data_9GZ3
# 
_entry.id   9GZ3 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9GZ3         pdb_00009gz3 10.2210/pdb9gz3/pdb 
WWPDB D_1292141912 ?            ?                   
EMDB  EMD-51721    ?            ?                   
# 
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 2025-03-12 ? 
2 'EM metadata'     1 0 2025-03-12 ? 
3 'Additional map'  1 0 2025-03-12 1 
4 FSC               1 0 2025-03-12 ? 
5 'Half map'        1 0 2025-03-12 1 
6 'Half map'        1 0 2025-03-12 2 
7 Image             1 0 2025-03-12 ? 
8 Mask              1 0 2025-03-12 1 
9 'Primary map'     1 0 2025-03-12 ? 
# 
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 'Additional map'  repository 'Initial release' ? ? 
4 4 FSC               repository 'Initial release' ? ? 
5 5 'Half map'        repository 'Initial release' ? ? 
6 6 'Half map'        repository 'Initial release' ? ? 
7 7 Image             repository 'Initial release' ? ? 
8 8 Mask              repository 'Initial release' ? ? 
9 9 '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                        9GZ3 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-03 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_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        'Beta-cardiac heavy meromyosin motor domain in the primed state' 
_pdbx_database_related.db_id          EMD-51721 
_pdbx_database_related.content_type   'associated EM volume' 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              C.A.Scarff@leeds.ac.uk 
_pdbx_contact_author.name_first         Charlie 
_pdbx_contact_author.name_last          Scarff 
_pdbx_contact_author.name_mi            A 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-6168-0060 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'McMillan, S.N.'   1 0000-0002-6833-5523 
'Pitts, J.R.T.'    2 0009-0009-5109-5218 
'Barua, B.'        3 ?                   
'Winkelmann, D.A.' 4 ?                   
'Scarff, C.A.'     5 0000-0001-6168-0060 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Biorxiv 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2692-8205 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Mavacamten inhibits myosin activity by stabilising the myosin interacting-heads motif and stalling motor force generation.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1101/2025.02.12.637875 
_citation.pdbx_database_id_PubMed   39990378 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'McMillan, S.N.'   1 0000-0002-6833-5523 
primary 'Pitts, J.R.T.'    2 0009-0009-5109-5218 
primary 'Barua, B.'        3 ?                   
primary 'Winkelmann, D.A.' 4 0000-0003-1932-2379 
primary 'Scarff, C.A.'     5 0000-0001-6168-0060 
# 
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 Myosin-7                   131852.484 1 ? ? ? ? 
2 non-polymer syn 'MAGNESIUM ION'            24.305     1 ? ? ? ? 
3 non-polymer syn "ADENOSINE-5'-DIPHOSPHATE" 427.201    1 ? ? ? ? 
4 non-polymer syn 'PHOSPHATE ION'            94.971     1 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
'Myosin heavy chain 7,Myosin heavy chain slow isoform,MyHC-slow,Myosin heavy chain,cardiac muscle beta isoform,MyHC-beta' 
# 
_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       
;GDSEMAVFGAAAPYLRKSEKERLEAQTRPFDLKKDVFVPDDKQEFVKAKIVSREGGKVTAETEYGKTVTVKEDQVMQQNP
PKFDKIEDMAMLTFLHEPAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNA
YQYMLTDRENQSILITGESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNS
SRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVA
SIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCH
PRVKVGNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFT
NEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSA
NFQKPRNIKGKPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADAPIEKGKGKAKKG
SSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQR
YRILNPAAIPEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFKAGLLGLLEEMRDERLSRIITRIQAQSRGVLARMEY
KKLLERRDSLLVIQWNIRAFMGVKNWPWMKLYFKIKPLLKSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLL
QEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTL
AKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQE
KKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEE
LESERTARAKVEKLRSDDYKDDDDK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GDSEMAVFGAAAPYLRKSEKERLEAQTRPFDLKKDVFVPDDKQEFVKAKIVSREGGKVTAETEYGKTVTVKEDQVMQQNP
PKFDKIEDMAMLTFLHEPAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNA
YQYMLTDRENQSILITGESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNS
SRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVA
SIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCH
PRVKVGNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFT
NEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSA
NFQKPRNIKGKPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADAPIEKGKGKAKKG
SSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQR
YRILNPAAIPEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFKAGLLGLLEEMRDERLSRIITRIQAQSRGVLARMEY
KKLLERRDSLLVIQWNIRAFMGVKNWPWMKLYFKIKPLLKSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLL
QEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTL
AKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQE
KKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEE
LESERTARAKVEKLRSDDYKDDDDK
;
_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 'MAGNESIUM ION'            MG  
3 "ADENOSINE-5'-DIPHOSPHATE" ADP 
4 'PHOSPHATE ION'            PO4 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1    GLY n 
1 2    ASP n 
1 3    SER n 
1 4    GLU n 
1 5    MET n 
1 6    ALA n 
1 7    VAL n 
1 8    PHE n 
1 9    GLY n 
1 10   ALA n 
1 11   ALA n 
1 12   ALA n 
1 13   PRO n 
1 14   TYR n 
1 15   LEU n 
1 16   ARG n 
1 17   LYS n 
1 18   SER n 
1 19   GLU n 
1 20   LYS n 
1 21   GLU n 
1 22   ARG n 
1 23   LEU n 
1 24   GLU n 
1 25   ALA n 
1 26   GLN n 
1 27   THR n 
1 28   ARG n 
1 29   PRO n 
1 30   PHE n 
1 31   ASP n 
1 32   LEU n 
1 33   LYS n 
1 34   LYS n 
1 35   ASP n 
1 36   VAL n 
1 37   PHE n 
1 38   VAL n 
1 39   PRO n 
1 40   ASP n 
1 41   ASP n 
1 42   LYS n 
1 43   GLN n 
1 44   GLU n 
1 45   PHE n 
1 46   VAL n 
1 47   LYS n 
1 48   ALA n 
1 49   LYS n 
1 50   ILE n 
1 51   VAL n 
1 52   SER n 
1 53   ARG n 
1 54   GLU n 
1 55   GLY n 
1 56   GLY n 
1 57   LYS n 
1 58   VAL n 
1 59   THR n 
1 60   ALA n 
1 61   GLU n 
1 62   THR n 
1 63   GLU n 
1 64   TYR n 
1 65   GLY n 
1 66   LYS n 
1 67   THR n 
1 68   VAL n 
1 69   THR n 
1 70   VAL n 
1 71   LYS n 
1 72   GLU n 
1 73   ASP n 
1 74   GLN n 
1 75   VAL n 
1 76   MET n 
1 77   GLN n 
1 78   GLN n 
1 79   ASN n 
1 80   PRO n 
1 81   PRO n 
1 82   LYS n 
1 83   PHE n 
1 84   ASP n 
1 85   LYS n 
1 86   ILE n 
1 87   GLU n 
1 88   ASP n 
1 89   MET n 
1 90   ALA n 
1 91   MET n 
1 92   LEU n 
1 93   THR n 
1 94   PHE n 
1 95   LEU n 
1 96   HIS n 
1 97   GLU n 
1 98   PRO n 
1 99   ALA n 
1 100  VAL n 
1 101  LEU n 
1 102  TYR n 
1 103  ASN n 
1 104  LEU n 
1 105  LYS n 
1 106  ASP n 
1 107  ARG n 
1 108  TYR n 
1 109  GLY n 
1 110  SER n 
1 111  TRP n 
1 112  MET n 
1 113  ILE n 
1 114  TYR n 
1 115  THR n 
1 116  TYR n 
1 117  SER n 
1 118  GLY n 
1 119  LEU n 
1 120  PHE n 
1 121  CYS n 
1 122  VAL n 
1 123  THR n 
1 124  VAL n 
1 125  ASN n 
1 126  PRO n 
1 127  TYR n 
1 128  LYS n 
1 129  TRP n 
1 130  LEU n 
1 131  PRO n 
1 132  VAL n 
1 133  TYR n 
1 134  THR n 
1 135  PRO n 
1 136  GLU n 
1 137  VAL n 
1 138  VAL n 
1 139  ALA n 
1 140  ALA n 
1 141  TYR n 
1 142  ARG n 
1 143  GLY n 
1 144  LYS n 
1 145  LYS n 
1 146  ARG n 
1 147  SER n 
1 148  GLU n 
1 149  ALA n 
1 150  PRO n 
1 151  PRO n 
1 152  HIS n 
1 153  ILE n 
1 154  PHE n 
1 155  SER n 
1 156  ILE n 
1 157  SER n 
1 158  ASP n 
1 159  ASN n 
1 160  ALA n 
1 161  TYR n 
1 162  GLN n 
1 163  TYR n 
1 164  MET n 
1 165  LEU n 
1 166  THR n 
1 167  ASP n 
1 168  ARG n 
1 169  GLU n 
1 170  ASN n 
1 171  GLN n 
1 172  SER n 
1 173  ILE n 
1 174  LEU n 
1 175  ILE n 
1 176  THR n 
1 177  GLY n 
1 178  GLU n 
1 179  SER n 
1 180  GLY n 
1 181  ALA n 
1 182  GLY n 
1 183  LYS n 
1 184  THR n 
1 185  VAL n 
1 186  ASN n 
1 187  THR n 
1 188  LYS n 
1 189  ARG n 
1 190  VAL n 
1 191  ILE n 
1 192  GLN n 
1 193  TYR n 
1 194  PHE n 
1 195  ALA n 
1 196  VAL n 
1 197  ILE n 
1 198  ALA n 
1 199  ALA n 
1 200  ILE n 
1 201  GLY n 
1 202  ASP n 
1 203  ARG n 
1 204  SER n 
1 205  LYS n 
1 206  LYS n 
1 207  ASP n 
1 208  GLN n 
1 209  SER n 
1 210  PRO n 
1 211  GLY n 
1 212  LYS n 
1 213  GLY n 
1 214  THR n 
1 215  LEU n 
1 216  GLU n 
1 217  ASP n 
1 218  GLN n 
1 219  ILE n 
1 220  ILE n 
1 221  GLN n 
1 222  ALA n 
1 223  ASN n 
1 224  PRO n 
1 225  ALA n 
1 226  LEU n 
1 227  GLU n 
1 228  ALA n 
1 229  PHE n 
1 230  GLY n 
1 231  ASN n 
1 232  ALA n 
1 233  LYS n 
1 234  THR n 
1 235  VAL n 
1 236  ARG n 
1 237  ASN n 
1 238  ASP n 
1 239  ASN n 
1 240  SER n 
1 241  SER n 
1 242  ARG n 
1 243  PHE n 
1 244  GLY n 
1 245  LYS n 
1 246  PHE n 
1 247  ILE n 
1 248  ARG n 
1 249  ILE n 
1 250  HIS n 
1 251  PHE n 
1 252  GLY n 
1 253  ALA n 
1 254  THR n 
1 255  GLY n 
1 256  LYS n 
1 257  LEU n 
1 258  ALA n 
1 259  SER n 
1 260  ALA n 
1 261  ASP n 
1 262  ILE n 
1 263  GLU n 
1 264  THR n 
1 265  TYR n 
1 266  LEU n 
1 267  LEU n 
1 268  GLU n 
1 269  LYS n 
1 270  SER n 
1 271  ARG n 
1 272  VAL n 
1 273  ILE n 
1 274  PHE n 
1 275  GLN n 
1 276  LEU n 
1 277  LYS n 
1 278  ALA n 
1 279  GLU n 
1 280  ARG n 
1 281  ASP n 
1 282  TYR n 
1 283  HIS n 
1 284  ILE n 
1 285  PHE n 
1 286  TYR n 
1 287  GLN n 
1 288  ILE n 
1 289  LEU n 
1 290  SER n 
1 291  ASN n 
1 292  LYS n 
1 293  LYS n 
1 294  PRO n 
1 295  GLU n 
1 296  LEU n 
1 297  LEU n 
1 298  ASP n 
1 299  MET n 
1 300  LEU n 
1 301  LEU n 
1 302  ILE n 
1 303  THR n 
1 304  ASN n 
1 305  ASN n 
1 306  PRO n 
1 307  TYR n 
1 308  ASP n 
1 309  TYR n 
1 310  ALA n 
1 311  PHE n 
1 312  ILE n 
1 313  SER n 
1 314  GLN n 
1 315  GLY n 
1 316  GLU n 
1 317  THR n 
1 318  THR n 
1 319  VAL n 
1 320  ALA n 
1 321  SER n 
1 322  ILE n 
1 323  ASP n 
1 324  ASP n 
1 325  ALA n 
1 326  GLU n 
1 327  GLU n 
1 328  LEU n 
1 329  MET n 
1 330  ALA n 
1 331  THR n 
1 332  ASP n 
1 333  ASN n 
1 334  ALA n 
1 335  PHE n 
1 336  ASP n 
1 337  VAL n 
1 338  LEU n 
1 339  GLY n 
1 340  PHE n 
1 341  THR n 
1 342  SER n 
1 343  GLU n 
1 344  GLU n 
1 345  LYS n 
1 346  ASN n 
1 347  SER n 
1 348  MET n 
1 349  TYR n 
1 350  LYS n 
1 351  LEU n 
1 352  THR n 
1 353  GLY n 
1 354  ALA n 
1 355  ILE n 
1 356  MET n 
1 357  HIS n 
1 358  PHE n 
1 359  GLY n 
1 360  ASN n 
1 361  MET n 
1 362  LYS n 
1 363  PHE n 
1 364  LYS n 
1 365  LEU n 
1 366  LYS n 
1 367  GLN n 
1 368  ARG n 
1 369  GLU n 
1 370  GLU n 
1 371  GLN n 
1 372  ALA n 
1 373  GLU n 
1 374  PRO n 
1 375  ASP n 
1 376  GLY n 
1 377  THR n 
1 378  GLU n 
1 379  GLU n 
1 380  ALA n 
1 381  ASP n 
1 382  LYS n 
1 383  SER n 
1 384  ALA n 
1 385  TYR n 
1 386  LEU n 
1 387  MET n 
1 388  GLY n 
1 389  LEU n 
1 390  ASN n 
1 391  SER n 
1 392  ALA n 
1 393  ASP n 
1 394  LEU n 
1 395  LEU n 
1 396  LYS n 
1 397  GLY n 
1 398  LEU n 
1 399  CYS n 
1 400  HIS n 
1 401  PRO n 
1 402  ARG n 
1 403  VAL n 
1 404  LYS n 
1 405  VAL n 
1 406  GLY n 
1 407  ASN n 
1 408  GLU n 
1 409  TYR n 
1 410  VAL n 
1 411  THR n 
1 412  LYS n 
1 413  GLY n 
1 414  GLN n 
1 415  ASN n 
1 416  VAL n 
1 417  GLN n 
1 418  GLN n 
1 419  VAL n 
1 420  ILE n 
1 421  TYR n 
1 422  ALA n 
1 423  THR n 
1 424  GLY n 
1 425  ALA n 
1 426  LEU n 
1 427  ALA n 
1 428  LYS n 
1 429  ALA n 
1 430  VAL n 
1 431  TYR n 
1 432  GLU n 
1 433  ARG n 
1 434  MET n 
1 435  PHE n 
1 436  ASN n 
1 437  TRP n 
1 438  MET n 
1 439  VAL n 
1 440  THR n 
1 441  ARG n 
1 442  ILE n 
1 443  ASN n 
1 444  ALA n 
1 445  THR n 
1 446  LEU n 
1 447  GLU n 
1 448  THR n 
1 449  LYS n 
1 450  GLN n 
1 451  PRO n 
1 452  ARG n 
1 453  GLN n 
1 454  TYR n 
1 455  PHE n 
1 456  ILE n 
1 457  GLY n 
1 458  VAL n 
1 459  LEU n 
1 460  ASP n 
1 461  ILE n 
1 462  ALA n 
1 463  GLY n 
1 464  PHE n 
1 465  GLU n 
1 466  ILE n 
1 467  PHE n 
1 468  ASP n 
1 469  PHE n 
1 470  ASN n 
1 471  SER n 
1 472  PHE n 
1 473  GLU n 
1 474  GLN n 
1 475  LEU n 
1 476  CYS n 
1 477  ILE n 
1 478  ASN n 
1 479  PHE n 
1 480  THR n 
1 481  ASN n 
1 482  GLU n 
1 483  LYS n 
1 484  LEU n 
1 485  GLN n 
1 486  GLN n 
1 487  PHE n 
1 488  PHE n 
1 489  ASN n 
1 490  HIS n 
1 491  HIS n 
1 492  MET n 
1 493  PHE n 
1 494  VAL n 
1 495  LEU n 
1 496  GLU n 
1 497  GLN n 
1 498  GLU n 
1 499  GLU n 
1 500  TYR n 
1 501  LYS n 
1 502  LYS n 
1 503  GLU n 
1 504  GLY n 
1 505  ILE n 
1 506  GLU n 
1 507  TRP n 
1 508  THR n 
1 509  PHE n 
1 510  ILE n 
1 511  ASP n 
1 512  PHE n 
1 513  GLY n 
1 514  MET n 
1 515  ASP n 
1 516  LEU n 
1 517  GLN n 
1 518  ALA n 
1 519  CYS n 
1 520  ILE n 
1 521  ASP n 
1 522  LEU n 
1 523  ILE n 
1 524  GLU n 
1 525  LYS n 
1 526  PRO n 
1 527  MET n 
1 528  GLY n 
1 529  ILE n 
1 530  MET n 
1 531  SER n 
1 532  ILE n 
1 533  LEU n 
1 534  GLU n 
1 535  GLU n 
1 536  GLU n 
1 537  CYS n 
1 538  MET n 
1 539  PHE n 
1 540  PRO n 
1 541  LYS n 
1 542  ALA n 
1 543  THR n 
1 544  ASP n 
1 545  MET n 
1 546  THR n 
1 547  PHE n 
1 548  LYS n 
1 549  ALA n 
1 550  LYS n 
1 551  LEU n 
1 552  PHE n 
1 553  ASP n 
1 554  ASN n 
1 555  HIS n 
1 556  LEU n 
1 557  GLY n 
1 558  LYS n 
1 559  SER n 
1 560  ALA n 
1 561  ASN n 
1 562  PHE n 
1 563  GLN n 
1 564  LYS n 
1 565  PRO n 
1 566  ARG n 
1 567  ASN n 
1 568  ILE n 
1 569  LYS n 
1 570  GLY n 
1 571  LYS n 
1 572  PRO n 
1 573  GLU n 
1 574  ALA n 
1 575  HIS n 
1 576  PHE n 
1 577  SER n 
1 578  LEU n 
1 579  ILE n 
1 580  HIS n 
1 581  TYR n 
1 582  ALA n 
1 583  GLY n 
1 584  ILE n 
1 585  VAL n 
1 586  ASP n 
1 587  TYR n 
1 588  ASN n 
1 589  ILE n 
1 590  ILE n 
1 591  GLY n 
1 592  TRP n 
1 593  LEU n 
1 594  GLN n 
1 595  LYS n 
1 596  ASN n 
1 597  LYS n 
1 598  ASP n 
1 599  PRO n 
1 600  LEU n 
1 601  ASN n 
1 602  GLU n 
1 603  THR n 
1 604  VAL n 
1 605  VAL n 
1 606  GLY n 
1 607  LEU n 
1 608  TYR n 
1 609  GLN n 
1 610  LYS n 
1 611  SER n 
1 612  SER n 
1 613  LEU n 
1 614  LYS n 
1 615  LEU n 
1 616  LEU n 
1 617  SER n 
1 618  THR n 
1 619  LEU n 
1 620  PHE n 
1 621  ALA n 
1 622  ASN n 
1 623  TYR n 
1 624  ALA n 
1 625  GLY n 
1 626  ALA n 
1 627  ASP n 
1 628  ALA n 
1 629  PRO n 
1 630  ILE n 
1 631  GLU n 
1 632  LYS n 
1 633  GLY n 
1 634  LYS n 
1 635  GLY n 
1 636  LYS n 
1 637  ALA n 
1 638  LYS n 
1 639  LYS n 
1 640  GLY n 
1 641  SER n 
1 642  SER n 
1 643  PHE n 
1 644  GLN n 
1 645  THR n 
1 646  VAL n 
1 647  SER n 
1 648  ALA n 
1 649  LEU n 
1 650  HIS n 
1 651  ARG n 
1 652  GLU n 
1 653  ASN n 
1 654  LEU n 
1 655  ASN n 
1 656  LYS n 
1 657  LEU n 
1 658  MET n 
1 659  THR n 
1 660  ASN n 
1 661  LEU n 
1 662  ARG n 
1 663  SER n 
1 664  THR n 
1 665  HIS n 
1 666  PRO n 
1 667  HIS n 
1 668  PHE n 
1 669  VAL n 
1 670  ARG n 
1 671  CYS n 
1 672  ILE n 
1 673  ILE n 
1 674  PRO n 
1 675  ASN n 
1 676  GLU n 
1 677  THR n 
1 678  LYS n 
1 679  SER n 
1 680  PRO n 
1 681  GLY n 
1 682  VAL n 
1 683  MET n 
1 684  ASP n 
1 685  ASN n 
1 686  PRO n 
1 687  LEU n 
1 688  VAL n 
1 689  MET n 
1 690  HIS n 
1 691  GLN n 
1 692  LEU n 
1 693  ARG n 
1 694  CYS n 
1 695  ASN n 
1 696  GLY n 
1 697  VAL n 
1 698  LEU n 
1 699  GLU n 
1 700  GLY n 
1 701  ILE n 
1 702  ARG n 
1 703  ILE n 
1 704  CYS n 
1 705  ARG n 
1 706  LYS n 
1 707  GLY n 
1 708  PHE n 
1 709  PRO n 
1 710  ASN n 
1 711  ARG n 
1 712  ILE n 
1 713  LEU n 
1 714  TYR n 
1 715  GLY n 
1 716  ASP n 
1 717  PHE n 
1 718  ARG n 
1 719  GLN n 
1 720  ARG n 
1 721  TYR n 
1 722  ARG n 
1 723  ILE n 
1 724  LEU n 
1 725  ASN n 
1 726  PRO n 
1 727  ALA n 
1 728  ALA n 
1 729  ILE n 
1 730  PRO n 
1 731  GLU n 
1 732  GLY n 
1 733  GLN n 
1 734  PHE n 
1 735  ILE n 
1 736  ASP n 
1 737  SER n 
1 738  ARG n 
1 739  LYS n 
1 740  GLY n 
1 741  ALA n 
1 742  GLU n 
1 743  LYS n 
1 744  LEU n 
1 745  LEU n 
1 746  SER n 
1 747  SER n 
1 748  LEU n 
1 749  ASP n 
1 750  ILE n 
1 751  ASP n 
1 752  HIS n 
1 753  ASN n 
1 754  GLN n 
1 755  TYR n 
1 756  LYS n 
1 757  PHE n 
1 758  GLY n 
1 759  HIS n 
1 760  THR n 
1 761  LYS n 
1 762  VAL n 
1 763  PHE n 
1 764  PHE n 
1 765  LYS n 
1 766  ALA n 
1 767  GLY n 
1 768  LEU n 
1 769  LEU n 
1 770  GLY n 
1 771  LEU n 
1 772  LEU n 
1 773  GLU n 
1 774  GLU n 
1 775  MET n 
1 776  ARG n 
1 777  ASP n 
1 778  GLU n 
1 779  ARG n 
1 780  LEU n 
1 781  SER n 
1 782  ARG n 
1 783  ILE n 
1 784  ILE n 
1 785  THR n 
1 786  ARG n 
1 787  ILE n 
1 788  GLN n 
1 789  ALA n 
1 790  GLN n 
1 791  SER n 
1 792  ARG n 
1 793  GLY n 
1 794  VAL n 
1 795  LEU n 
1 796  ALA n 
1 797  ARG n 
1 798  MET n 
1 799  GLU n 
1 800  TYR n 
1 801  LYS n 
1 802  LYS n 
1 803  LEU n 
1 804  LEU n 
1 805  GLU n 
1 806  ARG n 
1 807  ARG n 
1 808  ASP n 
1 809  SER n 
1 810  LEU n 
1 811  LEU n 
1 812  VAL n 
1 813  ILE n 
1 814  GLN n 
1 815  TRP n 
1 816  ASN n 
1 817  ILE n 
1 818  ARG n 
1 819  ALA n 
1 820  PHE n 
1 821  MET n 
1 822  GLY n 
1 823  VAL n 
1 824  LYS n 
1 825  ASN n 
1 826  TRP n 
1 827  PRO n 
1 828  TRP n 
1 829  MET n 
1 830  LYS n 
1 831  LEU n 
1 832  TYR n 
1 833  PHE n 
1 834  LYS n 
1 835  ILE n 
1 836  LYS n 
1 837  PRO n 
1 838  LEU n 
1 839  LEU n 
1 840  LYS n 
1 841  SER n 
1 842  ALA n 
1 843  GLU n 
1 844  ARG n 
1 845  GLU n 
1 846  LYS n 
1 847  GLU n 
1 848  MET n 
1 849  ALA n 
1 850  SER n 
1 851  MET n 
1 852  LYS n 
1 853  GLU n 
1 854  GLU n 
1 855  PHE n 
1 856  THR n 
1 857  ARG n 
1 858  LEU n 
1 859  LYS n 
1 860  GLU n 
1 861  ALA n 
1 862  LEU n 
1 863  GLU n 
1 864  LYS n 
1 865  SER n 
1 866  GLU n 
1 867  ALA n 
1 868  ARG n 
1 869  ARG n 
1 870  LYS n 
1 871  GLU n 
1 872  LEU n 
1 873  GLU n 
1 874  GLU n 
1 875  LYS n 
1 876  MET n 
1 877  VAL n 
1 878  SER n 
1 879  LEU n 
1 880  LEU n 
1 881  GLN n 
1 882  GLU n 
1 883  LYS n 
1 884  ASN n 
1 885  ASP n 
1 886  LEU n 
1 887  GLN n 
1 888  LEU n 
1 889  GLN n 
1 890  VAL n 
1 891  GLN n 
1 892  ALA n 
1 893  GLU n 
1 894  GLN n 
1 895  ASP n 
1 896  ASN n 
1 897  LEU n 
1 898  ALA n 
1 899  ASP n 
1 900  ALA n 
1 901  GLU n 
1 902  GLU n 
1 903  ARG n 
1 904  CYS n 
1 905  ASP n 
1 906  GLN n 
1 907  LEU n 
1 908  ILE n 
1 909  LYS n 
1 910  ASN n 
1 911  LYS n 
1 912  ILE n 
1 913  GLN n 
1 914  LEU n 
1 915  GLU n 
1 916  ALA n 
1 917  LYS n 
1 918  VAL n 
1 919  LYS n 
1 920  GLU n 
1 921  MET n 
1 922  ASN n 
1 923  GLU n 
1 924  ARG n 
1 925  LEU n 
1 926  GLU n 
1 927  ASP n 
1 928  GLU n 
1 929  GLU n 
1 930  GLU n 
1 931  MET n 
1 932  ASN n 
1 933  ALA n 
1 934  GLU n 
1 935  LEU n 
1 936  THR n 
1 937  ALA n 
1 938  LYS n 
1 939  LYS n 
1 940  ARG n 
1 941  LYS n 
1 942  LEU n 
1 943  GLU n 
1 944  ASP n 
1 945  GLU n 
1 946  CYS n 
1 947  SER n 
1 948  GLU n 
1 949  LEU n 
1 950  LYS n 
1 951  ARG n 
1 952  ASP n 
1 953  ILE n 
1 954  ASP n 
1 955  ASP n 
1 956  LEU n 
1 957  GLU n 
1 958  LEU n 
1 959  THR n 
1 960  LEU n 
1 961  ALA n 
1 962  LYS n 
1 963  VAL n 
1 964  GLU n 
1 965  LYS n 
1 966  GLU n 
1 967  LYS n 
1 968  HIS n 
1 969  ALA n 
1 970  THR n 
1 971  GLU n 
1 972  ASN n 
1 973  LYS n 
1 974  VAL n 
1 975  LYS n 
1 976  ASN n 
1 977  LEU n 
1 978  THR n 
1 979  GLU n 
1 980  GLU n 
1 981  MET n 
1 982  ALA n 
1 983  GLY n 
1 984  LEU n 
1 985  ASP n 
1 986  GLU n 
1 987  ILE n 
1 988  ILE n 
1 989  ALA n 
1 990  LYS n 
1 991  LEU n 
1 992  THR n 
1 993  LYS n 
1 994  GLU n 
1 995  LYS n 
1 996  LYS n 
1 997  ALA n 
1 998  LEU n 
1 999  GLN n 
1 1000 GLU n 
1 1001 ALA n 
1 1002 HIS n 
1 1003 GLN n 
1 1004 GLN n 
1 1005 ALA n 
1 1006 LEU n 
1 1007 ASP n 
1 1008 ASP n 
1 1009 LEU n 
1 1010 GLN n 
1 1011 ALA n 
1 1012 GLU n 
1 1013 GLU n 
1 1014 ASP n 
1 1015 LYS n 
1 1016 VAL n 
1 1017 ASN n 
1 1018 THR n 
1 1019 LEU n 
1 1020 THR n 
1 1021 LYS n 
1 1022 ALA n 
1 1023 LYS n 
1 1024 VAL n 
1 1025 LYS n 
1 1026 LEU n 
1 1027 GLU n 
1 1028 GLN n 
1 1029 GLN n 
1 1030 VAL n 
1 1031 ASP n 
1 1032 ASP n 
1 1033 LEU n 
1 1034 GLU n 
1 1035 GLY n 
1 1036 SER n 
1 1037 LEU n 
1 1038 GLU n 
1 1039 GLN n 
1 1040 GLU n 
1 1041 LYS n 
1 1042 LYS n 
1 1043 VAL n 
1 1044 ARG n 
1 1045 MET n 
1 1046 ASP n 
1 1047 LEU n 
1 1048 GLU n 
1 1049 ARG n 
1 1050 ALA n 
1 1051 LYS n 
1 1052 ARG n 
1 1053 LYS n 
1 1054 LEU n 
1 1055 GLU n 
1 1056 GLY n 
1 1057 ASP n 
1 1058 LEU n 
1 1059 LYS n 
1 1060 LEU n 
1 1061 THR n 
1 1062 GLN n 
1 1063 GLU n 
1 1064 SER n 
1 1065 ILE n 
1 1066 MET n 
1 1067 ASP n 
1 1068 LEU n 
1 1069 GLU n 
1 1070 ASN n 
1 1071 ASP n 
1 1072 LYS n 
1 1073 GLN n 
1 1074 GLN n 
1 1075 LEU n 
1 1076 ASP n 
1 1077 GLU n 
1 1078 ARG n 
1 1079 LEU n 
1 1080 LYS n 
1 1081 LYS n 
1 1082 LYS n 
1 1083 ASP n 
1 1084 PHE n 
1 1085 GLU n 
1 1086 LEU n 
1 1087 ASN n 
1 1088 ALA n 
1 1089 LEU n 
1 1090 ASN n 
1 1091 ALA n 
1 1092 ARG n 
1 1093 ILE n 
1 1094 GLU n 
1 1095 ASP n 
1 1096 GLU n 
1 1097 GLN n 
1 1098 ALA n 
1 1099 LEU n 
1 1100 GLY n 
1 1101 SER n 
1 1102 GLN n 
1 1103 LEU n 
1 1104 GLN n 
1 1105 LYS n 
1 1106 LYS n 
1 1107 LEU n 
1 1108 LYS n 
1 1109 GLU n 
1 1110 LEU n 
1 1111 GLN n 
1 1112 ALA n 
1 1113 ARG n 
1 1114 ILE n 
1 1115 GLU n 
1 1116 GLU n 
1 1117 LEU n 
1 1118 GLU n 
1 1119 GLU n 
1 1120 GLU n 
1 1121 LEU n 
1 1122 GLU n 
1 1123 SER n 
1 1124 GLU n 
1 1125 ARG n 
1 1126 THR n 
1 1127 ALA n 
1 1128 ARG n 
1 1129 ALA n 
1 1130 LYS n 
1 1131 VAL n 
1 1132 GLU n 
1 1133 LYS n 
1 1134 LEU n 
1 1135 ARG n 
1 1136 SER n 
1 1137 ASP n 
1 1138 ASP n 
1 1139 TYR n 
1 1140 LYS n 
1 1141 ASP n 
1 1142 ASP n 
1 1143 ASP n 
1 1144 ASP n 
1 1145 LYS 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                   1145 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'MYH7, MYHCB' 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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      'Mus musculus' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     10090 
_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 
PO4 non-polymer         . 'PHOSPHATE ION'            ? 'O4 P -3'           94.971  
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 
# 
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    GLY 1    2    ?   ?   ?   A . n 
A 1 2    ASP 2    3    3   ASP ASP A . n 
A 1 3    SER 3    4    4   SER SER A . n 
A 1 4    GLU 4    5    5   GLU GLU A . n 
A 1 5    MET 5    6    6   MET MET A . n 
A 1 6    ALA 6    7    7   ALA ALA A . n 
A 1 7    VAL 7    8    8   VAL VAL A . n 
A 1 8    PHE 8    9    9   PHE PHE A . n 
A 1 9    GLY 9    10   10  GLY GLY A . n 
A 1 10   ALA 10   11   11  ALA ALA A . n 
A 1 11   ALA 11   12   12  ALA ALA A . n 
A 1 12   ALA 12   13   13  ALA ALA A . n 
A 1 13   PRO 13   14   14  PRO PRO A . n 
A 1 14   TYR 14   15   15  TYR TYR A . n 
A 1 15   LEU 15   16   16  LEU LEU A . n 
A 1 16   ARG 16   17   17  ARG ARG A . n 
A 1 17   LYS 17   18   18  LYS LYS A . n 
A 1 18   SER 18   19   19  SER SER A . n 
A 1 19   GLU 19   20   20  GLU GLU A . n 
A 1 20   LYS 20   21   21  LYS LYS A . n 
A 1 21   GLU 21   22   22  GLU GLU A . n 
A 1 22   ARG 22   23   23  ARG ARG A . n 
A 1 23   LEU 23   24   24  LEU LEU A . n 
A 1 24   GLU 24   25   25  GLU GLU A . n 
A 1 25   ALA 25   26   26  ALA ALA A . n 
A 1 26   GLN 26   27   27  GLN GLN A . n 
A 1 27   THR 27   28   28  THR THR A . n 
A 1 28   ARG 28   29   29  ARG ARG A . n 
A 1 29   PRO 29   30   30  PRO PRO A . n 
A 1 30   PHE 30   31   31  PHE PHE A . n 
A 1 31   ASP 31   32   32  ASP ASP A . n 
A 1 32   LEU 32   33   33  LEU LEU A . n 
A 1 33   LYS 33   34   34  LYS LYS A . n 
A 1 34   LYS 34   35   35  LYS LYS A . n 
A 1 35   ASP 35   36   36  ASP ASP A . n 
A 1 36   VAL 36   37   37  VAL VAL A . n 
A 1 37   PHE 37   38   38  PHE PHE A . n 
A 1 38   VAL 38   39   39  VAL VAL A . n 
A 1 39   PRO 39   40   40  PRO PRO A . n 
A 1 40   ASP 40   41   41  ASP ASP A . n 
A 1 41   ASP 41   42   42  ASP ASP A . n 
A 1 42   LYS 42   43   43  LYS LYS A . n 
A 1 43   GLN 43   44   44  GLN GLN A . n 
A 1 44   GLU 44   45   45  GLU GLU A . n 
A 1 45   PHE 45   46   46  PHE PHE A . n 
A 1 46   VAL 46   47   47  VAL VAL A . n 
A 1 47   LYS 47   48   48  LYS LYS A . n 
A 1 48   ALA 48   49   49  ALA ALA A . n 
A 1 49   LYS 49   50   50  LYS LYS A . n 
A 1 50   ILE 50   51   51  ILE ILE A . n 
A 1 51   VAL 51   52   52  VAL VAL A . n 
A 1 52   SER 52   53   53  SER SER A . n 
A 1 53   ARG 53   54   54  ARG ARG A . n 
A 1 54   GLU 54   55   55  GLU GLU A . n 
A 1 55   GLY 55   56   56  GLY GLY A . n 
A 1 56   GLY 56   57   57  GLY GLY A . n 
A 1 57   LYS 57   58   58  LYS LYS A . n 
A 1 58   VAL 58   59   59  VAL VAL A . n 
A 1 59   THR 59   60   60  THR THR A . n 
A 1 60   ALA 60   61   61  ALA ALA A . n 
A 1 61   GLU 61   62   62  GLU GLU A . n 
A 1 62   THR 62   63   63  THR THR A . n 
A 1 63   GLU 63   64   64  GLU GLU A . n 
A 1 64   TYR 64   65   65  TYR TYR A . n 
A 1 65   GLY 65   66   66  GLY GLY A . n 
A 1 66   LYS 66   67   67  LYS LYS A . n 
A 1 67   THR 67   68   68  THR THR A . n 
A 1 68   VAL 68   69   69  VAL VAL A . n 
A 1 69   THR 69   70   70  THR THR A . n 
A 1 70   VAL 70   71   71  VAL VAL A . n 
A 1 71   LYS 71   72   72  LYS LYS A . n 
A 1 72   GLU 72   73   73  GLU GLU A . n 
A 1 73   ASP 73   74   74  ASP ASP A . n 
A 1 74   GLN 74   75   75  GLN GLN A . n 
A 1 75   VAL 75   76   76  VAL VAL A . n 
A 1 76   MET 76   77   77  MET MET A . n 
A 1 77   GLN 77   78   78  GLN GLN A . n 
A 1 78   GLN 78   79   79  GLN GLN A . n 
A 1 79   ASN 79   80   80  ASN ASN A . n 
A 1 80   PRO 80   81   81  PRO PRO A . n 
A 1 81   PRO 81   82   82  PRO PRO A . n 
A 1 82   LYS 82   83   83  LYS LYS A . n 
A 1 83   PHE 83   84   84  PHE PHE A . n 
A 1 84   ASP 84   85   85  ASP ASP A . n 
A 1 85   LYS 85   86   86  LYS LYS A . n 
A 1 86   ILE 86   87   87  ILE ILE A . n 
A 1 87   GLU 87   88   88  GLU GLU A . n 
A 1 88   ASP 88   89   89  ASP ASP A . n 
A 1 89   MET 89   90   90  MET MET A . n 
A 1 90   ALA 90   91   91  ALA ALA A . n 
A 1 91   MET 91   92   92  MET MET A . n 
A 1 92   LEU 92   93   93  LEU LEU A . n 
A 1 93   THR 93   94   94  THR THR A . n 
A 1 94   PHE 94   95   95  PHE PHE A . n 
A 1 95   LEU 95   96   96  LEU LEU A . n 
A 1 96   HIS 96   97   97  HIS HIS A . n 
A 1 97   GLU 97   98   98  GLU GLU A . n 
A 1 98   PRO 98   99   99  PRO PRO A . n 
A 1 99   ALA 99   100  100 ALA ALA A . n 
A 1 100  VAL 100  101  101 VAL VAL A . n 
A 1 101  LEU 101  102  102 LEU LEU A . n 
A 1 102  TYR 102  103  103 TYR TYR A . n 
A 1 103  ASN 103  104  104 ASN ASN A . n 
A 1 104  LEU 104  105  105 LEU LEU A . n 
A 1 105  LYS 105  106  106 LYS LYS A . n 
A 1 106  ASP 106  107  107 ASP ASP A . n 
A 1 107  ARG 107  108  108 ARG ARG A . n 
A 1 108  TYR 108  109  109 TYR TYR A . n 
A 1 109  GLY 109  110  110 GLY GLY A . n 
A 1 110  SER 110  111  111 SER SER A . n 
A 1 111  TRP 111  112  112 TRP TRP A . n 
A 1 112  MET 112  113  113 MET MET A . n 
A 1 113  ILE 113  114  114 ILE ILE A . n 
A 1 114  TYR 114  115  115 TYR TYR A . n 
A 1 115  THR 115  116  116 THR THR A . n 
A 1 116  TYR 116  117  117 TYR TYR A . n 
A 1 117  SER 117  118  118 SER SER A . n 
A 1 118  GLY 118  119  119 GLY GLY A . n 
A 1 119  LEU 119  120  120 LEU LEU A . n 
A 1 120  PHE 120  121  121 PHE PHE A . n 
A 1 121  CYS 121  122  122 CYS CYS A . n 
A 1 122  VAL 122  123  123 VAL VAL A . n 
A 1 123  THR 123  124  124 THR THR A . n 
A 1 124  VAL 124  125  125 VAL VAL A . n 
A 1 125  ASN 125  126  126 ASN ASN A . n 
A 1 126  PRO 126  127  127 PRO PRO A . n 
A 1 127  TYR 127  128  128 TYR TYR A . n 
A 1 128  LYS 128  129  129 LYS LYS A . n 
A 1 129  TRP 129  130  130 TRP TRP A . n 
A 1 130  LEU 130  131  131 LEU LEU A . n 
A 1 131  PRO 131  132  132 PRO PRO A . n 
A 1 132  VAL 132  133  133 VAL VAL A . n 
A 1 133  TYR 133  134  134 TYR TYR A . n 
A 1 134  THR 134  135  135 THR THR A . n 
A 1 135  PRO 135  136  136 PRO PRO A . n 
A 1 136  GLU 136  137  137 GLU GLU A . n 
A 1 137  VAL 137  138  138 VAL VAL A . n 
A 1 138  VAL 138  139  139 VAL VAL A . n 
A 1 139  ALA 139  140  140 ALA ALA A . n 
A 1 140  ALA 140  141  141 ALA ALA A . n 
A 1 141  TYR 141  142  142 TYR TYR A . n 
A 1 142  ARG 142  143  143 ARG ARG A . n 
A 1 143  GLY 143  144  144 GLY GLY A . n 
A 1 144  LYS 144  145  145 LYS LYS A . n 
A 1 145  LYS 145  146  146 LYS LYS A . n 
A 1 146  ARG 146  147  147 ARG ARG A . n 
A 1 147  SER 147  148  148 SER SER A . n 
A 1 148  GLU 148  149  149 GLU GLU A . n 
A 1 149  ALA 149  150  150 ALA ALA A . n 
A 1 150  PRO 150  151  151 PRO PRO A . n 
A 1 151  PRO 151  152  152 PRO PRO A . n 
A 1 152  HIS 152  153  153 HIS HIS A . n 
A 1 153  ILE 153  154  154 ILE ILE A . n 
A 1 154  PHE 154  155  155 PHE PHE A . n 
A 1 155  SER 155  156  156 SER SER A . n 
A 1 156  ILE 156  157  157 ILE ILE A . n 
A 1 157  SER 157  158  158 SER SER A . n 
A 1 158  ASP 158  159  159 ASP ASP A . n 
A 1 159  ASN 159  160  160 ASN ASN A . n 
A 1 160  ALA 160  161  161 ALA ALA A . n 
A 1 161  TYR 161  162  162 TYR TYR A . n 
A 1 162  GLN 162  163  163 GLN GLN A . n 
A 1 163  TYR 163  164  164 TYR TYR A . n 
A 1 164  MET 164  165  165 MET MET A . n 
A 1 165  LEU 165  166  166 LEU LEU A . n 
A 1 166  THR 166  167  167 THR THR A . n 
A 1 167  ASP 167  168  168 ASP ASP A . n 
A 1 168  ARG 168  169  169 ARG ARG A . n 
A 1 169  GLU 169  170  170 GLU GLU A . n 
A 1 170  ASN 170  171  171 ASN ASN A . n 
A 1 171  GLN 171  172  172 GLN GLN A . n 
A 1 172  SER 172  173  173 SER SER A . n 
A 1 173  ILE 173  174  174 ILE ILE A . n 
A 1 174  LEU 174  175  175 LEU LEU A . n 
A 1 175  ILE 175  176  176 ILE ILE A . n 
A 1 176  THR 176  177  177 THR THR A . n 
A 1 177  GLY 177  178  178 GLY GLY A . n 
A 1 178  GLU 178  179  179 GLU GLU A . n 
A 1 179  SER 179  180  180 SER SER A . n 
A 1 180  GLY 180  181  181 GLY GLY A . n 
A 1 181  ALA 181  182  182 ALA ALA A . n 
A 1 182  GLY 182  183  183 GLY GLY A . n 
A 1 183  LYS 183  184  184 LYS LYS A . n 
A 1 184  THR 184  185  185 THR THR A . n 
A 1 185  VAL 185  186  186 VAL VAL A . n 
A 1 186  ASN 186  187  187 ASN ASN A . n 
A 1 187  THR 187  188  188 THR THR A . n 
A 1 188  LYS 188  189  189 LYS LYS A . n 
A 1 189  ARG 189  190  190 ARG ARG A . n 
A 1 190  VAL 190  191  191 VAL VAL A . n 
A 1 191  ILE 191  192  192 ILE ILE A . n 
A 1 192  GLN 192  193  193 GLN GLN A . n 
A 1 193  TYR 193  194  194 TYR TYR A . n 
A 1 194  PHE 194  195  195 PHE PHE A . n 
A 1 195  ALA 195  196  196 ALA ALA A . n 
A 1 196  VAL 196  197  197 VAL VAL A . n 
A 1 197  ILE 197  198  198 ILE ILE A . n 
A 1 198  ALA 198  199  199 ALA ALA A . n 
A 1 199  ALA 199  200  200 ALA ALA A . n 
A 1 200  ILE 200  201  201 ILE ILE A . n 
A 1 201  GLY 201  202  202 GLY GLY A . n 
A 1 202  ASP 202  203  ?   ?   ?   A . n 
A 1 203  ARG 203  204  ?   ?   ?   A . n 
A 1 204  SER 204  205  ?   ?   ?   A . n 
A 1 205  LYS 205  206  ?   ?   ?   A . n 
A 1 206  LYS 206  207  ?   ?   ?   A . n 
A 1 207  ASP 207  208  ?   ?   ?   A . n 
A 1 208  GLN 208  209  ?   ?   ?   A . n 
A 1 209  SER 209  210  ?   ?   ?   A . n 
A 1 210  PRO 210  211  ?   ?   ?   A . n 
A 1 211  GLY 211  212  ?   ?   ?   A . n 
A 1 212  LYS 212  213  ?   ?   ?   A . n 
A 1 213  GLY 213  214  214 GLY GLY A . n 
A 1 214  THR 214  215  215 THR THR A . n 
A 1 215  LEU 215  216  216 LEU LEU A . n 
A 1 216  GLU 216  217  217 GLU GLU A . n 
A 1 217  ASP 217  218  218 ASP ASP A . n 
A 1 218  GLN 218  219  219 GLN GLN A . n 
A 1 219  ILE 219  220  220 ILE ILE A . n 
A 1 220  ILE 220  221  221 ILE ILE A . n 
A 1 221  GLN 221  222  222 GLN GLN A . n 
A 1 222  ALA 222  223  223 ALA ALA A . n 
A 1 223  ASN 223  224  224 ASN ASN A . n 
A 1 224  PRO 224  225  225 PRO PRO A . n 
A 1 225  ALA 225  226  226 ALA ALA A . n 
A 1 226  LEU 226  227  227 LEU LEU A . n 
A 1 227  GLU 227  228  228 GLU GLU A . n 
A 1 228  ALA 228  229  229 ALA ALA A . n 
A 1 229  PHE 229  230  230 PHE PHE A . n 
A 1 230  GLY 230  231  231 GLY GLY A . n 
A 1 231  ASN 231  232  232 ASN ASN A . n 
A 1 232  ALA 232  233  233 ALA ALA A . n 
A 1 233  LYS 233  234  234 LYS LYS A . n 
A 1 234  THR 234  235  235 THR THR A . n 
A 1 235  VAL 235  236  236 VAL VAL A . n 
A 1 236  ARG 236  237  237 ARG ARG A . n 
A 1 237  ASN 237  238  238 ASN ASN A . n 
A 1 238  ASP 238  239  239 ASP ASP A . n 
A 1 239  ASN 239  240  240 ASN ASN A . n 
A 1 240  SER 240  241  241 SER SER A . n 
A 1 241  SER 241  242  242 SER SER A . n 
A 1 242  ARG 242  243  243 ARG ARG A . n 
A 1 243  PHE 243  244  244 PHE PHE A . n 
A 1 244  GLY 244  245  245 GLY GLY A . n 
A 1 245  LYS 245  246  246 LYS LYS A . n 
A 1 246  PHE 246  247  247 PHE PHE A . n 
A 1 247  ILE 247  248  248 ILE ILE A . n 
A 1 248  ARG 248  249  249 ARG ARG A . n 
A 1 249  ILE 249  250  250 ILE ILE A . n 
A 1 250  HIS 250  251  251 HIS HIS A . n 
A 1 251  PHE 251  252  252 PHE PHE A . n 
A 1 252  GLY 252  253  253 GLY GLY A . n 
A 1 253  ALA 253  254  254 ALA ALA A . n 
A 1 254  THR 254  255  255 THR THR A . n 
A 1 255  GLY 255  256  256 GLY GLY A . n 
A 1 256  LYS 256  257  257 LYS LYS A . n 
A 1 257  LEU 257  258  258 LEU LEU A . n 
A 1 258  ALA 258  259  259 ALA ALA A . n 
A 1 259  SER 259  260  260 SER SER A . n 
A 1 260  ALA 260  261  261 ALA ALA A . n 
A 1 261  ASP 261  262  262 ASP ASP A . n 
A 1 262  ILE 262  263  263 ILE ILE A . n 
A 1 263  GLU 263  264  264 GLU GLU A . n 
A 1 264  THR 264  265  265 THR THR A . n 
A 1 265  TYR 265  266  266 TYR TYR A . n 
A 1 266  LEU 266  267  267 LEU LEU A . n 
A 1 267  LEU 267  268  268 LEU LEU A . n 
A 1 268  GLU 268  269  269 GLU GLU A . n 
A 1 269  LYS 269  270  270 LYS LYS A . n 
A 1 270  SER 270  271  271 SER SER A . n 
A 1 271  ARG 271  272  272 ARG ARG A . n 
A 1 272  VAL 272  273  273 VAL VAL A . n 
A 1 273  ILE 273  274  274 ILE ILE A . n 
A 1 274  PHE 274  275  275 PHE PHE A . n 
A 1 275  GLN 275  276  276 GLN GLN A . n 
A 1 276  LEU 276  277  277 LEU LEU A . n 
A 1 277  LYS 277  278  278 LYS LYS A . n 
A 1 278  ALA 278  279  279 ALA ALA A . n 
A 1 279  GLU 279  280  280 GLU GLU A . n 
A 1 280  ARG 280  281  281 ARG ARG A . n 
A 1 281  ASP 281  282  282 ASP ASP A . n 
A 1 282  TYR 282  283  283 TYR TYR A . n 
A 1 283  HIS 283  284  284 HIS HIS A . n 
A 1 284  ILE 284  285  285 ILE ILE A . n 
A 1 285  PHE 285  286  286 PHE PHE A . n 
A 1 286  TYR 286  287  287 TYR TYR A . n 
A 1 287  GLN 287  288  288 GLN GLN A . n 
A 1 288  ILE 288  289  289 ILE ILE A . n 
A 1 289  LEU 289  290  290 LEU LEU A . n 
A 1 290  SER 290  291  291 SER SER A . n 
A 1 291  ASN 291  292  292 ASN ASN A . n 
A 1 292  LYS 292  293  293 LYS LYS A . n 
A 1 293  LYS 293  294  294 LYS LYS A . n 
A 1 294  PRO 294  295  295 PRO PRO A . n 
A 1 295  GLU 295  296  296 GLU GLU A . n 
A 1 296  LEU 296  297  297 LEU LEU A . n 
A 1 297  LEU 297  298  298 LEU LEU A . n 
A 1 298  ASP 298  299  299 ASP ASP A . n 
A 1 299  MET 299  300  300 MET MET A . n 
A 1 300  LEU 300  301  301 LEU LEU A . n 
A 1 301  LEU 301  302  302 LEU LEU A . n 
A 1 302  ILE 302  303  303 ILE ILE A . n 
A 1 303  THR 303  304  304 THR THR A . n 
A 1 304  ASN 304  305  305 ASN ASN A . n 
A 1 305  ASN 305  306  306 ASN ASN A . n 
A 1 306  PRO 306  307  307 PRO PRO A . n 
A 1 307  TYR 307  308  308 TYR TYR A . n 
A 1 308  ASP 308  309  309 ASP ASP A . n 
A 1 309  TYR 309  310  310 TYR TYR A . n 
A 1 310  ALA 310  311  311 ALA ALA A . n 
A 1 311  PHE 311  312  312 PHE PHE A . n 
A 1 312  ILE 312  313  313 ILE ILE A . n 
A 1 313  SER 313  314  314 SER SER A . n 
A 1 314  GLN 314  315  315 GLN GLN A . n 
A 1 315  GLY 315  316  316 GLY GLY A . n 
A 1 316  GLU 316  317  317 GLU GLU A . n 
A 1 317  THR 317  318  318 THR THR A . n 
A 1 318  THR 318  319  319 THR THR A . n 
A 1 319  VAL 319  320  320 VAL VAL A . n 
A 1 320  ALA 320  321  321 ALA ALA A . n 
A 1 321  SER 321  322  322 SER SER A . n 
A 1 322  ILE 322  323  323 ILE ILE A . n 
A 1 323  ASP 323  324  324 ASP ASP A . n 
A 1 324  ASP 324  325  325 ASP ASP A . n 
A 1 325  ALA 325  326  326 ALA ALA A . n 
A 1 326  GLU 326  327  327 GLU GLU A . n 
A 1 327  GLU 327  328  328 GLU GLU A . n 
A 1 328  LEU 328  329  329 LEU LEU A . n 
A 1 329  MET 329  330  330 MET MET A . n 
A 1 330  ALA 330  331  331 ALA ALA A . n 
A 1 331  THR 331  332  332 THR THR A . n 
A 1 332  ASP 332  333  333 ASP ASP A . n 
A 1 333  ASN 333  334  334 ASN ASN A . n 
A 1 334  ALA 334  335  335 ALA ALA A . n 
A 1 335  PHE 335  336  336 PHE PHE A . n 
A 1 336  ASP 336  337  337 ASP ASP A . n 
A 1 337  VAL 337  338  338 VAL VAL A . n 
A 1 338  LEU 338  339  339 LEU LEU A . n 
A 1 339  GLY 339  340  340 GLY GLY A . n 
A 1 340  PHE 340  341  341 PHE PHE A . n 
A 1 341  THR 341  342  342 THR THR A . n 
A 1 342  SER 342  343  343 SER SER A . n 
A 1 343  GLU 343  344  344 GLU GLU A . n 
A 1 344  GLU 344  345  345 GLU GLU A . n 
A 1 345  LYS 345  346  346 LYS LYS A . n 
A 1 346  ASN 346  347  347 ASN ASN A . n 
A 1 347  SER 347  348  348 SER SER A . n 
A 1 348  MET 348  349  349 MET MET A . n 
A 1 349  TYR 349  350  350 TYR TYR A . n 
A 1 350  LYS 350  351  351 LYS LYS A . n 
A 1 351  LEU 351  352  352 LEU LEU A . n 
A 1 352  THR 352  353  353 THR THR A . n 
A 1 353  GLY 353  354  354 GLY GLY A . n 
A 1 354  ALA 354  355  355 ALA ALA A . n 
A 1 355  ILE 355  356  356 ILE ILE A . n 
A 1 356  MET 356  357  357 MET MET A . n 
A 1 357  HIS 357  358  358 HIS HIS A . n 
A 1 358  PHE 358  359  359 PHE PHE A . n 
A 1 359  GLY 359  360  360 GLY GLY A . n 
A 1 360  ASN 360  361  361 ASN ASN A . n 
A 1 361  MET 361  362  362 MET MET A . n 
A 1 362  LYS 362  363  363 LYS LYS A . n 
A 1 363  PHE 363  364  364 PHE PHE A . n 
A 1 364  LYS 364  365  365 LYS LYS A . n 
A 1 365  LEU 365  366  366 LEU LEU A . n 
A 1 366  LYS 366  367  367 LYS LYS A . n 
A 1 367  GLN 367  368  368 GLN GLN A . n 
A 1 368  ARG 368  369  369 ARG ARG A . n 
A 1 369  GLU 369  370  370 GLU GLU A . n 
A 1 370  GLU 370  371  371 GLU GLU A . n 
A 1 371  GLN 371  372  372 GLN GLN A . n 
A 1 372  ALA 372  373  373 ALA ALA A . n 
A 1 373  GLU 373  374  374 GLU GLU A . n 
A 1 374  PRO 374  375  375 PRO PRO A . n 
A 1 375  ASP 375  376  376 ASP ASP A . n 
A 1 376  GLY 376  377  377 GLY GLY A . n 
A 1 377  THR 377  378  378 THR THR A . n 
A 1 378  GLU 378  379  379 GLU GLU A . n 
A 1 379  GLU 379  380  380 GLU GLU A . n 
A 1 380  ALA 380  381  381 ALA ALA A . n 
A 1 381  ASP 381  382  382 ASP ASP A . n 
A 1 382  LYS 382  383  383 LYS LYS A . n 
A 1 383  SER 383  384  384 SER SER A . n 
A 1 384  ALA 384  385  385 ALA ALA A . n 
A 1 385  TYR 385  386  386 TYR TYR A . n 
A 1 386  LEU 386  387  387 LEU LEU A . n 
A 1 387  MET 387  388  388 MET MET A . n 
A 1 388  GLY 388  389  389 GLY GLY A . n 
A 1 389  LEU 389  390  390 LEU LEU A . n 
A 1 390  ASN 390  391  391 ASN ASN A . n 
A 1 391  SER 391  392  392 SER SER A . n 
A 1 392  ALA 392  393  393 ALA ALA A . n 
A 1 393  ASP 393  394  394 ASP ASP A . n 
A 1 394  LEU 394  395  395 LEU LEU A . n 
A 1 395  LEU 395  396  396 LEU LEU A . n 
A 1 396  LYS 396  397  397 LYS LYS A . n 
A 1 397  GLY 397  398  398 GLY GLY A . n 
A 1 398  LEU 398  399  399 LEU LEU A . n 
A 1 399  CYS 399  400  400 CYS CYS A . n 
A 1 400  HIS 400  401  401 HIS HIS A . n 
A 1 401  PRO 401  402  402 PRO PRO A . n 
A 1 402  ARG 402  403  403 ARG ARG A . n 
A 1 403  VAL 403  404  404 VAL VAL A . n 
A 1 404  LYS 404  405  405 LYS LYS A . n 
A 1 405  VAL 405  406  406 VAL VAL A . n 
A 1 406  GLY 406  407  407 GLY GLY A . n 
A 1 407  ASN 407  408  408 ASN ASN A . n 
A 1 408  GLU 408  409  409 GLU GLU A . n 
A 1 409  TYR 409  410  410 TYR TYR A . n 
A 1 410  VAL 410  411  411 VAL VAL A . n 
A 1 411  THR 411  412  412 THR THR A . n 
A 1 412  LYS 412  413  413 LYS LYS A . n 
A 1 413  GLY 413  414  414 GLY GLY A . n 
A 1 414  GLN 414  415  415 GLN GLN A . n 
A 1 415  ASN 415  416  416 ASN ASN A . n 
A 1 416  VAL 416  417  417 VAL VAL A . n 
A 1 417  GLN 417  418  418 GLN GLN A . n 
A 1 418  GLN 418  419  419 GLN GLN A . n 
A 1 419  VAL 419  420  420 VAL VAL A . n 
A 1 420  ILE 420  421  421 ILE ILE A . n 
A 1 421  TYR 421  422  422 TYR TYR A . n 
A 1 422  ALA 422  423  423 ALA ALA A . n 
A 1 423  THR 423  424  424 THR THR A . n 
A 1 424  GLY 424  425  425 GLY GLY A . n 
A 1 425  ALA 425  426  426 ALA ALA A . n 
A 1 426  LEU 426  427  427 LEU LEU A . n 
A 1 427  ALA 427  428  428 ALA ALA A . n 
A 1 428  LYS 428  429  429 LYS LYS A . n 
A 1 429  ALA 429  430  430 ALA ALA A . n 
A 1 430  VAL 430  431  431 VAL VAL A . n 
A 1 431  TYR 431  432  432 TYR TYR A . n 
A 1 432  GLU 432  433  433 GLU GLU A . n 
A 1 433  ARG 433  434  434 ARG ARG A . n 
A 1 434  MET 434  435  435 MET MET A . n 
A 1 435  PHE 435  436  436 PHE PHE A . n 
A 1 436  ASN 436  437  437 ASN ASN A . n 
A 1 437  TRP 437  438  438 TRP TRP A . n 
A 1 438  MET 438  439  439 MET MET A . n 
A 1 439  VAL 439  440  440 VAL VAL A . n 
A 1 440  THR 440  441  441 THR THR A . n 
A 1 441  ARG 441  442  442 ARG ARG A . n 
A 1 442  ILE 442  443  443 ILE ILE A . n 
A 1 443  ASN 443  444  444 ASN ASN A . n 
A 1 444  ALA 444  445  445 ALA ALA A . n 
A 1 445  THR 445  446  446 THR THR A . n 
A 1 446  LEU 446  447  447 LEU LEU A . n 
A 1 447  GLU 447  448  448 GLU GLU A . n 
A 1 448  THR 448  449  449 THR THR A . n 
A 1 449  LYS 449  450  450 LYS LYS A . n 
A 1 450  GLN 450  451  451 GLN GLN A . n 
A 1 451  PRO 451  452  452 PRO PRO A . n 
A 1 452  ARG 452  453  453 ARG ARG A . n 
A 1 453  GLN 453  454  454 GLN GLN A . n 
A 1 454  TYR 454  455  455 TYR TYR A . n 
A 1 455  PHE 455  456  456 PHE PHE A . n 
A 1 456  ILE 456  457  457 ILE ILE A . n 
A 1 457  GLY 457  458  458 GLY GLY A . n 
