49.03  ? 1115 GLU A N     1 
ATOM   7958 C  CA    . GLU A 1 1115 ? 139.022 97.822  150.001 1.00 49.03  ? 1115 GLU A CA    1 
ATOM   7959 C  C     . GLU A 1 1115 ? 139.329 97.850  151.494 1.00 49.03  ? 1115 GLU A C     1 
ATOM   7960 O  O     . GLU A 1 1115 ? 138.411 97.746  152.317 1.00 49.03  ? 1115 GLU A O     1 
ATOM   7961 C  CB    . GLU A 1 1115 ? 138.984 96.380  149.496 1.00 49.03  ? 1115 GLU A CB    1 
ATOM   7962 C  CG    . GLU A 1 1115 ? 137.863 95.533  150.077 1.00 49.03  ? 1115 GLU A CG    1 
ATOM   7963 C  CD    . GLU A 1 1115 ? 136.501 95.923  149.543 1.00 49.03  ? 1115 GLU A CD    1 
ATOM   7964 O  OE1   . GLU A 1 1115 ? 135.813 96.731  150.201 1.00 49.03  ? 1115 GLU A OE1   1 
ATOM   7965 O  OE2   . GLU A 1 1115 ? 136.117 95.424  148.466 1.00 49.03  ? 1115 GLU A OE2   1 
ATOM   7966 N  N     . SER A 1 1116 ? 140.603 97.990  151.864 1.00 47.64  ? 1116 SER A N     1 
ATOM   7967 C  CA    . SER A 1 1116 ? 140.957 98.064  153.278 1.00 47.64  ? 1116 SER A CA    1 
ATOM   7968 C  C     . SER A 1 1116 ? 140.336 99.289  153.940 1.00 47.64  ? 1116 SER A C     1 
ATOM   7969 O  O     . SER A 1 1116 ? 139.827 99.206  155.064 1.00 47.64  ? 1116 SER A O     1 
ATOM   7970 C  CB    . SER A 1 1116 ? 142.476 98.080  153.437 1.00 47.64  ? 1116 SER A CB    1 
ATOM   7971 O  OG    . SER A 1 1116 ? 143.020 99.304  152.977 1.00 47.64  ? 1116 SER A OG    1 
ATOM   7972 N  N     . GLU A 1 1117 ? 140.370 100.436 153.258 1.00 45.36  ? 1117 GLU A N     1 
ATOM   7973 C  CA    . GLU A 1 1117 ? 139.769 101.646 153.812 1.00 45.36  ? 1117 GLU A CA    1 
ATOM   7974 C  C     . GLU A 1 1117 ? 138.261 101.493 153.966 1.00 45.36  ? 1117 GLU A C     1 
ATOM   7975 O  O     . GLU A 1 1117 ? 137.684 101.935 154.966 1.00 45.36  ? 1117 GLU A O     1 
ATOM   7976 C  CB    . GLU A 1 1117 ? 140.099 102.846 152.927 1.00 45.36  ? 1117 GLU A CB    1 
ATOM   7977 C  CG    . GLU A 1 1117 ? 141.582 103.157 152.842 1.00 45.36  ? 1117 GLU A CG    1 
ATOM   7978 C  CD    . GLU A 1 1117 ? 141.876 104.345 151.953 1.00 45.36  ? 1117 GLU A CD    1 
ATOM   7979 O  OE1   . GLU A 1 1117 ? 141.355 105.445 152.234 1.00 45.36  ? 1117 GLU A OE1   1 
ATOM   7980 O  OE2   . GLU A 1 1117 ? 142.629 104.180 150.970 1.00 45.36  ? 1117 GLU A OE2   1 
ATOM   7981 N  N     . VAL A 1 1118 ? 137.606 100.874 152.982 1.00 43.50  ? 1118 VAL A N     1 
ATOM   7982 C  CA    . VAL A 1 1118 ? 136.166 100.648 153.071 1.00 43.50  ? 1118 VAL A CA    1 
ATOM   7983 C  C     . VAL A 1 1118 ? 135.843 99.735  154.246 1.00 43.50  ? 1118 VAL A C     1 
ATOM   7984 O  O     . VAL A 1 1118 ? 134.886 99.974  154.993 1.00 43.50  ? 1118 VAL A O     1 
ATOM   7985 C  CB    . VAL A 1 1118 ? 135.635 100.076 151.744 1.00 43.50  ? 1118 VAL A CB    1 
ATOM   7986 C  CG1   . VAL A 1 1118 ? 134.186 99.647  151.889 1.00 43.50  ? 1118 VAL A CG1   1 
ATOM   7987 C  CG2   . VAL A 1 1118 ? 135.782 101.100 150.635 1.00 43.50  ? 1118 VAL A CG2   1 
ATOM   7988 N  N     . ILE A 1 1119 ? 136.633 98.675  154.428 1.00 46.94  ? 1119 ILE A N     1 
ATOM   7989 C  CA    . ILE A 1 1119 ? 136.408 97.759  155.543 1.00 46.94  ? 1119 ILE A CA    1 
ATOM   7990 C  C     . ILE A 1 1119 ? 136.595 98.480  156.871 1.00 46.94  ? 1119 ILE A C     1 
ATOM   7991 O  O     . ILE A 1 1119 ? 135.810 98.296  157.810 1.00 46.94  ? 1119 ILE A O     1 
ATOM   7992 C  CB    . ILE A 1 1119 ? 137.334 96.535  155.422 1.00 46.94  ? 1119 ILE A CB    1 
ATOM   7993 C  CG1   . ILE A 1 1119 ? 136.845 95.610  154.307 1.00 46.94  ? 1119 ILE A CG1   1 
ATOM   7994 C  CG2   . ILE A 1 1119 ? 137.411 95.784  156.740 1.00 46.94  ? 1119 ILE A CG2   1 
ATOM   7995 C  CD1   . ILE A 1 1119 ? 137.862 94.578  153.881 1.00 46.94  ? 1119 ILE A CD1   1 
ATOM   7996 N  N     . ASP A 1 1120 ? 137.634 99.312  156.972 1.00 48.14  ? 1120 ASP A N     1 
ATOM   7997 C  CA    . ASP A 1 1120 ? 137.863 100.059 158.206 1.00 48.14  ? 1120 ASP A CA    1 
ATOM   7998 C  C     . ASP A 1 1120 ? 136.717 101.023 158.492 1.00 48.14  ? 1120 ASP A C     1 
ATOM   7999 O  O     . ASP A 1 1120 ? 136.285 101.161 159.643 1.00 48.14  ? 1120 ASP A O     1 
ATOM   8000 C  CB    . ASP A 1 1120 ? 139.188 100.813 158.125 1.00 48.14  ? 1120 ASP A CB    1 
ATOM   8001 C  CG    . ASP A 1 1120 ? 139.384 101.763 159.286 1.00 48.14  ? 1120 ASP A CG    1 
ATOM   8002 O  OD1   . ASP A 1 1120 ? 139.381 101.295 160.444 1.00 48.14  ? 1120 ASP A OD1   1 
ATOM   8003 O  OD2   . ASP A 1 1120 ? 139.536 102.978 159.042 1.00 48.14  ? 1120 ASP A OD2   1 
ATOM   8004 N  N     . ALA A 1 1121 ? 136.217 101.705 157.459 1.00 45.75  ? 1121 ALA A N     1 
ATOM   8005 C  CA    . ALA A 1 1121 ? 135.092 102.616 157.650 1.00 45.75  ? 1121 ALA A CA    1 
ATOM   8006 C  C     . ALA A 1 1121 ? 133.843 101.867 158.097 1.00 45.75  ? 1121 ALA A C     1 
ATOM   8007 O  O     . ALA A 1 1121 ? 133.124 102.322 158.995 1.00 45.75  ? 1121 ALA A O     1 
ATOM   8008 C  CB    . ALA A 1 1121 ? 134.820 103.391 156.362 1.00 45.75  ? 1121 ALA A CB    1 
ATOM   8009 N  N     . ALA A 1 1122 ? 133.570 100.714 157.482 1.00 45.48  ? 1122 ALA A N     1 
ATOM   8010 C  CA    . ALA A 1 1122 ? 132.411 99.922  157.878 1.00 45.48  ? 1122 ALA A CA    1 
ATOM   8011 C  C     . ALA A 1 1122 ? 132.543 99.436  159.315 1.00 45.48  ? 1122 ALA A C     1 
ATOM   8012 O  O     . ALA A 1 1122 ? 131.556 99.400  160.059 1.00 45.48  ? 1122 ALA A O     1 
ATOM   8013 C  CB    . ALA A 1 1122 ? 132.228 98.742  156.926 1.00 45.48  ? 1122 ALA A CB    1 
ATOM   8014 N  N     . ARG A 1 1123 ? 133.754 99.048  159.721 1.00 49.01  ? 1123 ARG A N     1 
ATOM   8015 C  CA    . ARG A 1 1123 ? 133.980 98.664  161.110 1.00 49.01  ? 1123 ARG A CA    1 
ATOM   8016 C  C     . ARG A 1 1123 ? 133.741 99.837  162.052 1.00 49.01  ? 1123 ARG A C     1 
ATOM   8017 O  O     . ARG A 1 1123 ? 133.124 99.679  163.111 1.00 49.01  ? 1123 ARG A O     1 
ATOM   8018 C  CB    . ARG A 1 1123 ? 135.400 98.126  161.280 1.00 49.01  ? 1123 ARG A CB    1 
ATOM   8019 C  CG    . ARG A 1 1123 ? 135.546 96.639  161.016 1.00 49.01  ? 1123 ARG A CG    1 
ATOM   8020 C  CD    . ARG A 1 1123 ? 136.921 96.143  161.433 1.00 49.01  ? 1123 ARG A CD    1 
ATOM   8021 N  NE    . ARG A 1 1123 ? 136.893 94.750  161.868 1.00 49.01  ? 1123 ARG A NE    1 
ATOM   8022 C  CZ    . ARG A 1 1123 ? 136.794 94.366  163.136 1.00 49.01  ? 1123 ARG A CZ    1 
ATOM   8023 N  NH1   . ARG A 1 1123 ? 136.710 95.272  164.100 1.00 49.01  ? 1123 ARG A NH1   1 
ATOM   8024 N  NH2   . ARG A 1 1123 ? 136.776 93.075  163.440 1.00 49.01  ? 1123 ARG A NH2   1 
ATOM   8025 N  N     . ALA A 1 1124 ? 134.225 101.025 161.681 1.00 49.51  ? 1124 ALA A N     1 
ATOM   8026 C  CA    . ALA A 1 1124 ? 134.069 102.192 162.543 1.00 49.51  ? 1124 ALA A CA    1 
ATOM   8027 C  C     . ALA A 1 1124 ? 132.617 102.639 162.633 1.00 49.51  ? 1124 ALA A C     1 
ATOM   8028 O  O     . ALA A 1 1124 ? 132.214 103.232 163.641 1.00 49.51  ? 1124 ALA A O     1 
ATOM   8029 C  CB    . ALA A 1 1124 ? 134.945 103.338 162.041 1.00 49.51  ? 1124 ALA A CB    1 
ATOM   8030 N  N     . ALA A 1 1125 ? 131.821 102.370 161.604 1.00 49.59  ? 1125 ALA A N     1 
ATOM   8031 C  CA    . ALA A 1 1125 ? 130.414 102.743 161.594 1.00 49.59  ? 1125 ALA A CA    1 
ATOM   8032 C  C     . ALA A 1 1125 ? 129.513 101.655 162.163 1.00 49.59  ? 1125 ALA A C     1 
ATOM   8033 O  O     . ALA A 1 1125 ? 128.287 101.777 162.072 1.00 49.59  ? 1125 ALA A O     1 
ATOM   8034 C  CB    . ALA A 1 1125 ? 129.969 103.092 160.172 1.00 49.59  ? 1125 ALA A CB    1 
ATOM   8035 N  N     . ASN A 1 1126 ? 130.091 100.601 162.735 1.00 54.39  ? 1126 ASN A N     1 
ATOM   8036 C  CA    . ASN A 1 1126 ? 129.348 99.452  163.251 1.00 54.39  ? 1126 ASN A CA    1 
ATOM   8037 C  C     . ASN A 1 1126 ? 128.480 98.840  162.151 1.00 54.39  ? 1126 ASN A C     1 
ATOM   8038 O  O     . ASN A 1 1126 ? 127.263 98.696  162.274 1.00 54.39  ? 1126 ASN A O     1 
ATOM   8039 C  CB    . ASN A 1 1126 ? 128.512 99.838  164.475 1.00 54.39  ? 1126 ASN A CB    1 
ATOM   8040 C  CG    . ASN A 1 1126 ? 127.891 98.634  165.165 1.00 54.39  ? 1126 ASN A CG    1 
ATOM   8041 O  OD1   . ASN A 1 1126 ? 128.053 97.496  164.725 1.00 54.39  ? 1126 ASN A OD1   1 
ATOM   8042 N  ND2   . ASN A 1 1126 ? 127.171 98.884  166.251 1.00 54.39  ? 1126 ASN A ND2   1 
ATOM   8043 N  N     . ALA A 1 1127 ? 129.142 98.486  161.052 1.00 47.43  ? 1127 ALA A N     1 
ATOM   8044 C  CA    . ALA A 1 1127 ? 128.471 97.840  159.934 1.00 47.43  ? 1127 ALA A CA    1 
ATOM   8045 C  C     . ALA A 1 1127 ? 129.145 96.558  159.475 1.00 47.43  ? 1127 ALA A C     1 
ATOM   8046 O  O     . ALA A 1 1127 ? 128.545 95.829  158.681 1.00 47.43  ? 1127 ALA A O     1 
ATOM   8047 C  CB    . ALA A 1 1127 ? 128.368 98.801  158.742 1.00 47.43  ? 1127 ALA A CB    1 
ATOM   8048 N  N     . HIS A 1 1128 ? 130.359 96.253  159.939 1.00 46.66  ? 1128 HIS A N     1 
ATOM   8049 C  CA    . HIS A 1 1128 ? 131.023 95.021  159.528 1.00 46.66  ? 1128 HIS A CA    1 
ATOM   8050 C  C     . HIS A 1 1128 ? 130.322 93.790  160.086 1.00 46.66  ? 1128 HIS A C     1 
ATOM   8051 O  O     . HIS A 1 1128 ? 130.512 92.684  159.568 1.00 46.66  ? 1128 HIS A O     1 
ATOM   8052 C  CB    . HIS A 1 1128 ? 132.486 95.043  159.967 1.00 46.66  ? 1128 HIS A CB    1 
ATOM   8053 C  CG    . HIS A 1 1128 ? 133.332 94.000  159.307 1.00 46.66  ? 1128 HIS A CG    1 
ATOM   8054 N  ND1   . HIS A 1 1128 ? 133.030 93.467  158.072 1.00 46.66  ? 1128 HIS A ND1   1 
ATOM   8055 C  CD2   . HIS A 1 1128 ? 134.474 93.393  159.709 1.00 46.66  ? 1128 HIS A CD2   1 
ATOM   8056 C  CE1   . HIS A 1 1128 ? 133.948 92.576  157.743 1.00 46.66  ? 1128 HIS A CE1   1 
ATOM   8057 N  NE2   . HIS A 1 1128 ? 134.835 92.512  158.719 1.00 46.66  ? 1128 HIS A NE2   1 
ATOM   8058 N  N     . GLY A 1 1129 ? 129.520 93.957  161.134 1.00 44.96  ? 1129 GLY A N     1 
ATOM   8059 C  CA    . GLY A 1 1129 ? 128.815 92.842  161.734 1.00 44.96  ? 1129 GLY A CA    1 
ATOM   8060 C  C     . GLY A 1 1129 ? 127.820 92.185  160.801 1.00 44.96  ? 1129 GLY A C     1 
ATOM   8061 O  O     . GLY A 1 1129 ? 127.991 91.023  160.421 1.00 44.96  ? 1129 GLY A O     1 
ATOM   8062 N  N     . PHE A 1 1130 ? 126.774 92.921  160.419 1.00 42.98  ? 1130 PHE A N     1 
ATOM   8063 C  CA    . PHE A 1 1130 ? 125.749 92.346  159.556 1.00 42.98  ? 1130 PHE A CA    1 
ATOM   8064 C  C     . PHE A 1 1130 ? 126.255 92.136  158.135 1.00 42.98  ? 1130 PHE A C     1 
ATOM   8065 O  O     . PHE A 1 1130 ? 125.791 91.221  157.446 1.00 42.98  ? 1130 PHE A O     1 
ATOM   8066 C  CB    . PHE A 1 1130 ? 124.500 93.229  159.557 1.00 42.98  ? 1130 PHE A CB    1 
ATOM   8067 C  CG    . PHE A 1 1130 ? 124.649 94.497  158.767 1.00 42.98  ? 1130 PHE A CG    1 
ATOM   8068 C  CD1   . PHE A 1 1130 ? 125.207 95.625  159.343 1.00 42.98  ? 1130 PHE A CD1   1 
ATOM   8069 C  CD2   . PHE A 1 1130 ? 124.218 94.567  157.451 1.00 42.98  ? 1130 PHE A CD2   1 
ATOM   8070 C  CE1   . PHE A 1 1130 ? 125.342 96.794  158.621 1.00 42.98  ? 1130 PHE A CE1   1 
ATOM   8071 C  CE2   . PHE A 1 1130 ? 124.353 95.733  156.725 1.00 42.98  ? 1130 PHE A CE2   1 
ATOM   8072 C  CZ    . PHE A 1 1130 ? 124.914 96.848  157.311 1.00 42.98  ? 1130 PHE A CZ    1 
ATOM   8073 N  N     . ILE A 1 1131 ? 127.189 92.972  157.676 1.00 43.49  ? 1131 ILE A N     1 
ATOM   8074 C  CA    . ILE A 1 1131 ? 127.703 92.840  156.315 1.00 43.49  ? 1131 ILE A CA    1 
ATOM   8075 C  C     . ILE A 1 1131 ? 128.415 91.504  156.143 1.00 43.49  ? 1131 ILE A C     1 
ATOM   8076 O  O     . ILE A 1 1131 ? 128.218 90.798  155.146 1.00 43.49  ? 1131 ILE A O     1 
ATOM   8077 C  CB    . ILE A 1 1131 ? 128.626 94.023  155.971 1.00 43.49  ? 1131 ILE A CB    1 
ATOM   8078 C  CG1   . ILE A 1 1131 ? 127.796 95.251  155.599 1.00 43.49  ? 1131 ILE A CG1   1 
ATOM   8079 C  CG2   . ILE A 1 1131 ? 129.560 93.659  154.833 1.00 43.49  ? 1131 ILE A CG2   1 
ATOM   8080 C  CD1   . ILE A 1 1131 ? 128.619 96.497  155.381 1.00 43.49  ? 1131 ILE A CD1   1 
ATOM   8081 N  N     . SER A 1 1132 ? 129.251 91.134  157.116 1.00 45.32  ? 1132 SER A N     1 
ATOM   8082 C  CA    . SER A 1 1132 ? 129.915 89.836  157.060 1.00 45.32  ? 1132 SER A CA    1 
ATOM   8083 C  C     . SER A 1 1132 ? 128.915 88.693  157.154 1.00 45.32  ? 1132 SER A C     1 
ATOM   8084 O  O     . SER A 1 1132 ? 129.160 87.611  156.609 1.00 45.32  ? 1132 SER A O     1 
ATOM   8085 C  CB    . SER A 1 1132 ? 130.951 89.726  158.177 1.00 45.32  ? 1132 SER A CB    1 
ATOM   8086 O  OG    . SER A 1 1132 ? 130.325 89.678  159.446 1.00 45.32  ? 1132 SER A OG    1 
ATOM   8087 N  N     . GLY A 1 1133 ? 127.792 88.909  157.841 1.00 44.32  ? 1133 GLY A N     1 
ATOM   8088 C  CA    . GLY A 1 1133 ? 126.755 87.894  157.890 1.00 44.32  ? 1133 GLY A CA    1 
ATOM   8089 C  C     . GLY A 1 1133 ? 126.142 87.608  156.535 1.00 44.32  ? 1133 GLY A C     1 
ATOM   8090 O  O     . GLY A 1 1133 ? 125.707 86.484  156.271 1.00 44.32  ? 1133 GLY A O     1 
ATOM   8091 N  N     . LEU A 1 1134 ? 126.092 88.612  155.664 1.00 44.81  ? 1134 LEU A N     1 
ATOM   8092 C  CA    . LEU A 1 1134 ? 125.574 88.408  154.323 1.00 44.81  ? 1134 LEU A CA    1 
ATOM   8093 C  C     . LEU A 1 1134 ? 126.478 87.447  153.553 1.00 44.81  ? 1134 LEU A C     1 
ATOM   8094 O  O     . LEU A 1 1134 ? 127.689 87.402  153.784 1.00 44.81  ? 1134 LEU A O     1 
ATOM   8095 C  CB    . LEU A 1 1134 ? 125.473 89.736  153.579 1.00 44.81  ? 1134 LEU A CB    1 
ATOM   8096 C  CG    . LEU A 1 1134 ? 124.789 90.885  154.322 1.00 44.81  ? 1134 LEU A CG    1 
ATOM   8097 C  CD1   . LEU A 1 1134 ? 124.847 92.160  153.499 1.00 44.81  ? 1134 LEU A CD1   1 
ATOM   8098 C  CD2   . LEU A 1 1134 ? 123.352 90.526  154.657 1.00 44.81  ? 1134 LEU A CD2   1 
ATOM   8099 N  N     . PRO A 1 1135 ? 125.909 86.656  152.641 1.00 47.12  ? 1135 PRO A N     1 
ATOM   8100 C  CA    . PRO A 1 1135 ? 126.737 85.665  151.929 1.00 47.12  ? 1135 PRO A CA    1 
ATOM   8101 C  C     . PRO A 1 1135 ? 127.842 86.283  151.089 1.00 47.12  ? 1135 PRO A C     1 
ATOM   8102 O  O     . PRO A 1 1135 ? 129.015 85.928  151.258 1.00 47.12  ? 1135 PRO A O     1 
ATOM   8103 C  CB    . PRO A 1 1135 ? 125.711 84.911  151.069 1.00 47.12  ? 1135 PRO A CB    1 
ATOM   8104 C  CG    . PRO A 1 1135 ? 124.394 85.162  151.725 1.00 47.12  ? 1135 PRO A CG    1 
ATOM   8105 C  CD    . PRO A 1 1135 ? 124.484 86.539  152.295 1.00 47.12  ? 1135 PRO A CD    1 
ATOM   8106 N  N     . GLU A 1 1136 ? 127.505 87.203  150.190 1.00 47.16  ? 1136 GLU A N     1 
ATOM   8107 C  CA    . GLU A 1 1136 ? 128.482 87.737  149.240 1.00 47.16  ? 1136 GLU A CA    1 
ATOM   8108 C  C     . GLU A 1 1136 ? 129.155 89.007  149.754 1.00 47.16  ? 1136 GLU A C     1 
ATOM   8109 O  O     . GLU A 1 1136 ? 129.241 90.005  149.040 1.00 47.16  ? 1136 GLU A O     1 
ATOM   8110 C  CB    . GLU A 1 1136 ? 127.808 87.986  147.897 1.00 47.16  ? 1136 GLU A CB    1 
ATOM   8111 C  CG    . GLU A 1 1136 ? 127.280 86.734  147.225 1.00 47.16  ? 1136 GLU A CG    1 
ATOM   8112 C  CD    . GLU A 1 1136 ? 125.773 86.620  147.322 1.00 47.16  ? 1136 GLU A CD    1 
ATOM   8113 O  OE1   . GLU A 1 1136 ? 125.235 86.800  148.435 1.00 47.16  ? 1136 GLU A OE1   1 
ATOM   8114 O  OE2   . GLU A 1 1136 ? 125.126 86.355  146.287 1.00 47.16  ? 1136 GLU A OE2   1 
ATOM   8115 N  N     . GLY A 1 1137 ? 129.649 88.963  150.992 1.00 43.09  ? 1137 GLY A N     1 
ATOM   8116 C  CA    . GLY A 1 1137 ? 130.444 90.031  151.578 1.00 43.09  ? 1137 GLY A CA    1 
ATOM   8117 C  C     . GLY A 1 1137 ? 130.001 91.443  151.251 1.00 43.09  ? 1137 GLY A C     1 
ATOM   8118 O  O     . GLY A 1 1137 ? 128.836 91.799  151.444 1.00 43.09  ? 1137 GLY A O     1 
ATOM   8119 N  N     . TYR A 1 1138 ? 130.929 92.254  150.750 1.00 42.81  ? 1138 TYR A N     1 
ATOM   8120 C  CA    . TYR A 1 1138 ? 130.618 93.604  150.283 1.00 42.81  ? 1138 TYR A CA    1 
ATOM   8121 C  C     . TYR A 1 1138 ? 130.290 93.608  148.793 1.00 42.81  ? 1138 TYR A C     1 
ATOM   8122 O  O     . TYR A 1 1138 ? 130.831 94.398  148.024 1.00 42.81  ? 1138 TYR A O     1 
ATOM   8123 C  CB    . TYR A 1 1138 ? 131.784 94.542  150.574 1.00 42.81  ? 1138 TYR A CB    1 
ATOM   8124 C  CG    . TYR A 1 1138 ? 132.156 94.681  152.032 1.00 42.81  ? 1138 TYR A CG    1 
ATOM   8125 C  CD1   . TYR A 1 1138 ? 132.882 93.693  152.682 1.00 42.81  ? 1138 TYR A CD1   1 
ATOM   8126 C  CD2   . TYR A 1 1138 ? 131.802 95.812  152.753 1.00 42.81  ? 1138 TYR A CD2   1 
ATOM   8127 C  CE1   . TYR A 1 1138 ? 133.230 93.820  154.011 1.00 42.81  ? 1138 TYR A CE1   1 
ATOM   8128 C  CE2   . TYR A 1 1138 ? 132.147 95.950  154.082 1.00 42.81  ? 1138 TYR A CE2   1 
ATOM   8129 C  CZ    . TYR A 1 1138 ? 132.860 94.950  154.706 1.00 42.81  ? 1138 TYR A CZ    1 
ATOM   8130 O  OH    . TYR A 1 1138 ? 133.207 95.078  156.030 1.00 42.81  ? 1138 TYR A OH    1 
ATOM   8131 N  N     . LYS A 1 1139 ? 129.397 92.715  148.369 1.00 41.31  ? 1139 LYS A N     1 
ATOM   8132 C  CA    . LYS A 1 1139 ? 129.027 92.636  146.964 1.00 41.31  ? 1139 LYS A CA    1 
ATOM   8133 C  C     . LYS A 1 1139 ? 127.540 92.418  146.734 1.00 41.31  ? 1139 LYS A C     1 
ATOM   8134 O  O     . LYS A 1 1139 ? 127.122 92.343  145.575 1.00 41.31  ? 1139 LYS A O     1 
ATOM   8135 C  CB    . LYS A 1 1139 ? 129.814 91.516  146.264 1.00 41.31  ? 1139 LYS A CB    1 
ATOM   8136 C  CG    . LYS A 1 1139 ? 131.280 91.834  146.026 1.00 41.31  ? 1139 LYS A CG    1 
ATOM   8137 C  CD    . LYS A 1 1139 ? 131.444 93.058  145.143 1.00 41.31  ? 1139 LYS A CD    1 
ATOM   8138 C  CE    . LYS A 1 1139 ? 132.906 93.297  144.803 1.00 41.31  ? 1139 LYS A CE    1 
ATOM   8139 N  NZ    . LYS A 1 1139 ? 133.815 92.788  145.866 1.00 41.31  ? 1139 LYS A NZ    1 
ATOM   8140 N  N     . THR A 1 1140 ? 126.737 92.309  147.783 1.00 36.92  ? 1140 THR A N     1 
ATOM   8141 C  CA    . THR A 1 1140 ? 125.317 92.031  147.611 1.00 36.92  ? 1140 THR A CA    1 
ATOM   8142 C  C     . THR A 1 1140 ? 124.628 93.213  146.938 1.00 36.92  ? 1140 THR A C     1 
ATOM   8143 O  O     . THR A 1 1140 ? 124.788 94.353  147.386 1.00 36.92  ? 1140 THR A O     1 
ATOM   8144 C  CB    . THR A 1 1140 ? 124.665 91.745  148.961 1.00 36.92  ? 1140 THR A CB    1 
ATOM   8145 O  OG1   . THR A 1 1140 ? 125.290 90.606  149.564 1.00 36.92  ? 1140 THR A OG1   1 
ATOM   8146 C  CG2   . THR A 1 1140 ? 123.182 91.470  148.790 1.00 36.92  ? 1140 THR A CG2   1 
ATOM   8147 N  N     . PRO A 1 1141 ? 123.877 92.993  145.861 1.00 32.23  ? 1141 PRO A N     1 
ATOM   8148 C  CA    . PRO A 1 1141 ? 123.106 94.093  145.274 1.00 32.23  ? 1141 PRO A CA    1 
ATOM   8149 C  C     . PRO A 1 1141 ? 122.065 94.608  146.257 1.00 32.23  ? 1141 PRO A C     1 
ATOM   8150 O  O     . PRO A 1 1141 ? 121.493 93.846  147.039 1.00 32.23  ? 1141 PRO A O     1 
ATOM   8151 C  CB    . PRO A 1 1141 ? 122.456 93.455  144.041 1.00 32.23  ? 1141 PRO A CB    1 
ATOM   8152 C  CG    . PRO A 1 1141 ? 122.460 91.989  144.323 1.00 32.23  ? 1141 PRO A CG    1 
ATOM   8153 C  CD    . PRO A 1 1141 ? 123.697 91.732  145.125 1.00 32.23  ? 1141 PRO A CD    1 
ATOM   8154 N  N     . VAL A 1 1142 ? 121.828 95.917  146.217 1.00 28.13  ? 1142 VAL A N     1 
ATOM   8155 C  CA    . VAL A 1 1142 ? 120.872 96.539  147.125 1.00 28.13  ? 1142 VAL A CA    1 
ATOM   8156 C  C     . VAL A 1 1142 ? 119.532 96.699  146.421 1.00 28.13  ? 1142 VAL A C     1 
ATOM   8157 O  O     . VAL A 1 1142 ? 118.529 96.107  146.833 1.00 28.13  ? 1142 VAL A O     1 
ATOM   8158 C  CB    . VAL A 1 1142 ? 121.392 97.893  147.640 1.00 28.13  ? 1142 VAL A CB    1 
ATOM   8159 C  CG1   . VAL A 1 1142 ? 120.304 98.618  148.409 1.00 28.13  ? 1142 VAL A CG1   1 
ATOM   8160 C  CG2   . VAL A 1 1142 ? 122.613 97.689  148.515 1.00 28.13  ? 1142 VAL A CG2   1 
ATOM   8161 N  N     . GLY A 1 1143 ? 119.509 97.478  145.351 1.00 32.23  ? 1143 GLY A N     1 
ATOM   8162 C  CA    . GLY A 1 1143 ? 118.291 97.765  144.622 1.00 32.23  ? 1143 GLY A CA    1 
ATOM   8163 C  C     . GLY A 1 1143 ? 117.964 99.247  144.627 1.00 32.23  ? 1143 GLY A C     1 
ATOM   8164 O  O     . GLY A 1 1143 ? 118.582 100.054 145.319 1.00 32.23  ? 1143 GLY A O     1 
ATOM   8165 N  N     . GLU A 1 1144 ? 116.955 99.587  143.830 1.00 32.62  ? 1144 GLU A N     1 
ATOM   8166 C  CA    . GLU A 1 1144 ? 116.581 100.983 143.652 1.00 32.62  ? 1144 GLU A CA    1 
ATOM   8167 C  C     . GLU A 1 1144 ? 116.061 101.571 144.959 1.00 32.62  ? 1144 GLU A C     1 
ATOM   8168 O  O     . GLU A 1 1144 ? 115.335 100.915 145.710 1.00 32.62  ? 1144 GLU A O     1 
ATOM   8169 C  CB    . GLU A 1 1144 ? 115.548 101.106 142.523 1.00 32.62  ? 1144 GLU A CB    1 
ATOM   8170 C  CG    . GLU A 1 1144 ? 114.140 100.564 142.800 1.00 32.62  ? 1144 GLU A CG    1 
ATOM   8171 C  CD    . GLU A 1 1144 ? 113.276 101.492 143.637 1.00 32.62  ? 1144 GLU A CD    1 
ATOM   8172 O  OE1   . GLU A 1 1144 ? 113.580 102.701 143.687 1.00 32.62  ? 1144 GLU A OE1   1 
ATOM   8173 O  OE2   . GLU A 1 1144 ? 112.296 101.011 144.243 1.00 32.62  ? 1144 GLU A OE2   1 
ATOM   8174 N  N     . ARG A 1 1145 ? 116.486 102.801 145.251 1.00 34.68  ? 1145 ARG A N     1 
ATOM   8175 C  CA    . ARG A 1 1145 ? 116.071 103.614 146.393 1.00 34.68  ? 1145 ARG A CA    1 
ATOM   8176 C  C     . ARG A 1 1145 ? 116.573 103.044 147.718 1.00 34.68  ? 1145 ARG A C     1 
ATOM   8177 O  O     . ARG A 1 1145 ? 116.403 103.686 148.762 1.00 34.68  ? 1145 ARG A O     1 
ATOM   8178 C  CB    . ARG A 1 1145 ? 114.543 103.799 146.437 1.00 34.68  ? 1145 ARG A CB    1 
ATOM   8179 C  CG    . ARG A 1 1145 ? 113.998 104.737 147.509 1.00 34.68  ? 1145 ARG A CG    1 
ATOM   8180 C  CD    . ARG A 1 1145 ? 114.693 106.088 147.486 1.00 34.68  ? 1145 ARG A CD    1 
ATOM   8181 N  NE    . ARG A 1 1145 ? 114.010 107.050 146.627 1.00 34.68  ? 1145 ARG A NE    1 
ATOM   8182 C  CZ    . ARG A 1 1145 ? 114.169 108.367 146.709 1.00 34.68  ? 1145 ARG A CZ    1 
ATOM   8183 N  NH1   . ARG A 1 1145 ? 114.988 108.881 147.616 1.00 34.68  ? 1145 ARG A NH1   1 
ATOM   8184 N  NH2   . ARG A 1 1145 ? 113.510 109.171 145.887 1.00 34.68  ? 1145 ARG A NH2   1 
ATOM   8185 N  N     . GLY A 1 1146 ? 117.238 101.894 147.712 1.00 35.94  ? 1146 GLY A N     1 
ATOM   8186 C  CA    . GLY A 1 1146 ? 117.663 101.293 148.958 1.00 35.94  ? 1146 GLY A CA    1 
ATOM   8187 C  C     . GLY A 1 1146 ? 116.615 100.377 149.552 1.00 35.94  ? 1146 GLY A C     1 
ATOM   8188 O  O     . GLY A 1 1146 ? 116.194 100.557 150.697 1.00 35.94  ? 1146 GLY A O     1 
ATOM   8189 N  N     . VAL A 1 1147 ? 116.177 99.393  148.774 1.00 33.38  ? 1147 VAL A N     1 
ATOM   8190 C  CA    . VAL A 1 1147 ? 115.225 98.394  149.241 1.00 33.38  ? 1147 VAL A CA    1 
ATOM   8191 C  C     . VAL A 1 1147 ? 116.009 97.091  149.319 1.00 33.38  ? 1147 VAL A C     1 
ATOM   8192 O  O     . VAL A 1 1147 ? 117.211 97.075  149.034 1.00 33.38  ? 1147 VAL A O     1 
ATOM   8193 C  CB    . VAL A 1 1147 ? 113.998 98.300  148.312 1.00 33.38  ? 1147 VAL A CB    1 
ATOM   8194 C  CG1   . VAL A 1 1147 ? 112.863 97.520  148.961 1.00 33.38  ? 1147 VAL A CG1   1 
ATOM   8195 C  CG2   . VAL A 1 1147 ? 113.515 99.687  147.942 1.00 33.38  ? 1147 VAL A CG2   1 
ATOM   8196 N  N     . GLN A 1 1148 ? 115.362 96.008  149.748 1.00 36.14  ? 1148 GLN A N     1 
ATOM   8197 C  CA    . GLN A 1 1148 ? 116.007 94.726  150.015 1.00 36.14  ? 1148 GLN A CA    1 
ATOM   8198 C  C     . GLN A 1 1148 ? 116.999 94.818  151.165 1.00 36.14  ? 1148 GLN A C     1 
ATOM   8199 O  O     . GLN A 1 1148 ? 117.897 93.979  151.282 1.00 36.14  ? 1148 GLN A O     1 
ATOM   8200 C  CB    . GLN A 1 1148 ? 116.695 94.160  148.766 1.00 36.14  ? 1148 GLN A CB    1 
ATOM   8201 C  CG    . GLN A 1 1148 ? 115.805 94.116  147.535 1.00 36.14  ? 1148 GLN A CG    1 
ATOM   8202 C  CD    . GLN A 1 1148 ? 116.534 93.609  146.310 1.00 36.14  ? 1148 GLN A CD    1 
ATOM   8203 O  OE1   . GLN A 1 1148 ? 115.976 93.571  145.213 1.00 36.14  ? 1148 GLN A OE1   1 
ATOM   8204 N  NE2   . GLN A 1 1148 ? 117.788 93.217  146.488 1.00 36.14  ? 1148 GLN A NE2   1 
ATOM   8205 N  N     . LEU A 1 1149 ? 116.853 95.834  152.010 1.00 35.39  ? 1149 LEU A N     1 
ATOM   8206 C  CA    . LEU A 1 1149 ? 117.614 95.970  153.241 1.00 35.39  ? 1149 LEU A CA    1 
ATOM   8207 C  C     . LEU A 1 1149 ? 116.668 96.516  154.305 1.00 35.39  ? 1149 LEU A C     1 
ATOM   8208 O  O     . LEU A 1 1149 ? 115.451 96.572  154.110 1.00 35.39  ? 1149 LEU A O     1 
ATOM   8209 C  CB    . LEU A 1 1149 ? 118.842 96.866  153.034 1.00 35.39  ? 1149 LEU A CB    1 
ATOM   8210 C  CG    . LEU A 1 1149 ? 120.009 96.268  152.248 1.00 35.39  ? 1149 LEU A CG    1 
ATOM   8211 C  CD1   . LEU A 1 1149 ? 121.119 97.289  152.079 1.00 35.39  ? 1149 LEU A CD1   1 
ATOM   8212 C  CD2   . LEU A 1 1149 ? 120.529 95.019  152.933 1.00 35.39  ? 1149 LEU A CD2   1 
ATOM   8213 N  N     . SER A 1 1150 ? 117.226 96.924  155.437 1.00 42.70  ? 1150 SER A N     1 
ATOM   8214 C  CA    . SER A 1 1150 ? 116.452 97.509  156.518 1.00 42.70  ? 1150 SER A CA    1 
ATOM   8215 C  C     . SER A 1 1150 ? 116.834 98.972  156.698 1.00 42.70  ? 1150 SER A C     1 
ATOM   8216 O  O     . SER A 1 1150 ? 117.906 99.412  156.276 1.00 42.70  ? 1150 SER A O     1 
ATOM   8217 C  CB    . SER A 1 1150 ? 116.673 96.749  157.829 1.00 42.70  ? 1150 SER A CB    1 
ATOM   8218 O  OG    . SER A 1 1150 ? 117.984 96.958  158.321 1.00 42.70  ? 1150 SER A OG    1 
ATOM   8219 N  N     . GLY A 1 1151 ? 115.933 99.725  157.332 1.00 42.81  ? 1151 GLY A N     1 
ATOM   8220 C  CA    . GLY A 1 1151 ? 116.216 101.128 157.589 1.00 42.81  ? 1151 GLY A CA    1 
ATOM   8221 C  C     . GLY A 1 1151 ? 117.465 101.321 158.425 1.00 42.81  ? 1151 GLY A C     1 
ATOM   8222 O  O     . GLY A 1 1151 ? 118.280 102.206 158.148 1.00 42.81  ? 1151 GLY A O     1 
ATOM   8223 N  N     . GLY A 1 1152 ? 117.641 100.485 159.449 1.00 45.64  ? 1152 GLY A N     1 
ATOM   8224 C  CA    . GLY A 1 1152 ? 118.850 100.562 160.252 1.00 45.64  ? 1152 GLY A CA    1 
ATOM   8225 C  C     . GLY A 1 1152 ? 120.098 100.264 159.446 1.00 45.64  ? 1152 GLY A C     1 
ATOM   8226 O  O     . GLY A 1 1152 ? 121.105 100.967 159.554 1.00 45.64  ? 1152 GLY A O     1 
ATOM   8227 N  N     . GLN A 1 1153 ? 120.046 99.220  158.616 1.00 40.62  ? 1153 GLN A N     1 
ATOM   8228 C  CA    . GLN A 1 1153 ? 121.202 98.874  157.795 1.00 40.62  ? 1153 GLN A CA    1 
ATOM   8229 C  C     . GLN A 1 1153 ? 121.484 99.948  156.749 1.00 40.62  ? 1153 GLN A C     1 
ATOM   8230 O  O     . GLN A 1 1153 ? 122.648 100.280 156.491 1.00 40.62  ? 1153 GLN A O     1 
ATOM   8231 C  CB    . GLN A 1 1153 ? 120.985 97.513  157.137 1.00 40.62  ? 1153 GLN A CB    1 
ATOM   8232 C  CG    . GLN A 1 1153 ? 121.153 96.344  158.096 1.00 40.62  ? 1153 GLN A CG    1 
ATOM   8233 C  CD    . GLN A 1 1153 ? 120.353 95.126  157.686 1.00 40.62  ? 1153 GLN A CD    1 
ATOM   8234 O  OE1   . GLN A 1 1153 ? 119.368 95.232  156.959 1.00 40.62  ? 1153 GLN A OE1   1 