A 1 458  VAL 458  459  459 VAL VAL A . n 
A 1 459  LEU 459  460  460 LEU LEU A . n 
A 1 460  ASP 460  461  461 ASP ASP A . n 
A 1 461  ILE 461  462  462 ILE ILE A . n 
A 1 462  ALA 462  463  463 ALA ALA A . n 
A 1 463  GLY 463  464  464 GLY GLY A . n 
A 1 464  PHE 464  465  465 PHE PHE A . n 
A 1 465  GLU 465  466  466 GLU GLU A . n 
A 1 466  ILE 466  467  467 ILE ILE A . n 
A 1 467  PHE 467  468  468 PHE PHE A . n 
A 1 468  ASP 468  469  469 ASP ASP A . n 
A 1 469  PHE 469  470  470 PHE PHE A . n 
A 1 470  ASN 470  471  471 ASN ASN A . n 
A 1 471  SER 471  472  472 SER SER A . n 
A 1 472  PHE 472  473  473 PHE PHE A . n 
A 1 473  GLU 473  474  474 GLU GLU A . n 
A 1 474  GLN 474  475  475 GLN GLN A . n 
A 1 475  LEU 475  476  476 LEU LEU A . n 
A 1 476  CYS 476  477  477 CYS CYS A . n 
A 1 477  ILE 477  478  478 ILE ILE A . n 
A 1 478  ASN 478  479  479 ASN ASN A . n 
A 1 479  PHE 479  480  480 PHE PHE A . n 
A 1 480  THR 480  481  481 THR THR A . n 
A 1 481  ASN 481  482  482 ASN ASN A . n 
A 1 482  GLU 482  483  483 GLU GLU A . n 
A 1 483  LYS 483  484  484 LYS LYS A . n 
A 1 484  LEU 484  485  485 LEU LEU A . n 
A 1 485  GLN 485  486  486 GLN GLN A . n 
A 1 486  GLN 486  487  487 GLN GLN A . n 
A 1 487  PHE 487  488  488 PHE PHE A . n 
A 1 488  PHE 488  489  489 PHE PHE A . n 
A 1 489  ASN 489  490  490 ASN ASN A . n 
A 1 490  HIS 490  491  491 HIS HIS A . n 
A 1 491  HIS 491  492  492 HIS HIS A . n 
A 1 492  MET 492  493  493 MET MET A . n 
A 1 493  PHE 493  494  494 PHE PHE A . n 
A 1 494  VAL 494  495  495 VAL VAL A . n 
A 1 495  LEU 495  496  496 LEU LEU A . n 
A 1 496  GLU 496  497  497 GLU GLU A . n 
A 1 497  GLN 497  498  498 GLN GLN A . n 
A 1 498  GLU 498  499  499 GLU GLU A . n 
A 1 499  GLU 499  500  500 GLU GLU A . n 
A 1 500  TYR 500  501  501 TYR TYR A . n 
A 1 501  LYS 501  502  502 LYS LYS A . n 
A 1 502  LYS 502  503  503 LYS LYS A . n 
A 1 503  GLU 503  504  504 GLU GLU A . n 
A 1 504  GLY 504  505  505 GLY GLY A . n 
A 1 505  ILE 505  506  506 ILE ILE A . n 
A 1 506  GLU 506  507  507 GLU GLU A . n 
A 1 507  TRP 507  508  508 TRP TRP A . n 
A 1 508  THR 508  509  509 THR THR A . n 
A 1 509  PHE 509  510  510 PHE PHE A . n 
A 1 510  ILE 510  511  511 ILE ILE A . n 
A 1 511  ASP 511  512  512 ASP ASP A . n 
A 1 512  PHE 512  513  513 PHE PHE A . n 
A 1 513  GLY 513  514  514 GLY GLY A . n 
A 1 514  MET 514  515  515 MET MET A . n 
A 1 515  ASP 515  516  516 ASP ASP A . n 
A 1 516  LEU 516  517  517 LEU LEU A . n 
A 1 517  GLN 517  518  518 GLN GLN A . n 
A 1 518  ALA 518  519  519 ALA ALA A . n 
A 1 519  CYS 519  520  520 CYS CYS A . n 
A 1 520  ILE 520  521  521 ILE ILE A . n 
A 1 521  ASP 521  522  522 ASP ASP A . n 
A 1 522  LEU 522  523  523 LEU LEU A . n 
A 1 523  ILE 523  524  524 ILE ILE A . n 
A 1 524  GLU 524  525  525 GLU GLU A . n 
A 1 525  LYS 525  526  526 LYS LYS A . n 
A 1 526  PRO 526  527  527 PRO PRO A . n 
A 1 527  MET 527  528  528 MET MET A . n 
A 1 528  GLY 528  529  529 GLY GLY A . n 
A 1 529  ILE 529  530  530 ILE ILE A . n 
A 1 530  MET 530  531  531 MET MET A . n 
A 1 531  SER 531  532  532 SER SER A . n 
A 1 532  ILE 532  533  533 ILE ILE A . n 
A 1 533  LEU 533  534  534 LEU LEU A . n 
A 1 534  GLU 534  535  535 GLU GLU A . n 
A 1 535  GLU 535  536  536 GLU GLU A . n 
A 1 536  GLU 536  537  537 GLU GLU A . n 
A 1 537  CYS 537  538  538 CYS CYS A . n 
A 1 538  MET 538  539  539 MET MET A . n 
A 1 539  PHE 539  540  540 PHE PHE A . n 
A 1 540  PRO 540  541  541 PRO PRO A . n 
A 1 541  LYS 541  542  542 LYS LYS A . n 
A 1 542  ALA 542  543  543 ALA ALA A . n 
A 1 543  THR 543  544  544 THR THR A . n 
A 1 544  ASP 544  545  545 ASP ASP A . n 
A 1 545  MET 545  546  546 MET MET A . n 
A 1 546  THR 546  547  547 THR THR A . n 
A 1 547  PHE 547  548  548 PHE PHE A . n 
A 1 548  LYS 548  549  549 LYS LYS A . n 
A 1 549  ALA 549  550  550 ALA ALA A . n 
A 1 550  LYS 550  551  551 LYS LYS A . n 
A 1 551  LEU 551  552  552 LEU LEU A . n 
A 1 552  PHE 552  553  553 PHE PHE A . n 
A 1 553  ASP 553  554  554 ASP ASP A . n 
A 1 554  ASN 554  555  555 ASN ASN A . n 
A 1 555  HIS 555  556  556 HIS HIS A . n 
A 1 556  LEU 556  557  557 LEU LEU A . n 
A 1 557  GLY 557  558  558 GLY GLY A . n 
A 1 558  LYS 558  559  559 LYS LYS A . n 
A 1 559  SER 559  560  560 SER SER A . n 
A 1 560  ALA 560  561  561 ALA ALA A . n 
A 1 561  ASN 561  562  562 ASN ASN A . n 
A 1 562  PHE 562  563  563 PHE PHE A . n 
A 1 563  GLN 563  564  564 GLN GLN A . n 
A 1 564  LYS 564  565  565 LYS LYS A . n 
A 1 565  PRO 565  566  566 PRO PRO A . n 
A 1 566  ARG 566  567  567 ARG ARG A . n 
A 1 567  ASN 567  568  568 ASN ASN A . n 
A 1 568  ILE 568  569  569 ILE ILE A . n 
A 1 569  LYS 569  570  570 LYS LYS A . n 
A 1 570  GLY 570  571  571 GLY GLY A . n 
A 1 571  LYS 571  572  572 LYS LYS A . n 
A 1 572  PRO 572  573  573 PRO PRO A . n 
A 1 573  GLU 573  574  574 GLU GLU A . n 
A 1 574  ALA 574  575  575 ALA ALA A . n 
A 1 575  HIS 575  576  576 HIS HIS A . n 
A 1 576  PHE 576  577  577 PHE PHE A . n 
A 1 577  SER 577  578  578 SER SER A . n 
A 1 578  LEU 578  579  579 LEU LEU A . n 
A 1 579  ILE 579  580  580 ILE ILE A . n 
A 1 580  HIS 580  581  581 HIS HIS A . n 
A 1 581  TYR 581  582  582 TYR TYR A . n 
A 1 582  ALA 582  583  583 ALA ALA A . n 
A 1 583  GLY 583  584  584 GLY GLY A . n 
A 1 584  ILE 584  585  585 ILE ILE A . n 
A 1 585  VAL 585  586  586 VAL VAL A . n 
A 1 586  ASP 586  587  587 ASP ASP A . n 
A 1 587  TYR 587  588  588 TYR TYR A . n 
A 1 588  ASN 588  589  589 ASN ASN A . n 
A 1 589  ILE 589  590  590 ILE ILE A . n 
A 1 590  ILE 590  591  591 ILE ILE A . n 
A 1 591  GLY 591  592  592 GLY GLY A . n 
A 1 592  TRP 592  593  593 TRP TRP A . n 
A 1 593  LEU 593  594  594 LEU LEU A . n 
A 1 594  GLN 594  595  595 GLN GLN A . n 
A 1 595  LYS 595  596  596 LYS LYS A . n 
A 1 596  ASN 596  597  597 ASN ASN A . n 
A 1 597  LYS 597  598  598 LYS LYS A . n 
A 1 598  ASP 598  599  599 ASP ASP A . n 
A 1 599  PRO 599  600  600 PRO PRO A . n 
A 1 600  LEU 600  601  601 LEU LEU A . n 
A 1 601  ASN 601  602  602 ASN ASN A . n 
A 1 602  GLU 602  603  603 GLU GLU A . n 
A 1 603  THR 603  604  604 THR THR A . n 
A 1 604  VAL 604  605  605 VAL VAL A . n 
A 1 605  VAL 605  606  606 VAL VAL A . n 
A 1 606  GLY 606  607  607 GLY GLY A . n 
A 1 607  LEU 607  608  608 LEU LEU A . n 
A 1 608  TYR 608  609  609 TYR TYR A . n 
A 1 609  GLN 609  610  610 GLN GLN A . n 
A 1 610  LYS 610  611  611 LYS LYS A . n 
A 1 611  SER 611  612  612 SER SER A . n 
A 1 612  SER 612  613  613 SER SER A . n 
A 1 613  LEU 613  614  614 LEU LEU A . n 
A 1 614  LYS 614  615  615 LYS LYS A . n 
A 1 615  LEU 615  616  616 LEU LEU A . n 
A 1 616  LEU 616  617  617 LEU LEU A . n 
A 1 617  SER 617  618  618 SER SER A . n 
A 1 618  THR 618  619  619 THR THR A . n 
A 1 619  LEU 619  620  620 LEU LEU A . n 
A 1 620  PHE 620  621  621 PHE PHE A . n 
A 1 621  ALA 621  622  622 ALA ALA A . n 
A 1 622  ASN 622  623  623 ASN ASN A . n 
A 1 623  TYR 623  624  624 TYR TYR A . n 
A 1 624  ALA 624  625  ?   ?   ?   A . n 
A 1 625  GLY 625  626  ?   ?   ?   A . n 
A 1 626  ALA 626  627  ?   ?   ?   A . n 
A 1 627  ASP 627  628  ?   ?   ?   A . n 
A 1 628  ALA 628  629  ?   ?   ?   A . n 
A 1 629  PRO 629  630  ?   ?   ?   A . n 
A 1 630  ILE 630  631  ?   ?   ?   A . n 
A 1 631  GLU 631  632  ?   ?   ?   A . n 
A 1 632  LYS 632  633  ?   ?   ?   A . n 
A 1 633  GLY 633  634  ?   ?   ?   A . n 
A 1 634  LYS 634  635  ?   ?   ?   A . n 
A 1 635  GLY 635  636  ?   ?   ?   A . n 
A 1 636  LYS 636  637  ?   ?   ?   A . n 
A 1 637  ALA 637  638  ?   ?   ?   A . n 
A 1 638  LYS 638  639  ?   ?   ?   A . n 
A 1 639  LYS 639  640  ?   ?   ?   A . n 
A 1 640  GLY 640  641  ?   ?   ?   A . n 
A 1 641  SER 641  642  ?   ?   ?   A . n 
A 1 642  SER 642  643  ?   ?   ?   A . n 
A 1 643  PHE 643  644  644 PHE PHE A . n 
A 1 644  GLN 644  645  645 GLN GLN A . n 
A 1 645  THR 645  646  646 THR THR A . n 
A 1 646  VAL 646  647  647 VAL VAL A . n 
A 1 647  SER 647  648  648 SER SER A . n 
A 1 648  ALA 648  649  649 ALA ALA A . n 
A 1 649  LEU 649  650  650 LEU LEU A . n 
A 1 650  HIS 650  651  651 HIS HIS A . n 
A 1 651  ARG 651  652  652 ARG ARG A . n 
A 1 652  GLU 652  653  653 GLU GLU A . n 
A 1 653  ASN 653  654  654 ASN ASN A . n 
A 1 654  LEU 654  655  655 LEU LEU A . n 
A 1 655  ASN 655  656  656 ASN ASN A . n 
A 1 656  LYS 656  657  657 LYS LYS A . n 
A 1 657  LEU 657  658  658 LEU LEU A . n 
A 1 658  MET 658  659  659 MET MET A . n 
A 1 659  THR 659  660  660 THR THR A . n 
A 1 660  ASN 660  661  661 ASN ASN A . n 
A 1 661  LEU 661  662  662 LEU LEU A . n 
A 1 662  ARG 662  663  663 ARG ARG A . n 
A 1 663  SER 663  664  664 SER SER A . n 
A 1 664  THR 664  665  665 THR THR A . n 
A 1 665  HIS 665  666  666 HIS HIS A . n 
A 1 666  PRO 666  667  667 PRO PRO A . n 
A 1 667  HIS 667  668  668 HIS HIS A . n 
A 1 668  PHE 668  669  669 PHE PHE A . n 
A 1 669  VAL 669  670  670 VAL VAL A . n 
A 1 670  ARG 670  671  671 ARG ARG A . n 
A 1 671  CYS 671  672  672 CYS CYS A . n 
A 1 672  ILE 672  673  673 ILE ILE A . n 
A 1 673  ILE 673  674  674 ILE ILE A . n 
A 1 674  PRO 674  675  675 PRO PRO A . n 
A 1 675  ASN 675  676  676 ASN ASN A . n 
A 1 676  GLU 676  677  677 GLU GLU A . n 
A 1 677  THR 677  678  678 THR THR A . n 
A 1 678  LYS 678  679  679 LYS LYS A . n 
A 1 679  SER 679  680  680 SER SER A . n 
A 1 680  PRO 680  681  681 PRO PRO A . n 
A 1 681  GLY 681  682  682 GLY GLY A . n 
A 1 682  VAL 682  683  683 VAL VAL A . n 
A 1 683  MET 683  684  684 MET MET A . n 
A 1 684  ASP 684  685  685 ASP ASP A . n 
A 1 685  ASN 685  686  686 ASN ASN A . n 
A 1 686  PRO 686  687  687 PRO PRO A . n 
A 1 687  LEU 687  688  688 LEU LEU A . n 
A 1 688  VAL 688  689  689 VAL VAL A . n 
A 1 689  MET 689  690  690 MET MET A . n 
A 1 690  HIS 690  691  691 HIS HIS A . n 
A 1 691  GLN 691  692  692 GLN GLN A . n 
A 1 692  LEU 692  693  693 LEU LEU A . n 
A 1 693  ARG 693  694  694 ARG ARG A . n 
A 1 694  CYS 694  695  695 CYS CYS A . n 
A 1 695  ASN 695  696  696 ASN ASN A . n 
A 1 696  GLY 696  697  697 GLY GLY A . n 
A 1 697  VAL 697  698  698 VAL VAL A . n 
A 1 698  LEU 698  699  699 LEU LEU A . n 
A 1 699  GLU 699  700  700 GLU GLU A . n 
A 1 700  GLY 700  701  701 GLY GLY A . n 
A 1 701  ILE 701  702  702 ILE ILE A . n 
A 1 702  ARG 702  703  703 ARG ARG A . n 
A 1 703  ILE 703  704  704 ILE ILE A . n 
A 1 704  CYS 704  705  705 CYS CYS A . n 
A 1 705  ARG 705  706  706 ARG ARG A . n 
A 1 706  LYS 706  707  707 LYS LYS A . n 
A 1 707  GLY 707  708  708 GLY GLY A . n 
A 1 708  PHE 708  709  709 PHE PHE A . n 
A 1 709  PRO 709  710  710 PRO PRO A . n 
A 1 710  ASN 710  711  711 ASN ASN A . n 
A 1 711  ARG 711  712  712 ARG ARG A . n 
A 1 712  ILE 712  713  713 ILE ILE A . n 
A 1 713  LEU 713  714  714 LEU LEU A . n 
A 1 714  TYR 714  715  715 TYR TYR A . n 
A 1 715  GLY 715  716  716 GLY GLY A . n 
A 1 716  ASP 716  717  717 ASP ASP A . n 
A 1 717  PHE 717  718  718 PHE PHE A . n 
A 1 718  ARG 718  719  719 ARG ARG A . n 
A 1 719  GLN 719  720  720 GLN GLN A . n 
A 1 720  ARG 720  721  721 ARG ARG A . n 
A 1 721  TYR 721  722  722 TYR TYR A . n 
A 1 722  ARG 722  723  723 ARG ARG A . n 
A 1 723  ILE 723  724  724 ILE ILE A . n 
A 1 724  LEU 724  725  725 LEU LEU A . n 
A 1 725  ASN 725  726  726 ASN ASN A . n 
A 1 726  PRO 726  727  727 PRO PRO A . n 
A 1 727  ALA 727  728  728 ALA ALA A . n 
A 1 728  ALA 728  729  729 ALA ALA A . n 
A 1 729  ILE 729  730  730 ILE ILE A . n 
A 1 730  PRO 730  731  731 PRO PRO A . n 
A 1 731  GLU 731  732  732 GLU GLU A . n 
A 1 732  GLY 732  733  733 GLY GLY A . n 
A 1 733  GLN 733  734  734 GLN GLN A . n 
A 1 734  PHE 734  735  735 PHE PHE A . n 
A 1 735  ILE 735  736  736 ILE ILE A . n 
A 1 736  ASP 736  737  737 ASP ASP A . n 
A 1 737  SER 737  738  738 SER SER A . n 
A 1 738  ARG 738  739  739 ARG ARG A . n 
A 1 739  LYS 739  740  740 LYS LYS A . n 
A 1 740  GLY 740  741  741 GLY GLY A . n 
A 1 741  ALA 741  742  742 ALA ALA A . n 
A 1 742  GLU 742  743  743 GLU GLU A . n 
A 1 743  LYS 743  744  744 LYS LYS A . n 
A 1 744  LEU 744  745  745 LEU LEU A . n 
A 1 745  LEU 745  746  746 LEU LEU A . n 
A 1 746  SER 746  747  747 SER SER A . n 
A 1 747  SER 747  748  748 SER SER A . n 
A 1 748  LEU 748  749  749 LEU LEU A . n 
A 1 749  ASP 749  750  750 ASP ASP A . n 
A 1 750  ILE 750  751  751 ILE ILE A . n 
A 1 751  ASP 751  752  752 ASP ASP A . n 
A 1 752  HIS 752  753  753 HIS HIS A . n 
A 1 753  ASN 753  754  754 ASN ASN A . n 
A 1 754  GLN 754  755  755 GLN GLN A . n 
A 1 755  TYR 755  756  756 TYR TYR A . n 
A 1 756  LYS 756  757  757 LYS LYS A . n 
A 1 757  PHE 757  758  758 PHE PHE A . n 
A 1 758  GLY 758  759  759 GLY GLY A . n 
A 1 759  HIS 759  760  760 HIS HIS A . n 
A 1 760  THR 760  761  761 THR THR A . n 
A 1 761  LYS 761  762  762 LYS LYS A . n 
A 1 762  VAL 762  763  763 VAL VAL A . n 
A 1 763  PHE 763  764  764 PHE PHE A . n 
A 1 764  PHE 764  765  765 PHE PHE A . n 
A 1 765  LYS 765  766  766 LYS LYS A . n 
A 1 766  ALA 766  767  767 ALA ALA A . n 
A 1 767  GLY 767  768  768 GLY GLY A . n 
A 1 768  LEU 768  769  769 LEU LEU A . n 
A 1 769  LEU 769  770  770 LEU LEU A . n 
A 1 770  GLY 770  771  771 GLY GLY A . n 
A 1 771  LEU 771  772  772 LEU LEU A . n 
A 1 772  LEU 772  773  773 LEU LEU A . n 
A 1 773  GLU 773  774  774 GLU GLU A . n 
A 1 774  GLU 774  775  775 GLU GLU A . n 
A 1 775  MET 775  776  776 MET MET A . n 
A 1 776  ARG 776  777  777 ARG ARG A . n 
A 1 777  ASP 777  778  778 ASP ASP A . n 
A 1 778  GLU 778  779  779 GLU GLU A . n 
A 1 779  ARG 779  780  780 ARG ARG A . n 
A 1 780  LEU 780  781  781 LEU LEU A . n 
A 1 781  SER 781  782  782 SER SER A . n 
A 1 782  ARG 782  783  783 ARG ARG A . n 
A 1 783  ILE 783  784  784 ILE ILE A . n 
A 1 784  ILE 784  785  785 ILE ILE A . n 
A 1 785  THR 785  786  786 THR THR A . n 
A 1 786  ARG 786  787  787 ARG ARG A . n 
A 1 787  ILE 787  788  788 ILE ILE A . n 
A 1 788  GLN 788  789  789 GLN GLN A . n 
A 1 789  ALA 789  790  790 ALA ALA A . n 
A 1 790  GLN 790  791  791 GLN GLN A . n 
A 1 791  SER 791  792  792 SER SER A . n 
A 1 792  ARG 792  793  793 ARG ARG A . n 
A 1 793  GLY 793  794  794 GLY GLY A . n 
A 1 794  VAL 794  795  795 VAL VAL A . n 
A 1 795  LEU 795  796  796 LEU LEU A . n 
A 1 796  ALA 796  797  ?   ?   ?   A . n 
A 1 797  ARG 797  798  ?   ?   ?   A . n 
A 1 798  MET 798  799  ?   ?   ?   A . n 
A 1 799  GLU 799  800  ?   ?   ?   A . n 
A 1 800  TYR 800  801  ?   ?   ?   A . n 
A 1 801  LYS 801  802  ?   ?   ?   A . n 
A 1 802  LYS 802  803  ?   ?   ?   A . n 
A 1 803  LEU 803  804  ?   ?   ?   A . n 
A 1 804  LEU 804  805  ?   ?   ?   A . n 
A 1 805  GLU 805  806  ?   ?   ?   A . n 
A 1 806  ARG 806  807  ?   ?   ?   A . n 
A 1 807  ARG 807  808  ?   ?   ?   A . n 
A 1 808  ASP 808  809  ?   ?   ?   A . n 
A 1 809  SER 809  810  ?   ?   ?   A . n 
A 1 810  LEU 810  811  ?   ?   ?   A . n 
A 1 811  LEU 811  812  ?   ?   ?   A . n 
A 1 812  VAL 812  813  ?   ?   ?   A . n 
A 1 813  ILE 813  814  ?   ?   ?   A . n 
A 1 814  GLN 814  815  ?   ?   ?   A . n 
A 1 815  TRP 815  816  ?   ?   ?   A . n 
A 1 816  ASN 816  817  ?   ?   ?   A . n 
A 1 817  ILE 817  818  ?   ?   ?   A . n 
A 1 818  ARG 818  819  ?   ?   ?   A . n 
A 1 819  ALA 819  820  ?   ?   ?   A . n 
A 1 820  PHE 820  821  ?   ?   ?   A . n 
A 1 821  MET 821  822  ?   ?   ?   A . n 
A 1 822  GLY 822  823  ?   ?   ?   A . n 
A 1 823  VAL 823  824  ?   ?   ?   A . n 
A 1 824  LYS 824  825  ?   ?   ?   A . n 
A 1 825  ASN 825  826  ?   ?   ?   A . n 
A 1 826  TRP 826  827  ?   ?   ?   A . n 
A 1 827  PRO 827  828  ?   ?   ?   A . n 
A 1 828  TRP 828  829  ?   ?   ?   A . n 
A 1 829  MET 829  830  ?   ?   ?   A . n 
A 1 830  LYS 830  831  ?   ?   ?   A . n 
A 1 831  LEU 831  832  ?   ?   ?   A . n 
A 1 832  TYR 832  833  ?   ?   ?   A . n 
A 1 833  PHE 833  834  ?   ?   ?   A . n 
A 1 834  LYS 834  835  ?   ?   ?   A . n 
A 1 835  ILE 835  836  ?   ?   ?   A . n 
A 1 836  LYS 836  837  ?   ?   ?   A . n 
A 1 837  PRO 837  838  ?   ?   ?   A . n 
A 1 838  LEU 838  839  ?   ?   ?   A . n 
A 1 839  LEU 839  840  ?   ?   ?   A . n 
A 1 840  LYS 840  841  ?   ?   ?   A . n 
A 1 841  SER 841  842  ?   ?   ?   A . n 
A 1 842  ALA 842  843  ?   ?   ?   A . n 
A 1 843  GLU 843  844  ?   ?   ?   A . n 
A 1 844  ARG 844  845  ?   ?   ?   A . n 
A 1 845  GLU 845  846  ?   ?   ?   A . n 
A 1 846  LYS 846  847  ?   ?   ?   A . n 
A 1 847  GLU 847  848  ?   ?   ?   A . n 
A 1 848  MET 848  849  ?   ?   ?   A . n 
A 1 849  ALA 849  850  ?   ?   ?   A . n 
A 1 850  SER 850  851  ?   ?   ?   A . n 
A 1 851  MET 851  852  ?   ?   ?   A . n 
A 1 852  LYS 852  853  ?   ?   ?   A . n 
A 1 853  GLU 853  854  ?   ?   ?   A . n 
A 1 854  GLU 854  855  ?   ?   ?   A . n 
A 1 855  PHE 855  856  ?   ?   ?   A . n 
A 1 856  THR 856  857  ?   ?   ?   A . n 
A 1 857  ARG 857  858  ?   ?   ?   A . n 
A 1 858  LEU 858  859  ?   ?   ?   A . n 
A 1 859  LYS 859  860  ?   ?   ?   A . n 
A 1 860  GLU 860  861  ?   ?   ?   A . n 
A 1 861  ALA 861  862  ?   ?   ?   A . n 
A 1 862  LEU 862  863  ?   ?   ?   A . n 
A 1 863  GLU 863  864  ?   ?   ?   A . n 
A 1 864  LYS 864  865  ?   ?   ?   A . n 
A 1 865  SER 865  866  ?   ?   ?   A . n 
A 1 866  GLU 866  867  ?   ?   ?   A . n 
A 1 867  ALA 867  868  ?   ?   ?   A . n 
A 1 868  ARG 868  869  ?   ?   ?   A . n 
A 1 869  ARG 869  870  ?   ?   ?   A . n 
A 1 870  LYS 870  871  ?   ?   ?   A . n 
A 1 871  GLU 871  872  ?   ?   ?   A . n 
A 1 872  LEU 872  873  ?   ?   ?   A . n 
A 1 873  GLU 873  874  ?   ?   ?   A . n 
A 1 874  GLU 874  875  ?   ?   ?   A . n 
A 1 875  LYS 875  876  ?   ?   ?   A . n 
A 1 876  MET 876  877  ?   ?   ?   A . n 
A 1 877  VAL 877  878  ?   ?   ?   A . n 
A 1 878  SER 878  879  ?   ?   ?   A . n 
A 1 879  LEU 879  880  ?   ?   ?   A . n 
A 1 880  LEU 880  881  ?   ?   ?   A . n 
A 1 881  GLN 881  882  ?   ?   ?   A . n 
A 1 882  GLU 882  883  ?   ?   ?   A . n 
A 1 883  LYS 883  884  ?   ?   ?   A . n 
A 1 884  ASN 884  885  ?   ?   ?   A . n 
A 1 885  ASP 885  886  ?   ?   ?   A . n 
A 1 886  LEU 886  887  ?   ?   ?   A . n 
A 1 887  GLN 887  888  ?   ?   ?   A . n 
A 1 888  LEU 888  889  ?   ?   ?   A . n 
A 1 889  GLN 889  890  ?   ?   ?   A . n 
A 1 890  VAL 890  891  ?   ?   ?   A . n 
A 1 891  GLN 891  892  ?   ?   ?   A . n 
A 1 892  ALA 892  893  ?   ?   ?   A . n 
A 1 893  GLU 893  894  ?   ?   ?   A . n 
A 1 894  GLN 894  895  ?   ?   ?   A . n 
A 1 895  ASP 895  896  ?   ?   ?   A . n 
A 1 896  ASN 896  897  ?   ?   ?   A . n 
A 1 897  LEU 897  898  ?   ?   ?   A . n 
A 1 898  ALA 898  899  ?   ?   ?   A . n 
A 1 899  ASP 899  900  ?   ?   ?   A . n 
A 1 900  ALA 900  901  ?   ?   ?   A . n 
A 1 901  GLU 901  902  ?   ?   ?   A . n 
A 1 902  GLU 902  903  ?   ?   ?   A . n 
A 1 903  ARG 903  904  ?   ?   ?   A . n 
A 1 904  CYS 904  905  ?   ?   ?   A . n 
A 1 905  ASP 905  906  ?   ?   ?   A . n 
A 1 906  GLN 906  907  ?   ?   ?   A . n 
A 1 907  LEU 907  908  ?   ?   ?   A . n 
A 1 908  ILE 908  909  ?   ?   ?   A . n 
A 1 909  LYS 909  910  ?   ?   ?   A . n 
A 1 910  ASN 910  911  ?   ?   ?   A . n 
A 1 911  LYS 911  912  ?   ?   ?   A . n 
A 1 912  ILE 912  913  ?   ?   ?   A . n 
A 1 913  GLN 913  914  ?   ?   ?   A . n 
A 1 914  LEU 914  915  ?   ?   ?   A . n 
A 1 915  GLU 915  916  ?   ?   ?   A . n 
A 1 916  ALA 916  917  ?   ?   ?   A . n 
A 1 917  LYS 917  918  ?   ?   ?   A . n 
A 1 918  VAL 918  919  ?   ?   ?   A . n 
A 1 919  LYS 919  920  ?   ?   ?   A . n 
A 1 920  GLU 920  921  ?   ?   ?   A . n 
A 1 921  MET 921  922  ?   ?   ?   A . n 
A 1 922  ASN 922  923  ?   ?   ?   A . n 
A 1 923  GLU 923  924  ?   ?   ?   A . n 
A 1 924  ARG 924  925  ?   ?   ?   A . n 
A 1 925  LEU 925  926  ?   ?   ?   A . n 
A 1 926  GLU 926  927  ?   ?   ?   A . n 
A 1 927  ASP 927  928  ?   ?   ?   A . n 
A 1 928  GLU 928  929  ?   ?   ?   A . n 
A 1 929  GLU 929  930  ?   ?   ?   A . n 
A 1 930  GLU 930  931  ?   ?   ?   A . n 
A 1 931  MET 931  932  ?   ?   ?   A . n 
A 1 932  ASN 932  933  ?   ?   ?   A . n 
A 1 933  ALA 933  934  ?   ?   ?   A . n 
A 1 934  GLU 934  935  ?   ?   ?   A . n 
A 1 935  LEU 935  936  ?   ?   ?   A . n 
A 1 936  THR 936  937  ?   ?   ?   A . n 
A 1 937  ALA 937  938  ?   ?   ?   A . n 
A 1 938  LYS 938  939  ?   ?   ?   A . n 
A 1 939  LYS 939  940  ?   ?   ?   A . n 
A 1 940  ARG 940  941  ?   ?   ?   A . n 
A 1 941  LYS 941  942  ?   ?   ?   A . n 
A 1 942  LEU 942  943  ?   ?   ?   A . n 
A 1 943  GLU 943  944  ?   ?   ?   A . n 
A 1 944  ASP 944  945  ?   ?   ?   A . n 
A 1 945  GLU 945  946  ?   ?   ?   A . n 
A 1 946  CYS 946  947  ?   ?   ?   A . n 
A 1 947  SER 947  948  ?   ?   ?   A . n 
A 1 948  GLU 948  949  ?   ?   ?   A . n 
A 1 949  LEU 949  950  ?   ?   ?   A . n 
A 1 950  LYS 950  951  ?   ?   ?   A . n 
A 1 951  ARG 951  952  ?   ?   ?   A . n 
A 1 952  ASP 952  953  ?   ?   ?   A . n 
A 1 953  ILE 953  954  ?   ?   ?   A . n 
A 1 954  ASP 954  955  ?   ?   ?   A . n 
A 1 955  ASP 955  956  ?   ?   ?   A . n 
A 1 956  LEU 956  957  ?   ?   ?   A . n 
A 1 957  GLU 957  958  ?   ?   ?   A . n 
A 1 958  LEU 958  959  ?   ?   ?   A . n 
A 1 959  THR 959  960  ?   ?   ?   A . n 
A 1 960  LEU 960  961  ?   ?   ?   A . n 
A 1 961  ALA 961  962  ?   ?   ?   A . n 
A 1 962  LYS 962  963  ?   ?   ?   A . n 
A 1 963  VAL 963  964  ?   ?   ?   A . n 
A 1 964  GLU 964  965  ?   ?   ?   A . n 
A 1 965  LYS 965  966  ?   ?   ?   A . n 
A 1 966  GLU 966  967  ?   ?   ?   A . n 
A 1 967  LYS 967  968  ?   ?   ?   A . n 
A 1 968  HIS 968  969  ?   ?   ?   A . n 
A 1 969  ALA 969  970  ?   ?   ?   A . n 
A 1 970  THR 970  971  ?   ?   ?   A . n 
A 1 971  GLU 971  972  ?   ?   ?   A . n 
A 1 972  ASN 972  973  ?   ?   ?   A . n 
A 1 973  LYS 973  974  ?   ?   ?   A . n 
A 1 974  VAL 974  975  ?   ?   ?   A . n 
A 1 975  LYS 975  976  ?   ?   ?   A . n 
A 1 976  ASN 976  977  ?   ?   ?   A . n 
A 1 977  LEU 977  978  ?   ?   ?   A . n 
A 1 978  THR 978  979  ?   ?   ?   A . n 
A 1 979  GLU 979  980  ?   ?   ?   A . n 
A 1 980  GLU 980  981  ?   ?   ?   A . n 
A 1 981  MET 981  982  ?   ?   ?   A . n 
A 1 982  ALA 982  983  ?   ?   ?   A . n 
A 1 983  GLY 983  984  ?   ?   ?   A . n 
A 1 984  LEU 984  985  ?   ?   ?   A . n 
A 1 985  ASP 985  986  ?   ?   ?   A . n 
A 1 986  GLU 986  987  ?   ?   ?   A . n 
A 1 987  ILE 987  988  ?   ?   ?   A . n 
A 1 988  ILE 988  989  ?   ?   ?   A . n 
A 1 989  ALA 989  990  ?   ?   ?   A . n 
A 1 990  LYS 990  991  ?   ?   ?   A . n 
A 1 991  LEU 991  992  ?   ?   ?   A . n 
A 1 992  THR 992  993  ?   ?   ?   A . n 
A 1 993  LYS 993  994  ?   ?   ?   A . n 
A 1 994  GLU 994  995  ?   ?   ?   A . n 
A 1 995  LYS 995  996  ?   ?   ?   A . n 
A 1 996  LYS 996  997  ?   ?   ?   A . n 
A 1 997  ALA 997  998  ?   ?   ?   A . n 
A 1 998  LEU 998  999  ?   ?   ?   A . n 
A 1 999  GLN 999  1000 ?   ?   ?   A . n 
A 1 1000 GLU 1000 1001 ?   ?   ?   A . n 
A 1 1001 ALA 1001 1002 ?   ?   ?   A . n 
A 1 1002 HIS 1002 1003 ?   ?   ?   A . n 
A 1 1003 GLN 1003 1004 ?   ?   ?   A . n 
A 1 1004 GLN 1004 1005 ?   ?   ?   A . n 
A 1 1005 ALA 1005 1006 ?   ?   ?   A . n 
A 1 1006 LEU 1006 1007 ?   ?   ?   A . n 
A 1 1007 ASP 1007 1008 ?   ?   ?   A . n 
A 1 1008 ASP 1008 1009 ?   ?   ?   A . n 
A 1 1009 LEU 1009 1010 ?   ?   ?   A . n 
A 1 1010 GLN 1010 1011 ?   ?   ?   A . n 
A 1 1011 ALA 1011 1012 ?   ?   ?   A . n 
A 1 1012 GLU 1012 1013 ?   ?   ?   A . n 
A 1 1013 GLU 1013 1014 ?   ?   ?   A . n 
A 1 1014 ASP 1014 1015 ?   ?   ?   A . n 
A 1 1015 LYS 1015 1016 ?   ?   ?   A . n 
A 1 1016 VAL 1016 1017 ?   ?   ?   A . n 
A 1 1017 ASN 1017 1018 ?   ?   ?   A . n 
A 1 1018 THR 1018 1019 ?   ?   ?   A . n 
A 1 1019 LEU 1019 1020 ?   ?   ?   A . n 
A 1 1020 THR 1020 1021 ?   ?   ?   A . n 
A 1 1021 LYS 1021 1022 ?   ?   ?   A . n 
A 1 1022 ALA 1022 1023 ?   ?   ?   A . n 
A 1 1023 LYS 1023 1024 ?   ?   ?   A . n 
A 1 1024 VAL 1024 1025 ?   ?   ?   A . n 
A 1 1025 LYS 1025 1026 ?   ?   ?   A . n 
A 1 1026 LEU 1026 1027 ?   ?   ?   A . n 
A 1 1027 GLU 1027 1028 ?   ?   ?   A . n 
A 1 1028 GLN 1028 1029 ?   ?   ?   A . n 
A 1 1029 GLN 1029 1030 ?   ?   ?   A . n 
A 1 1030 VAL 1030 1031 ?   ?   ?   A . n 
A 1 1031 ASP 1031 1032 ?   ?   ?   A . n 
A 1 1032 ASP 1032 1033 ?   ?   ?   A . n 
A 1 1033 LEU 1033 1034 ?   ?   ?   A . n 
A 1 1034 GLU 1034 1035 ?   ?   ?   A . n 
A 1 1035 GLY 1035 1036 ?   ?   ?   A . n 
A 1 1036 SER 1036 1037 ?   ?   ?   A . n 
A 1 1037 LEU 1037 1038 ?   ?   ?   A . n 
A 1 1038 GLU 1038 1039 ?   ?   ?   A . n 
A 1 1039 GLN 1039 1040 ?   ?   ?   A . n 
A 1 1040 GLU 1040 1041 ?   ?   ?   A . n 
A 1 1041 LYS 1041 1042 ?   ?   ?   A . n 
A 1 1042 LYS 1042 1043 ?   ?   ?   A . n 
A 1 1043 VAL 1043 1044 ?   ?   ?   A . n 
A 1 1044 ARG 1044 1045 ?   ?   ?   A . n 
A 1 1045 MET 1045 1046 ?   ?   ?   A . n 
A 1 1046 ASP 1046 1047 ?   ?   ?   A . n 
A 1 1047 LEU 1047 1048 ?   ?   ?   A . n 
A 1 1048 GLU 1048 1049 ?   ?   ?   A . n 
A 1 1049 ARG 1049 1050 ?   ?   ?   A . n 
A 1 1050 ALA 1050 1051 ?   ?   ?   A . n 
A 1 1051 LYS 1051 1052 ?   ?   ?   A . n 
A 1 1052 ARG 1052 1053 ?   ?   ?   A . n 
A 1 1053 LYS 1053 1054 ?   ?   ?   A . n 
A 1 1054 LEU 1054 1055 ?   ?   ?   A . n 
A 1 1055 GLU 1055 1056 ?   ?   ?   A . n 
A 1 1056 GLY 1056 1057 ?   ?   ?   A . n 
A 1 1057 ASP 1057 1058 ?   ?   ?   A . n 
A 1 1058 LEU 1058 1059 ?   ?   ?   A . n 
A 1 1059 LYS 1059 1060 ?   ?   ?   A . n 
A 1 1060 LEU 1060 1061 ?   ?   ?   A . n 
A 1 1061 THR 1061 1062 ?   ?   ?   A . n 
A 1 1062 GLN 1062 1063 ?   ?   ?   A . n 
A 1 1063 GLU 1063 1064 ?   ?   ?   A . n 
A 1 1064 SER 1064 1065 ?   ?   ?   A . n 
A 1 1065 ILE 1065 1066 ?   ?   ?   A . n 
A 1 1066 MET 1066 1067 ?   ?   ?   A . n 
A 1 1067 ASP 1067 1068 ?   ?   ?   A . n 
A 1 1068 LEU 1068 1069 ?   ?   ?   A . n 
A 1 1069 GLU 1069 1070 ?   ?   ?   A . n 
A 1 1070 ASN 1070 1071 ?   ?   ?   A . n 
A 1 1071 ASP 1071 1072 ?   ?   ?   A . n 
A 1 1072 LYS 1072 1073 ?   ?   ?   A . n 
A 1 1073 GLN 1073 1074 ?   ?   ?   A . n 
A 1 1074 GLN 1074 1075 ?   ?   ?   A . n 
A 1 1075 LEU 1075 1076 ?   ?   ?   A . n 
A 1 1076 ASP 1076 1077 ?   ?   ?   A . n 
A 1 1077 GLU 1077 1078 ?   ?   ?   A . n 
A 1 1078 ARG 1078 1079 ?   ?   ?   A . n 
A 1 1079 LEU 1079 1080 ?   ?   ?   A . n 
A 1 1080 LYS 1080 1081 ?   ?   ?   A . n 
A 1 1081 LYS 1081 1082 ?   ?   ?   A . n 
A 1 1082 LYS 1082 1083 ?   ?   ?   A . n 
A 1 1083 ASP 1083 1084 ?   ?   ?   A . n 
A 1 1084 PHE 1084 1085 ?   ?   ?   A . n 
A 1 1085 GLU 1085 1086 ?   ?   ?   A . n 
A 1 1086 LEU 1086 1087 ?   ?   ?   A . n 
A 1 1087 ASN 1087 1088 ?   ?   ?   A . n 
A 1 1088 ALA 1088 1089 ?   ?   ?   A . n 
A 1 1089 LEU 1089 1090 ?   ?   ?   A . n 
A 1 1090 ASN 1090 1091 ?   ?   ?   A . n 
A 1 1091 ALA 1091 1092 ?   ?   ?   A . n 
A 1 1092 ARG 1092 1093 ?   ?   ?   A . n 
A 1 1093 ILE 1093 1094 ?   ?   ?   A . n 
A 1 1094 GLU 1094 1095 ?   ?   ?   A . n 
A 1 1095 ASP 1095 1096 ?   ?   ?   A . n 
A 1 1096 GLU 1096 1097 ?   ?   ?   A . n 
A 1 1097 GLN 1097 1098 ?   ?   ?   A . n 
A 1 1098 ALA 1098 1099 ?   ?   ?   A . n 
A 1 1099 LEU 1099 1100 ?   ?   ?   A . n 
A 1 1100 GLY 1100 1101 ?   ?   ?   A . n 
A 1 1101 SER 1101 1102 ?   ?   ?   A . n 
A 1 1102 GLN 1102 1103 ?   ?   ?   A . n 
A 1 1103 LEU 1103 1104 ?   ?   ?   A . n 
A 1 1104 GLN 1104 1105 ?   ?   ?   A . n 
A 1 1105 LYS 1105 1106 ?   ?   ?   A . n 
A 1 1106 LYS 1106 1107 ?   ?   ?   A . n 
A 1 1107 LEU 1107 1108 ?   ?   ?   A . n 
A 1 1108 LYS 1108 1109 ?   ?   ?   A . n 
A 1 1109 GLU 1109 1110 ?   ?   ?   A . n 
A 1 1110 LEU 1110 1111 ?   ?   ?   A . n 
A 1 1111 GLN 1111 1112 ?   ?   ?   A . n 
A 1 1112 ALA 1112 1113 ?   ?   ?   A . n 
A 1 1113 ARG 1113 1114 ?   ?   ?   A . n 
A 1 1114 ILE 1114 1115 ?   ?   ?   A . n 
A 1 1115 GLU 1115 1116 ?   ?   ?   A . n 
A 1 1116 GLU 1116 1117 ?   ?   ?   A . n 
A 1 1117 LEU 1117 1118 ?   ?   ?   A . n 
A 1 1118 GLU 1118 1119 ?   ?   ?   A . n 
A 1 1119 GLU 1119 1120 ?   ?   ?   A . n 
A 1 1120 GLU 1120 1121 ?   ?   ?   A . n 
A 1 1121 LEU 1121 1122 ?   ?   ?   A . n 
A 1 1122 GLU 1122 1123 ?   ?   ?   A . n 
A 1 1123 SER 1123 1124 ?   ?   ?   A . n 
A 1 1124 GLU 1124 1125 ?   ?   ?   A . n 
A 1 1125 ARG 1125 1126 ?   ?   ?   A . n 
A 1 1126 THR 1126 1127 ?   ?   ?   A . n 
A 1 1127 ALA 1127 1128 ?   ?   ?   A . n 
A 1 1128 ARG 1128 1129 ?   ?   ?   A . n 
A 1 1129 ALA 1129 1130 ?   ?   ?   A . n 
A 1 1130 LYS 1130 1131 ?   ?   ?   A . n 
A 1 1131 VAL 1131 1132 ?   ?   ?   A . n 
A 1 1132 GLU 1132 1133 ?   ?   ?   A . n 
A 1 1133 LYS 1133 1134 ?   ?   ?   A . n 
A 1 1134 LEU 1134 1135 ?   ?   ?   A . n 
A 1 1135 ARG 1135 1136 ?   ?   ?   A . n 
A 1 1136 SER 1136 1137 ?   ?   ?   A . n 
A 1 1137 ASP 1137 1138 ?   ?   ?   A . n 
A 1 1138 ASP 1138 1139 ?   ?   ?   A . n 
A 1 1139 TYR 1139 1140 ?   ?   ?   A . n 
A 1 1140 LYS 1140 1141 ?   ?   ?   A . n 
A 1 1141 ASP 1141 1142 ?   ?   ?   A . n 
A 1 1142 ASP 1142 1143 ?   ?   ?   A . n 
A 1 1143 ASP 1143 1144 ?   ?   ?   A . n 
A 1 1144 ASP 1144 1145 ?   ?   ?   A . n 
A 1 1145 LYS 1145 1146 ?   ?   ?   A . n 
# 
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 MG  1 1201 797 MG  MG  A . 
C 3 ADP 1 1202 798 ADP ADP A . 
D 4 PO4 1 1203 799 PO4 PO4 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                     9GZ3 
_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                         9GZ3 
_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                   9GZ3 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_struct.entry_id                     9GZ3 
_struct.title                        'Beta-cardiac heavy meromyosin motor domain in the primed state' 
_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        9GZ3 
_struct_keywords.text            'Mavacamten, Inhibitor, Primed myosin, MOTOR PROTEIN' 
_struct_keywords.pdbx_keywords   'MOTOR 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 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    MYH7_HUMAN 
_struct_ref.pdbx_db_accession          P12883 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;GDSEMAVFGAAAPYLRKSEKERLEAQTRPFDLKKDVFVPDDKQEFVKAKIVSREGGKVTAETEYGKTVTVKEDQVMQQNP
PKFDKIEDMAMLTFLHEPAVLYNLKDRYGSWMIYTYSGLFCVTVNPYKWLPVYTPEVVAAYRGKKRSEAPPHIFSISDNA
YQYMLTDRENQSILITGESGAGKTVNTKRVIQYFAVIAAIGDRSKKDQSPGKGTLEDQIIQANPALEAFGNAKTVRNDNS
SRFGKFIRIHFGATGKLASADIETYLLEKSRVIFQLKAERDYHIFYQILSNKKPELLDMLLITNNPYDYAFISQGETTVA
SIDDAEELMATDNAFDVLGFTSEEKNSMYKLTGAIMHFGNMKFKLKQREEQAEPDGTEEADKSAYLMGLNSADLLKGLCH
PRVKVGNEYVTKGQNVQQVIYATGALAKAVYERMFNWMVTRINATLETKQPRQYFIGVLDIAGFEIFDFNSFEQLCINFT
NEKLQQFFNHHMFVLEQEEYKKEGIEWTFIDFGMDLQACIDLIEKPMGIMSILEEECMFPKATDMTFKAKLFDNHLGKSA
NFQKPRNIKGKPEAHFSLIHYAGIVDYNIIGWLQKNKDPLNETVVGLYQKSSLKLLSTLFANYAGADAPIEKGKGKAKKG
SSFQTVSALHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQR
YRILNPAAIPEGQFIDSRKGAEKLLSSLDIDHNQYKFGHTKVFFKAGLLGLLEEMRDERLSRIITRIQAQSRGVLARMEY
KKLLERRDSLLVIQWNIRAFMGVKNWPWMKLYFKIKPLLKSAEREKEMASMKEEFTRLKEALEKSEARRKELEEKMVSLL
QEKNDLQLQVQAEQDNLADAEERCDQLIKNKIQLEAKVKEMNERLEDEEEMNAELTAKKRKLEDECSELKRDIDDLELTL
AKVEKEKHATENKVKNLTEEMAGLDEIIAKLTKEKKALQEAHQQALDDLQAEEDKVNTLTKAKVKLEQQVDDLEGSLEQE
KKVRMDLERAKRKLEGDLKLTQESIMDLENDKQQLDERLKKKDFELNALNARIEDEQALGSQLQKKLKELQARIEELEEE
LEAERTARAKVEKLRSD
;
_struct_ref.pdbx_align_begin           2 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9GZ3 
_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                 1137 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P12883 
_struct_ref_seq.db_align_beg                  2 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1138 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       2 
_struct_ref_seq.pdbx_auth_seq_align_end       1138 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9GZ3 SER A 1123 ? UNP P12883 ALA 1124 variant          1124 1 
1 9GZ3 ASP A 1138 ? UNP P12883 ?   ?    'expression tag' 1139 2 
1 9GZ3 TYR A 1139 ? UNP P12883 ?   ?    'expression tag' 1140 3 
1 9GZ3 LYS A 1140 ? UNP P12883 ?   ?    'expression tag' 1141 4 
1 9GZ3 ASP A 1141 ? UNP P12883 ?   ?    'expression tag' 1142 5 
1 9GZ3 ASP A 1142 ? UNP P12883 ?   ?    'expression tag' 1143 6 
1 9GZ3 ASP A 1143 ? UNP P12883 ?   ?    'expression tag' 1144 7 
1 9GZ3 ASP A 1144 ? UNP P12883 ?   ?    'expression tag' 1145 8 
1 9GZ3 LYS A 1145 ? UNP P12883 ?   ?    'expression tag' 1146 9 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_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 
# 
_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   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 SER A 3   ? LEU A 15  ? SER A 4   LEU A 16  5 ? 13 
HELX_P HELX_P2  AA2 LYS A 20  ? ALA A 25  ? LYS A 21  ALA A 26  1 ? 6  
HELX_P HELX_P3  AA3 GLN A 26  ? ARG A 28  ? GLN A 27  ARG A 29  5 ? 3  
HELX_P HELX_P4  AA4 PRO A 80  ? ASP A 84  ? PRO A 81  ASP A 85  5 ? 5  
HELX_P HELX_P5  AA5 ASP A 88  ? LEU A 92  ? ASP A 89  LEU A 93  5 ? 5  
HELX_P HELX_P6  AA6 HIS A 96  ? GLY A 109 ? HIS A 97  GLY A 110 1 ? 14 
HELX_P HELX_P7  AA7 LEU A 130 ? TYR A 133 ? LEU A 131 TYR A 134 5 ? 4  
HELX_P HELX_P8  AA8 THR A 134 ? ARG A 142 ? THR A 135 ARG A 143 1 ? 9  
HELX_P HELX_P9  AA9 HIS A 152 ? ARG A 168 ? HIS A 153 ARG A 169 1 ? 17 
HELX_P HELX_P10 AB1 GLY A 182 ? GLY A 201 ? GLY A 183 GLY A 202 1 ? 20 
HELX_P HELX_P11 AB2 THR A 214 ? ASN A 231 ? THR A 215 ASN A 232 1 ? 18 
HELX_P HELX_P12 AB3 LYS A 269 ? ILE A 273 ? LYS A 270 ILE A 274 5 ? 5  
HELX_P HELX_P13 AB4 TYR A 282 ? ASN A 291 ? TYR A 283 ASN A 292 1 ? 10 
HELX_P HELX_P14 AB5 LYS A 293 ? ASP A 298 ? LYS A 294 ASP A 299 1 ? 6  
HELX_P HELX_P15 AB6 ASN A 305 ? TYR A 309 ? ASN A 306 TYR A 310 5 ? 5  
HELX_P HELX_P16 AB7 ASP A 323 ? LEU A 338 ? ASP A 324 LEU A 339 1 ? 16 
HELX_P HELX_P17 AB8 THR A 341 ? GLY A 359 ? THR A 342 GLY A 360 1 ? 19 
HELX_P HELX_P18 AB9 THR A 377 ? MET A 387 ? THR A 378 MET A 388 1 ? 11 
HELX_P HELX_P19 AC1 ASN A 390 ? HIS A 400 ? ASN A 391 HIS A 401 1 ? 11 
HELX_P HELX_P20 AC2 ASN A 415 ? GLU A 447 ? ASN A 416 GLU A 448 1 ? 33 
HELX_P HELX_P21 AC3 SER A 471 ? VAL A 494 ? SER A 472 VAL A 495 1 ? 24 
HELX_P HELX_P22 AC4 VAL A 494 ? GLU A 503 ? VAL A 495 GLU A 504 1 ? 10 
HELX_P HELX_P23 AC5 LEU A 516 ? GLU A 524 ? LEU A 517 GLU A 525 1 ? 9  
HELX_P HELX_P24 AC6 GLY A 528 ? GLU A 536 ? GLY A 529 GLU A 537 1 ? 9  
HELX_P HELX_P25 AC7 THR A 543 ? LEU A 556 ? THR A 544 LEU A 557 1 ? 14 
HELX_P HELX_P26 AC8 GLY A 591 ? ASN A 596 ? GLY A 592 ASN A 597 1 ? 6  
HELX_P HELX_P27 AC9 ASN A 601 ? GLN A 609 ? ASN A 602 GLN A 610 1 ? 9  
HELX_P HELX_P28 AD1 LEU A 613 ? PHE A 620 ? LEU A 614 PHE A 621 1 ? 8  
HELX_P HELX_P29 AD2 THR A 645 ? LEU A 661 ? THR A 646 LEU A 662 1 ? 17 
HELX_P HELX_P30 AD3 ARG A 662 ? THR A 664 ? ARG A 663 THR A 665 5 ? 3  
HELX_P HELX_P31 AD4 ASP A 684 ? ASN A 695 ? ASP A 685 ASN A 696 1 ? 12 
HELX_P HELX_P32 AD5 GLY A 696 ? GLY A 707 ? GLY A 697 GLY A 708 1 ? 12 
HELX_P HELX_P33 AD6 TYR A 714 ? ARG A 722 ? TYR A 715 ARG A 723 1 ? 9  
HELX_P HELX_P34 AD7 ASP A 736 ? SER A 747 ? ASP A 737 SER A 748 1 ? 12 
HELX_P HELX_P35 AD8 GLY A 767 ? LEU A 795 ? GLY A 768 LEU A 796 1 ? 29 
# 
_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 THR 184 OG1 ? ? ? 1_555 B MG  . MG  ? ? A THR 185  A MG  1201 1_555 ? ? ? ? ? ? ? 2.147 ? ? 
metalc2 metalc ? ? A SER 241 OG  ? ? ? 1_555 B MG  . MG  ? ? A SER 242  A MG  1201 1_555 ? ? ? ? ? ? ? 2.088 ? ? 
metalc3 metalc ? ? B MG  .   MG  ? ? ? 1_555 C ADP . O1B ? ? A MG  1201 A ADP 1202 1_555 ? ? ? ? ? ? ? 2.093 ? ? 
metalc4 metalc ? ? B MG  .   MG  ? ? ? 1_555 D PO4 . O2  ? ? A MG  1201 A PO4 1203 1_555 ? ? ? ? ? ? ? 2.556 ? ? 
# 
_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 OG1 ? A THR 184 ? A THR 185  ? 1_555 MG ? B MG . ? A MG 1201 ? 1_555 OG  ? A SER 241 ? A SER 242  ? 1_555 96.2  ? 
2 OG1 ? A THR 184 ? A THR 185  ? 1_555 MG ? B MG . ? A MG 1201 ? 1_555 O1B ? C ADP .   ? A ADP 1202 ? 1_555 65.4  ? 
3 OG  ? A SER 241 ? A SER 242  ? 1_555 MG ? B MG . ? A MG 1201 ? 1_555 O1B ? C ADP .   ? A ADP 1202 ? 1_555 113.0 ? 
4 OG1 ? A THR 184 ? A THR 185  ? 1_555 MG ? B MG . ? A MG 1201 ? 1_555 O2  ? D PO4 .   ? A PO4 1203 ? 1_555 131.2 ? 
5 OG  ? A SER 241 ? A SER 242  ? 1_555 MG ? B MG . ? A MG 1201 ? 1_555 O2  ? D PO4 .   ? A PO4 1203 ? 1_555 62.1  ? 
6 O1B ? C ADP .   ? A ADP 1202 ? 1_555 MG ? B MG . ? A MG 1201 ? 1_555 O2  ? D PO4 .   ? A PO4 1203 ? 1_555 83.0  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 7 ? 
AA3 ? 2 ? 
AA4 ? 2 ? 
AA5 ? 3 ? 
AA6 ? 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 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-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 THR A 67  ? LYS A 71  ? THR A 68  LYS A 72  
AA1 2 LYS A 57  ? THR A 62  ? LYS A 58  THR A 63  
AA1 3 PHE A 45  ? GLU A 54  ? PHE A 46  GLU A 55  
AA1 4 ASP A 35  ? PRO A 39  ? ASP A 36  PRO A 40  
AA1 5 MET A 76  ? GLN A 77  ? MET A 77  GLN A 78  
AA2 1 TYR A 114 ? TYR A 116 ? TYR A 115 TYR A 117 
AA2 2 CYS A 121 ? VAL A 124 ? CYS A 122 VAL A 125 
AA2 3 HIS A 665 ? ILE A 672 ? HIS A 666 ILE A 673 
AA2 4 GLN A 171 ? THR A 176 ? GLN A 172 THR A 177 
AA2 5 TYR A 454 ? ASP A 460 ? TYR A 455 ASP A 461 
AA2 6 PHE A 243 ? PHE A 251 ? PHE A 244 PHE A 252 
AA2 7 LEU A 257 ? LEU A 267 ? LEU A 258 LEU A 268 
AA3 1 PHE A 363 ? LEU A 365 ? PHE A 364 LEU A 366 
AA3 2 ALA A 372 ? PRO A 374 ? ALA A 373 PRO A 375 
AA4 1 ARG A 402 ? VAL A 405 ? ARG A 403 VAL A 406 
AA4 2 GLU A 408 ? THR A 411 ? GLU A 409 THR A 412 
AA5 1 PHE A 562 ? GLN A 563 ? PHE A 563 GLN A 564 
AA5 2 SER A 577 ? HIS A 580 ? SER A 578 HIS A 581 
AA5 3 GLY A 583 ? VAL A 585 ? GLY A 584 VAL A 586 
AA6 1 ASN A 710 ? LEU A 713 ? ASN A 711 LEU A 714 
AA6 2 LYS A 761 ? PHE A 764 ? LYS A 762 PHE A 765 
AA6 3 TYR A 755 ? PHE A 757 ? TYR A 756 PHE A 758 
# 
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 VAL A 68  ? O VAL A 69  N ALA A 60  ? N ALA A 61  
AA1 2 3 O GLU A 61  ? O GLU A 62  N LYS A 49  ? N LYS A 50  
AA1 3 4 O ALA A 48  ? O ALA A 49  N VAL A 36  ? N VAL A 37  
AA1 4 5 N PHE A 37  ? N PHE A 38  O MET A 76  ? O MET A 77  
AA2 1 2 N THR A 115 ? N THR A 116 O VAL A 122 ? O VAL A 123 
AA2 2 3 N CYS A 121 ? N CYS A 122 O ARG A 670 ? O ARG A 671 
AA2 3 4 O HIS A 667 ? O HIS A 668 N SER A 172 ? N SER A 173 
AA2 4 5 N ILE A 173 ? N ILE A 174 O LEU A 459 ? O LEU A 460 
AA2 5 6 O VAL A 458 ? O VAL A 459 N ILE A 247 ? N ILE A 248 
AA2 6 7 N HIS A 250 ? N HIS A 251 O SER A 259 ? O SER A 260 
AA3 1 2 N LYS A 364 ? N LYS A 365 O GLU A 373 ? O GLU A 374 
AA4 1 2 N VAL A 405 ? N VAL A 406 O GLU A 408 ? O GLU A 409 
AA5 1 2 N GLN A 563 ? N GLN A 564 O SER A 577 ? O SER A 578 
AA5 2 3 N LEU A 578 ? N LEU A 579 O VAL A 585 ? O VAL A 586 
AA6 1 2 N ASN A 710 ? N ASN A 711 O PHE A 764 ? O PHE A 765 
AA6 2 3 O PHE A 763 ? O PHE A 764 N LYS A 756 ? N LYS A 757 
# 
_pdbx_entry_details.entry_id                   9GZ3 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_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 GLN A 44  ? ? -162.01 115.53  
2  1 TRP A 112 ? ? 56.53   19.21   
3  1 TYR A 128 ? ? -74.14  44.96   
4  1 GLU A 149 ? ? -93.18  -60.63  
5  1 ARG A 243 ? ? -69.72  22.08   
6  1 LYS A 293 ? ? 58.84   17.62   
7  1 LEU A 302 ? ? -79.78  44.07   
8  1 GLN A 454 ? ? -140.26 -33.99  
9  1 PHE A 468 ? ? -90.63  -155.68 
10 1 PHE A 470 ? ? -174.72 59.48   
11 1 ASN A 471 ? ? -66.64  86.46   
12 1 PRO A 527 ? ? -71.64  20.66   
13 1 ASP A 587 ? ? -100.42 79.06   
14 1 LYS A 598 ? ? -136.86 -37.26  
15 1 LYS A 679 ? ? 59.97   14.05   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9GZ3 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         REAL 
_em_3d_fitting.ref_protocol      'FLEXIBLE FIT' 
# 
_em_3d_fitting_list.id                            1 
_em_3d_fitting_list.3d_fitting_id                 1 
_em_3d_fitting_list.pdb_entry_id                  . 
_em_3d_fitting_list.pdb_chain_id                  . 
_em_3d_fitting_list.pdb_chain_residue_range       . 
_em_3d_fitting_list.details                       ? 
_em_3d_fitting_list.chain_id                      ? 
_em_3d_fitting_list.chain_residue_range           ? 
_em_3d_fitting_list.source_name                   Modeller 
_em_3d_fitting_list.type                          'in silico model' 
_em_3d_fitting_list.accession_code                6Z47 
_em_3d_fitting_list.initial_refinement_model_id   1 
# 
_em_3d_reconstruction.entry_id                    9GZ3 
_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                  3.4 
_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               88809 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          1 
_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       ? 
_em_buffer.pH            7.2 
# 
_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                 'Beta-cardiac heavy meromyosin in the primed state' 
_em_entity_assembly.details              'Complex crosslinked with bis(sulfosuccinimidyl)suberate (BS3)' 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        9GZ3 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'FEI TITAN KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           'FEI TITAN KRIOS AUTOGRID HOLDER' 
_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             1500 
_em_imaging.nominal_defocus_max             3000 
_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             'COMA FREE' 
_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    GOLD 
_em_sample_support.grid_mesh_size   300 
_em_sample_support.grid_type        'Quantifoil R1.2/1.3' 
_em_sample_support.details          ? 
_em_sample_support.specimen_id      1 
_em_sample_support.citation_id      ? 