ATOM   8235 N  NE2   . GLN A 1 1153 ? 120.772 93.959  158.158 1.00 40.62  ? 1153 GLN A NE2   1 
ATOM   8236 N  N     . LYS A 1 1154 ? 120.433 100.506 156.141 1.00 35.75  ? 1154 LYS A N     1 
ATOM   8237 C  CA    . LYS A 1 1154 ? 120.627 101.592 155.186 1.00 35.75  ? 1154 LYS A CA    1 
ATOM   8238 C  C     . LYS A 1 1154 ? 121.285 102.792 155.850 1.00 35.75  ? 1154 LYS A C     1 
ATOM   8239 O  O     . LYS A 1 1154 ? 122.204 103.401 155.288 1.00 35.75  ? 1154 LYS A O     1 
ATOM   8240 C  CB    . LYS A 1 1154 ? 119.289 102.002 154.576 1.00 35.75  ? 1154 LYS A CB    1 
ATOM   8241 C  CG    . LYS A 1 1154 ? 118.716 101.014 153.591 1.00 35.75  ? 1154 LYS A CG    1 
ATOM   8242 C  CD    . LYS A 1 1154 ? 117.207 101.133 153.550 1.00 35.75  ? 1154 LYS A CD    1 
ATOM   8243 C  CE    . LYS A 1 1154 ? 116.778 102.538 153.166 1.00 35.75  ? 1154 LYS A CE    1 
ATOM   8244 N  NZ    . LYS A 1 1154 ? 115.301 102.641 153.015 1.00 35.75  ? 1154 LYS A NZ    1 
ATOM   8245 N  N     . GLN A 1 1155 ? 120.828 103.144 157.051 1.00 43.01  ? 1155 GLN A N     1 
ATOM   8246 C  CA    . GLN A 1 1155 ? 121.403 104.288 157.743 1.00 43.01  ? 1155 GLN A CA    1 
ATOM   8247 C  C     . GLN A 1 1155 ? 122.838 104.012 158.175 1.00 43.01  ? 1155 GLN A C     1 
ATOM   8248 O  O     . GLN A 1 1155 ? 123.680 104.916 158.136 1.00 43.01  ? 1155 GLN A O     1 
ATOM   8249 C  CB    . GLN A 1 1155 ? 120.527 104.655 158.937 1.00 43.01  ? 1155 GLN A CB    1 
ATOM   8250 C  CG    . GLN A 1 1155 ? 120.770 106.040 159.479 1.00 43.01  ? 1155 GLN A CG    1 
ATOM   8251 C  CD    . GLN A 1 1155 ? 119.683 106.469 160.435 1.00 43.01  ? 1155 GLN A CD    1 
ATOM   8252 O  OE1   . GLN A 1 1155 ? 118.815 105.678 160.802 1.00 43.01  ? 1155 GLN A OE1   1 
ATOM   8253 N  NE2   . GLN A 1 1155 ? 119.707 107.734 160.825 1.00 43.01  ? 1155 GLN A NE2   1 
ATOM   8254 N  N     . ARG A 1 1156 ? 123.138 102.772 158.568 1.00 40.89  ? 1156 ARG A N     1 
ATOM   8255 C  CA    . ARG A 1 1156 ? 124.516 102.412 158.886 1.00 40.89  ? 1156 ARG A CA    1 
ATOM   8256 C  C     . ARG A 1 1156 ? 125.415 102.549 157.666 1.00 40.89  ? 1156 ARG A C     1 
ATOM   8257 O  O     . ARG A 1 1156 ? 126.537 103.058 157.767 1.00 40.89  ? 1156 ARG A O     1 
ATOM   8258 C  CB    . ARG A 1 1156 ? 124.576 100.986 159.432 1.00 40.89  ? 1156 ARG A CB    1 
ATOM   8259 C  CG    . ARG A 1 1156 ? 123.965 100.810 160.810 1.00 40.89  ? 1156 ARG A CG    1 
ATOM   8260 C  CD    . ARG A 1 1156 ? 123.944 99.343  161.202 1.00 40.89  ? 1156 ARG A CD    1 
ATOM   8261 N  NE    . ARG A 1 1156 ? 123.213 99.110  162.442 1.00 40.89  ? 1156 ARG A NE    1 
ATOM   8262 C  CZ    . ARG A 1 1156 ? 122.980 97.906  162.952 1.00 40.89  ? 1156 ARG A CZ    1 
ATOM   8263 N  NH1   . ARG A 1 1156 ? 123.423 96.824  162.327 1.00 40.89  ? 1156 ARG A NH1   1 
ATOM   8264 N  NH2   . ARG A 1 1156 ? 122.305 97.781  164.085 1.00 40.89  ? 1156 ARG A NH2   1 
ATOM   8265 N  N     . ILE A 1 1157 ? 124.940 102.102 156.501 1.00 33.00  ? 1157 ILE A N     1 
ATOM   8266 C  CA    . ILE A 1 1157 ? 125.737 102.225 155.283 1.00 33.00  ? 1157 ILE A CA    1 
ATOM   8267 C  C     . ILE A 1 1157 ? 125.949 103.692 154.928 1.00 33.00  ? 1157 ILE A C     1 
ATOM   8268 O  O     . ILE A 1 1157 ? 127.042 104.095 154.505 1.00 33.00  ? 1157 ILE A O     1 
ATOM   8269 C  CB    . ILE A 1 1157 ? 125.075 101.447 154.131 1.00 33.00  ? 1157 ILE A CB    1 
ATOM   8270 C  CG1   . ILE A 1 1157 ? 125.244 99.943  154.343 1.00 33.00  ? 1157 ILE A CG1   1 
ATOM   8271 C  CG2   . ILE A 1 1157 ? 125.681 101.842 152.803 1.00 33.00  ? 1157 ILE A CG2   1 
ATOM   8272 C  CD1   . ILE A 1 1157 ? 124.195 99.110  153.647 1.00 33.00  ? 1157 ILE A CD1   1 
ATOM   8273 N  N     . ALA A 1 1158 ? 124.910 104.515 155.089 1.00 31.74  ? 1158 ALA A N     1 
ATOM   8274 C  CA    . ALA A 1 1158 ? 125.050 105.942 154.809 1.00 31.74  ? 1158 ALA A CA    1 
ATOM   8275 C  C     . ALA A 1 1158 ? 126.066 106.596 155.739 1.00 31.74  ? 1158 ALA A C     1 
ATOM   8276 O  O     . ALA A 1 1158 ? 126.891 107.408 155.300 1.00 31.74  ? 1158 ALA A O     1 
ATOM   8277 C  CB    . ALA A 1 1158 ? 123.695 106.637 154.922 1.00 31.74  ? 1158 ALA A CB    1 
ATOM   8278 N  N     . ILE A 1 1159 ? 126.024 106.254 157.028 1.00 31.46  ? 1159 ILE A N     1 
ATOM   8279 C  CA    . ILE A 1 1159 ? 126.995 106.804 157.970 1.00 31.46  ? 1159 ILE A CA    1 
ATOM   8280 C  C     . ILE A 1 1159 ? 128.401 106.325 157.628 1.00 31.46  ? 1159 ILE A C     1 
ATOM   8281 O  O     . ILE A 1 1159 ? 129.377 107.074 157.760 1.00 31.46  ? 1159 ILE A O     1 
ATOM   8282 C  CB    . ILE A 1 1159 ? 126.603 106.442 159.414 1.00 31.46  ? 1159 ILE A CB    1 
ATOM   8283 C  CG1   . ILE A 1 1159 ? 125.290 107.125 159.795 1.00 31.46  ? 1159 ILE A CG1   1 
ATOM   8284 C  CG2   . ILE A 1 1159 ? 127.696 106.847 160.386 1.00 31.46  ? 1159 ILE A CG2   1 
ATOM   8285 C  CD1   . ILE A 1 1159 ? 124.740 106.675 161.129 1.00 31.46  ? 1159 ILE A CD1   1 
ATOM   8286 N  N     . ALA A 1 1160 ? 128.527 105.073 157.181 1.00 31.60  ? 1160 ALA A N     1 
ATOM   8287 C  CA    . ALA A 1 1160 ? 129.830 104.566 156.763 1.00 31.60  ? 1160 ALA A CA    1 
ATOM   8288 C  C     . ALA A 1 1160 ? 130.370 105.349 155.574 1.00 31.60  ? 1160 ALA A C     1 
ATOM   8289 O  O     . ALA A 1 1160 ? 131.555 105.694 155.536 1.00 31.60  ? 1160 ALA A O     1 
ATOM   8290 C  CB    . ALA A 1 1160 ? 129.732 103.079 156.426 1.00 31.60  ? 1160 ALA A CB    1 
ATOM   8291 N  N     . ARG A 1 1161 ? 129.514 105.644 154.595 1.00 26.21  ? 1161 ARG A N     1 
ATOM   8292 C  CA    . ARG A 1 1161 ? 129.949 106.454 153.461 1.00 26.21  ? 1161 ARG A CA    1 
ATOM   8293 C  C     . ARG A 1 1161 ? 130.370 107.848 153.912 1.00 26.21  ? 1161 ARG A C     1 
ATOM   8294 O  O     . ARG A 1 1161 ? 131.404 108.372 153.470 1.00 26.21  ? 1161 ARG A O     1 
ATOM   8295 C  CB    . ARG A 1 1161 ? 128.832 106.540 152.421 1.00 26.21  ? 1161 ARG A CB    1 
ATOM   8296 C  CG    . ARG A 1 1161 ? 128.850 107.810 151.593 1.00 26.21  ? 1161 ARG A CG    1 
ATOM   8297 C  CD    . ARG A 1 1161 ? 127.460 108.162 151.095 1.00 26.21  ? 1161 ARG A CD    1 
ATOM   8298 N  NE    . ARG A 1 1161 ? 126.913 107.133 150.218 1.00 26.21  ? 1161 ARG A NE    1 
ATOM   8299 C  CZ    . ARG A 1 1161 ? 125.750 107.235 149.585 1.00 26.21  ? 1161 ARG A CZ    1 
ATOM   8300 N  NH1   . ARG A 1 1161 ? 125.007 108.322 149.733 1.00 26.21  ? 1161 ARG A NH1   1 
ATOM   8301 N  NH2   . ARG A 1 1161 ? 125.329 106.251 148.804 1.00 26.21  ? 1161 ARG A NH2   1 
ATOM   8302 N  N     . ALA A 1 1162 ? 129.589 108.455 154.809 1.00 29.25  ? 1162 ALA A N     1 
ATOM   8303 C  CA    . ALA A 1 1162 ? 129.906 109.800 155.278 1.00 29.25  ? 1162 ALA A CA    1 
ATOM   8304 C  C     . ALA A 1 1162 ? 131.241 109.836 156.010 1.00 29.25  ? 1162 ALA A C     1 
ATOM   8305 O  O     . ALA A 1 1162 ? 132.029 110.772 155.830 1.00 29.25  ? 1162 ALA A O     1 
ATOM   8306 C  CB    . ALA A 1 1162 ? 128.787 110.321 156.179 1.00 29.25  ? 1162 ALA A CB    1 
ATOM   8307 N  N     . VAL A 1 1163 ? 131.515 108.833 156.845 1.00 30.47  ? 1163 VAL A N     1 
ATOM   8308 C  CA    . VAL A 1 1163 ? 132.787 108.826 157.561 1.00 30.47  ? 1163 VAL A CA    1 
ATOM   8309 C  C     . VAL A 1 1163 ? 133.933 108.450 156.626 1.00 30.47  ? 1163 VAL A C     1 
ATOM   8310 O  O     . VAL A 1 1163 ? 135.076 108.868 156.843 1.00 30.47  ? 1163 VAL A O     1 
ATOM   8311 C  CB    . VAL A 1 1163 ? 132.724 107.898 158.789 1.00 30.47  ? 1163 VAL A CB    1 
ATOM   8312 C  CG1   . VAL A 1 1163 ? 132.536 106.454 158.375 1.00 30.47  ? 1163 VAL A CG1   1 
ATOM   8313 C  CG2   . VAL A 1 1163 ? 133.970 108.056 159.649 1.00 30.47  ? 1163 VAL A CG2   1 
ATOM   8314 N  N     . LEU A 1 1164 ? 133.659 107.674 155.573 1.00 30.82  ? 1164 LEU A N     1 
ATOM   8315 C  CA    . LEU A 1 1164 ? 134.692 107.391 154.583 1.00 30.82  ? 1164 LEU A CA    1 
ATOM   8316 C  C     . LEU A 1 1164 ? 135.105 108.656 153.846 1.00 30.82  ? 1164 LEU A C     1 
ATOM   8317 O  O     . LEU A 1 1164 ? 136.290 108.851 153.551 1.00 30.82  ? 1164 LEU A O     1 
ATOM   8318 C  CB    . LEU A 1 1164 ? 134.206 106.334 153.592 1.00 30.82  ? 1164 LEU A CB    1 
ATOM   8319 C  CG    . LEU A 1 1164 ? 135.193 105.998 152.472 1.00 30.82  ? 1164 LEU A CG    1 
ATOM   8320 C  CD1   . LEU A 1 1164 ? 136.539 105.595 153.049 1.00 30.82  ? 1164 LEU A CD1   1 
ATOM   8321 C  CD2   . LEU A 1 1164 ? 134.645 104.907 151.573 1.00 30.82  ? 1164 LEU A CD2   1 
ATOM   8322 N  N     . LYS A 1 1165 ? 134.141 109.526 153.533 1.00 32.44  ? 1165 LYS A N     1 
ATOM   8323 C  CA    . LYS A 1 1165 ? 134.489 110.787 152.884 1.00 32.44  ? 1165 LYS A CA    1 
ATOM   8324 C  C     . LYS A 1 1165 ? 135.417 111.618 153.762 1.00 32.44  ? 1165 LYS A C     1 
ATOM   8325 O  O     . LYS A 1 1165 ? 136.348 112.259 153.261 1.00 32.44  ? 1165 LYS A O     1 
ATOM   8326 C  CB    . LYS A 1 1165 ? 133.230 111.580 152.541 1.00 32.44  ? 1165 LYS A CB    1 
ATOM   8327 C  CG    . LYS A 1 1165 ? 133.522 112.877 151.803 1.00 32.44  ? 1165 LYS A CG    1 
ATOM   8328 C  CD    . LYS A 1 1165 ? 132.256 113.651 151.503 1.00 32.44  ? 1165 LYS A CD    1 
ATOM   8329 C  CE    . LYS A 1 1165 ? 132.568 114.937 150.761 1.00 32.44  ? 1165 LYS A CE    1 
ATOM   8330 N  NZ    . LYS A 1 1165 ? 131.342 115.739 150.502 1.00 32.44  ? 1165 LYS A NZ    1 
ATOM   8331 N  N     . ASN A 1 1166 ? 135.176 111.617 155.074 1.00 37.76  ? 1166 ASN A N     1 
ATOM   8332 C  CA    . ASN A 1 1166 ? 136.011 112.295 156.060 1.00 37.76  ? 1166 ASN A CA    1 
ATOM   8333 C  C     . ASN A 1 1166 ? 136.126 113.785 155.758 1.00 37.76  ? 1166 ASN A C     1 
ATOM   8334 O  O     . ASN A 1 1166 ? 137.199 114.256 155.359 1.00 37.76  ? 1166 ASN A O     1 
ATOM   8335 C  CB    . ASN A 1 1166 ? 137.400 111.655 156.115 1.00 37.76  ? 1166 ASN A CB    1 
ATOM   8336 C  CG    . ASN A 1 1166 ? 138.221 112.145 157.288 1.00 37.76  ? 1166 ASN A CG    1 
ATOM   8337 O  OD1   . ASN A 1 1166 ? 137.790 112.069 158.437 1.00 37.76  ? 1166 ASN A OD1   1 
ATOM   8338 N  ND2   . ASN A 1 1166 ? 139.413 112.655 157.002 1.00 37.76  ? 1166 ASN A ND2   1 
ATOM   8339 N  N     . PRO A 1 1167 ? 135.056 114.555 155.927 1.00 39.97  ? 1167 PRO A N     1 
ATOM   8340 C  CA    . PRO A 1 1167 ? 135.122 115.993 155.667 1.00 39.97  ? 1167 PRO A CA    1 
ATOM   8341 C  C     . PRO A 1 1167 ? 135.546 116.781 156.899 1.00 39.97  ? 1167 PRO A C     1 
ATOM   8342 O  O     . PRO A 1 1167 ? 135.498 116.300 158.032 1.00 39.97  ? 1167 PRO A O     1 
ATOM   8343 C  CB    . PRO A 1 1167 ? 133.678 116.335 155.276 1.00 39.97  ? 1167 PRO A CB    1 
ATOM   8344 C  CG    . PRO A 1 1167 ? 132.842 115.328 156.018 1.00 39.97  ? 1167 PRO A CG    1 
ATOM   8345 C  CD    . PRO A 1 1167 ? 133.716 114.144 156.378 1.00 39.97  ? 1167 PRO A CD    1 
ATOM   8346 N  N     . THR A 1 1168 ? 135.975 118.020 156.648 1.00 43.81  ? 1168 THR A N     1 
ATOM   8347 C  CA    . THR A 1 1168 ? 136.345 118.906 157.747 1.00 43.81  ? 1168 THR A CA    1 
ATOM   8348 C  C     . THR A 1 1168 ? 135.125 119.306 158.566 1.00 43.81  ? 1168 THR A C     1 
ATOM   8349 O  O     . THR A 1 1168 ? 135.207 119.425 159.794 1.00 43.81  ? 1168 THR A O     1 
ATOM   8350 C  CB    . THR A 1 1168 ? 137.056 120.145 157.210 1.00 43.81  ? 1168 THR A CB    1 
ATOM   8351 O  OG1   . THR A 1 1168 ? 136.241 120.766 156.208 1.00 43.81  ? 1168 THR A OG1   1 
ATOM   8352 C  CG2   . THR A 1 1168 ? 138.395 119.765 156.600 1.00 43.81  ? 1168 THR A CG2   1 
ATOM   8353 N  N     . VAL A 1 1169 ? 133.991 119.523 157.907 1.00 43.87  ? 1169 VAL A N     1 
ATOM   8354 C  CA    . VAL A 1 1169 ? 132.734 119.859 158.565 1.00 43.87  ? 1169 VAL A CA    1 
ATOM   8355 C  C     . VAL A 1 1169 ? 131.738 118.754 158.251 1.00 43.87  ? 1169 VAL A C     1 
ATOM   8356 O  O     . VAL A 1 1169 ? 131.467 118.472 157.077 1.00 43.87  ? 1169 VAL A O     1 
ATOM   8357 C  CB    . VAL A 1 1169 ? 132.199 121.225 158.111 1.00 43.87  ? 1169 VAL A CB    1 
ATOM   8358 C  CG1   . VAL A 1 1169 ? 131.081 121.688 159.027 1.00 43.87  ? 1169 VAL A CG1   1 
ATOM   8359 C  CG2   . VAL A 1 1169 ? 133.320 122.248 158.072 1.00 43.87  ? 1169 VAL A CG2   1 
ATOM   8360 N  N     . LEU A 1 1170 ? 131.194 118.131 159.293 1.00 45.12  ? 1170 LEU A N     1 
ATOM   8361 C  CA    . LEU A 1 1170 ? 130.260 117.018 159.146 1.00 45.12  ? 1170 LEU A CA    1 
ATOM   8362 C  C     . LEU A 1 1170 ? 128.858 117.537 159.442 1.00 45.12  ? 1170 LEU A C     1 
ATOM   8363 O  O     . LEU A 1 1170 ? 128.452 117.632 160.602 1.00 45.12  ? 1170 LEU A O     1 
ATOM   8364 C  CB    . LEU A 1 1170 ? 130.639 115.870 160.075 1.00 45.12  ? 1170 LEU A CB    1 
ATOM   8365 C  CG    . LEU A 1 1170 ? 129.786 114.606 159.969 1.00 45.12  ? 1170 LEU A CG    1 
ATOM   8366 C  CD1   . LEU A 1 1170 ? 129.763 114.093 158.539 1.00 45.12  ? 1170 LEU A CD1   1 
ATOM   8367 C  CD2   . LEU A 1 1170 ? 130.301 113.537 160.916 1.00 45.12  ? 1170 LEU A CD2   1 
ATOM   8368 N  N     . LEU A 1 1171 ? 128.113 117.867 158.386 1.00 43.76  ? 1171 LEU A N     1 
ATOM   8369 C  CA    . LEU A 1 1171 ? 126.762 118.407 158.534 1.00 43.76  ? 1171 LEU A CA    1 
ATOM   8370 C  C     . LEU A 1 1171 ? 125.807 117.269 158.898 1.00 43.76  ? 1171 LEU A C     1 
ATOM   8371 O  O     . LEU A 1 1171 ? 125.006 116.791 158.093 1.00 43.76  ? 1171 LEU A O     1 
ATOM   8372 C  CB    . LEU A 1 1171 ? 126.322 119.116 157.262 1.00 43.76  ? 1171 LEU A CB    1 
ATOM   8373 C  CG    . LEU A 1 1171 ? 127.056 120.387 156.831 1.00 43.76  ? 1171 LEU A CG    1 