# 
_em_vitrification.entry_id              9GZ3 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              95 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   281 
_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                9GZ3 
_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 GLY 2    ? A GLY 1    
2   1 Y 1 A ASP 203  ? A ASP 202  
3   1 Y 1 A ARG 204  ? A ARG 203  
4   1 Y 1 A SER 205  ? A SER 204  
5   1 Y 1 A LYS 206  ? A LYS 205  
6   1 Y 1 A LYS 207  ? A LYS 206  
7   1 Y 1 A ASP 208  ? A ASP 207  
8   1 Y 1 A GLN 209  ? A GLN 208  
9   1 Y 1 A SER 210  ? A SER 209  
10  1 Y 1 A PRO 211  ? A PRO 210  
11  1 Y 1 A GLY 212  ? A GLY 211  
12  1 Y 1 A LYS 213  ? A LYS 212  
13  1 Y 1 A ALA 625  ? A ALA 624  
14  1 Y 1 A GLY 626  ? A GLY 625  
15  1 Y 1 A ALA 627  ? A ALA 626  
16  1 Y 1 A ASP 628  ? A ASP 627  
17  1 Y 1 A ALA 629  ? A ALA 628  
18  1 Y 1 A PRO 630  ? A PRO 629  
19  1 Y 1 A ILE 631  ? A ILE 630  
20  1 Y 1 A GLU 632  ? A GLU 631  
21  1 Y 1 A LYS 633  ? A LYS 632  
22  1 Y 1 A GLY 634  ? A GLY 633  
23  1 Y 1 A LYS 635  ? A LYS 634  
24  1 Y 1 A GLY 636  ? A GLY 635  
25  1 Y 1 A LYS 637  ? A LYS 636  
26  1 Y 1 A ALA 638  ? A ALA 637  
27  1 Y 1 A LYS 639  ? A LYS 638  
28  1 Y 1 A LYS 640  ? A LYS 639  
29  1 Y 1 A GLY 641  ? A GLY 640  
30  1 Y 1 A SER 642  ? A SER 641  
31  1 Y 1 A SER 643  ? A SER 642  
32  1 Y 1 A ALA 797  ? A ALA 796  
33  1 Y 1 A ARG 798  ? A ARG 797  
34  1 Y 1 A MET 799  ? A MET 798  
35  1 Y 1 A GLU 800  ? A GLU 799  
36  1 Y 1 A TYR 801  ? A TYR 800  
37  1 Y 1 A LYS 802  ? A LYS 801  
38  1 Y 1 A LYS 803  ? A LYS 802  
39  1 Y 1 A LEU 804  ? A LEU 803  
40  1 Y 1 A LEU 805  ? A LEU 804  
41  1 Y 1 A GLU 806  ? A GLU 805  
42  1 Y 1 A ARG 807  ? A ARG 806  
43  1 Y 1 A ARG 808  ? A ARG 807  
44  1 Y 1 A ASP 809  ? A ASP 808  
45  1 Y 1 A SER 810  ? A SER 809  
46  1 Y 1 A LEU 811  ? A LEU 810  
47  1 Y 1 A LEU 812  ? A LEU 811  
48  1 Y 1 A VAL 813  ? A VAL 812  
49  1 Y 1 A ILE 814  ? A ILE 813  
50  1 Y 1 A GLN 815  ? A GLN 814  
51  1 Y 1 A TRP 816  ? A TRP 815  
52  1 Y 1 A ASN 817  ? A ASN 816  
53  1 Y 1 A ILE 818  ? A ILE 817  
54  1 Y 1 A ARG 819  ? A ARG 818  
55  1 Y 1 A ALA 820  ? A ALA 819  
56  1 Y 1 A PHE 821  ? A PHE 820  
57  1 Y 1 A MET 822  ? A MET 821  
58  1 Y 1 A GLY 823  ? A GLY 822  
59  1 Y 1 A VAL 824  ? A VAL 823  
60  1 Y 1 A LYS 825  ? A LYS 824  
61  1 Y 1 A ASN 826  ? A ASN 825  
62  1 Y 1 A TRP 827  ? A TRP 826  
63  1 Y 1 A PRO 828  ? A PRO 827  
64  1 Y 1 A TRP 829  ? A TRP 828  
65  1 Y 1 A MET 830  ? A MET 829  
66  1 Y 1 A LYS 831  ? A LYS 830  
67  1 Y 1 A LEU 832  ? A LEU 831  
68  1 Y 1 A TYR 833  ? A TYR 832  
69  1 Y 1 A PHE 834  ? A PHE 833  
70  1 Y 1 A LYS 835  ? A LYS 834  
71  1 Y 1 A ILE 836  ? A ILE 835  
72  1 Y 1 A LYS 837  ? A LYS 836  
73  1 Y 1 A PRO 838  ? A PRO 837  
74  1 Y 1 A LEU 839  ? A LEU 838  
75  1 Y 1 A LEU 840  ? A LEU 839  
76  1 Y 1 A LYS 841  ? A LYS 840  
77  1 Y 1 A SER 842  ? A SER 841  
78  1 Y 1 A ALA 843  ? A ALA 842  
79  1 Y 1 A GLU 844  ? A GLU 843  
80  1 Y 1 A ARG 845  ? A ARG 844  
81  1 Y 1 A GLU 846  ? A GLU 845  
82  1 Y 1 A LYS 847  ? A LYS 846  
83  1 Y 1 A GLU 848  ? A GLU 847  
84  1 Y 1 A MET 849  ? A MET 848  
85  1 Y 1 A ALA 850  ? A ALA 849  
86  1 Y 1 A SER 851  ? A SER 850  
87  1 Y 1 A MET 852  ? A MET 851  
88  1 Y 1 A LYS 853  ? A LYS 852  
89  1 Y 1 A GLU 854  ? A GLU 853  
90  1 Y 1 A GLU 855  ? A GLU 854  
91  1 Y 1 A PHE 856  ? A PHE 855  
92  1 Y 1 A THR 857  ? A THR 856  
93  1 Y 1 A ARG 858  ? A ARG 857  
94  1 Y 1 A LEU 859  ? A LEU 858  
95  1 Y 1 A LYS 860  ? A LYS 859  
96  1 Y 1 A GLU 861  ? A GLU 860  
97  1 Y 1 A ALA 862  ? A ALA 861  
98  1 Y 1 A LEU 863  ? A LEU 862  
99  1 Y 1 A GLU 864  ? A GLU 863  
100 1 Y 1 A LYS 865  ? A LYS 864  
101 1 Y 1 A SER 866  ? A SER 865  
102 1 Y 1 A GLU 867  ? A GLU 866  
103 1 Y 1 A ALA 868  ? A ALA 867  
104 1 Y 1 A ARG 869  ? A ARG 868  
105 1 Y 1 A ARG 870  ? A ARG 869  
106 1 Y 1 A LYS 871  ? A LYS 870  
107 1 Y 1 A GLU 872  ? A GLU 871  
108 1 Y 1 A LEU 873  ? A LEU 872  
109 1 Y 1 A GLU 874  ? A GLU 873  
110 1 Y 1 A GLU 875  ? A GLU 874  
111 1 Y 1 A LYS 876  ? A LYS 875  
112 1 Y 1 A MET 877  ? A MET 876  
113 1 Y 1 A VAL 878  ? A VAL 877  
114 1 Y 1 A SER 879  ? A SER 878  
115 1 Y 1 A LEU 880  ? A LEU 879  
116 1 Y 1 A LEU 881  ? A LEU 880  
117 1 Y 1 A GLN 882  ? A GLN 881  
118 1 Y 1 A GLU 883  ? A GLU 882  
119 1 Y 1 A LYS 884  ? A LYS 883  
120 1 Y 1 A ASN 885  ? A ASN 884  
121 1 Y 1 A ASP 886  ? A ASP 885  
122 1 Y 1 A LEU 887  ? A LEU 886  
123 1 Y 1 A GLN 888  ? A GLN 887  
124 1 Y 1 A LEU 889  ? A LEU 888  
125 1 Y 1 A GLN 890  ? A GLN 889  
126 1 Y 1 A VAL 891  ? A VAL 890  
127 1 Y 1 A GLN 892  ? A GLN 891  
128 1 Y 1 A ALA 893  ? A ALA 892  
129 1 Y 1 A GLU 894  ? A GLU 893  
130 1 Y 1 A GLN 895  ? A GLN 894  
131 1 Y 1 A ASP 896  ? A ASP 895  
132 1 Y 1 A ASN 897  ? A ASN 896  
133 1 Y 1 A LEU 898  ? A LEU 897  
134 1 Y 1 A ALA 899  ? A ALA 898  
135 1 Y 1 A ASP 900  ? A ASP 899  
136 1 Y 1 A ALA 901  ? A ALA 900  
137 1 Y 1 A GLU 902  ? A GLU 901  
138 1 Y 1 A GLU 903  ? A GLU 902  
139 1 Y 1 A ARG 904  ? A ARG 903  
140 1 Y 1 A CYS 905  ? A CYS 904  
141 1 Y 1 A ASP 906  ? A ASP 905  
142 1 Y 1 A GLN 907  ? A GLN 906  
143 1 Y 1 A LEU 908  ? A LEU 907  
144 1 Y 1 A ILE 909  ? A ILE 908  
145 1 Y 1 A LYS 910  ? A LYS 909  
146 1 Y 1 A ASN 911  ? A ASN 910  
147 1 Y 1 A LYS 912  ? A LYS 911  
148 1 Y 1 A ILE 913  ? A ILE 912  
149 1 Y 1 A GLN 914  ? A GLN 913  
150 1 Y 1 A LEU 915  ? A LEU 914  
151 1 Y 1 A GLU 916  ? A GLU 915  
152 1 Y 1 A ALA 917  ? A ALA 916  
153 1 Y 1 A LYS 918  ? A LYS 917  
154 1 Y 1 A VAL 919  ? A VAL 918  
155 1 Y 1 A LYS 920  ? A LYS 919  
156 1 Y 1 A GLU 921  ? A GLU 920  
157 1 Y 1 A MET 922  ? A MET 921  
158 1 Y 1 A ASN 923  ? A ASN 922  
159 1 Y 1 A GLU 924  ? A GLU 923  
160 1 Y 1 A ARG 925  ? A ARG 924  
161 1 Y 1 A LEU 926  ? A LEU 925  
162 1 Y 1 A GLU 927  ? A GLU 926  
163 1 Y 1 A ASP 928  ? A ASP 927  
164 1 Y 1 A GLU 929  ? A GLU 928  
165 1 Y 1 A GLU 930  ? A GLU 929  
166 1 Y 1 A GLU 931  ? A GLU 930  
167 1 Y 1 A MET 932  ? A MET 931  
168 1 Y 1 A ASN 933  ? A ASN 932  
169 1 Y 1 A ALA 934  ? A ALA 933  
170 1 Y 1 A GLU 935  ? A GLU 934  
171 1 Y 1 A LEU 936  ? A LEU 935  
172 1 Y 1 A THR 937  ? A THR 936  
173 1 Y 1 A ALA 938  ? A ALA 937  
174 1 Y 1 A LYS 939  ? A LYS 938  
175 1 Y 1 A LYS 940  ? A LYS 939  
176 1 Y 1 A ARG 941  ? A ARG 940  
177 1 Y 1 A LYS 942  ? A LYS 941  
178 1 Y 1 A LEU 943  ? A LEU 942  
179 1 Y 1 A GLU 944  ? A GLU 943  
180 1 Y 1 A ASP 945  ? A ASP 944  
181 1 Y 1 A GLU 946  ? A GLU 945  
182 1 Y 1 A CYS 947  ? A CYS 946  
183 1 Y 1 A SER 948  ? A SER 947  
184 1 Y 1 A GLU 949  ? A GLU 948  
185 1 Y 1 A LEU 950  ? A LEU 949  
186 1 Y 1 A LYS 951  ? A LYS 950  
187 1 Y 1 A ARG 952  ? A ARG 951  
188 1 Y 1 A ASP 953  ? A ASP 952  
189 1 Y 1 A ILE 954  ? A ILE 953  
190 1 Y 1 A ASP 955  ? A ASP 954  
191 1 Y 1 A ASP 956  ? A ASP 955  
192 1 Y 1 A LEU 957  ? A LEU 956  
193 1 Y 1 A GLU 958  ? A GLU 957  
194 1 Y 1 A LEU 959  ? A LEU 958  
195 1 Y 1 A THR 960  ? A THR 959  
196 1 Y 1 A LEU 961  ? A LEU 960  
197 1 Y 1 A ALA 962  ? A ALA 961  
198 1 Y 1 A LYS 963  ? A LYS 962  
199 1 Y 1 A VAL 964  ? A VAL 963  
200 1 Y 1 A GLU 965  ? A GLU 964  
201 1 Y 1 A LYS 966  ? A LYS 965  
202 1 Y 1 A GLU 967  ? A GLU 966  
203 1 Y 1 A LYS 968  ? A LYS 967  
204 1 Y 1 A HIS 969  ? A HIS 968  
205 1 Y 1 A ALA 970  ? A ALA 969  
206 1 Y 1 A THR 971  ? A THR 970  
207 1 Y 1 A GLU 972  ? A GLU 971  
208 1 Y 1 A ASN 973  ? A ASN 972  
209 1 Y 1 A LYS 974  ? A LYS 973  
210 1 Y 1 A VAL 975  ? A VAL 974  
211 1 Y 1 A LYS 976  ? A LYS 975  
212 1 Y 1 A ASN 977  ? A ASN 976  
213 1 Y 1 A LEU 978  ? A LEU 977  
214 1 Y 1 A THR 979  ? A THR 978  
215 1 Y 1 A GLU 980  ? A GLU 979  
216 1 Y 1 A GLU 981  ? A GLU 980  
217 1 Y 1 A MET 982  ? A MET 981  
218 1 Y 1 A ALA 983  ? A ALA 982  
219 1 Y 1 A GLY 984  ? A GLY 983  
220 1 Y 1 A LEU 985  ? A LEU 984  
221 1 Y 1 A ASP 986  ? A ASP 985  
222 1 Y 1 A GLU 987  ? A GLU 986  
223 1 Y 1 A ILE 988  ? A ILE 987  
224 1 Y 1 A ILE 989  ? A ILE 988  
225 1 Y 1 A ALA 990  ? A ALA 989  
226 1 Y 1 A LYS 991  ? A LYS 990  
227 1 Y 1 A LEU 992  ? A LEU 991  
228 1 Y 1 A THR 993  ? A THR 992  
229 1 Y 1 A LYS 994  ? A LYS 993  
230 1 Y 1 A GLU 995  ? A GLU 994  
231 1 Y 1 A LYS 996  ? A LYS 995  
232 1 Y 1 A LYS 997  ? A LYS 996  
233 1 Y 1 A ALA 998  ? A ALA 997  
234 1 Y 1 A LEU 999  ? A LEU 998  
235 1 Y 1 A GLN 1000 ? A GLN 999  
236 1 Y 1 A GLU 1001 ? A GLU 1000 
237 1 Y 1 A ALA 1002 ? A ALA 1001 
238 1 Y 1 A HIS 1003 ? A HIS 1002 
239 1 Y 1 A GLN 1004 ? A GLN 1003 
240 1 Y 1 A GLN 1005 ? A GLN 1004 
241 1 Y 1 A ALA 1006 ? A ALA 1005 
242 1 Y 1 A LEU 1007 ? A LEU 1006 
243 1 Y 1 A ASP 1008 ? A ASP 1007 
244 1 Y 1 A ASP 1009 ? A ASP 1008 
245 1 Y 1 A LEU 1010 ? A LEU 1009 
246 1 Y 1 A GLN 1011 ? A GLN 1010 
247 1 Y 1 A ALA 1012 ? A ALA 1011 
248 1 Y 1 A GLU 1013 ? A GLU 1012 
249 1 Y 1 A GLU 1014 ? A GLU 1013 
250 1 Y 1 A ASP 1015 ? A ASP 1014 
251 1 Y 1 A LYS 1016 ? A LYS 1015 
252 1 Y 1 A VAL 1017 ? A VAL 1016 
253 1 Y 1 A ASN 1018 ? A ASN 1017 
254 1 Y 1 A THR 1019 ? A THR 1018 
255 1 Y 1 A LEU 1020 ? A LEU 1019 
256 1 Y 1 A THR 1021 ? A THR 1020 
257 1 Y 1 A LYS 1022 ? A LYS 1021 
258 1 Y 1 A ALA 1023 ? A ALA 1022 
259 1 Y 1 A LYS 1024 ? A LYS 1023 
260 1 Y 1 A VAL 1025 ? A VAL 1024 
261 1 Y 1 A LYS 1026 ? A LYS 1025 
262 1 Y 1 A LEU 1027 ? A LEU 1026 
263 1 Y 1 A GLU 1028 ? A GLU 1027 
264 1 Y 1 A GLN 1029 ? A GLN 1028 
265 1 Y 1 A GLN 1030 ? A GLN 1029 
266 1 Y 1 A VAL 1031 ? A VAL 1030 
267 1 Y 1 A ASP 1032 ? A ASP 1031 
268 1 Y 1 A ASP 1033 ? A ASP 1032 
269 1 Y 1 A LEU 1034 ? A LEU 1033 
270 1 Y 1 A GLU 1035 ? A GLU 1034 
271 1 Y 1 A GLY 1036 ? A GLY 1035 
272 1 Y 1 A SER 1037 ? A SER 1036 
273 1 Y 1 A LEU 1038 ? A LEU 1037 
274 1 Y 1 A GLU 1039 ? A GLU 1038 
275 1 Y 1 A GLN 1040 ? A GLN 1039 
276 1 Y 1 A GLU 1041 ? A GLU 1040 
277 1 Y 1 A LYS 1042 ? A LYS 1041 
278 1 Y 1 A LYS 1043 ? A LYS 1042 
279 1 Y 1 A VAL 1044 ? A VAL 1043 
280 1 Y 1 A ARG 1045 ? A ARG 1044 
281 1 Y 1 A MET 1046 ? A MET 1045 
282 1 Y 1 A ASP 1047 ? A ASP 1046 
283 1 Y 1 A LEU 1048 ? A LEU 1047 
284 1 Y 1 A GLU 1049 ? A GLU 1048 
285 1 Y 1 A ARG 1050 ? A ARG 1049 
286 1 Y 1 A ALA 1051 ? A ALA 1050 
287 1 Y 1 A LYS 1052 ? A LYS 1051 
288 1 Y 1 A ARG 1053 ? A ARG 1052 
289 1 Y 1 A LYS 1054 ? A LYS 1053 
290 1 Y 1 A LEU 1055 ? A LEU 1054 
291 1 Y 1 A GLU 1056 ? A GLU 1055 
292 1 Y 1 A GLY 1057 ? A GLY 1056 
293 1 Y 1 A ASP 1058 ? A ASP 1057 
294 1 Y 1 A LEU 1059 ? A LEU 1058 
295 1 Y 1 A LYS 1060 ? A LYS 1059 
296 1 Y 1 A LEU 1061 ? A LEU 1060 
297 1 Y 1 A THR 1062 ? A THR 1061 
298 1 Y 1 A GLN 1063 ? A GLN 1062 
299 1 Y 1 A GLU 1064 ? A GLU 1063 
300 1 Y 1 A SER 1065 ? A SER 1064 
301 1 Y 1 A ILE 1066 ? A ILE 1065 
302 1 Y 1 A MET 1067 ? A MET 1066 
303 1 Y 1 A ASP 1068 ? A ASP 1067 
304 1 Y 1 A LEU 1069 ? A LEU 1068 
305 1 Y 1 A GLU 1070 ? A GLU 1069 
306 1 Y 1 A ASN 1071 ? A ASN 1070 
307 1 Y 1 A ASP 1072 ? A ASP 1071 
308 1 Y 1 A LYS 1073 ? A LYS 1072 
309 1 Y 1 A GLN 1074 ? A GLN 1073 
310 1 Y 1 A GLN 1075 ? A GLN 1074 
311 1 Y 1 A LEU 1076 ? A LEU 1075 
312 1 Y 1 A ASP 1077 ? A ASP 1076 
313 1 Y 1 A GLU 1078 ? A GLU 1077 
314 1 Y 1 A ARG 1079 ? A ARG 1078 
315 1 Y 1 A LEU 1080 ? A LEU 1079 
316 1 Y 1 A LYS 1081 ? A LYS 1080 
317 1 Y 1 A LYS 1082 ? A LYS 1081 
318 1 Y 1 A LYS 1083 ? A LYS 1082 
319 1 Y 1 A ASP 1084 ? A ASP 1083 
320 1 Y 1 A PHE 1085 ? A PHE 1084 
321 1 Y 1 A GLU 1086 ? A GLU 1085 
322 1 Y 1 A LEU 1087 ? A LEU 1086 
323 1 Y 1 A ASN 1088 ? A ASN 1087 
324 1 Y 1 A ALA 1089 ? A ALA 1088 
325 1 Y 1 A LEU 1090 ? A LEU 1089 
326 1 Y 1 A ASN 1091 ? A ASN 1090 
327 1 Y 1 A ALA 1092 ? A ALA 1091 
328 1 Y 1 A ARG 1093 ? A ARG 1092 
329 1 Y 1 A ILE 1094 ? A ILE 1093 
330 1 Y 1 A GLU 1095 ? A GLU 1094 
331 1 Y 1 A ASP 1096 ? A ASP 1095 
332 1 Y 1 A GLU 1097 ? A GLU 1096 
333 1 Y 1 A GLN 1098 ? A GLN 1097 
334 1 Y 1 A ALA 1099 ? A ALA 1098 
335 1 Y 1 A LEU 1100 ? A LEU 1099 
336 1 Y 1 A GLY 1101 ? A GLY 1100 
337 1 Y 1 A SER 1102 ? A SER 1101 
338 1 Y 1 A GLN 1103 ? A GLN 1102 
339 1 Y 1 A LEU 1104 ? A LEU 1103 
340 1 Y 1 A GLN 1105 ? A GLN 1104 
341 1 Y 1 A LYS 1106 ? A LYS 1105 
342 1 Y 1 A LYS 1107 ? A LYS 1106 
343 1 Y 1 A LEU 1108 ? A LEU 1107 
344 1 Y 1 A LYS 1109 ? A LYS 1108 
345 1 Y 1 A GLU 1110 ? A GLU 1109 
346 1 Y 1 A LEU 1111 ? A LEU 1110 
347 1 Y 1 A GLN 1112 ? A GLN 1111 
348 1 Y 1 A ALA 1113 ? A ALA 1112 
349 1 Y 1 A ARG 1114 ? A ARG 1113 
350 1 Y 1 A ILE 1115 ? A ILE 1114 
351 1 Y 1 A GLU 1116 ? A GLU 1115 
352 1 Y 1 A GLU 1117 ? A GLU 1116 
353 1 Y 1 A LEU 1118 ? A LEU 1117 
354 1 Y 1 A GLU 1119 ? A GLU 1118 
355 1 Y 1 A GLU 1120 ? A GLU 1119 
356 1 Y 1 A GLU 1121 ? A GLU 1120 
357 1 Y 1 A LEU 1122 ? A LEU 1121 
358 1 Y 1 A GLU 1123 ? A GLU 1122 
359 1 Y 1 A SER 1124 ? A SER 1123 
360 1 Y 1 A GLU 1125 ? A GLU 1124 
361 1 Y 1 A ARG 1126 ? A ARG 1125 
362 1 Y 1 A THR 1127 ? A THR 1126 
363 1 Y 1 A ALA 1128 ? A ALA 1127 
364 1 Y 1 A ARG 1129 ? A ARG 1128 
365 1 Y 1 A ALA 1130 ? A ALA 1129 
366 1 Y 1 A LYS 1131 ? A LYS 1130 
367 1 Y 1 A VAL 1132 ? A VAL 1131 
368 1 Y 1 A GLU 1133 ? A GLU 1132 
369 1 Y 1 A LYS 1134 ? A LYS 1133 
370 1 Y 1 A LEU 1135 ? A LEU 1134 
371 1 Y 1 A ARG 1136 ? A ARG 1135 
372 1 Y 1 A SER 1137 ? A SER 1136 
373 1 Y 1 A ASP 1138 ? A ASP 1137 
374 1 Y 1 A ASP 1139 ? A ASP 1138 
375 1 Y 1 A TYR 1140 ? A TYR 1139 
376 1 Y 1 A LYS 1141 ? A LYS 1140 
377 1 Y 1 A ASP 1142 ? A ASP 1141 
378 1 Y 1 A ASP 1143 ? A ASP 1142 
379 1 Y 1 A ASP 1144 ? A ASP 1143 
380 1 Y 1 A ASP 1145 ? A ASP 1144 
381 1 Y 1 A LYS 1146 ? A LYS 1145 
# 
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 
PO4 P      P  N N 313 
PO4 O1     O  N N 314 
PO4 O2     O  N N 315 
PO4 O3     O  N N 316 
PO4 O4     O  N N 317 
PRO N      N  N N 318 
PRO CA     C  N S 319 
PRO C      C  N N 320 
PRO O      O  N N 321 
PRO CB     C  N N 322 
PRO CG     C  N N 323 
PRO CD     C  N N 324 
PRO OXT    O  N N 325 
PRO H      H  N N 326 
PRO HA     H  N N 327 
PRO HB2    H  N N 328 
PRO HB3    H  N N 329 
PRO HG2    H  N N 330 
PRO HG3    H  N N 331 
PRO HD2    H  N N 332 
PRO HD3    H  N N 333 
PRO HXT    H  N N 334 
SER N      N  N N 335 
SER CA     C  N S 336 
SER C      C  N N 337 
SER O      O  N N 338 
SER CB     C  N N 339 
SER OG     O  N N 340 
SER OXT    O  N N 341 
SER H      H  N N 342 
SER H2     H  N N 343 
SER HA     H  N N 344 
SER HB2    H  N N 345 
SER HB3    H  N N 346 
SER HG     H  N N 347 
SER HXT    H  N N 348 
THR N      N  N N 349 
THR CA     C  N S 350 
THR C      C  N N 351 
THR O      O  N N 352 
THR CB     C  N R 353 
THR OG1    O  N N 354 
THR CG2    C  N N 355 
THR OXT    O  N N 356 
THR H      H  N N 357 
THR H2     H  N N 358 
THR HA     H  N N 359 
THR HB     H  N N 360 
THR HG1    H  N N 361 
THR HG21   H  N N 362 
THR HG22   H  N N 363 
THR HG23   H  N N 364 
THR HXT    H  N N 365 
TRP N      N  N N 366 
TRP CA     C  N S 367 
TRP C      C  N N 368 
TRP O      O  N N 369 
TRP CB     C  N N 370 
TRP CG     C  Y N 371 
TRP CD1    C  Y N 372 
TRP CD2    C  Y N 373 
TRP NE1    N  Y N 374 
TRP CE2    C  Y N 375 
TRP CE3    C  Y N 376 
TRP CZ2    C  Y N 377 
TRP CZ3    C  Y N 378 
TRP CH2    C  Y N 379 
TRP OXT    O  N N 380 
TRP H      H  N N 381 
TRP H2     H  N N 382 
TRP HA     H  N N 383 
TRP HB2    H  N N 384 
TRP HB3    H  N N 385 
TRP HD1    H  N N 386 
TRP HE1    H  N N 387 
TRP HE3    H  N N 388 
TRP HZ2    H  N N 389 
TRP HZ3    H  N N 390 
TRP HH2    H  N N 391 
TRP HXT    H  N N 392 
TYR N      N  N N 393 
TYR CA     C  N S 394 
TYR C      C  N N 395 
TYR O      O  N N 396 
TYR CB     C  N N 397 
TYR CG     C  Y N 398 
TYR CD1    C  Y N 399 
TYR CD2    C  Y N 400 
TYR CE1    C  Y N 401 
TYR CE2    C  Y N 402 
TYR CZ     C  Y N 403 
TYR OH     O  N N 404 
TYR OXT    O  N N 405 
TYR H      H  N N 406 
TYR H2     H  N N 407 
TYR HA     H  N N 408 
TYR HB2    H  N N 409 
TYR HB3    H  N N 410 
TYR HD1    H  N N 411 
TYR HD2    H  N N 412 
TYR HE1    H  N N 413 
TYR HE2    H  N N 414 
TYR HH     H  N N 415 
TYR HXT    H  N N 416 
VAL N      N  N N 417 
VAL CA     C  N S 418 
VAL C      C  N N 419 
VAL O      O  N N 420 
VAL CB     C  N N 421 
VAL CG1    C  N N 422 
VAL CG2    C  N N 423 
VAL OXT    O  N N 424 
VAL H      H  N N 425 
VAL H2     H  N N 426 
VAL HA     H  N N 427 
VAL HB     H  N N 428 
VAL HG11   H  N N 429 
VAL HG12   H  N N 430 
VAL HG13   H  N N 431 
VAL HG21   H  N N 432 
VAL HG22   H  N N 433 
VAL HG23   H  N N 434 
VAL HXT    H  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 
PO4 P     O1     doub N N 302 
PO4 P     O2     sing N N 303 
PO4 P     O3     sing N N 304 
PO4 P     O4     sing N N 305 
PRO N     CA     sing N N 306 
PRO N     CD     sing N N 307 
PRO N     H      sing N N 308 
PRO CA    C      sing N N 309 
PRO CA    CB     sing N N 310 
PRO CA    HA     sing N N 311 
PRO C     O      doub N N 312 
PRO C     OXT    sing N N 313 
PRO CB    CG     sing N N 314 
PRO CB    HB2    sing N N 315 
PRO CB    HB3    sing N N 316 
PRO CG    CD     sing N N 317 
PRO CG    HG2    sing N N 318 
PRO CG    HG3    sing N N 319 
PRO CD    HD2    sing N N 320 
PRO CD    HD3    sing N N 321 
PRO OXT   HXT    sing N N 322 
SER N     CA     sing N N 323 
SER N     H      sing N N 324 
SER N     H2     sing N N 325 
SER CA    C      sing N N 326 
SER CA    CB     sing N N 327 
SER CA    HA     sing N N 328 
SER C     O      doub N N 329 
SER C     OXT    sing N N 330 
SER CB    OG     sing N N 331 
SER CB    HB2    sing N N 332 
SER CB    HB3    sing N N 333 
SER OG    HG     sing N N 334 
SER OXT   HXT    sing N N 335 
THR N     CA     sing N N 336 
THR N     H      sing N N 337 
THR N     H2     sing N N 338 
THR CA    C      sing N N 339 
THR CA    CB     sing N N 340 
THR CA    HA     sing N N 341 
THR C     O      doub N N 342 
THR C     OXT    sing N N 343 
THR CB    OG1    sing N N 344 
THR CB    CG2    sing N N 345 
THR CB    HB     sing N N 346 
THR OG1   HG1    sing N N 347 
THR CG2   HG21   sing N N 348 
THR CG2   HG22   sing N N 349 
THR CG2   HG23   sing N N 350 
THR OXT   HXT    sing N N 351 
TRP N     CA     sing N N 352 
TRP N     H      sing N N 353 
TRP N     H2     sing N N 354 
TRP CA    C      sing N N 355 
TRP CA    CB     sing N N 356 
TRP CA    HA     sing N N 357 
TRP C     O      doub N N 358 
TRP C     OXT    sing N N 359 
TRP CB    CG     sing N N 360 
TRP CB    HB2    sing N N 361 
TRP CB    HB3    sing N N 362 
TRP CG    CD1    doub Y N 363 
TRP CG    CD2    sing Y N 364 
TRP CD1   NE1    sing Y N 365 
TRP CD1   HD1    sing N N 366 
TRP CD2   CE2    doub Y N 367 
TRP CD2   CE3    sing Y N 368 
TRP NE1   CE2    sing Y N 369 
TRP NE1   HE1    sing N N 370 
TRP CE2   CZ2    sing Y N 371 
TRP CE3   CZ3    doub Y N 372 
TRP CE3   HE3    sing N N 373 
TRP CZ2   CH2    doub Y N 374 
TRP CZ2   HZ2    sing N N 375 
TRP CZ3   CH2    sing Y N 376 
TRP CZ3   HZ3    sing N N 377 
TRP CH2   HH2    sing N N 378 
TRP OXT   HXT    sing N N 379 
TYR N     CA     sing N N 380 
TYR N     H      sing N N 381 
TYR N     H2     sing N N 382 
TYR CA    C      sing N N 383 
TYR CA    CB     sing N N 384 
TYR CA    HA     sing N N 385 
TYR C     O      doub N N 386 
TYR C     OXT    sing N N 387 
TYR CB    CG     sing N N 388 
TYR CB    HB2    sing N N 389 
TYR CB    HB3    sing N N 390 
TYR CG    CD1    doub Y N 391 
TYR CG    CD2    sing Y N 392 
TYR CD1   CE1    sing Y N 393 
TYR CD1   HD1    sing N N 394 
TYR CD2   CE2    doub Y N 395 
TYR CD2   HD2    sing N N 396 
TYR CE1   CZ     doub Y N 397 
TYR CE1   HE1    sing N N 398 
TYR CE2   CZ     sing Y N 399 
TYR CE2   HE2    sing N N 400 
TYR CZ    OH     sing N N 401 
TYR OH    HH     sing N N 402 
TYR OXT   HXT    sing N N 403 
VAL N     CA     sing N N 404 
VAL N     H      sing N N 405 
VAL N     H2     sing N N 406 
VAL CA    C      sing N N 407 
VAL CA    CB     sing N N 408 
VAL CA    HA     sing N N 409 
VAL C     O      doub N N 410 
VAL C     OXT    sing N N 411 
VAL CB    CG1    sing N N 412 
VAL CB    CG2    sing N N 413 
VAL CB    HB     sing N N 414 
VAL CG1   HG11   sing N N 415 
VAL CG1   HG12   sing N N 416 
VAL CG1   HG13   sing N N 417 
VAL CG2   HG21   sing N N 418 
VAL CG2   HG22   sing N N 419 
VAL CG2   HG23   sing N N 420 
VAL OXT   HXT    sing N N 421 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-10-03 
_em_admin.deposition_site    PDBE 
_em_admin.entry_id           9GZ3 
_em_admin.last_update        2025-03-12 
_em_admin.map_release_date   2025-03-12 
_em_admin.title              'Beta-cardiac heavy meromyosin motor domain in the primed state' 
# 
loop_
_em_buffer_component.buffer_id 
_em_buffer_component.concentration 
_em_buffer_component.concentration_units 
_em_buffer_component.formula 
_em_buffer_component.id 
_em_buffer_component.name 
1 50  mM KCl   1 'Potassium chloride'                   
1 10  mM MOPS  2 '3-(N-morpholino)propanesulfonic acid' 
1 2   mM MgCl2 3 'Magnesium chloride'                   
1 1   mM ATP   4 'Adenosine triphosphate'               
1 1   mM EGTA  5 'egtazic acid'                         
1 2.5 %  DMSO  6 Dimethylsulfoxide                      
# 
_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                ? 
_em_entity_assembly_molwt.value                ? 
# 
_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          9606 
_em_entity_assembly_naturalsource.organism             'Homo sapiens' 
_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          10090 
_em_entity_assembly_recombinant.organism             'Mus musculus' 
_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               3.6 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         42.9 
_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                    1 
_em_image_recording.num_real_images                     9948 
# 
_em_particle_selection.details                  ? 
_em_particle_selection.id                       1 
_em_particle_selection.image_processing_id      1 
_em_particle_selection.method                   ? 
_em_particle_selection.num_particles_selected   3436065 
_em_particle_selection.reference_model          ? 
# 
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 
'PARTICLE SELECTION'            ? 1  1 ? ? Topaz     ? 
'IMAGE ACQUISITION'             ? 2  ? ? 1 EPU       ? 
MASKING                         ? 3  ? ? ? ?         ? 
'CTF CORRECTION'                ? 4  1 ? ? CTFFIND   ? 
'LAYERLINE INDEXING'            ? 5  ? ? ? ?         ? 
'DIFFRACTION INDEXING'          ? 6  ? ? ? ?         ? 
'MODEL FITTING'                 ? 7  ? 1 ? ISOLDE    ? 
'MODEL FITTING'                 ? 8  ? 1 ? Coot      ? 
OTHER                           ? 9  ? ? ? ?         ? 
'MODEL REFINEMENT'              ? 10 ? 1 ? PHENIX    ? 
'INITIAL EULER ASSIGNMENT'      ? 11 1 ? ? cryoSPARC ? 
'FINAL EULER ASSIGNMENT'        ? 12 1 ? ? cryoSPARC ? 
CLASSIFICATION                  ? 13 1 ? ? cryoSPARC ? 
RECONSTRUCTION                  ? 14 1 ? ? cryoSPARC ? 
'VOLUME SELECTION'              ? 15 1 1 1 ?         ? 
'SERIES ALIGNMENT'              ? 16 1 1 1 ?         ? 
'MOLECULAR REPLACEMENT'         ? 17 1 1 1 ?         ? 
'LATTICE DISTORTION CORRECTION' ? 18 1 1 1 ?         ? 
'SYMMETRY DETERMINATION'        ? 19 1 1 1 ?         ? 
'CRYSTALLOGRAPHY MERGING'       ? 20 1 1 1 ?         ? 
# 
_em_specimen.concentration           0.34 
_em_specimen.details                 'Crosslinked with bis(sulfosuccinimidyl)suberate (BS3)' 
_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   'British Heart Foundation' 
_pdbx_audit_support.country                'United Kingdom' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      Modeller 
_pdbx_initial_refinement_model.accession_code   6Z47 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9GZ3 
_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  
# 
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     . ASP A 1 2   ? 125.627 151.049 130.213 1.00 69.06  ? 3    ASP A N     1 
ATOM   2    C  CA    . ASP A 1 2   ? 126.564 151.778 129.369 1.00 69.06  ? 3    ASP A CA    1 
ATOM   3    C  C     . ASP A 1 2   ? 127.446 150.801 128.597 1.00 69.06  ? 3    ASP A C     1 
ATOM   4    O  O     . ASP A 1 2   ? 127.860 149.774 129.138 1.00 69.06  ? 3    ASP A O     1 
ATOM   5    C  CB    . ASP A 1 2   ? 127.412 152.728 130.215 1.00 69.06  ? 3    ASP A CB    1 
ATOM   6    C  CG    . ASP A 1 2   ? 126.572 153.755 130.949 1.00 69.06  ? 3    ASP A CG    1 
ATOM   7    O  OD1   . ASP A 1 2   ? 127.144 154.561 131.711 1.00 69.06  ? 3    ASP A OD1   1 
ATOM   8    O  OD2   . ASP A 1 2   ? 125.337 153.753 130.765 1.00 69.06  ? 3    ASP A OD2   1 
ATOM   9    N  N     . SER A 1 3   ? 127.719 151.131 127.331 1.00 69.63  ? 4    SER A N     1 
ATOM   10   C  CA    . SER A 1 3   ? 128.259 150.147 126.394 1.00 69.63  ? 4    SER A CA    1 
ATOM   11   C  C     . SER A 1 3   ? 129.715 149.818 126.702 1.00 69.63  ? 4    SER A C     1 
ATOM   12   O  O     . SER A 1 3   ? 130.090 148.642 126.778 1.00 69.63  ? 4    SER A O     1 
ATOM   13   C  CB    . SER A 1 3   ? 128.119 150.664 124.963 1.00 69.63  ? 4    SER A CB    1 
ATOM   14   O  OG    . SER A 1 3   ? 128.836 151.875 124.792 1.00 69.63  ? 4    SER A OG    1 
ATOM   15   N  N     . GLU A 1 4   ? 130.557 150.847 126.831 1.00 65.72  ? 5    GLU A N     1 
ATOM   16   C  CA    . GLU A 1 4   ? 131.956 150.639 127.193 1.00 65.72  ? 5    GLU A CA    1 
ATOM   17   C  C     . GLU A 1 4   ? 132.084 150.040 128.588 1.00 65.72  ? 5    GLU A C     1 
ATOM   18   O  O     . GLU A 1 4   ? 132.933 149.173 128.830 1.00 65.72  ? 5    GLU A O     1 
ATOM   19   C  CB    . GLU A 1 4   ? 132.714 151.964 127.104 1.00 65.72  ? 5    GLU A CB    1 
ATOM   20   C  CG    . GLU A 1 4   ? 134.184 151.888 127.481 1.00 65.72  ? 5    GLU A CG    1 
ATOM   21   C  CD    . GLU A 1 4   ? 134.927 153.174 127.186 1.00 65.72  ? 5    GLU A CD    1 
ATOM   22   O  OE1   . GLU A 1 4   ? 134.286 154.245 127.189 1.00 65.72  ? 5    GLU A OE1   1 
ATOM   23   O  OE2   . GLU A 1 4   ? 136.152 153.115 126.951 1.00 65.72  ? 5    GLU A OE2   1 
ATOM   24   N  N     . MET A 1 5   ? 131.223 150.468 129.509 1.00 58.80  ? 6    MET A N     1 
ATOM   25   C  CA    . MET A 1 5   ? 131.246 150.036 130.900 1.00 58.80  ? 6    MET A CA    1 
ATOM   26   C  C     . MET A 1 5   ? 130.497 148.731 131.150 1.00 58.80  ? 6    MET A C     1 
ATOM   27   O  O     . MET A 1 5   ? 130.286 148.387 132.317 1.00 58.80  ? 6    MET A O     1 
ATOM   28   C  CB    . MET A 1 5   ? 130.650 151.143 131.769 1.00 58.80  ? 6    MET A CB    1 
ATOM   29   C  CG    . MET A 1 5   ? 131.447 152.426 131.745 1.00 58.80  ? 6    MET A CG    1 
ATOM   30   S  SD    . MET A 1 5   ? 133.078 152.166 132.439 1.00 58.80  ? 6    MET A SD    1 
ATOM   31   C  CE    . MET A 1 5   ? 132.636 152.000 134.162 1.00 58.80  ? 6    MET A CE    1 
ATOM   32   N  N     . ALA A 1 6   ? 130.058 148.042 130.089 1.00 57.69  ? 7    ALA A N     1 
ATOM   33   C  CA    . ALA A 1 6   ? 129.229 146.842 130.222 1.00 57.69  ? 7    ALA A CA    1 
ATOM   34   C  C     . ALA A 1 6   ? 129.919 145.717 130.988 1.00 57.69  ? 7    ALA A C     1 
ATOM   35   O  O     . ALA A 1 6   ? 129.245 144.903 131.630 1.00 57.69  ? 7    ALA A O     1 
ATOM   36   C  CB    . ALA A 1 6   ? 128.808 146.345 128.839 1.00 57.69  ? 7    ALA A CB    1 
ATOM   37   N  N     . VAL A 1 7   ? 131.252 145.645 130.917 1.00 50.82  ? 8    VAL A N     1 
ATOM   38   C  CA    . VAL A 1 7   ? 132.008 144.626 131.640 1.00 50.82  ? 8    VAL A CA    1 
ATOM   39   C  C     . VAL A 1 7   ? 131.915 144.801 133.161 1.00 50.82  ? 8    VAL A C     1 
ATOM   40   O  O     . VAL A 1 7   ? 132.011 143.819 133.907 1.00 50.82  ? 8    VAL A O     1 
ATOM   41   C  CB    . VAL A 1 7   ? 133.462 144.610 131.114 1.00 50.82  ? 8    VAL A CB    1 
ATOM   42   C  CG1   . VAL A 1 7   ? 134.221 145.872 131.493 1.00 50.82  ? 8    VAL A CG1   1 
ATOM   43   C  CG2   . VAL A 1 7   ? 134.208 143.352 131.546 1.00 50.82  ? 8    VAL A CG2   1 
ATOM   44   N  N     . PHE A 1 8   ? 131.699 146.021 133.652 1.00 45.89  ? 9    PHE A N     1 
ATOM   45   C  CA    . PHE A 1 8   ? 131.654 146.254 135.092 1.00 45.89  ? 9    PHE A CA    1 
ATOM   46   C  C     . PHE A 1 8   ? 130.256 146.142 135.688 1.00 45.89  ? 9    PHE A C     1 
ATOM   47   O  O     . PHE A 1 8   ? 130.122 146.250 136.910 1.00 45.89  ? 9    PHE A O     1 
ATOM   48   C  CB    . PHE A 1 8   ? 132.273 147.613 135.440 1.00 45.89  ? 9    PHE A CB    1 
ATOM   49   C  CG    . PHE A 1 8   ? 133.708 147.750 135.006 1.00 45.89  ? 9    PHE A CG    1 
ATOM   50   C  CD1   . PHE A 1 8   ? 134.675 146.897 135.509 1.00 45.89  ? 9    PHE A CD1   1 
ATOM   51   C  CD2   . PHE A 1 8   ? 134.095 148.742 134.125 1.00 45.89  ? 9    PHE A CD2   1 
ATOM   52   C  CE1   . PHE A 1 8   ? 135.993 147.009 135.118 1.00 45.89  ? 9    PHE A CE1   1 
ATOM   53   C  CE2   . PHE A 1 8   ? 135.416 148.869 133.740 1.00 45.89  ? 9    PHE A CE2   1 
ATOM   54   C  CZ    . PHE A 1 8   ? 136.364 147.999 134.236 1.00 45.89  ? 9    PHE A CZ    1 
ATOM   55   N  N     . GLY A 1 9   ? 129.235 145.896 134.866 1.00 42.76  ? 10   GLY A N     1 
ATOM   56   C  CA    . GLY A 1 9   ? 127.884 145.602 135.332 1.00 42.76  ? 10   GLY A CA    1 
ATOM   57   C  C     . GLY A 1 9   ? 127.245 146.705 136.154 1.00 42.76  ? 10   GLY A C     1 
ATOM   58   O  O     . GLY A 1 9   ? 127.302 147.887 135.806 1.00 42.76  ? 10   GLY A O     1 
ATOM   59   N  N     . ALA A 1 10  ? 126.587 146.306 137.248 1.00 40.07  ? 11   ALA A N     1 
ATOM   60   C  CA    . ALA A 1 10  ? 125.850 147.237 138.102 1.00 40.07  ? 11   ALA A CA    1 
ATOM   61   C  C     . ALA A 1 10  ? 126.746 148.216 138.854 1.00 40.07  ? 11   ALA A C     1 
ATOM   62   O  O     . ALA A 1 10  ? 126.246 149.222 139.366 1.00 40.07  ? 11   ALA A O     1 
ATOM   63   C  CB    . ALA A 1 10  ? 124.994 146.462 139.102 1.00 40.07  ? 11   ALA A CB    1 
ATOM   64   N  N     . ALA A 1 11  ? 128.045 147.940 138.945 1.00 39.35  ? 12   ALA A N     1 
ATOM   65   C  CA    . ALA A 1 11  ? 129.003 148.847 139.562 1.00 39.35  ? 12   ALA A CA    1 
ATOM   66   C  C     . ALA A 1 11  ? 129.423 150.004 138.662 1.00 39.35  ? 12   ALA A C     1 
ATOM   67   O  O     . ALA A 1 11  ? 130.095 150.916 139.153 1.00 39.35  ? 12   ALA A O     1 
ATOM   68   C  CB    . ALA A 1 11  ? 130.244 148.066 139.995 1.00 39.35  ? 12   ALA A CB    1 
ATOM   69   N  N     . ALA A 1 12  ? 129.101 149.946 137.367 1.00 40.21  ? 13   ALA A N     1 
ATOM   70   C  CA    . ALA A 1 12  ? 129.528 150.959 136.399 1.00 40.21  ? 13   ALA A CA    1 
ATOM   71   C  C     . ALA A 1 12  ? 129.204 152.419 136.744 1.00 40.21  ? 13   ALA A C     1 
ATOM   72   O  O     . ALA A 1 12  ? 130.078 153.265 136.495 1.00 40.21  ? 13   ALA A O     1 
ATOM   73   C  CB    . ALA A 1 12  ? 128.988 150.602 135.006 1.00 40.21  ? 13   ALA A CB    1 
ATOM   74   N  N     . PRO A 1 13  ? 128.014 152.808 137.247 1.00 36.89  ? 14   PRO A N     1 
ATOM   75   C  CA    . PRO A 1 13  ? 127.830 154.220 137.659 1.00 36.89  ? 14   PRO A CA    1 
ATOM   76   C  C     . PRO A 1 13  ? 128.754 154.701 138.781 1.00 36.89  ? 14   PRO A C     1 
ATOM   77   O  O     . PRO A 1 13  ? 128.822 155.914 139.015 1.00 36.89  ? 14   PRO A O     1 
ATOM   78   C  CB    . PRO A 1 13  ? 126.362 154.277 138.098 1.00 36.89  ? 14   PRO A CB    1 
ATOM   79   C  CG    . PRO A 1 13  ? 125.718 153.199 137.376 1.00 36.89  ? 14   PRO A CG    1 
ATOM   80   C  CD    . PRO A 1 13  ? 126.718 152.099 137.334 1.00 36.89  ? 14   PRO A CD    1 
ATOM   81   N  N     . TYR A 1 14  ? 129.445 153.804 139.483 1.00 34.42  ? 15   TYR A N     1 
ATOM   82   C  CA    . TYR A 1 14  ? 130.383 154.174 140.532 1.00 34.42  ? 15   TYR A CA    1 
ATOM   83   C  C     . TYR A 1 14  ? 131.826 153.922 140.124 1.00 34.42  ? 15   TYR A C     1 
ATOM   84   O  O     . TYR A 1 14  ? 132.715 153.948 140.980 1.00 34.42  ? 15   TYR A O     1 
ATOM   85   C  CB    . TYR A 1 14  ? 130.069 153.426 141.827 1.00 34.42  ? 15   TYR A CB    1 
ATOM   86   C  CG    . TYR A 1 14  ? 128.643 153.557 142.298 1.00 34.42  ? 15   TYR A CG    1 
ATOM   87   C  CD1   . TYR A 1 14  ? 127.952 154.754 142.162 1.00 34.42  ? 15   TYR A CD1   1 
ATOM   88   C  CD2   . TYR A 1 14  ? 127.987 152.484 142.876 1.00 34.42  ? 15   TYR A CD2   1 
ATOM   89   C  CE1   . TYR A 1 14  ? 126.656 154.877 142.590 1.00 34.42  ? 15   TYR A CE1   1 
ATOM   90   C  CE2   . TYR A 1 14  ? 126.688 152.597 143.302 1.00 34.42  ? 15   TYR A CE2   1 
ATOM   91   C  CZ    . TYR A 1 14  ? 126.028 153.798 143.158 1.00 34.42  ? 15   TYR A CZ    1 
ATOM   92   O  OH    . TYR A 1 14  ? 124.726 153.921 143.577 1.00 34.42  ? 15   TYR A OH    1 
ATOM   93   N  N     . LEU A 1 15  ? 132.078 153.656 138.846 1.00 36.55  ? 16   LEU A N     1 
ATOM   94   C  CA    . LEU A 1 15  ? 133.432 153.515 138.333 1.00 36.55  ? 16   LEU A CA    1 
ATOM   95   C  C     . LEU A 1 15  ? 133.773 154.486 137.217 1.00 36.55  ? 16   LEU A C     1 
ATOM   96   O  O     . LEU A 1 15  ? 134.919 154.920 137.147 1.00 36.55  ? 16   LEU A O     1 
ATOM   97   C  CB    . LEU A 1 15  ? 133.689 152.083 137.842 1.00 36.55  ? 16   LEU A CB    1 
ATOM   98   C  CG    . LEU A 1 15  ? 133.813 151.029 138.935 1.00 36.55  ? 16   LEU A CG    1 
ATOM   99   C  CD1   . LEU A 1 15  ? 133.810 149.634 138.361 1.00 36.55  ? 16   LEU A CD1   1 
ATOM   100  C  CD2   . LEU A 1 15  ? 135.114 151.287 139.642 1.00 36.55  ? 16   LEU A CD2   1 
ATOM   101  N  N     . ARG A 1 16  ? 132.814 154.879 136.380 1.00 41.74  ? 17   ARG A N     1 
ATOM   102  C  CA    . ARG A 1 16  ? 132.991 156.038 135.518 1.00 41.74  ? 17   ARG A CA    1 
ATOM   103  C  C     . ARG A 1 16  ? 131.689 156.821 135.459 1.00 41.74  ? 17   ARG A C     1 
ATOM   104  O  O     . ARG A 1 16  ? 130.602 156.260 135.611 1.00 41.74  ? 17   ARG A O     1 
ATOM   105  C  CB    . ARG A 1 16  ? 133.387 155.640 134.088 1.00 41.74  ? 17   ARG A CB    1 
ATOM   106  C  CG    . ARG A 1 16  ? 134.819 155.172 133.915 1.00 41.74  ? 17   ARG A CG    1 
ATOM   107  C  CD    . ARG A 1 16  ? 135.224 155.123 132.458 1.00 41.74  ? 17   ARG A CD    1 
ATOM   108  N  NE    . ARG A 1 16  ? 136.669 155.012 132.301 1.00 41.74  ? 17   ARG A NE    1 
ATOM   109  C  CZ    . ARG A 1 16  ? 137.267 153.994 131.692 1.00 41.74  ? 17   ARG A CZ    1 
ATOM   110  N  NH1   . ARG A 1 16  ? 138.588 153.938 131.624 1.00 41.74  ? 17   ARG A NH1   1 
ATOM   111  N  NH2   . ARG A 1 16  ? 136.542 153.013 131.178 1.00 41.74  ? 17   ARG A NH2   1 
ATOM   112  N  N     . LYS A 1 17  ? 131.816 158.131 135.257 1.00 55.91  ? 18   LYS A N     1 
ATOM   113  C  CA    . LYS A 1 17  ? 130.692 158.953 134.831 1.00 55.91  ? 18   LYS A CA    1 
ATOM   114  C  C     . LYS A 1 17  ? 130.130 158.460 133.504 1.00 55.91  ? 18   LYS A C     1 
ATOM   115  O  O     . LYS A 1 17  ? 130.849 157.904 132.669 1.00 55.91  ? 18   LYS A O     1 
ATOM   116  C  CB    . LYS A 1 17  ? 131.089 160.427 134.727 1.00 55.91  ? 18   LYS A CB    1 
ATOM   117  C  CG    . LYS A 1 17  ? 132.412 160.726 134.062 1.00 55.91  ? 18   LYS A CG    1 
ATOM   118  C  CD    . LYS A 1 17  ? 132.524 162.227 133.866 1.00 55.91  ? 18   LYS A CD    1 
ATOM   119  C  CE    . LYS A 1 17  ? 133.789 162.627 133.145 1.00 55.91  ? 18   LYS A CE    1 
ATOM   120  N  NZ    . LYS A 1 17  ? 133.866 164.108 133.037 1.00 55.91  ? 18   LYS A NZ    1 
ATOM   121  N  N     . SER A 1 18  ? 128.822 158.644 133.335 1.00 65.50  ? 19   SER A N     1 
ATOM   122  C  CA    . SER A 1 18  ? 128.071 158.079 132.223 1.00 65.50  ? 19   SER A CA    1 
ATOM   123  C  C     . SER A 1 18  ? 128.530 158.675 130.894 1.00 65.50  ? 19   SER A C     1 
ATOM   124  O  O     . SER A 1 18  ? 129.112 159.763 130.837 1.00 65.50  ? 19   SER A O     1 
ATOM   125  C  CB    . SER A 1 18  ? 126.575 158.325 132.406 1.00 65.50  ? 19   SER A CB    1 
ATOM   126  O  OG    . SER A 1 18  ? 126.271 159.701 132.260 1.00 65.50  ? 19   SER A OG    1 
ATOM   127  N  N     . GLU A 1 19  ? 128.269 157.927 129.814 1.00 69.23  ? 20   GLU A N     1 
ATOM   128  C  CA    . GLU A 1 19  ? 128.548 158.375 128.449 1.00 69.23  ? 20   GLU A CA    1 
ATOM   129  C  C     . GLU A 1 19  ? 127.839 159.671 128.067 1.00 69.23  ? 20   GLU A C     1 
ATOM   130  O  O     . GLU A 1 19  ? 128.280 160.344 127.129 1.00 69.23  ? 20   GLU A O     1 
ATOM   131  C  CB    . GLU A 1 19  ? 128.167 157.276 127.453 1.00 69.23  ? 20   GLU A CB    1 
ATOM   132  C  CG    . GLU A 1 19  ? 129.149 156.099 127.345 1.00 69.23  ? 20   GLU A CG    1 
ATOM   133  C  CD    . GLU A 1 19  ? 130.459 156.446 126.642 1.00 69.23  ? 20   GLU A CD    1 
ATOM   134  O  OE1   . GLU A 1 19  ? 131.305 157.154 127.225 1.00 69.23  ? 20   GLU A OE1   1 
ATOM   135  O  OE2   . GLU A 1 19  ? 130.644 155.998 125.490 1.00 69.23  ? 20   GLU A OE2   1 
ATOM   136  N  N     . LYS A 1 20  ? 126.762 160.038 128.761 1.00 71.81  ? 21   LYS A N     1 
ATOM   137  C  CA    . LYS A 1 20  ? 126.216 161.382 128.620 1.00 71.81  ? 21   LYS A CA    1 
ATOM   138  C  C     . LYS A 1 20  ? 127.163 162.421 129.208 1.00 71.81  ? 21   LYS A C     1 
ATOM   139  O  O     . LYS A 1 20  ? 127.570 163.364 128.519 1.00 71.81  ? 21   LYS A O     1 
ATOM   140  C  CB    . LYS A 1 20  ? 124.848 161.466 129.298 1.00 71.81  ? 21   LYS A CB    1 
ATOM   141  C  CG    . LYS A 1 20  ? 124.175 162.817 129.152 1.00 71.81  ? 21   LYS A CG    1 
ATOM   142  C  CD    . LYS A 1 20  ? 122.841 162.847 129.874 1.00 71.81  ? 21   LYS A CD    1 
ATOM   143  C  CE    . LYS A 1 20  ? 122.208 164.226 129.806 1.00 71.81  ? 21   LYS A CE    1 
ATOM   144  N  NZ    . LYS A 1 20  ? 120.922 164.282 130.553 1.00 71.81  ? 21   LYS A NZ    1 
ATOM   145  N  N     . GLU A 1 21  ? 127.489 162.279 130.500 1.00 72.11  ? 22   GLU A N     1 
ATOM   146  C  CA    . GLU A 1 21  ? 128.277 163.281 131.215 1.00 72.11  ? 22   GLU A CA    1 
ATOM   147  C  C     . GLU A 1 21  ? 129.684 163.444 130.650 1.00 72.11  ? 22   GLU A C     1 
ATOM   148  O  O     . GLU A 1 21  ? 130.226 164.552 130.681 1.00 72.11  ? 22   GLU A O     1 
ATOM   149  C  CB    . GLU A 1 21  ? 128.342 162.927 132.700 1.00 72.11  ? 22   GLU A CB    1 
ATOM   150  C  CG    . GLU A 1 21  ? 127.053 163.197 133.462 1.00 72.11  ? 22   GLU A CG    1 
ATOM   151  C  CD    . GLU A 1 21  ? 127.017 164.574 134.100 1.00 72.11  ? 22   GLU A CD    1 
ATOM   152  O  OE1   . GLU A 1 21  ? 126.192 164.782 135.015 1.00 72.11  ? 22   GLU A OE1   1 
ATOM   153  O  OE2   . GLU A 1 21  ? 127.818 165.444 133.700 1.00 72.11  ? 22   GLU A OE2   1 
ATOM   154  N  N     . ARG A 1 22  ? 130.301 162.352 130.172 1.00 70.78  ? 23   ARG A N     1 
ATOM   155  C  CA    . ARG A 1 22  ? 131.620 162.413 129.533 1.00 70.78  ? 23   ARG A CA    1 
ATOM   156  C  C     . ARG A 1 22  ? 131.646 163.349 128.328 1.00 70.78  ? 23   ARG A C     1 
ATOM   157  O  O     . ARG A 1 22  ? 132.695 163.922 128.008 1.00 70.78  ? 23   ARG A O     1 
ATOM   158  C  CB    . ARG A 1 22  ? 132.080 161.010 129.137 1.00 70.78  ? 23   ARG A CB    1 
ATOM   159  C  CG    . ARG A 1 22  ? 132.533 160.193 130.335 1.00 70.78  ? 23   ARG A CG    1 
ATOM   160  C  CD    . ARG A 1 22  ? 132.694 158.713 130.032 1.00 70.78  ? 23   ARG A CD    1 
ATOM   161  N  NE    . ARG A 1 22  ? 133.787 158.450 129.106 1.00 70.78  ? 23   ARG A NE    1 
ATOM   162  C  CZ    . ARG A 1 22  ? 134.079 157.247 128.627 1.00 70.78  ? 23   ARG A CZ    1 
ATOM   163  N  NH1   . ARG A 1 22  ? 135.104 157.089 127.801 1.00 70.78  ? 23   ARG A NH1   1 
ATOM   164  N  NH2   . ARG A 1 22  ? 133.349 156.199 128.981 1.00 70.78  ? 23   ARG A NH2   1 
ATOM   165  N  N     . LEU A 1 23  ? 130.511 163.511 127.651 1.00 75.12  ? 24   LEU A N     1 
ATOM   166  C  CA    . LEU A 1 23  ? 130.340 164.467 126.567 1.00 75.12  ? 24   LEU A CA    1 
ATOM   167  C  C     . LEU A 1 23  ? 129.795 165.794 127.080 1.00 75.12  ? 24   LEU A C     1 
ATOM   168  O  O     . LEU A 1 23  ? 130.252 166.857 126.646 1.00 75.12  ? 24   LEU A O     1 
ATOM   169  C  CB    . LEU A 1 23  ? 129.418 163.893 125.489 1.00 75.12  ? 24   LEU A CB    1 
ATOM   170  C  CG    . LEU A 1 23  ? 130.049 162.908 124.503 1.00 75.12  ? 24   LEU A CG    1 
ATOM   171  C  CD1   . LEU A 1 23  ? 129.110 162.664 123.339 1.00 75.12  ? 24   LEU A CD1   1 
ATOM   172  C  CD2   . LEU A 1 23  ? 131.391 163.422 124.003 1.00 75.12  ? 24   LEU A CD2   1 
ATOM   173  N  N     . GLU A 1 24  ? 128.786 165.738 127.959 1.00 77.34  ? 25   GLU A N     1 
ATOM   174  C  CA    . GLU A 1 24  ? 128.105 166.941 128.434 1.00 77.34  ? 25   GLU A CA    1 
ATOM   175  C  C     . GLU A 1 24  ? 129.050 167.854 129.214 1.00 77.34  ? 25   GLU A C     1 
ATOM   176  O  O     . GLU A 1 24  ? 128.870 169.077 129.202 1.00 77.34  ? 25   GLU A O     1 
ATOM   177  C  CB    . GLU A 1 24  ? 126.880 166.528 129.268 1.00 77.34  ? 25   GLU A CB    1 
ATOM   178  C  CG    . GLU A 1 24  ? 125.902 167.633 129.731 1.00 77.34  ? 25   GLU A CG    1 
ATOM   179  C  CD    . GLU A 1 24  ? 126.354 168.421 130.950 1.00 77.34  ? 25   GLU A CD    1 
ATOM   180  O  OE1   . GLU A 1 24  ? 127.183 167.899 131.724 1.00 77.34  ? 25   GLU A OE1   1 
ATOM   181  O  OE2   . GLU A 1 24  ? 125.881 169.563 131.130 1.00 77.34  ? 25   GLU A OE2   1 
ATOM   182  N  N     . ALA A 1 25  ? 130.039 167.281 129.916 1.00 74.05  ? 26   ALA A N     1 
ATOM   183  C  CA    . ALA A 1 25  ? 130.994 168.089 130.677 1.00 74.05  ? 26   ALA A CA    1 
ATOM   184  C  C     . ALA A 1 25  ? 131.846 168.986 129.786 1.00 74.05  ? 26   ALA A C     1 
ATOM   185  O  O     . ALA A 1 25  ? 132.314 170.036 130.236 1.00 74.05  ? 26   ALA A O     1 
ATOM   186  C  CB    . ALA A 1 25  ? 131.905 167.191 131.511 1.00 74.05  ? 26   ALA A CB    1 
ATOM   187  N  N     . GLN A 1 26  ? 132.073 168.590 128.531 1.00 78.37  ? 27   GLN A N     1 
ATOM   188  C  CA    . GLN A 1 26  ? 132.791 169.442 127.588 1.00 78.37  ? 27   GLN A CA    1 
ATOM   189  C  C     . GLN A 1 26  ? 131.969 170.639 127.118 1.00 78.37  ? 27   GLN A C     1 
ATOM   190  O  O     . GLN A 1 26  ? 132.516 171.516 126.441 1.00 78.37  ? 27   GLN A O     1 
ATOM   191  C  CB    . GLN A 1 26  ? 133.258 168.628 126.380 1.00 78.37  ? 27   GLN A CB    1 
ATOM   192  C  CG    . GLN A 1 26  ? 133.992 167.339 126.735 1.00 78.37  ? 27   GLN A CG    1 
ATOM   193  C  CD    . GLN A 1 26  ? 134.520 166.612 125.511 1.00 78.37  ? 27   GLN A CD    1 
ATOM   194  O  OE1   . GLN A 1 26  ? 133.781 165.920 124.811 1.00 78.37  ? 27   GLN A OE1   1 
ATOM   195  N  NE2   . GLN A 1 26  ? 135.816 166.756 125.260 1.00 78.37  ? 27   GLN A NE2   1 
ATOM   196  N  N     . THR A 1 27  ? 130.678 170.682 127.431 1.00 79.00  ? 28   THR A N     1 
ATOM   197  C  CA    . THR A 1 27  ? 129.800 171.785 127.070 1.00 79.00  ? 28   THR A CA    1 
ATOM   198  C  C     . THR A 1 27  ? 129.709 172.868 128.140 1.00 79.00  ? 28   THR A C     1 
ATOM   199  O  O     . THR A 1 27  ? 129.003 173.857 127.916 1.00 79.00  ? 28   THR A O     1 
ATOM   200  C  CB    . THR A 1 27  ? 128.394 171.260 126.764 1.00 79.00  ? 28   THR A CB    1 
ATOM   201  O  OG1   . THR A 1 27  ? 127.751 170.891 127.990 1.00 79.00  ? 28   THR A OG1   1 
ATOM   202  C  CG2   . THR A 1 27  ? 128.464 170.046 125.848 1.00 79.00  ? 28   THR A CG2   1 
ATOM   203  N  N     . ARG A 1 28  ? 130.345 172.667 129.300 1.00 71.89  ? 29   ARG A N     1 
ATOM   204  C  CA    . ARG A 1 28  ? 130.195 173.553 130.455 1.00 71.89  ? 29   ARG A CA    1 
ATOM   205  C  C     . ARG A 1 28  ? 130.600 174.995 130.140 1.00 71.89  ? 29   ARG A C     1 
ATOM   206  O  O     . ARG A 1 28  ? 131.548 175.223 129.379 1.00 71.89  ? 29   ARG A O     1 
ATOM   207  C  CB    . ARG A 1 28  ? 131.042 173.037 131.621 1.00 71.89  ? 29   ARG A CB    1 
ATOM   208  C  CG    . ARG A 1 28  ? 130.505 171.797 132.303 1.00 71.89  ? 29   ARG A CG    1 
ATOM   209  C  CD    . ARG A 1 28  ? 131.424 171.366 133.435 1.00 71.89  ? 29   ARG A CD    1 
ATOM   210  N  NE    . ARG A 1 28  ? 131.413 172.312 134.543 1.00 71.89  ? 29   ARG A NE    1 
ATOM   211  C  CZ    . ARG A 1 28  ? 130.551 172.263 135.552 1.00 71.89  ? 29   ARG A CZ    1 
ATOM   212  N  NH1   . ARG A 1 28  ? 130.597 173.176 136.512 1.00 71.89  ? 29   ARG A NH1   1 
ATOM   213  N  NH2   . ARG A 1 28  ? 129.631 171.308 135.594 1.00 71.89  ? 29   ARG A NH2   1 
ATOM   214  N  N     . PRO A 1 29  ? 129.902 175.985 130.702 1.00 74.45  ? 30   PRO A N     1 
ATOM   215  C  CA    . PRO A 1 29  ? 130.335 177.385 130.567 1.00 74.45  ? 30   PRO A CA    1 
ATOM   216  C  C     . PRO A 1 29  ? 131.608 177.657 131.357 1.00 74.45  ? 30   PRO A C     1 
ATOM   217  O  O     . PRO A 1 29  ? 131.708 177.317 132.538 1.00 74.45  ? 30   PRO A O     1 
ATOM   218  C  CB    . PRO A 1 29  ? 129.141 178.179 131.109 1.00 74.45  ? 30   PRO A CB    1 
ATOM   219  C  CG    . PRO A 1 29  ? 128.479 177.253 132.068 1.00 74.45  ? 30   PRO A CG    1 
ATOM   220  C  CD    . PRO A 1 29  ? 128.680 175.862 131.520 1.00 74.45  ? 30   PRO A CD    1 
ATOM   221  N  N     . PHE A 1 30  ? 132.588 178.270 130.695 1.00 69.59  ? 31   PHE A N     1 
ATOM   222  C  CA    . PHE A 1 30  ? 133.913 178.402 131.286 1.00 69.59  ? 31   PHE A CA    1 
ATOM   223  C  C     . PHE A 1 30  ? 134.674 179.543 130.629 1.00 69.59  ? 31   PHE A C     1 
ATOM   224  O  O     . PHE A 1 30  ? 134.807 179.580 129.402 1.00 69.59  ? 31   PHE A O     1 
ATOM   225  C  CB    . PHE A 1 30  ? 134.687 177.090 131.147 1.00 69.59  ? 31   PHE A CB    1 
ATOM   226  C  CG    . PHE A 1 30  ? 136.108 177.169 131.607 1.00 69.59  ? 31   PHE A CG    1 
ATOM   227  C  CD1   . PHE A 1 30  ? 136.412 177.112 132.955 1.00 69.59  ? 31   PHE A CD1   1 
ATOM   228  C  CD2   . PHE A 1 30  ? 137.145 177.238 130.689 1.00 69.59  ? 31   PHE A CD2   1 
ATOM   229  C  CE1   . PHE A 1 30  ? 137.719 177.162 133.381 1.00 69.59  ? 31   PHE A CE1   1 
ATOM   230  C  CE2   . PHE A 1 30  ? 138.454 177.289 131.109 1.00 69.59  ? 31   PHE A CE2   1 
ATOM   231  C  CZ    . PHE A 1 30  ? 138.741 177.250 132.457 1.00 69.59  ? 31   PHE A CZ    1 
ATOM   232  N  N     . ASP A 1 31  ? 135.167 180.468 131.450 1.00 70.21  ? 32   ASP A N     1 
ATOM   233  C  CA    . ASP A 1 31  ? 136.051 181.545 131.015 1.00 70.21  ? 32   ASP A CA    1 
ATOM   234  C  C     . ASP A 1 31  ? 137.367 181.313 131.749 1.00 70.21  ? 32   ASP A C     1 
ATOM   235  O  O     . ASP A 1 31  ? 137.423 181.437 132.977 1.00 70.21  ? 32   ASP A O     1 
ATOM   236  C  CB    . ASP A 1 31  ? 135.430 182.911 131.333 1.00 70.21  ? 32   ASP A CB    1 
ATOM   237  C  CG    . ASP A 1 31  ? 136.204 184.094 130.740 1.00 70.21  ? 32   ASP A CG    1 
ATOM   238  O  OD1   . ASP A 1 31  ? 137.443 184.178 130.854 1.00 70.21  ? 32   ASP A OD1   1 
ATOM   239  O  OD2   . ASP A 1 31  ? 135.542 184.968 130.140 1.00 70.21  ? 32   ASP A OD2   1 
ATOM   240  N  N     . LEU A 1 32  ? 138.414 180.960 130.993 1.00 69.30  ? 33   LEU A N     1 
ATOM   241  C  CA    . LEU A 1 32  ? 139.729 180.680 131.572 1.00 69.30  ? 33   LEU A CA    1 
ATOM   242  C  C     . LEU A 1 32  ? 140.341 181.896 132.262 1.00 69.30  ? 33   LEU A C     1 
ATOM   243  O  O     . LEU A 1 32  ? 141.079 181.747 133.243 1.00 69.30  ? 33   LEU A O     1 
ATOM   244  C  CB    . LEU A 1 32  ? 140.664 180.151 130.483 1.00 69.30  ? 33   LEU A CB    1 
ATOM   245  C  CG    . LEU A 1 32  ? 142.086 179.741 130.867 1.00 69.30  ? 33   LEU A CG    1 
ATOM   246  C  CD1   . LEU A 1 32  ? 142.051 178.614 131.875 1.00 69.30  ? 33   LEU A CD1   1 
ATOM   247  C  CD2   . LEU A 1 32  ? 142.874 179.330 129.639 1.00 69.30  ? 33   LEU A CD2   1 
ATOM   248  N  N     . LYS A 1 33  ? 140.025 183.102 131.793 1.00 70.26  ? 34   LYS A N     1 
ATOM   249  C  CA    . LYS A 1 33  ? 140.513 184.312 132.448 1.00 70.26  ? 34   LYS A CA    1 
ATOM   250  C  C     . LYS A 1 33  ? 139.840 184.569 133.791 1.00 70.26  ? 34   LYS A C     1 
ATOM   251  O  O     . LYS A 1 33  ? 140.366 185.352 134.587 1.00 70.26  ? 34   LYS A O     1 
ATOM   252  C  CB    . LYS A 1 33  ? 140.343 185.550 131.550 1.00 70.26  ? 34   LYS A CB    1 
ATOM   253  C  CG    . LYS A 1 33  ? 140.462 185.386 130.015 1.00 70.26  ? 34   LYS A CG    1 
ATOM   254  C  CD    . LYS A 1 33  ? 141.727 184.653 129.537 1.00 70.26  ? 34   LYS A CD    1 
ATOM   255  C  CE    . LYS A 1 33  ? 141.766 184.557 128.024 1.00 70.26  ? 34   LYS A CE    1 
ATOM   256  N  NZ    . LYS A 1 33  ? 140.647 183.726 127.505 1.00 70.26  ? 34   LYS A NZ    1 
ATOM   257  N  N     . LYS A 1 34  ? 138.696 183.946 134.061 1.00 69.99  ? 35   LYS A N     1 
ATOM   258  C  CA    . LYS A 1 34  ? 137.905 184.262 135.245 1.00 69.99  ? 35   LYS A CA    1 
ATOM   259  C  C     . LYS A 1 34  ? 137.829 183.142 136.270 1.00 69.99  ? 35   LYS A C     1 
ATOM   260  O  O     . LYS A 1 34  ? 137.870 183.419 137.471 1.00 69.99  ? 35   LYS A O     1 
ATOM   261  C  CB    . LYS A 1 34  ? 136.485 184.661 134.833 1.00 69.99  ? 35   LYS A CB    1 
ATOM   262  C  CG    . LYS A 1 34  ? 136.433 185.874 133.921 1.00 69.99  ? 35   LYS A CG    1 
ATOM   263  C  CD    . LYS A 1 34  ? 135.004 186.333 133.690 1.00 69.99  ? 35   LYS A CD    1 
ATOM   264  C  CE    . LYS A 1 34  ? 134.958 187.561 132.797 1.00 69.99  ? 35   LYS A CE    1 
ATOM   265  N  NZ    . LYS A 1 34  ? 135.331 187.237 131.393 1.00 69.99  ? 35   LYS A NZ    1 
ATOM   266  N  N     . ASP A 1 35  ? 137.718 181.885 135.841 1.00 65.75  ? 36   ASP A N     1 
ATOM   267  C  CA    . ASP A 1 35  ? 137.529 180.776 136.776 1.00 65.75  ? 36   ASP A CA    1 
ATOM   268  C  C     . ASP A 1 35  ? 138.821 180.483 137.532 1.00 65.75  ? 36   ASP A C     1 
ATOM   269  O  O     . ASP A 1 35  ? 139.812 180.035 136.948 1.00 65.75  ? 36   ASP A O     1 
ATOM   270  C  CB    . ASP A 1 35  ? 137.041 179.540 136.028 1.00 65.75  ? 36   ASP A CB    1 
ATOM   271  C  CG    . ASP A 1 35  ? 135.536 179.526 135.853 1.00 65.75  ? 36   ASP A CG    1 
ATOM   272  O  OD1   . ASP A 1 35  ? 134.901 180.579 136.070 1.00 65.75  ? 36   ASP A OD1   1 
ATOM   273  O  OD2   . ASP A 1 35  ? 134.985 178.459 135.509 1.00 65.75  ? 36   ASP A OD2   1 
ATOM   274  N  N     . VAL A 1 36  ? 138.797 180.744 138.842 1.00 57.45  ? 37   VAL A N     1 
ATOM   275  C  CA    . VAL A 1 36  ? 139.949 180.659 139.733 1.00 57.45  ? 37   VAL A CA    1 
ATOM   276  C  C     . VAL A 1 36  ? 139.486 180.085 141.064 1.00 57.45  ? 37   VAL A C     1 
ATOM   277  O  O     . VAL A 1 36  ? 138.294 180.060 141.375 1.00 57.45  ? 37   VAL A O     1 
ATOM   278  C  CB    . VAL A 1 36  ? 140.629 182.025 139.978 1.00 57.45  ? 37   VAL A CB    1 
ATOM   279  C  CG1   . VAL A 1 36  ? 141.197 182.622 138.706 1.00 57.45  ? 37   VAL A CG1   1 
ATOM   280  C  CG2   . VAL A 1 36  ? 139.618 182.989 140.567 1.00 57.45  ? 37   VAL A CG2   1 
ATOM   281  N  N     . PHE A 1 37  ? 140.445 179.607 141.850 1.00 47.65  ? 38   PHE A N     1 
ATOM   282  C  CA    . PHE A 1 37  ? 140.232 179.349 143.268 1.00 47.65  ? 38   PHE A CA    1 
ATOM   283  C  C     . PHE A 1 37  ? 140.773 180.501 144.105 1.00 47.65  ? 38   PHE A C     1 
ATOM   284  O  O     . PHE A 1 37  ? 141.844 181.039 143.815 1.00 47.65  ? 38   PHE A O     1 
ATOM   285  C  CB    . PHE A 1 37  ? 140.898 178.049 143.701 1.00 47.65  ? 38   PHE A CB    1 
ATOM   286  C  CG    . PHE A 1 37  ? 140.366 176.835 143.016 1.00 47.65  ? 38   PHE A CG    1 
ATOM   287  C  CD1   . PHE A 1 37  ? 139.173 176.271 143.412 1.00 47.65  ? 38   PHE A CD1   1 
ATOM   288  C  CD2   . PHE A 1 37  ? 141.074 176.241 141.994 1.00 47.65  ? 38   PHE A CD2   1 
ATOM   289  C  CE1   . PHE A 1 37  ? 138.686 175.146 142.787 1.00 47.65  ? 38   PHE A CE1   1 
ATOM   290  C  CE2   . PHE A 1 37  ? 140.591 175.115 141.368 1.00 47.65  ? 38   PHE A CE2   1 
ATOM   291  C  CZ    . PHE A 1 37  ? 139.396 174.568 141.766 1.00 47.65  ? 38   PHE A CZ    1 
ATOM   292  N  N     . VAL A 1 38  ? 140.041 180.860 145.156 1.00 53.14  ? 39   VAL A N     1 
ATOM   293  C  CA    . VAL A 1 38  ? 140.487 181.869 146.117 1.00 53.14  ? 39   VAL A CA    1 
ATOM   294  C  C     . VAL A 1 38  ? 140.467 181.265 147.519 1.00 53.14  ? 39   VAL A C     1 
ATOM   295  O  O     . VAL A 1 38  ? 139.672 180.351 147.782 1.00 53.14  ? 39   VAL A O     1 
ATOM   296  C  CB    . VAL A 1 38  ? 139.617 183.139 146.033 1.00 53.14  ? 39   VAL A CB    1 
ATOM   297  C  CG1   . VAL A 1 38  ? 139.781 183.821 144.684 1.00 53.14  ? 39   VAL A CG1   1 
ATOM   298  C  CG2   . VAL A 1 38  ? 138.152 182.818 146.277 1.00 53.14  ? 39   VAL A CG2   1 
ATOM   299  N  N     . PRO A 1 39  ? 141.347 181.687 148.430 1.00 54.55  ? 40   PRO A N     1 
ATOM   300  C  CA    . PRO A 1 39  ? 141.324 181.126 149.785 1.00 54.55  ? 40   PRO A CA    1 
ATOM   301  C  C     . PRO A 1 39  ? 140.150 181.643 150.600 1.00 54.55  ? 40   PRO A C     1 
ATOM   302  O  O     . PRO A 1 39  ? 139.687 182.772 150.421 1.00 54.55  ? 40   PRO A O     1 
ATOM   303  C  CB    . PRO A 1 39  ? 142.655 181.591 150.378 1.00 54.55  ? 40   PRO A CB    1 
ATOM   304  C  CG    . PRO A 1 39  ? 142.925 182.863 149.676 1.00 54.55  ? 40   PRO A CG    1 
ATOM   305  C  CD    . PRO A 1 39  ? 142.444 182.658 148.271 1.00 54.55  ? 40   PRO A CD    1 
ATOM   306  N  N     . ASP A 1 40  ? 139.670 180.798 151.512 1.00 53.21  ? 41   ASP A N     1 
ATOM   307  C  CA    . ASP A 1 40  ? 138.652 181.206 152.470 1.00 53.21  ? 41   ASP A CA    1 
ATOM   308  C  C     . ASP A 1 40  ? 138.894 180.457 153.777 1.00 53.21  ? 41   ASP A C     1 
ATOM   309  O  O     . ASP A 1 40  ? 139.483 179.373 153.784 1.00 53.21  ? 41   ASP A O     1 
ATOM   310  C  CB    . ASP A 1 40  ? 137.248 180.953 151.893 1.00 53.21  ? 41   ASP A CB    1 
ATOM   311  C  CG    . ASP A 1 40  ? 136.133 181.466 152.782 1.00 53.21  ? 41   ASP A CG    1 
ATOM   312  O  OD1   . ASP A 1 40  ? 135.544 182.511 152.437 1.00 53.21  ? 41   ASP A OD1   1 
ATOM   313  O  OD2   . ASP A 1 40  ? 135.824 180.817 153.803 1.00 53.21  ? 41   ASP A OD2   1 
ATOM   314  N  N     . ASP A 1 41  ? 138.442 181.052 154.887 1.00 55.12  ? 42   ASP A N     1 
ATOM   315  C  CA    . ASP A 1 41  ? 138.803 180.564 156.217 1.00 55.12  ? 42   ASP A CA    1 
ATOM   316  C  C     . ASP A 1 41  ? 137.955 179.377 156.665 1.00 55.12  ? 42   ASP A C     1 
ATOM   317  O  O     . ASP A 1 41  ? 138.492 178.399 157.197 1.00 55.12  ? 42   ASP A O     1 
ATOM   318  C  CB    . ASP A 1 41  ? 138.702 181.699 157.235 1.00 55.12  ? 42   ASP A CB    1 
ATOM   319  C  CG    . ASP A 1 41  ? 139.699 182.808 156.968 1.00 55.12  ? 42   ASP A CG    1 
ATOM   320  O  OD1   . ASP A 1 41  ? 140.810 182.754 157.537 1.00 55.12  ? 42   ASP A OD1   1 
ATOM   321  O  OD2   . ASP A 1 41  ? 139.373 183.729 156.192 1.00 55.12  ? 42   ASP A OD2   1 
ATOM   322  N  N     . LYS A 1 42  ? 136.637 179.431 156.462 1.00 56.08  ? 43   LYS A N     1 
ATOM   323  C  CA    . LYS A 1 42  ? 135.758 178.376 156.959 1.00 56.08  ? 43   LYS A CA    1 
ATOM   324  C  C     . LYS A 1 42  ? 135.717 177.169 156.033 1.00 56.08  ? 43   LYS A C     1 
ATOM   325  O  O     . LYS A 1 42  ? 135.130 176.143 156.392 1.00 56.08  ? 43   LYS A O     1 
ATOM   326  C  CB    . LYS A 1 42  ? 134.345 178.921 157.174 1.00 56.08  ? 43   LYS A CB    1 
ATOM   327  C  CG    . LYS A 1 42  ? 134.247 179.941 158.302 1.00 56.08  ? 43   LYS A CG    1 
ATOM   328  C  CD    . LYS A 1 42  ? 132.831 180.471 158.464 1.00 56.08  ? 43   LYS A CD    1 
ATOM   329  C  CE    . LYS A 1 42  ? 132.416 181.324 157.280 1.00 56.08  ? 43   LYS A CE    1 
ATOM   330  N  NZ    . LYS A 1 42  ? 133.170 182.606 157.233 1.00 56.08  ? 43   LYS A NZ    1 
ATOM   331  N  N     . GLN A 1 43  ? 136.332 177.287 154.861 1.00 52.29  ? 44   GLN A N     1 
ATOM   332  C  CA    . GLN A 1 43  ? 136.350 176.260 153.824 1.00 52.29  ? 44   GLN A CA    1 
ATOM   333  C  C     . GLN A 1 43  ? 137.513 176.653 152.920 1.00 52.29  ? 44   GLN A C     1 
ATOM   334  O  O     . GLN A 1 43  ? 137.506 177.754 152.361 1.00 52.29  ? 44   GLN A O     1 
ATOM   335  C  CB    . GLN A 1 43  ? 134.998 176.142 153.098 1.00 52.29  ? 44   GLN A CB    1 
ATOM   336  C  CG    . GLN A 1 43  ? 134.401 177.390 152.441 1.00 52.29  ? 44   GLN A CG    1 
ATOM   337  C  CD    . GLN A 1 43  ? 132.898 177.307 152.300 1.00 52.29  ? 44   GLN A CD    1 
ATOM   338  O  OE1   . GLN A 1 43  ? 132.314 176.228 152.396 1.00 52.29  ? 44   GLN A OE1   1 
ATOM   339  N  NE2   . GLN A 1 43  ? 132.260 178.448 152.072 1.00 52.29  ? 44   GLN A NE2   1 
ATOM   340  N  N     . GLU A 1 44  ? 138.544 175.792 152.874 1.00 42.69  ? 45   GLU A N     1 
ATOM   341  C  CA    . GLU A 1 44  ? 139.917 176.204 152.556 1.00 42.69  ? 45   GLU A CA    1 
ATOM   342  C  C     . GLU A 1 44  ? 140.047 176.915 151.215 1.00 42.69  ? 45   GLU A C     1 
ATOM   343  O  O     . GLU A 1 44  ? 140.852 177.843 151.085 1.00 42.69  ? 45   GLU A O     1 
ATOM   344  C  CB    . GLU A 1 44  ? 140.842 174.993 152.593 1.00 42.69  ? 45   GLU A CB    1 
ATOM   345  C  CG    . GLU A 1 44  ? 141.077 174.455 153.985 1.00 42.69  ? 45   GLU A CG    1 
ATOM   346  C  CD    . GLU A 1 44  ? 142.238 175.132 154.683 1.00 42.69  ? 45   GLU A CD    1 
ATOM   347  O  OE1   . GLU A 1 44  ? 143.384 174.981 154.209 1.00 42.69  ? 45   GLU A OE1   1 
ATOM   348  O  OE2   . GLU A 1 44  ? 142.008 175.810 155.705 1.00 42.69  ? 45   GLU A OE2   1 
ATOM   349  N  N     . PHE A 1 45  ? 139.260 176.523 150.220 1.00 40.98  ? 46   PHE A N     1 
ATOM   350  C  CA    . PHE A 1 45  ? 139.248 177.226 148.950 1.00 40.98  ? 46   PHE A CA    1 
ATOM   351  C  C     . PHE A 1 45  ? 137.829 177.222 148.410 1.00 40.98  ? 46   PHE A C     1 
ATOM   352  O  O     . PHE A 1 45  ? 137.058 176.296 148.663 1.00 40.98  ? 46   PHE A O     1 
ATOM   353  C  CB    . PHE A 1 45  ? 140.186 176.588 147.928 1.00 40.98  ? 46   PHE A CB    1 
ATOM   354  C  CG    . PHE A 1 45  ? 141.616 176.516 148.373 1.00 40.98  ? 46   PHE A CG    1 
ATOM   355  C  CD1   . PHE A 1 45  ? 142.464 177.592 148.199 1.00 40.98  ? 46   PHE A CD1   1 
ATOM   356  C  CD2   . PHE A 1 45  ? 142.113 175.364 148.952 1.00 40.98  ? 46   PHE A CD2   1 
ATOM   357  C  CE1   . PHE A 1 45  ? 143.782 177.526 148.607 1.00 40.98  ? 46   PHE A CE1   1 
ATOM   358  C  CE2   . PHE A 1 45  ? 143.426 175.291 149.360 1.00 40.98  ? 46   PHE A CE2   1 
ATOM   359  C  CZ    . PHE A 1 45  ? 144.262 176.373 149.187 1.00 40.98  ? 46   PHE A CZ    1 
ATOM   360  N  N     . VAL A 1 46  ? 137.491 178.258 147.646 1.00 48.82  ? 47   VAL A N     1 
ATOM   361  C  CA    . VAL A 1 46  ? 136.196 178.367 146.985 1.00 48.82  ? 47   VAL A CA    1 
ATOM   362  C  C     . VAL A 1 46  ? 136.459 178.730 145.531 1.00 48.82  ? 47   VAL A C     1 
ATOM   363  O  O     . VAL A 1 46  ? 137.382 179.498 145.237 1.00 48.82  ? 47   VAL A O     1 
ATOM   364  C  CB    . VAL A 1 46  ? 135.279 179.433 147.644 1.00 48.82  ? 47   VAL A CB    1 
ATOM   365  C  CG1   . VAL A 1 46  ? 133.857 179.346 147.115 1.00 48.82  ? 47   VAL A CG1   1 
ATOM   366  C  CG2   . VAL A 1 46  ? 135.250 179.325 149.161 1.00 48.82  ? 47   VAL A CG2   1 
ATOM   367  N  N     . LYS A 1 47  ? 135.675 178.153 144.621 1.00 54.30  ? 48   LYS A N     1 
ATOM   368  C  CA    . LYS A 1 47  ? 135.687 178.592 143.234 1.00 54.30  ? 48   LYS A CA    1 
ATOM   369  C  C     . LYS A 1 47  ? 135.202 180.033 143.146 1.00 54.30  ? 48   LYS A C     1 
ATOM   370  O  O     . LYS A 1 47  ? 134.341 180.467 143.915 1.00 54.30  ? 48   LYS A O     1 
ATOM   371  C  CB    . LYS A 1 47  ? 134.804 177.689 142.376 1.00 54.30  ? 48   LYS A CB    1 
ATOM   372  C  CG    . LYS A 1 47  ? 135.314 176.275 142.228 1.00 54.30  ? 48   LYS A CG    1 
ATOM   373  C  CD    . LYS A 1 47  ? 134.376 175.439 141.380 1.00 54.30  ? 48   LYS A CD    1 
ATOM   374  C  CE    . LYS A 1 47  ? 134.858 174.003 141.287 1.00 54.30  ? 48   LYS A CE    1 
ATOM   375  N  NZ    . LYS A 1 47  ? 133.956 173.150 140.466 1.00 54.30  ? 48   LYS A NZ    1 
ATOM   376  N  N     . ALA A 1 48  ? 135.756 180.780 142.196 1.00 61.87  ? 49   ALA A N     1 
ATOM   377  C  CA    . ALA A 1 48  ? 135.387 182.179 142.067 1.00 61.87  ? 49   ALA A CA    1 
ATOM   378  C  C     . ALA A 1 48  ? 135.587 182.637 140.633 1.00 61.87  ? 49   ALA A C     1 
ATOM   379  O  O     . ALA A 1 48  ? 136.336 182.033 139.861 1.00 61.87  ? 49   ALA A O     1 
ATOM   380  C  CB    . ALA A 1 48  ? 136.198 183.064 143.019 1.00 61.87  ? 49   ALA A CB    1 
ATOM   381  N  N     . LYS A 1 49  ? 134.903 183.723 140.291 1.00 73.63  ? 50   LYS A N     1 
ATOM   382  C  CA    . LYS A 1 49  ? 135.086 184.423 139.028 1.00 73.63  ? 50   LYS A CA    1 
ATOM   383  C  C     . LYS A 1 49  ? 135.762 185.759 139.296 1.00 73.63  ? 50   LYS A C     1 
ATOM   384  O  O     . LYS A 1 49  ? 135.285 186.532 140.132 1.00 73.63  ? 50   LYS A O     1 
ATOM   385  C  CB    . LYS A 1 49  ? 133.744 184.633 138.327 1.00 73.63  ? 50   LYS A CB    1 
ATOM   386  C  CG    . LYS A 1 49  ? 133.278 183.428 137.532 1.00 73.63  ? 50   LYS A CG    1 
ATOM   387  C  CD    . LYS A 1 49  ? 131.793 183.509 137.235 1.00 73.63  ? 50   LYS A CD    1 
ATOM   388  C  CE    . LYS A 1 49  ? 131.378 182.441 136.245 1.00 73.63  ? 50   LYS A CE    1 
ATOM   389  N  NZ    . LYS A 1 49  ? 131.844 181.097 136.678 1.00 73.63  ? 50   LYS A NZ    1 
ATOM   390  N  N     . ILE A 1 50  ? 136.885 186.005 138.610 1.00 79.28  ? 51   ILE A N     1 
ATOM   391  C  CA    . ILE A 1 50  ? 137.562 187.299 138.676 1.00 79.28  ? 51   ILE A CA    1 
ATOM   392  C  C     . ILE A 1 50  ? 136.632 188.402 138.190 1.00 79.28  ? 51   ILE A C     1 
ATOM   393  O  O     . ILE A 1 50  ? 136.031 188.303 137.113 1.00 79.28  ? 51   ILE A O     1 
ATOM   394  C  CB    . ILE A 1 50  ? 138.862 187.259 137.856 1.00 79.28  ? 51   ILE A CB    1 
ATOM   395  C  CG1   . ILE A 1 50  ? 139.885 186.339 138.518 1.00 79.28  ? 51   ILE A CG1   1 
ATOM   396  C  CG2   . ILE A 1 50  ? 139.458 188.651 137.688 1.00 79.28  ? 51   ILE A CG2   1 
ATOM   397  C  CD1   . ILE A 1 50  ? 141.169 186.209 137.731 1.00 79.28  ? 51   ILE A CD1   1 
ATOM   398  N  N     . VAL A 1 51  ? 136.510 189.460 138.986 1.00 87.19  ? 52   VAL A N     1 
ATOM   399  C  CA    . VAL A 1 51  ? 135.685 190.606 138.637 1.00 87.19  ? 52   VAL A CA    1 
ATOM   400  C  C     . VAL A 1 51  ? 136.522 191.755 138.087 1.00 87.19  ? 52   VAL A C     1 
ATOM   401  O  O     . VAL A 1 51  ? 136.140 192.382 137.097 1.00 87.19  ? 52   VAL A O     1 
ATOM   402  C  CB    . VAL A 1 51  ? 134.861 191.042 139.871 1.00 87.19  ? 52   VAL A CB    1 
ATOM   403  C  CG1   . VAL A 1 51  ? 134.127 192.355 139.626 1.00 87.19  ? 52   VAL A CG1   1 
ATOM   404  C  CG2   . VAL A 1 51  ? 133.881 189.951 140.260 1.00 87.19  ? 52   VAL A CG2   1 
ATOM   405  N  N     . SER A 1 52  ? 137.705 191.988 138.654 1.00 92.62  ? 53   SER A N     1 
ATOM   406  C  CA    . SER A 1 52  ? 138.599 193.009 138.125 1.00 92.62  ? 53   SER A CA    1 
ATOM   407  C  C     . SER A 1 52  ? 140.027 192.715 138.557 1.00 92.62  ? 53   SER A C     1 
ATOM   408  O  O     . SER A 1 52  ? 140.272 191.955 139.498 1.00 92.62  ? 53   SER A O     1 
ATOM   409  C  CB    . SER A 1 52  ? 138.186 194.410 138.593 1.00 92.62  ? 53   SER A CB    1 
ATOM   410  O  OG    . SER A 1 52  ? 138.453 194.585 139.973 1.00 92.62  ? 53   SER A OG    1 
ATOM   411  N  N     . ARG A 1 53  ? 140.967 193.337 137.849 1.00 97.96  ? 54   ARG A N     1 
ATOM   412  C  CA    . ARG A 1 53  ? 142.364 193.414 138.255 1.00 97.96  ? 54   ARG A CA    1 
ATOM   413  C  C     . ARG A 1 53  ? 142.653 194.801 138.814 1.00 97.96  ? 54   ARG A C     1 
ATOM   414  O  O     . ARG A 1 53  ? 142.319 195.810 138.184 1.00 97.96  ? 54   ARG A O     1 
ATOM   415  C  CB    . ARG A 1 53  ? 143.286 193.117 137.071 1.00 97.96  ? 54   ARG A CB    1 
ATOM   416  C  CG    . ARG A 1 53  ? 143.354 191.645 136.693 1.00 97.96  ? 54   ARG A CG    1 
ATOM   417  C  CD    . ARG A 1 53  ? 143.979 190.813 137.800 1.00 97.96  ? 54   ARG A CD    1 
ATOM   418  N  NE    . ARG A 1 53  ? 145.293 191.313 138.189 1.00 97.96  ? 54   ARG A NE    1 
ATOM   419  C  CZ    . ARG A 1 53  ? 146.426 191.014 137.560 1.00 97.96  ? 54   ARG A CZ    1 
ATOM   420  N  NH1   . ARG A 1 53  ? 147.563 191.584 137.931 1.00 97.96  ? 54   ARG A NH1   1 
ATOM   421  N  NH2   . ARG A 1 53  ? 146.416 190.182 136.528 1.00 97.96  ? 54   ARG A NH2   1 
ATOM   422  N  N     . GLU A 1 54  ? 143.314 194.846 139.971 1.00 98.54  ? 55   GLU A N     1 
ATOM   423  C  CA    . GLU A 1 54  ? 143.616 196.091 140.678 1.00 98.54  ? 55   GLU A CA    1 
ATOM   424  C  C     . GLU A 1 54  ? 145.117 196.157 140.964 1.00 98.54  ? 55   GLU A C     1 
ATOM   425  O  O     . GLU A 1 54  ? 145.561 196.274 142.106 1.00 98.54  ? 55   GLU A O     1 
ATOM   426  C  CB    . GLU A 1 54  ? 142.830 196.214 141.984 1.00 98.54  ? 55   GLU A CB    1 
ATOM   427  C  CG    . GLU A 1 54  ? 141.314 196.062 141.888 1.00 98.54  ? 55   GLU A CG    1 
ATOM   428  C  CD    . GLU A 1 54  ? 140.660 197.092 140.984 1.00 98.54  ? 55   GLU A CD    1 
ATOM   429  O  OE1   . GLU A 1 54  ? 140.550 198.263 141.403 1.00 98.54  ? 55   GLU A OE1   1 
ATOM   430  O  OE2   . GLU A 1 54  ? 140.216 196.729 139.877 1.00 98.54  ? 55   GLU A OE2   1 
ATOM   431  N  N     . GLY A 1 55  ? 145.906 196.088 139.895 1.00 96.69  ? 56   GLY A N     1 
ATOM   432  C  CA    . GLY A 1 55  ? 147.346 195.955 139.994 1.00 96.69  ? 56   GLY A CA    1 
ATOM   433  C  C     . GLY A 1 55  ? 147.805 194.638 140.584 1.00 96.69  ? 56   GLY A C     1 
ATOM   434  O  O     . GLY A 1 55  ? 147.438 193.572 140.083 1.00 96.69  ? 56   GLY A O     1 
ATOM   435  N  N     . GLY A 1 56  ? 148.602 194.692 141.653 1.00 94.94  ? 57   GLY A N     1 
ATOM   436  C  CA    . GLY A 1 56  ? 148.977 193.484 142.364 1.00 94.94  ? 57   GLY A CA    1 
ATOM   437  C  C     . GLY A 1 56  ? 147.904 192.878 143.241 1.00 94.94  ? 57   GLY A C     1 
ATOM   438  O  O     . GLY A 1 56  ? 148.150 191.838 143.857 1.00 94.94  ? 57   GLY A O     1 
ATOM   439  N  N     . LYS A 1 57  ? 146.731 193.497 143.330 1.00 95.33  ? 58   LYS A N     1 
ATOM   440  C  CA    . LYS A 1 57  ? 145.572 192.909 143.979 1.00 95.33  ? 58   LYS A CA    1 
ATOM   441  C  C     . LYS A 1 57  ? 144.559 192.480 142.926 1.00 95.33  ? 58   LYS A C     1 
ATOM   442  O  O     . LYS A 1 57  ? 144.618 192.903 141.769 1.00 95.33  ? 58   LYS A O     1 
ATOM   443  C  CB    . LYS A 1 57  ? 144.924 193.897 144.957 1.00 95.33  ? 58   LYS A CB    1 
ATOM   444  C  CG    . LYS A 1 57  ? 145.846 194.416 146.054 1.00 95.33  ? 58   LYS A CG    1 
ATOM   445  C  CD    . LYS A 1 57  ? 146.393 193.286 146.912 1.00 95.33  ? 58   LYS A CD    1 
ATOM   446  C  CE    . LYS A 1 57  ? 147.815 193.573 147.371 1.00 95.33  ? 58   LYS A CE    1 
ATOM   447  N  NZ    . LYS A 1 57  ? 148.790 193.593 146.248 1.00 95.33  ? 58   LYS A NZ    1 
ATOM   448  N  N     . VAL A 1 58  ? 143.625 191.618 143.338 1.00 93.06  ? 59   VAL A N     1 
ATOM   449  C  CA    . VAL A 1 58  ? 142.572 191.097 142.470 1.00 93.06  ? 59   VAL A CA    1 
ATOM   450  C  C     . VAL A 1 58  ? 141.291 191.119 143.297 1.00 93.06  ? 59   VAL A C     1 
ATOM   451  O  O     . VAL A 1 58  ? 141.318 190.927 144.516 1.00 93.06  ? 59   VAL A O     1 
ATOM   452  C  CB    . VAL A 1 58  ? 142.859 189.647 141.942 1.00 93.06  ? 59   VAL A CB    1 
ATOM   453  C  CG1   . VAL A 1 58  ? 141.873 189.220 140.853 1.00 93.06  ? 59   VAL A CG1   1 
ATOM   454  C  CG2   . VAL A 1 58  ? 144.268 189.475 141.392 1.00 93.06  ? 59   VAL A CG2   1 
ATOM   455  N  N     . THR A 1 59  ? 140.161 191.356 142.630 1.00 91.59  ? 60   THR A N     1 
ATOM   456  C  CA    . THR A 1 59  ? 138.841 191.221 143.226 1.00 91.59  ? 60   THR A CA    1 
ATOM   457  C  C     . THR A 1 59  ? 138.064 190.149 142.475 1.00 91.59  ? 60   THR A C     1 
ATOM   458  O  O     . THR A 1 59  ? 138.249 189.959 141.269 1.00 91.59  ? 60   THR A O     1 
ATOM   459  C  CB    . THR A 1 59  ? 138.055 192.541 143.194 1.00 91.59  ? 60   THR A CB    1 
ATOM   460  O  OG1   . THR A 1 59  ? 137.530 192.758 141.877 1.00 91.59  ? 60   THR A OG1   1 
ATOM   461  C  CG2   . THR A 1 59  ? 138.937 193.715 143.592 1.00 91.59  ? 60   THR A CG2   1 
ATOM   462  N  N     . ALA A 1 60  ? 137.189 189.449 143.193 1.00 87.41  ? 61   ALA A N     1 
ATOM   463  C  CA    . ALA A 1 60  ? 136.498 188.310 142.609 1.00 87.41  ? 61   ALA A CA    1 
ATOM   464  C  C     . ALA A 1 60  ? 135.142 188.123 143.272 1.00 87.41  ? 61   ALA A C     1 
ATOM   465  O  O     . ALA A 1 60  ? 134.895 188.602 144.381 1.00 87.41  ? 61   ALA A O     1 
ATOM   466  C  CB    . ALA A 1 60  ? 137.331 187.030 142.735 1.00 87.41  ? 61   ALA A CB    1 
ATOM   467  N  N     . GLU A 1 61  ? 134.260 187.421 142.564 1.00 83.70  ? 62   GLU A N     1 
ATOM   468  C  CA    . GLU A 1 61  ? 132.986 186.953 143.096 1.00 83.70  ? 62   GLU A CA    1 
ATOM   469  C  C     . GLU A 1 61  ? 133.065 185.442 143.272 1.00 83.70  ? 62   GLU A C     1 
ATOM   470  O  O     . GLU A 1 61  ? 133.310 184.715 142.304 1.00 83.70  ? 62   GLU A O     1 
ATOM   471  C  CB    . GLU A 1 61  ? 131.838 187.364 142.168 1.00 83.70  ? 62   GLU A CB    1 
ATOM   472  C  CG    . GLU A 1 61  ? 130.442 186.920 142.587 1.00 83.70  ? 62   GLU A CG    1 
ATOM   473  C  CD    . GLU A 1 61  ? 129.985 185.651 141.893 1.00 83.70  ? 62   GLU A CD    1 
ATOM   474  O  OE1   . GLU A 1 61  ? 130.731 185.134 141.036 1.00 83.70  ? 62   GLU A OE1   1 
ATOM   475  O  OE2   . GLU A 1 61  ? 128.877 185.169 142.208 1.00 83.70  ? 62   GLU A OE2   1 
ATOM   476  N  N     . THR A 1 62  ? 132.854 184.978 144.501 1.00 79.16  ? 63   THR A N     1 
ATOM   477  C  CA    . THR A 1 62  ? 132.876 183.557 144.819 1.00 79.16  ? 63   THR A CA    1 
ATOM   478  C  C     . THR A 1 62  ? 131.635 182.837 144.308 1.00 79.16  ? 63   THR A C     1 
ATOM   479  O  O     . THR A 1 62  ? 130.622 183.447 143.961 1.00 79.16  ? 63   THR A O     1 
ATOM   480  C  CB    . THR A 1 62  ? 132.985 183.338 146.324 1.00 79.16  ? 63   THR A CB    1 
ATOM   481  O  OG1   . THR A 1 62  ? 131.854 183.926 146.978 1.00 79.16  ? 63   THR A OG1   1 
ATOM   482  C  CG2   . THR A 1 62  ? 134.253 183.953 146.848 1.00 79.16  ? 63   THR A CG2   1 
ATOM   483  N  N     . GLU A 1 63  ? 131.742 181.503 144.262 1.00 77.69  ? 64   GLU A N     1 
ATOM   484  C  CA    . GLU A 1 63  ? 130.632 180.631 143.885 1.00 77.69  ? 64   GLU A CA    1 
ATOM   485  C  C     . GLU A 1 63  ? 129.421 180.776 144.809 1.00 77.69  ? 64   GLU A C     1 
ATOM   486  O  O     . GLU A 1 63  ? 128.292 180.502 144.383 1.00 77.69  ? 64   GLU A O     1 
ATOM   487  C  CB    . GLU A 1 63  ? 131.133 179.176 143.866 1.00 77.69  ? 64   GLU A CB    1 
ATOM   488  C  CG    . GLU A 1 63  ? 130.167 178.080 143.373 1.00 77.69  ? 64   GLU A CG    1 
ATOM   489  C  CD    . GLU A 1 63  ? 129.760 178.173 141.899 1.00 77.69  ? 64   GLU A CD    1 
ATOM   490  O  OE1   . GLU A 1 63  ? 130.300 179.003 141.136 1.00 77.69  ? 64   GLU A OE1   1 
ATOM   491  O  OE2   . GLU A 1 63  ? 128.873 177.389 141.500 1.00 77.69  ? 64   GLU A OE2   1 
ATOM   492  N  N     . TYR A 1 64  ? 129.616 181.234 146.046 1.00 82.33  ? 65   TYR A N     1 
ATOM   493  C  CA    . TYR A 1 64  ? 128.511 181.562 146.935 1.00 82.33  ? 65   TYR A CA    1 
ATOM   494  C  C     . TYR A 1 64  ? 128.125 183.037 146.869 1.00 82.33  ? 65   TYR A C     1 
ATOM   495  O  O     . TYR A 1 64  ? 127.411 183.524 147.753 1.00 82.33  ? 65   TYR A O     1 
ATOM   496  C  CB    . TYR A 1 64  ? 128.842 181.148 148.369 1.00 82.33  ? 65   TYR A CB    1 
ATOM   497  C  CG    . TYR A 1 64  ? 129.128 179.671 148.502 1.00 82.33  ? 65   TYR A CG    1 
ATOM   498  C  CD1   . TYR A 1 64  ? 128.165 178.729 148.156 1.00 82.33  ? 65   TYR A CD1   1 
ATOM   499  C  CD2   . TYR A 1 64  ? 130.353 179.215 148.971 1.00 82.33  ? 65   TYR A CD2   1 
ATOM   500  C  CE1   . TYR A 1 64  ? 128.412 177.374 148.276 1.00 82.33  ? 65   TYR A CE1   1 
ATOM   501  C  CE2   . TYR A 1 64  ? 130.611 177.859 149.092 1.00 82.33  ? 65   TYR A CE2   1 
ATOM   502  C  CZ    . TYR A 1 64  ? 129.635 176.947 148.744 1.00 82.33  ? 65   TYR A CZ    1 
ATOM   503  O  OH    . TYR A 1 64  ? 129.885 175.601 148.855 1.00 82.33  ? 65   TYR A OH    1 
ATOM   504  N  N     . GLY A 1 65  ? 128.586 183.752 145.844 1.00 85.88  ? 66   GLY A N     1 
ATOM   505  C  CA    . GLY A 1 65  ? 128.230 185.135 145.609 1.00 85.88  ? 66   GLY A CA    1 
ATOM   506  C  C     . GLY A 1 65  ? 128.902 186.163 146.492 1.00 85.88  ? 66   GLY A C     1 
ATOM   507  O  O     . GLY A 1 65  ? 128.678 187.363 146.286 1.00 85.88  ? 66   GLY A O     1 
ATOM   508  N  N     . LYS A 1 66  ? 129.707 185.748 147.466 1.00 88.11  ? 67   LYS A N     1 
ATOM   509  C  CA    . LYS A 1 66  ? 130.395 186.706 148.321 1.00 88.11  ? 67   LYS A CA    1 
ATOM   510  C  C     . LYS A 1 66  ? 131.523 187.376 147.545 1.00 88.11  ? 67   LYS A C     1 
ATOM   511  O  O     . LYS A 1 66  ? 132.298 186.704 146.858 1.00 88.11  ? 67   LYS A O     1 
ATOM   512  C  CB    . LYS A 1 66  ? 130.935 186.012 149.569 1.00 88.11  ? 67   LYS A CB    1 
ATOM   513  C  CG    . LYS A 1 66  ? 129.919 185.906 150.697 1.00 88.11  ? 67   LYS A CG    1 
ATOM   514  C  CD    . LYS A 1 66  ? 130.061 184.598 151.457 1.00 88.11  ? 67   LYS A CD    1 
ATOM   515  C  CE    . LYS A 1 66  ? 131.159 184.685 152.505 1.00 88.11  ? 67   LYS A CE    1 
ATOM   516  N  NZ    . LYS A 1 66  ? 130.758 185.528 153.664 1.00 88.11  ? 67   LYS A NZ    1 
ATOM   517  N  N     . THR A 1 67  ? 131.616 188.700 147.649 1.00 91.60  ? 68   THR A N     1 
ATOM   518  C  CA    . THR A 1 67  ? 132.757 189.410 147.088 1.00 91.60  ? 68   THR A CA    1 
ATOM   519  C  C     . THR A 1 67  ? 133.998 189.219 147.955 1.00 91.60  ? 68   THR A C     1 
ATOM   520  O  O     . THR A 1 67  ? 133.925 189.184 149.187 1.00 91.60  ? 68   THR A O     1 
ATOM   521  C  CB    . THR A 1 67  ? 132.432 190.899 146.906 1.00 91.60  ? 68   THR A CB    1 
ATOM   522  O  OG1   . THR A 1 67  ? 133.574 191.586 146.379 1.00 91.60  ? 68   THR A OG1   1 
ATOM   523  C  CG2   . THR A 1 67  ? 131.967 191.558 148.208 1.00 91.60  ? 68   THR A CG2   1 
ATOM   524  N  N     . VAL A 1 68  ? 135.139 189.036 147.290 1.00 92.33  ? 69   VAL A N     1 
ATOM   525  C  CA    . VAL A 1 68  ? 136.424 188.766 147.929 1.00 92.33  ? 69   VAL A CA    1 
ATOM   526  C  C     . VAL A 1 68  ? 137.485 189.611 147.226 1.00 92.33  ? 69   VAL A C     1 
ATOM   527  O  O     . VAL A 1 68  ? 137.430 189.798 146.007 1.00 92.33  ? 69   VAL A O     1 
ATOM   528  C  CB    . VAL A 1 68  ? 136.727 187.241 147.885 1.00 92.33  ? 69   VAL A CB    1 
ATOM   529  C  CG1   . VAL A 1 68  ? 138.160 186.909 148.178 1.00 92.33  ? 69   VAL A CG1   1 
ATOM   530  C  CG2   . VAL A 1 68  ? 135.887 186.504 148.921 1.00 92.33  ? 69   VAL A CG2   1 
ATOM   531  N  N     . THR A 1 69  ? 138.450 190.128 147.992 1.00 92.69  ? 70   THR A N     1 
ATOM   532  C  CA    . THR A 1 69  ? 139.644 190.763 147.444 1.00 92.69  ? 70   THR A CA    1 
ATOM   533  C  C     . THR A 1 69  ? 140.883 190.054 147.979 1.00 92.69  ? 70   THR A C     1 
ATOM   534  O  O     . THR A 1 69  ? 141.064 189.955 149.197 1.00 92.69  ? 70   THR A O     1 
ATOM   535  C  CB    . THR A 1 69  ? 139.676 192.250 147.802 1.00 92.69  ? 70   THR A CB    1 
ATOM   536  O  OG1   . THR A 1 69  ? 138.470 192.875 147.346 1.00 92.69  ? 70   THR A OG1   1 
ATOM   537  C  CG2   . THR A 1 69  ? 140.869 192.933 147.153 1.00 92.69  ? 70   THR A CG2   1 
ATOM   538  N  N     . VAL A 1 70  ? 141.734 189.567 147.069 1.00 85.62  ? 71   VAL A N     1 
ATOM   539  C  CA    . VAL A 1 70  ? 142.894 188.738 147.398 1.00 85.62  ? 71   VAL A CA    1 
ATOM   540  C  C     . VAL A 1 70  ? 144.050 189.159 146.491 1.00 85.62  ? 71   VAL A C     1 
ATOM   541  O  O     . VAL A 1 70  ? 143.848 189.572 145.346 1.00 85.62  ? 71   VAL A O     1 
ATOM   542  C  CB    . VAL A 1 70  ? 142.522 187.217 147.277 1.00 85.62  ? 71   VAL A CB    1 
ATOM   543  C  CG1   . VAL A 1 70  ? 143.707 186.273 147.152 1.00 85.62  ? 71   VAL A CG1   1 
ATOM   544  C  CG2   . VAL A 1 70  ? 141.787 186.763 148.517 1.00 85.62  ? 71   VAL A CG2   1 
ATOM   545  N  N     . LYS A 1 71  ? 145.272 189.050 147.018 1.00 84.13  ? 72   LYS A N     1 
ATOM   546  C  CA    . LYS A 1 71  ? 146.487 189.402 146.297 1.00 84.13  ? 72   LYS A CA    1 
ATOM   547  C  C     . LYS A 1 71  ? 146.797 188.409 145.176 1.00 84.13  ? 72   LYS A C     1 
ATOM   548  O  O     . LYS A 1 71  ? 146.511 187.213 145.268 1.00 84.13  ? 72   LYS A O     1 
ATOM   549  C  CB    . LYS A 1 71  ? 147.653 189.512 147.279 1.00 84.13  ? 72   LYS A CB    1 
ATOM   550  C  CG    . LYS A 1 71  ? 147.957 188.242 148.054 1.00 84.13  ? 72   LYS A CG    1 
ATOM   551  C  CD    . LYS A 1 71  ? 149.091 188.474 149.041 1.00 84.13  ? 72   LYS A CD    1 
ATOM   552  C  CE    . LYS A 1 71  ? 148.677 189.438 150.142 1.00 84.13  ? 72   LYS A CE    1 
ATOM   553  N  NZ    . LYS A 1 71  ? 149.783 189.697 151.104 1.00 84.13  ? 72   LYS A NZ    1 
ATOM   554  N  N     . GLU A 1 72  ? 147.375 188.947 144.095 1.00 84.39  ? 73   GLU A N     1 
ATOM   555  C  CA    . GLU A 1 72  ? 147.518 188.260 142.813 1.00 84.39  ? 73   GLU A CA    1 
ATOM   556  C  C     . GLU A 1 72  ? 148.467 187.064 142.857 1.00 84.39  ? 73   GLU A C     1 
ATOM   557  O  O     . GLU A 1 72  ? 148.320 186.147 142.042 1.00 84.39  ? 73   GLU A O     1 
ATOM   558  C  CB    . GLU A 1 72  ? 147.983 189.281 141.762 1.00 84.39  ? 73   GLU A CB    1 
ATOM   559  C  CG    . GLU A 1 72  ? 147.987 188.828 140.301 1.00 84.39  ? 73   GLU A CG    1 
ATOM   560  C  CD    . GLU A 1 72  ? 149.308 188.214 139.872 1.00 84.39  ? 73   GLU A CD    1 
ATOM   561  O  OE1   . GLU A 1 72  ? 150.311 188.398 140.594 1.00 84.39  ? 73   GLU A OE1   1 
ATOM   562  O  OE2   . GLU A 1 72  ? 149.344 187.545 138.819 1.00 84.39  ? 73   GLU A OE2   1 
ATOM   563  N  N     . ASP A 1 73  ? 149.387 187.004 143.816 1.00 80.12  ? 74   ASP A N     1 
ATOM   564  C  CA    . ASP A 1 73  ? 150.191 185.796 143.961 1.00 80.12  ? 74   ASP A CA    1 
ATOM   565  C  C     . ASP A 1 73  ? 149.422 184.653 144.604 1.00 80.12  ? 74   ASP A C     1 
ATOM   566  O  O     . ASP A 1 73  ? 149.854 183.499 144.512 1.00 80.12  ? 74   ASP A O     1 
ATOM   567  C  CB    . ASP A 1 73  ? 151.463 186.095 144.759 1.00 80.12  ? 74   ASP A CB    1 
ATOM   568  C  CG    . ASP A 1 73  ? 151.178 186.773 146.077 1.00 80.12  ? 74   ASP A CG    1 
ATOM   569  O  OD1   . ASP A 1 73  ? 150.500 187.821 146.058 1.00 80.12  ? 74   ASP A OD1   1 
ATOM   570  O  OD2   . ASP A 1 73  ? 151.627 186.265 147.126 1.00 80.12  ? 74   ASP A OD2   1 
ATOM   571  N  N     . GLN A 1 74  ? 148.292 184.944 145.239 1.00 74.78  ? 75   GLN A N     1 
ATOM   572  C  CA    . GLN A 1 74  ? 147.514 183.952 145.963 1.00 74.78  ? 75   GLN A CA    1 
ATOM   573  C  C     . GLN A 1 74  ? 146.357 183.388 145.144 1.00 74.78  ? 75   GLN A C     1 
ATOM   574  O  O     . GLN A 1 74  ? 146.024 182.208 145.295 1.00 74.78  ? 75   GLN A O     1 
ATOM   575  C  CB    . GLN A 1 74  ? 146.992 184.573 147.265 1.00 74.78  ? 75   GLN A CB    1 
ATOM   576  C  CG    . GLN A 1 74  ? 146.328 183.618 148.237 1.00 74.78  ? 75   GLN A CG    1 
ATOM   577  C  CD    . GLN A 1 74  ? 146.167 184.227 149.617 1.00 74.78  ? 75   GLN A CD    1 
ATOM   578  O  OE1   . GLN A 1 74  ? 145.885 185.416 149.752 1.00 74.78  ? 75   GLN A OE1   1 
ATOM   579  N  NE2   . GLN A 1 74  ? 146.348 183.412 150.649 1.00 74.78  ? 75   GLN A NE2   1 
ATOM   580  N  N     . VAL A 1 75  ? 145.758 184.193 144.262 1.00 68.80  ? 76   VAL A N     1 
ATOM   581  C  CA    . VAL A 1 75  ? 144.705 183.714 143.371 1.00 68.80  ? 76   VAL A CA    1 
ATOM   582  C  C     . VAL A 1 75  ? 145.289 182.825 142.274 1.00 68.80  ? 76   VAL A C     1 
ATOM   583  O  O     . VAL A 1 75  ? 146.394 183.062 141.766 1.00 68.80  ? 76   VAL A O     1 
ATOM   584  C  CB    . VAL A 1 75  ? 143.918 184.913 142.805 1.00 68.80  ? 76   VAL A CB    1 
ATOM   585  C  CG1   . VAL A 1 75  ? 144.792 185.824 141.952 1.00 68.80  ? 76   VAL A CG1   1 
ATOM   586  C  CG2   . VAL A 1 75  ? 142.691 184.466 142.036 1.00 68.80  ? 76   VAL A CG2   1 
ATOM   587  N  N     . MET A 1 76  ? 144.575 181.744 141.960 1.00 52.12  ? 77   MET A N     1 
ATOM   588  C  CA    . MET A 1 76  ? 145.167 180.560 141.352 1.00 52.12  ? 77   MET A CA    1 
ATOM   589  C  C     . MET A 1 76  ? 144.123 179.844 140.499 1.00 52.12  ? 77   MET A C     1 
ATOM   590  O  O     . MET A 1 76  ? 142.992 179.629 140.945 1.00 52.12  ? 77   MET A O     1 
ATOM   591  C  CB    . MET A 1 76  ? 145.766 179.688 142.463 1.00 52.12  ? 77   MET A CB    1 
ATOM   592  C  CG    . MET A 1 76  ? 144.805 179.352 143.596 1.00 52.12  ? 77   MET A CG    1 
ATOM   593  S  SD    . MET A 1 76  ? 145.625 178.875 145.131 1.00 52.12  ? 77   MET A SD    1 
ATOM   594  C  CE    . MET A 1 76  ? 146.645 177.521 144.593 1.00 52.12  ? 77   MET A CE    1 
ATOM   595  N  N     . GLN A 1 77  ? 144.496 179.539 139.253 1.00 53.46  ? 78   GLN A N     1 
ATOM   596  C  CA    . GLN A 1 77  ? 143.549 179.163 138.201 1.00 53.46  ? 78   GLN A CA    1 
ATOM   597  C  C     . GLN A 1 77  ? 142.858 177.826 138.466 1.00 53.46  ? 78   GLN A C     1 
ATOM   598  O  O     . GLN A 1 77  ? 143.436 176.900 139.040 1.00 53.46  ? 78   GLN A O     1 
ATOM   599  C  CB    . GLN A 1 77  ? 144.249 179.119 136.839 1.00 53.46  ? 78   GLN A CB    1 
ATOM   600  C  CG    . GLN A 1 77  ? 144.516 180.483 136.192 1.00 53.46  ? 78   GLN A CG    1 
ATOM   601  C  CD    . GLN A 1 77  ? 145.620 181.278 136.859 1.00 53.46  ? 78   GLN A CD    1 
ATOM   602  O  OE1   . GLN A 1 77  ? 146.425 180.737 137.614 1.00 53.46  ? 78   GLN A OE1   1 
ATOM   603  N  NE2   . GLN A 1 77  ? 145.661 182.575 136.582 1.00 53.46  ? 78   GLN A NE2   1 
ATOM   604  N  N     . GLN A 1 78  ? 141.601 177.735 138.029 1.00 54.43  ? 79   GLN A N     1 
ATOM   605  C  CA    . GLN A 1 78  ? 140.904 176.457 137.942 1.00 54.43  ? 79   GLN A CA    1 
ATOM   606  C  C     . GLN A 1 78  ? 141.486 175.559 136.858 1.00 54.43  ? 79   GLN A C     1 
ATOM   607  O  O     . GLN A 1 78  ? 141.977 176.021 135.827 1.00 54.43  ? 79   GLN A O     1 
ATOM   608  C  CB    . GLN A 1 78  ? 139.417 176.667 137.671 1.00 54.43  ? 79   GLN A CB    1 
ATOM   609  C  CG    . GLN A 1 78  ? 138.633 177.123 138.879 1.00 54.43  ? 79   GLN A CG    1 
ATOM   610  C  CD    . GLN A 1 78  ? 137.145 177.193 138.616 1.00 54.43  ? 79   GLN A CD    1 
ATOM   611  O  OE1   . GLN A 1 78  ? 136.479 178.153 138.999 1.00 54.43  ? 79   GLN A OE1   1 
ATOM   612  N  NE2   . GLN A 1 78  ? 136.615 176.171 137.958 1.00 54.43  ? 79   GLN A NE2   1 
ATOM   613  N  N     . ASN A 1 79  ? 141.428 174.259 137.113 1.00 50.15  ? 80   ASN A N     1 
ATOM   614  C  CA    . ASN A 1 79  ? 141.519 173.264 136.055 1.00 50.15  ? 80   ASN A CA    1 
ATOM   615  C  C     . ASN A 1 79  ? 140.331 173.379 135.101 1.00 50.15  ? 80   ASN A C     1 
ATOM   616  O  O     . ASN A 1 79  ? 139.185 173.483 135.559 1.00 50.15  ? 80   ASN A O     1 
ATOM   617  C  CB    . ASN A 1 79  ? 141.592 171.863 136.660 1.00 50.15  ? 80   ASN A CB    1 
ATOM   618  C  CG    . ASN A 1 79  ? 140.517 171.619 137.703 1.00 50.15  ? 80   ASN A CG    1 
ATOM   619  O  OD1   . ASN A 1 79  ? 140.176 172.510 138.478 1.00 50.15  ? 80   ASN A OD1   1 
ATOM   620  N  ND2   . ASN A 1 79  ? 139.992 170.402 137.738 1.00 50.15  ? 80   ASN A ND2   1 
ATOM   621  N  N     . PRO A 1 80  ? 140.559 173.407 133.788 1.00 48.64  ? 81   PRO A N     1 
ATOM   622  C  CA    . PRO A 1 80  ? 139.460 173.614 132.825 1.00 48.64  ? 81   PRO A CA    1 
ATOM   623  C  C     . PRO A 1 80  ? 138.562 172.388 132.731 1.00 48.64  ? 81   PRO A C     1 
ATOM   624  O  O     . PRO A 1 80  ? 139.010 171.272 133.037 1.00 48.64  ? 81   PRO A O     1 
ATOM   625  C  CB    . PRO A 1 80  ? 140.213 173.877 131.509 1.00 48.64  ? 81   PRO A CB    1 
ATOM   626  C  CG    . PRO A 1 80  ? 141.505 173.196 131.669 1.00 48.64  ? 81   PRO A CG    1 
ATOM   627  C  CD    . PRO A 1 80  ? 141.864 173.274 133.120 1.00 48.64  ? 81   PRO A CD    1 
ATOM   628  N  N     . PRO A 1 81  ? 137.291 172.555 132.313 1.00 48.65  ? 82   PRO A N     1 
ATOM   629  C  CA    . PRO A 1 81  ? 136.250 171.559 132.650 1.00 48.65  ? 82   PRO A CA    1 
ATOM   630  C  C     . PRO A 1 81  ? 136.395 170.197 131.996 1.00 48.65  ? 82   PRO A C     1 
ATOM   631  O  O     . PRO A 1 81  ? 135.780 169.243 132.481 1.00 48.65  ? 82   PRO A O     1 
ATOM   632  C  CB    . PRO A 1 81  ? 134.950 172.233 132.186 1.00 48.65  ? 82   PRO A CB    1 
ATOM   633  C  CG    . PRO A 1 81  ? 135.372 173.266 131.235 1.00 48.65  ? 82   PRO A CG    1 
ATOM   634  C  CD    . PRO A 1 81  ? 136.677 173.759 131.731 1.00 48.65  ? 82   PRO A CD    1 
ATOM   635  N  N     . LYS A 1 82  ? 137.135 170.080 130.893 1.00 45.99  ? 83   LYS A N     1 
ATOM   636  C  CA    . LYS A 1 82  ? 137.438 168.779 130.298 1.00 45.99  ? 83   LYS A CA    1 