ATOM   8374 C  CD1   . LEU A 1 1171 ? 126.544 120.840 155.473 1.00 43.76  ? 1171 LEU A CD1   1 
ATOM   8375 C  CD2   . LEU A 1 1171 ? 126.914 121.495 157.857 1.00 43.76  ? 1171 LEU A CD2   1 
ATOM   8376 N  N     . LEU A 1 1172 ? 125.907 116.835 160.150 1.00 51.95  ? 1172 LEU A N     1 
ATOM   8377 C  CA    . LEU A 1 1172 ? 125.068 115.752 160.634 1.00 51.95  ? 1172 LEU A CA    1 
ATOM   8378 C  C     . LEU A 1 1172 ? 123.634 116.234 160.833 1.00 51.95  ? 1172 LEU A C     1 
ATOM   8379 O  O     . LEU A 1 1172 ? 123.356 117.433 160.917 1.00 51.95  ? 1172 LEU A O     1 
ATOM   8380 C  CB    . LEU A 1 1172 ? 125.625 115.188 161.942 1.00 51.95  ? 1172 LEU A CB    1 
ATOM   8381 C  CG    . LEU A 1 1172 ? 125.395 113.702 162.222 1.00 51.95  ? 1172 LEU A CG    1 
ATOM   8382 C  CD1   . LEU A 1 1172 ? 126.079 112.849 161.171 1.00 51.95  ? 1172 LEU A CD1   1 
ATOM   8383 C  CD2   . LEU A 1 1172 ? 125.899 113.339 163.607 1.00 51.95  ? 1172 LEU A CD2   1 
ATOM   8384 N  N     . ASP A 1 1173 ? 122.717 115.277 160.902 1.00 56.10  ? 1173 ASP A N     1 
ATOM   8385 C  CA    . ASP A 1 1173 ? 121.304 115.567 161.117 1.00 56.10  ? 1173 ASP A CA    1 
ATOM   8386 C  C     . ASP A 1 1173 ? 120.706 114.404 161.902 1.00 56.10  ? 1173 ASP A C     1 
ATOM   8387 O  O     . ASP A 1 1173 ? 121.433 113.635 162.539 1.00 56.10  ? 1173 ASP A O     1 
ATOM   8388 C  CB    . ASP A 1 1173 ? 120.588 115.828 159.781 1.00 56.10  ? 1173 ASP A CB    1 
ATOM   8389 C  CG    . ASP A 1 1173 ? 120.592 114.622 158.871 1.00 56.10  ? 1173 ASP A CG    1 
ATOM   8390 O  OD1   . ASP A 1 1173 ? 121.365 113.677 159.132 1.00 56.10  ? 1173 ASP A OD1   1 
ATOM   8391 O  OD2   . ASP A 1 1173 ? 119.821 114.619 157.888 1.00 56.10  ? 1173 ASP A OD2   1 
ATOM   8392 N  N     . GLU A 1 1174 ? 119.378 114.282 161.867 1.00 60.50  ? 1174 GLU A N     1 
ATOM   8393 C  CA    . GLU A 1 1174 ? 118.685 113.238 162.613 1.00 60.50  ? 1174 GLU A CA    1 
ATOM   8394 C  C     . GLU A 1 1174 ? 119.228 111.866 162.240 1.00 60.50  ? 1174 GLU A C     1 
ATOM   8395 O  O     . GLU A 1 1174 ? 119.027 111.391 161.117 1.00 60.50  ? 1174 GLU A O     1 
ATOM   8396 C  CB    . GLU A 1 1174 ? 117.179 113.308 162.354 1.00 60.50  ? 1174 GLU A CB    1 
ATOM   8397 C  CG    . GLU A 1 1174 ? 116.385 112.169 162.969 1.00 60.50  ? 1174 GLU A CG    1 
ATOM   8398 C  CD    . GLU A 1 1174 ? 116.289 112.276 164.478 1.00 60.50  ? 1174 GLU A CD    1 
ATOM   8399 O  OE1   . GLU A 1 1174 ? 116.322 113.410 164.996 1.00 60.50  ? 1174 GLU A OE1   1 
ATOM   8400 O  OE2   . GLU A 1 1174 ? 116.179 111.226 165.145 1.00 60.50  ? 1174 GLU A OE2   1 
ATOM   8401 N  N     . ALA A 1 1175 ? 119.917 111.225 163.181 1.00 64.36  ? 1175 ALA A N     1 
ATOM   8402 C  CA    . ALA A 1 1175 ? 120.593 109.962 162.934 1.00 64.36  ? 1175 ALA A CA    1 
ATOM   8403 C  C     . ALA A 1 1175 ? 120.023 108.793 163.719 1.00 64.36  ? 1175 ALA A C     1 
ATOM   8404 O  O     . ALA A 1 1175 ? 120.044 107.668 163.217 1.00 64.36  ? 1175 ALA A O     1 
ATOM   8405 C  CB    . ALA A 1 1175 ? 122.091 110.087 163.253 1.00 64.36  ? 1175 ALA A CB    1 
ATOM   8406 N  N     . THR A 1 1176 ? 119.517 109.021 164.928 1.00 70.91  ? 1176 THR A N     1 
ATOM   8407 C  CA    . THR A 1 1176 ? 118.951 107.947 165.743 1.00 70.91  ? 1176 THR A CA    1 
ATOM   8408 C  C     . THR A 1 1176 ? 117.456 107.794 165.458 1.00 70.91  ? 1176 THR A C     1 
ATOM   8409 O  O     . THR A 1 1176 ? 116.601 107.929 166.332 1.00 70.91  ? 1176 THR A O     1 
ATOM   8410 C  CB    . THR A 1 1176 ? 119.213 108.213 167.220 1.00 70.91  ? 1176 THR A CB    1 
ATOM   8411 O  OG1   . THR A 1 1176 ? 118.633 109.470 167.591 1.00 70.91  ? 1176 THR A OG1   1 
ATOM   8412 C  CG2   . THR A 1 1176 ? 120.707 108.253 167.493 1.00 70.91  ? 1176 THR A CG2   1 
ATOM   8413 N  N     . SER A 1 1177 ? 117.152 107.502 164.194 1.00 61.67  ? 1177 SER A N     1 
ATOM   8414 C  CA    . SER A 1 1177 ? 115.775 107.323 163.747 1.00 61.67  ? 1177 SER A CA    1 
ATOM   8415 C  C     . SER A 1 1177 ? 115.391 105.849 163.676 1.00 61.67  ? 1177 SER A C     1 
ATOM   8416 O  O     . SER A 1 1177 ? 114.430 105.420 164.321 1.00 61.67  ? 1177 SER A O     1 
ATOM   8417 C  CB    . SER A 1 1177 ? 115.575 107.994 162.383 1.00 61.67  ? 1177 SER A CB    1 
ATOM   8418 O  OG    . SER A 1 1177 ? 116.652 107.700 161.511 1.00 61.67  ? 1177 SER A OG    1 
ATOM   8419 N  N     . ALA A 1 1178 ? 116.131 105.062 162.898 1.00 61.94  ? 1178 ALA A N     1 
ATOM   8420 C  CA    . ALA A 1 1178 ? 115.871 103.638 162.748 1.00 61.94  ? 1178 ALA A CA    1 
ATOM   8421 C  C     . ALA A 1 1178 ? 116.914 102.772 163.444 1.00 61.94  ? 1178 ALA A C     1 
ATOM   8422 O  O     . ALA A 1 1178 ? 116.942 101.558 163.225 1.00 61.94  ? 1178 ALA A O     1 
ATOM   8423 C  CB    . ALA A 1 1178 ? 115.792 103.270 161.266 1.00 61.94  ? 1178 ALA A CB    1 
ATOM   8424 N  N     . LEU A 1 1179 ? 117.770 103.366 164.273 1.00 68.72  ? 1179 LEU A N     1 
ATOM   8425 C  CA    . LEU A 1 1179 ? 118.823 102.640 164.969 1.00 68.72  ? 1179 LEU A CA    1 
ATOM   8426 C  C     . LEU A 1 1179 ? 118.506 102.402 166.439 1.00 68.72  ? 1179 LEU A C     1 
ATOM   8427 O  O     . LEU A 1 1179 ? 119.412 102.072 167.210 1.00 68.72  ? 1179 LEU A O     1 
ATOM   8428 C  CB    . LEU A 1 1179 ? 120.152 103.387 164.845 1.00 68.72  ? 1179 LEU A CB    1 
ATOM   8429 C  CG    . LEU A 1 1179 ? 120.757 103.493 163.446 1.00 68.72  ? 1179 LEU A CG    1 
ATOM   8430 C  CD1   . LEU A 1 1179 ? 121.994 104.377 163.469 1.00 68.72  ? 1179 LEU A CD1   1 
ATOM   8431 C  CD2   . LEU A 1 1179 ? 121.090 102.114 162.902 1.00 68.72  ? 1179 LEU A CD2   1 
ATOM   8432 N  N     . ASP A 1 1180 ? 117.248 102.558 166.847 1.00 80.35  ? 1180 ASP A N     1 
ATOM   8433 C  CA    . ASP A 1 1180 ? 116.884 102.380 168.247 1.00 80.35  ? 1180 ASP A CA    1 
ATOM   8434 C  C     . ASP A 1 1180 ? 116.895 100.902 168.616 1.00 80.35  ? 1180 ASP A C     1 
ATOM   8435 O  O     . ASP A 1 1180 ? 115.838 100.281 168.763 1.00 80.35  ? 1180 ASP A O     1 
ATOM   8436 C  CB    . ASP A 1 1180 ? 115.511 102.995 168.528 1.00 80.35  ? 1180 ASP A CB    1 
ATOM   8437 C  CG    . ASP A 1 1180 ? 115.178 103.028 170.007 1.00 80.35  ? 1180 ASP A CG    1 
ATOM   8438 O  OD1   . ASP A 1 1180 ? 115.749 103.873 170.728 1.00 80.35  ? 1180 ASP A OD1   1 
ATOM   8439 O  OD2   . ASP A 1 1180 ? 114.347 102.208 170.449 1.00 80.35  ? 1180 ASP A OD2   1 
ATOM   8440 N  N     . ALA A 1 1181 ? 118.086 100.336 168.767 1.00 90.41  ? 1181 ALA A N     1 
ATOM   8441 C  CA    . ALA A 1 1181 ? 118.244 98.919  169.066 1.00 90.41  ? 1181 ALA A CA    1 
ATOM   8442 C  C     . ALA A 1 1181 ? 119.513 98.754  169.896 1.00 90.41  ? 1181 ALA A C     1 
ATOM   8443 O  O     . ALA A 1 1181 ? 120.035 99.725  170.452 1.00 90.41  ? 1181 ALA A O     1 
ATOM   8444 C  CB    . ALA A 1 1181 ? 118.262 98.093  167.769 1.00 90.41  ? 1181 ALA A CB    1 
ATOM   8445 N  N     . GLU A 1 1182 ? 120.018 97.520  169.971 1.00 99.77  ? 1182 GLU A N     1 
ATOM   8446 C  CA    . GLU A 1 1182 ? 121.204 97.220  170.765 1.00 99.77  ? 1182 GLU A CA    1 
ATOM   8447 C  C     . GLU A 1 1182 ? 122.459 97.904  170.242 1.00 99.77  ? 1182 GLU A C     1 
ATOM   8448 O  O     . GLU A 1 1182 ? 123.475 97.913  170.945 1.00 99.77  ? 1182 GLU A O     1 
ATOM   8449 C  CB    . GLU A 1 1182 ? 121.433 95.708  170.814 1.00 99.77  ? 1182 GLU A CB    1 
ATOM   8450 C  CG    . GLU A 1 1182 ? 120.464 94.960  171.711 1.00 99.77  ? 1182 GLU A CG    1 
ATOM   8451 C  CD    . GLU A 1 1182 ? 119.244 94.463  170.963 1.00 99.77  ? 1182 GLU A CD    1 
ATOM   8452 O  OE1   . GLU A 1 1182 ? 119.109 94.785  169.764 1.00 99.77  ? 1182 GLU A OE1   1 
ATOM   8453 O  OE2   . GLU A 1 1182 ? 118.423 93.746  171.571 1.00 99.77  ? 1182 GLU A OE2   1 
ATOM   8454 N  N     . SER A 1 1183 ? 122.426 98.455  169.033 1.00 89.19  ? 1183 SER A N     1 
ATOM   8455 C  CA    . SER A 1 1183 ? 123.568 99.161  168.473 1.00 89.19  ? 1183 SER A CA    1 
ATOM   8456 C  C     . SER A 1 1183 ? 123.581 100.644 168.819 1.00 89.19  ? 1183 SER A C     1 
ATOM   8457 O  O     . SER A 1 1183 ? 124.517 101.345 168.426 1.00 89.19  ? 1183 SER A O     1 
ATOM   8458 C  CB    . SER A 1 1183 ? 123.593 98.991  166.951 1.00 89.19  ? 1183 SER A CB    1 
ATOM   8459 O  OG    . SER A 1 1183 ? 122.449 99.578  166.356 1.00 89.19  ? 1183 SER A OG    1 
ATOM   8460 N  N     . GLU A 1 1184 ? 122.579 101.135 169.553 1.00 95.40  ? 1184 GLU A N     1 
ATOM   8461 C  CA    . GLU A 1 1184 ? 122.463 102.571 169.787 1.00 95.40  ? 1184 GLU A CA    1 
ATOM   8462 C  C     . GLU A 1 1184 ? 123.666 103.112 170.553 1.00 95.40  ? 1184 GLU A C     1 
ATOM   8463 O  O     . GLU A 1 1184 ? 124.193 104.181 170.225 1.00 95.40  ? 1184 GLU A O     1 
ATOM   8464 C  CB    . GLU A 1 1184 ? 121.165 102.874 170.536 1.00 95.40  ? 1184 GLU A CB    1 
ATOM   8465 C  CG    . GLU A 1 1184 ? 120.957 104.345 170.858 1.00 95.40  ? 1184 GLU A CG    1 
ATOM   8466 C  CD    . GLU A 1 1184 ? 120.911 105.217 169.618 1.00 95.40  ? 1184 GLU A CD    1 
ATOM   8467 O  OE1   . GLU A 1 1184 ? 119.801 105.455 169.097 1.00 95.40  ? 1184 GLU A OE1   1 
ATOM   8468 O  OE2   . GLU A 1 1184 ? 121.983 105.671 169.166 1.00 95.40  ? 1184 GLU A OE2   1 
ATOM   8469 N  N     . CYS A 1 1185 ? 124.114 102.385 171.580 1.00 95.79  ? 1185 CYS A N     1 
ATOM   8470 C  CA    . CYS A 1 1185 ? 125.252 102.847 172.370 1.00 95.79  ? 1185 CYS A CA    1 
ATOM   8471 C  C     . CYS A 1 1185 ? 126.532 102.873 171.544 1.00 95.79  ? 1185 CYS A C     1 
ATOM   8472 O  O     . CYS A 1 1185 ? 127.364 103.773 171.703 1.00 95.79  ? 1185 CYS A O     1 
ATOM   8473 C  CB    . CYS A 1 1185 ? 125.431 101.965 173.605 1.00 95.79  ? 1185 CYS A CB    1 
ATOM   8474 S  SG    . CYS A 1 1185 ? 126.503 102.672 174.880 1.00 95.79  ? 1185 CYS A SG    1 
ATOM   8475 N  N     . VAL A 1 1186 ? 126.717 101.883 170.668 1.00 91.11  ? 1186 VAL A N     1 
ATOM   8476 C  CA    . VAL A 1 1186 ? 127.947 101.806 169.885 1.00 91.11  ? 1186 VAL A CA    1 
ATOM   8477 C  C     . VAL A 1 1186 ? 128.022 102.952 168.883 1.00 91.11  ? 1186 VAL A C     1 
ATOM   8478 O  O     . VAL A 1 1186 ? 129.065 103.603 168.740 1.00 91.11  ? 1186 VAL A O     1 
ATOM   8479 C  CB    . VAL A 1 1186 ? 128.052 100.438 169.188 1.00 91.11  ? 1186 VAL A CB    1 
ATOM   8480 C  CG1   . VAL A 1 1186 ? 129.332 100.356 168.372 1.00 91.11  ? 1186 VAL A CG1   1 
ATOM   8481 C  CG2   . VAL A 1 1186 ? 127.993 99.319  170.213 1.00 91.11  ? 1186 VAL A CG2   1 
ATOM   8482 N  N     . LEU A 1 1187 ? 126.923 103.215 168.171 1.00 87.09  ? 1187 LEU A N     1 
ATOM   8483 C  CA    . LEU A 1 1187 ? 126.930 104.277 167.167 1.00 87.09  ? 1187 LEU A CA    1 
ATOM   8484 C  C     . LEU A 1 1187 ? 127.136 105.651 167.791 1.00 87.09  ? 1187 LEU A C     1 
ATOM   8485 O  O     . LEU A 1 1187 ? 127.861 106.480 167.233 1.00 87.09  ? 1187 LEU A O     1 
ATOM   8486 C  CB    . LEU A 1 1187 ? 125.643 104.252 166.340 1.00 87.09  ? 1187 LEU A CB    1 
ATOM   8487 C  CG    . LEU A 1 1187 ? 125.486 103.233 165.203 1.00 87.09  ? 1187 LEU A CG    1 
ATOM   8488 C  CD1   . LEU A 1 1187 ? 126.473 103.560 164.093 1.00 87.09  ? 1187 LEU A CD1   1 
ATOM   8489 C  CD2   . LEU A 1 1187 ? 125.659 101.792 165.640 1.00 87.09  ? 1187 LEU A CD2   1 
ATOM   8490 N  N     . GLN A 1 1188 ? 126.504 105.925 168.935 1.00 92.88  ? 1188 GLN A N     1 
ATOM   8491 C  CA    . GLN A 1 1188 ? 126.647 107.251 169.532 1.00 92.88  ? 1188 GLN A CA    1 
ATOM   8492 C  C     . GLN A 1 1188 ? 128.072 107.489 170.022 1.00 92.88  ? 1188 GLN A C     1 
ATOM   8493 O  O     . GLN A 1 1188 ? 128.612 108.590 169.860 1.00 92.88  ? 1188 GLN A O     1 
ATOM   8494 C  CB    . GLN A 1 1188 ? 125.629 107.444 170.660 1.00 92.88  ? 1188 GLN A CB    1 
ATOM   8495 C  CG    . GLN A 1 1188 ? 125.747 106.481 171.825 1.00 92.88  ? 1188 GLN A CG    1 
ATOM   8496 C  CD    . GLN A 1 1188 ? 126.567 107.045 172.967 1.00 92.88  ? 1188 GLN A CD    1 
ATOM   8497 O  OE1   . GLN A 1 1188 ? 126.957 108.213 172.950 1.00 92.88  ? 1188 GLN A OE1   1 
ATOM   8498 N  NE2   . GLN A 1 1188 ? 126.829 106.217 173.972 1.00 92.88  ? 1188 GLN A NE2   1 
ATOM   8499 N  N     . GLU A 1 1189 ? 128.706 106.466 170.602 1.00 91.39  ? 1189 GLU A N     1 
ATOM   8500 C  CA    . GLU A 1 1189 ? 130.099 106.605 171.019 1.00 91.39  ? 1189 GLU A CA    1 
ATOM   8501 C  C     . GLU A 1 1189 ? 131.016 106.804 169.819 1.00 91.39  ? 1189 GLU A C     1 
ATOM   8502 O  O     . GLU A 1 1189 ? 131.944 107.622 169.865 1.00 91.39  ? 1189 GLU A O     1 
ATOM   8503 C  CB    . GLU A 1 1189 ? 130.532 105.380 171.824 1.00 91.39  ? 1189 GLU A CB    1 
ATOM   8504 C  CG    . GLU A 1 1189 ? 129.873 105.266 173.185 1.00 91.39  ? 1189 GLU A CG    1 
ATOM   8505 C  CD    . GLU A 1 1189 ? 130.589 106.071 174.251 1.00 91.39  ? 1189 GLU A CD    1 
ATOM   8506 O  OE1   . GLU A 1 1189 ? 130.087 106.125 175.393 1.00 91.39  ? 1189 GLU A OE1   1 
ATOM   8507 O  OE2   . GLU A 1 1189 ? 131.654 106.650 173.948 1.00 91.39  ? 1189 GLU A OE2   1 
ATOM   8508 N  N     . ALA A 1 1190 ? 130.776 106.059 168.737 1.00 87.25  ? 1190 ALA A N     1 
ATOM   8509 C  CA    . ALA A 1 1190 ? 131.586 106.220 167.535 1.00 87.25  ? 1190 ALA A CA    1 
ATOM   8510 C  C     . ALA A 1 1190 ? 131.423 107.614 166.946 1.00 87.25  ? 1190 ALA A C     1 
ATOM   8511 O  O     . ALA A 1 1190 ? 132.401 108.231 166.512 1.00 87.25  ? 1190 ALA A O     1 