ATOM   637  C  C     . LYS A 1 82  ? 138.172 167.834 131.253 1.00 45.99  ? 83   LYS A C     1 
ATOM   638  O  O     . LYS A 1 82  ? 138.076 166.612 131.095 1.00 45.99  ? 83   LYS A O     1 
ATOM   639  C  CB    . LYS A 1 82  ? 138.226 169.019 128.999 1.00 45.99  ? 83   LYS A CB    1 
ATOM   640  C  CG    . LYS A 1 82  ? 138.580 167.801 128.147 1.00 45.99  ? 83   LYS A CG    1 
ATOM   641  C  CD    . LYS A 1 82  ? 140.024 167.357 128.339 1.00 45.99  ? 83   LYS A CD    1 
ATOM   642  C  CE    . LYS A 1 82  ? 140.976 168.381 127.739 1.00 45.99  ? 83   LYS A CE    1 
ATOM   643  N  NZ    . LYS A 1 82  ? 142.388 167.924 127.766 1.00 45.99  ? 83   LYS A NZ    1 
ATOM   644  N  N     . PHE A 1 83  ? 138.857 168.362 132.262 1.00 41.91  ? 84   PHE A N     1 
ATOM   645  C  CA    . PHE A 1 83  ? 139.557 167.562 133.257 1.00 41.91  ? 84   PHE A CA    1 
ATOM   646  C  C     . PHE A 1 83  ? 138.712 167.179 134.466 1.00 41.91  ? 84   PHE A C     1 
ATOM   647  O  O     . PHE A 1 83  ? 139.282 166.655 135.424 1.00 41.91  ? 84   PHE A O     1 
ATOM   648  C  CB    . PHE A 1 83  ? 140.815 168.291 133.726 1.00 41.91  ? 84   PHE A CB    1 
ATOM   649  C  CG    . PHE A 1 83  ? 141.836 168.460 132.653 1.00 41.91  ? 84   PHE A CG    1 
ATOM   650  C  CD1   . PHE A 1 83  ? 142.703 167.431 132.345 1.00 41.91  ? 84   PHE A CD1   1 
ATOM   651  C  CD2   . PHE A 1 83  ? 141.918 169.638 131.940 1.00 41.91  ? 84   PHE A CD2   1 
ATOM   652  C  CE1   . PHE A 1 83  ? 143.644 167.577 131.348 1.00 41.91  ? 84   PHE A CE1   1 
ATOM   653  C  CE2   . PHE A 1 83  ? 142.852 169.792 130.942 1.00 41.91  ? 84   PHE A CE2   1 
ATOM   654  C  CZ    . PHE A 1 83  ? 143.719 168.760 130.648 1.00 41.91  ? 84   PHE A CZ    1 
ATOM   655  N  N     . ASP A 1 84  ? 137.427 167.552 134.502 1.00 38.11  ? 85   ASP A N     1 
ATOM   656  C  CA    . ASP A 1 84  ? 136.524 167.200 135.602 1.00 38.11  ? 85   ASP A CA    1 
ATOM   657  C  C     . ASP A 1 84  ? 136.545 165.708 135.917 1.00 38.11  ? 85   ASP A C     1 
ATOM   658  O  O     . ASP A 1 84  ? 136.454 164.875 135.012 1.00 38.11  ? 85   ASP A O     1 
ATOM   659  C  CB    . ASP A 1 84  ? 135.095 167.623 135.264 1.00 38.11  ? 85   ASP A CB    1 
ATOM   660  C  CG    . ASP A 1 84  ? 134.849 169.089 135.515 1.00 38.11  ? 85   ASP A CG    1 
ATOM   661  O  OD1   . ASP A 1 84  ? 135.821 169.799 135.846 1.00 38.11  ? 85   ASP A OD1   1 
ATOM   662  O  OD2   . ASP A 1 84  ? 133.686 169.530 135.387 1.00 38.11  ? 85   ASP A OD2   1 
ATOM   663  N  N     . LYS A 1 85  ? 136.719 165.387 137.203 1.00 24.93  ? 86   LYS A N     1 
ATOM   664  C  CA    . LYS A 1 85  ? 136.674 164.028 137.750 1.00 24.93  ? 86   LYS A CA    1 
ATOM   665  C  C     . LYS A 1 85  ? 137.737 163.098 137.166 1.00 24.93  ? 86   LYS A C     1 
ATOM   666  O  O     . LYS A 1 85  ? 137.505 161.889 137.095 1.00 24.93  ? 86   LYS A O     1 
ATOM   667  C  CB    . LYS A 1 85  ? 135.281 163.408 137.604 1.00 24.93  ? 86   LYS A CB    1 
ATOM   668  C  CG    . LYS A 1 85  ? 134.164 164.286 138.134 1.00 24.93  ? 86   LYS A CG    1 
ATOM   669  C  CD    . LYS A 1 85  ? 132.829 163.573 138.055 1.00 24.93  ? 86   LYS A CD    1 
ATOM   670  C  CE    . LYS A 1 85  ? 131.708 164.410 138.636 1.00 24.93  ? 86   LYS A CE    1 
ATOM   671  N  NZ    . LYS A 1 85  ? 131.245 165.463 137.700 1.00 24.93  ? 86   LYS A NZ    1 
ATOM   672  N  N     . ILE A 1 86  ? 138.848 163.673 136.681 1.00 25.05  ? 87   ILE A N     1 
ATOM   673  C  CA    . ILE A 1 86  ? 139.933 162.938 136.029 1.00 25.05  ? 87   ILE A CA    1 
ATOM   674  C  C     . ILE A 1 86  ? 140.454 161.787 136.893 1.00 25.05  ? 87   ILE A C     1 
ATOM   675  O  O     . ILE A 1 86  ? 140.556 161.889 138.119 1.00 25.05  ? 87   ILE A O     1 
ATOM   676  C  CB    . ILE A 1 86  ? 141.051 163.926 135.638 1.00 25.05  ? 87   ILE A CB    1 
ATOM   677  C  CG1   . ILE A 1 86  ? 142.177 163.254 134.853 1.00 25.05  ? 87   ILE A CG1   1 
ATOM   678  C  CG2   . ILE A 1 86  ? 141.591 164.664 136.843 1.00 25.05  ? 87   ILE A CG2   1 
ATOM   679  C  CD1   . ILE A 1 86  ? 142.992 164.217 134.028 1.00 25.05  ? 87   ILE A CD1   1 
ATOM   680  N  N     . GLU A 1 87  ? 140.732 160.660 136.237 1.00 28.31  ? 88   GLU A N     1 
ATOM   681  C  CA    . GLU A 1 87  ? 141.033 159.404 136.911 1.00 28.31  ? 88   GLU A CA    1 
ATOM   682  C  C     . GLU A 1 87  ? 142.454 159.347 137.449 1.00 28.31  ? 88   GLU A C     1 
ATOM   683  O  O     . GLU A 1 87  ? 142.720 158.588 138.386 1.00 28.31  ? 88   GLU A O     1 
ATOM   684  C  CB    . GLU A 1 87  ? 140.798 158.235 135.958 1.00 28.31  ? 88   GLU A CB    1 
ATOM   685  C  CG    . GLU A 1 87  ? 139.335 157.955 135.687 1.00 28.31  ? 88   GLU A CG    1 
ATOM   686  C  CD    . GLU A 1 87  ? 139.133 157.119 134.450 1.00 28.31  ? 88   GLU A CD    1 
ATOM   687  O  OE1   . GLU A 1 87  ? 140.069 156.383 134.078 1.00 28.31  ? 88   GLU A OE1   1 
ATOM   688  O  OE2   . GLU A 1 87  ? 138.041 157.195 133.853 1.00 28.31  ? 88   GLU A OE2   1 
ATOM   689  N  N     . ASP A 1 88  ? 143.379 160.103 136.866 1.00 25.69  ? 89   ASP A N     1 
ATOM   690  C  CA    . ASP A 1 88  ? 144.776 160.101 137.299 1.00 25.69  ? 89   ASP A CA    1 
ATOM   691  C  C     . ASP A 1 88  ? 145.192 161.566 137.347 1.00 25.69  ? 89   ASP A C     1 
ATOM   692  O  O     . ASP A 1 88  ? 145.474 162.169 136.309 1.00 25.69  ? 89   ASP A O     1 
ATOM   693  C  CB    . ASP A 1 88  ? 145.638 159.283 136.339 1.00 25.69  ? 89   ASP A CB    1 
ATOM   694  C  CG    . ASP A 1 88  ? 147.078 159.107 136.808 1.00 25.69  ? 89   ASP A CG    1 
ATOM   695  O  OD1   . ASP A 1 88  ? 147.468 159.635 137.863 1.00 25.69  ? 89   ASP A OD1   1 
ATOM   696  O  OD2   . ASP A 1 88  ? 147.836 158.414 136.103 1.00 25.69  ? 89   ASP A OD2   1 
ATOM   697  N  N     . MET A 1 89  ? 145.223 162.126 138.560 1.00 25.73  ? 90   MET A N     1 
ATOM   698  C  CA    . MET A 1 89  ? 145.305 163.568 138.770 1.00 25.73  ? 90   MET A CA    1 
ATOM   699  C  C     . MET A 1 89  ? 146.615 164.190 138.314 1.00 25.73  ? 90   MET A C     1 
ATOM   700  O  O     . MET A 1 89  ? 146.690 165.420 138.237 1.00 25.73  ? 90   MET A O     1 
ATOM   701  C  CB    . MET A 1 89  ? 145.052 163.902 140.234 1.00 25.73  ? 90   MET A CB    1 
ATOM   702  C  CG    . MET A 1 89  ? 143.680 163.478 140.657 1.00 25.73  ? 90   MET A CG    1 
ATOM   703  S  SD    . MET A 1 89  ? 143.092 164.094 142.236 1.00 25.73  ? 90   MET A SD    1 
ATOM   704  C  CE    . MET A 1 89  ? 144.140 163.217 143.370 1.00 25.73  ? 90   MET A CE    1 
ATOM   705  N  N     . ALA A 1 90  ? 147.655 163.384 138.076 1.00 28.21  ? 91   ALA A N     1 
ATOM   706  C  CA    . ALA A 1 90  ? 148.909 163.883 137.513 1.00 28.21  ? 91   ALA A CA    1 
ATOM   707  C  C     . ALA A 1 90  ? 148.721 164.611 136.182 1.00 28.21  ? 91   ALA A C     1 
ATOM   708  O  O     . ALA A 1 90  ? 149.468 165.547 135.880 1.00 28.21  ? 91   ALA A O     1 
ATOM   709  C  CB    . ALA A 1 90  ? 149.895 162.729 137.346 1.00 28.21  ? 91   ALA A CB    1 
ATOM   710  N  N     . MET A 1 91  ? 147.727 164.223 135.390 1.00 33.23  ? 92   MET A N     1 
ATOM   711  C  CA    . MET A 1 91  ? 147.526 164.783 134.062 1.00 33.23  ? 92   MET A CA    1 
ATOM   712  C  C     . MET A 1 91  ? 146.759 166.099 134.055 1.00 33.23  ? 92   MET A C     1 
ATOM   713  O  O     . MET A 1 91  ? 146.379 166.550 132.971 1.00 33.23  ? 92   MET A O     1 
ATOM   714  C  CB    . MET A 1 91  ? 146.818 163.761 133.176 1.00 33.23  ? 92   MET A CB    1 
ATOM   715  C  CG    . MET A 1 91  ? 147.594 162.471 133.052 1.00 33.23  ? 92   MET A CG    1 
ATOM   716  S  SD    . MET A 1 91  ? 149.243 162.786 132.394 1.00 33.23  ? 92   MET A SD    1 
ATOM   717  C  CE    . MET A 1 91  ? 149.999 161.174 132.556 1.00 33.23  ? 92   MET A CE    1 
ATOM   718  N  N     . LEU A 1 92  ? 146.485 166.694 135.215 1.00 34.14  ? 93   LEU A N     1 
ATOM   719  C  CA    . LEU A 1 92  ? 145.860 168.012 135.260 1.00 34.14  ? 93   LEU A CA    1 
ATOM   720  C  C     . LEU A 1 92  ? 146.756 169.076 134.629 1.00 34.14  ? 93   LEU A C     1 
ATOM   721  O  O     . LEU A 1 92  ? 147.986 168.999 134.680 1.00 34.14  ? 93   LEU A O     1 
ATOM   722  C  CB    . LEU A 1 92  ? 145.524 168.396 136.703 1.00 34.14  ? 93   LEU A CB    1 
ATOM   723  C  CG    . LEU A 1 92  ? 144.355 167.682 137.382 1.00 34.14  ? 93   LEU A CG    1 
ATOM   724  C  CD1   . LEU A 1 92  ? 144.417 167.894 138.872 1.00 34.14  ? 93   LEU A CD1   1 
ATOM   725  C  CD2   . LEU A 1 92  ? 143.040 168.200 136.845 1.00 34.14  ? 93   LEU A CD2   1 
ATOM   726  N  N     . THR A 1 93  ? 146.114 170.074 134.017 1.00 38.52  ? 94   THR A N     1 
ATOM   727  C  CA    . THR A 1 93  ? 146.838 171.224 133.484 1.00 38.52  ? 94   THR A CA    1 
ATOM   728  C  C     . THR A 1 93  ? 147.331 172.129 134.603 1.00 38.52  ? 94   THR A C     1 
ATOM   729  O  O     . THR A 1 93  ? 148.456 172.640 134.554 1.00 38.52  ? 94   THR A O     1 
ATOM   730  C  CB    . THR A 1 93  ? 145.933 171.990 132.515 1.00 38.52  ? 94   THR A CB    1 
ATOM   731  O  OG1   . THR A 1 93  ? 145.679 171.177 131.367 1.00 38.52  ? 94   THR A OG1   1 
ATOM   732  C  CG2   . THR A 1 93  ? 146.561 173.295 132.050 1.00 38.52  ? 94   THR A CG2   1 
ATOM   733  N  N     . PHE A 1 94  ? 146.544 172.272 135.656 1.00 39.40  ? 95   PHE A N     1 
ATOM   734  C  CA    . PHE A 1 94  ? 146.972 172.984 136.845 1.00 39.40  ? 95   PHE A CA    1 
ATOM   735  C  C     . PHE A 1 94  ? 146.949 172.021 138.016 1.00 39.40  ? 95   PHE A C     1 
ATOM   736  O  O     . PHE A 1 94  ? 145.935 171.364 138.267 1.00 39.40  ? 95   PHE A O     1 
ATOM   737  C  CB    . PHE A 1 94  ? 146.079 174.191 137.122 1.00 39.40  ? 95   PHE A CB    1 
ATOM   738  C  CG    . PHE A 1 94  ? 146.219 175.289 136.114 1.00 39.40  ? 95   PHE A CG    1 
ATOM   739  C  CD1   . PHE A 1 94  ? 147.330 176.112 136.125 1.00 39.40  ? 95   PHE A CD1   1 
ATOM   740  C  CD2   . PHE A 1 94  ? 145.239 175.505 135.165 1.00 39.40  ? 95   PHE A CD2   1 
ATOM   741  C  CE1   . PHE A 1 94  ? 147.463 177.129 135.201 1.00 39.40  ? 95   PHE A CE1   1 
ATOM   742  C  CE2   . PHE A 1 94  ? 145.367 176.521 134.238 1.00 39.40  ? 95   PHE A CE2   1 
ATOM   743  C  CZ    . PHE A 1 94  ? 146.480 177.332 134.257 1.00 39.40  ? 95   PHE A CZ    1 
ATOM   744  N  N     . LEU A 1 95  ? 148.069 171.940 138.723 1.00 33.02  ? 96   LEU A N     1 
ATOM   745  C  CA    . LEU A 1 95  ? 148.184 171.151 139.939 1.00 33.02  ? 96   LEU A CA    1 
ATOM   746  C  C     . LEU A 1 95  ? 148.575 172.083 141.072 1.00 33.02  ? 96   LEU A C     1 
ATOM   747  O  O     . LEU A 1 95  ? 149.620 172.738 141.004 1.00 33.02  ? 96   LEU A O     1 
ATOM   748  C  CB    . LEU A 1 95  ? 149.227 170.055 139.769 1.00 33.02  ? 96   LEU A CB    1 
ATOM   749  C  CG    . LEU A 1 95  ? 149.479 169.255 141.028 1.00 33.02  ? 96   LEU A CG    1 
ATOM   750  C  CD1   . LEU A 1 95  ? 148.297 168.391 141.280 1.00 33.02  ? 96   LEU A CD1   1 
ATOM   751  C  CD2   . LEU A 1 95  ? 150.705 168.439 140.854 1.00 33.02  ? 96   LEU A CD2   1 
ATOM   752  N  N     . HIS A 1 96  ? 147.755 172.107 142.116 1.00 37.07  ? 97   HIS A N     1 
ATOM   753  C  CA    . HIS A 1 96  ? 147.918 172.955 143.293 1.00 37.07  ? 97   HIS A CA    1 
ATOM   754  C  C     . HIS A 1 96  ? 146.958 172.429 144.356 1.00 37.07  ? 97   HIS A C     1 
ATOM   755  O  O     . HIS A 1 96  ? 146.245 171.450 144.121 1.00 37.07  ? 97   HIS A O     1 
ATOM   756  C  CB    . HIS A 1 96  ? 147.696 174.428 142.928 1.00 37.07  ? 97   HIS A CB    1 
ATOM   757  C  CG    . HIS A 1 96  ? 146.503 174.674 142.051 1.00 37.07  ? 97   HIS A CG    1 
ATOM   758  N  ND1   . HIS A 1 96  ? 145.316 175.174 142.530 1.00 37.07  ? 97   HIS A ND1   1 
ATOM   759  C  CD2   . HIS A 1 96  ? 146.326 174.512 140.719 1.00 37.07  ? 97   HIS A CD2   1 
ATOM   760  C  CE1   . HIS A 1 96  ? 144.451 175.293 141.540 1.00 37.07  ? 97   HIS A CE1   1 
ATOM   761  N  NE2   . HIS A 1 96  ? 145.039 174.896 140.428 1.00 37.07  ? 97   HIS A NE2   1 
ATOM   762  N  N     . GLU A 1 97  ? 147.004 173.039 145.564 1.00 34.79  ? 98   GLU A N     1 
ATOM   763  C  CA    . GLU A 1 97  ? 146.188 172.664 146.730 1.00 34.79  ? 98   GLU A CA    1 
ATOM   764  C  C     . GLU A 1 97  ? 144.689 172.486 146.419 1.00 34.79  ? 98   GLU A C     1 
ATOM   765  O  O     . GLU A 1 97  ? 144.183 171.386 146.664 1.00 34.79  ? 98   GLU A O     1 
ATOM   766  C  CB    . GLU A 1 97  ? 146.425 173.629 147.912 1.00 34.79  ? 98   GLU A CB    1 
ATOM   767  C  CG    . GLU A 1 97  ? 147.751 173.510 148.617 1.00 34.79  ? 98   GLU A CG    1 
ATOM   768  C  CD    . GLU A 1 97  ? 147.989 174.656 149.577 1.00 34.79  ? 98   GLU A CD    1 
ATOM   769  O  OE1   . GLU A 1 97  ? 148.196 175.793 149.107 1.00 34.79  ? 98   GLU A OE1   1 
ATOM   770  O  OE2   . GLU A 1 97  ? 147.959 174.422 150.804 1.00 34.79  ? 98   GLU A OE2   1 
ATOM   771  N  N     . PRO A 1 98  ? 143.928 173.476 145.906 1.00 34.56  ? 99   PRO A N     1 
ATOM   772  C  CA    . PRO A 1 98  ? 142.498 173.221 145.679 1.00 34.56  ? 99   PRO A CA    1 
ATOM   773  C  C     . PRO A 1 98  ? 142.210 172.330 144.495 1.00 34.56  ? 99   PRO A C     1 
ATOM   774  O  O     . PRO A 1 98  ? 141.092 171.807 144.409 1.00 34.56  ? 99   PRO A O     1 
ATOM   775  C  CB    . PRO A 1 98  ? 141.919 174.610 145.429 1.00 34.56  ? 99   PRO A CB    1 
ATOM   776  C  CG    . PRO A 1 98  ? 142.994 175.357 144.937 1.00 34.56  ? 99   PRO A CG    1 
ATOM   777  C  CD    . PRO A 1 98  ? 144.215 174.886 145.584 1.00 34.56  ? 99   PRO A CD    1 
ATOM   778  N  N     . ALA A 1 99  ? 143.144 172.204 143.551 1.00 30.95  ? 100  ALA A N     1 
ATOM   779  C  CA    . ALA A 1 99  ? 142.930 171.346 142.390 1.00 30.95  ? 100  ALA A CA    1 
ATOM   780  C  C     . ALA A 1 99  ? 142.740 169.896 142.802 1.00 30.95  ? 100  ALA A C     1 
ATOM   781  O  O     . ALA A 1 99  ? 141.806 169.234 142.346 1.00 30.95  ? 100  ALA A O     1 
ATOM   782  C  CB    . ALA A 1 99  ? 144.096 171.482 141.415 1.00 30.95  ? 100  ALA A CB    1 
ATOM   783  N  N     . VAL A 1 100 ? 143.618 169.383 143.658 1.00 24.83  ? 101  VAL A N     1 
ATOM   784  C  CA    . VAL A 1 100 ? 143.463 168.017 144.140 1.00 24.83  ? 101  VAL A CA    1 
ATOM   785  C  C     . VAL A 1 100 ? 142.269 167.906 145.082 1.00 24.83  ? 101  VAL A C     1 
ATOM   786  O  O     . VAL A 1 100 ? 141.531 166.914 145.047 1.00 24.83  ? 101  VAL A O     1 
ATOM   787  C  CB    . VAL A 1 100 ? 144.774 167.547 144.790 1.00 24.83  ? 101  VAL A CB    1 
ATOM   788  C  CG1   . VAL A 1 100 ? 144.611 166.245 145.529 1.00 24.83  ? 101  VAL A CG1   1 
ATOM   789  C  CG2   . VAL A 1 100 ? 145.784 167.347 143.728 1.00 24.83  ? 101  VAL A CG2   1 
ATOM   790  N  N     . LEU A 1 101 ? 142.033 168.933 145.901 1.00 26.68  ? 102  LEU A N     1 
ATOM   791  C  CA    . LEU A 1 101 ? 140.863 168.964 146.781 1.00 26.68  ? 102  LEU A CA    1 
ATOM   792  C  C     . LEU A 1 101 ? 139.549 168.901 146.010 1.00 26.68  ? 102  LEU A C     1 
ATOM   793  O  O     . LEU A 1 101 ? 138.725 168.014 146.249 1.00 26.68  ? 102  LEU A O     1 
ATOM   794  C  CB    . LEU A 1 101 ? 140.898 170.215 147.652 1.00 26.68  ? 102  LEU A CB    1 
ATOM   795  C  CG    . LEU A 1 101 ? 139.645 170.392 148.497 1.00 26.68  ? 102  LEU A CG    1 
ATOM   796  C  CD1   . LEU A 1 101 ? 139.578 169.289 149.498 1.00 26.68  ? 102  LEU A CD1   1 
ATOM   797  C  CD2   . LEU A 1 101 ? 139.651 171.737 149.181 1.00 26.68  ? 102  LEU A CD2   1 
ATOM   798  N  N     . TYR A 1 102 ? 139.328 169.834 145.087 1.00 28.44  ? 103  TYR A N     1 
ATOM   799  C  CA    . TYR A 1 102 ? 138.042 169.872 144.405 1.00 28.44  ? 103  TYR A CA    1 
ATOM   800  C  C     . TYR A 1 102 ? 137.865 168.746 143.401 1.00 28.44  ? 103  TYR A C     1 
ATOM   801  O  O     . TYR A 1 102 ? 136.724 168.403 143.080 1.00 28.44  ? 103  TYR A O     1 
ATOM   802  C  CB    . TYR A 1 102 ? 137.812 171.227 143.753 1.00 28.44  ? 103  TYR A CB    1 
ATOM   803  C  CG    . TYR A 1 102 ? 137.189 172.200 144.717 1.00 28.44  ? 103  TYR A CG    1 
ATOM   804  C  CD1   . TYR A 1 102 ? 135.813 172.243 144.878 1.00 28.44  ? 103  TYR A CD1   1 
ATOM   805  C  CD2   . TYR A 1 102 ? 137.967 173.042 145.495 1.00 28.44  ? 103  TYR A CD2   1 
ATOM   806  C  CE1   . TYR A 1 102 ? 135.227 173.116 145.765 1.00 28.44  ? 103  TYR A CE1   1 
ATOM   807  C  CE2   . TYR A 1 102 ? 137.388 173.924 146.387 1.00 28.44  ? 103  TYR A CE2   1 
ATOM   808  C  CZ    . TYR A 1 102 ? 136.018 173.953 146.516 1.00 28.44  ? 103  TYR A CZ    1 
ATOM   809  O  OH    . TYR A 1 102 ? 135.432 174.826 147.398 1.00 28.44  ? 103  TYR A OH    1 
ATOM   810  N  N     . ASN A 1 103 ? 138.949 168.181 142.876 1.00 22.18  ? 104  ASN A N     1 
ATOM   811  C  CA    . ASN A 1 103 ? 138.804 166.976 142.069 1.00 22.18  ? 104  ASN A CA    1 
ATOM   812  C  C     . ASN A 1 103 ? 138.386 165.780 142.909 1.00 22.18  ? 104  ASN A C     1 
ATOM   813  O  O     . ASN A 1 103 ? 137.569 164.968 142.466 1.00 22.18  ? 104  ASN A O     1 
ATOM   814  C  CB    . ASN A 1 103 ? 140.091 166.644 141.344 1.00 22.18  ? 104  ASN A CB    1 
ATOM   815  C  CG    . ASN A 1 103 ? 139.889 165.578 140.344 1.00 22.18  ? 104  ASN A CG    1 
ATOM   816  O  OD1   . ASN A 1 103 ? 139.083 165.725 139.436 1.00 22.18  ? 104  ASN A OD1   1 
ATOM   817  N  ND2   . ASN A 1 103 ? 140.543 164.456 140.541 1.00 22.18  ? 104  ASN A ND2   1 
ATOM   818  N  N     . LEU A 1 104 ? 138.967 165.628 144.101 1.00 20.24  ? 105  LEU A N     1 
ATOM   819  C  CA    . LEU A 1 104 ? 138.536 164.565 145.003 1.00 20.24  ? 105  LEU A CA    1 
ATOM   820  C  C     . LEU A 1 104 ? 137.116 164.777 145.505 1.00 20.24  ? 105  LEU A C     1 
ATOM   821  O  O     . LEU A 1 104 ? 136.373 163.807 145.665 1.00 20.24  ? 105  LEU A O     1 
ATOM   822  C  CB    . LEU A 1 104 ? 139.501 164.418 146.172 1.00 20.24  ? 105  LEU A CB    1 
ATOM   823  C  CG    . LEU A 1 104 ? 140.841 163.803 145.800 1.00 20.24  ? 105  LEU A CG    1 
ATOM   824  C  CD1   . LEU A 1 104 ? 141.822 163.959 146.930 1.00 20.24  ? 105  LEU A CD1   1 
ATOM   825  C  CD2   . LEU A 1 104 ? 140.630 162.347 145.494 1.00 20.24  ? 105  LEU A CD2   1 
ATOM   826  N  N     . LYS A 1 105 ? 136.729 166.020 145.790 1.00 22.35  ? 106  LYS A N     1 
ATOM   827  C  CA    . LYS A 1 105 ? 135.342 166.293 146.160 1.00 22.35  ? 106  LYS A CA    1 
ATOM   828  C  C     . LYS A 1 105 ? 134.375 165.993 145.020 1.00 22.35  ? 106  LYS A C     1 
ATOM   829  O  O     . LYS A 1 105 ? 133.267 165.501 145.258 1.00 22.35  ? 106  LYS A O     1 
ATOM   830  C  CB    . LYS A 1 105 ? 135.187 167.742 146.608 1.00 22.35  ? 106  LYS A CB    1 
ATOM   831  C  CG    . LYS A 1 105 ? 133.836 168.043 147.216 1.00 22.35  ? 106  LYS A CG    1 
ATOM   832  C  CD    . LYS A 1 105 ? 133.742 169.473 147.691 1.00 22.35  ? 106  LYS A CD    1 
ATOM   833  C  CE    . LYS A 1 105 ? 132.431 169.708 148.416 1.00 22.35  ? 106  LYS A CE    1 
ATOM   834  N  NZ    . LYS A 1 105 ? 131.266 169.548 147.504 1.00 22.35  ? 106  LYS A NZ    1 
ATOM   835  N  N     . ASP A 1 106 ? 134.774 166.260 143.774 1.00 21.40  ? 107  ASP A N     1 
ATOM   836  C  CA    . ASP A 1 106 ? 133.878 165.997 142.650 1.00 21.40  ? 107  ASP A CA    1 
ATOM   837  C  C     . ASP A 1 106 ? 133.772 164.518 142.295 1.00 21.40  ? 107  ASP A C     1 
ATOM   838  O  O     . ASP A 1 106 ? 132.714 164.078 141.837 1.00 21.40  ? 107  ASP A O     1 
ATOM   839  C  CB    . ASP A 1 106 ? 134.320 166.790 141.420 1.00 21.40  ? 107  ASP A CB    1 
ATOM   840  C  CG    . ASP A 1 106 ? 134.000 168.262 141.529 1.00 21.40  ? 107  ASP A CG    1 
ATOM   841  O  OD1   . ASP A 1 106 ? 133.176 168.624 142.390 1.00 21.40  ? 107  ASP A OD1   1 
ATOM   842  O  OD2   . ASP A 1 106 ? 134.564 169.057 140.753 1.00 21.40  ? 107  ASP A OD2   1 
ATOM   843  N  N     . ARG A 1 107 ? 134.836 163.739 142.480 1.00 20.52  ? 108  ARG A N     1 
ATOM   844  C  CA    . ARG A 1 107 ? 134.708 162.290 142.377 1.00 20.52  ? 108  ARG A CA    1 
ATOM   845  C  C     . ARG A 1 107 ? 133.892 161.722 143.532 1.00 20.52  ? 108  ARG A C     1 
ATOM   846  O  O     . ARG A 1 107 ? 133.036 160.855 143.329 1.00 20.52  ? 108  ARG A O     1 
ATOM   847  C  CB    . ARG A 1 107 ? 136.083 161.642 142.294 1.00 20.52  ? 108  ARG A CB    1 
ATOM   848  C  CG    . ARG A 1 107 ? 136.763 161.935 140.982 1.00 20.52  ? 108  ARG A CG    1 
ATOM   849  C  CD    . ARG A 1 107 ? 138.102 161.249 140.868 1.00 20.52  ? 108  ARG A CD    1 
ATOM   850  N  NE    . ARG A 1 107 ? 138.021 159.792 140.902 1.00 20.52  ? 108  ARG A NE    1 
ATOM   851  C  CZ    . ARG A 1 107 ? 137.556 159.020 139.922 1.00 20.52  ? 108  ARG A CZ    1 
ATOM   852  N  NH1   . ARG A 1 107 ? 137.468 157.712 140.100 1.00 20.52  ? 108  ARG A NH1   1 
ATOM   853  N  NH2   . ARG A 1 107 ? 137.185 159.540 138.762 1.00 20.52  ? 108  ARG A NH2   1 
ATOM   854  N  N     . TYR A 1 108 ? 134.180 162.158 144.760 1.00 20.31  ? 109  TYR A N     1 
ATOM   855  C  CA    . TYR A 1 108 ? 133.387 161.738 145.913 1.00 20.31  ? 109  TYR A CA    1 
ATOM   856  C  C     . TYR A 1 108 ? 131.956 162.256 145.854 1.00 20.31  ? 109  TYR A C     1 
ATOM   857  O  O     . TYR A 1 108 ? 131.056 161.637 146.427 1.00 20.31  ? 109  TYR A O     1 
ATOM   858  C  CB    . TYR A 1 108 ? 134.063 162.185 147.203 1.00 20.31  ? 109  TYR A CB    1 
ATOM   859  C  CG    . TYR A 1 108 ? 133.503 161.581 148.457 1.00 20.31  ? 109  TYR A CG    1 
ATOM   860  C  CD1   . TYR A 1 108 ? 133.682 160.244 148.737 1.00 20.31  ? 109  TYR A CD1   1 
ATOM   861  C  CD2   . TYR A 1 108 ? 132.846 162.364 149.387 1.00 20.31  ? 109  TYR A CD2   1 
ATOM   862  C  CE1   . TYR A 1 108 ? 133.196 159.696 149.894 1.00 20.31  ? 109  TYR A CE1   1 
ATOM   863  C  CE2   . TYR A 1 108 ? 132.355 161.826 150.543 1.00 20.31  ? 109  TYR A CE2   1 
ATOM   864  C  CZ    . TYR A 1 108 ? 132.532 160.490 150.792 1.00 20.31  ? 109  TYR A CZ    1 
ATOM   865  O  OH    . TYR A 1 108 ? 132.040 159.936 151.947 1.00 20.31  ? 109  TYR A OH    1 
ATOM   866  N  N     . GLY A 1 109 ? 131.720 163.385 145.185 1.00 20.15  ? 110  GLY A N     1 
ATOM   867  C  CA    . GLY A 1 109 ? 130.366 163.893 145.014 1.00 20.15  ? 110  GLY A CA    1 
ATOM   868  C  C     . GLY A 1 109 ? 129.448 163.043 144.153 1.00 20.15  ? 110  GLY A C     1 
ATOM   869  O  O     . GLY A 1 109 ? 128.250 163.339 144.099 1.00 20.15  ? 110  GLY A O     1 
ATOM   870  N  N     . SER A 1 110 ? 129.966 162.011 143.479 1.00 21.29  ? 111  SER A N     1 
ATOM   871  C  CA    . SER A 1 110 ? 129.128 160.977 142.881 1.00 21.29  ? 111  SER A CA    1 
ATOM   872  C  C     . SER A 1 110 ? 129.576 159.591 143.325 1.00 21.29  ? 111  SER A C     1 
ATOM   873  O  O     . SER A 1 110 ? 129.400 158.618 142.592 1.00 21.29  ? 111  SER A O     1 
ATOM   874  C  CB    . SER A 1 110 ? 129.125 161.071 141.357 1.00 21.29  ? 111  SER A CB    1 
ATOM   875  O  OG    . SER A 1 110 ? 130.422 160.886 140.835 1.00 21.29  ? 111  SER A OG    1 
ATOM   876  N  N     . TRP A 1 111 ? 130.180 159.502 144.513 1.00 21.54  ? 112  TRP A N     1 
ATOM   877  C  CA    . TRP A 1 111 ? 130.683 158.269 145.131 1.00 21.54  ? 112  TRP A CA    1 
ATOM   878  C  C     . TRP A 1 111 ? 131.693 157.491 144.284 1.00 21.54  ? 112  TRP A C     1 
ATOM   879  O  O     . TRP A 1 111 ? 131.894 156.299 144.514 1.00 21.54  ? 112  TRP A O     1 
ATOM   880  C  CB    . TRP A 1 111 ? 129.541 157.349 145.578 1.00 21.54  ? 112  TRP A CB    1 
ATOM   881  C  CG    . TRP A 1 111 ? 128.849 157.831 146.818 1.00 21.54  ? 112  TRP A CG    1 
ATOM   882  C  CD1   . TRP A 1 111 ? 129.250 157.617 148.102 1.00 21.54  ? 112  TRP A CD1   1 
ATOM   883  C  CD2   . TRP A 1 111 ? 127.640 158.592 146.900 1.00 21.54  ? 112  TRP A CD2   1 
ATOM   884  N  NE1   . TRP A 1 111 ? 128.372 158.199 148.979 1.00 21.54  ? 112  TRP A NE1   1 
ATOM   885  C  CE2   . TRP A 1 111 ? 127.373 158.805 148.266 1.00 21.54  ? 112  TRP A CE2   1 
ATOM   886  C  CE3   . TRP A 1 111 ? 126.756 159.115 145.953 1.00 21.54  ? 112  TRP A CE3   1 
ATOM   887  C  CZ2   . TRP A 1 111 ? 126.263 159.517 148.708 1.00 21.54  ? 112  TRP A CZ2   1 
ATOM   888  C  CZ3   . TRP A 1 111 ? 125.651 159.825 146.395 1.00 21.54  ? 112  TRP A CZ3   1 
ATOM   889  C  CH2   . TRP A 1 111 ? 125.416 160.019 147.759 1.00 21.54  ? 112  TRP A CH2   1 
ATOM   890  N  N     . MET A 1 112 ? 132.332 158.104 143.295 1.00 22.73  ? 113  MET A N     1 
ATOM   891  C  CA    . MET A 1 112 ? 133.575 157.539 142.772 1.00 22.73  ? 113  MET A CA    1 
ATOM   892  C  C     . MET A 1 112 ? 134.669 157.804 143.797 1.00 22.73  ? 113  MET A C     1 
ATOM   893  O  O     . MET A 1 112 ? 135.162 158.924 143.923 1.00 22.73  ? 113  MET A O     1 
ATOM   894  C  CB    . MET A 1 112 ? 133.927 158.143 141.418 1.00 22.73  ? 113  MET A CB    1 
ATOM   895  C  CG    . MET A 1 112 ? 133.094 157.632 140.267 1.00 22.73  ? 113  MET A CG    1 
ATOM   896  S  SD    . MET A 1 112 ? 133.639 158.315 138.699 1.00 22.73  ? 113  MET A SD    1 
ATOM   897  C  CE    . MET A 1 112 ? 132.785 159.879 138.719 1.00 22.73  ? 113  MET A CE    1 
ATOM   898  N  N     . ILE A 1 113 ? 135.043 156.781 144.555 1.00 21.65  ? 114  ILE A N     1 
ATOM   899  C  CA    . ILE A 1 113 ? 135.888 157.002 145.723 1.00 21.65  ? 114  ILE A CA    1 
ATOM   900  C  C     . ILE A 1 113 ? 137.386 156.890 145.422 1.00 21.65  ? 114  ILE A C     1 
ATOM   901  O  O     . ILE A 1 113 ? 138.170 157.700 145.915 1.00 21.65  ? 114  ILE A O     1 
ATOM   902  C  CB    . ILE A 1 113 ? 135.424 156.078 146.870 1.00 21.65  ? 114  ILE A CB    1 
ATOM   903  C  CG1   . ILE A 1 113 ? 135.680 154.597 146.571 1.00 21.65  ? 114  ILE A CG1   1 
ATOM   904  C  CG2   . ILE A 1 113 ? 133.965 156.334 147.132 1.00 21.65  ? 114  ILE A CG2   1 
ATOM   905  C  CD1   . ILE A 1 113 ? 135.081 153.618 147.541 1.00 21.65  ? 114  ILE A CD1   1 
ATOM   906  N  N     . TYR A 1 114 ? 137.840 155.947 144.599 1.00 23.36  ? 115  TYR A N     1 
ATOM   907  C  CA    . TYR A 1 114 ? 139.269 155.803 144.350 1.00 23.36  ? 115  TYR A CA    1 
ATOM   908  C  C     . TYR A 1 114 ? 139.733 156.795 143.295 1.00 23.36  ? 115  TYR A C     1 
ATOM   909  O  O     . TYR A 1 114 ? 139.008 157.093 142.345 1.00 23.36  ? 115  TYR A O     1 
ATOM   910  C  CB    . TYR A 1 114 ? 139.578 154.384 143.887 1.00 23.36  ? 115  TYR A CB    1 
ATOM   911  C  CG    . TYR A 1 114 ? 139.245 153.313 144.897 1.00 23.36  ? 115  TYR A CG    1 
ATOM   912  C  CD1   . TYR A 1 114 ? 140.120 152.985 145.917 1.00 23.36  ? 115  TYR A CD1   1 
ATOM   913  C  CD2   . TYR A 1 114 ? 138.044 152.626 144.822 1.00 23.36  ? 115  TYR A CD2   1 
ATOM   914  C  CE1   . TYR A 1 114 ? 139.806 151.997 146.828 1.00 23.36  ? 115  TYR A CE1   1 
ATOM   915  C  CE2   . TYR A 1 114 ? 137.718 151.651 145.733 1.00 23.36  ? 115  TYR A CE2   1 
ATOM   916  C  CZ    . TYR A 1 114 ? 138.601 151.339 146.731 1.00 23.36  ? 115  TYR A CZ    1 
ATOM   917  O  OH    . TYR A 1 114 ? 138.266 150.367 147.638 1.00 23.36  ? 115  TYR A OH    1 
ATOM   918  N  N     . THR A 1 115 ? 140.955 157.301 143.456 1.00 22.43  ? 116  THR A N     1 
ATOM   919  C  CA    . THR A 1 115 ? 141.568 158.176 142.466 1.00 22.43  ? 116  THR A CA    1 
ATOM   920  C  C     . THR A 1 115 ? 143.065 157.914 142.465 1.00 22.43  ? 116  THR A C     1 
ATOM   921  O  O     . THR A 1 115 ? 143.651 157.726 143.530 1.00 22.43  ? 116  THR A O     1 
ATOM   922  C  CB    . THR A 1 115 ? 141.314 159.647 142.806 1.00 22.43  ? 116  THR A CB    1 
ATOM   923  O  OG1   . THR A 1 115 ? 139.939 159.840 143.141 1.00 22.43  ? 116  THR A OG1   1 
ATOM   924  C  CG2   . THR A 1 115 ? 141.646 160.533 141.642 1.00 22.43  ? 116  THR A CG2   1 
ATOM   925  N  N     . TYR A 1 116 ? 143.696 157.955 141.296 1.00 25.63  ? 117  TYR A N     1 
ATOM   926  C  CA    . TYR A 1 116 ? 145.147 157.876 141.296 1.00 25.63  ? 117  TYR A CA    1 
ATOM   927  C  C     . TYR A 1 116 ? 145.776 159.245 141.514 1.00 25.63  ? 117  TYR A C     1 
ATOM   928  O  O     . TYR A 1 116 ? 145.153 160.292 141.330 1.00 25.63  ? 117  TYR A O     1 
ATOM   929  C  CB    . TYR A 1 116 ? 145.699 157.280 140.006 1.00 25.63  ? 117  TYR A CB    1 
ATOM   930  C  CG    . TYR A 1 116 ? 145.170 155.927 139.625 1.00 25.63  ? 117  TYR A CG    1 
ATOM   931  C  CD1   . TYR A 1 116 ? 145.430 154.816 140.412 1.00 25.63  ? 117  TYR A CD1   1 
ATOM   932  C  CD2   . TYR A 1 116 ? 144.492 155.739 138.433 1.00 25.63  ? 117  TYR A CD2   1 
ATOM   933  C  CE1   . TYR A 1 116 ? 144.980 153.564 140.050 1.00 25.63  ? 117  TYR A CE1   1 
ATOM   934  C  CE2   . TYR A 1 116 ? 144.044 154.490 138.058 1.00 25.63  ? 117  TYR A CE2   1 
ATOM   935  C  CZ    . TYR A 1 116 ? 144.290 153.409 138.871 1.00 25.63  ? 117  TYR A CZ    1 
ATOM   936  O  OH    . TYR A 1 116 ? 143.827 152.171 138.504 1.00 25.63  ? 117  TYR A OH    1 
ATOM   937  N  N     . SER A 1 117 ? 147.031 159.215 141.948 1.00 22.59  ? 118  SER A N     1 
ATOM   938  C  CA    . SER A 1 117 ? 147.857 160.396 142.100 1.00 22.59  ? 118  SER A CA    1 
ATOM   939  C  C     . SER A 1 117 ? 149.243 160.080 141.545 1.00 22.59  ? 118  SER A C     1 
ATOM   940  O  O     . SER A 1 117 ? 150.254 160.150 142.233 1.00 22.59  ? 118  SER A O     1 
ATOM   941  C  CB    . SER A 1 117 ? 147.926 160.829 143.555 1.00 22.59  ? 118  SER A CB    1 
ATOM   942  O  OG    . SER A 1 117 ? 146.669 161.281 143.989 1.00 22.59  ? 118  SER A OG    1 
ATOM   943  N  N     . GLY A 1 118 ? 149.295 159.733 140.265 1.00 23.72  ? 119  GLY A N     1 
ATOM   944  C  CA    . GLY A 1 118 ? 150.514 159.218 139.682 1.00 23.72  ? 119  GLY A CA    1 
ATOM   945  C  C     . GLY A 1 118 ? 150.887 157.861 140.236 1.00 23.72  ? 119  GLY A C     1 
ATOM   946  O  O     . GLY A 1 118 ? 150.157 156.889 140.036 1.00 23.72  ? 119  GLY A O     1 
ATOM   947  N  N     . LEU A 1 119 ? 152.010 157.775 140.937 1.00 22.77  ? 120  LEU A N     1 
ATOM   948  C  CA    . LEU A 1 119 ? 152.543 156.493 141.380 1.00 22.77  ? 120  LEU A CA    1 
ATOM   949  C  C     . LEU A 1 119 ? 151.803 155.877 142.568 1.00 22.77  ? 120  LEU A C     1 
ATOM   950  O  O     . LEU A 1 119 ? 152.222 154.816 143.044 1.00 22.77  ? 120  LEU A O     1 
ATOM   951  C  CB    . LEU A 1 119 ? 154.023 156.651 141.721 1.00 22.77  ? 120  LEU A CB    1 
ATOM   952  C  CG    . LEU A 1 119 ? 154.904 157.003 140.525 1.00 22.77  ? 120  LEU A CG    1 
ATOM   953  C  CD1   . LEU A 1 119 ? 156.329 157.293 140.966 1.00 22.77  ? 120  LEU A CD1   1 
ATOM   954  C  CD2   . LEU A 1 119 ? 154.871 155.879 139.507 1.00 22.77  ? 120  LEU A CD2   1 
ATOM   955  N  N     . PHE A 1 120 ? 150.727 156.489 143.058 1.00 22.00  ? 121  PHE A N     1 
ATOM   956  C  CA    . PHE A 1 120 ? 149.974 155.940 144.181 1.00 22.00  ? 121  PHE A CA    1 
ATOM   957  C  C     . PHE A 1 120 ? 148.503 156.301 144.008 1.00 22.00  ? 121  PHE A C     1 
ATOM   958  O  O     . PHE A 1 120 ? 148.094 156.830 142.971 1.00 22.00  ? 121  PHE A O     1 
ATOM   959  C  CB    . PHE A 1 120 ? 150.581 156.402 145.514 1.00 22.00  ? 121  PHE A CB    1 
ATOM   960  C  CG    . PHE A 1 120 ? 150.550 157.888 145.737 1.00 22.00  ? 121  PHE A CG    1 
ATOM   961  C  CD1   . PHE A 1 120 ? 151.613 158.677 145.337 1.00 22.00  ? 121  PHE A CD1   1 
ATOM   962  C  CD2   . PHE A 1 120 ? 149.500 158.486 146.403 1.00 22.00  ? 121  PHE A CD2   1 
ATOM   963  C  CE1   . PHE A 1 120 ? 151.607 160.033 145.556 1.00 22.00  ? 121  PHE A CE1   1 
ATOM   964  C  CE2   . PHE A 1 120 ? 149.493 159.844 146.628 1.00 22.00  ? 121  PHE A CE2   1 
ATOM   965  C  CZ    . PHE A 1 120 ? 150.546 160.616 146.202 1.00 22.00  ? 121  PHE A CZ    1 
ATOM   966  N  N     . CYS A 1 121 ? 147.700 156.005 145.024 1.00 21.81  ? 122  CYS A N     1 
ATOM   967  C  CA    . CYS A 1 121 ? 146.260 156.196 144.971 1.00 21.81  ? 122  CYS A CA    1 
ATOM   968  C  C     . CYS A 1 121 ? 145.756 156.915 146.208 1.00 21.81  ? 122  CYS A C     1 
ATOM   969  O  O     . CYS A 1 121 ? 146.347 156.818 147.282 1.00 21.81  ? 122  CYS A O     1 
ATOM   970  C  CB    . CYS A 1 121 ? 145.563 154.863 144.849 1.00 21.81  ? 122  CYS A CB    1 
ATOM   971  S  SG    . CYS A 1 121 ? 143.772 154.873 144.960 1.00 21.81  ? 122  CYS A SG    1 
ATOM   972  N  N     . VAL A 1 122 ? 144.648 157.633 146.044 1.00 20.15  ? 123  VAL A N     1 
ATOM   973  C  CA    . VAL A 1 122 ? 143.948 158.298 147.138 1.00 20.15  ? 123  VAL A CA    1 
ATOM   974  C  C     . VAL A 1 122 ? 142.561 157.689 147.274 1.00 20.15  ? 123  VAL A C     1 
ATOM   975  O  O     . VAL A 1 122 ? 141.814 157.623 146.294 1.00 20.15  ? 123  VAL A O     1 
ATOM   976  C  CB    . VAL A 1 122 ? 143.851 159.814 146.899 1.00 20.15  ? 123  VAL A CB    1 
ATOM   977  C  CG1   . VAL A 1 122 ? 143.063 160.469 147.996 1.00 20.15  ? 123  VAL A CG1   1 
ATOM   978  C  CG2   . VAL A 1 122 ? 145.226 160.418 146.828 1.00 20.15  ? 123  VAL A CG2   1 
ATOM   979  N  N     . THR A 1 123 ? 142.216 157.250 148.482 1.00 20.45  ? 124  THR A N     1 
ATOM   980  C  CA    . THR A 1 123 ? 140.945 156.578 148.749 1.00 20.45  ? 124  THR A CA    1 
ATOM   981  C  C     . THR A 1 123 ? 140.175 157.355 149.810 1.00 20.45  ? 124  THR A C     1 
ATOM   982  O  O     . THR A 1 123 ? 140.489 157.274 151.000 1.00 20.45  ? 124  THR A O     1 
ATOM   983  C  CB    . THR A 1 123 ? 141.175 155.143 149.204 1.00 20.45  ? 124  THR A CB    1 
ATOM   984  O  OG1   . THR A 1 123 ? 141.940 154.440 148.218 1.00 20.45  ? 124  THR A OG1   1 
ATOM   985  C  CG2   . THR A 1 123 ? 139.856 154.442 149.450 1.00 20.45  ? 124  THR A CG2   1 
ATOM   986  N  N     . VAL A 1 124 ? 139.174 158.122 149.383 1.00 19.54  ? 125  VAL A N     1 
ATOM   987  C  CA    . VAL A 1 124 ? 138.256 158.731 150.329 1.00 19.54  ? 125  VAL A CA    1 
ATOM   988  C  C     . VAL A 1 124 ? 137.362 157.627 150.895 1.00 19.54  ? 125  VAL A C     1 
ATOM   989  O  O     . VAL A 1 124 ? 137.151 156.591 150.257 1.00 19.54  ? 125  VAL A O     1 
ATOM   990  C  CB    . VAL A 1 124 ? 137.473 159.852 149.621 1.00 19.54  ? 125  VAL A CB    1 
ATOM   991  C  CG1   . VAL A 1 124 ? 136.642 160.660 150.582 1.00 19.54  ? 125  VAL A CG1   1 
ATOM   992  C  CG2   . VAL A 1 124 ? 138.429 160.753 148.884 1.00 19.54  ? 125  VAL A CG2   1 
ATOM   993  N  N     . ASN A 1 125 ? 136.879 157.813 152.129 1.00 22.76  ? 126  ASN A N     1 
ATOM   994  C  CA    . ASN A 1 125 ? 136.036 156.830 152.803 1.00 22.76  ? 126  ASN A CA    1 
ATOM   995  C  C     . ASN A 1 125 ? 134.559 157.150 152.578 1.00 22.76  ? 126  ASN A C     1 
ATOM   996  O  O     . ASN A 1 125 ? 134.077 158.173 153.079 1.00 22.76  ? 126  ASN A O     1 
ATOM   997  C  CB    . ASN A 1 125 ? 136.375 156.819 154.296 1.00 22.76  ? 126  ASN A CB    1 
ATOM   998  C  CG    . ASN A 1 125 ? 135.649 155.748 155.100 1.00 22.76  ? 126  ASN A CG    1 
ATOM   999  O  OD1   . ASN A 1 125 ? 134.749 155.067 154.628 1.00 22.76  ? 126  ASN A OD1   1 
ATOM   1000 N  ND2   . ASN A 1 125 ? 136.052 155.612 156.354 1.00 22.76  ? 126  ASN A ND2   1 
ATOM   1001 N  N     . PRO A 1 126 ? 133.809 156.311 151.874 1.00 24.24  ? 127  PRO A N     1 
ATOM   1002 C  CA    . PRO A 1 126 ? 132.346 156.390 151.930 1.00 24.24  ? 127  PRO A CA    1 
ATOM   1003 C  C     . PRO A 1 126 ? 131.736 155.599 153.089 1.00 24.24  ? 127  PRO A C     1 
ATOM   1004 O  O     . PRO A 1 126 ? 131.847 154.370 153.153 1.00 24.24  ? 127  PRO A O     1 
ATOM   1005 C  CB    . PRO A 1 126 ? 131.936 155.853 150.557 1.00 24.24  ? 127  PRO A CB    1 
ATOM   1006 C  CG    . PRO A 1 126 ? 132.950 154.802 150.275 1.00 24.24  ? 127  PRO A CG    1 
ATOM   1007 C  CD    . PRO A 1 126 ? 134.248 155.292 150.903 1.00 24.24  ? 127  PRO A CD    1 
ATOM   1008 N  N     . TYR A 1 127 ? 131.068 156.266 154.030 1.00 26.97  ? 128  TYR A N     1 
ATOM   1009 C  CA    . TYR A 1 127 ? 130.338 155.536 155.072 1.00 26.97  ? 128  TYR A CA    1 
ATOM   1010 C  C     . TYR A 1 127 ? 129.036 154.879 154.606 1.00 26.97  ? 128  TYR A C     1 
ATOM   1011 O  O     . TYR A 1 127 ? 128.005 154.981 155.277 1.00 26.97  ? 128  TYR A O     1 
ATOM   1012 C  CB    . TYR A 1 127 ? 130.073 156.448 156.269 1.00 26.97  ? 128  TYR A CB    1 
ATOM   1013 C  CG    . TYR A 1 127 ? 131.338 156.987 156.891 1.00 26.97  ? 128  TYR A CG    1 
ATOM   1014 C  CD1   . TYR A 1 127 ? 132.123 156.174 157.693 1.00 26.97  ? 128  TYR A CD1   1 
ATOM   1015 C  CD2   . TYR A 1 127 ? 131.735 158.299 156.704 1.00 26.97  ? 128  TYR A CD2   1 
ATOM   1016 C  CE1   . TYR A 1 127 ? 133.302 156.627 158.232 1.00 26.97  ? 128  TYR A CE1   1 
ATOM   1017 C  CE2   . TYR A 1 127 ? 132.894 158.776 157.283 1.00 26.97  ? 128  TYR A CE2   1 
ATOM   1018 C  CZ    . TYR A 1 127 ? 133.678 157.927 158.037 1.00 26.97  ? 128  TYR A CZ    1 
ATOM   1019 O  OH    . TYR A 1 127 ? 134.808 158.391 158.659 1.00 26.97  ? 128  TYR A OH    1 
ATOM   1020 N  N     . LYS A 1 128 ? 129.083 154.218 153.453 1.00 27.12  ? 129  LYS A N     1 
ATOM   1021 C  CA    . LYS A 1 128 ? 127.965 153.582 152.777 1.00 27.12  ? 129  LYS A CA    1 
ATOM   1022 C  C     . LYS A 1 128 ? 128.571 152.461 151.952 1.00 27.12  ? 129  LYS A C     1 
ATOM   1023 O  O     . LYS A 1 128 ? 129.501 152.708 151.182 1.00 27.12  ? 129  LYS A O     1 
ATOM   1024 C  CB    . LYS A 1 128 ? 127.209 154.563 151.877 1.00 27.12  ? 129  LYS A CB    1 
ATOM   1025 C  CG    . LYS A 1 128 ? 126.221 153.897 150.926 1.00 27.12  ? 129  LYS A CG    1 
ATOM   1026 C  CD    . LYS A 1 128 ? 125.510 154.911 150.036 1.00 27.12  ? 129  LYS A CD    1 
ATOM   1027 C  CE    . LYS A 1 128 ? 124.700 154.219 148.948 1.00 27.12  ? 129  LYS A CE    1 
ATOM   1028 N  NZ    . LYS A 1 128 ? 124.003 155.188 148.065 1.00 27.12  ? 129  LYS A NZ    1 
ATOM   1029 N  N     . TRP A 1 129 ? 128.071 151.242 152.128 1.00 28.05  ? 130  TRP A N     1 
ATOM   1030 C  CA    . TRP A 1 129 ? 128.554 150.125 151.328 1.00 28.05  ? 130  TRP A CA    1 
ATOM   1031 C  C     . TRP A 1 129 ? 128.128 150.270 149.876 1.00 28.05  ? 130  TRP A C     1 
ATOM   1032 O  O     . TRP A 1 129 ? 127.004 150.678 149.575 1.00 28.05  ? 130  TRP A O     1 
ATOM   1033 C  CB    . TRP A 1 129 ? 128.065 148.804 151.906 1.00 28.05  ? 130  TRP A CB    1 
ATOM   1034 C  CG    . TRP A 1 129 ? 128.688 148.511 153.225 1.00 28.05  ? 130  TRP A CG    1 
ATOM   1035 C  CD1   . TRP A 1 129 ? 128.137 148.695 154.457 1.00 28.05  ? 130  TRP A CD1   1 
ATOM   1036 C  CD2   . TRP A 1 129 ? 129.997 147.984 153.445 1.00 28.05  ? 130  TRP A CD2   1 
ATOM   1037 N  NE1   . TRP A 1 129 ? 129.023 148.311 155.433 1.00 28.05  ? 130  TRP A NE1   1 
ATOM   1038 C  CE2   . TRP A 1 129 ? 130.173 147.870 154.836 1.00 28.05  ? 130  TRP A CE2   1 
ATOM   1039 C  CE3   . TRP A 1 129 ? 131.037 147.593 152.599 1.00 28.05  ? 130  TRP A CE3   1 
ATOM   1040 C  CZ2   . TRP A 1 129 ? 131.343 147.386 155.399 1.00 28.05  ? 130  TRP A CZ2   1 
ATOM   1041 C  CZ3   . TRP A 1 129 ? 132.195 147.112 153.157 1.00 28.05  ? 130  TRP A CZ3   1 
ATOM   1042 C  CH2   . TRP A 1 129 ? 132.342 147.012 154.545 1.00 28.05  ? 130  TRP A CH2   1 
ATOM   1043 N  N     . LEU A 1 130 ? 129.042 149.932 148.974 1.00 26.74  ? 131  LEU A N     1 
ATOM   1044 C  CA    . LEU A 1 130 ? 128.824 150.102 147.554 1.00 26.74  ? 131  LEU A CA    1 
ATOM   1045 C  C     . LEU A 1 130 ? 128.964 148.775 146.817 1.00 26.74  ? 131  LEU A C     1 
ATOM   1046 O  O     . LEU A 1 130 ? 129.761 147.922 147.215 1.00 26.74  ? 131  LEU A O     1 
ATOM   1047 C  CB    . LEU A 1 130 ? 129.832 151.110 146.988 1.00 26.74  ? 131  LEU A CB    1 
ATOM   1048 C  CG    . LEU A 1 130 ? 129.790 152.553 147.477 1.00 26.74  ? 131  LEU A CG    1 
ATOM   1049 C  CD1   . LEU A 1 130 ? 130.890 153.330 146.809 1.00 26.74  ? 131  LEU A CD1   1 
ATOM   1050 C  CD2   . LEU A 1 130 ? 128.453 153.184 147.178 1.00 26.74  ? 131  LEU A CD2   1 
ATOM   1051 N  N     . PRO A 1 131 ? 128.208 148.575 145.731 1.00 27.46  ? 132  PRO A N     1 
ATOM   1052 C  CA    . PRO A 1 131 ? 128.306 147.323 144.963 1.00 27.46  ? 132  PRO A CA    1 
ATOM   1053 C  C     . PRO A 1 131 ? 129.584 147.161 144.152 1.00 27.46  ? 132  PRO A C     1 
ATOM   1054 O  O     . PRO A 1 131 ? 129.718 146.160 143.444 1.00 27.46  ? 132  PRO A O     1 
ATOM   1055 C  CB    . PRO A 1 131 ? 127.082 147.391 144.045 1.00 27.46  ? 132  PRO A CB    1 
ATOM   1056 C  CG    . PRO A 1 131 ? 126.829 148.834 143.880 1.00 27.46  ? 132  PRO A CG    1 
ATOM   1057 C  CD    . PRO A 1 131 ? 127.151 149.453 145.198 1.00 27.46  ? 132  PRO A CD    1 
ATOM   1058 N  N     . VAL A 1 132 ? 130.515 148.109 144.206 1.00 25.81  ? 133  VAL A N     1 
ATOM   1059 C  CA    . VAL A 1 132 ? 131.768 148.112 143.455 1.00 25.81  ? 133  VAL A CA    1 
ATOM   1060 C  C     . VAL A 1 132 ? 132.738 146.986 143.849 1.00 25.81  ? 133  VAL A C     1 
ATOM   1061 O  O     . VAL A 1 132 ? 133.764 146.776 143.194 1.00 25.81  ? 133  VAL A O     1 
ATOM   1062 C  CB    . VAL A 1 132 ? 132.413 149.503 143.639 1.00 25.81  ? 133  VAL A CB    1 
ATOM   1063 C  CG1   . VAL A 1 132 ? 133.391 149.835 142.559 1.00 25.81  ? 133  VAL A CG1   1 
ATOM   1064 C  CG2   . VAL A 1 132 ? 131.363 150.565 143.698 1.00 25.81  ? 133  VAL A CG2   1 
ATOM   1065 N  N     . TYR A 1 133 ? 132.399 146.190 144.860 1.00 25.70  ? 134  TYR A N     1 
ATOM   1066 C  CA    . TYR A 1 133 ? 133.238 145.068 145.261 1.00 25.70  ? 134  TYR A CA    1 
ATOM   1067 C  C     . TYR A 1 133 ? 132.637 143.700 144.963 1.00 25.70  ? 134  TYR A C     1 
ATOM   1068 O  O     . TYR A 1 133 ? 133.106 142.708 145.531 1.00 25.70  ? 134  TYR A O     1 
ATOM   1069 C  CB    . TYR A 1 133 ? 133.588 145.160 146.744 1.00 25.70  ? 134  TYR A CB    1 
ATOM   1070 C  CG    . TYR A 1 133 ? 134.198 146.471 147.164 1.00 25.70  ? 134  TYR A CG    1 
ATOM   1071 C  CD1   . TYR A 1 133 ? 135.378 146.914 146.590 1.00 25.70  ? 134  TYR A CD1   1 
ATOM   1072 C  CD2   . TYR A 1 133 ? 133.624 147.240 148.165 1.00 25.70  ? 134  TYR A CD2   1 
ATOM   1073 C  CE1   . TYR A 1 133 ? 135.958 148.096 146.980 1.00 25.70  ? 134  TYR A CE1   1 
ATOM   1074 C  CE2   . TYR A 1 133 ? 134.196 148.428 148.558 1.00 25.70  ? 134  TYR A CE2   1 
ATOM   1075 C  CZ    . TYR A 1 133 ? 135.364 148.850 147.959 1.00 25.70  ? 134  TYR A CZ    1 
ATOM   1076 O  OH    . TYR A 1 133 ? 135.953 150.031 148.338 1.00 25.70  ? 134  TYR A OH    1 
ATOM   1077 N  N     . THR A 1 134 ? 131.573 143.630 144.159 1.00 31.29  ? 135  THR A N     1 
ATOM   1078 C  CA    . THR A 1 134 ? 130.976 142.354 143.775 1.00 31.29  ? 135  THR A CA    1 
ATOM   1079 C  C     . THR A 1 134 ? 131.994 141.475 143.037 1.00 31.29  ? 135  THR A C     1 
ATOM   1080 O  O     . THR A 1 134 ? 132.890 141.992 142.366 1.00 31.29  ? 135  THR A O     1 
ATOM   1081 C  CB    . THR A 1 134 ? 129.741 142.605 142.901 1.00 31.29  ? 135  THR A CB    1 
ATOM   1082 O  OG1   . THR A 1 134 ? 130.023 143.616 141.930 1.00 31.29  ? 135  THR A OG1   1 
ATOM   1083 C  CG2   . THR A 1 134 ? 128.553 143.029 143.750 1.00 31.29  ? 135  THR A CG2   1 
ATOM   1084 N  N     . PRO A 1 135 ? 131.895 140.142 143.163 1.00 32.96  ? 136  PRO A N     1 
ATOM   1085 C  CA    . PRO A 1 135 ? 132.991 139.273 142.693 1.00 32.96  ? 136  PRO A CA    1 
ATOM   1086 C  C     . PRO A 1 135 ? 133.139 139.179 141.182 1.00 32.96  ? 136  PRO A C     1 
ATOM   1087 O  O     . PRO A 1 135 ? 134.199 138.745 140.715 1.00 32.96  ? 136  PRO A O     1 
ATOM   1088 C  CB    . PRO A 1 135 ? 132.641 137.910 143.299 1.00 32.96  ? 136  PRO A CB    1 
ATOM   1089 C  CG    . PRO A 1 135 ? 131.186 137.946 143.465 1.00 32.96  ? 136  PRO A CG    1 
ATOM   1090 C  CD    . PRO A 1 135 ? 130.864 139.349 143.858 1.00 32.96  ? 136  PRO A CD    1 
ATOM   1091 N  N     . GLU A 1 136 ? 132.114 139.535 140.405 1.00 38.03  ? 137  GLU A N     1 
ATOM   1092 C  CA    . GLU A 1 136 ? 132.274 139.613 138.955 1.00 38.03  ? 137  GLU A CA    1 
ATOM   1093 C  C     . GLU A 1 136 ? 133.185 140.769 138.545 1.00 38.03  ? 137  GLU A C     1 
ATOM   1094 O  O     . GLU A 1 136 ? 133.862 140.682 137.514 1.00 38.03  ? 137  GLU A O     1 
ATOM   1095 C  CB    . GLU A 1 136 ? 130.883 139.727 138.311 1.00 38.03  ? 137  GLU A CB    1 
ATOM   1096 C  CG    . GLU A 1 136 ? 130.790 139.761 136.774 1.00 38.03  ? 137  GLU A CG    1 
ATOM   1097 C  CD    . GLU A 1 136 ? 131.015 141.131 136.159 1.00 38.03  ? 137  GLU A CD    1 
ATOM   1098 O  OE1   . GLU A 1 136 ? 130.659 142.137 136.804 1.00 38.03  ? 137  GLU A OE1   1 
ATOM   1099 O  OE2   . GLU A 1 136 ? 131.542 141.194 135.029 1.00 38.03  ? 137  GLU A OE2   1 
ATOM   1100 N  N     . VAL A 1 137 ? 133.228 141.841 139.340 1.00 34.05  ? 138  VAL A N     1 
ATOM   1101 C  CA    . VAL A 1 137 ? 134.091 142.986 139.050 1.00 34.05  ? 138  VAL A CA    1 
ATOM   1102 C  C     . VAL A 1 137 ? 135.568 142.617 139.217 1.00 34.05  ? 138  VAL A C     1 
ATOM   1103 O  O     . VAL A 1 137 ? 136.441 143.192 138.551 1.00 34.05  ? 138  VAL A O     1 
ATOM   1104 C  CB    . VAL A 1 137 ? 133.654 144.170 139.940 1.00 34.05  ? 138  VAL A CB    1 
ATOM   1105 C  CG1   . VAL A 1 137 ? 134.508 145.412 139.741 1.00 34.05  ? 138  VAL A CG1   1 
ATOM   1106 C  CG2   . VAL A 1 137 ? 132.215 144.507 139.654 1.00 34.05  ? 138  VAL A CG2   1 
ATOM   1107 N  N     . VAL A 1 138 ? 135.868 141.628 140.067 1.00 33.78  ? 139  VAL A N     1 
ATOM   1108 C  CA    . VAL A 1 138 ? 137.214 141.059 140.143 1.00 33.78  ? 139  VAL A CA    1 
ATOM   1109 C  C     . VAL A 1 138 ? 137.619 140.425 138.816 1.00 33.78  ? 139  VAL A C     1 
ATOM   1110 O  O     . VAL A 1 138 ? 138.754 140.593 138.352 1.00 33.78  ? 139  VAL A O     1 
ATOM   1111 C  CB    . VAL A 1 138 ? 137.286 140.040 141.297 1.00 33.78  ? 139  VAL A CB    1 
ATOM   1112 C  CG1   . VAL A 1 138 ? 138.611 139.287 141.295 1.00 33.78  ? 139  VAL A CG1   1 
ATOM   1113 C  CG2   . VAL A 1 138 ? 137.056 140.720 142.625 1.00 33.78  ? 139  VAL A CG2   1 
ATOM   1114 N  N     . ALA A 1 139 ? 136.692 139.719 138.165 1.00 33.59  ? 140  ALA A N     1 
ATOM   1115 C  CA    . ALA A 1 139 ? 136.987 139.146 136.855 1.00 33.59  ? 140  ALA A CA    1 
ATOM   1116 C  C     . ALA A 1 139 ? 137.120 140.224 135.786 1.00 33.59  ? 140  ALA A C     1 
ATOM   1117 O  O     . ALA A 1 139 ? 137.938 140.096 134.868 1.00 33.59  ? 140  ALA A O     1 
ATOM   1118 C  CB    . ALA A 1 139 ? 135.901 138.144 136.469 1.00 33.59  ? 140  ALA A CB    1 
ATOM   1119 N  N     . ALA A 1 140 ? 136.309 141.278 135.880 1.00 35.63  ? 141  ALA A N     1 
ATOM   1120 C  CA    . ALA A 1 140 ? 136.422 142.411 134.966 1.00 35.63  ? 141  ALA A CA    1 
ATOM   1121 C  C     . ALA A 1 140 ? 137.743 143.152 135.114 1.00 35.63  ? 141  ALA A C     1 
ATOM   1122 O  O     . ALA A 1 140 ? 138.283 143.653 134.124 1.00 35.63  ? 141  ALA A O     1 
ATOM   1123 C  CB    . ALA A 1 140 ? 135.259 143.375 135.184 1.00 35.63  ? 141  ALA A CB    1 
ATOM   1124 N  N     . TYR A 1 141 ? 138.279 143.234 136.329 1.00 33.78  ? 142  TYR A N     1 
ATOM   1125 C  CA    . TYR A 1 141 ? 139.546 143.920 136.556 1.00 33.78  ? 142  TYR A CA    1 
ATOM   1126 C  C     . TYR A 1 141 ? 140.784 143.121 136.181 1.00 33.78  ? 142  TYR A C     1 
ATOM   1127 O  O     . TYR A 1 141 ? 141.853 143.731 136.086 1.00 33.78  ? 142  TYR A O     1 
ATOM   1128 C  CB    . TYR A 1 141 ? 139.640 144.376 138.007 1.00 33.78  ? 142  TYR A CB    1 
ATOM   1129 C  CG    . TYR A 1 141 ? 139.211 145.803 138.147 1.00 33.78  ? 142  TYR A CG    1 
ATOM   1130 C  CD1   . TYR A 1 141 ? 140.068 146.828 137.794 1.00 33.78  ? 142  TYR A CD1   1 
ATOM   1131 C  CD2   . TYR A 1 141 ? 137.933 146.129 138.562 1.00 33.78  ? 142  TYR A CD2   1 
ATOM   1132 C  CE1   . TYR A 1 141 ? 139.685 148.135 137.898 1.00 33.78  ? 142  TYR A CE1   1 
ATOM   1133 C  CE2   . TYR A 1 141 ? 137.538 147.443 138.665 1.00 33.78  ? 142  TYR A CE2   1 
ATOM   1134 C  CZ    . TYR A 1 141 ? 138.421 148.439 138.325 1.00 33.78  ? 142  TYR A CZ    1 
ATOM   1135 O  OH    . TYR A 1 141 ? 138.044 149.752 138.416 1.00 33.78  ? 142  TYR A OH    1 
ATOM   1136 N  N     . ARG A 1 142 ? 140.684 141.790 136.079 1.00 34.64  ? 143  ARG A N     1 
ATOM   1137 C  CA    . ARG A 1 142 ? 141.838 140.911 135.871 1.00 34.64  ? 143  ARG A CA    1 
ATOM   1138 C  C     . ARG A 1 142 ? 142.672 141.304 134.655 1.00 34.64  ? 143  ARG A C     1 
ATOM   1139 O  O     . ARG A 1 142 ? 142.152 141.455 133.547 1.00 34.64  ? 143  ARG A O     1 
ATOM   1140 C  CB    . ARG A 1 142 ? 141.382 139.460 135.734 1.00 34.64  ? 143  ARG A CB    1 
ATOM   1141 C  CG    . ARG A 1 142 ? 142.540 138.486 135.746 1.00 34.64  ? 143  ARG A CG    1 
ATOM   1142 C  CD    . ARG A 1 142 ? 142.079 137.050 135.662 1.00 34.64  ? 143  ARG A CD    1 
ATOM   1143 N  NE    . ARG A 1 142 ? 143.198 136.130 135.842 1.00 34.64  ? 143  ARG A NE    1 
ATOM   1144 C  CZ    . ARG A 1 142 ? 143.068 134.826 136.057 1.00 34.64  ? 143  ARG A CZ    1 
ATOM   1145 N  NH1   . ARG A 1 142 ? 144.146 134.072 136.228 1.00 34.64  ? 143  ARG A NH1   1 
ATOM   1146 N  NH2   . ARG A 1 142 ? 141.862 134.278 136.121 1.00 34.64  ? 143  ARG A NH2   1 
ATOM   1147 N  N     . GLY A 1 143 ? 143.971 141.481 134.883 1.00 34.42  ? 144  GLY A N     1 
ATOM   1148 C  CA    . GLY A 1 143 ? 144.965 141.666 133.844 1.00 34.42  ? 144  GLY A CA    1 
ATOM   1149 C  C     . GLY A 1 143 ? 144.953 143.001 133.132 1.00 34.42  ? 144  GLY A C     1 
ATOM   1150 O  O     . GLY A 1 143 ? 145.750 143.191 132.207 1.00 34.42  ? 144  GLY A O     1 
ATOM   1151 N  N     . LYS A 1 144 ? 144.089 143.933 133.521 1.00 35.95  ? 145  LYS A N     1 
ATOM   1152 C  CA    . LYS A 1 144 ? 144.050 145.235 132.875 1.00 35.95  ? 145  LYS A CA    1 
ATOM   1153 C  C     . LYS A 1 144 ? 145.139 146.151 133.423 1.00 35.95  ? 145  LYS A C     1 
ATOM   1154 O  O     . LYS A 1 144 ? 145.585 146.008 134.564 1.00 35.95  ? 145  LYS A O     1 
ATOM   1155 C  CB    . LYS A 1 144 ? 142.680 145.884 133.059 1.00 35.95  ? 145  LYS A CB    1 
ATOM   1156 C  CG    . LYS A 1 144 ? 141.571 145.153 132.331 1.00 35.95  ? 145  LYS A CG    1 
ATOM   1157 C  CD    . LYS A 1 144 ? 140.311 145.990 132.241 1.00 35.95  ? 145  LYS A CD    1 
ATOM   1158 C  CE    . LYS A 1 144 ? 139.251 145.271 131.429 1.00 35.95  ? 145  LYS A CE    1 
ATOM   1159 N  NZ    . LYS A 1 144 ? 139.719 144.999 130.045 1.00 35.95  ? 145  LYS A NZ    1 
ATOM   1160 N  N     . LYS A 1 145 ? 145.567 147.096 132.590 1.00 37.61  ? 146  LYS A N     1 
ATOM   1161 C  CA    . LYS A 1 145 ? 146.488 148.139 133.019 1.00 37.61  ? 146  LYS A CA    1 
ATOM   1162 C  C     . LYS A 1 145 ? 145.746 149.257 133.740 1.00 37.61  ? 146  LYS A C     1 
ATOM   1163 O  O     . LYS A 1 145 ? 144.553 149.485 133.519 1.00 37.61  ? 146  LYS A O     1 
ATOM   1164 C  CB    . LYS A 1 145 ? 147.277 148.717 131.839 1.00 37.61  ? 146  LYS A CB    1 
ATOM   1165 C  CG    . LYS A 1 145 ? 148.036 147.717 130.950 1.00 37.61  ? 146  LYS A CG    1 
ATOM   1166 C  CD    . LYS A 1 145 ? 148.886 146.680 131.694 1.00 37.61  ? 146  LYS A CD    1 
ATOM   1167 C  CE    . LYS A 1 145 ? 149.962 147.301 132.596 1.00 37.61  ? 146  LYS A CE    1 
ATOM   1168 N  NZ    . LYS A 1 145 ? 150.996 148.027 131.809 1.00 37.61  ? 146  LYS A NZ    1 
ATOM   1169 N  N     . ARG A 1 146 ? 146.472 149.945 134.628 1.00 34.32  ? 147  ARG A N     1 
ATOM   1170 C  CA    . ARG A 1 146 ? 145.968 151.144 135.294 1.00 34.32  ? 147  ARG A CA    1 
ATOM   1171 C  C     . ARG A 1 146 ? 145.573 152.262 134.333 1.00 34.32  ? 147  ARG A C     1 
ATOM   1172 O  O     . ARG A 1 146 ? 144.765 153.120 134.705 1.00 34.32  ? 147  ARG A O     1 
ATOM   1173 C  CB    . ARG A 1 146 ? 147.024 151.678 136.266 1.00 34.32  ? 147  ARG A CB    1 
ATOM   1174 C  CG    . ARG A 1 146 ? 147.234 150.840 137.516 1.00 34.32  ? 147  ARG A CG    1 
ATOM   1175 C  CD    . ARG A 1 146 ? 148.308 151.449 138.411 1.00 34.32  ? 147  ARG A CD    1 
ATOM   1176 N  NE    . ARG A 1 146 ? 147.984 152.801 138.850 1.00 34.32  ? 147  ARG A NE    1 
ATOM   1177 C  CZ    . ARG A 1 146 ? 148.896 153.733 139.093 1.00 34.32  ? 147  ARG A CZ    1 
ATOM   1178 N  NH1   . ARG A 1 146 ? 148.532 154.969 139.393 1.00 34.32  ? 147  ARG A NH1   1 
ATOM   1179 N  NH2   . ARG A 1 146 ? 150.181 153.441 138.971 1.00 34.32  ? 147  ARG A NH2   1 
ATOM   1180 N  N     . SER A 1 147 ? 146.111 152.280 133.113 1.00 39.29  ? 148  SER A N     1 
ATOM   1181 C  CA    . SER A 1 147 ? 145.682 153.258 132.124 1.00 39.29  ? 148  SER A CA    1 
ATOM   1182 C  C     . SER A 1 147 ? 144.345 152.915 131.474 1.00 39.29  ? 148  SER A C     1 
ATOM   1183 O  O     . SER A 1 147 ? 143.697 153.810 130.923 1.00 39.29  ? 148  SER A O     1 
ATOM   1184 C  CB    . SER A 1 147 ? 146.756 153.403 131.047 1.00 39.29  ? 148  SER A CB    1 
ATOM   1185 O  OG    . SER A 1 147 ? 148.031 153.609 131.631 1.00 39.29  ? 148  SER A OG    1 
ATOM   1186 N  N     . GLU A 1 148 ? 143.911 151.656 131.535 1.00 41.64  ? 149  GLU A N     1 
ATOM   1187 C  CA    . GLU A 1 148 ? 142.683 151.228 130.867 1.00 41.64  ? 149  GLU A CA    1 
ATOM   1188 C  C     . GLU A 1 148 ? 141.470 151.297 131.789 1.00 41.64  ? 149  GLU A C     1 
ATOM   1189 O  O     . GLU A 1 148 ? 140.508 152.020 131.516 1.00 41.64  ? 149  GLU A O     1 
ATOM   1190 C  CB    . GLU A 1 148 ? 142.814 149.802 130.323 1.00 41.64  ? 149  GLU A CB    1 
ATOM   1191 C  CG    . GLU A 1 148 ? 144.055 149.510 129.516 1.00 41.64  ? 149  GLU A CG    1 
ATOM   1192 C  CD    . GLU A 1 148 ? 144.152 148.041 129.155 1.00 41.64  ? 149  GLU A CD    1 
ATOM   1193 O  OE1   . GLU A 1 148 ? 143.242 147.539 128.461 1.00 41.64  ? 149  GLU A OE1   1 
ATOM   1194 O  OE2   . GLU A 1 148 ? 145.127 147.383 129.563 1.00 41.64  ? 149  GLU A OE2   1 
ATOM   1195 N  N     . ALA A 1 149 ? 141.512 150.550 132.874 1.00 38.81  ? 150  ALA A N     1 
ATOM   1196 C  CA    . ALA A 1 149 ? 140.438 150.440 133.842 1.00 38.81  ? 150  ALA A CA    1 
ATOM   1197 C  C     . ALA A 1 149 ? 140.424 151.648 134.785 1.00 38.81  ? 150  ALA A C     1 
ATOM   1198 O  O     . ALA A 1 149 ? 141.468 152.258 135.031 1.00 38.81  ? 150  ALA A O     1 
ATOM   1199 C  CB    . ALA A 1 149 ? 140.624 149.145 134.632 1.00 38.81  ? 150  ALA A CB    1 
ATOM   1200 N  N     . PRO A 1 150 ? 139.255 152.024 135.312 1.00 33.49  ? 151  PRO A N     1 
ATOM   1201 C  CA    . PRO A 1 150 ? 139.183 153.164 136.234 1.00 33.49  ? 151  PRO A CA    1 
ATOM   1202 C  C     . PRO A 1 150 ? 139.823 152.839 137.572 1.00 33.49  ? 151  PRO A C     1 
ATOM   1203 O  O     . PRO A 1 150 ? 140.022 151.655 137.880 1.00 33.49  ? 151  PRO A O     1 
ATOM   1204 C  CB    . PRO A 1 150 ? 137.670 153.395 136.368 1.00 33.49  ? 151  PRO A CB    1 
ATOM   1205 C  CG    . PRO A 1 150 ? 137.056 152.127 136.085 1.00 33.49  ? 151  PRO A CG    1 
ATOM   1206 C  CD    . PRO A 1 150 ? 137.923 151.431 135.092 1.00 33.49  ? 151  PRO A CD    1 
ATOM   1207 N  N     . PRO A 1 151 ? 140.190 153.853 138.373 1.00 28.05  ? 152  PRO A N     1 
ATOM   1208 C  CA    . PRO A 1 151 ? 140.886 153.587 139.642 1.00 28.05  ? 152  PRO A CA    1 
ATOM   1209 C  C     . PRO A 1 151 ? 140.029 152.830 140.638 1.00 28.05  ? 152  PRO A C     1 
ATOM   1210 O  O     . PRO A 1 151 ? 138.872 153.182 140.880 1.00 28.05  ? 152  PRO A O     1 
ATOM   1211 C  CB    . PRO A 1 151 ? 141.232 154.988 140.156 1.00 28.05  ? 152  PRO A CB    1 
ATOM   1212 C  CG    . PRO A 1 151 ? 140.287 155.885 139.493 1.00 28.05  ? 152  PRO A CG    1 
ATOM   1213 C  CD    . PRO A 1 151 ? 140.059 155.304 138.146 1.00 28.05  ? 152  PRO A CD    1 
ATOM   1214 N  N     . HIS A 1 152 ? 140.627 151.804 141.239 1.00 26.99  ? 153  HIS A N     1 
ATOM   1215 C  CA    . HIS A 1 152 ? 139.957 150.953 142.206 1.00 26.99  ? 153  HIS A CA    1 
ATOM   1216 C  C     . HIS A 1 152 ? 141.041 150.139 142.898 1.00 26.99  ? 153  HIS A C     1 
ATOM   1217 O  O     . HIS A 1 152 ? 142.135 149.965 142.356 1.00 26.99  ? 153  HIS A O     1 
ATOM   1218 C  CB    . HIS A 1 152 ? 138.930 150.057 141.509 1.00 26.99  ? 153  HIS A CB    1 
ATOM   1219 C  CG    . HIS A 1 152 ? 138.006 149.342 142.433 1.00 26.99  ? 153  HIS A CG    1 
ATOM   1220 N  ND1   . HIS A 1 152 ? 138.276 148.101 142.964 1.00 26.99  ? 153  HIS A ND1   1 
ATOM   1221 C  CD2   . HIS A 1 152 ? 136.810 149.715 142.938 1.00 26.99  ? 153  HIS A CD2   1 
ATOM   1222 C  CE1   . HIS A 1 152 ? 137.276 147.735 143.744 1.00 26.99  ? 153  HIS A CE1   1 
ATOM   1223 N  NE2   . HIS A 1 152 ? 136.372 148.696 143.743 1.00 26.99  ? 153  HIS A NE2   1 
ATOM   1224 N  N     . ILE A 1 153 ? 140.741 149.689 144.122 1.00 25.21  ? 154  ILE A N     1 
ATOM   1225 C  CA    . ILE A 1 153 ? 141.676 148.873 144.900 1.00 25.21  ? 154  ILE A CA    1 
ATOM   1226 C  C     . ILE A 1 153 ? 142.038 147.580 144.168 1.00 25.21  ? 154  ILE A C     1 
ATOM   1227 O  O     . ILE A 1 153 ? 143.167 147.088 144.291 1.00 25.21  ? 154  ILE A O     1 
ATOM   1228 C  CB    . ILE A 1 153 ? 141.123 148.627 146.325 1.00 25.21  ? 154  ILE A CB    1 
ATOM   1229 C  CG1   . ILE A 1 153 ? 142.166 147.960 147.218 1.00 25.21  ? 154  ILE A CG1   1 
ATOM   1230 C  CG2   . ILE A 1 153 ? 139.848 147.808 146.328 1.00 25.21  ? 154  ILE A CG2   1 
ATOM   1231 C  CD1   . ILE A 1 153 ? 143.375 148.804 147.479 1.00 25.21  ? 154  ILE A CD1   1 
ATOM   1232 N  N     . PHE A 1 154 ? 141.095 147.002 143.417 1.00 25.52  ? 155  PHE A N     1 
ATOM   1233 C  CA    . PHE A 1 154 ? 141.394 145.838 142.588 1.00 25.52  ? 155  PHE A CA    1 
ATOM   1234 C  C     . PHE A 1 154 ? 142.440 146.139 141.521 1.00 25.52  ? 155  PHE A C     1 
ATOM   1235 O  O     . PHE A 1 154 ? 143.243 145.263 141.184 1.00 25.52  ? 155  PHE A O     1 
ATOM   1236 C  CB    . PHE A 1 154 ? 140.119 145.309 141.929 1.00 25.52  ? 155  PHE A CB    1 
ATOM   1237 C  CG    . PHE A 1 154 ? 139.079 144.795 142.891 1.00 25.52  ? 155  PHE A CG    1 
ATOM   1238 C  CD1   . PHE A 1 154 ? 139.404 144.428 144.182 1.00 25.52  ? 155  PHE A CD1   1 
ATOM   1239 C  CD2   . PHE A 1 154 ? 137.766 144.672 142.483 1.00 25.52  ? 155  PHE A CD2   1 
ATOM   1240 C  CE1   . PHE A 1 154 ? 138.440 143.957 145.041 1.00 25.52  ? 155  PHE A CE1   1 
ATOM   1241 C  CE2   . PHE A 1 154 ? 136.801 144.215 143.345 1.00 25.52  ? 155  PHE A CE2   1 
ATOM   1242 C  CZ    . PHE A 1 154 ? 137.139 143.850 144.621 1.00 25.52  ? 155  PHE A CZ    1 
ATOM   1243 N  N     . SER A 1 155 ? 142.455 147.365 140.991 1.00 28.17  ? 156  SER A N     1 
ATOM   1244 C  CA    . SER A 1 155 ? 143.428 147.738 139.967 1.00 28.17  ? 156  SER A CA    1 
ATOM   1245 C  C     . SER A 1 155 ? 144.845 147.836 140.518 1.00 28.17  ? 156  SER A C     1 
ATOM   1246 O  O     . SER A 1 155 ? 145.807 147.544 139.801 1.00 28.17  ? 156  SER A O     1 
ATOM   1247 C  CB    . SER A 1 155 ? 143.029 149.056 139.315 1.00 28.17  ? 156  SER A CB    1 
ATOM   1248 O  OG    . SER A 1 155 ? 143.983 149.446 138.348 1.00 28.17  ? 156  SER A OG    1 
ATOM   1249 N  N     . ILE A 1 156 ? 144.994 148.259 141.772 1.00 27.12  ? 157  ILE A N     1 
ATOM   1250 C  CA    . ILE A 1 156 ? 146.315 148.452 142.361 1.00 27.12  ? 157  ILE A CA    1 
ATOM   1251 C  C     . ILE A 1 156 ? 146.934 147.116 142.741 1.00 27.12  ? 157  ILE A C     1 
ATOM   1252 O  O     . ILE A 1 156 ? 148.135 146.900 142.552 1.00 27.12  ? 157  ILE A O     1 
ATOM   1253 C  CB    . ILE A 1 156 ? 146.173 149.373 143.581 1.00 27.12  ? 157  ILE A CB    1 
ATOM   1254 C  CG1   . ILE A 1 156 ? 145.604 150.707 143.144 1.00 27.12  ? 157  ILE A CG1   1 
ATOM   1255 C  CG2   . ILE A 1 156 ? 147.511 149.621 144.228 1.00 27.12  ? 157  ILE A CG2   1 
ATOM   1256 C  CD1   . ILE A 1 156 ? 144.913 151.388 144.244 1.00 27.12  ? 157  ILE A CD1   1 
ATOM   1257 N  N     . SER A 1 157 ? 146.123 146.214 143.296 1.00 25.47  ? 158  SER A N     1 
ATOM   1258 C  CA    . SER A 1 157 ? 146.533 144.829 143.497 1.00 25.47  ? 158  SER A CA    1 
ATOM   1259 C  C     . SER A 1 157 ? 146.912 144.163 142.182 1.00 25.47  ? 158  SER A C     1 
ATOM   1260 O  O     . SER A 1 157 ? 147.917 143.447 142.105 1.00 25.47  ? 158  SER A O     1 
ATOM   1261 C  CB    . SER A 1 157 ? 145.412 144.059 144.178 1.00 25.47  ? 158  SER A CB    1 
ATOM   1262 O  OG    . SER A 1 157 ? 144.183 144.324 143.533 1.00 25.47  ? 158  SER A OG    1 
ATOM   1263 N  N     . ASP A 1 158 ? 146.092 144.366 141.143 1.00 29.09  ? 159  ASP A N     1 
ATOM   1264 C  CA    . ASP A 1 158 ? 146.362 143.775 139.833 1.00 29.09  ? 159  ASP A CA    1 
ATOM   1265 C  C     . ASP A 1 158 ? 147.635 144.330 139.212 1.00 29.09  ? 159  ASP A C     1 
ATOM   1266 O  O     . ASP A 1 158 ? 148.414 143.577 138.616 1.00 29.09  ? 159  ASP A O     1 
ATOM   1267 C  CB    . ASP A 1 158 ? 145.183 144.014 138.895 1.00 29.09  ? 159  ASP A CB    1 
ATOM   1268 C  CG    . ASP A 1 158 ? 145.281 143.202 137.632 1.00 29.09  ? 159  ASP A CG    1 
ATOM   1269 O  OD1   . ASP A 1 158 ? 145.976 142.167 137.644 1.00 29.09  ? 159  ASP A OD1   1 
ATOM   1270 O  OD2   . ASP A 1 158 ? 144.679 143.606 136.619 1.00 29.09  ? 159  ASP A OD2   1 
ATOM   1271 N  N     . ASN A 1 159 ? 147.841 145.647 139.306 1.00 29.21  ? 160  ASN A N     1 
ATOM   1272 C  CA    . ASN A 1 159 ? 149.073 146.250 138.810 1.00 29.21  ? 160  ASN A CA    1 
ATOM   1273 C  C     . ASN A 1 159 ? 150.285 145.745 139.580 1.00 29.21  ? 160  ASN A C     1 
ATOM   1274 O  O     . ASN A 1 159 ? 151.349 145.519 138.994 1.00 29.21  ? 160  ASN A O     1 
ATOM   1275 C  CB    . ASN A 1 159 ? 148.987 147.769 138.888 1.00 29.21  ? 160  ASN A CB    1 
ATOM   1276 C  CG    . ASN A 1 159 ? 150.119 148.447 138.159 1.00 29.21  ? 160  ASN A CG    1 
ATOM   1277 O  OD1   . ASN A 1 159 ? 150.063 148.640 136.947 1.00 29.21  ? 160  ASN A OD1   1 
ATOM   1278 N  ND2   . ASN A 1 159 ? 151.162 148.807 138.891 1.00 29.21  ? 160  ASN A ND2   1 
ATOM   1279 N  N     . ALA A 1 160 ? 150.151 145.599 140.901 1.00 27.37  ? 161  ALA A N     1 
ATOM   1280 C  CA    . ALA A 1 160 ? 151.212 145.000 141.705 1.00 27.37  ? 161  ALA A CA    1 
ATOM   1281 C  C     . ALA A 1 160 ? 151.471 143.556 141.302 1.00 27.37  ? 161  ALA A C     1 
ATOM   1282 O  O     . ALA A 1 160 ? 152.621 143.108 141.287 1.00 27.37  ? 161  ALA A O     1 
ATOM   1283 C  CB    . ALA A 1 160 ? 150.867 145.081 143.190 1.00 27.37  ? 161  ALA A CB    1 
ATOM   1284 N  N     . TYR A 1 161 ? 150.414 142.808 140.992 1.00 31.09  ? 162  TYR A N     1 
ATOM   1285 C  CA    . TYR A 1 161 ? 150.592 141.428 140.557 1.00 31.09  ? 162  TYR A CA    1 
ATOM   1286 C  C     . TYR A 1 161 ? 151.288 141.341 139.203 1.00 31.09  ? 162  TYR A C     1 
ATOM   1287 O  O     . TYR A 1 161 ? 152.163 140.489 139.011 1.00 31.09  ? 162  TYR A O     1 
ATOM   1288 C  CB    . TYR A 1 161 ? 149.244 140.721 140.511 1.00 31.09  ? 162  TYR A CB    1 
ATOM   1289 C  CG    . TYR A 1 161 ? 149.339 139.275 140.109 1.00 31.09  ? 162  TYR A CG    1 
ATOM   1290 C  CD1   . TYR A 1 161 ? 149.907 138.342 140.960 1.00 31.09  ? 162  TYR A CD1   1 
ATOM   1291 C  CD2   . TYR A 1 161 ? 148.849 138.838 138.889 1.00 31.09  ? 162  TYR A CD2   1 
ATOM   1292 C  CE1   . TYR A 1 161 ? 150.001 137.016 140.604 1.00 31.09  ? 162  TYR A CE1   1 
ATOM   1293 C  CE2   . TYR A 1 161 ? 148.931 137.510 138.525 1.00 31.09  ? 162  TYR A CE2   1 
ATOM   1294 C  CZ    . TYR A 1 161 ? 149.512 136.604 139.388 1.00 31.09  ? 162  TYR A CZ    1 
ATOM   1295 O  OH    . TYR A 1 161 ? 149.597 135.277 139.040 1.00 31.09  ? 162  TYR A OH    1 
ATOM   1296 N  N     . GLN A 1 162 ? 150.898 142.191 138.248 1.00 31.93  ? 163  GLN A N     1 
ATOM   1297 C  CA    . GLN A 1 162 ? 151.559 142.213 136.941 1.00 31.93  ? 163  GLN A CA    1 
ATOM   1298 C  C     . GLN A 1 162 ? 153.014 142.659 137.031 1.00 31.93  ? 163  GLN A C     1 
ATOM   1299 O  O     . GLN A 1 162 ? 153.865 142.153 136.289 1.00 31.93  ? 163  GLN A O     1 
ATOM   1300 C  CB    . GLN A 1 162 ? 150.798 143.107 135.971 1.00 31.93  ? 163  GLN A CB    1 
ATOM   1301 C  CG    . GLN A 1 162 ? 149.468 142.548 135.552 1.00 31.93  ? 163  GLN A CG    1 
ATOM   1302 C  CD    . GLN A 1 162 ? 148.643 143.567 134.817 1.00 31.93  ? 163  GLN A CD    1 
ATOM   1303 O  OE1   . GLN A 1 162 ? 149.151 144.291 133.966 1.00 31.93  ? 163  GLN A OE1   1 
ATOM   1304 N  NE2   . GLN A 1 162 ? 147.365 143.647 135.154 1.00 31.93  ? 163  GLN A NE2   1 
ATOM   1305 N  N     . TYR A 1 163 ? 153.314 143.625 137.906 1.00 30.27  ? 164  TYR A N     1 
ATOM   1306 C  CA    . TYR A 1 163 ? 154.702 144.024 138.138 1.00 30.27  ? 164  TYR A CA    1 
ATOM   1307 C  C     . TYR A 1 163 ? 155.524 142.895 138.743 1.00 30.27  ? 164  TYR A C     1 
ATOM   1308 O  O     . TYR A 1 163 ? 156.725 142.789 138.469 1.00 30.27  ? 164  TYR A O     1 
ATOM   1309 C  CB    . TYR A 1 163 ? 154.763 145.259 139.030 1.00 30.27  ? 164  TYR A CB    1 
ATOM   1310 C  CG    . TYR A 1 163 ? 154.745 146.566 138.280 1.00 30.27  ? 164  TYR A CG    1 
ATOM   1311 C  CD1   . TYR A 1 163 ? 153.720 146.879 137.404 1.00 30.27  ? 164  TYR A CD1   1 
ATOM   1312 C  CD2   . TYR A 1 163 ? 155.763 147.490 138.453 1.00 30.27  ? 164  TYR A CD2   1 
ATOM   1313 C  CE1   . TYR A 1 163 ? 153.708 148.078 136.722 1.00 30.27  ? 164  TYR A CE1   1 
ATOM   1314 C  CE2   . TYR A 1 163 ? 155.761 148.691 137.776 1.00 30.27  ? 164  TYR A CE2   1 
ATOM   1315 C  CZ    . TYR A 1 163 ? 154.733 148.979 136.913 1.00 30.27  ? 164  TYR A CZ    1 
ATOM   1316 O  OH    . TYR A 1 163 ? 154.733 150.175 136.237 1.00 30.27  ? 164  TYR A OH    1 
ATOM   1317 N  N     . MET A 1 164 ? 154.916 142.100 139.629 1.00 30.85  ? 165  MET A N     1 
ATOM   1318 C  CA    . MET A 1 164 ? 155.603 140.953 140.218 1.00 30.85  ? 165  MET A CA    1 
ATOM   1319 C  C     . MET A 1 164 ? 156.047 139.967 139.146 1.00 30.85  ? 165  MET A C     1 
ATOM   1320 O  O     . MET A 1 164 ? 157.201 139.527 139.135 1.00 30.85  ? 165  MET A O     1 
ATOM   1321 C  CB    . MET A 1 164 ? 154.704 140.261 141.242 1.00 30.85  ? 165  MET A CB    1 
ATOM   1322 C  CG    . MET A 1 164 ? 155.396 139.114 141.962 1.00 30.85  ? 165  MET A CG    1 
ATOM   1323 S  SD    . MET A 1 164 ? 154.329 138.153 143.047 1.00 30.85  ? 165  MET A SD    1 
ATOM   1324 C  CE    . MET A 1 164 ? 153.416 137.191 141.856 1.00 30.85  ? 165  MET A CE    1 
ATOM   1325 N  N     . LEU A 1 165 ? 155.132 139.593 138.250 1.00 31.92  ? 166  LEU A N     1 
ATOM   1326 C  CA    . LEU A 1 165 ? 155.454 138.651 137.181 1.00 31.92  ? 166  LEU A CA    1 
ATOM   1327 C  C     . LEU A 1 165 ? 156.463 139.216 136.186 1.00 31.92  ? 166  LEU A C     1 
ATOM   1328 O  O     . LEU A 1 165 ? 157.251 138.457 135.609 1.00 31.92  ? 166  LEU A O     1 
ATOM   1329 C  CB    . LEU A 1 165 ? 154.177 138.241 136.452 1.00 31.92  ? 166  LEU A CB    1 
ATOM   1330 C  CG    . LEU A 1 165 ? 153.152 137.493 137.301 1.00 31.92  ? 166  LEU A CG    1 
ATOM   1331 C  CD1   . LEU A 1 165 ? 151.944 137.124 136.463 1.00 31.92  ? 166  LEU A CD1   1 
ATOM   1332 C  CD2   . LEU A 1 165 ? 153.776 136.257 137.925 1.00 31.92  ? 166  LEU A CD2   1 
ATOM   1333 N  N     . THR A 1 166 ? 156.469 140.533 135.982 1.00 33.74  ? 167  THR A N     1 
ATOM   1334 C  CA    . THR A 1 166 ? 157.330 141.122 134.962 1.00 33.74  ? 167  THR A CA    1 
ATOM   1335 C  C     . THR A 1 166 ? 158.748 141.355 135.471 1.00 33.74  ? 167  THR A C     1 
ATOM   1336 O  O     . THR A 1 166 ? 159.719 140.983 134.805 1.00 33.74  ? 167  THR A O     1 
ATOM   1337 C  CB    . THR A 1 166 ? 156.718 142.432 134.464 1.00 33.74  ? 167  THR A CB    1 
ATOM   1338 O  OG1   . THR A 1 166 ? 155.390 142.184 133.985 1.00 33.74  ? 167  THR A OG1   1 
ATOM   1339 C  CG2   . THR A 1 166 ? 157.550 143.026 133.345 1.00 33.74  ? 167  THR A CG2   1 
ATOM   1340 N  N     . ASP A 1 167 ? 158.893 141.947 136.655 1.00 35.01  ? 168  ASP A N     1 
ATOM   1341 C  CA    . ASP A 1 167 ? 160.206 142.318 137.171 1.00 35.01  ? 168  ASP A CA    1 
ATOM   1342 C  C     . ASP A 1 167 ? 160.791 141.291 138.129 1.00 35.01  ? 168  ASP A C     1 
ATOM   1343 O  O     . ASP A 1 167 ? 161.933 141.468 138.564 1.00 35.01  ? 168  ASP A O     1 
ATOM   1344 C  CB    . ASP A 1 167 ? 160.135 143.676 137.874 1.00 35.01  ? 168  ASP A CB    1 
ATOM   1345 C  CG    . ASP A 1 167 ? 159.714 144.790 136.946 1.00 35.01  ? 168  ASP A CG    1 
ATOM   1346 O  OD1   . ASP A 1 167 ? 159.616 144.544 135.727 1.00 35.01  ? 168  ASP A OD1   1 
ATOM   1347 O  OD2   . ASP A 1 167 ? 159.478 145.913 137.436 1.00 35.01  ? 168  ASP A OD2   1 
ATOM   1348 N  N     . ARG A 1 168 ? 160.031 140.238 138.462 1.00 35.76  ? 169  ARG A N     1 
ATOM   1349 C  CA    . ARG A 1 168 ? 160.456 139.132 139.333 1.00 35.76  ? 169  ARG A CA    1 
ATOM   1350 C  C     . ARG A 1 168 ? 160.899 139.609 140.714 1.00 35.76  ? 169  ARG A C     1 
ATOM   1351 O  O     . ARG A 1 168 ? 161.778 139.009 141.335 1.00 35.76  ? 169  ARG A O     1 
ATOM   1352 C  CB    . ARG A 1 168 ? 161.555 138.286 138.685 1.00 35.76  ? 169  ARG A CB    1 
ATOM   1353 C  CG    . ARG A 1 168 ? 161.142 137.596 137.404 1.00 35.76  ? 169  ARG A CG    1 
ATOM   1354 C  CD    . ARG A 1 168 ? 162.307 136.803 136.860 1.00 35.76  ? 169  ARG A CD    1 
ATOM   1355 N  NE    . ARG A 1 168 ? 162.781 135.831 137.841 1.00 35.76  ? 169  ARG A NE    1 
ATOM   1356 C  CZ    . ARG A 1 168 ? 164.058 135.657 138.166 1.00 35.76  ? 169  ARG A CZ    1 
ATOM   1357 N  NH1   . ARG A 1 168 ? 164.391 134.776 139.100 1.00 35.76  ? 169  ARG A NH1   1 
ATOM   1358 N  NH2   . ARG A 1 168 ? 164.999 136.386 137.581 1.00 35.76  ? 169  ARG A NH2   1 
ATOM   1359 N  N     . GLU A 1 169 ? 160.297 140.685 141.209 1.00 29.89  ? 170  GLU A N     1 
ATOM   1360 C  CA    . GLU A 1 169 ? 160.641 141.229 142.510 1.00 29.89  ? 170  GLU A CA    1 
ATOM   1361 C  C     . GLU A 1 169 ? 159.422 141.238 143.420 1.00 29.89  ? 170  GLU A C     1 
ATOM   1362 O  O     . GLU A 1 169 ? 158.279 141.339 142.963 1.00 29.89  ? 170  GLU A O     1 
ATOM   1363 C  CB    . GLU A 1 169 ? 161.232 142.641 142.382 1.00 29.89  ? 170  GLU A CB    1 
ATOM   1364 C  CG    . GLU A 1 169 ? 160.237 143.732 142.048 1.00 29.89  ? 170  GLU A CG    1 
ATOM   1365 C  CD    . GLU A 1 169 ? 160.893 145.079 141.885 1.00 29.89  ? 170  GLU A CD    1 
ATOM   1366 O  OE1   . GLU A 1 169 ? 161.969 145.290 142.479 1.00 29.89  ? 170  GLU A OE1   1 
ATOM   1367 O  OE2   . GLU A 1 169 ? 160.335 145.928 141.162 1.00 29.89  ? 170  GLU A OE2   1 
ATOM   1368 N  N     . ASN A 1 170 ? 159.692 141.053 144.710 1.00 27.03  ? 171  ASN A N     1 
ATOM   1369 C  CA    . ASN A 1 170 ? 158.655 140.988 145.728 1.00 27.03  ? 171  ASN A CA    1 
ATOM   1370 C  C     . ASN A 1 170 ? 157.905 142.307 145.815 1.00 27.03  ? 171  ASN A C     1 
ATOM   1371 O  O     . ASN A 1 170 ? 158.516 143.376 145.825 1.00 27.03  ? 171  ASN A O     1 
ATOM   1372 C  CB    . ASN A 1 170 ? 159.289 140.653 147.069 1.00 27.03  ? 171  ASN A CB    1 
ATOM   1373 C  CG    . ASN A 1 170 ? 160.031 139.343 147.040 1.00 27.03  ? 171  ASN A CG    1 
ATOM   1374 O  OD1   . ASN A 1 170 ? 159.480 138.320 146.652 1.00 27.03  ? 171  ASN A OD1   1 
ATOM   1375 N  ND2   . ASN A 1 170 ? 161.293 139.368 147.443 1.00 27.03  ? 171  ASN A ND2   1 
ATOM   1376 N  N     . GLN A 1 171 ? 156.583 142.240 145.842 1.00 24.43  ? 172  GLN A N     1 
ATOM   1377 C  CA    . GLN A 1 171 ? 155.774 143.441 145.961 1.00 24.43  ? 172  GLN A CA    1 
ATOM   1378 C  C     . GLN A 1 171 ? 155.390 143.689 147.412 1.00 24.43  ? 172  GLN A C     1 
ATOM   1379 O  O     . GLN A 1 171 ? 155.396 142.782 148.243 1.00 24.43  ? 172  GLN A O     1 
ATOM   1380 C  CB    . GLN A 1 171 ? 154.518 143.327 145.105 1.00 24.43  ? 172  GLN A CB    1 
ATOM   1381 C  CG    . GLN A 1 171 ? 154.830 143.028 143.676 1.00 24.43  ? 172  GLN A CG    1 
ATOM   1382 C  CD    . GLN A 1 171 ? 155.678 144.093 143.050 1.00 24.43  ? 172  GLN A CD    1 
ATOM   1383 O  OE1   . GLN A 1 171 ? 155.325 145.270 143.058 1.00 24.43  ? 172  GLN A OE1   1 
ATOM   1384 N  NE2   . GLN A 1 171 ? 156.811 143.690 142.498 1.00 24.43  ? 172  GLN A NE2   1 
ATOM   1385 N  N     . SER A 1 172 ? 155.060 144.939 147.713 1.00 20.69  ? 173  SER A N     1 
ATOM   1386 C  CA    . SER A 1 172 ? 154.347 145.268 148.934 1.00 20.69  ? 173  SER A CA    1 
ATOM   1387 C  C     . SER A 1 172 ? 153.314 146.339 148.650 1.00 20.69  ? 173  SER A C     1 
ATOM   1388 O  O     . SER A 1 172 ? 153.582 147.283 147.907 1.00 20.69  ? 173  SER A O     1 
ATOM   1389 C  CB    . SER A 1 172 ? 155.290 145.748 150.030 1.00 20.69  ? 173  SER A CB    1 
ATOM   1390 O  OG    . SER A 1 172 ? 156.345 144.835 150.212 1.00 20.69  ? 173  SER A OG    1 
ATOM   1391 N  N     . ILE A 1 173 ? 152.135 146.189 149.236 1.00 16.97  ? 174  ILE A N     1 
ATOM   1392 C  CA    . ILE A 1 173 ? 151.076 147.182 149.134 1.00 16.97  ? 174  ILE A CA    1 
ATOM   1393 C  C     . ILE A 1 173 ? 150.933 147.822 150.504 1.00 16.97  ? 174  ILE A C     1 
ATOM   1394 O  O     . ILE A 1 173 ? 150.547 147.155 151.469 1.00 16.97  ? 174  ILE A O     1 
ATOM   1395 C  CB    . ILE A 1 173 ? 149.761 146.559 148.655 1.00 16.97  ? 174  ILE A CB    1 
ATOM   1396 C  CG1   . ILE A 1 173 ? 149.950 146.000 147.250 1.00 16.97  ? 174  ILE A CG1   1 
ATOM   1397 C  CG2   . ILE A 1 173 ? 148.653 147.584 148.668 1.00 16.97  ? 174  ILE A CG2   1 
ATOM   1398 C  CD1   . ILE A 1 173 ? 148.888 145.047 146.838 1.00 16.97  ? 174  ILE A CD1   1 
ATOM   1399 N  N     . LEU A 1 174 ? 151.237 149.107 150.594 1.00 17.82  ? 175  LEU A N     1 
ATOM   1400 C  CA    . LEU A 1 174 ? 151.342 149.799 151.871 1.00 17.82  ? 175  LEU A CA    1 
ATOM   1401 C  C     . LEU A 1 174 ? 150.198 150.795 151.986 1.00 17.82  ? 175  LEU A C     1 
ATOM   1402 O  O     . LEU A 1 174 ? 150.213 151.845 151.339 1.00 17.82  ? 175  LEU A O     1 
ATOM   1403 C  CB    . LEU A 1 174 ? 152.691 150.492 151.990 1.00 17.82  ? 175  LEU A CB    1 
ATOM   1404 C  CG    . LEU A 1 174 ? 153.851 149.528 151.769 1.00 17.82  ? 175  LEU A CG    1 
ATOM   1405 C  CD1   . LEU A 1 174 ? 155.149 150.270 151.808 1.00 17.82  ? 175  LEU A CD1   1 
ATOM   1406 C  CD2   . LEU A 1 174 ? 153.843 148.426 152.781 1.00 17.82  ? 175  LEU A CD2   1 
ATOM   1407 N  N     . ILE A 1 175 ? 149.226 150.471 152.826 1.00 17.73  ? 176  ILE A N     1 
ATOM   1408 C  CA    . ILE A 1 175 ? 147.983 151.218 152.946 1.00 17.73  ? 176  ILE A CA    1 
ATOM   1409 C  C     . ILE A 1 175 ? 148.067 152.065 154.207 1.00 17.73  ? 176  ILE A C     1 
ATOM   1410 O  O     . ILE A 1 175 ? 148.339 151.542 155.293 1.00 17.73  ? 176  ILE A O     1 
ATOM   1411 C  CB    . ILE A 1 175 ? 146.781 150.268 152.986 1.00 17.73  ? 176  ILE A CB    1 
ATOM   1412 C  CG1   . ILE A 1 175 ? 146.902 149.235 151.870 1.00 17.73  ? 176  ILE A CG1   1 
ATOM   1413 C  CG2   . ILE A 1 175 ? 145.526 151.037 152.809 1.00 17.73  ? 176  ILE A CG2   1 
ATOM   1414 C  CD1   . ILE A 1 175 ? 145.718 148.323 151.740 1.00 17.73  ? 176  ILE A CD1   1 
ATOM   1415 N  N     . THR A 1 176 ? 147.853 153.375 154.072 1.00 20.56  ? 177  THR A N     1 
ATOM   1416 C  CA    . THR A 1 176 ? 148.219 154.344 155.099 1.00 20.56  ? 177  THR A CA    1 
ATOM   1417 C  C     . THR A 1 176 ? 147.138 155.405 155.242 1.00 20.56  ? 177  THR A C     1 
ATOM   1418 O  O     . THR A 1 176 ? 146.480 155.780 154.272 1.00 20.56  ? 177  THR A O     1 
ATOM   1419 C  CB    . THR A 1 176 ? 149.528 155.091 154.787 1.00 20.56  ? 177  THR A CB    1 
ATOM   1420 O  OG1   . THR A 1 176 ? 149.430 155.701 153.501 1.00 20.56  ? 177  THR A OG1   1 
ATOM   1421 C  CG2   . THR A 1 176 ? 150.725 154.180 154.787 1.00 20.56  ? 177  THR A CG2   1 
ATOM   1422 N  N     . GLY A 1 177 ? 146.971 155.886 156.462 1.00 22.96  ? 178  GLY A N     1 
ATOM   1423 C  CA    . GLY A 1 177 ? 145.947 156.864 156.768 1.00 22.96  ? 178  GLY A CA    1 
ATOM   1424 C  C     . GLY A 1 177 ? 145.660 156.876 158.252 1.00 22.96  ? 178  GLY A C     1 
ATOM   1425 O  O     . GLY A 1 177 ? 146.220 156.099 159.021 1.00 22.96  ? 178  GLY A O     1 
ATOM   1426 N  N     . GLU A 1 178 ? 144.765 157.782 158.641 1.00 26.75  ? 179  GLU A N     1 
ATOM   1427 C  CA    . GLU A 1 178 ? 144.349 157.870 160.033 1.00 26.75  ? 179  GLU A CA    1 
ATOM   1428 C  C     . GLU A 1 178 ? 143.478 156.686 160.447 1.00 26.75  ? 179  GLU A C     1 
ATOM   1429 O  O     . GLU A 1 178 ? 143.105 155.826 159.646 1.00 26.75  ? 179  GLU A O     1 
ATOM   1430 C  CB    . GLU A 1 178 ? 143.621 159.183 160.290 1.00 26.75  ? 179  GLU A CB    1 
ATOM   1431 C  CG    . GLU A 1 178 ? 144.426 160.402 159.924 1.00 26.75  ? 179  GLU A CG    1 
ATOM   1432 C  CD    . GLU A 1 178 ? 143.785 161.677 160.409 1.00 26.75  ? 179  GLU A CD    1 
ATOM   1433 O  OE1   . GLU A 1 178 ? 142.757 161.592 161.112 1.00 26.75  ? 179  GLU A OE1   1 
ATOM   1434 O  OE2   . GLU A 1 178 ? 144.307 162.764 160.088 1.00 26.75  ? 179  GLU A OE2   1 
ATOM   1435 N  N     . SER A 1 179 ? 143.164 156.658 161.739 1.00 26.29  ? 180  SER A N     1 
ATOM   1436 C  CA    . SER A 1 179 ? 142.132 155.782 162.275 1.00 26.29  ? 180  SER A CA    1 
ATOM   1437 C  C     . SER A 1 179 ? 140.771 156.159 161.707 1.00 26.29  ? 180  SER A C     1 
ATOM   1438 O  O     . SER A 1 179 ? 140.359 157.319 161.782 1.00 26.29  ? 180  SER A O     1 
ATOM   1439 C  CB    . SER A 1 179 ? 142.118 155.871 163.800 1.00 26.29  ? 180  SER A CB    1 
ATOM   1440 O  OG    . SER A 1 179 ? 141.109 155.051 164.357 1.00 26.29  ? 180  SER A OG    1 
ATOM   1441 N  N     . GLY A 1 180 ? 140.058 155.180 161.159 1.00 24.02  ? 181  GLY A N     1 
ATOM   1442 C  CA    . GLY A 1 180 ? 138.783 155.470 160.539 1.00 24.02  ? 181  GLY A CA    1 
ATOM   1443 C  C     . GLY A 1 180 ? 138.826 155.779 159.064 1.00 24.02  ? 181  GLY A C     1 
ATOM   1444 O  O     . GLY A 1 180 ? 137.798 156.173 158.505 1.00 24.02  ? 181  GLY A O     1 
ATOM   1445 N  N     . ALA A 1 181 ? 139.976 155.622 158.417 1.00 22.85  ? 182  ALA A N     1 
ATOM   1446 C  CA    . ALA A 1 181 ? 140.119 156.001 157.019 1.00 22.85  ? 182  ALA A CA    1 
ATOM   1447 C  C     . ALA A 1 181 ? 139.826 154.871 156.041 1.00 22.85  ? 182  ALA A C     1 
ATOM   1448 O  O     . ALA A 1 181 ? 139.390 155.144 154.919 1.00 22.85  ? 182  ALA A O     1 
ATOM   1449 C  CB    . ALA A 1 181 ? 141.526 156.537 156.770 1.00 22.85  ? 182  ALA A CB    1 
ATOM   1450 N  N     . GLY A 1 182 ? 140.035 153.615 156.417 1.00 20.78  ? 183  GLY A N     1 
ATOM   1451 C  CA    . GLY A 1 182 ? 139.715 152.549 155.487 1.00 20.78  ? 183  GLY A CA    1 
ATOM   1452 C  C     . GLY A 1 182 ? 140.809 151.539 155.220 1.00 20.78  ? 183  GLY A C     1 
ATOM   1453 O  O     . GLY A 1 182 ? 140.745 150.811 154.230 1.00 20.78  ? 183  GLY A O     1 
ATOM   1454 N  N     . LYS A 1 183 ? 141.831 151.512 156.073 1.00 20.34  ? 184  LYS A N     1 
ATOM   1455 C  CA    . LYS A 1 183 ? 142.985 150.640 155.864 1.00 20.34  ? 184  LYS A CA    1 
ATOM   1456 C  C     . LYS A 1 183 ? 142.624 149.165 156.005 1.00 20.34  ? 184  LYS A C     1 
ATOM   1457 O  O     . LYS A 1 183 ? 143.185 148.318 155.303 1.00 20.34  ? 184  LYS A O     1 
ATOM   1458 C  CB    . LYS A 1 183 ? 144.092 151.019 156.841 1.00 20.34  ? 184  LYS A CB    1 
ATOM   1459 C  CG    . LYS A 1 183 ? 144.480 152.482 156.758 1.00 20.34  ? 184  LYS A CG    1 
ATOM   1460 C  CD    . LYS A 1 183 ? 145.470 152.888 157.824 1.00 20.34  ? 184  LYS A CD    1 
ATOM   1461 C  CE    . LYS A 1 183 ? 144.968 152.514 159.194 1.00 20.34  ? 184  LYS A CE    1 
ATOM   1462 N  NZ    . LYS A 1 183 ? 143.605 153.038 159.466 1.00 20.34  ? 184  LYS A NZ    1 
ATOM   1463 N  N     . THR A 1 184 ? 141.732 148.833 156.938 1.00 19.74  ? 185  THR A N     1 
ATOM   1464 C  CA    . THR A 1 184 ? 141.382 147.435 157.176 1.00 19.74  ? 185  THR A CA    1 
ATOM   1465 C  C     . THR A 1 184 ? 140.564 146.839 156.035 1.00 19.74  ? 185  THR A C     1 
ATOM   1466 O  O     . THR A 1 184 ? 140.892 145.756 155.539 1.00 19.74  ? 185  THR A O     1 
ATOM   1467 C  CB    . THR A 1 184 ? 140.630 147.290 158.497 1.00 19.74  ? 185  THR A CB    1 
ATOM   1468 O  OG1   . THR A 1 184 ? 141.305 148.032 159.520 1.00 19.74  ? 185  THR A OG1   1 
ATOM   1469 C  CG2   . THR A 1 184 ? 140.552 145.835 158.904 1.00 19.74  ? 185  THR A CG2   1 
ATOM   1470 N  N     . VAL A 1 185 ? 139.464 147.498 155.646 1.00 20.56  ? 186  VAL A N     1 
ATOM   1471 C  CA    . VAL A 1 185 ? 138.640 147.019 154.532 1.00 20.56  ? 186  VAL A CA    1 
ATOM   1472 C  C     . VAL A 1 185 ? 139.420 146.949 153.221 1.00 20.56  ? 186  VAL A C     1 
ATOM   1473 O  O     . VAL A 1 185 ? 139.279 145.979 152.471 1.00 20.56  ? 186  VAL A O     1 
ATOM   1474 C  CB    . VAL A 1 185 ? 137.364 147.867 154.388 1.00 20.56  ? 186  VAL A CB    1 
ATOM   1475 C  CG1   . VAL A 1 185 ? 136.403 147.548 155.487 1.00 20.56  ? 186  VAL A CG1   1 
ATOM   1476 C  CG2   . VAL A 1 185 ? 137.699 149.301 154.489 1.00 20.56  ? 186  VAL A CG2   1 
ATOM   1477 N  N     . ASN A 1 186 ? 140.237 147.964 152.915 1.00 20.29  ? 187  ASN A N     1 
ATOM   1478 C  CA    . ASN A 1 186 ? 141.072 147.914 151.717 1.00 20.29  ? 187  ASN A CA    1 
ATOM   1479 C  C     . ASN A 1 186 ? 142.072 146.772 151.760 1.00 20.29  ? 187  ASN A C     1 
ATOM   1480 O  O     . ASN A 1 186 ? 142.416 146.225 150.713 1.00 20.29  ? 187  ASN A O     1 
ATOM   1481 C  CB    . ASN A 1 186 ? 141.787 149.241 151.507 1.00 20.29  ? 187  ASN A CB    1 
ATOM   1482 C  CG    . ASN A 1 186 ? 140.876 150.295 150.942 1.00 20.29  ? 187  ASN A CG    1 
ATOM   1483 O  OD1   . ASN A 1 186 ? 140.557 150.282 149.760 1.00 20.29  ? 187  ASN A OD1   1 
ATOM   1484 N  ND2   . ASN A 1 186 ? 140.447 151.218 151.784 1.00 20.29  ? 187  ASN A ND2   1 
ATOM   1485 N  N     . THR A 1 187 ? 142.572 146.418 152.943 1.00 20.19  ? 188  THR A N     1 
ATOM   1486 C  CA    . THR A 1 187 ? 143.380 145.210 153.061 1.00 20.19  ? 188  THR A CA    1 
ATOM   1487 C  C     . THR A 1 187 ? 142.549 143.968 152.764 1.00 20.19  ? 188  THR A C     1 
ATOM   1488 O  O     . THR A 1 187 ? 143.009 143.054 152.070 1.00 20.19  ? 188  THR A O     1 
ATOM   1489 C  CB    . THR A 1 187 ? 143.993 145.118 154.455 1.00 20.19  ? 188  THR A CB    1 
ATOM   1490 O  OG1   . THR A 1 187 ? 144.762 146.297 154.716 1.00 20.19  ? 188  THR A OG1   1 
ATOM   1491 C  CG2   . THR A 1 187 ? 144.887 143.890 154.571 1.00 20.19  ? 188  THR A CG2   1 
ATOM   1492 N  N     . LYS A 1 188 ? 141.315 143.929 153.277 1.00 19.30  ? 189  LYS A N     1 
ATOM   1493 C  CA    . LYS A 1 188 ? 140.408 142.817 153.011 1.00 19.30  ? 189  LYS A CA    1 
ATOM   1494 C  C     . LYS A 1 188 ? 140.055 142.704 151.533 1.00 19.30  ? 189  LYS A C     1 
ATOM   1495 O  O     . LYS A 1 188 ? 139.970 141.593 151.000 1.00 19.30  ? 189  LYS A O     1 
ATOM   1496 C  CB    . LYS A 1 188 ? 139.134 142.980 153.837 1.00 19.30  ? 189  LYS A CB    1 
ATOM   1497 C  CG    . LYS A 1 188 ? 139.317 142.840 155.329 1.00 19.30  ? 189  LYS A CG    1 
ATOM   1498 C  CD    . LYS A 1 188 ? 137.989 143.007 156.039 1.00 19.30  ? 189  LYS A CD    1 
ATOM   1499 C  CE    . LYS A 1 188 ? 138.143 142.873 157.536 1.00 19.30  ? 189  LYS A CE    1 
ATOM   1500 N  NZ    . LYS A 1 188 ? 136.838 143.013 158.229 1.00 19.30  ? 189  LYS A NZ    1 
ATOM   1501 N  N     . ARG A 1 189 ? 139.837 143.841 150.859 1.00 20.47  ? 190  ARG A N     1 
ATOM   1502 C  CA    . ARG A 1 189 ? 139.537 143.832 149.427 1.00 20.47  ? 190  ARG A CA    1 
ATOM   1503 C  C     . ARG A 1 189 ? 140.714 143.337 148.596 1.00 20.47  ? 190  ARG A C     1 
ATOM   1504 O  O     . ARG A 1 189 ? 140.514 142.669 147.577 1.00 20.47  ? 190  ARG A O     1 
ATOM   1505 C  CB    . ARG A 1 189 ? 139.124 145.219 148.948 1.00 20.47  ? 190  ARG A CB    1 
ATOM   1506 C  CG    . ARG A 1 189 ? 137.871 145.821 149.571 1.00 20.47  ? 190  ARG A CG    1 
ATOM   1507 C  CD    . ARG A 1 189 ? 136.592 145.053 149.329 1.00 20.47  ? 190  ARG A CD    1 
ATOM   1508 N  NE    . ARG A 1 189 ? 136.328 144.025 150.328 1.00 20.47  ? 190  ARG A NE    1 
ATOM   1509 C  CZ    . ARG A 1 189 ? 135.746 144.265 151.498 1.00 20.47  ? 190  ARG A CZ    1 
ATOM   1510 N  NH1   . ARG A 1 189 ? 135.448 143.268 152.314 1.00 20.47  ? 190  ARG A NH1   1 
ATOM   1511 N  NH2   . ARG A 1 189 ? 135.372 145.495 151.811 1.00 20.47  ? 190  ARG A NH2   1 
ATOM   1512 N  N     . VAL A 1 190 ? 141.938 143.710 148.975 1.00 20.38  ? 191  VAL A N     1 
ATOM   1513 C  CA    . VAL A 1 190 ? 143.134 143.179 148.324 1.00 20.38  ? 191  VAL A CA    1 
ATOM   1514 C  C     . VAL A 1 190 ? 143.203 141.665 148.475 1.00 20.38  ? 191  VAL A C     1 
ATOM   1515 O  O     . VAL A 1 190 ? 143.431 140.940 147.499 1.00 20.38  ? 191  VAL A O     1 
ATOM   1516 C  CB    . VAL A 1 190 ? 144.391 143.870 148.876 1.00 20.38  ? 191  VAL A CB    1 
ATOM   1517 C  CG1   . VAL A 1 190 ? 145.624 143.164 148.434 1.00 20.38  ? 191  VAL A CG1   1 
ATOM   1518 C  CG2   . VAL A 1 190 ? 144.463 145.272 148.349 1.00 20.38  ? 191  VAL A CG2   1 
ATOM   1519 N  N     . ILE A 1 191 ? 143.003 141.167 149.698 1.00 22.45  ? 192  ILE A N     1 
ATOM   1520 C  CA    . ILE A 1 191 ? 143.031 139.726 149.945 1.00 22.45  ? 192  ILE A CA    1 
ATOM   1521 C  C     . ILE A 1 191 ? 141.863 139.042 149.239 1.00 22.45  ? 192  ILE A C     1 
ATOM   1522 O  O     . ILE A 1 191 ? 141.998 137.921 148.732 1.00 22.45  ? 192  ILE A O     1 
ATOM   1523 C  CB    . ILE A 1 191 ? 143.032 139.457 151.462 1.00 22.45  ? 192  ILE A CB    1 