ATOM   8512 C  CB    . ALA A 1 1190 ? 131.217 105.153 166.506 1.00 87.25  ? 1190 ALA A CB    1 
ATOM   8513 N  N     . LEU A 1 1191 ? 130.191 108.127 166.923 1.00 84.61  ? 1191 LEU A N     1 
ATOM   8514 C  CA    . LEU A 1 1191 ? 129.956 109.480 166.432 1.00 84.61  ? 1191 LEU A CA    1 
ATOM   8515 C  C     . LEU A 1 1191 ? 130.647 110.512 167.312 1.00 84.61  ? 1191 LEU A C     1 
ATOM   8516 O  O     . LEU A 1 1191 ? 131.221 111.484 166.807 1.00 84.61  ? 1191 LEU A O     1 
ATOM   8517 C  CB    . LEU A 1 1191 ? 128.456 109.758 166.358 1.00 84.61  ? 1191 LEU A CB    1 
ATOM   8518 C  CG    . LEU A 1 1191 ? 127.671 109.011 165.278 1.00 84.61  ? 1191 LEU A CG    1 
ATOM   8519 C  CD1   . LEU A 1 1191 ? 126.178 109.250 165.445 1.00 84.61  ? 1191 LEU A CD1   1 
ATOM   8520 C  CD2   . LEU A 1 1191 ? 128.133 109.421 163.890 1.00 84.61  ? 1191 LEU A CD2   1 
ATOM   8521 N  N     . GLU A 1 1192 ? 130.596 110.322 168.633 1.00 84.75  ? 1192 GLU A N     1 
ATOM   8522 C  CA    . GLU A 1 1192 ? 131.268 111.248 169.539 1.00 84.75  ? 1192 GLU A CA    1 
ATOM   8523 C  C     . GLU A 1 1192 ? 132.772 111.237 169.308 1.00 84.75  ? 1192 GLU A C     1 
ATOM   8524 O  O     . GLU A 1 1192 ? 133.423 112.288 169.348 1.00 84.75  ? 1192 GLU A O     1 
ATOM   8525 C  CB    . GLU A 1 1192 ? 130.915 110.902 170.990 1.00 84.75  ? 1192 GLU A CB    1 
ATOM   8526 C  CG    . GLU A 1 1192 ? 131.322 111.941 172.041 1.00 84.75  ? 1192 GLU A CG    1 
ATOM   8527 C  CD    . GLU A 1 1192 ? 132.757 111.809 172.535 1.00 84.75  ? 1192 GLU A CD    1 
ATOM   8528 O  OE1   . GLU A 1 1192 ? 133.541 111.028 171.960 1.00 84.75  ? 1192 GLU A OE1   1 
ATOM   8529 O  OE2   . GLU A 1 1192 ? 133.105 112.501 173.514 1.00 84.75  ? 1192 GLU A OE2   1 
ATOM   8530 N  N     . ARG A 1 1193 ? 133.345 110.054 169.079 1.00 81.63  ? 1193 ARG A N     1 
ATOM   8531 C  CA    . ARG A 1 1193 ? 134.766 109.974 168.757 1.00 81.63  ? 1193 ARG A CA    1 
ATOM   8532 C  C     . ARG A 1 1193 ? 135.067 110.654 167.426 1.00 81.63  ? 1193 ARG A C     1 
ATOM   8533 O  O     . ARG A 1 1193 ? 136.094 111.328 167.280 1.00 81.63  ? 1193 ARG A O     1 
ATOM   8534 C  CB    . ARG A 1 1193 ? 135.214 108.513 168.727 1.00 81.63  ? 1193 ARG A CB    1 
ATOM   8535 C  CG    . ARG A 1 1193 ? 136.720 108.326 168.659 1.00 81.63  ? 1193 ARG A CG    1 
ATOM   8536 C  CD    . ARG A 1 1193 ? 137.097 106.853 168.705 1.00 81.63  ? 1193 ARG A CD    1 
ATOM   8537 N  NE    . ARG A 1 1193 ? 136.676 106.217 169.950 1.00 81.63  ? 1193 ARG A NE    1 
ATOM   8538 C  CZ    . ARG A 1 1193 ? 135.810 105.211 170.018 1.00 81.63  ? 1193 ARG A CZ    1 
ATOM   8539 N  NH1   . ARG A 1 1193 ? 135.483 104.692 171.193 1.00 81.63  ? 1193 ARG A NH1   1 
ATOM   8540 N  NH2   . ARG A 1 1193 ? 135.270 104.724 168.910 1.00 81.63  ? 1193 ARG A NH2   1 
ATOM   8541 N  N     . LEU A 1 1194 ? 134.182 110.481 166.441 1.00 75.91  ? 1194 LEU A N     1 
ATOM   8542 C  CA    . LEU A 1 1194 ? 134.397 111.066 165.120 1.00 75.91  ? 1194 LEU A CA    1 
ATOM   8543 C  C     . LEU A 1 1194 ? 134.361 112.588 165.168 1.00 75.91  ? 1194 LEU A C     1 
ATOM   8544 O  O     . LEU A 1 1194 ? 135.178 113.253 164.520 1.00 75.91  ? 1194 LEU A O     1 
ATOM   8545 C  CB    . LEU A 1 1194 ? 133.349 110.534 164.143 1.00 75.91  ? 1194 LEU A CB    1 
ATOM   8546 C  CG    . LEU A 1 1194 ? 133.357 111.102 162.723 1.00 75.91  ? 1194 LEU A CG    1 
ATOM   8547 C  CD1   . LEU A 1 1194 ? 134.701 110.862 162.057 1.00 75.91  ? 1194 LEU A CD1   1 
ATOM   8548 C  CD2   . LEU A 1 1194 ? 132.230 110.496 161.900 1.00 75.91  ? 1194 LEU A CD2   1 
ATOM   8549 N  N     . MET A 1 1195 ? 133.428 113.159 165.926 1.00 79.03  ? 1195 MET A N     1 
ATOM   8550 C  CA    . MET A 1 1195 ? 133.273 114.608 165.999 1.00 79.03  ? 1195 MET A CA    1 
ATOM   8551 C  C     . MET A 1 1195 ? 134.288 115.274 166.921 1.00 79.03  ? 1195 MET A C     1 
ATOM   8552 O  O     . MET A 1 1195 ? 134.106 116.446 167.269 1.00 79.03  ? 1195 MET A O     1 
ATOM   8553 C  CB    . MET A 1 1195 ? 131.844 114.963 166.433 1.00 79.03  ? 1195 MET A CB    1 
ATOM   8554 C  CG    . MET A 1 1195 ? 131.418 114.447 167.810 1.00 79.03  ? 1195 MET A CG    1 
ATOM   8555 S  SD    . MET A 1 1195 ? 131.998 115.380 169.243 1.00 79.03  ? 1195 MET A SD    1 
ATOM   8556 C  CE    . MET A 1 1195 ? 131.022 116.872 169.092 1.00 79.03  ? 1195 MET A CE    1 
ATOM   8557 N  N     . ARG A 1 1196 ? 135.350 114.565 167.312 1.00 77.41  ? 1196 ARG A N     1 
ATOM   8558 C  CA    . ARG A 1 1196 ? 136.337 115.146 168.216 1.00 77.41  ? 1196 ARG A CA    1 
ATOM   8559 C  C     . ARG A 1 1196 ? 137.022 116.354 167.588 1.00 77.41  ? 1196 ARG A C     1 
ATOM   8560 O  O     . ARG A 1 1196 ? 137.229 117.375 168.254 1.00 77.41  ? 1196 ARG A O     1 
ATOM   8561 C  CB    . ARG A 1 1196 ? 137.366 114.089 168.615 1.00 77.41  ? 1196 ARG A CB    1 
ATOM   8562 C  CG    . ARG A 1 1196 ? 138.457 114.602 169.539 1.00 77.41  ? 1196 ARG A CG    1 
ATOM   8563 C  CD    . ARG A 1 1196 ? 137.885 115.003 170.889 1.00 77.41  ? 1196 ARG A CD    1 
ATOM   8564 N  NE    . ARG A 1 1196 ? 137.345 113.857 171.615 1.00 77.41  ? 1196 ARG A NE    1 
ATOM   8565 C  CZ    . ARG A 1 1196 ? 136.583 113.952 172.700 1.00 77.41  ? 1196 ARG A CZ    1 
ATOM   8566 N  NH1   . ARG A 1 1196 ? 136.137 112.855 173.297 1.00 77.41  ? 1196 ARG A NH1   1 
ATOM   8567 N  NH2   . ARG A 1 1196 ? 136.266 115.143 173.189 1.00 77.41  ? 1196 ARG A NH2   1 
ATOM   8568 N  N     . GLY A 1 1197 ? 137.377 116.261 166.310 1.00 65.75  ? 1197 GLY A N     1 
ATOM   8569 C  CA    . GLY A 1 1197 ? 138.024 117.364 165.628 1.00 65.75  ? 1197 GLY A CA    1 
ATOM   8570 C  C     . GLY A 1 1197 ? 137.250 117.855 164.422 1.00 65.75  ? 1197 GLY A C     1 
ATOM   8571 O  O     . GLY A 1 1197 ? 137.842 118.218 163.402 1.00 65.75  ? 1197 GLY A O     1 
ATOM   8572 N  N     . ARG A 1 1198 ? 135.924 117.874 164.529 1.00 59.90  ? 1198 ARG A N     1 
ATOM   8573 C  CA    . ARG A 1 1198 ? 135.061 118.256 163.423 1.00 59.90  ? 1198 ARG A CA    1 
ATOM   8574 C  C     . ARG A 1 1198 ? 133.923 119.122 163.942 1.00 59.90  ? 1198 ARG A C     1 
ATOM   8575 O  O     . ARG A 1 1198 ? 133.564 119.072 165.121 1.00 59.90  ? 1198 ARG A O     1 
ATOM   8576 C  CB    . ARG A 1 1198 ? 134.500 117.025 162.700 1.00 59.90  ? 1198 ARG A CB    1 
ATOM   8577 C  CG    . ARG A 1 1198 ? 135.341 116.554 161.529 1.00 59.90  ? 1198 ARG A CG    1 
ATOM   8578 C  CD    . ARG A 1 1198 ? 134.832 115.229 160.985 1.00 59.90  ? 1198 ARG A CD    1 
ATOM   8579 N  NE    . ARG A 1 1198 ? 135.632 114.101 161.453 1.00 59.90  ? 1198 ARG A NE    1 
ATOM   8580 C  CZ    . ARG A 1 1198 ? 136.824 113.774 160.964 1.00 59.90  ? 1198 ARG A CZ    1 
ATOM   8581 N  NH1   . ARG A 1 1198 ? 137.361 114.487 159.984 1.00 59.90  ? 1198 ARG A NH1   1 
ATOM   8582 N  NH2   . ARG A 1 1198 ? 137.479 112.731 161.453 1.00 59.90  ? 1198 ARG A NH2   1 
ATOM   8583 N  N     . THR A 1 1199 ? 133.357 119.919 163.042 1.00 55.70  ? 1199 THR A N     1 
ATOM   8584 C  CA    . THR A 1 1199 ? 132.219 120.774 163.350 1.00 55.70  ? 1199 THR A CA    1 
ATOM   8585 C  C     . THR A 1 1199 ? 130.947 120.126 162.820 1.00 55.70  ? 1199 THR A C     1 
ATOM   8586 O  O     . THR A 1 1199 ? 130.861 119.801 161.631 1.00 55.70  ? 1199 THR A O     1 
ATOM   8587 C  CB    . THR A 1 1199 ? 132.399 122.163 162.739 1.00 55.70  ? 1199 THR A CB    1 
ATOM   8588 O  OG1   . THR A 1 1199 ? 133.668 122.699 163.135 1.00 55.70  ? 1199 THR A OG1   1 
ATOM   8589 C  CG2   . THR A 1 1199 ? 131.297 123.094 163.203 1.00 55.70  ? 1199 THR A CG2   1 
ATOM   8590 N  N     . THR A 1 1200 ? 129.960 119.948 163.697 1.00 60.12  ? 1200 THR A N     1 
ATOM   8591 C  CA    . THR A 1 1200 ? 128.740 119.230 163.359 1.00 60.12  ? 1200 THR A CA    1 
ATOM   8592 C  C     . THR A 1 1200 ? 127.519 120.083 163.669 1.00 60.12  ? 1200 THR A C     1 
ATOM   8593 O  O     . THR A 1 1200 ? 127.551 120.953 164.543 1.00 60.12  ? 1200 THR A O     1 
ATOM   8594 C  CB    . THR A 1 1200 ? 128.642 117.902 164.118 1.00 60.12  ? 1200 THR A CB    1 
ATOM   8595 O  OG1   . THR A 1 1200 ? 128.893 118.126 165.510 1.00 60.12  ? 1200 THR A OG1   1 
ATOM   8596 C  CG2   . THR A 1 1200 ? 129.657 116.906 163.579 1.00 60.12  ? 1200 THR A CG2   1 
ATOM   8597 N  N     . VAL A 1 1201 ? 126.438 119.823 162.935 1.00 59.28  ? 1201 VAL A N     1 
ATOM   8598 C  CA    . VAL A 1 1201 ? 125.188 120.557 163.094 1.00 59.28  ? 1201 VAL A CA    1 
ATOM   8599 C  C     . VAL A 1 1201 ? 124.046 119.578 163.328 1.00 59.28  ? 1201 VAL A C     1 
ATOM   8600 O  O     . VAL A 1 1201 ? 122.909 119.826 162.908 1.00 59.28  ? 1201 VAL A O     1 
ATOM   8601 C  CB    . VAL A 1 1201 ? 124.904 121.452 161.873 1.00 59.28  ? 1201 VAL A CB    1 
ATOM   8602 C  CG1   . VAL A 1 1201 ? 125.970 122.526 161.744 1.00 59.28  ? 1201 VAL A CG1   1 
ATOM   8603 C  CG2   . VAL A 1 1201 ? 124.828 120.617 160.610 1.00 59.28  ? 1201 VAL A CG2   1 
ATOM   8604 N  N     . VAL A 1 1202 ? 124.345 118.456 163.989 1.00 62.07  ? 1202 VAL A N     1 
ATOM   8605 C  CA    . VAL A 1 1202 ? 123.370 117.384 164.165 1.00 62.07  ? 1202 VAL A CA    1 
ATOM   8606 C  C     . VAL A 1 1202 ? 122.081 117.930 164.759 1.00 62.07  ? 1202 VAL A C     1 
ATOM   8607 O  O     . VAL A 1 1202 ? 122.096 118.753 165.680 1.00 62.07  ? 1202 VAL A O     1 
ATOM   8608 C  CB    . VAL A 1 1202 ? 123.966 116.259 165.032 1.00 62.07  ? 1202 VAL A CB    1 
ATOM   8609 C  CG1   . VAL A 1 1202 ? 124.253 116.748 166.444 1.00 62.07  ? 1202 VAL A CG1   1 
ATOM   8610 C  CG2   . VAL A 1 1202 ? 123.024 115.067 165.068 1.00 62.07  ? 1202 VAL A CG2   1 
ATOM   8611 N  N     . VAL A 1 1203 ? 120.954 117.493 164.202 1.00 61.55  ? 1203 VAL A N     1 
ATOM   8612 C  CA    . VAL A 1 1203 ? 119.630 117.844 164.697 1.00 61.55  ? 1203 VAL A CA    1 
ATOM   8613 C  C     . VAL A 1 1203 ? 119.000 116.590 165.281 1.00 61.55  ? 1203 VAL A C     1 
ATOM   8614 O  O     . VAL A 1 1203 ? 119.167 115.491 164.741 1.00 61.55  ? 1203 VAL A O     1 
ATOM   8615 C  CB    . VAL A 1 1203 ? 118.741 118.453 163.594 1.00 61.55  ? 1203 VAL A CB    1 
ATOM   8616 C  CG1   . VAL A 1 1203 ? 119.354 119.740 163.072 1.00 61.55  ? 1203 VAL A CG1   1 
ATOM   8617 C  CG2   . VAL A 1 1203 ? 118.525 117.467 162.458 1.00 61.55  ? 1203 VAL A CG2   1 
ATOM   8618 N  N     . ALA A 1 1204 ? 118.300 116.747 166.402 1.00 72.89  ? 1204 ALA A N     1 
ATOM   8619 C  CA    . ALA A 1 1204 ? 117.696 115.596 167.067 1.00 72.89  ? 1204 ALA A CA    1 
ATOM   8620 C  C     . ALA A 1 1204 ? 116.564 116.075 167.956 1.00 72.89  ? 1204 ALA A C     1 
ATOM   8621 O  O     . ALA A 1 1204 ? 116.796 116.845 168.894 1.00 72.89  ? 1204 ALA A O     1 
ATOM   8622 C  CB    . ALA A 1 1204 ? 118.736 114.829 167.884 1.00 72.89  ? 1204 ALA A CB    1 
ATOM   8623 N  N     . HIS A 1 1205 ? 115.348 115.625 167.663 1.00 76.87  ? 1205 HIS A N     1 
ATOM   8624 C  CA    . HIS A 1 1205 ? 114.199 115.859 168.524 1.00 76.87  ? 1205 HIS A CA    1 
ATOM   8625 C  C     . HIS A 1 1205 ? 114.028 114.770 169.574 1.00 76.87  ? 1205 HIS A C     1 
ATOM   8626 O  O     . HIS A 1 1205 ? 113.138 114.880 170.424 1.00 76.87  ? 1205 HIS A O     1 
ATOM   8627 C  CB    . HIS A 1 1205 ? 112.927 115.978 167.680 1.00 76.87  ? 1205 HIS A CB    1 
ATOM   8628 C  CG    . HIS A 1 1205 ? 112.595 114.737 166.913 1.00 76.87  ? 1205 HIS A CG    1 
ATOM   8629 N  ND1   . HIS A 1 1205 ? 111.857 113.704 167.450 1.00 76.87  ? 1205 HIS A ND1   1 
ATOM   8630 C  CD2   . HIS A 1 1205 ? 112.903 114.362 165.649 1.00 76.87  ? 1205 HIS A CD2   1 
ATOM   8631 C  CE1   . HIS A 1 1205 ? 111.725 112.746 166.550 1.00 76.87  ? 1205 HIS A CE1   1 
ATOM   8632 N  NE2   . HIS A 1 1205 ? 112.350 113.121 165.448 1.00 76.87  ? 1205 HIS A NE2   1 
ATOM   8633 N  N     . ARG A 1 1206 ? 114.856 113.723 169.534 1.00 88.83  ? 1206 ARG A N     1 
ATOM   8634 C  CA    . ARG A 1 1206 ? 114.800 112.680 170.550 1.00 88.83  ? 1206 ARG A CA    1 
ATOM   8635 C  C     . ARG A 1 1206 ? 115.352 113.151 171.888 1.00 88.83  ? 1206 ARG A C     1 
ATOM   8636 O  O     . ARG A 1 1206 ? 114.988 112.585 172.925 1.00 88.83  ? 1206 ARG A O     1 
ATOM   8637 C  CB    . ARG A 1 1206 ? 115.564 111.443 170.077 1.00 88.83  ? 1206 ARG A CB    1 
ATOM   8638 C  CG    . ARG A 1 1206 ? 115.070 110.142 170.682 1.00 88.83  ? 1206 ARG A CG    1 
ATOM   8639 C  CD    . ARG A 1 1206 ? 115.904 108.962 170.212 1.00 88.83  ? 1206 ARG A CD    1 
ATOM   8640 N  NE    . ARG A 1 1206 ? 115.488 108.487 168.895 1.00 88.83  ? 1206 ARG A NE    1 
ATOM   8641 C  CZ    . ARG A 1 1206 ? 114.497 107.626 168.689 1.00 88.83  ? 1206 ARG A CZ    1 
ATOM   8642 N  NH1   . ARG A 1 1206 ? 114.189 107.249 167.455 1.00 88.83  ? 1206 ARG A NH1   1 
ATOM   8643 N  NH2   . ARG A 1 1206 ? 113.814 107.139 169.716 1.00 88.83  ? 1206 ARG A NH2   1 
ATOM   8644 N  N     . LEU A 1 1207 ? 116.222 114.164 171.883 1.00 103.09 ? 1207 LEU A N     1 
ATOM   8645 C  CA    . LEU A 1 1207 ? 116.769 114.759 173.103 1.00 103.09 ? 1207 LEU A CA    1 
ATOM   8646 C  C     . LEU A 1 1207 ? 117.508 113.734 173.959 1.00 103.09 ? 1207 LEU A C     1 
ATOM   8647 O  O     . LEU A 1 1207 ? 117.479 113.801 175.190 1.00 103.09 ? 1207 LEU A O     1 
ATOM   8648 C  CB    . LEU A 1 1207 ? 115.674 115.447 173.924 1.00 103.09 ? 1207 LEU A CB    1 
ATOM   8649 C  CG    . LEU A 1 1207 ? 115.416 116.927 173.640 1.00 103.09 ? 1207 LEU A CG    1 
ATOM   8650 C  CD1   . LEU A 1 1207 ? 114.833 117.126 172.250 1.00 103.09 ? 1207 LEU A CD1   1 