ATOM   1524 C  CG1   . ILE A 1 191 ? 144.296 140.018 152.095 1.00 22.45  ? 192  ILE A CG1   1 
ATOM   1525 C  CG2   . ILE A 1 191 ? 143.028 137.982 151.767 1.00 22.45  ? 192  ILE A CG2   1 
ATOM   1526 C  CD1   . ILE A 1 191 ? 145.557 139.559 151.440 1.00 22.45  ? 192  ILE A CD1   1 
ATOM   1527 N  N     . GLN A 1 192 ? 140.708 139.721 149.178 1.00 24.45  ? 193  GLN A N     1 
ATOM   1528 C  CA    . GLN A 1 192 ? 139.558 139.231 148.416 1.00 24.45  ? 193  GLN A CA    1 
ATOM   1529 C  C     . GLN A 1 192 ? 139.881 139.046 146.938 1.00 24.45  ? 193  GLN A C     1 
ATOM   1530 O  O     . GLN A 1 192 ? 139.503 138.028 146.345 1.00 24.45  ? 193  GLN A O     1 
ATOM   1531 C  CB    . GLN A 1 192 ? 138.366 140.177 148.580 1.00 24.45  ? 193  GLN A CB    1 
ATOM   1532 C  CG    . GLN A 1 192 ? 137.214 139.887 147.639 1.00 24.45  ? 193  GLN A CG    1 
ATOM   1533 C  CD    . GLN A 1 192 ? 136.079 140.868 147.769 1.00 24.45  ? 193  GLN A CD    1 
ATOM   1534 O  OE1   . GLN A 1 192 ? 135.944 141.550 148.781 1.00 24.45  ? 193  GLN A OE1   1 
ATOM   1535 N  NE2   . GLN A 1 192 ? 135.257 140.953 146.736 1.00 24.45  ? 193  GLN A NE2   1 
ATOM   1536 N  N     . TYR A 1 193 ? 140.556 140.032 146.327 1.00 26.40  ? 194  TYR A N     1 
ATOM   1537 C  CA    . TYR A 1 193 ? 140.938 139.943 144.917 1.00 26.40  ? 194  TYR A CA    1 
ATOM   1538 C  C     . TYR A 1 193 ? 141.794 138.710 144.645 1.00 26.40  ? 194  TYR A C     1 
ATOM   1539 O  O     . TYR A 1 193 ? 141.458 137.900 143.777 1.00 26.40  ? 194  TYR A O     1 
ATOM   1540 C  CB    . TYR A 1 193 ? 141.627 141.242 144.457 1.00 26.40  ? 194  TYR A CB    1 
ATOM   1541 C  CG    . TYR A 1 193 ? 142.327 141.172 143.101 1.00 26.40  ? 194  TYR A CG    1 
ATOM   1542 C  CD1   . TYR A 1 193 ? 143.653 140.763 142.972 1.00 26.40  ? 194  TYR A CD1   1 
ATOM   1543 C  CD2   . TYR A 1 193 ? 141.621 141.443 141.937 1.00 26.40  ? 194  TYR A CD2   1 
ATOM   1544 C  CE1   . TYR A 1 193 ? 144.263 140.686 141.743 1.00 26.40  ? 194  TYR A CE1   1 
ATOM   1545 C  CE2   . TYR A 1 193 ? 142.223 141.352 140.698 1.00 26.40  ? 194  TYR A CE2   1 
ATOM   1546 C  CZ    . TYR A 1 193 ? 143.545 140.978 140.613 1.00 26.40  ? 194  TYR A CZ    1 
ATOM   1547 O  OH    . TYR A 1 193 ? 144.154 140.865 139.391 1.00 26.40  ? 194  TYR A OH    1 
ATOM   1548 N  N     . PHE A 1 194 ? 142.904 138.558 145.375 1.00 25.60  ? 195  PHE A N     1 
ATOM   1549 C  CA    . PHE A 1 194 ? 143.808 137.429 145.149 1.00 25.60  ? 195  PHE A CA    1 
ATOM   1550 C  C     . PHE A 1 194 ? 143.142 136.089 145.439 1.00 25.60  ? 195  PHE A C     1 
ATOM   1551 O  O     . PHE A 1 194 ? 143.490 135.083 144.815 1.00 25.60  ? 195  PHE A O     1 
ATOM   1552 C  CB    . PHE A 1 194 ? 145.091 137.582 145.965 1.00 25.60  ? 195  PHE A CB    1 
ATOM   1553 C  CG    . PHE A 1 194 ? 145.906 138.788 145.595 1.00 25.60  ? 195  PHE A CG    1 
ATOM   1554 C  CD1   . PHE A 1 194 ? 146.281 138.998 144.284 1.00 25.60  ? 195  PHE A CD1   1 
ATOM   1555 C  CD2   . PHE A 1 194 ? 146.304 139.706 146.551 1.00 25.60  ? 195  PHE A CD2   1 
ATOM   1556 C  CE1   . PHE A 1 194 ? 147.029 140.108 143.929 1.00 25.60  ? 195  PHE A CE1   1 
ATOM   1557 C  CE2   . PHE A 1 194 ? 147.059 140.812 146.199 1.00 25.60  ? 195  PHE A CE2   1 
ATOM   1558 C  CZ    . PHE A 1 194 ? 147.415 141.014 144.889 1.00 25.60  ? 195  PHE A CZ    1 
ATOM   1559 N  N     . ALA A 1 195 ? 142.220 136.048 146.401 1.00 28.41  ? 196  ALA A N     1 
ATOM   1560 C  CA    . ALA A 1 195 ? 141.450 134.833 146.651 1.00 28.41  ? 196  ALA A CA    1 
ATOM   1561 C  C     . ALA A 1 195 ? 140.560 134.462 145.467 1.00 28.41  ? 196  ALA A C     1 
ATOM   1562 O  O     . ALA A 1 195 ? 140.604 133.326 144.980 1.00 28.41  ? 196  ALA A O     1 
ATOM   1563 C  CB    . ALA A 1 195 ? 140.605 135.005 147.910 1.00 28.41  ? 196  ALA A CB    1 
ATOM   1564 N  N     . VAL A 1 196 ? 139.745 135.411 144.994 1.00 29.49  ? 197  VAL A N     1 
ATOM   1565 C  CA    . VAL A 1 196 ? 138.796 135.151 143.909 1.00 29.49  ? 197  VAL A CA    1 
ATOM   1566 C  C     . VAL A 1 196 ? 139.510 134.847 142.590 1.00 29.49  ? 197  VAL A C     1 
ATOM   1567 O  O     . VAL A 1 196 ? 139.087 133.953 141.843 1.00 29.49  ? 197  VAL A O     1 
ATOM   1568 C  CB    . VAL A 1 196 ? 137.809 136.330 143.790 1.00 29.49  ? 197  VAL A CB    1 
ATOM   1569 C  CG1   . VAL A 1 196 ? 136.943 136.224 142.545 1.00 29.49  ? 197  VAL A CG1   1 
ATOM   1570 C  CG2   . VAL A 1 196 ? 136.924 136.378 145.020 1.00 29.49  ? 197  VAL A CG2   1 
ATOM   1571 N  N     . ILE A 1 197 ? 140.586 135.585 142.281 1.00 29.87  ? 198  ILE A N     1 
ATOM   1572 C  CA    . ILE A 1 197 ? 141.453 135.263 141.140 1.00 29.87  ? 198  ILE A CA    1 
ATOM   1573 C  C     . ILE A 1 197 ? 141.963 133.827 141.226 1.00 29.87  ? 198  ILE A C     1 
ATOM   1574 O  O     . ILE A 1 197 ? 141.896 133.065 140.254 1.00 29.87  ? 198  ILE A O     1 
ATOM   1575 C  CB    . ILE A 1 197 ? 142.614 136.272 141.045 1.00 29.87  ? 198  ILE A CB    1 
ATOM   1576 C  CG1   . ILE A 1 197 ? 142.092 137.643 140.613 1.00 29.87  ? 198  ILE A CG1   1 
ATOM   1577 C  CG2   . ILE A 1 197 ? 143.715 135.780 140.116 1.00 29.87  ? 198  ILE A CG2   1 
ATOM   1578 C  CD1   . ILE A 1 197 ? 141.423 137.643 139.277 1.00 29.87  ? 198  ILE A CD1   1 
ATOM   1579 N  N     . ALA A 1 198 ? 142.480 133.440 142.388 1.00 32.74  ? 199  ALA A N     1 
ATOM   1580 C  CA    . ALA A 1 198 ? 142.974 132.079 142.557 1.00 32.74  ? 199  ALA A CA    1 
ATOM   1581 C  C     . ALA A 1 198 ? 141.849 131.049 142.563 1.00 32.74  ? 199  ALA A C     1 
ATOM   1582 O  O     . ALA A 1 198 ? 142.070 129.896 142.176 1.00 32.74  ? 199  ALA A O     1 
ATOM   1583 C  CB    . ALA A 1 198 ? 143.788 131.967 143.838 1.00 32.74  ? 199  ALA A CB    1 
ATOM   1584 N  N     . ALA A 1 199 ? 140.643 131.434 142.995 1.00 32.77  ? 200  ALA A N     1 
ATOM   1585 C  CA    . ALA A 1 199 ? 139.537 130.481 143.026 1.00 32.77  ? 200  ALA A CA    1 
ATOM   1586 C  C     . ALA A 1 199 ? 138.924 130.216 141.656 1.00 32.77  ? 200  ALA A C     1 
ATOM   1587 O  O     . ALA A 1 199 ? 138.430 129.108 141.419 1.00 32.77  ? 200  ALA A O     1 
ATOM   1588 C  CB    . ALA A 1 199 ? 138.452 130.969 143.985 1.00 32.77  ? 200  ALA A CB    1 
ATOM   1589 N  N     . ILE A 1 200 ? 138.928 131.192 140.747 1.00 34.89  ? 201  ILE A N     1 
ATOM   1590 C  CA    . ILE A 1 200 ? 138.573 130.878 139.364 1.00 34.89  ? 201  ILE A CA    1 
ATOM   1591 C  C     . ILE A 1 200 ? 139.732 130.182 138.651 1.00 34.89  ? 201  ILE A C     1 
ATOM   1592 O  O     . ILE A 1 200 ? 139.521 129.236 137.884 1.00 34.89  ? 201  ILE A O     1 
ATOM   1593 C  CB    . ILE A 1 200 ? 138.062 132.127 138.609 1.00 34.89  ? 201  ILE A CB    1 
ATOM   1594 C  CG1   . ILE A 1 200 ? 139.089 133.262 138.551 1.00 34.89  ? 201  ILE A CG1   1 
ATOM   1595 C  CG2   . ILE A 1 200 ? 136.761 132.620 139.221 1.00 34.89  ? 201  ILE A CG2   1 
ATOM   1596 C  CD1   . ILE A 1 200 ? 138.731 134.354 137.574 1.00 34.89  ? 201  ILE A CD1   1 
ATOM   1597 N  N     . GLY A 1 201 ? 140.965 130.622 138.893 1.00 34.10  ? 202  GLY A N     1 
ATOM   1598 C  CA    . GLY A 1 201 ? 142.125 130.078 138.214 1.00 34.10  ? 202  GLY A CA    1 
ATOM   1599 C  C     . GLY A 1 201 ? 142.601 130.944 137.065 1.00 34.10  ? 202  GLY A C     1 
ATOM   1600 O  O     . GLY A 1 201 ? 143.524 131.742 137.219 1.00 34.10  ? 202  GLY A O     1 
ATOM   1601 N  N     . GLY A 1 213 ? 141.523 122.838 146.324 1.00 38.87  ? 214  GLY A N     1 
ATOM   1602 C  CA    . GLY A 1 213 ? 141.966 123.237 147.646 1.00 38.87  ? 214  GLY A CA    1 
ATOM   1603 C  C     . GLY A 1 213 ? 141.007 124.183 148.340 1.00 38.87  ? 214  GLY A C     1 
ATOM   1604 O  O     . GLY A 1 213 ? 139.943 124.501 147.810 1.00 38.87  ? 214  GLY A O     1 
ATOM   1605 N  N     . THR A 1 214 ? 141.392 124.641 149.534 1.00 37.20  ? 215  THR A N     1 
ATOM   1606 C  CA    . THR A 1 214 ? 140.560 125.553 150.307 1.00 37.20  ? 215  THR A CA    1 
ATOM   1607 C  C     . THR A 1 214 ? 141.356 126.711 150.896 1.00 37.20  ? 215  THR A C     1 
ATOM   1608 O  O     . THR A 1 214 ? 140.796 127.480 151.691 1.00 37.20  ? 215  THR A O     1 
ATOM   1609 C  CB    . THR A 1 214 ? 139.818 124.797 151.419 1.00 37.20  ? 215  THR A CB    1 
ATOM   1610 O  OG1   . THR A 1 214 ? 138.819 125.646 151.997 1.00 37.20  ? 215  THR A OG1   1 
ATOM   1611 C  CG2   . THR A 1 214 ? 140.780 124.303 152.491 1.00 37.20  ? 215  THR A CG2   1 
ATOM   1612 N  N     . LEU A 1 215 ? 142.649 126.822 150.554 1.00 36.14  ? 216  LEU A N     1 
ATOM   1613 C  CA    . LEU A 1 215 ? 143.507 127.917 151.010 1.00 36.14  ? 216  LEU A CA    1 
ATOM   1614 C  C     . LEU A 1 215 ? 142.931 129.282 150.654 1.00 36.14  ? 216  LEU A C     1 
ATOM   1615 O  O     . LEU A 1 215 ? 143.023 130.225 151.450 1.00 36.14  ? 216  LEU A O     1 
ATOM   1616 C  CB    . LEU A 1 215 ? 144.900 127.757 150.404 1.00 36.14  ? 216  LEU A CB    1 
ATOM   1617 C  CG    . LEU A 1 215 ? 145.856 128.948 150.466 1.00 36.14  ? 216  LEU A CG    1 
ATOM   1618 C  CD1   . LEU A 1 215 ? 146.284 129.252 151.885 1.00 36.14  ? 216  LEU A CD1   1 
ATOM   1619 C  CD2   . LEU A 1 215 ? 147.046 128.702 149.583 1.00 36.14  ? 216  LEU A CD2   1 
ATOM   1620 N  N     . GLU A 1 216 ? 142.351 129.399 149.450 1.00 36.53  ? 217  GLU A N     1 
ATOM   1621 C  CA    . GLU A 1 216 ? 141.765 130.646 148.958 1.00 36.53  ? 217  GLU A CA    1 
ATOM   1622 C  C     . GLU A 1 216 ? 140.694 131.192 149.895 1.00 36.53  ? 217  GLU A C     1 
ATOM   1623 O  O     . GLU A 1 216 ? 140.528 132.411 150.010 1.00 36.53  ? 217  GLU A O     1 
ATOM   1624 C  CB    . GLU A 1 216 ? 141.158 130.441 147.565 1.00 36.53  ? 217  GLU A CB    1 
ATOM   1625 C  CG    . GLU A 1 216 ? 142.093 129.912 146.475 1.00 36.53  ? 217  GLU A CG    1 
ATOM   1626 C  CD    . GLU A 1 216 ? 142.248 128.399 146.478 1.00 36.53  ? 217  GLU A CD    1 
ATOM   1627 O  OE1   . GLU A 1 216 ? 141.658 127.735 147.355 1.00 36.53  ? 217  GLU A OE1   1 
ATOM   1628 O  OE2   . GLU A 1 216 ? 142.958 127.874 145.596 1.00 36.53  ? 217  GLU A OE2   1 
ATOM   1629 N  N     . ASP A 1 217 ? 139.966 130.310 150.573 1.00 35.27  ? 218  ASP A N     1 
ATOM   1630 C  CA    . ASP A 1 217 ? 138.986 130.708 151.570 1.00 35.27  ? 218  ASP A CA    1 
ATOM   1631 C  C     . ASP A 1 217 ? 139.604 130.925 152.943 1.00 35.27  ? 218  ASP A C     1 
ATOM   1632 O  O     . ASP A 1 217 ? 139.146 131.807 153.677 1.00 35.27  ? 218  ASP A O     1 
ATOM   1633 C  CB    . ASP A 1 217 ? 137.872 129.673 151.673 1.00 35.27  ? 218  ASP A CB    1 
ATOM   1634 C  CG    . ASP A 1 217 ? 136.689 130.193 152.442 1.00 35.27  ? 218  ASP A CG    1 
ATOM   1635 O  OD1   . ASP A 1 217 ? 136.147 131.246 152.047 1.00 35.27  ? 218  ASP A OD1   1 
ATOM   1636 O  OD2   . ASP A 1 217 ? 136.307 129.561 153.445 1.00 35.27  ? 218  ASP A OD2   1 
ATOM   1637 N  N     . GLN A 1 218 ? 140.558 130.068 153.337 1.00 33.35  ? 219  GLN A N     1 
ATOM   1638 C  CA    . GLN A 1 218 ? 141.222 130.204 154.635 1.00 33.35  ? 219  GLN A CA    1 
ATOM   1639 C  C     . GLN A 1 218 ? 141.898 131.561 154.804 1.00 33.35  ? 219  GLN A C     1 
ATOM   1640 O  O     . GLN A 1 218 ? 141.861 132.142 155.893 1.00 33.35  ? 219  GLN A O     1 
ATOM   1641 C  CB    . GLN A 1 218 ? 142.237 129.080 154.829 1.00 33.35  ? 219  GLN A CB    1 
ATOM   1642 C  CG    . GLN A 1 218 ? 141.604 127.731 155.065 1.00 33.35  ? 219  GLN A CG    1 
ATOM   1643 C  CD    . GLN A 1 218 ? 142.618 126.655 155.358 1.00 33.35  ? 219  GLN A CD    1 
ATOM   1644 O  OE1   . GLN A 1 218 ? 143.744 126.702 154.872 1.00 33.35  ? 219  GLN A OE1   1 
ATOM   1645 N  NE2   . GLN A 1 218 ? 142.223 125.670 156.154 1.00 33.35  ? 219  GLN A NE2   1 
ATOM   1646 N  N     . ILE A 1 219 ? 142.511 132.088 153.740 1.00 29.52  ? 220  ILE A N     1 
ATOM   1647 C  CA    . ILE A 1 219 ? 143.115 133.415 153.809 1.00 29.52  ? 220  ILE A CA    1 
ATOM   1648 C  C     . ILE A 1 219 ? 142.064 134.522 153.863 1.00 29.52  ? 220  ILE A C     1 
ATOM   1649 O  O     . ILE A 1 219 ? 142.340 135.613 154.372 1.00 29.52  ? 220  ILE A O     1 
ATOM   1650 C  CB    . ILE A 1 219 ? 144.114 133.591 152.644 1.00 29.52  ? 220  ILE A CB    1 
ATOM   1651 C  CG1   . ILE A 1 219 ? 145.009 134.810 152.864 1.00 29.52  ? 220  ILE A CG1   1 
ATOM   1652 C  CG2   . ILE A 1 219 ? 143.396 133.701 151.315 1.00 29.52  ? 220  ILE A CG2   1 
ATOM   1653 C  CD1   . ILE A 1 219 ? 145.652 134.854 154.229 1.00 29.52  ? 220  ILE A CD1   1 
ATOM   1654 N  N     . ILE A 1 220 ? 140.839 134.258 153.421 1.00 29.57  ? 221  ILE A N     1 
ATOM   1655 C  CA    . ILE A 1 220 ? 139.765 135.200 153.698 1.00 29.57  ? 221  ILE A CA    1 
ATOM   1656 C  C     . ILE A 1 220 ? 139.330 135.086 155.148 1.00 29.57  ? 221  ILE A C     1 
ATOM   1657 O  O     . ILE A 1 220 ? 139.229 136.089 155.861 1.00 29.57  ? 221  ILE A O     1 
ATOM   1658 C  CB    . ILE A 1 220 ? 138.588 134.962 152.739 1.00 29.57  ? 221  ILE A CB    1 
ATOM   1659 C  CG1   . ILE A 1 220 ? 139.013 135.256 151.308 1.00 29.57  ? 221  ILE A CG1   1 
ATOM   1660 C  CG2   . ILE A 1 220 ? 137.403 135.830 153.122 1.00 29.57  ? 221  ILE A CG2   1 
ATOM   1661 C  CD1   . ILE A 1 220 ? 139.391 136.679 151.095 1.00 29.57  ? 221  ILE A CD1   1 
ATOM   1662 N  N     . GLN A 1 221 ? 139.060 133.860 155.599 1.00 32.17  ? 222  GLN A N     1 
ATOM   1663 C  CA    . GLN A 1 221 ? 138.556 133.619 156.945 1.00 32.17  ? 222  GLN A CA    1 
ATOM   1664 C  C     . GLN A 1 221 ? 139.593 133.864 158.036 1.00 32.17  ? 222  GLN A C     1 
ATOM   1665 O  O     . GLN A 1 221 ? 139.215 133.975 159.205 1.00 32.17  ? 222  GLN A O     1 
ATOM   1666 C  CB    . GLN A 1 221 ? 138.003 132.198 157.048 1.00 32.17  ? 222  GLN A CB    1 
ATOM   1667 C  CG    . GLN A 1 221 ? 136.807 131.885 156.133 1.00 32.17  ? 222  GLN A CG    1 
ATOM   1668 C  CD    . GLN A 1 221 ? 135.520 132.670 156.412 1.00 32.17  ? 222  GLN A CD    1 
ATOM   1669 O  OE1   . GLN A 1 221 ? 135.406 133.431 157.373 1.00 32.17  ? 222  GLN A OE1   1 
ATOM   1670 N  NE2   . GLN A 1 221 ? 134.533 132.466 155.554 1.00 32.17  ? 222  GLN A NE2   1 
ATOM   1671 N  N     . ALA A 1 222 ? 140.889 133.871 157.704 1.00 28.25  ? 223  ALA A N     1 
ATOM   1672 C  CA    . ALA A 1 222 ? 141.920 134.287 158.657 1.00 28.25  ? 223  ALA A CA    1 
ATOM   1673 C  C     . ALA A 1 222 ? 141.748 135.708 159.183 1.00 28.25  ? 223  ALA A C     1 
ATOM   1674 O  O     . ALA A 1 222 ? 142.256 136.009 160.264 1.00 28.25  ? 223  ALA A O     1 
ATOM   1675 C  CB    . ALA A 1 222 ? 143.308 134.163 158.034 1.00 28.25  ? 223  ALA A CB    1 
ATOM   1676 N  N     . ASN A 1 223 ? 141.063 136.595 158.453 1.00 26.53  ? 224  ASN A N     1 
ATOM   1677 C  CA    . ASN A 1 223 ? 140.784 137.920 159.008 1.00 26.53  ? 224  ASN A CA    1 
ATOM   1678 C  C     . ASN A 1 223 ? 139.733 137.897 160.120 1.00 26.53  ? 224  ASN A C     1 
ATOM   1679 O  O     . ASN A 1 223 ? 140.071 138.310 161.243 1.00 26.53  ? 224  ASN A O     1 
ATOM   1680 C  CB    . ASN A 1 223 ? 140.507 138.930 157.886 1.00 26.53  ? 224  ASN A CB    1 
ATOM   1681 C  CG    . ASN A 1 223 ? 141.674 139.078 156.944 1.00 26.53  ? 224  ASN A CG    1 
ATOM   1682 O  OD1   . ASN A 1 223 ? 142.644 139.763 157.253 1.00 26.53  ? 224  ASN A OD1   1 
ATOM   1683 N  ND2   . ASN A 1 223 ? 141.583 138.447 155.782 1.00 26.53  ? 224  ASN A ND2   1 
ATOM   1684 N  N     . PRO A 1 224 ? 138.458 137.487 159.895 1.00 26.78  ? 225  PRO A N     1 
ATOM   1685 C  CA    . PRO A 1 224 ? 137.438 137.632 160.966 1.00 26.78  ? 225  PRO A CA    1 
ATOM   1686 C  C     . PRO A 1 224 ? 137.735 136.901 162.271 1.00 26.78  ? 225  PRO A C     1 
ATOM   1687 O  O     . PRO A 1 224 ? 137.156 137.263 163.301 1.00 26.78  ? 225  PRO A O     1 
ATOM   1688 C  CB    . PRO A 1 224 ? 136.163 137.066 160.328 1.00 26.78  ? 225  PRO A CB    1 
ATOM   1689 C  CG    . PRO A 1 224 ? 136.613 136.239 159.244 1.00 26.78  ? 225  PRO A CG    1 
ATOM   1690 C  CD    . PRO A 1 224 ? 137.820 136.875 158.710 1.00 26.78  ? 225  PRO A CD    1 
ATOM   1691 N  N     . ALA A 1 225 ? 138.565 135.858 162.244 1.00 25.33  ? 226  ALA A N     1 
ATOM   1692 C  CA    . ALA A 1 225 ? 139.111 135.294 163.473 1.00 25.33  ? 226  ALA A CA    1 
ATOM   1693 C  C     . ALA A 1 225 ? 139.862 136.340 164.287 1.00 25.33  ? 226  ALA A C     1 
ATOM   1694 O  O     . ALA A 1 225 ? 139.587 136.527 165.476 1.00 25.33  ? 226  ALA A O     1 
ATOM   1695 C  CB    . ALA A 1 225 ? 140.029 134.122 163.147 1.00 25.33  ? 226  ALA A CB    1 
ATOM   1696 N  N     . LEU A 1 226 ? 140.813 137.037 163.660 1.00 22.07  ? 227  LEU A N     1 
ATOM   1697 C  CA    . LEU A 1 226 ? 141.586 138.051 164.372 1.00 22.07  ? 227  LEU A CA    1 
ATOM   1698 C  C     . LEU A 1 226 ? 140.763 139.288 164.699 1.00 22.07  ? 227  LEU A C     1 
ATOM   1699 O  O     . LEU A 1 226 ? 140.994 139.916 165.736 1.00 22.07  ? 227  LEU A O     1 
ATOM   1700 C  CB    . LEU A 1 226 ? 142.822 138.442 163.568 1.00 22.07  ? 227  LEU A CB    1 
ATOM   1701 C  CG    . LEU A 1 226 ? 143.844 137.341 163.313 1.00 22.07  ? 227  LEU A CG    1 
ATOM   1702 C  CD1   . LEU A 1 226 ? 144.946 137.851 162.414 1.00 22.07  ? 227  LEU A CD1   1 
ATOM   1703 C  CD2   . LEU A 1 226 ? 144.407 136.849 164.627 1.00 22.07  ? 227  LEU A CD2   1 
ATOM   1704 N  N     . GLU A 1 227 ? 139.835 139.684 163.817 1.00 22.23  ? 228  GLU A N     1 
ATOM   1705 C  CA    . GLU A 1 227 ? 139.015 140.872 164.064 1.00 22.23  ? 228  GLU A CA    1 
ATOM   1706 C  C     . GLU A 1 227 ? 138.144 140.748 165.310 1.00 22.23  ? 228  GLU A C     1 
ATOM   1707 O  O     . GLU A 1 227 ? 137.736 141.770 165.867 1.00 22.23  ? 228  GLU A O     1 
ATOM   1708 C  CB    . GLU A 1 227 ? 138.119 141.190 162.864 1.00 22.23  ? 228  GLU A CB    1 
ATOM   1709 C  CG    . GLU A 1 227 ? 138.796 141.262 161.492 1.00 22.23  ? 228  GLU A CG    1 
ATOM   1710 C  CD    . GLU A 1 227 ? 140.084 142.070 161.440 1.00 22.23  ? 228  GLU A CD    1 
ATOM   1711 O  OE1   . GLU A 1 227 ? 140.999 141.651 160.702 1.00 22.23  ? 228  GLU A OE1   1 
ATOM   1712 O  OE2   . GLU A 1 227 ? 140.174 143.144 162.065 1.00 22.23  ? 228  GLU A OE2   1 
ATOM   1713 N  N     . ALA A 1 228 ? 137.810 139.528 165.727 1.00 23.53  ? 229  ALA A N     1 
ATOM   1714 C  CA    . ALA A 1 228 ? 137.089 139.337 166.979 1.00 23.53  ? 229  ALA A CA    1 
ATOM   1715 C  C     . ALA A 1 228 ? 137.950 139.728 168.170 1.00 23.53  ? 229  ALA A C     1 
ATOM   1716 O  O     . ALA A 1 228 ? 137.504 140.459 169.061 1.00 23.53  ? 229  ALA A O     1 
ATOM   1717 C  CB    . ALA A 1 228 ? 136.640 137.884 167.109 1.00 23.53  ? 229  ALA A CB    1 
ATOM   1718 N  N     . PHE A 1 229 ? 139.193 139.252 168.194 1.00 21.59  ? 230  PHE A N     1 
ATOM   1719 C  CA    . PHE A 1 229 ? 140.081 139.429 169.331 1.00 21.59  ? 230  PHE A CA    1 
ATOM   1720 C  C     . PHE A 1 229 ? 140.926 140.680 169.247 1.00 21.59  ? 230  PHE A C     1 
ATOM   1721 O  O     . PHE A 1 229 ? 141.441 141.117 170.274 1.00 21.59  ? 230  PHE A O     1 
ATOM   1722 C  CB    . PHE A 1 229 ? 141.031 138.240 169.470 1.00 21.59  ? 230  PHE A CB    1 
ATOM   1723 C  CG    . PHE A 1 229 ? 140.375 136.990 169.951 1.00 21.59  ? 230  PHE A CG    1 
ATOM   1724 C  CD1   . PHE A 1 229 ? 139.701 136.161 169.075 1.00 21.59  ? 230  PHE A CD1   1 
ATOM   1725 C  CD2   . PHE A 1 229 ? 140.448 136.634 171.283 1.00 21.59  ? 230  PHE A CD2   1 
ATOM   1726 C  CE1   . PHE A 1 229 ? 139.105 135.010 169.521 1.00 21.59  ? 230  PHE A CE1   1 
ATOM   1727 C  CE2   . PHE A 1 229 ? 139.851 135.482 171.734 1.00 21.59  ? 230  PHE A CE2   1 
ATOM   1728 C  CZ    . PHE A 1 229 ? 139.182 134.667 170.850 1.00 21.59  ? 230  PHE A CZ    1 
ATOM   1729 N  N     . GLY A 1 230 ? 141.144 141.220 168.055 1.00 19.16  ? 231  GLY A N     1 
ATOM   1730 C  CA    . GLY A 1 230 ? 142.060 142.330 167.911 1.00 19.16  ? 231  GLY A CA    1 
ATOM   1731 C  C     . GLY A 1 230 ? 141.449 143.693 167.669 1.00 19.16  ? 231  GLY A C     1 
ATOM   1732 O  O     . GLY A 1 230 ? 142.164 144.693 167.723 1.00 19.16  ? 231  GLY A O     1 
ATOM   1733 N  N     . ASN A 1 231 ? 140.152 143.770 167.401 1.00 19.87  ? 232  ASN A N     1 
ATOM   1734 C  CA    . ASN A 1 231 ? 139.506 145.045 167.140 1.00 19.87  ? 232  ASN A CA    1 
ATOM   1735 C  C     . ASN A 1 231 ? 138.568 145.416 168.273 1.00 19.87  ? 232  ASN A C     1 
ATOM   1736 O  O     . ASN A 1 231 ? 137.950 144.556 168.897 1.00 19.87  ? 232  ASN A O     1 
ATOM   1737 C  CB    . ASN A 1 231 ? 138.714 145.022 165.835 1.00 19.87  ? 232  ASN A CB    1 
ATOM   1738 C  CG    . ASN A 1 231 ? 139.563 144.685 164.642 1.00 19.87  ? 232  ASN A CG    1 
ATOM   1739 O  OD1   . ASN A 1 231 ? 140.750 144.411 164.764 1.00 19.87  ? 232  ASN A OD1   1 
ATOM   1740 N  ND2   . ASN A 1 231 ? 138.957 144.711 163.467 1.00 19.87  ? 232  ASN A ND2   1 
ATOM   1741 N  N     . ALA A 1 232 ? 138.452 146.713 168.518 1.00 21.59  ? 233  ALA A N     1 
ATOM   1742 C  CA    . ALA A 1 232 ? 137.549 147.212 169.537 1.00 21.59  ? 233  ALA A CA    1 
ATOM   1743 C  C     . ALA A 1 232 ? 137.014 148.570 169.132 1.00 21.59  ? 233  ALA A C     1 
ATOM   1744 O  O     . ALA A 1 232 ? 137.728 149.358 168.510 1.00 21.59  ? 233  ALA A O     1 
ATOM   1745 C  CB    . ALA A 1 232 ? 138.256 147.317 170.874 1.00 21.59  ? 233  ALA A CB    1 
ATOM   1746 N  N     . LYS A 1 233 ? 135.761 148.829 169.487 1.00 23.52  ? 234  LYS A N     1 
ATOM   1747 C  CA    . LYS A 1 233 ? 135.156 150.129 169.241 1.00 23.52  ? 234  LYS A CA    1 
ATOM   1748 C  C     . LYS A 1 233 ? 135.881 151.230 169.998 1.00 23.52  ? 234  LYS A C     1 
ATOM   1749 O  O     . LYS A 1 233 ? 135.989 151.185 171.224 1.00 23.52  ? 234  LYS A O     1 
ATOM   1750 C  CB    . LYS A 1 233 ? 133.686 150.116 169.641 1.00 23.52  ? 234  LYS A CB    1 
ATOM   1751 C  CG    . LYS A 1 233 ? 132.992 151.423 169.322 1.00 23.52  ? 234  LYS A CG    1 
ATOM   1752 C  CD    . LYS A 1 233 ? 132.534 152.160 170.551 1.00 23.52  ? 234  LYS A CD    1 
ATOM   1753 C  CE    . LYS A 1 233 ? 131.759 153.393 170.164 1.00 23.52  ? 234  LYS A CE    1 
ATOM   1754 N  NZ    . LYS A 1 233 ? 131.519 154.259 171.337 1.00 23.52  ? 234  LYS A NZ    1 
ATOM   1755 N  N     . THR A 1 234 ? 136.382 152.214 169.262 1.00 23.89  ? 235  THR A N     1 
ATOM   1756 C  CA    . THR A 1 234 ? 136.879 153.457 169.826 1.00 23.89  ? 235  THR A CA    1 
ATOM   1757 C  C     . THR A 1 234 ? 136.137 154.591 169.142 1.00 23.89  ? 235  THR A C     1 
ATOM   1758 O  O     . THR A 1 234 ? 135.470 154.384 168.128 1.00 23.89  ? 235  THR A O     1 
ATOM   1759 C  CB    . THR A 1 234 ? 138.384 153.641 169.644 1.00 23.89  ? 235  THR A CB    1 
ATOM   1760 O  OG1   . THR A 1 234 ? 138.701 153.609 168.254 1.00 23.89  ? 235  THR A OG1   1 
ATOM   1761 C  CG2   . THR A 1 234 ? 139.146 152.545 170.340 1.00 23.89  ? 235  THR A CG2   1 
ATOM   1762 N  N     . VAL A 1 235 ? 136.202 155.776 169.757 1.00 26.63  ? 236  VAL A N     1 
ATOM   1763 C  CA    . VAL A 1 235 ? 135.425 156.936 169.315 1.00 26.63  ? 236  VAL A CA    1 
ATOM   1764 C  C     . VAL A 1 235 ? 135.737 157.330 167.870 1.00 26.63  ? 236  VAL A C     1 
ATOM   1765 O  O     . VAL A 1 235 ? 134.858 157.822 167.153 1.00 26.63  ? 236  VAL A O     1 
ATOM   1766 C  CB    . VAL A 1 235 ? 135.614 158.105 170.315 1.00 26.63  ? 236  VAL A CB    1 
ATOM   1767 C  CG1   . VAL A 1 235 ? 136.997 158.754 170.225 1.00 26.63  ? 236  VAL A CG1   1 
ATOM   1768 C  CG2   . VAL A 1 235 ? 134.509 159.141 170.154 1.00 26.63  ? 236  VAL A CG2   1 
ATOM   1769 N  N     . ARG A 1 236 ? 136.971 157.100 167.408 1.00 27.17  ? 237  ARG A N     1 
ATOM   1770 C  CA    . ARG A 1 236 ? 137.322 157.397 166.025 1.00 27.17  ? 237  ARG A CA    1 
ATOM   1771 C  C     . ARG A 1 236 ? 136.767 156.377 165.036 1.00 27.17  ? 237  ARG A C     1 
ATOM   1772 O  O     . ARG A 1 236 ? 136.444 156.748 163.903 1.00 27.17  ? 237  ARG A O     1 
ATOM   1773 C  CB    . ARG A 1 236 ? 138.838 157.503 165.884 1.00 27.17  ? 237  ARG A CB    1 
ATOM   1774 C  CG    . ARG A 1 236 ? 139.361 158.868 166.301 1.00 27.17  ? 237  ARG A CG    1 
ATOM   1775 C  CD    . ARG A 1 236 ? 138.969 159.964 165.316 1.00 27.17  ? 237  ARG A CD    1 
ATOM   1776 N  NE    . ARG A 1 236 ? 139.473 159.730 163.971 1.00 27.17  ? 237  ARG A NE    1 
ATOM   1777 C  CZ    . ARG A 1 236 ? 140.223 160.592 163.290 1.00 27.17  ? 237  ARG A CZ    1 
ATOM   1778 N  NH1   . ARG A 1 236 ? 140.815 160.224 162.169 1.00 27.17  ? 237  ARG A NH1   1 
ATOM   1779 N  NH2   . ARG A 1 236 ? 140.491 161.782 163.807 1.00 27.17  ? 237  ARG A NH2   1 
ATOM   1780 N  N     . ASN A 1 237 ? 136.626 155.111 165.434 1.00 24.48  ? 238  ASN A N     1 
ATOM   1781 C  CA    . ASN A 1 237 ? 136.123 154.091 164.520 1.00 24.48  ? 238  ASN A CA    1 
ATOM   1782 C  C     . ASN A 1 237 ? 135.540 152.936 165.321 1.00 24.48  ? 238  ASN A C     1 
ATOM   1783 O  O     . ASN A 1 237 ? 136.226 152.358 166.166 1.00 24.48  ? 238  ASN A O     1 
ATOM   1784 C  CB    . ASN A 1 237 ? 137.248 153.574 163.622 1.00 24.48  ? 238  ASN A CB    1 
ATOM   1785 C  CG    . ASN A 1 237 ? 136.807 152.460 162.704 1.00 24.48  ? 238  ASN A CG    1 
ATOM   1786 O  OD1   . ASN A 1 237 ? 135.621 152.286 162.425 1.00 24.48  ? 238  ASN A OD1   1 
ATOM   1787 N  ND2   . ASN A 1 237 ? 137.766 151.675 162.247 1.00 24.48  ? 238  ASN A ND2   1 
ATOM   1788 N  N     . ASP A 1 238 ? 134.289 152.581 165.006 1.00 24.59  ? 239  ASP A N     1 
ATOM   1789 C  CA    . ASP A 1 238 ? 133.580 151.473 165.643 1.00 24.59  ? 239  ASP A CA    1 
ATOM   1790 C  C     . ASP A 1 238 ? 134.236 150.107 165.455 1.00 24.59  ? 239  ASP A C     1 
ATOM   1791 O  O     . ASP A 1 238 ? 133.908 149.179 166.197 1.00 24.59  ? 239  ASP A O     1 
ATOM   1792 C  CB    . ASP A 1 238 ? 132.147 151.409 165.125 1.00 24.59  ? 239  ASP A CB    1 
ATOM   1793 C  CG    . ASP A 1 238 ? 131.327 152.610 165.535 1.00 24.59  ? 239  ASP A CG    1 
ATOM   1794 O  OD1   . ASP A 1 238 ? 131.880 153.504 166.205 1.00 24.59  ? 239  ASP A OD1   1 
ATOM   1795 O  OD2   . ASP A 1 238 ? 130.125 152.655 165.203 1.00 24.59  ? 239  ASP A OD2   1 
ATOM   1796 N  N     . ASN A 1 239 ? 135.126 149.944 164.480 1.00 20.72  ? 240  ASN A N     1 
ATOM   1797 C  CA    . ASN A 1 239 ? 135.816 148.675 164.271 1.00 20.72  ? 240  ASN A CA    1 
ATOM   1798 C  C     . ASN A 1 239 ? 137.330 148.884 164.238 1.00 20.72  ? 240  ASN A C     1 
ATOM   1799 O  O     . ASN A 1 239 ? 138.039 148.219 163.479 1.00 20.72  ? 240  ASN A O     1 
ATOM   1800 C  CB    . ASN A 1 239 ? 135.299 147.987 163.003 1.00 20.72  ? 240  ASN A CB    1 
ATOM   1801 C  CG    . ASN A 1 239 ? 135.691 146.522 162.918 1.00 20.72  ? 240  ASN A CG    1 
ATOM   1802 O  OD1   . ASN A 1 239 ? 136.057 145.916 163.917 1.00 20.72  ? 240  ASN A OD1   1 
ATOM   1803 N  ND2   . ASN A 1 239 ? 135.632 145.959 161.722 1.00 20.72  ? 240  ASN A ND2   1 
ATOM   1804 N  N     . SER A 1 240 ? 137.811 149.887 164.979 1.00 20.68  ? 241  SER A N     1 
ATOM   1805 C  CA    . SER A 1 240 ? 139.228 150.245 165.021 1.00 20.68  ? 241  SER A CA    1 
ATOM   1806 C  C     . SER A 1 240 ? 140.114 149.060 165.376 1.00 20.68  ? 241  SER A C     1 
ATOM   1807 O  O     . SER A 1 240 ? 139.940 148.427 166.416 1.00 20.68  ? 241  SER A O     1 
ATOM   1808 C  CB    . SER A 1 240 ? 139.433 151.359 166.034 1.00 20.68  ? 241  SER A CB    1 
ATOM   1809 O  OG    . SER A 1 240 ? 139.532 150.822 167.336 1.00 20.68  ? 241  SER A OG    1 
ATOM   1810 N  N     . SER A 1 241 ? 141.090 148.797 164.514 1.00 19.85  ? 242  SER A N     1 
ATOM   1811 C  CA    . SER A 1 241 ? 141.903 147.583 164.561 1.00 19.85  ? 242  SER A CA    1 
ATOM   1812 C  C     . SER A 1 241 ? 143.182 147.808 165.352 1.00 19.85  ? 242  SER A C     1 
ATOM   1813 O  O     . SER A 1 241 ? 144.204 148.221 164.811 1.00 19.85  ? 242  SER A O     1 
ATOM   1814 C  CB    . SER A 1 241 ? 142.216 147.097 163.152 1.00 19.85  ? 242  SER A CB    1 
ATOM   1815 O  OG    . SER A 1 241 ? 142.708 148.145 162.341 1.00 19.85  ? 242  SER A OG    1 
ATOM   1816 N  N     . ARG A 1 242 ? 143.131 147.522 166.654 1.00 17.92  ? 243  ARG A N     1 
ATOM   1817 C  CA    . ARG A 1 242 ? 144.170 147.873 167.623 1.00 17.92  ? 243  ARG A CA    1 
ATOM   1818 C  C     . ARG A 1 242 ? 145.481 147.097 167.474 1.00 17.92  ? 243  ARG A C     1 
ATOM   1819 O  O     . ARG A 1 242 ? 146.237 146.988 168.443 1.00 17.92  ? 243  ARG A O     1 
ATOM   1820 C  CB    . ARG A 1 242 ? 143.669 147.659 169.051 1.00 17.92  ? 243  ARG A CB    1 
ATOM   1821 C  CG    . ARG A 1 242 ? 142.258 148.090 169.345 1.00 17.92  ? 243  ARG A CG    1 
ATOM   1822 C  CD    . ARG A 1 242 ? 142.038 149.548 169.042 1.00 17.92  ? 243  ARG A CD    1 
ATOM   1823 N  NE    . ARG A 1 242 ? 142.938 150.402 169.806 1.00 17.92  ? 243  ARG A NE    1 
ATOM   1824 C  CZ    . ARG A 1 242 ? 143.352 151.599 169.406 1.00 17.92  ? 243  ARG A CZ    1 
ATOM   1825 N  NH1   . ARG A 1 242 ? 144.248 152.265 170.111 1.00 17.92  ? 243  ARG A NH1   1 
ATOM   1826 N  NH2   . ARG A 1 242 ? 142.912 152.107 168.268 1.00 17.92  ? 243  ARG A NH2   1 
ATOM   1827 N  N     . PHE A 1 243 ? 145.765 146.539 166.300 1.00 18.54  ? 244  PHE A N     1 
ATOM   1828 C  CA    . PHE A 1 243 ? 147.027 145.868 166.040 1.00 18.54  ? 244  PHE A CA    1 
ATOM   1829 C  C     . PHE A 1 243 ? 147.454 146.121 164.601 1.00 18.54  ? 244  PHE A C     1 
ATOM   1830 O  O     . PHE A 1 243 ? 146.623 146.168 163.694 1.00 18.54  ? 244  PHE A O     1 
ATOM   1831 C  CB    . PHE A 1 243 ? 146.945 144.351 166.327 1.00 18.54  ? 244  PHE A CB    1 
ATOM   1832 C  CG    . PHE A 1 243 ? 146.024 143.582 165.417 1.00 18.54  ? 244  PHE A CG    1 
ATOM   1833 C  CD1   . PHE A 1 243 ? 144.650 143.653 165.555 1.00 18.54  ? 244  PHE A CD1   1 
ATOM   1834 C  CD2   . PHE A 1 243 ? 146.544 142.773 164.430 1.00 18.54  ? 244  PHE A CD2   1 
ATOM   1835 C  CE1   . PHE A 1 243 ? 143.824 142.947 164.720 1.00 18.54  ? 244  PHE A CE1   1 
ATOM   1836 C  CE2   . PHE A 1 243 ? 145.718 142.068 163.594 1.00 18.54  ? 244  PHE A CE2   1 
ATOM   1837 C  CZ    . PHE A 1 243 ? 144.359 142.156 163.739 1.00 18.54  ? 244  PHE A CZ    1 
ATOM   1838 N  N     . GLY A 1 244 ? 148.756 146.316 164.408 1.00 21.96  ? 245  GLY A N     1 
ATOM   1839 C  CA    . GLY A 1 244 ? 149.303 146.486 163.072 1.00 21.96  ? 245  GLY A CA    1 
ATOM   1840 C  C     . GLY A 1 244 ? 149.589 145.151 162.419 1.00 21.96  ? 245  GLY A C     1 
ATOM   1841 O  O     . GLY A 1 244 ? 150.274 144.302 162.995 1.00 21.96  ? 245  GLY A O     1 
ATOM   1842 N  N     . LYS A 1 245 ? 149.076 144.965 161.207 1.00 20.60  ? 246  LYS A N     1 
ATOM   1843 C  CA    . LYS A 1 245 ? 149.063 143.667 160.548 1.00 20.60  ? 246  LYS A CA    1 
ATOM   1844 C  C     . LYS A 1 245 ? 149.799 143.752 159.220 1.00 20.60  ? 246  LYS A C     1 
ATOM   1845 O  O     . LYS A 1 245 ? 149.584 144.689 158.449 1.00 20.60  ? 246  LYS A O     1 
ATOM   1846 C  CB    . LYS A 1 245 ? 147.620 143.209 160.352 1.00 20.60  ? 246  LYS A CB    1 
ATOM   1847 C  CG    . LYS A 1 245 ? 147.407 142.058 159.404 1.00 20.60  ? 246  LYS A CG    1 
ATOM   1848 C  CD    . LYS A 1 245 ? 145.995 141.477 159.532 1.00 20.60  ? 246  LYS A CD    1 
ATOM   1849 C  CE    . LYS A 1 245 ? 144.909 142.547 159.711 1.00 20.60  ? 246  LYS A CE    1 
ATOM   1850 N  NZ    . LYS A 1 245 ? 144.710 143.401 158.511 1.00 20.60  ? 246  LYS A NZ    1 
ATOM   1851 N  N     . PHE A 1 246 ? 150.659 142.768 158.955 1.00 20.23  ? 247  PHE A N     1 
ATOM   1852 C  CA    . PHE A 1 246 ? 151.399 142.658 157.699 1.00 20.23  ? 247  PHE A CA    1 
ATOM   1853 C  C     . PHE A 1 246 ? 151.143 141.260 157.152 1.00 20.23  ? 247  PHE A C     1 
ATOM   1854 O  O     . PHE A 1 246 ? 151.650 140.278 157.702 1.00 20.23  ? 247  PHE A O     1 
ATOM   1855 C  CB    . PHE A 1 246 ? 152.889 142.904 157.948 1.00 20.23  ? 247  PHE A CB    1 
ATOM   1856 C  CG    . PHE A 1 246 ? 153.742 142.929 156.708 1.00 20.23  ? 247  PHE A CG    1 
ATOM   1857 C  CD1   . PHE A 1 246 ? 153.452 143.787 155.661 1.00 20.23  ? 247  PHE A CD1   1 
ATOM   1858 C  CD2   . PHE A 1 246 ? 154.876 142.138 156.622 1.00 20.23  ? 247  PHE A CD2   1 
ATOM   1859 C  CE1   . PHE A 1 246 ? 154.253 143.825 154.536 1.00 20.23  ? 247  PHE A CE1   1 
ATOM   1860 C  CE2   . PHE A 1 246 ? 155.680 142.174 155.501 1.00 20.23  ? 247  PHE A CE2   1 
ATOM   1861 C  CZ    . PHE A 1 246 ? 155.365 143.018 154.458 1.00 20.23  ? 247  PHE A CZ    1 
ATOM   1862 N  N     . ILE A 1 247 ? 150.386 141.165 156.063 1.00 18.33  ? 248  ILE A N     1 
ATOM   1863 C  CA    . ILE A 1 247 ? 150.004 139.887 155.473 1.00 18.33  ? 248  ILE A CA    1 
ATOM   1864 C  C     . ILE A 1 247 ? 150.918 139.617 154.293 1.00 18.33  ? 248  ILE A C     1 
ATOM   1865 O  O     . ILE A 1 247 ? 150.807 140.277 153.260 1.00 18.33  ? 248  ILE A O     1 
ATOM   1866 C  CB    . ILE A 1 247 ? 148.544 139.900 155.012 1.00 18.33  ? 248  ILE A CB    1 
ATOM   1867 C  CG1   . ILE A 1 247 ? 147.619 140.304 156.151 1.00 18.33  ? 248  ILE A CG1   1 
ATOM   1868 C  CG2   . ILE A 1 247 ? 148.154 138.546 154.513 1.00 18.33  ? 248  ILE A CG2   1 
ATOM   1869 C  CD1   . ILE A 1 247 ? 146.189 140.498 155.720 1.00 18.33  ? 248  ILE A CD1   1 
ATOM   1870 N  N     . ARG A 1 248 ? 151.785 138.620 154.404 1.00 23.41  ? 249  ARG A N     1 
ATOM   1871 C  CA    . ARG A 1 248 ? 152.573 138.172 153.262 1.00 23.41  ? 249  ARG A CA    1 
ATOM   1872 C  C     . ARG A 1 248 ? 151.809 137.080 152.525 1.00 23.41  ? 249  ARG A C     1 
ATOM   1873 O  O     . ARG A 1 248 ? 151.718 135.952 153.009 1.00 23.41  ? 249  ARG A O     1 
ATOM   1874 C  CB    . ARG A 1 248 ? 153.935 137.655 153.707 1.00 23.41  ? 249  ARG A CB    1 
ATOM   1875 C  CG    . ARG A 1 248 ? 154.726 138.609 154.556 1.00 23.41  ? 249  ARG A CG    1 
ATOM   1876 C  CD    . ARG A 1 248 ? 156.187 138.238 154.520 1.00 23.41  ? 249  ARG A CD    1 
ATOM   1877 N  NE    . ARG A 1 248 ? 156.402 136.840 154.865 1.00 23.41  ? 249  ARG A NE    1 
ATOM   1878 C  CZ    . ARG A 1 248 ? 157.486 136.154 154.524 1.00 23.41  ? 249  ARG A CZ    1 
ATOM   1879 N  NH1   . ARG A 1 248 ? 157.590 134.872 154.840 1.00 23.41  ? 249  ARG A NH1   1 
ATOM   1880 N  NH2   . ARG A 1 248 ? 158.456 136.743 153.842 1.00 23.41  ? 249  ARG A NH2   1 
ATOM   1881 N  N     . ILE A 1 249 ? 151.280 137.401 151.353 1.00 25.15  ? 250  ILE A N     1 
ATOM   1882 C  CA    . ILE A 1 249 ? 150.748 136.399 150.438 1.00 25.15  ? 250  ILE A CA    1 
ATOM   1883 C  C     . ILE A 1 249 ? 151.896 135.879 149.593 1.00 25.15  ? 250  ILE A C     1 
ATOM   1884 O  O     . ILE A 1 249 ? 152.641 136.667 149.008 1.00 25.15  ? 250  ILE A O     1 
ATOM   1885 C  CB    . ILE A 1 249 ? 149.646 136.995 149.549 1.00 25.15  ? 250  ILE A CB    1 
ATOM   1886 C  CG1   . ILE A 1 249 ? 148.578 137.673 150.388 1.00 25.15  ? 250  ILE A CG1   1 
ATOM   1887 C  CG2   . ILE A 1 249 ? 149.007 135.931 148.732 1.00 25.15  ? 250  ILE A CG2   1 
ATOM   1888 C  CD1   . ILE A 1 249 ? 147.893 136.714 151.315 1.00 25.15  ? 250  ILE A CD1   1 
ATOM   1889 N  N     . HIS A 1 250 ? 152.032 134.563 149.497 1.00 29.92  ? 251  HIS A N     1 
ATOM   1890 C  CA    . HIS A 1 250 ? 153.111 133.971 148.722 1.00 29.92  ? 251  HIS A CA    1 
ATOM   1891 C  C     . HIS A 1 250 ? 152.588 133.366 147.428 1.00 29.92  ? 251  HIS A C     1 
ATOM   1892 O  O     . HIS A 1 250 ? 151.542 132.711 147.413 1.00 29.92  ? 251  HIS A O     1 
ATOM   1893 C  CB    . HIS A 1 250 ? 153.833 132.890 149.521 1.00 29.92  ? 251  HIS A CB    1 
ATOM   1894 C  CG    . HIS A 1 250 ? 154.764 133.428 150.555 1.00 29.92  ? 251  HIS A CG    1 
ATOM   1895 N  ND1   . HIS A 1 250 ? 155.979 133.991 150.238 1.00 29.92  ? 251  HIS A ND1   1 
ATOM   1896 C  CD2   . HIS A 1 250 ? 154.673 133.464 151.904 1.00 29.92  ? 251  HIS A CD2   1 
ATOM   1897 C  CE1   . HIS A 1 250 ? 156.592 134.363 151.346 1.00 29.92  ? 251  HIS A CE1   1 
ATOM   1898 N  NE2   . HIS A 1 250 ? 155.820 134.056 152.372 1.00 29.92  ? 251  HIS A NE2   1 
ATOM   1899 N  N     . PHE A 1 251 ? 153.332 133.579 146.346 1.00 33.35  ? 252  PHE A N     1 
ATOM   1900 C  CA    . PHE A 1 251 ? 152.974 133.081 145.028 1.00 33.35  ? 252  PHE A CA    1 
ATOM   1901 C  C     . PHE A 1 251 ? 154.100 132.246 144.437 1.00 33.35  ? 252  PHE A C     1 
ATOM   1902 O  O     . PHE A 1 251 ? 155.282 132.545 144.627 1.00 33.35  ? 252  PHE A O     1 
ATOM   1903 C  CB    . PHE A 1 251 ? 152.616 134.205 144.061 1.00 33.35  ? 252  PHE A CB    1 
ATOM   1904 C  CG    . PHE A 1 251 ? 151.367 134.941 144.423 1.00 33.35  ? 252  PHE A CG    1 
ATOM   1905 C  CD1   . PHE A 1 251 ? 150.140 134.500 143.956 1.00 33.35  ? 252  PHE A CD1   1 
ATOM   1906 C  CD2   . PHE A 1 251 ? 151.415 136.086 145.184 1.00 33.35  ? 252  PHE A CD2   1 
ATOM   1907 C  CE1   . PHE A 1 251 ? 148.979 135.173 144.272 1.00 33.35  ? 252  PHE A CE1   1 
ATOM   1908 C  CE2   . PHE A 1 251 ? 150.257 136.763 145.494 1.00 33.35  ? 252  PHE A CE2   1 
ATOM   1909 C  CZ    . PHE A 1 251 ? 149.038 136.306 145.038 1.00 33.35  ? 252  PHE A CZ    1 
ATOM   1910 N  N     . GLY A 1 252 ? 153.712 131.199 143.722 1.00 42.61  ? 253  GLY A N     1 
ATOM   1911 C  CA    . GLY A 1 252 ? 154.656 130.345 143.039 1.00 42.61  ? 253  GLY A CA    1 
ATOM   1912 C  C     . GLY A 1 252 ? 155.149 130.978 141.754 1.00 42.61  ? 253  GLY A C     1 
ATOM   1913 O  O     . GLY A 1 252 ? 154.691 132.051 141.357 1.00 42.61  ? 253  GLY A O     1 
ATOM   1914 N  N     . ALA A 1 253 ? 156.133 130.310 141.138 1.00 46.90  ? 254  ALA A N     1 
ATOM   1915 C  CA    . ALA A 1 253 ? 156.745 130.808 139.906 1.00 46.90  ? 254  ALA A CA    1 
ATOM   1916 C  C     . ALA A 1 253 ? 155.738 130.925 138.769 1.00 46.90  ? 254  ALA A C     1 
ATOM   1917 O  O     . ALA A 1 253 ? 155.848 131.831 137.935 1.00 46.90  ? 254  ALA A O     1 
ATOM   1918 C  CB    . ALA A 1 253 ? 157.902 129.899 139.493 1.00 46.90  ? 254  ALA A CB    1 
ATOM   1919 N  N     . THR A 1 254 ? 154.745 130.035 138.726 1.00 47.88  ? 255  THR A N     1 
ATOM   1920 C  CA    . THR A 1 254 ? 153.674 130.129 137.742 1.00 47.88  ? 255  THR A CA    1 
ATOM   1921 C  C     . THR A 1 254 ? 152.715 131.286 138.039 1.00 47.88  ? 255  THR A C     1 
ATOM   1922 O  O     . THR A 1 254 ? 151.981 131.717 137.143 1.00 47.88  ? 255  THR A O     1 
ATOM   1923 C  CB    . THR A 1 254 ? 152.945 128.773 137.704 1.00 47.88  ? 255  THR A CB    1 
ATOM   1924 O  OG1   . THR A 1 254 ? 153.921 127.726 137.642 1.00 47.88  ? 255  THR A OG1   1 
ATOM   1925 C  CG2   . THR A 1 254 ? 152.065 128.617 136.464 1.00 47.88  ? 255  THR A CG2   1 
ATOM   1926 N  N     . GLY A 1 255 ? 152.775 131.870 139.236 1.00 39.81  ? 256  GLY A N     1 
ATOM   1927 C  CA    . GLY A 1 255 ? 151.894 132.957 139.609 1.00 39.81  ? 256  GLY A CA    1 
ATOM   1928 C  C     . GLY A 1 255 ? 150.656 132.559 140.382 1.00 39.81  ? 256  GLY A C     1 
ATOM   1929 O  O     . GLY A 1 255 ? 149.868 133.437 140.748 1.00 39.81  ? 256  GLY A O     1 
ATOM   1930 N  N     . LYS A 1 256 ? 150.453 131.271 140.626 1.00 39.05  ? 257  LYS A N     1 
ATOM   1931 C  CA    . LYS A 1 256 ? 149.318 130.808 141.406 1.00 39.05  ? 257  LYS A CA    1 
ATOM   1932 C  C     . LYS A 1 256 ? 149.527 131.091 142.894 1.00 39.05  ? 257  LYS A C     1 
ATOM   1933 O  O     . LYS A 1 256 ? 150.648 131.298 143.366 1.00 39.05  ? 257  LYS A O     1 
ATOM   1934 C  CB    . LYS A 1 256 ? 149.087 129.319 141.153 1.00 39.05  ? 257  LYS A CB    1 
ATOM   1935 C  CG    . LYS A 1 256 ? 149.959 128.389 141.972 1.00 39.05  ? 257  LYS A CG    1 
ATOM   1936 C  CD    . LYS A 1 256 ? 149.805 126.958 141.496 1.00 39.05  ? 257  LYS A CD    1 
ATOM   1937 C  CE    . LYS A 1 256 ? 150.189 125.980 142.579 1.00 39.05  ? 257  LYS A CE    1 
ATOM   1938 N  NZ    . LYS A 1 256 ? 149.059 125.785 143.518 1.00 39.05  ? 257  LYS A NZ    1 
ATOM   1939 N  N     . LEU A 1 257 ? 148.413 131.140 143.624 1.00 36.23  ? 258  LEU A N     1 
ATOM   1940 C  CA    . LEU A 1 257 ? 148.428 131.306 145.077 1.00 36.23  ? 258  LEU A CA    1 
ATOM   1941 C  C     . LEU A 1 257 ? 149.055 130.093 145.758 1.00 36.23  ? 258  LEU A C     1 
ATOM   1942 O  O     . LEU A 1 257 ? 148.572 128.967 145.599 1.00 36.23  ? 258  LEU A O     1 
ATOM   1943 C  CB    . LEU A 1 257 ? 147.003 131.530 145.572 1.00 36.23  ? 258  LEU A CB    1 
ATOM   1944 C  CG    . LEU A 1 257 ? 146.721 131.662 147.062 1.00 36.23  ? 258  LEU A CG    1 
ATOM   1945 C  CD1   . LEU A 1 257 ? 147.445 132.845 147.577 1.00 36.23  ? 258  LEU A CD1   1 
ATOM   1946 C  CD2   . LEU A 1 257 ? 145.236 131.843 147.296 1.00 36.23  ? 258  LEU A CD2   1 
ATOM   1947 N  N     . ALA A 1 258 ? 150.123 130.319 146.526 1.00 34.99  ? 259  ALA A N     1 
ATOM   1948 C  CA    . ALA A 1 258 ? 150.868 129.227 147.144 1.00 34.99  ? 259  ALA A CA    1 
ATOM   1949 C  C     . ALA A 1 258 ? 150.592 129.071 148.637 1.00 34.99  ? 259  ALA A C     1 
ATOM   1950 O  O     . ALA A 1 258 ? 150.201 127.987 149.078 1.00 34.99  ? 259  ALA A O     1 
ATOM   1951 C  CB    . ALA A 1 258 ? 152.365 129.438 146.911 1.00 34.99  ? 259  ALA A CB    1 
ATOM   1952 N  N     . SER A 1 259 ? 150.801 130.127 149.423 1.00 31.66  ? 260  SER A N     1 
ATOM   1953 C  CA    . SER A 1 259 ? 150.633 130.088 150.874 1.00 31.66  ? 260  SER A CA    1 
ATOM   1954 C  C     . SER A 1 259 ? 150.532 131.522 151.379 1.00 31.66  ? 260  SER A C     1 
ATOM   1955 O  O     . SER A 1 259 ? 150.630 132.478 150.605 1.00 31.66  ? 260  SER A O     1 
ATOM   1956 C  CB    . SER A 1 259 ? 151.777 129.331 151.557 1.00 31.66  ? 260  SER A CB    1 
ATOM   1957 O  OG    . SER A 1 259 ? 153.002 130.024 151.430 1.00 31.66  ? 260  SER A OG    1 
ATOM   1958 N  N     . ALA A 1 260 ? 150.336 131.672 152.689 1.00 26.58  ? 261  ALA A N     1 
ATOM   1959 C  CA    . ALA A 1 260 ? 150.345 132.999 153.290 1.00 26.58  ? 261  ALA A CA    1 
ATOM   1960 C  C     . ALA A 1 260 ? 150.852 132.948 154.724 1.00 26.58  ? 261  ALA A C     1 
ATOM   1961 O  O     . ALA A 1 260 ? 150.735 131.926 155.401 1.00 26.58  ? 261  ALA A O     1 
ATOM   1962 C  CB    . ALA A 1 260 ? 148.958 133.632 153.253 1.00 26.58  ? 261  ALA A CB    1 
ATOM   1963 N  N     . ASP A 1 261 ? 151.415 134.070 155.181 1.00 23.66  ? 262  ASP A N     1 
ATOM   1964 C  CA    . ASP A 1 261 ? 151.857 134.274 156.557 1.00 23.66  ? 262  ASP A CA    1 
ATOM   1965 C  C     . ASP A 1 261 ? 151.262 135.570 157.093 1.00 23.66  ? 262  ASP A C     1 
ATOM   1966 O  O     . ASP A 1 261 ? 151.213 136.576 156.382 1.00 23.66  ? 262  ASP A O     1 