ATOM   8651 C  CD2   . LEU A 1 1207 ? 114.488 117.504 174.692 1.00 103.09 ? 1207 LEU A CD2   1 
ATOM   8652 N  N     . SER A 1 1208 ? 118.175 112.777 173.316 1.00 106.82 ? 1208 SER A N     1 
ATOM   8653 C  CA    . SER A 1 1208 ? 118.902 111.745 174.043 1.00 106.82 ? 1208 SER A CA    1 
ATOM   8654 C  C     . SER A 1 1208 ? 120.344 111.642 173.563 1.00 106.82 ? 1208 SER A C     1 
ATOM   8655 O  O     . SER A 1 1208 ? 121.246 111.337 174.350 1.00 106.82 ? 1208 SER A O     1 
ATOM   8656 C  CB    . SER A 1 1208 ? 118.198 110.394 173.897 1.00 106.82 ? 1208 SER A CB    1 
ATOM   8657 O  OG    . SER A 1 1208 ? 117.861 110.141 172.545 1.00 106.82 ? 1208 SER A OG    1 
ATOM   8658 N  N     . THR A 1 1209 ? 120.571 111.891 172.273 1.00 109.01 ? 1209 THR A N     1 
ATOM   8659 C  CA    . THR A 1 1209 ? 121.888 111.761 171.662 1.00 109.01 ? 1209 THR A CA    1 
ATOM   8660 C  C     . THR A 1 1209 ? 122.536 113.113 171.379 1.00 109.01 ? 1209 THR A C     1 
ATOM   8661 O  O     . THR A 1 1209 ? 123.334 113.236 170.443 1.00 109.01 ? 1209 THR A O     1 
ATOM   8662 C  CB    . THR A 1 1209 ? 121.793 110.936 170.378 1.00 109.01 ? 1209 THR A CB    1 
ATOM   8663 O  OG1   . THR A 1 1209 ? 123.078 110.878 169.747 1.00 109.01 ? 1209 THR A OG1   1 
ATOM   8664 C  CG2   . THR A 1 1209 ? 120.782 111.551 169.420 1.00 109.01 ? 1209 THR A CG2   1 
ATOM   8665 N  N     . ILE A 1 1210 ? 122.215 114.130 172.176 1.00 114.94 ? 1210 ILE A N     1 
ATOM   8666 C  CA    . ILE A 1 1210 ? 122.731 115.477 171.961 1.00 114.94 ? 1210 ILE A CA    1 
ATOM   8667 C  C     . ILE A 1 1210 ? 123.544 115.919 173.171 1.00 114.94 ? 1210 ILE A C     1 
ATOM   8668 O  O     . ILE A 1 1210 ? 123.524 117.096 173.549 1.00 114.94 ? 1210 ILE A O     1 
ATOM   8669 C  CB    . ILE A 1 1210 ? 121.596 116.473 171.663 1.00 114.94 ? 1210 ILE A CB    1 
ATOM   8670 C  CG1   . ILE A 1 1210 ? 120.413 116.241 172.602 1.00 114.94 ? 1210 ILE A CG1   1 
ATOM   8671 C  CG2   . ILE A 1 1210 ? 121.158 116.360 170.212 1.00 114.94 ? 1210 ILE A CG2   1 
ATOM   8672 C  CD1   . ILE A 1 1210 ? 119.311 117.265 172.444 1.00 114.94 ? 1210 ILE A CD1   1 
ATOM   8673 N  N     . ARG A 1 1211 ? 124.254 114.975 173.794 1.00 117.81 ? 1211 ARG A N     1 
ATOM   8674 C  CA    . ARG A 1 1211 ? 125.024 115.283 174.995 1.00 117.81 ? 1211 ARG A CA    1 
ATOM   8675 C  C     . ARG A 1 1211 ? 126.126 116.307 174.751 1.00 117.81 ? 1211 ARG A C     1 
ATOM   8676 O  O     . ARG A 1 1211 ? 126.638 116.883 175.717 1.00 117.81 ? 1211 ARG A O     1 
ATOM   8677 C  CB    . ARG A 1 1211 ? 125.630 114.005 175.577 1.00 117.81 ? 1211 ARG A CB    1 
ATOM   8678 C  CG    . ARG A 1 1211 ? 124.749 113.316 176.608 1.00 117.81 ? 1211 ARG A CG    1 
ATOM   8679 C  CD    . ARG A 1 1211 ? 123.823 112.300 175.962 1.00 117.81 ? 1211 ARG A CD    1 
ATOM   8680 N  NE    . ARG A 1 1211 ? 124.561 111.258 175.256 1.00 117.81 ? 1211 ARG A NE    1 
ATOM   8681 C  CZ    . ARG A 1 1211 ? 125.064 110.174 175.838 1.00 117.81 ? 1211 ARG A CZ    1 
ATOM   8682 N  NH1   . ARG A 1 1211 ? 124.907 109.986 177.142 1.00 117.81 ? 1211 ARG A NH1   1 
ATOM   8683 N  NH2   . ARG A 1 1211 ? 125.723 109.277 175.118 1.00 117.81 ? 1211 ARG A NH2   1 
ATOM   8684 N  N     . GLY A 1 1212 ? 126.516 116.542 173.498 1.00 115.87 ? 1212 GLY A N     1 
ATOM   8685 C  CA    . GLY A 1 1212 ? 127.497 117.573 173.214 1.00 115.87 ? 1212 GLY A CA    1 
ATOM   8686 C  C     . GLY A 1 1212 ? 126.987 118.946 173.600 1.00 115.87 ? 1212 GLY A C     1 
ATOM   8687 O  O     . GLY A 1 1212 ? 126.142 119.522 172.909 1.00 115.87 ? 1212 GLY A O     1 
ATOM   8688 N  N     . VAL A 1 1213 ? 127.502 119.479 174.704 1.00 120.01 ? 1213 VAL A N     1 
ATOM   8689 C  CA    . VAL A 1 1213 ? 126.927 120.687 175.322 1.00 120.01 ? 1213 VAL A CA    1 
ATOM   8690 C  C     . VAL A 1 1213 ? 127.690 121.877 174.747 1.00 120.01 ? 1213 VAL A C     1 
ATOM   8691 O  O     . VAL A 1 1213 ? 128.602 122.438 175.360 1.00 120.01 ? 1213 VAL A O     1 
ATOM   8692 C  CB    . VAL A 1 1213 ? 126.992 120.623 176.855 1.00 120.01 ? 1213 VAL A CB    1 
ATOM   8693 C  CG1   . VAL A 1 1213 ? 125.969 119.642 177.396 1.00 120.01 ? 1213 VAL A CG1   1 
ATOM   8694 C  CG2   . VAL A 1 1213 ? 128.380 120.189 177.320 1.00 120.01 ? 1213 VAL A CG2   1 
ATOM   8695 N  N     . ASP A 1 1214 ? 127.306 122.291 173.535 1.00 104.95 ? 1214 ASP A N     1 
ATOM   8696 C  CA    . ASP A 1 1214 ? 127.963 123.448 172.930 1.00 104.95 ? 1214 ASP A CA    1 
ATOM   8697 C  C     . ASP A 1 1214 ? 127.017 124.597 172.596 1.00 104.95 ? 1214 ASP A C     1 
ATOM   8698 O  O     . ASP A 1 1214 ? 127.100 125.649 173.234 1.00 104.95 ? 1214 ASP A O     1 
ATOM   8699 C  CB    . ASP A 1 1214 ? 128.724 122.988 171.685 1.00 104.95 ? 1214 ASP A CB    1 
ATOM   8700 C  CG    . ASP A 1 1214 ? 129.699 121.865 171.981 1.00 104.95 ? 1214 ASP A CG    1 
ATOM   8701 O  OD1   . ASP A 1 1214 ? 130.301 121.870 173.075 1.00 104.95 ? 1214 ASP A OD1   1 
ATOM   8702 O  OD2   . ASP A 1 1214 ? 129.862 120.975 171.120 1.00 104.95 ? 1214 ASP A OD2   1 
ATOM   8703 N  N     . CYS A 1 1215 ? 126.123 124.440 171.622 1.00 100.62 ? 1215 CYS A N     1 
ATOM   8704 C  CA    . CYS A 1 1215 ? 125.405 125.590 171.069 1.00 100.62 ? 1215 CYS A CA    1 
ATOM   8705 C  C     . CYS A 1 1215 ? 124.003 125.209 170.588 1.00 100.62 ? 1215 CYS A C     1 
ATOM   8706 O  O     . CYS A 1 1215 ? 123.609 125.525 169.465 1.00 100.62 ? 1215 CYS A O     1 
ATOM   8707 C  CB    . CYS A 1 1215 ? 126.219 126.239 169.951 1.00 100.62 ? 1215 CYS A CB    1 
ATOM   8708 S  SG    . CYS A 1 1215 ? 127.484 127.400 170.525 1.00 100.62 ? 1215 CYS A SG    1 
ATOM   8709 N  N     . ILE A 1 1216 ? 123.240 124.508 171.426 1.00 101.75 ? 1216 ILE A N     1 
ATOM   8710 C  CA    . ILE A 1 1216 ? 122.008 123.825 171.023 1.00 101.75 ? 1216 ILE A CA    1 
ATOM   8711 C  C     . ILE A 1 1216 ? 121.110 124.591 170.053 1.00 101.75 ? 1216 ILE A C     1 
ATOM   8712 O  O     . ILE A 1 1216 ? 120.584 123.999 169.105 1.00 101.75 ? 1216 ILE A O     1 
ATOM   8713 C  CB    . ILE A 1 1216 ? 121.200 123.405 172.264 1.00 101.75 ? 1216 ILE A CB    1 
ATOM   8714 C  CG1   . ILE A 1 1216 ? 120.818 124.620 173.112 1.00 101.75 ? 1216 ILE A CG1   1 
ATOM   8715 C  CG2   . ILE A 1 1216 ? 121.960 122.378 173.046 1.00 101.75 ? 1216 ILE A CG2   1 
ATOM   8716 C  CD1   . ILE A 1 1216 ? 119.842 124.301 174.210 1.00 101.75 ? 1216 ILE A CD1   1 
ATOM   8717 N  N     . GLY A 1 1217 ? 120.919 125.892 170.260 1.00 98.40  ? 1217 GLY A N     1 
ATOM   8718 C  CA    . GLY A 1 1217 ? 120.031 126.611 169.364 1.00 98.40  ? 1217 GLY A CA    1 
ATOM   8719 C  C     . GLY A 1 1217 ? 118.578 126.223 169.556 1.00 98.40  ? 1217 GLY A C     1 
ATOM   8720 O  O     . GLY A 1 1217 ? 118.001 125.515 168.726 1.00 98.40  ? 1217 GLY A O     1 
ATOM   8721 N  N     . VAL A 1 1218 ? 117.989 126.666 170.669 1.00 99.45  ? 1218 VAL A N     1 
ATOM   8722 C  CA    . VAL A 1 1218 ? 116.730 126.095 171.144 1.00 99.45  ? 1218 VAL A CA    1 
ATOM   8723 C  C     . VAL A 1 1218 ? 115.598 126.296 170.137 1.00 99.45  ? 1218 VAL A C     1 
ATOM   8724 O  O     . VAL A 1 1218 ? 114.834 125.365 169.855 1.00 99.45  ? 1218 VAL A O     1 
ATOM   8725 C  CB    . VAL A 1 1218 ? 116.381 126.676 172.529 1.00 99.45  ? 1218 VAL A CB    1 
ATOM   8726 C  CG1   . VAL A 1 1218 ? 116.379 128.201 172.500 1.00 99.45  ? 1218 VAL A CG1   1 
ATOM   8727 C  CG2   . VAL A 1 1218 ? 115.046 126.143 173.008 1.00 99.45  ? 1218 VAL A CG2   1 
ATOM   8728 N  N     . ILE A 1 1219 ? 115.463 127.495 169.575 1.00 92.85  ? 1219 ILE A N     1 
ATOM   8729 C  CA    . ILE A 1 1219 ? 114.280 127.849 168.797 1.00 92.85  ? 1219 ILE A CA    1 
ATOM   8730 C  C     . ILE A 1 1219 ? 114.698 128.267 167.395 1.00 92.85  ? 1219 ILE A C     1 
ATOM   8731 O  O     . ILE A 1 1219 ? 115.621 129.072 167.231 1.00 92.85  ? 1219 ILE A O     1 
ATOM   8732 C  CB    . ILE A 1 1219 ? 113.467 128.969 169.476 1.00 92.85  ? 1219 ILE A CB    1 
ATOM   8733 C  CG1   . ILE A 1 1219 ? 112.836 128.458 170.773 1.00 92.85  ? 1219 ILE A CG1   1 
ATOM   8734 C  CG2   . ILE A 1 1219 ? 112.392 129.505 168.539 1.00 92.85  ? 1219 ILE A CG2   1 
ATOM   8735 C  CD1   . ILE A 1 1219 ? 112.120 129.526 171.568 1.00 92.85  ? 1219 ILE A CD1   1 
ATOM   8736 N  N     . GLN A 1 1220 ? 114.013 127.718 166.384 1.00 81.00  ? 1220 GLN A N     1 
ATOM   8737 C  CA    . GLN A 1 1220 ? 114.244 128.076 164.988 1.00 81.00  ? 1220 GLN A CA    1 
ATOM   8738 C  C     . GLN A 1 1220 ? 112.950 128.440 164.268 1.00 81.00  ? 1220 GLN A C     1 
ATOM   8739 O  O     . GLN A 1 1220 ? 112.884 128.332 163.040 1.00 81.00  ? 1220 GLN A O     1 
ATOM   8740 C  CB    . GLN A 1 1220 ? 114.950 126.943 164.241 1.00 81.00  ? 1220 GLN A CB    1 
ATOM   8741 C  CG    . GLN A 1 1220 ? 116.396 126.751 164.637 1.00 81.00  ? 1220 GLN A CG    1 
ATOM   8742 C  CD    . GLN A 1 1220 ? 116.539 126.028 165.954 1.00 81.00  ? 1220 GLN A CD    1 
ATOM   8743 O  OE1   . GLN A 1 1220 ? 115.601 125.388 166.428 1.00 81.00  ? 1220 GLN A OE1   1 
ATOM   8744 N  NE2   . GLN A 1 1220 ? 117.711 126.138 166.564 1.00 81.00  ? 1220 GLN A NE2   1 
ATOM   8745 N  N     . ASP A 1 1221 ? 111.923 128.872 164.999 1.00 72.79  ? 1221 ASP A N     1 
ATOM   8746 C  CA    . ASP A 1 1221 ? 110.648 129.211 164.380 1.00 72.79  ? 1221 ASP A CA    1 
ATOM   8747 C  C     . ASP A 1 1221 ? 110.742 130.537 163.638 1.00 72.79  ? 1221 ASP A C     1 
ATOM   8748 O  O     . ASP A 1 1221 ? 110.430 131.593 164.198 1.00 72.79  ? 1221 ASP A O     1 
ATOM   8749 C  CB    . ASP A 1 1221 ? 109.538 129.267 165.431 1.00 72.79  ? 1221 ASP A CB    1 
ATOM   8750 C  CG    . ASP A 1 1221 ? 108.166 129.461 164.818 1.00 72.79  ? 1221 ASP A CG    1 
ATOM   8751 O  OD1   . ASP A 1 1221 ? 107.785 130.623 164.564 1.00 72.79  ? 1221 ASP A OD1   1 
ATOM   8752 O  OD2   . ASP A 1 1221 ? 107.470 128.451 164.586 1.00 72.79  ? 1221 ASP A OD2   1 
ATOM   8753 N  N     . GLY A 1 1222 ? 111.174 130.494 162.380 1.00 58.91  ? 1222 GLY A N     1 
ATOM   8754 C  CA    . GLY A 1 1222 ? 111.340 131.702 161.597 1.00 58.91  ? 1222 GLY A CA    1 
ATOM   8755 C  C     . GLY A 1 1222 ? 112.569 132.486 162.006 1.00 58.91  ? 1222 GLY A C     1 
ATOM   8756 O  O     . GLY A 1 1222 ? 113.493 132.675 161.210 1.00 58.91  ? 1222 GLY A O     1 
ATOM   8757 N  N     . ARG A 1 1223 ? 112.585 132.947 163.251 1.00 69.35  ? 1223 ARG A N     1 
ATOM   8758 C  CA    . ARG A 1 1223 ? 113.703 133.671 163.825 1.00 69.35  ? 1223 ARG A CA    1 
ATOM   8759 C  C     . ARG A 1 1223 ? 114.531 132.720 164.687 1.00 69.35  ? 1223 ARG A C     1 
ATOM   8760 O  O     . ARG A 1 1223 ? 114.316 131.504 164.694 1.00 69.35  ? 1223 ARG A O     1 
ATOM   8761 C  CB    . ARG A 1 1223 ? 113.190 134.869 164.623 1.00 69.35  ? 1223 ARG A CB    1 
ATOM   8762 C  CG    . ARG A 1 1223 ? 112.338 134.481 165.817 1.00 69.35  ? 1223 ARG A CG    1 
ATOM   8763 C  CD    . ARG A 1 1223 ? 111.242 135.503 166.072 1.00 69.35  ? 1223 ARG A CD    1 
ATOM   8764 N  NE    . ARG A 1 1223 ? 110.099 135.320 165.182 1.00 69.35  ? 1223 ARG A NE    1 
ATOM   8765 C  CZ    . ARG A 1 1223 ? 109.210 134.337 165.289 1.00 69.35  ? 1223 ARG A CZ    1 
ATOM   8766 N  NH1   . ARG A 1 1223 ? 108.203 134.257 164.430 1.00 69.35  ? 1223 ARG A NH1   1 
ATOM   8767 N  NH2   . ARG A 1 1223 ? 109.322 133.435 166.256 1.00 69.35  ? 1223 ARG A NH2   1 
ATOM   8768 N  N     . ILE A 1 1224 ? 115.492 133.271 165.422 1.00 76.13  ? 1224 ILE A N     1 
ATOM   8769 C  CA    . ILE A 1 1224 ? 116.350 132.481 166.294 1.00 76.13  ? 1224 ILE A CA    1 
ATOM   8770 C  C     . ILE A 1 1224 ? 116.281 133.056 167.702 1.00 76.13  ? 1224 ILE A C     1 
ATOM   8771 O  O     . ILE A 1 1224 ? 115.975 134.236 167.902 1.00 76.13  ? 1224 ILE A O     1 
ATOM   8772 C  CB    . ILE A 1 1224 ? 117.808 132.441 165.784 1.00 76.13  ? 1224 ILE A CB    1 
ATOM   8773 C  CG1   . ILE A 1 1224 ? 118.564 131.259 166.394 1.00 76.13  ? 1224 ILE A CG1   1 
ATOM   8774 C  CG2   . ILE A 1 1224 ? 118.523 133.747 166.095 1.00 76.13  ? 1224 ILE A CG2   1 
ATOM   8775 C  CD1   . ILE A 1 1224 ? 118.312 129.945 165.692 1.00 76.13  ? 1224 ILE A CD1   1 
ATOM   8776 N  N     . VAL A 1 1225 ? 116.554 132.202 168.683 1.00 96.33  ? 1225 VAL A N     1 
ATOM   8777 C  CA    . VAL A 1 1225 ? 116.569 132.580 170.089 1.00 96.33  ? 1225 VAL A CA    1 
ATOM   8778 C  C     . VAL A 1 1225 ? 117.943 132.242 170.652 1.00 96.33  ? 1225 VAL A C     1 
ATOM   8779 O  O     . VAL A 1 1225 ? 118.623 131.331 170.164 1.00 96.33  ? 1225 VAL A O     1 
ATOM   8780 C  CB    . VAL A 1 1225 ? 115.430 131.873 170.860 1.00 96.33  ? 1225 VAL A CB    1 
ATOM   8781 C  CG1   . VAL A 1 1225 ? 115.556 132.068 172.365 1.00 96.33  ? 1225 VAL A CG1   1 
ATOM   8782 C  CG2   . VAL A 1 1225 ? 114.083 132.388 170.380 1.00 96.33  ? 1225 VAL A CG2   1 
ATOM   8783 N  N     . GLU A 1 1226 ? 118.363 133.009 171.661 1.00 117.18 ? 1226 GLU A N     1 
ATOM   8784 C  CA    . GLU A 1 1226 ? 119.676 132.856 172.280 1.00 117.18 ? 1226 GLU A CA    1 
ATOM   8785 C  C     . GLU A 1 1226 ? 119.993 131.394 172.558 1.00 117.18 ? 1226 GLU A C     1 
ATOM   8786 O  O     . GLU A 1 1226 ? 119.261 130.712 173.282 1.00 117.18 ? 1226 GLU A O     1 
ATOM   8787 C  CB    . GLU A 1 1226 ? 119.731 133.668 173.576 1.00 117.18 ? 1226 GLU A CB    1 
ATOM   8788 C  CG    . GLU A 1 1226 ? 121.119 133.785 174.178 1.00 117.18 ? 1226 GLU A CG    1 
ATOM   8789 C  CD    . GLU A 1 1226 ? 121.324 132.846 175.350 1.00 117.18 ? 1226 GLU A CD    1 
ATOM   8790 O  OE1   . GLU A 1 1226 ? 120.379 132.675 176.148 1.00 117.18 ? 1226 GLU A OE1   1 
ATOM   8791 O  OE2   . GLU A 1 1226 ? 122.430 132.280 175.473 1.00 117.18 ? 1226 GLU A OE2   1 
ATOM   8792 N  N     . GLN A 1 1227 ? 121.093 130.918 171.974 1.00 114.48 ? 1227 GLN A N     1 
ATOM   8793 C  CA    . GLN A 1 1227 ? 121.439 129.503 172.045 1.00 114.48 ? 1227 GLN A CA    1 
ATOM   8794 C  C     . GLN A 1 1227 ? 122.024 129.137 173.405 1.00 114.48 ? 1227 GLN A C     1 
ATOM   8795 O  O     . GLN A 1 1227 ? 121.461 128.315 174.136 1.00 114.48 ? 1227 GLN A O     1 
ATOM   8796 C  CB    . GLN A 1 1227 ? 122.427 129.156 170.928 1.00 114.48 ? 1227 GLN A CB    1 
ATOM   8797 C  CG    . GLN A 1 1227 ? 121.991 129.624 169.550 1.00 114.48 ? 1227 GLN A CG    1 
ATOM   8798 C  CD    . GLN A 1 1227 ? 122.787 128.973 168.436 1.00 114.48 ? 1227 GLN A CD    1 
ATOM   8799 O  OE1   . GLN A 1 1227 ? 123.732 128.225 168.686 1.00 114.48 ? 1227 GLN A OE1   1 
ATOM   8800 N  NE2   . GLN A 1 1227 ? 122.403 129.252 167.196 1.00 114.48 ? 1227 GLN A NE2   1 
ATOM   8801 N  N     . GLY A 1 1228 ? 123.152 129.744 173.761 1.00 127.02 ? 1228 GLY A N     1 
ATOM   8802 C  CA    . GLY A 1 1228 ? 123.841 129.386 174.985 1.00 127.02 ? 1228 GLY A CA    1 
ATOM   8803 C  C     . GLY A 1 1228 ? 124.521 128.037 174.886 1.00 127.02 ? 1228 GLY A C     1 
ATOM   8804 O  O     . GLY A 1 1228 ? 125.396 127.837 174.038 1.00 127.02 ? 1228 GLY A O     1 
ATOM   8805 N  N     . SER A 1 1229 ? 124.124 127.101 175.745 1.00 135.35 ? 1229 SER A N     1 
ATOM   8806 C  CA    . SER A 1 1229 ? 124.680 125.756 175.727 1.00 135.35 ? 1229 SER A CA    1 
ATOM   8807 C  C     . SER A 1 1229 ? 123.642 124.791 176.280 1.00 135.35 ? 1229 SER A C     1 
ATOM   8808 O  O     . SER A 1 1229 ? 122.667 125.193 176.921 1.00 135.35 ? 1229 SER A O     1 
ATOM   8809 C  CB    . SER A 1 1229 ? 125.988 125.676 176.522 1.00 135.35 ? 1229 SER A CB    1 
ATOM   8810 O  OG    . SER A 1 1229 ? 125.745 125.714 177.917 1.00 135.35 ? 1229 SER A OG    1 
ATOM   8811 N  N     . HIS A 1 1230 ? 123.859 123.502 176.011 1.00 137.48 ? 1230 HIS A N     1 
ATOM   8812 C  CA    . HIS A 1 1230 ? 122.915 122.478 176.450 1.00 137.48 ? 1230 HIS A CA    1 
ATOM   8813 C  C     . HIS A 1 1230 ? 122.826 122.427 177.969 1.00 137.48 ? 1230 HIS A C     1 
ATOM   8814 O  O     . HIS A 1 1230 ? 121.728 122.378 178.536 1.00 137.48 ? 1230 HIS A O     1 
ATOM   8815 C  CB    . HIS A 1 1230 ? 123.328 121.119 175.887 1.00 137.48 ? 1230 HIS A CB    1 
ATOM   8816 C  CG    . HIS A 1 1230 ? 122.280 120.059 176.017 1.00 137.48 ? 1230 HIS A CG    1 
ATOM   8817 N  ND1   . HIS A 1 1230 ? 121.596 119.556 174.931 1.00 137.48 ? 1230 HIS A ND1   1 
ATOM   8818 C  CD2   . HIS A 1 1230 ? 121.804 119.401 177.100 1.00 137.48 ? 1230 HIS A CD2   1 
ATOM   8819 C  CE1   . HIS A 1 1230 ? 120.742 118.635 175.340 1.00 137.48 ? 1230 HIS A CE1   1 
ATOM   8820 N  NE2   . HIS A 1 1230 ? 120.847 118.522 176.652 1.00 137.48 ? 1230 HIS A NE2   1 
ATOM   8821 N  N     . SER A 1 1231 ? 123.977 122.441 178.647 1.00 145.49 ? 1231 SER A N     1 
ATOM   8822 C  CA    . SER A 1 1231 ? 123.971 122.469 180.105 1.00 145.49 ? 1231 SER A CA    1 
ATOM   8823 C  C     . SER A 1 1231 ? 123.338 123.749 180.630 1.00 145.49 ? 1231 SER A C     1 
ATOM   8824 O  O     . SER A 1 1231 ? 122.681 123.733 181.678 1.00 145.49 ? 1231 SER A O     1 
ATOM   8825 C  CB    . SER A 1 1231 ? 125.396 122.320 180.640 1.00 145.49 ? 1231 SER A CB    1 
ATOM   8826 O  OG    . SER A 1 1231 ? 126.189 123.443 180.298 1.00 145.49 ? 1231 SER A OG    1 
ATOM   8827 N  N     . GLU A 1 1232 ? 123.515 124.861 179.913 1.00 149.37 ? 1232 GLU A N     1 
ATOM   8828 C  CA    . GLU A 1 1232 ? 122.907 126.119 180.332 1.00 149.37 ? 1232 GLU A CA    1 
ATOM   8829 C  C     . GLU A 1 1232 ? 121.388 126.007 180.365 1.00 149.37 ? 1232 GLU A C     1 
ATOM   8830 O  O     . GLU A 1 1232 ? 120.757 126.293 181.387 1.00 149.37 ? 1232 GLU A O     1 
ATOM   8831 C  CB    . GLU A 1 1232 ? 123.344 127.248 179.398 1.00 149.37 ? 1232 GLU A CB    1 
ATOM   8832 C  CG    . GLU A 1 1232 ? 122.871 128.625 179.825 1.00 149.37 ? 1232 GLU A CG    1 
ATOM   8833 C  CD    . GLU A 1 1232 ? 123.630 129.151 181.025 1.00 149.37 ? 1232 GLU A CD    1 
ATOM   8834 O  OE1   . GLU A 1 1232 ? 124.806 128.768 181.198 1.00 149.37 ? 1232 GLU A OE1   1 
ATOM   8835 O  OE2   . GLU A 1 1232 ? 123.051 129.946 181.795 1.00 149.37 ? 1232 GLU A OE2   1 
ATOM   8836 N  N     . LEU A 1 1233 ? 120.784 125.558 179.261 1.00 149.29 ? 1233 LEU A N     1 
ATOM   8837 C  CA    . LEU A 1 1233 ? 119.332 125.442 179.211 1.00 149.29 ? 1233 LEU A CA    1 
ATOM   8838 C  C     . LEU A 1 1233 ? 118.814 124.295 180.067 1.00 149.29 ? 1233 LEU A C     1 
ATOM   8839 O  O     . LEU A 1 1233 ? 117.650 124.326 180.483 1.00 149.29 ? 1233 LEU A O     1 
ATOM   8840 C  CB    . LEU A 1 1233 ? 118.861 125.283 177.763 1.00 149.29 ? 1233 LEU A CB    1 
ATOM   8841 C  CG    . LEU A 1 1233 ? 117.353 125.413 177.531 1.00 149.29 ? 1233 LEU A CG    1 
ATOM   8842 C  CD1   . LEU A 1 1233 ? 116.809 126.640 178.239 1.00 149.29 ? 1233 LEU A CD1   1 
ATOM   8843 C  CD2   . LEU A 1 1233 ? 117.053 125.504 176.051 1.00 149.29 ? 1233 LEU A CD2   1 
ATOM   8844 N  N     . VAL A 1 1234 ? 119.647 123.289 180.345 1.00 151.43 ? 1234 VAL A N     1 
ATOM   8845 C  CA    . VAL A 1 1234 ? 119.293 122.307 181.365 1.00 151.43 ? 1234 VAL A CA    1 
ATOM   8846 C  C     . VAL A 1 1234 ? 119.170 122.990 182.721 1.00 151.43 ? 1234 VAL A C     1 
ATOM   8847 O  O     . VAL A 1 1234 ? 118.232 122.728 183.485 1.00 151.43 ? 1234 VAL A O     1 
ATOM   8848 C  CB    . VAL A 1 1234 ? 120.324 121.162 181.388 1.00 151.43 ? 1234 VAL A CB    1 
ATOM   8849 C  CG1   . VAL A 1 1234 ? 120.287 120.431 182.722 1.00 151.43 ? 1234 VAL A CG1   1 
ATOM   8850 C  CG2   . VAL A 1 1234 ? 120.066 120.194 180.244 1.00 151.43 ? 1234 VAL A CG2   1 
ATOM   8851 N  N     . SER A 1 1235 ? 120.105 123.887 183.034 1.00 156.24 ? 1235 SER A N     1 
ATOM   8852 C  CA    . SER A 1 1235 ? 120.036 124.674 184.257 1.00 156.24 ? 1235 SER A CA    1 
ATOM   8853 C  C     . SER A 1 1235 ? 119.084 125.859 184.156 1.00 156.24 ? 1235 SER A C     1 
ATOM   8854 O  O     . SER A 1 1235 ? 118.596 126.332 185.190 1.00 156.24 ? 1235 SER A O     1 
ATOM   8855 C  CB    . SER A 1 1235 ? 121.431 125.179 184.641 1.00 156.24 ? 1235 SER A CB    1 
ATOM   8856 O  OG    . SER A 1 1235 ? 122.117 125.688 183.510 1.00 156.24 ? 1235 SER A OG    1 
ATOM   8857 N  N     . ARG A 1 1236 ? 118.809 126.350 182.949 1.00 148.58 ? 1236 ARG A N     1 
ATOM   8858 C  CA    . ARG A 1 1236 ? 117.909 127.478 182.768 1.00 148.58 ? 1236 ARG A CA    1 
ATOM   8859 C  C     . ARG A 1 1236 ? 116.462 127.073 183.038 1.00 148.58 ? 1236 ARG A C     1 
ATOM   8860 O  O     . ARG A 1 1236 ? 116.123 125.887 183.022 1.00 148.58 ? 1236 ARG A O     1 
ATOM   8861 C  CB    . ARG A 1 1236 ? 118.043 128.042 181.354 1.00 148.58 ? 1236 ARG A CB    1 
ATOM   8862 C  CG    . ARG A 1 1236 ? 119.227 128.980 181.158 1.00 148.58 ? 1236 ARG A CG    1 
ATOM   8863 C  CD    . ARG A 1 1236 ? 119.179 129.671 179.800 1.00 148.58 ? 1236 ARG A CD    1 
ATOM   8864 N  NE    . ARG A 1 1236 ? 119.460 128.759 178.694 1.00 148.58 ? 1236 ARG A NE    1 
ATOM   8865 C  CZ    . ARG A 1 1236 ? 119.335 129.082 177.410 1.00 148.58 ? 1236 ARG A CZ    1 
ATOM   8866 N  NH1   . ARG A 1 1236 ? 118.932 130.297 177.066 1.00 148.58 ? 1236 ARG A NH1   1 
ATOM   8867 N  NH2   . ARG A 1 1236 ? 119.614 128.192 176.468 1.00 148.58 ? 1236 ARG A NH2   1 
ATOM   8868 N  N     . PRO A 1 1237 ? 115.582 128.052 183.294 1.00 153.86 ? 1237 PRO A N     1 
ATOM   8869 C  CA    . PRO A 1 1237 ? 114.165 127.731 183.520 1.00 153.86 ? 1237 PRO A CA    1 
ATOM   8870 C  C     . PRO A 1 1237 ? 113.450 127.288 182.253 1.00 153.86 ? 1237 PRO A C     1 
ATOM   8871 O  O     . PRO A 1 1237 ? 114.090 127.061 181.220 1.00 153.86 ? 1237 PRO A O     1 
ATOM   8872 C  CB    . PRO A 1 1237 ? 113.585 129.047 184.058 1.00 153.86 ? 1237 PRO A CB    1 
ATOM   8873 C  CG    . PRO A 1 1237 ? 114.534 130.101 183.600 1.00 153.86 ? 1237 PRO A CG    1 
ATOM   8874 C  CD    . PRO A 1 1237 ? 115.883 129.459 183.611 1.00 153.86 ? 1237 PRO A CD    1 
ATOM   8875 N  N     . GLU A 1 1238 ? 112.127 127.141 182.344 1.00 155.15 ? 1238 GLU A N     1 
ATOM   8876 C  CA    . GLU A 1 1238 ? 111.295 126.603 181.270 1.00 155.15 ? 1238 GLU A CA    1 
ATOM   8877 C  C     . GLU A 1 1238 ? 111.662 127.178 179.907 1.00 155.15 ? 1238 GLU A C     1 
ATOM   8878 O  O     . GLU A 1 1238 ? 111.860 128.386 179.757 1.00 155.15 ? 1238 GLU A O     1 
ATOM   8879 C  CB    . GLU A 1 1238 ? 109.820 126.885 181.568 1.00 155.15 ? 1238 GLU A CB    1 
ATOM   8880 C  CG    . GLU A 1 1238 ? 109.219 126.016 182.658 1.00 155.15 ? 1238 GLU A CG    1 
ATOM   8881 C  CD    . GLU A 1 1238 ? 107.737 126.273 182.851 1.00 155.15 ? 1238 GLU A CD    1 
ATOM   8882 O  OE1   . GLU A 1 1238 ? 107.222 127.254 182.273 1.00 155.15 ? 1238 GLU A OE1   1 
ATOM   8883 O  OE2   . GLU A 1 1238 ? 107.085 125.494 183.577 1.00 155.15 ? 1238 GLU A OE2   1 
ATOM   8884 N  N     . GLY A 1 1239 ? 111.747 126.295 178.916 1.00 147.14 ? 1239 GLY A N     1 
ATOM   8885 C  CA    . GLY A 1 1239 ? 112.059 126.675 177.553 1.00 147.14 ? 1239 GLY A CA    1 
ATOM   8886 C  C     . GLY A 1 1239 ? 111.545 125.616 176.603 1.00 147.14 ? 1239 GLY A C     1 
ATOM   8887 O  O     . GLY A 1 1239 ? 110.955 124.615 177.015 1.00 147.14 ? 1239 GLY A O     1 
ATOM   8888 N  N     . ALA A 1 1240 ? 111.773 125.854 175.310 1.00 142.11 ? 1240 ALA A N     1 
ATOM   8889 C  CA    . ALA A 1 1240 ? 111.314 124.912 174.293 1.00 142.11 ? 1240 ALA A CA    1 
ATOM   8890 C  C     . ALA A 1 1240 ? 112.001 123.560 174.447 1.00 142.11 ? 1240 ALA A C     1 
ATOM   8891 O  O     . ALA A 1 1240 ? 111.366 122.508 174.313 1.00 142.11 ? 1240 ALA A O     1 
ATOM   8892 C  CB    . ALA A 1 1240 ? 111.548 125.487 172.896 1.00 142.11 ? 1240 ALA A CB    1 
ATOM   8893 N  N     . TYR A 1 1241 ? 113.308 123.566 174.716 1.00 139.02 ? 1241 TYR A N     1 
ATOM   8894 C  CA    . TYR A 1 1241 ? 114.004 122.312 174.989 1.00 139.02 ? 1241 TYR A CA    1 
ATOM   8895 C  C     . TYR A 1 1241 ? 113.564 121.719 176.322 1.00 139.02 ? 1241 TYR A C     1 
ATOM   8896 O  O     . TYR A 1 1241 ? 113.442 120.496 176.456 1.00 139.02 ? 1241 TYR A O     1 
ATOM   8897 C  CB    . TYR A 1 1241 ? 115.517 122.535 174.965 1.00 139.02 ? 1241 TYR A CB    1 
ATOM   8898 C  CG    . TYR A 1 1241 ? 116.324 121.432 175.616 1.00 139.02 ? 1241 TYR A CG    1 
ATOM   8899 C  CD1   . TYR A 1 1241 ? 116.682 120.294 174.906 1.00 139.02 ? 1241 TYR A CD1   1 
ATOM   8900 C  CD2   . TYR A 1 1241 ? 116.743 121.537 176.937 1.00 139.02 ? 1241 TYR A CD2   1 
ATOM   8901 C  CE1   . TYR A 1 1241 ? 117.422 119.287 175.497 1.00 139.02 ? 1241 TYR A CE1   1 
ATOM   8902 C  CE2   . TYR A 1 1241 ? 117.481 120.535 177.535 1.00 139.02 ? 1241 TYR A CE2   1 
ATOM   8903 C  CZ    . TYR A 1 1241 ? 117.818 119.413 176.811 1.00 139.02 ? 1241 TYR A CZ    1 
ATOM   8904 O  OH    . TYR A 1 1241 ? 118.555 118.413 177.403 1.00 139.02 ? 1241 TYR A OH    1 
ATOM   8905 N  N     . SER A 1 1242 ? 113.328 122.571 177.323 1.00 140.53 ? 1242 SER A N     1 
ATOM   8906 C  CA    . SER A 1 1242 ? 112.917 122.083 178.636 1.00 140.53 ? 1242 SER A CA    1 
ATOM   8907 C  C     . SER A 1 1242 ? 111.546 121.419 178.574 1.00 140.53 ? 1242 SER A C     1 
ATOM   8908 O  O     . SER A 1 1242 ? 111.336 120.347 179.155 1.00 140.53 ? 1242 SER A O     1 
ATOM   8909 C  CB    . SER A 1 1242 ? 112.916 123.234 179.643 1.00 140.53 ? 1242 SER A CB    1 
ATOM   8910 O  OG    . SER A 1 1242 ? 114.193 123.843 179.716 1.00 140.53 ? 1242 SER A OG    1 
ATOM   8911 N  N     . ARG A 1 1243 ? 110.597 122.042 177.871 1.00 136.20 ? 1243 ARG A N     1 
ATOM   8912 C  CA    . ARG A 1 1243 ? 109.273 121.443 177.738 1.00 136.20 ? 1243 ARG A CA    1 
ATOM   8913 C  C     . ARG A 1 1243 ? 109.333 120.153 176.927 1.00 136.20 ? 1243 ARG A C     1 
ATOM   8914 O  O     . ARG A 1 1243 ? 108.612 119.193 177.225 1.00 136.20 ? 1243 ARG A O     1 
ATOM   8915 C  CB    . ARG A 1 1243 ? 108.295 122.443 177.112 1.00 136.20 ? 1243 ARG A CB    1 
ATOM   8916 C  CG    . ARG A 1 1243 ? 108.576 122.791 175.659 1.00 136.20 ? 1243 ARG A CG    1 
ATOM   8917 C  CD    . ARG A 1 1243 ? 107.761 123.985 175.192 1.00 136.20 ? 1243 ARG A CD    1 
ATOM   8918 N  NE    . ARG A 1 1243 ? 106.326 123.720 175.219 1.00 136.20 ? 1243 ARG A NE    1 
ATOM   8919 C  CZ    . ARG A 1 1243 ? 105.423 124.435 174.555 1.00 136.20 ? 1243 ARG A CZ    1 
ATOM   8920 N  NH1   . ARG A 1 1243 ? 105.806 125.462 173.809 1.00 136.20 ? 1243 ARG A NH1   1 
ATOM   8921 N  NH2   . ARG A 1 1243 ? 104.137 124.122 174.637 1.00 136.20 ? 1243 ARG A NH2   1 
ATOM   8922 N  N     . LEU A 1 1244 ? 110.193 120.107 175.906 1.00 128.42 ? 1244 LEU A N     1 
ATOM   8923 C  CA    . LEU A 1 1244 ? 110.360 118.877 175.138 1.00 128.42 ? 1244 LEU A CA    1 
ATOM   8924 C  C     . LEU A 1 1244 ? 110.913 117.758 176.009 1.00 128.42 ? 1244 LEU A C     1 
ATOM   8925 O  O     . LEU A 1 1244 ? 110.448 116.615 175.932 1.00 128.42 ? 1244 LEU A O     1 
ATOM   8926 C  CB    . LEU A 1 1244 ? 111.276 119.124 173.940 1.00 128.42 ? 1244 LEU A CB    1 
ATOM   8927 C  CG    . LEU A 1 1244 ? 110.651 119.817 172.730 1.00 128.42 ? 1244 LEU A CG    1 
ATOM   8928 C  CD1   . LEU A 1 1244 ? 111.721 120.161 171.707 1.00 128.42 ? 1244 LEU A CD1   1 
ATOM   8929 C  CD2   . LEU A 1 1244 ? 109.569 118.945 172.116 1.00 128.42 ? 1244 LEU A CD2   1 
ATOM   8930 N  N     . LEU A 1 1245 ? 111.909 118.067 176.843 1.00 130.83 ? 1245 LEU A N     1 
ATOM   8931 C  CA    . LEU A 1 1245 ? 112.463 117.057 177.739 1.00 130.83 ? 1245 LEU A CA    1 
ATOM   8932 C  C     . LEU A 1 1245 ? 111.425 116.596 178.753 1.00 130.83 ? 1245 LEU A C     1 
ATOM   8933 O  O     . LEU A 1 1245 ? 111.338 115.401 179.059 1.00 130.83 ? 1245 LEU A O     1 
ATOM   8934 C  CB    . LEU A 1 1245 ? 113.707 117.605 178.441 1.00 130.83 ? 1245 LEU A CB    1 
ATOM   8935 C  CG    . LEU A 1 1245 ? 114.600 116.600 179.174 1.00 130.83 ? 1245 LEU A CG    1 
ATOM   8936 C  CD1   . LEU A 1 1245 ? 116.058 117.010 179.058 1.00 130.83 ? 1245 LEU A CD1   1 
ATOM   8937 C  CD2   . LEU A 1 1245 ? 114.203 116.469 180.638 1.00 130.83 ? 1245 LEU A CD2   1 
ATOM   8938 N  N     . GLN A 1 1246 ? 110.632 117.528 179.287 1.00 132.52 ? 1246 GLN A N     1 
ATOM   8939 C  CA    . GLN A 1 1246 ? 109.579 117.153 180.225 1.00 132.52 ? 1246 GLN A CA    1 
ATOM   8940 C  C     . GLN A 1 1246 ? 108.558 116.233 179.568 1.00 132.52 ? 1246 GLN A C     1 
ATOM   8941 O  O     . GLN A 1 1246 ? 108.150 115.225 180.158 1.00 132.52 ? 1246 GLN A O     1 
ATOM   8942 C  CB    . GLN A 1 1246 ? 108.896 118.403 180.778 1.00 132.52 ? 1246 GLN A CB    1 
ATOM   8943 C  CG    . GLN A 1 1246 ? 109.704 119.141 181.831 1.00 132.52 ? 1246 GLN A CG    1 
ATOM   8944 C  CD    . GLN A 1 1246 ? 109.438 120.633 181.827 1.00 132.52 ? 1246 GLN A CD    1 
ATOM   8945 O  OE1   . GLN A 1 1246 ? 108.648 121.132 181.026 1.00 132.52 ? 1246 GLN A OE1   1 
ATOM   8946 N  NE2   . GLN A 1 1246 ? 110.096 121.354 182.728 1.00 132.52 ? 1246 GLN A NE2   1 
ATOM   8947 N  N     . LEU A 1 1247 ? 108.139 116.560 178.343 1.00 127.02 ? 1247 LEU A N     1 
ATOM   8948 C  CA    . LEU A 1 1247 ? 107.172 115.723 177.641 1.00 127.02 ? 1247 LEU A CA    1 
ATOM   8949 C  C     . LEU A 1 1247 ? 107.751 114.349 177.323 1.00 127.02 ? 1247 LEU A C     1 
ATOM   8950 O  O     . LEU A 1 1247 ? 107.053 113.334 177.434 1.00 127.02 ? 1247 LEU A O     1 
ATOM   8951 C  CB    . LEU A 1 1247 ? 106.705 116.423 176.365 1.00 127.02 ? 1247 LEU A CB    1 
ATOM   8952 C  CG    . LEU A 1 1247 ? 105.648 117.513 176.551 1.00 127.02 ? 1247 LEU A CG    1 
ATOM   8953 C  CD1   . LEU A 1 1247 ? 105.216 118.080 175.208 1.00 127.02 ? 1247 LEU A CD1   1 
ATOM   8954 C  CD2   . LEU A 1 1247 ? 104.450 116.976 177.321 1.00 127.02 ? 1247 LEU A CD2   1 
ATOM   8955 N  N     . GLN A 1 1248 ? 109.024 114.296 176.919 1.00 122.11 ? 1248 GLN A N     1 
ATOM   8956 C  CA    . GLN A 1 1248 ? 109.660 113.011 176.648 1.00 122.11 ? 1248 GLN A CA    1 
ATOM   8957 C  C     . GLN A 1 1248 ? 109.744 112.160 177.909 1.00 122.11 ? 1248 GLN A C     1 
ATOM   8958 O  O     . GLN A 1 1248 ? 109.483 110.952 177.870 1.00 122.11 ? 1248 GLN A O     1 
ATOM   8959 C  CB    . GLN A 1 1248 ? 111.052 113.228 176.052 1.00 122.11 ? 1248 GLN A CB    1 
ATOM   8960 C  CG    . GLN A 1 1248 ? 111.046 113.680 174.600 1.00 122.11 ? 1248 GLN A CG    1 
ATOM   8961 C  CD    . GLN A 1 1248 ? 110.688 112.560 173.641 1.00 122.11 ? 1248 GLN A CD    1 
ATOM   8962 O  OE1   . GLN A 1 1248 ? 111.055 111.405 173.853 1.00 122.11 ? 1248 GLN A OE1   1 
ATOM   8963 N  NE2   . GLN A 1 1248 ? 109.969 112.899 172.577 1.00 122.11 ? 1248 GLN A NE2   1 
ATOM   8964 N  N     . THR A 1 1249 ? 110.107 112.773 179.040 1.00 128.45 ? 1249 THR A N     1 
ATOM   8965 C  CA    . THR A 1 1249 ? 110.172 112.033 180.297 1.00 128.45 ? 1249 THR A CA    1 
ATOM   8966 C  C     . THR A 1 1249 ? 108.790 111.558 180.730 1.00 128.45 ? 1249 THR A C     1 
ATOM   8967 O  O     . THR A 1 1249 ? 108.653 110.464 181.290 1.00 128.45 ? 1249 THR A O     1 
ATOM   8968 C  CB    . THR A 1 1249 ? 110.808 112.896 181.386 1.00 128.45 ? 1249 THR A CB    1 
ATOM   8969 O  OG1   . THR A 1 1249 ? 110.200 114.193 181.388 1.00 128.45 ? 1249 THR A OG1   1 
ATOM   8970 C  CG2   . THR A 1 1249 ? 112.303 113.041 181.143 1.00 128.45 ? 1249 THR A CG2   1 
ATOM   8971 N  N     . HIS A 1 1250 ? 107.757 112.371 180.492 1.00 128.53 ? 1250 HIS A N     1 
ATOM   8972 C  CA    . HIS A 1 1250 ? 106.393 111.925 180.758 1.00 128.53 ? 1250 HIS A CA    1 
ATOM   8973 C  C     . HIS A 1 1250 ? 106.032 110.728 179.889 1.00 128.53 ? 1250 HIS A C     1 
ATOM   8974 O  O     . HIS A 1 1250 ? 105.381 109.785 180.354 1.00 128.53 ? 1250 HIS A O     1 
ATOM   8975 C  CB    . HIS A 1 1250 ? 105.407 113.070 180.529 1.00 128.53 ? 1250 HIS A CB    1 
ATOM   8976 C  CG    . HIS A 1 1250 ? 105.614 114.238 181.441 1.00 128.53 ? 1250 HIS A CG    1 
ATOM   8977 N  ND1   . HIS A 1 1250 ? 106.364 114.158 182.595 1.00 128.53 ? 1250 HIS A ND1   1 
ATOM   8978 C  CD2   . HIS A 1 1250 ? 105.171 115.516 181.369 1.00 128.53 ? 1250 HIS A CD2   1 
ATOM   8979 C  CE1   . HIS A 1 1250 ? 106.373 115.335 183.194 1.00 128.53 ? 1250 HIS A CE1   1 
ATOM   8980 N  NE2   . HIS A 1 1250 ? 105.657 116.176 182.471 1.00 128.53 ? 1250 HIS A NE2   1 
ATOM   8981 N  N     . ARG A 1 1251 ? 106.442 110.753 178.619 1.00 120.61 ? 1251 ARG A N     1 
ATOM   8982 C  CA    . ARG A 1 1251 ? 106.256 109.586 177.763 1.00 120.61 ? 1251 ARG A CA    1 
ATOM   8983 C  C     . ARG A 1 1251 ? 107.070 108.403 178.273 1.00 120.61 ? 1251 ARG A C     1 
ATOM   8984 O  O     . ARG A 1 1251 ? 106.626 107.252 178.190 1.00 120.61 ? 1251 ARG A O     1 
ATOM   8985 C  CB    . ARG A 1 1251 ? 106.637 109.928 176.322 1.00 120.61 ? 1251 ARG A CB    1 
ATOM   8986 C  CG    . ARG A 1 1251 ? 106.211 108.891 175.291 1.00 120.61 ? 1251 ARG A CG    1 
ATOM   8987 C  CD    . ARG A 1 1251 ? 104.750 108.499 175.454 1.00 120.61 ? 1251 ARG A CD    1 
ATOM   8988 N  NE    . ARG A 1 1251 ? 103.854 109.645 175.337 1.00 120.61 ? 1251 ARG A NE    1 
ATOM   8989 C  CZ    . ARG A 1 1251 ? 102.714 109.772 176.008 1.00 120.61 ? 1251 ARG A CZ    1 
ATOM   8990 N  NH1   . ARG A 1 1251 ? 102.327 108.822 176.847 1.00 120.61 ? 1251 ARG A NH1   1 
ATOM   8991 N  NH2   . ARG A 1 1251 ? 101.960 110.850 175.840 1.00 120.61 ? 1251 ARG A NH2   1 
ATOM   8992 N  N     . ILE A 1 1252 ? 108.259 108.668 178.809 1.00 121.83 ? 1252 ILE A N     1 
ATOM   8993 C  CA    . ILE A 1 1252 ? 109.109 107.623 179.370 1.00 121.83 ? 1252 ILE A CA    1 
ATOM   8994 C  C     . ILE A 1 1252 ? 108.422 106.964 180.561 1.00 121.83 ? 1252 ILE A C     1 
ATOM   8995 O  O     . ILE A 1 1252 ? 108.348 105.738 180.655 1.00 121.83 ? 1252 ILE A O     1 
ATOM   8996 C  CB    . ILE A 1 1252 ? 110.488 108.185 179.778 1.00 121.83 ? 1252 ILE A CB    1 
ATOM   8997 C  CG1   . ILE A 1 1252 ? 111.357 108.429 178.543 1.00 121.83 ? 1252 ILE A CG1   1 
ATOM   8998 C  CG2   . ILE A 1 1252 ? 111.190 107.241 180.742 1.00 121.83 ? 1252 ILE A CG2   1 
ATOM   8999 C  CD1   . ILE A 1 1252 ? 112.557 109.313 178.806 1.00 121.83 ? 1252 ILE A CD1   1 
ATOM   9000 O  OXT   . ILE A 1 1252 ? 107.915 107.641 181.455 1.00 121.83 ? 1252 ILE A OXT   1 
HETATM 9001 V  V     . VO4 B 2 .    ? 114.056 98.935  161.160 1.00 56.25  ? 1301 VO4 A V     1 
HETATM 9002 O  O1    . VO4 B 2 .    ? 115.498 99.019  159.912 1.00 56.25  ? 1301 VO4 A O1    1 
HETATM 9003 O  O2    . VO4 B 2 .    ? 113.773 100.669 161.907 1.00 56.25  ? 1301 VO4 A O2    1 
HETATM 9004 O  O3    . VO4 B 2 .    ? 112.465 98.366  160.270 1.00 56.25  ? 1301 VO4 A O3    1 
HETATM 9005 O  O4    . VO4 B 2 .    ? 114.489 97.700  162.550 1.00 56.25  ? 1301 VO4 A O4    1 
HETATM 9006 P  PB    . ADP C 3 .    ? 113.519 95.275  160.330 1.00 43.77  ? 1302 ADP A PB    1 
HETATM 9007 O  O1B   . ADP C 3 .    ? 112.129 95.518  159.802 1.00 43.77  ? 1302 ADP A O1B   1 
HETATM 9008 O  O2B   . ADP C 3 .    ? 113.553 94.701  161.723 1.00 43.77  ? 1302 ADP A O2B   1 
HETATM 9009 O  O3B   . ADP C 3 .    ? 114.490 96.403  160.092 1.00 43.77  ? 1302 ADP A O3B   1 
HETATM 9010 P  PA    . ADP C 3 .    ? 113.492 93.914  157.917 1.00 43.77  ? 1302 ADP A PA    1 
HETATM 9011 O  O1A   . ADP C 3 .    ? 113.514 95.268  157.252 1.00 43.77  ? 1302 ADP A O1A   1 
HETATM 9012 O  O2A   . ADP C 3 .    ? 112.190 93.163  158.031 1.00 43.77  ? 1302 ADP A O2A   1 
HETATM 9013 O  O3A   . ADP C 3 .    ? 114.081 94.091  159.400 1.00 43.77  ? 1302 ADP A O3A   1 
HETATM 9014 O  "O5'" . ADP C 3 .    ? 114.580 92.979  157.189 1.00 43.77  ? 1302 ADP A "O5'" 1 
HETATM 9015 C  "C5'" . ADP C 3 .    ? 115.119 91.826  157.828 1.00 43.77  ? 1302 ADP A "C5'" 1 
HETATM 9016 C  "C4'" . ADP C 3 .    ? 116.075 91.145  156.858 1.00 43.77  ? 1302 ADP A "C4'" 1 
HETATM 9017 O  "O4'" . ADP C 3 .    ? 115.353 90.700  155.711 1.00 43.77  ? 1302 ADP A "O4'" 1 
HETATM 9018 C  "C3'" . ADP C 3 .    ? 117.147 92.105  156.373 1.00 43.77  ? 1302 ADP A "C3'" 1 
HETATM 9019 O  "O3'" . ADP C 3 .    ? 118.429 91.672  156.832 1.00 43.77  ? 1302 ADP A "O3'" 1 
HETATM 9020 C  "C2'" . ADP C 3 .    ? 117.104 92.059  154.860 1.00 43.77  ? 1302 ADP A "C2'" 1 
HETATM 9021 O  "O2'" . ADP C 3 .    ? 118.373 91.645  154.351 1.00 43.77  ? 1302 ADP A "O2'" 1 
HETATM 9022 C  "C1'" . ADP C 3 .    ? 116.047 91.029  154.507 1.00 43.77  ? 1302 ADP A "C1'" 1 
HETATM 9023 N  N9    . ADP C 3 .    ? 115.089 91.601  153.532 1.00 43.77  ? 1302 ADP A N9    1 
HETATM 9024 C  C8    . ADP C 3 .    ? 114.082 92.441  153.829 1.00 43.77  ? 1302 ADP A C8    1 
HETATM 9025 N  N7    . ADP C 3 .    ? 113.384 92.781  152.717 1.00 43.77  ? 1302 ADP A N7    1 
HETATM 9026 C  C5    . ADP C 3 .    ? 113.952 92.148  151.676 1.00 43.77  ? 1302 ADP A C5    1 
HETATM 9027 C  C6    . ADP C 3 .    ? 113.711 92.067  150.218 1.00 43.77  ? 1302 ADP A C6    1 
HETATM 9028 N  N6    . ADP C 3 .    ? 112.698 92.752  149.636 1.00 43.77  ? 1302 ADP A N6    1 
HETATM 9029 N  N1    . ADP C 3 .    ? 114.537 91.289  149.487 1.00 43.77  ? 1302 ADP A N1    1 
HETATM 9030 C  C2    . ADP C 3 .    ? 115.546 90.606  150.052 1.00 43.77  ? 1302 ADP A C2    1 
HETATM 9031 N  N3    . ADP C 3 .    ? 115.822 90.632  151.368 1.00 43.77  ? 1302 ADP A N3    1 
HETATM 9032 C  C4    . ADP C 3 .    ? 115.075 91.372  152.218 1.00 43.77  ? 1302 ADP A C4    1 
HETATM 9033 V  V     . VO4 D 2 .    ? 111.988 116.987 160.890 1.00 45.74  ? 1303 VO4 A V     1 
HETATM 9034 O  O1    . VO4 D 2 .    ? 110.441 116.656 159.821 1.00 45.74  ? 1303 VO4 A O1    1 
HETATM 9035 O  O2    . VO4 D 2 .    ? 112.505 115.369 161.762 1.00 45.74  ? 1303 VO4 A O2    1 
HETATM 9036 O  O3    . VO4 D 2 .    ? 113.421 117.588 159.780 1.00 45.74  ? 1303 VO4 A O3    1 
HETATM 9037 O  O4    . VO4 D 2 .    ? 111.587 118.320 162.196 1.00 45.74  ? 1303 VO4 A O4    1 
HETATM 9038 P  PB    . ADP E 3 .    ? 112.098 120.572 159.663 1.00 36.18  ? 1304 ADP A PB    1 
HETATM 9039 O  O1B   . ADP E 3 .    ? 113.444 120.390 159.011 1.00 36.18  ? 1304 ADP A O1B   1 
HETATM 9040 O  O2B   . ADP E 3 .    ? 112.153 121.283 160.991 1.00 36.18  ? 1304 ADP A O2B   1 
HETATM 9041 O  O3B   . ADP E 3 .    ? 111.217 119.350 159.642 1.00 36.18  ? 1304 ADP A O3B   1 
HETATM 9042 P  PA    . ADP E 3 .    ? 111.755 121.673 157.144 1.00 36.18  ? 1304 ADP A PA    1 
HETATM 9043 O  O1A   . ADP E 3 .    ? 111.790 120.260 156.616 1.00 36.18  ? 1304 ADP A O1A   1 
HETATM 9044 O  O2A   . ADP E 3 .    ? 112.987 122.536 157.042 1.00 36.18  ? 1304 ADP A O2A   1 
HETATM 9045 O  O3A   . ADP E 3 .    ? 111.338 121.604 158.693 1.00 36.18  ? 1304 ADP A O3A   1 
HETATM 9046 O  "O5'" . ADP E 3 .    ? 110.517 122.435 156.455 1.00 36.18  ? 1304 ADP A "O5'" 1 
HETATM 9047 C  "C5'" . ADP E 3 .    ? 109.941 123.601 157.038 1.00 36.18  ? 1304 ADP A "C5'" 1 
HETATM 9048 C  "C4'" . ADP E 3 .    ? 108.833 124.096 156.119 1.00 36.18  ? 1304 ADP A "C4'" 1 
HETATM 9049 O  "O4'" . ADP E 3 .    ? 109.391 124.477 154.862 1.00 36.18  ? 1304 ADP A "O4'" 1 
HETATM 9050 C  "C3'" . ADP E 3 .    ? 107.811 123.007 155.847 1.00 36.18  ? 1304 ADP A "C3'" 1 
HETATM 9051 O  "O3'" . ADP E 3 .    ? 106.548 123.379 156.402 1.00 36.18  ? 1304 ADP A "O3'" 1 
HETATM 9052 C  "C2'" . ADP E 3 .    ? 107.696 122.899 154.342 1.00 36.18  ? 1304 ADP A "C2'" 1 
HETATM 9053 O  "O2'" . ADP E 3 .    ? 106.349 123.153 153.939 1.00 36.18  ? 1304 ADP A "O2'" 1 
HETATM 9054 C  "C1'" . ADP E 3 .    ? 108.612 123.970 153.779 1.00 36.18  ? 1304 ADP A "C1'" 1 
HETATM 9055 N  N9    . ADP E 3 .    ? 109.515 123.380 152.762 1.00 36.18  ? 1304 ADP A N9    1 
HETATM 9056 C  C8    . ADP E 3 .    ? 110.620 122.660 153.025 1.00 36.18  ? 1304 ADP A C8    1 
HETATM 9057 N  N7    . ADP E 3 .    ? 111.229 122.264 151.880 1.00 36.18  ? 1304 ADP A N7    1 
HETATM 9058 C  C5    . ADP E 3 .    ? 110.503 122.738 150.853 1.00 36.18  ? 1304 ADP A C5    1 
HETATM 9059 C  C6    . ADP E 3 .    ? 110.587 122.686 149.376 1.00 36.18  ? 1304 ADP A C6    1 
HETATM 9060 N  N6    . ADP E 3 .    ? 111.594 122.029 148.753 1.00 36.18  ? 1304 ADP A N6    1 
HETATM 9061 N  N1    . ADP E 3 .    ? 109.623 123.313 148.670 1.00 36.18  ? 1304 ADP A N1    1 
HETATM 9062 C  C2    . ADP E 3 .    ? 108.617 123.967 149.276 1.00 36.18  ? 1304 ADP A C2    1 
HETATM 9063 N  N3    . ADP E 3 .    ? 108.479 124.056 150.610 1.00 36.18  ? 1304 ADP A N3    1 
HETATM 9064 C  C4    . ADP E 3 .    ? 109.374 123.471 151.439 1.00 36.18  ? 1304 ADP A C4    1 
HETATM 9065 MG MG    . MG  F 4 .    ? 111.154 97.824  158.724 1.00 43.42  ? 1305 MG  A MG    1 
HETATM 9066 MG MG    . MG  G 4 .    ? 113.954 117.126 157.790 1.00 35.93  ? 1306 MG  A MG    1 
# 