ATOM   1967 C  CB    . ASP A 1 261 ? 153.395 134.378 156.703 1.00 23.66  ? 262  ASP A CB    1 
ATOM   1968 C  CG    . ASP A 1 261 ? 154.159 133.176 156.157 1.00 23.66  ? 262  ASP A CG    1 
ATOM   1969 O  OD1   . ASP A 1 261 ? 153.564 132.167 155.748 1.00 23.66  ? 262  ASP A OD1   1 
ATOM   1970 O  OD2   . ASP A 1 261 ? 155.404 133.250 156.147 1.00 23.66  ? 262  ASP A OD2   1 
ATOM   1971 N  N     . ILE A 1 262 ? 150.829 135.550 158.352 1.00 19.97  ? 263  ILE A N     1 
ATOM   1972 C  CA    . ILE A 1 262 ? 150.393 136.742 159.073 1.00 19.97  ? 263  ILE A CA    1 
ATOM   1973 C  C     . ILE A 1 262 ? 151.476 137.125 160.070 1.00 19.97  ? 263  ILE A C     1 
ATOM   1974 O  O     . ILE A 1 262 ? 152.026 136.258 160.757 1.00 19.97  ? 263  ILE A O     1 
ATOM   1975 C  CB    . ILE A 1 262 ? 149.057 136.515 159.804 1.00 19.97  ? 263  ILE A CB    1 
ATOM   1976 C  CG1   . ILE A 1 262 ? 148.058 135.780 158.915 1.00 19.97  ? 263  ILE A CG1   1 
ATOM   1977 C  CG2   . ILE A 1 262 ? 148.462 137.836 160.242 1.00 19.97  ? 263  ILE A CG2   1 
ATOM   1978 C  CD1   . ILE A 1 262 ? 147.632 136.549 157.695 1.00 19.97  ? 263  ILE A CD1   1 
ATOM   1979 N  N     . GLU A 1 263 ? 151.793 138.417 160.146 1.00 23.25  ? 264  GLU A N     1 
ATOM   1980 C  CA    . GLU A 1 263 ? 152.505 138.977 161.289 1.00 23.25  ? 264  GLU A CA    1 
ATOM   1981 C  C     . GLU A 1 263 ? 151.705 140.116 161.903 1.00 23.25  ? 264  GLU A C     1 
ATOM   1982 O  O     . GLU A 1 263 ? 151.056 140.884 161.190 1.00 23.25  ? 264  GLU A O     1 
ATOM   1983 C  CB    . GLU A 1 263 ? 153.892 139.473 160.892 1.00 23.25  ? 264  GLU A CB    1 
ATOM   1984 C  CG    . GLU A 1 263 ? 154.901 138.361 160.674 1.00 23.25  ? 264  GLU A CG    1 
ATOM   1985 C  CD    . GLU A 1 263 ? 155.148 137.551 161.929 1.00 23.25  ? 264  GLU A CD    1 
ATOM   1986 O  OE1   . GLU A 1 263 ? 155.859 138.048 162.827 1.00 23.25  ? 264  GLU A OE1   1 
ATOM   1987 O  OE2   . GLU A 1 263 ? 154.634 136.418 162.020 1.00 23.25  ? 264  GLU A OE2   1 
ATOM   1988 N  N     . THR A 1 264 ? 151.760 140.223 163.233 1.00 22.37  ? 265  THR A N     1 
ATOM   1989 C  CA    . THR A 1 264 ? 150.963 141.182 164.001 1.00 22.37  ? 265  THR A CA    1 
ATOM   1990 C  C     . THR A 1 264 ? 151.867 141.812 165.050 1.00 22.37  ? 265  THR A C     1 
ATOM   1991 O  O     . THR A 1 264 ? 152.296 141.128 165.984 1.00 22.37  ? 265  THR A O     1 
ATOM   1992 C  CB    . THR A 1 264 ? 149.763 140.519 164.679 1.00 22.37  ? 265  THR A CB    1 
ATOM   1993 O  OG1   . THR A 1 264 ? 150.219 139.427 165.485 1.00 22.37  ? 265  THR A OG1   1 
ATOM   1994 C  CG2   . THR A 1 264 ? 148.742 140.020 163.672 1.00 22.37  ? 265  THR A CG2   1 
ATOM   1995 N  N     . TYR A 1 265 ? 152.159 143.104 164.904 1.00 26.78  ? 266  TYR A N     1 
ATOM   1996 C  CA    . TYR A 1 265 ? 153.349 143.663 165.535 1.00 26.78  ? 266  TYR A CA    1 
ATOM   1997 C  C     . TYR A 1 265 ? 153.150 144.132 166.972 1.00 26.78  ? 266  TYR A C     1 
ATOM   1998 O  O     . TYR A 1 265 ? 154.029 143.904 167.811 1.00 26.78  ? 266  TYR A O     1 
ATOM   1999 C  CB    . TYR A 1 265 ? 153.902 144.803 164.678 1.00 26.78  ? 266  TYR A CB    1 
ATOM   2000 C  CG    . TYR A 1 265 ? 154.632 144.270 163.481 1.00 26.78  ? 266  TYR A CG    1 
ATOM   2001 C  CD1   . TYR A 1 265 ? 155.760 143.481 163.656 1.00 26.78  ? 266  TYR A CD1   1 
ATOM   2002 C  CD2   . TYR A 1 265 ? 154.186 144.506 162.194 1.00 26.78  ? 266  TYR A CD2   1 
ATOM   2003 C  CE1   . TYR A 1 265 ? 156.456 142.990 162.591 1.00 26.78  ? 266  TYR A CE1   1 
ATOM   2004 C  CE2   . TYR A 1 265 ? 154.867 143.991 161.112 1.00 26.78  ? 266  TYR A CE2   1 
ATOM   2005 C  CZ    . TYR A 1 265 ? 156.007 143.238 161.323 1.00 26.78  ? 266  TYR A CZ    1 
ATOM   2006 O  OH    . TYR A 1 265 ? 156.693 142.688 160.270 1.00 26.78  ? 266  TYR A OH    1 
ATOM   2007 N  N     . LEU A 1 266 ? 152.029 144.764 167.298 1.00 22.79  ? 267  LEU A N     1 
ATOM   2008 C  CA    . LEU A 1 266 ? 151.798 145.140 168.683 1.00 22.79  ? 267  LEU A CA    1 
ATOM   2009 C  C     . LEU A 1 266 ? 150.307 145.058 168.955 1.00 22.79  ? 267  LEU A C     1 
ATOM   2010 O  O     . LEU A 1 266 ? 149.500 145.295 168.061 1.00 22.79  ? 267  LEU A O     1 
ATOM   2011 C  CB    . LEU A 1 266 ? 152.328 146.549 168.966 1.00 22.79  ? 267  LEU A CB    1 
ATOM   2012 C  CG    . LEU A 1 266 ? 152.357 147.026 170.415 1.00 22.79  ? 267  LEU A CG    1 
ATOM   2013 C  CD1   . LEU A 1 266 ? 153.400 146.256 171.202 1.00 22.79  ? 267  LEU A CD1   1 
ATOM   2014 C  CD2   . LEU A 1 266 ? 152.621 148.493 170.483 1.00 22.79  ? 267  LEU A CD2   1 
ATOM   2015 N  N     . LEU A 1 267 ? 149.943 144.755 170.196 1.00 20.66  ? 268  LEU A N     1 
ATOM   2016 C  CA    . LEU A 1 267 ? 148.551 144.741 170.615 1.00 20.66  ? 268  LEU A CA    1 
ATOM   2017 C  C     . LEU A 1 267 ? 148.372 145.691 171.790 1.00 20.66  ? 268  LEU A C     1 
ATOM   2018 O  O     . LEU A 1 267 ? 149.226 145.759 172.677 1.00 20.66  ? 268  LEU A O     1 
ATOM   2019 C  CB    . LEU A 1 267 ? 148.120 143.320 170.990 1.00 20.66  ? 268  LEU A CB    1 
ATOM   2020 C  CG    . LEU A 1 267 ? 146.695 143.077 171.470 1.00 20.66  ? 268  LEU A CG    1 
ATOM   2021 C  CD1   . LEU A 1 267 ? 145.743 143.307 170.337 1.00 20.66  ? 268  LEU A CD1   1 
ATOM   2022 C  CD2   . LEU A 1 267 ? 146.560 141.666 171.979 1.00 20.66  ? 268  LEU A CD2   1 
ATOM   2023 N  N     . GLU A 1 268 ? 147.259 146.425 171.796 1.00 19.90  ? 269  GLU A N     1 
ATOM   2024 C  CA    . GLU A 1 268 ? 146.909 147.328 172.890 1.00 19.90  ? 269  GLU A CA    1 
ATOM   2025 C  C     . GLU A 1 268 ? 146.408 146.545 174.102 1.00 19.90  ? 269  GLU A C     1 
ATOM   2026 O  O     . GLU A 1 268 ? 145.222 146.597 174.438 1.00 19.90  ? 269  GLU A O     1 
ATOM   2027 C  CB    . GLU A 1 268 ? 145.876 148.352 172.414 1.00 19.90  ? 269  GLU A CB    1 
ATOM   2028 C  CG    . GLU A 1 268 ? 145.630 149.529 173.347 1.00 19.90  ? 269  GLU A CG    1 
ATOM   2029 C  CD    . GLU A 1 268 ? 144.673 150.531 172.759 1.00 19.90  ? 269  GLU A CD    1 
ATOM   2030 O  OE1   . GLU A 1 268 ? 143.530 150.146 172.450 1.00 19.90  ? 269  GLU A OE1   1 
ATOM   2031 O  OE2   . GLU A 1 268 ? 145.054 151.709 172.607 1.00 19.90  ? 269  GLU A OE2   1 
ATOM   2032 N  N     . LYS A 1 269 ? 147.293 145.741 174.700 1.00 22.36  ? 270  LYS A N     1 
ATOM   2033 C  CA    . LYS A 1 269 ? 146.933 144.755 175.717 1.00 22.36  ? 270  LYS A CA    1 
ATOM   2034 C  C     . LYS A 1 269 ? 146.326 145.365 176.975 1.00 22.36  ? 270  LYS A C     1 
ATOM   2035 O  O     . LYS A 1 269 ? 145.655 144.653 177.725 1.00 22.36  ? 270  LYS A O     1 
ATOM   2036 C  CB    . LYS A 1 269 ? 148.167 143.921 176.065 1.00 22.36  ? 270  LYS A CB    1 
ATOM   2037 C  CG    . LYS A 1 269 ? 149.311 144.734 176.635 1.00 22.36  ? 270  LYS A CG    1 
ATOM   2038 C  CD    . LYS A 1 269 ? 150.618 143.956 176.651 1.00 22.36  ? 270  LYS A CD    1 
ATOM   2039 C  CE    . LYS A 1 269 ? 150.684 142.963 177.781 1.00 22.36  ? 270  LYS A CE    1 
ATOM   2040 N  NZ    . LYS A 1 269 ? 151.994 142.263 177.784 1.00 22.36  ? 270  LYS A NZ    1 
ATOM   2041 N  N     . SER A 1 270 ? 146.540 146.657 177.228 1.00 22.39  ? 271  SER A N     1 
ATOM   2042 C  CA    . SER A 1 270 ? 145.895 147.314 178.358 1.00 22.39  ? 271  SER A CA    1 
ATOM   2043 C  C     . SER A 1 270 ? 144.406 147.571 178.161 1.00 22.39  ? 271  SER A C     1 
ATOM   2044 O  O     . SER A 1 270 ? 143.723 147.886 179.138 1.00 22.39  ? 271  SER A O     1 
ATOM   2045 C  CB    . SER A 1 270 ? 146.595 148.633 178.664 1.00 22.39  ? 271  SER A CB    1 
ATOM   2046 O  OG    . SER A 1 270 ? 146.270 149.080 179.967 1.00 22.39  ? 271  SER A OG    1 
ATOM   2047 N  N     . ARG A 1 271 ? 143.893 147.501 176.932 1.00 21.14  ? 272  ARG A N     1 
ATOM   2048 C  CA    . ARG A 1 271 ? 142.459 147.675 176.707 1.00 21.14  ? 272  ARG A CA    1 
ATOM   2049 C  C     . ARG A 1 271 ? 141.618 146.558 177.326 1.00 21.14  ? 272  ARG A C     1 
ATOM   2050 O  O     . ARG A 1 271 ? 140.452 146.791 177.662 1.00 21.14  ? 272  ARG A O     1 
ATOM   2051 C  CB    . ARG A 1 271 ? 142.198 147.816 175.201 1.00 21.14  ? 272  ARG A CB    1 
ATOM   2052 C  CG    . ARG A 1 271 ? 140.752 148.035 174.782 1.00 21.14  ? 272  ARG A CG    1 
ATOM   2053 C  CD    . ARG A 1 271 ? 140.638 148.420 173.339 1.00 21.14  ? 272  ARG A CD    1 
ATOM   2054 N  NE    . ARG A 1 271 ? 141.211 149.722 173.056 1.00 21.14  ? 272  ARG A NE    1 
ATOM   2055 C  CZ    . ARG A 1 271 ? 140.587 150.873 173.269 1.00 21.14  ? 272  ARG A CZ    1 
ATOM   2056 N  NH1   . ARG A 1 271 ? 141.239 152.018 173.161 1.00 21.14  ? 272  ARG A NH1   1 
ATOM   2057 N  NH2   . ARG A 1 271 ? 139.331 150.878 173.685 1.00 21.14  ? 272  ARG A NH2   1 
ATOM   2058 N  N     . VAL A 1 272 ? 142.202 145.376 177.548 1.00 21.17  ? 273  VAL A N     1 
ATOM   2059 C  CA    . VAL A 1 272 ? 141.539 144.254 178.215 1.00 21.17  ? 273  VAL A CA    1 
ATOM   2060 C  C     . VAL A 1 272 ? 141.043 144.579 179.627 1.00 21.17  ? 273  VAL A C     1 
ATOM   2061 O  O     . VAL A 1 272 ? 140.065 143.985 180.090 1.00 21.17  ? 273  VAL A O     1 
ATOM   2062 C  CB    . VAL A 1 272 ? 142.544 143.079 178.212 1.00 21.17  ? 273  VAL A CB    1 
ATOM   2063 C  CG1   . VAL A 1 272 ? 142.008 141.819 178.870 1.00 21.17  ? 273  VAL A CG1   1 
ATOM   2064 C  CG2   . VAL A 1 272 ? 142.991 142.798 176.808 1.00 21.17  ? 273  VAL A CG2   1 
ATOM   2065 N  N     . ILE A 1 273 ? 141.599 145.604 180.277 1.00 22.58  ? 274  ILE A N     1 
ATOM   2066 C  CA    . ILE A 1 273 ? 141.271 145.899 181.669 1.00 22.58  ? 274  ILE A CA    1 
ATOM   2067 C  C     . ILE A 1 273 ? 140.947 147.373 181.852 1.00 22.58  ? 274  ILE A C     1 
ATOM   2068 O  O     . ILE A 1 273 ? 140.464 147.778 182.913 1.00 22.58  ? 274  ILE A O     1 
ATOM   2069 C  CB    . ILE A 1 273 ? 142.413 145.529 182.637 1.00 22.58  ? 274  ILE A CB    1 
ATOM   2070 C  CG1   . ILE A 1 273 ? 143.566 146.518 182.506 1.00 22.58  ? 274  ILE A CG1   1 
ATOM   2071 C  CG2   . ILE A 1 273 ? 142.910 144.106 182.449 1.00 22.58  ? 274  ILE A CG2   1 
ATOM   2072 C  CD1   . ILE A 1 273 ? 144.618 146.339 183.554 1.00 22.58  ? 274  ILE A CD1   1 
ATOM   2073 N  N     . PHE A 1 274 ? 141.200 148.190 180.836 1.00 26.39  ? 275  PHE A N     1 
ATOM   2074 C  CA    . PHE A 1 274 ? 141.002 149.624 180.985 1.00 26.39  ? 275  PHE A CA    1 
ATOM   2075 C  C     . PHE A 1 274 ? 140.404 150.167 179.700 1.00 26.39  ? 275  PHE A C     1 
ATOM   2076 O  O     . PHE A 1 274 ? 140.942 149.944 178.613 1.00 26.39  ? 275  PHE A O     1 
ATOM   2077 C  CB    . PHE A 1 274 ? 142.338 150.308 181.320 1.00 26.39  ? 275  PHE A CB    1 
ATOM   2078 C  CG    . PHE A 1 274 ? 142.236 151.782 181.619 1.00 26.39  ? 275  PHE A CG    1 
ATOM   2079 C  CD1   . PHE A 1 274 ? 142.311 152.733 180.612 1.00 26.39  ? 275  PHE A CD1   1 
ATOM   2080 C  CD2   . PHE A 1 274 ? 142.092 152.214 182.927 1.00 26.39  ? 275  PHE A CD2   1 
ATOM   2081 C  CE1   . PHE A 1 274 ? 142.226 154.081 180.902 1.00 26.39  ? 275  PHE A CE1   1 
ATOM   2082 C  CE2   . PHE A 1 274 ? 142.008 153.561 183.223 1.00 26.39  ? 275  PHE A CE2   1 
ATOM   2083 C  CZ    . PHE A 1 274 ? 142.075 154.494 182.208 1.00 26.39  ? 275  PHE A CZ    1 
ATOM   2084 N  N     . GLN A 1 275 ? 139.298 150.890 179.837 1.00 29.14  ? 276  GLN A N     1 
ATOM   2085 C  CA    . GLN A 1 275 ? 138.605 151.503 178.719 1.00 29.14  ? 276  GLN A CA    1 
ATOM   2086 C  C     . GLN A 1 275 ? 138.211 152.911 179.117 1.00 29.14  ? 276  GLN A C     1 
ATOM   2087 O  O     . GLN A 1 275 ? 137.775 153.146 180.246 1.00 29.14  ? 276  GLN A O     1 
ATOM   2088 C  CB    . GLN A 1 275 ? 137.346 150.726 178.316 1.00 29.14  ? 276  GLN A CB    1 
ATOM   2089 C  CG    . GLN A 1 275 ? 137.570 149.300 177.865 1.00 29.14  ? 276  GLN A CG    1 
ATOM   2090 C  CD    . GLN A 1 275 ? 137.519 148.317 179.007 1.00 29.14  ? 276  GLN A CD    1 
ATOM   2091 O  OE1   . GLN A 1 275 ? 137.687 148.685 180.163 1.00 29.14  ? 276  GLN A OE1   1 
ATOM   2092 N  NE2   . GLN A 1 275 ? 137.277 147.059 178.693 1.00 29.14  ? 276  GLN A NE2   1 
ATOM   2093 N  N     . LEU A 1 276 ? 138.365 153.839 178.187 1.00 32.14  ? 277  LEU A N     1 
ATOM   2094 C  CA    . LEU A 1 276 ? 137.816 155.165 178.367 1.00 32.14  ? 277  LEU A CA    1 
ATOM   2095 C  C     . LEU A 1 276 ? 136.321 155.132 178.078 1.00 32.14  ? 277  LEU A C     1 
ATOM   2096 O  O     . LEU A 1 276 ? 135.805 154.177 177.494 1.00 32.14  ? 277  LEU A O     1 
ATOM   2097 C  CB    . LEU A 1 276 ? 138.534 156.155 177.453 1.00 32.14  ? 277  LEU A CB    1 
ATOM   2098 C  CG    . LEU A 1 276 ? 140.053 156.179 177.653 1.00 32.14  ? 277  LEU A CG    1 
ATOM   2099 C  CD1   . LEU A 1 276 ? 140.733 157.044 176.611 1.00 32.14  ? 277  LEU A CD1   1 
ATOM   2100 C  CD2   . LEU A 1 276 ? 140.401 156.659 179.051 1.00 32.14  ? 277  LEU A CD2   1 
ATOM   2101 N  N     . LYS A 1 277 ? 135.616 156.157 178.555 1.00 33.56  ? 278  LYS A N     1 
ATOM   2102 C  CA    . LYS A 1 277 ? 134.267 156.435 178.077 1.00 33.56  ? 278  LYS A CA    1 
ATOM   2103 C  C     . LYS A 1 277 ? 134.260 156.600 176.558 1.00 33.56  ? 278  LYS A C     1 
ATOM   2104 O  O     . LYS A 1 277 ? 135.240 157.065 175.969 1.00 33.56  ? 278  LYS A O     1 
ATOM   2105 C  CB    . LYS A 1 277 ? 133.741 157.695 178.772 1.00 33.56  ? 278  LYS A CB    1 
ATOM   2106 C  CG    . LYS A 1 277 ? 132.348 158.157 178.385 1.00 33.56  ? 278  LYS A CG    1 
ATOM   2107 C  CD    . LYS A 1 277 ? 131.303 157.110 178.699 1.00 33.56  ? 278  LYS A CD    1 
ATOM   2108 C  CE    . LYS A 1 277 ? 129.907 157.671 178.499 1.00 33.56  ? 278  LYS A CE    1 
ATOM   2109 N  NZ    . LYS A 1 277 ? 129.646 157.970 177.065 1.00 33.56  ? 278  LYS A NZ    1 
ATOM   2110 N  N     . ALA A 1 278 ? 133.142 156.184 175.936 1.00 30.30  ? 279  ALA A N     1 
ATOM   2111 C  CA    . ALA A 1 278 ? 132.860 156.061 174.498 1.00 30.30  ? 279  ALA A CA    1 
ATOM   2112 C  C     . ALA A 1 278 ? 133.566 154.889 173.830 1.00 30.30  ? 279  ALA A C     1 
ATOM   2113 O  O     . ALA A 1 278 ? 133.602 154.835 172.599 1.00 30.30  ? 279  ALA A O     1 
ATOM   2114 C  CB    . ALA A 1 278 ? 133.129 157.341 173.689 1.00 30.30  ? 279  ALA A CB    1 
ATOM   2115 N  N     . GLU A 1 279 ? 134.123 153.942 174.583 1.00 27.89  ? 280  GLU A N     1 
ATOM   2116 C  CA    . GLU A 1 279 ? 134.897 152.863 173.986 1.00 27.89  ? 280  GLU A CA    1 
ATOM   2117 C  C     . GLU A 1 279 ? 134.444 151.518 174.535 1.00 27.89  ? 280  GLU A C     1 
ATOM   2118 O  O     . GLU A 1 279 ? 133.840 151.426 175.604 1.00 27.89  ? 280  GLU A O     1 
ATOM   2119 C  CB    . GLU A 1 279 ? 136.400 153.022 174.251 1.00 27.89  ? 280  GLU A CB    1 
ATOM   2120 C  CG    . GLU A 1 279 ? 136.957 154.400 173.964 1.00 27.89  ? 280  GLU A CG    1 
ATOM   2121 C  CD    . GLU A 1 279 ? 138.461 154.441 173.998 1.00 27.89  ? 280  GLU A CD    1 
ATOM   2122 O  OE1   . GLU A 1 279 ? 139.083 153.393 174.257 1.00 27.89  ? 280  GLU A OE1   1 
ATOM   2123 O  OE2   . GLU A 1 279 ? 139.023 155.529 173.768 1.00 27.89  ? 280  GLU A OE2   1 
ATOM   2124 N  N     . ARG A 1 280 ? 134.738 150.473 173.770 1.00 29.43  ? 281  ARG A N     1 
ATOM   2125 C  CA    . ARG A 1 280 ? 134.532 149.085 174.147 1.00 29.43  ? 281  ARG A CA    1 
ATOM   2126 C  C     . ARG A 1 280 ? 135.854 148.414 174.485 1.00 29.43  ? 281  ARG A C     1 
ATOM   2127 O  O     . ARG A 1 280 ? 136.934 148.929 174.197 1.00 29.43  ? 281  ARG A O     1 
ATOM   2128 C  CB    . ARG A 1 280 ? 133.878 148.301 173.009 1.00 29.43  ? 281  ARG A CB    1 
ATOM   2129 C  CG    . ARG A 1 280 ? 132.384 148.233 172.935 1.00 29.43  ? 281  ARG A CG    1 
ATOM   2130 C  CD    . ARG A 1 280 ? 132.051 147.294 171.800 1.00 29.43  ? 281  ARG A CD    1 
ATOM   2131 N  NE    . ARG A 1 280 ? 130.743 146.673 171.920 1.00 29.43  ? 281  ARG A NE    1 
ATOM   2132 C  CZ    . ARG A 1 280 ? 130.342 145.668 171.152 1.00 29.43  ? 281  ARG A CZ    1 
ATOM   2133 N  NH1   . ARG A 1 280 ? 129.155 145.116 171.340 1.00 29.43  ? 281  ARG A NH1   1 
ATOM   2134 N  NH2   . ARG A 1 280 ? 131.156 145.181 170.229 1.00 29.43  ? 281  ARG A NH2   1 
ATOM   2135 N  N     . ASP A 1 281 ? 135.747 147.246 175.121 1.00 27.31  ? 282  ASP A N     1 
ATOM   2136 C  CA    . ASP A 1 281 ? 136.763 146.203 175.053 1.00 27.31  ? 282  ASP A CA    1 
ATOM   2137 C  C     . ASP A 1 281 ? 136.791 145.571 173.657 1.00 27.31  ? 282  ASP A C     1 
ATOM   2138 O  O     . ASP A 1 281 ? 136.017 145.923 172.768 1.00 27.31  ? 282  ASP A O     1 
ATOM   2139 C  CB    . ASP A 1 281 ? 136.506 145.158 176.134 1.00 27.31  ? 282  ASP A CB    1 
ATOM   2140 C  CG    . ASP A 1 281 ? 137.769 144.478 176.602 1.00 27.31  ? 282  ASP A CG    1 
ATOM   2141 O  OD1   . ASP A 1 281 ? 138.677 144.289 175.774 1.00 27.31  ? 282  ASP A OD1   1 
ATOM   2142 O  OD2   . ASP A 1 281 ? 137.871 144.169 177.805 1.00 27.31  ? 282  ASP A OD2   1 
ATOM   2143 N  N     . TYR A 1 282 ? 137.671 144.586 173.485 1.00 24.10  ? 283  TYR A N     1 
ATOM   2144 C  CA    . TYR A 1 282 ? 137.712 143.776 172.274 1.00 24.10  ? 283  TYR A CA    1 
ATOM   2145 C  C     . TYR A 1 282 ? 136.388 143.054 172.044 1.00 24.10  ? 283  TYR A C     1 
ATOM   2146 O  O     . TYR A 1 282 ? 135.669 142.728 172.988 1.00 24.10  ? 283  TYR A O     1 
ATOM   2147 C  CB    . TYR A 1 282 ? 138.864 142.782 172.349 1.00 24.10  ? 283  TYR A CB    1 
ATOM   2148 C  CG    . TYR A 1 282 ? 140.223 143.452 172.354 1.00 24.10  ? 283  TYR A CG    1 
ATOM   2149 C  CD1   . TYR A 1 282 ? 140.758 143.992 171.198 1.00 24.10  ? 283  TYR A CD1   1 
ATOM   2150 C  CD2   . TYR A 1 282 ? 140.974 143.527 173.510 1.00 24.10  ? 283  TYR A CD2   1 
ATOM   2151 C  CE1   . TYR A 1 282 ? 141.999 144.573 171.194 1.00 24.10  ? 283  TYR A CE1   1 
ATOM   2152 C  CE2   . TYR A 1 282 ? 142.207 144.122 173.513 1.00 24.10  ? 283  TYR A CE2   1 
ATOM   2153 C  CZ    . TYR A 1 282 ? 142.711 144.638 172.354 1.00 24.10  ? 283  TYR A CZ    1 
ATOM   2154 O  OH    . TYR A 1 282 ? 143.936 145.246 172.360 1.00 24.10  ? 283  TYR A OH    1 
ATOM   2155 N  N     . HIS A 1 283 ? 136.050 142.867 170.761 1.00 25.70  ? 284  HIS A N     1 
ATOM   2156 C  CA    . HIS A 1 283 ? 134.732 142.375 170.358 1.00 25.70  ? 284  HIS A CA    1 
ATOM   2157 C  C     . HIS A 1 283 ? 134.384 140.996 170.905 1.00 25.70  ? 284  HIS A C     1 
ATOM   2158 O  O     . HIS A 1 283 ? 133.195 140.709 171.083 1.00 25.70  ? 284  HIS A O     1 
ATOM   2159 C  CB    . HIS A 1 283 ? 134.603 142.367 168.837 1.00 25.70  ? 284  HIS A CB    1 
ATOM   2160 C  CG    . HIS A 1 283 ? 134.698 143.723 168.215 1.00 25.70  ? 284  HIS A CG    1 
ATOM   2161 N  ND1   . HIS A 1 283 ? 134.019 144.814 168.711 1.00 25.70  ? 284  HIS A ND1   1 
ATOM   2162 C  CD2   . HIS A 1 283 ? 135.356 144.158 167.116 1.00 25.70  ? 284  HIS A CD2   1 
ATOM   2163 C  CE1   . HIS A 1 283 ? 134.275 145.868 167.960 1.00 25.70  ? 284  HIS A CE1   1 
ATOM   2164 N  NE2   . HIS A 1 283 ? 135.084 145.497 166.985 1.00 25.70  ? 284  HIS A NE2   1 
ATOM   2165 N  N     . ILE A 1 284 ? 135.375 140.110 171.078 1.00 25.19  ? 285  ILE A N     1 
ATOM   2166 C  CA    . ILE A 1 284 ? 135.122 138.738 171.536 1.00 25.19  ? 285  ILE A CA    1 
ATOM   2167 C  C     . ILE A 1 284 ? 134.384 138.719 172.876 1.00 25.19  ? 285  ILE A C     1 
ATOM   2168 O  O     . ILE A 1 284 ? 133.521 137.865 173.106 1.00 25.19  ? 285  ILE A O     1 
ATOM   2169 C  CB    . ILE A 1 284 ? 136.427 137.912 171.557 1.00 25.19  ? 285  ILE A CB    1 
ATOM   2170 C  CG1   . ILE A 1 284 ? 136.134 136.452 171.885 1.00 25.19  ? 285  ILE A CG1   1 
ATOM   2171 C  CG2   . ILE A 1 284 ? 137.477 138.479 172.496 1.00 25.19  ? 285  ILE A CG2   1 
ATOM   2172 C  CD1   . ILE A 1 284 ? 135.252 135.785 170.878 1.00 25.19  ? 285  ILE A CD1   1 
ATOM   2173 N  N     . PHE A 1 285 ? 134.709 139.655 173.776 1.00 27.89  ? 286  PHE A N     1 
ATOM   2174 C  CA    . PHE A 1 285 ? 134.050 139.726 175.078 1.00 27.89  ? 286  PHE A CA    1 
ATOM   2175 C  C     . PHE A 1 285 ? 132.560 140.032 174.953 1.00 27.89  ? 286  PHE A C     1 
ATOM   2176 O  O     . PHE A 1 285 ? 131.737 139.417 175.637 1.00 27.89  ? 286  PHE A O     1 
ATOM   2177 C  CB    . PHE A 1 285 ? 134.730 140.782 175.950 1.00 27.89  ? 286  PHE A CB    1 
ATOM   2178 C  CG    . PHE A 1 285 ? 136.151 140.457 176.299 1.00 27.89  ? 286  PHE A CG    1 
ATOM   2179 C  CD1   . PHE A 1 285 ? 136.440 139.504 177.251 1.00 27.89  ? 286  PHE A CD1   1 
ATOM   2180 C  CD2   . PHE A 1 285 ? 137.196 141.103 175.674 1.00 27.89  ? 286  PHE A CD2   1 
ATOM   2181 C  CE1   . PHE A 1 285 ? 137.737 139.206 177.576 1.00 27.89  ? 286  PHE A CE1   1 
ATOM   2182 C  CE2   . PHE A 1 285 ? 138.494 140.801 175.992 1.00 27.89  ? 286  PHE A CE2   1 
ATOM   2183 C  CZ    . PHE A 1 285 ? 138.762 139.852 176.946 1.00 27.89  ? 286  PHE A CZ    1 
ATOM   2184 N  N     . TYR A 1 286 ? 132.193 140.969 174.085 1.00 32.74  ? 287  TYR A N     1 
ATOM   2185 C  CA    . TYR A 1 286 ? 130.791 141.348 173.960 1.00 32.74  ? 287  TYR A CA    1 
ATOM   2186 C  C     . TYR A 1 286 ? 129.969 140.426 173.078 1.00 32.74  ? 287  TYR A C     1 
ATOM   2187 O  O     . TYR A 1 286 ? 128.758 140.314 173.285 1.00 32.74  ? 287  TYR A O     1 
ATOM   2188 C  CB    . TYR A 1 286 ? 130.683 142.764 173.423 1.00 32.74  ? 287  TYR A CB    1 
ATOM   2189 C  CG    . TYR A 1 286 ? 131.382 143.761 174.285 1.00 32.74  ? 287  TYR A CG    1 
ATOM   2190 C  CD1   . TYR A 1 286 ? 130.807 144.187 175.468 1.00 32.74  ? 287  TYR A CD1   1 
ATOM   2191 C  CD2   . TYR A 1 286 ? 132.621 144.260 173.937 1.00 32.74  ? 287  TYR A CD2   1 
ATOM   2192 C  CE1   . TYR A 1 286 ? 131.434 145.101 176.267 1.00 32.74  ? 287  TYR A CE1   1 
ATOM   2193 C  CE2   . TYR A 1 286 ? 133.256 145.171 174.735 1.00 32.74  ? 287  TYR A CE2   1 
ATOM   2194 C  CZ    . TYR A 1 286 ? 132.662 145.584 175.906 1.00 32.74  ? 287  TYR A CZ    1 
ATOM   2195 O  OH    . TYR A 1 286 ? 133.280 146.504 176.717 1.00 32.74  ? 287  TYR A OH    1 
ATOM   2196 N  N     . GLN A 1 287 ? 130.573 139.774 172.092 1.00 36.00  ? 288  GLN A N     1 
ATOM   2197 C  CA    . GLN A 1 287 ? 129.795 138.857 171.271 1.00 36.00  ? 288  GLN A CA    1 
ATOM   2198 C  C     . GLN A 1 287 ? 129.599 137.488 171.907 1.00 36.00  ? 288  GLN A C     1 
ATOM   2199 O  O     . GLN A 1 287 ? 128.698 136.758 171.485 1.00 36.00  ? 288  GLN A O     1 
ATOM   2200 C  CB    . GLN A 1 287 ? 130.403 138.759 169.868 1.00 36.00  ? 288  GLN A CB    1 
ATOM   2201 C  CG    . GLN A 1 287 ? 131.671 137.978 169.713 1.00 36.00  ? 288  GLN A CG    1 
ATOM   2202 C  CD    . GLN A 1 287 ? 132.393 138.361 168.435 1.00 36.00  ? 288  GLN A CD    1 
ATOM   2203 O  OE1   . GLN A 1 287 ? 132.224 139.467 167.926 1.00 36.00  ? 288  GLN A OE1   1 
ATOM   2204 N  NE2   . GLN A 1 287 ? 133.192 137.447 167.906 1.00 36.00  ? 288  GLN A NE2   1 
ATOM   2205 N  N     . ILE A 1 288 ? 130.432 137.105 172.875 1.00 35.13  ? 289  ILE A N     1 
ATOM   2206 C  CA    . ILE A 1 288 ? 130.103 135.965 173.730 1.00 35.13  ? 289  ILE A CA    1 
ATOM   2207 C  C     . ILE A 1 288 ? 128.805 136.216 174.494 1.00 35.13  ? 289  ILE A C     1 
ATOM   2208 O  O     . ILE A 1 288 ? 127.930 135.344 174.566 1.00 35.13  ? 289  ILE A O     1 
ATOM   2209 C  CB    . ILE A 1 288 ? 131.280 135.646 174.675 1.00 35.13  ? 289  ILE A CB    1 
ATOM   2210 C  CG1   . ILE A 1 288 ? 132.384 134.911 173.925 1.00 35.13  ? 289  ILE A CG1   1 
ATOM   2211 C  CG2   . ILE A 1 288 ? 130.852 134.799 175.849 1.00 35.13  ? 289  ILE A CG2   1 
ATOM   2212 C  CD1   . ILE A 1 288 ? 133.637 134.748 174.727 1.00 35.13  ? 289  ILE A CD1   1 
ATOM   2213 N  N     . LEU A 1 289 ? 128.639 137.423 175.030 1.00 39.35  ? 290  LEU A N     1 
ATOM   2214 C  CA    . LEU A 1 289 ? 127.441 137.745 175.798 1.00 39.35  ? 290  LEU A CA    1 
ATOM   2215 C  C     . LEU A 1 289 ? 126.206 137.895 174.918 1.00 39.35  ? 290  LEU A C     1 
ATOM   2216 O  O     . LEU A 1 289 ? 125.170 137.276 175.185 1.00 39.35  ? 290  LEU A O     1 
ATOM   2217 C  CB    . LEU A 1 289 ? 127.682 139.030 176.582 1.00 39.35  ? 290  LEU A CB    1 
ATOM   2218 C  CG    . LEU A 1 289 ? 128.784 138.908 177.622 1.00 39.35  ? 290  LEU A CG    1 
ATOM   2219 C  CD1   . LEU A 1 289 ? 129.063 140.228 178.263 1.00 39.35  ? 290  LEU A CD1   1 
ATOM   2220 C  CD2   . LEU A 1 289 ? 128.325 137.948 178.654 1.00 39.35  ? 290  LEU A CD2   1 
ATOM   2221 N  N     . SER A 1 290 ? 126.296 138.721 173.872 1.00 44.57  ? 291  SER A N     1 
ATOM   2222 C  CA    . SER A 1 290 ? 125.099 139.294 173.256 1.00 44.57  ? 291  SER A CA    1 
ATOM   2223 C  C     . SER A 1 290 ? 124.283 138.273 172.474 1.00 44.57  ? 291  SER A C     1 
ATOM   2224 O  O     . SER A 1 290 ? 123.072 138.456 172.310 1.00 44.57  ? 291  SER A O     1 
ATOM   2225 C  CB    . SER A 1 290 ? 125.481 140.465 172.351 1.00 44.57  ? 291  SER A CB    1 
ATOM   2226 O  OG    . SER A 1 290 ? 126.147 141.482 173.081 1.00 44.57  ? 291  SER A OG    1 
ATOM   2227 N  N     . ASN A 1 291 ? 124.910 137.200 171.981 1.00 49.42  ? 292  ASN A N     1 
ATOM   2228 C  CA    . ASN A 1 291 ? 124.151 136.147 171.309 1.00 49.42  ? 292  ASN A CA    1 
ATOM   2229 C  C     . ASN A 1 291 ? 123.312 135.312 172.280 1.00 49.42  ? 292  ASN A C     1 
ATOM   2230 O  O     . ASN A 1 291 ? 122.452 134.544 171.830 1.00 49.42  ? 292  ASN A O     1 
ATOM   2231 C  CB    . ASN A 1 291 ? 125.126 135.266 170.510 1.00 49.42  ? 292  ASN A CB    1 
ATOM   2232 C  CG    . ASN A 1 291 ? 124.429 134.246 169.620 1.00 49.42  ? 292  ASN A CG    1 
ATOM   2233 O  OD1   . ASN A 1 291 ? 124.314 133.075 169.973 1.00 49.42  ? 292  ASN A OD1   1 
ATOM   2234 N  ND2   . ASN A 1 291 ? 123.960 134.693 168.461 1.00 49.42  ? 292  ASN A ND2   1 
ATOM   2235 N  N     . LYS A 1 292 ? 123.525 135.463 173.596 1.00 54.03  ? 293  LYS A N     1 
ATOM   2236 C  CA    . LYS A 1 292 ? 122.900 134.672 174.666 1.00 54.03  ? 293  LYS A CA    1 
ATOM   2237 C  C     . LYS A 1 292 ? 123.177 133.171 174.560 1.00 54.03  ? 293  LYS A C     1 
ATOM   2238 O  O     . LYS A 1 292 ? 122.447 132.375 175.159 1.00 54.03  ? 293  LYS A O     1 
ATOM   2239 C  CB    . LYS A 1 292 ? 121.388 134.936 174.795 1.00 54.03  ? 293  LYS A CB    1 
ATOM   2240 C  CG    . LYS A 1 292 ? 120.966 136.390 174.574 1.00 54.03  ? 293  LYS A CG    1 
ATOM   2241 C  CD    . LYS A 1 292 ? 119.473 136.514 174.318 1.00 54.03  ? 293  LYS A CD    1 
ATOM   2242 C  CE    . LYS A 1 292 ? 119.093 137.950 173.992 1.00 54.03  ? 293  LYS A CE    1 
ATOM   2243 N  NZ    . LYS A 1 292 ? 119.879 138.928 174.792 1.00 54.03  ? 293  LYS A NZ    1 
ATOM   2244 N  N     . LYS A 1 293 ? 124.202 132.769 173.784 1.00 52.98  ? 294  LYS A N     1 
ATOM   2245 C  CA    . LYS A 1 293 ? 124.451 131.411 173.307 1.00 52.98  ? 294  LYS A CA    1 
ATOM   2246 C  C     . LYS A 1 293 ? 124.658 130.448 174.470 1.00 52.98  ? 294  LYS A C     1 
ATOM   2247 O  O     . LYS A 1 293 ? 125.674 130.532 175.171 1.00 52.98  ? 294  LYS A O     1 
ATOM   2248 C  CB    . LYS A 1 293 ? 125.682 131.385 172.402 1.00 52.98  ? 294  LYS A CB    1 
ATOM   2249 C  CG    . LYS A 1 293 ? 125.823 130.137 171.549 1.00 52.98  ? 294  LYS A CG    1 
ATOM   2250 C  CD    . LYS A 1 293 ? 126.890 130.344 170.492 1.00 52.98  ? 294  LYS A CD    1 
ATOM   2251 C  CE    . LYS A 1 293 ? 127.135 129.100 169.667 1.00 52.98  ? 294  LYS A CE    1 
ATOM   2252 N  NZ    . LYS A 1 293 ? 127.966 129.403 168.472 1.00 52.98  ? 294  LYS A NZ    1 
ATOM   2253 N  N     . PRO A 1 294 ? 123.712 129.536 174.710 1.00 56.52  ? 295  PRO A N     1 
ATOM   2254 C  CA    . PRO A 1 294 ? 123.826 128.642 175.874 1.00 56.52  ? 295  PRO A CA    1 
ATOM   2255 C  C     . PRO A 1 294 ? 124.968 127.641 175.785 1.00 56.52  ? 295  PRO A C     1 
ATOM   2256 O  O     . PRO A 1 294 ? 125.480 127.220 176.829 1.00 56.52  ? 295  PRO A O     1 
ATOM   2257 C  CB    . PRO A 1 294 ? 122.460 127.945 175.913 1.00 56.52  ? 295  PRO A CB    1 
ATOM   2258 C  CG    . PRO A 1 294 ? 121.970 128.006 174.512 1.00 56.52  ? 295  PRO A CG    1 
ATOM   2259 C  CD    . PRO A 1 294 ? 122.482 129.290 173.939 1.00 56.52  ? 295  PRO A CD    1 
ATOM   2260 N  N     . GLU A 1 295 ? 125.368 127.232 174.576 1.00 56.97  ? 296  GLU A N     1 
ATOM   2261 C  CA    . GLU A 1 295 ? 126.533 126.366 174.402 1.00 56.97  ? 296  GLU A CA    1 
ATOM   2262 C  C     . GLU A 1 295 ? 127.841 126.981 174.895 1.00 56.97  ? 296  GLU A C     1 
ATOM   2263 O  O     . GLU A 1 295 ? 128.799 126.240 175.136 1.00 56.97  ? 296  GLU A O     1 
ATOM   2264 C  CB    . GLU A 1 295 ? 126.675 125.974 172.929 1.00 56.97  ? 296  GLU A CB    1 
ATOM   2265 C  CG    . GLU A 1 295 ? 125.471 125.238 172.346 1.00 56.97  ? 296  GLU A CG    1 
ATOM   2266 C  CD    . GLU A 1 295 ? 125.187 123.900 173.017 1.00 56.97  ? 296  GLU A CD    1 
ATOM   2267 O  OE1   . GLU A 1 295 ? 126.131 123.255 173.521 1.00 56.97  ? 296  GLU A OE1   1 
ATOM   2268 O  OE2   . GLU A 1 295 ? 124.008 123.491 173.042 1.00 56.97  ? 296  GLU A OE2   1 
ATOM   2269 N  N     . LEU A 1 296 ? 127.916 128.302 175.045 1.00 51.34  ? 297  LEU A N     1 
ATOM   2270 C  CA    . LEU A 1 296 ? 129.027 128.924 175.755 1.00 51.34  ? 297  LEU A CA    1 
ATOM   2271 C  C     . LEU A 1 296 ? 128.699 129.181 177.220 1.00 51.34  ? 297  LEU A C     1 
ATOM   2272 O  O     . LEU A 1 296 ? 129.424 128.734 178.114 1.00 51.34  ? 297  LEU A O     1 
ATOM   2273 C  CB    . LEU A 1 296 ? 129.426 130.242 175.086 1.00 51.34  ? 297  LEU A CB    1 
ATOM   2274 C  CG    . LEU A 1 296 ? 129.905 130.176 173.642 1.00 51.34  ? 297  LEU A CG    1 
ATOM   2275 C  CD1   . LEU A 1 296 ? 130.329 131.556 173.169 1.00 51.34  ? 297  LEU A CD1   1 
ATOM   2276 C  CD2   . LEU A 1 296 ? 131.036 129.177 173.516 1.00 51.34  ? 297  LEU A CD2   1 
ATOM   2277 N  N     . LEU A 1 297 ? 127.602 129.886 177.476 1.00 49.48  ? 298  LEU A N     1 
ATOM   2278 C  CA    . LEU A 1 297 ? 127.311 130.474 178.776 1.00 49.48  ? 298  LEU A CA    1 
ATOM   2279 C  C     . LEU A 1 297 ? 126.827 129.465 179.811 1.00 49.48  ? 298  LEU A C     1 
ATOM   2280 O  O     . LEU A 1 297 ? 126.528 129.862 180.941 1.00 49.48  ? 298  LEU A O     1 
ATOM   2281 C  CB    . LEU A 1 297 ? 126.288 131.595 178.598 1.00 49.48  ? 298  LEU A CB    1 
ATOM   2282 C  CG    . LEU A 1 297 ? 126.687 132.632 177.542 1.00 49.48  ? 298  LEU A CG    1 
ATOM   2283 C  CD1   . LEU A 1 297 ? 125.733 133.792 177.538 1.00 49.48  ? 298  LEU A CD1   1 
ATOM   2284 C  CD2   . LEU A 1 297 ? 128.092 133.156 177.794 1.00 49.48  ? 298  LEU A CD2   1 
ATOM   2285 N  N     . ASP A 1 298 ? 126.724 128.187 179.457 1.00 53.50  ? 299  ASP A N     1 
ATOM   2286 C  CA    . ASP A 1 298 ? 126.675 127.119 180.446 1.00 53.50  ? 299  ASP A CA    1 
ATOM   2287 C  C     . ASP A 1 298 ? 128.031 126.475 180.674 1.00 53.50  ? 299  ASP A C     1 
ATOM   2288 O  O     . ASP A 1 298 ? 128.281 125.949 181.764 1.00 53.50  ? 299  ASP A O     1 
ATOM   2289 C  CB    . ASP A 1 298 ? 125.673 126.043 180.019 1.00 53.50  ? 299  ASP A CB    1 
ATOM   2290 C  CG    . ASP A 1 298 ? 124.251 126.550 180.008 1.00 53.50  ? 299  ASP A CG    1 
ATOM   2291 O  OD1   . ASP A 1 298 ? 123.984 127.576 180.668 1.00 53.50  ? 299  ASP A OD1   1 
ATOM   2292 O  OD2   . ASP A 1 298 ? 123.403 125.928 179.338 1.00 53.50  ? 299  ASP A OD2   1 
ATOM   2293 N  N     . MET A 1 299 ? 128.915 126.516 179.676 1.00 50.87  ? 300  MET A N     1 
ATOM   2294 C  CA    . MET A 1 299 ? 130.255 125.965 179.834 1.00 50.87  ? 300  MET A CA    1 
ATOM   2295 C  C     . MET A 1 299 ? 131.120 126.937 180.614 1.00 50.87  ? 300  MET A C     1 
ATOM   2296 O  O     . MET A 1 299 ? 131.811 126.555 181.563 1.00 50.87  ? 300  MET A O     1 
ATOM   2297 C  CB    . MET A 1 299 ? 130.877 125.686 178.467 1.00 50.87  ? 300  MET A CB    1 
ATOM   2298 C  CG    . MET A 1 299 ? 132.329 125.254 178.525 1.00 50.87  ? 300  MET A CG    1 
ATOM   2299 S  SD    . MET A 1 299 ? 132.994 124.878 176.895 1.00 50.87  ? 300  MET A SD    1 
ATOM   2300 C  CE    . MET A 1 299 ? 133.095 126.525 176.201 1.00 50.87  ? 300  MET A CE    1 
ATOM   2301 N  N     . LEU A 1 300 ? 131.088 128.196 180.211 1.00 46.44  ? 301  LEU A N     1 
ATOM   2302 C  CA    . LEU A 1 300 ? 131.622 129.279 181.014 1.00 46.44  ? 301  LEU A CA    1 
ATOM   2303 C  C     . LEU A 1 300 ? 130.579 129.640 182.058 1.00 46.44  ? 301  LEU A C     1 
ATOM   2304 O  O     . LEU A 1 300 ? 129.387 129.720 181.751 1.00 46.44  ? 301  LEU A O     1 
ATOM   2305 C  CB    . LEU A 1 300 ? 131.939 130.491 180.142 1.00 46.44  ? 301  LEU A CB    1 
ATOM   2306 C  CG    . LEU A 1 300 ? 132.676 130.201 178.835 1.00 46.44  ? 301  LEU A CG    1 
ATOM   2307 C  CD1   . LEU A 1 300 ? 132.986 131.463 178.059 1.00 46.44  ? 301  LEU A CD1   1 
ATOM   2308 C  CD2   . LEU A 1 300 ? 133.936 129.448 179.119 1.00 46.44  ? 301  LEU A CD2   1 
ATOM   2309 N  N     . LEU A 1 301 ? 131.013 129.851 183.296 1.00 41.49  ? 302  LEU A N     1 
ATOM   2310 C  CA    . LEU A 1 301 ? 130.075 130.184 184.372 1.00 41.49  ? 302  LEU A CA    1 
ATOM   2311 C  C     . LEU A 1 301 ? 129.650 131.652 184.374 1.00 41.49  ? 302  LEU A C     1 
ATOM   2312 O  O     . LEU A 1 301 ? 129.591 132.293 185.423 1.00 41.49  ? 302  LEU A O     1 
ATOM   2313 C  CB    . LEU A 1 301 ? 130.704 129.790 185.704 1.00 41.49  ? 302  LEU A CB    1 
ATOM   2314 C  CG    . LEU A 1 301 ? 131.080 128.306 185.754 1.00 41.49  ? 302  LEU A CG    1 
ATOM   2315 C  CD1   . LEU A 1 301 ? 131.819 127.961 187.033 1.00 41.49  ? 302  LEU A CD1   1 
ATOM   2316 C  CD2   . LEU A 1 301 ? 129.852 127.428 185.586 1.00 41.49  ? 302  LEU A CD2   1 
ATOM   2317 N  N     . ILE A 1 302 ? 129.341 132.189 183.197 1.00 44.24  ? 303  ILE A N     1 
ATOM   2318 C  CA    . ILE A 1 302 ? 129.017 133.593 183.014 1.00 44.24  ? 303  ILE A CA    1 
ATOM   2319 C  C     . ILE A 1 302 ? 127.532 133.811 183.319 1.00 44.24  ? 303  ILE A C     1 
ATOM   2320 O  O     . ILE A 1 302 ? 126.727 132.877 183.299 1.00 44.24  ? 303  ILE A O     1 
ATOM   2321 C  CB    . ILE A 1 302 ? 129.407 133.953 181.557 1.00 44.24  ? 303  ILE A CB    1 
ATOM   2322 C  CG1   . ILE A 1 302 ? 130.924 133.958 181.427 1.00 44.24  ? 303  ILE A CG1   1 
ATOM   2323 C  CG2   . ILE A 1 302 ? 129.038 135.340 181.095 1.00 44.24  ? 303  ILE A CG2   1 
ATOM   2324 C  CD1   . ILE A 1 302 ? 131.402 134.127 180.010 1.00 44.24  ? 303  ILE A CD1   1 
ATOM   2325 N  N     . THR A 1 303 ? 127.157 135.059 183.609 1.00 49.63  ? 304  THR A N     1 
ATOM   2326 C  CA    . THR A 1 303 ? 125.781 135.516 183.512 1.00 49.63  ? 304  THR A CA    1 
ATOM   2327 C  C     . THR A 1 303 ? 125.693 136.589 182.432 1.00 49.63  ? 304  THR A C     1 
ATOM   2328 O  O     . THR A 1 303 ? 126.655 137.316 182.173 1.00 49.63  ? 304  THR A O     1 
ATOM   2329 C  CB    . THR A 1 303 ? 125.251 136.041 184.859 1.00 49.63  ? 304  THR A CB    1 
ATOM   2330 O  OG1   . THR A 1 303 ? 123.857 136.349 184.740 1.00 49.63  ? 304  THR A OG1   1 
ATOM   2331 C  CG2   . THR A 1 303 ? 126.010 137.271 185.336 1.00 49.63  ? 304  THR A CG2   1 
ATOM   2332 N  N     . ASN A 1 304 ? 124.543 136.656 181.768 1.00 51.91  ? 305  ASN A N     1 
ATOM   2333 C  CA    . ASN A 1 304 ? 124.381 137.329 180.475 1.00 51.91  ? 305  ASN A CA    1 
ATOM   2334 C  C     . ASN A 1 304 ? 124.427 138.852 180.553 1.00 51.91  ? 305  ASN A C     1 
ATOM   2335 O  O     . ASN A 1 304 ? 124.059 139.476 179.553 1.00 51.91  ? 305  ASN A O     1 
ATOM   2336 C  CB    . ASN A 1 304 ? 123.057 136.909 179.839 1.00 51.91  ? 305  ASN A CB    1 
ATOM   2337 C  CG    . ASN A 1 304 ? 122.916 135.410 179.731 1.00 51.91  ? 305  ASN A CG    1 
ATOM   2338 O  OD1   . ASN A 1 304 ? 123.850 134.671 180.022 1.00 51.91  ? 305  ASN A OD1   1 
ATOM   2339 N  ND2   . ASN A 1 304 ? 121.742 134.950 179.314 1.00 51.91  ? 305  ASN A ND2   1 
ATOM   2340 N  N     . ASN A 1 305 ? 124.845 139.479 181.650 1.00 50.90  ? 306  ASN A N     1 
ATOM   2341 C  CA    . ASN A 1 305 ? 124.841 140.927 181.781 1.00 50.90  ? 306  ASN A CA    1 
ATOM   2342 C  C     . ASN A 1 305 ? 126.288 141.391 181.822 1.00 50.90  ? 306  ASN A C     1 
ATOM   2343 O  O     . ASN A 1 305 ? 127.052 140.935 182.686 1.00 50.90  ? 306  ASN A O     1 
ATOM   2344 C  CB    . ASN A 1 305 ? 124.096 141.332 183.063 1.00 50.90  ? 306  ASN A CB    1 
ATOM   2345 C  CG    . ASN A 1 305 ? 124.063 142.852 183.324 1.00 50.90  ? 306  ASN A CG    1 
ATOM   2346 O  OD1   . ASN A 1 305 ? 124.482 143.676 182.512 1.00 50.90  ? 306  ASN A OD1   1 
ATOM   2347 N  ND2   . ASN A 1 305 ? 123.549 143.214 184.493 1.00 50.90  ? 306  ASN A ND2   1 
ATOM   2348 N  N     . PRO A 1 306 ? 126.710 142.269 180.909 1.00 48.15  ? 307  PRO A N     1 
ATOM   2349 C  CA    . PRO A 1 306 ? 128.102 142.739 180.929 1.00 48.15  ? 307  PRO A CA    1 
ATOM   2350 C  C     . PRO A 1 306 ? 128.423 143.629 182.109 1.00 48.15  ? 307  PRO A C     1 
ATOM   2351 O  O     . PRO A 1 306 ? 129.599 143.735 182.474 1.00 48.15  ? 307  PRO A O     1 
ATOM   2352 C  CB    . PRO A 1 306 ? 128.234 143.503 179.609 1.00 48.15  ? 307  PRO A CB    1 
ATOM   2353 C  CG    . PRO A 1 306 ? 126.853 143.891 179.257 1.00 48.15  ? 307  PRO A CG    1 
ATOM   2354 C  CD    . PRO A 1 306 ? 125.960 142.811 179.765 1.00 48.15  ? 307  PRO A CD    1 
ATOM   2355 N  N     . TYR A 1 307 ? 127.426 144.278 182.710 1.00 50.00  ? 308  TYR A N     1 
ATOM   2356 C  CA    . TYR A 1 307 ? 127.688 145.391 183.611 1.00 50.00  ? 308  TYR A CA    1 
ATOM   2357 C  C     . TYR A 1 307 ? 128.249 144.975 184.967 1.00 50.00  ? 308  TYR A C     1 
ATOM   2358 O  O     . TYR A 1 307 ? 128.698 145.850 185.714 1.00 50.00  ? 308  TYR A O     1 
ATOM   2359 C  CB    . TYR A 1 307 ? 126.433 146.238 183.798 1.00 50.00  ? 308  TYR A CB    1 
ATOM   2360 C  CG    . TYR A 1 307 ? 126.185 147.175 182.640 1.00 50.00  ? 308  TYR A CG    1 
ATOM   2361 C  CD1   . TYR A 1 307 ? 126.970 148.312 182.473 1.00 50.00  ? 308  TYR A CD1   1 
ATOM   2362 C  CD2   . TYR A 1 307 ? 125.167 146.939 181.726 1.00 50.00  ? 308  TYR A CD2   1 
ATOM   2363 C  CE1   . TYR A 1 307 ? 126.772 149.171 181.412 1.00 50.00  ? 308  TYR A CE1   1 
ATOM   2364 C  CE2   . TYR A 1 307 ? 124.947 147.807 180.668 1.00 50.00  ? 308  TYR A CE2   1 
ATOM   2365 C  CZ    . TYR A 1 307 ? 125.756 148.918 180.517 1.00 50.00  ? 308  TYR A CZ    1 
ATOM   2366 O  OH    . TYR A 1 307 ? 125.533 149.794 179.482 1.00 50.00  ? 308  TYR A OH    1 
ATOM   2367 N  N     . ASP A 1 308 ? 128.232 143.693 185.317 1.00 50.63  ? 309  ASP A N     1 
ATOM   2368 C  CA    . ASP A 1 308 ? 128.859 143.253 186.555 1.00 50.63  ? 309  ASP A CA    1 
ATOM   2369 C  C     . ASP A 1 308 ? 130.285 142.731 186.391 1.00 50.63  ? 309  ASP A C     1 
ATOM   2370 O  O     . ASP A 1 308 ? 130.902 142.343 187.387 1.00 50.63  ? 309  ASP A O     1 
ATOM   2371 C  CB    . ASP A 1 308 ? 127.969 142.200 187.239 1.00 50.63  ? 309  ASP A CB    1 
ATOM   2372 C  CG    . ASP A 1 308 ? 127.717 140.950 186.382 1.00 50.63  ? 309  ASP A CG    1 
ATOM   2373 O  OD1   . ASP A 1 308 ? 128.342 140.741 185.320 1.00 50.63  ? 309  ASP A OD1   1 
ATOM   2374 O  OD2   . ASP A 1 308 ? 126.854 140.150 186.795 1.00 50.63  ? 309  ASP A OD2   1 
ATOM   2375 N  N     . TYR A 1 309 ? 130.819 142.707 185.172 1.00 42.83  ? 310  TYR A N     1 
ATOM   2376 C  CA    . TYR A 1 309 ? 132.223 142.386 184.930 1.00 42.83  ? 310  TYR A CA    1 
ATOM   2377 C  C     . TYR A 1 309 ? 133.049 143.665 184.899 1.00 42.83  ? 310  TYR A C     1 
ATOM   2378 O  O     . TYR A 1 309 ? 132.911 144.471 183.976 1.00 42.83  ? 310  TYR A O     1 
ATOM   2379 C  CB    . TYR A 1 309 ? 132.359 141.593 183.636 1.00 42.83  ? 310  TYR A CB    1 
ATOM   2380 C  CG    . TYR A 1 309 ? 131.648 140.271 183.725 1.00 42.83  ? 310  TYR A CG    1 
ATOM   2381 C  CD1   . TYR A 1 309 ? 132.063 139.311 184.631 1.00 42.83  ? 310  TYR A CD1   1 
ATOM   2382 C  CD2   . TYR A 1 309 ? 130.527 140.008 182.956 1.00 42.83  ? 310  TYR A CD2   1 
ATOM   2383 C  CE1   . TYR A 1 309 ? 131.432 138.097 184.718 1.00 42.83  ? 310  TYR A CE1   1 
ATOM   2384 C  CE2   . TYR A 1 309 ? 129.870 138.803 183.057 1.00 42.83  ? 310  TYR A CE2   1 
ATOM   2385 C  CZ    . TYR A 1 309 ? 130.334 137.851 183.936 1.00 42.83  ? 310  TYR A CZ    1 
ATOM   2386 O  OH    . TYR A 1 309 ? 129.676 136.658 184.069 1.00 42.83  ? 310  TYR A OH    1 
ATOM   2387 N  N     . ALA A 1 310 ? 133.904 143.847 185.911 1.00 39.01  ? 311  ALA A N     1 
ATOM   2388 C  CA    . ALA A 1 310 ? 134.592 145.120 186.124 1.00 39.01  ? 311  ALA A CA    1 
ATOM   2389 C  C     . ALA A 1 310 ? 135.579 145.446 185.010 1.00 39.01  ? 311  ALA A C     1 
ATOM   2390 O  O     . ALA A 1 310 ? 135.861 146.623 184.762 1.00 39.01  ? 311  ALA A O     1 
ATOM   2391 C  CB    . ALA A 1 310 ? 135.308 145.109 187.472 1.00 39.01  ? 311  ALA A CB    1 
ATOM   2392 N  N     . PHE A 1 311 ? 136.111 144.434 184.331 1.00 30.35  ? 312  PHE A N     1 
ATOM   2393 C  CA    . PHE A 1 311 ? 137.020 144.671 183.218 1.00 30.35  ? 312  PHE A CA    1 
ATOM   2394 C  C     . PHE A 1 311 ? 136.296 145.127 181.962 1.00 30.35  ? 312  PHE A C     1 
ATOM   2395 O  O     . PHE A 1 311 ? 136.917 145.728 181.081 1.00 30.35  ? 312  PHE A O     1 
ATOM   2396 C  CB    . PHE A 1 311 ? 137.834 143.411 182.919 1.00 30.35  ? 312  PHE A CB    1 
ATOM   2397 C  CG    . PHE A 1 311 ? 138.994 143.189 183.851 1.00 30.35  ? 312  PHE A CG    1 
ATOM   2398 C  CD1   . PHE A 1 311 ? 139.274 144.075 184.875 1.00 30.35  ? 312  PHE A CD1   1 
ATOM   2399 C  CD2   . PHE A 1 311 ? 139.830 142.107 183.670 1.00 30.35  ? 312  PHE A CD2   1 
ATOM   2400 C  CE1   . PHE A 1 311 ? 140.353 143.876 185.702 1.00 30.35  ? 312  PHE A CE1   1 
ATOM   2401 C  CE2   . PHE A 1 311 ? 140.901 141.901 184.499 1.00 30.35  ? 312  PHE A CE2   1 
ATOM   2402 C  CZ    . PHE A 1 311 ? 141.167 142.787 185.511 1.00 30.35  ? 312  PHE A CZ    1 
ATOM   2403 N  N     . ILE A 1 312 ? 135.004 144.849 181.868 1.00 34.92  ? 313  ILE A N     1 
ATOM   2404 C  CA    . ILE A 1 312 ? 134.247 145.012 180.637 1.00 34.92  ? 313  ILE A CA    1 
ATOM   2405 C  C     . ILE A 1 312 ? 133.140 146.057 180.752 1.00 34.92  ? 313  ILE A C     1 
ATOM   2406 O  O     . ILE A 1 312 ? 132.840 146.740 179.756 1.00 34.92  ? 313  ILE A O     1 
ATOM   2407 C  CB    . ILE A 1 312 ? 133.690 143.627 180.215 1.00 34.92  ? 313  ILE A CB    1 
ATOM   2408 C  CG1   . ILE A 1 312 ? 134.816 142.784 179.627 1.00 34.92  ? 313  ILE A CG1   1 
ATOM   2409 C  CG2   . ILE A 1 312 ? 132.494 143.646 179.295 1.00 34.92  ? 313  ILE A CG2   1 
ATOM   2410 C  CD1   . ILE A 1 312 ? 134.554 141.347 179.700 1.00 34.92  ? 313  ILE A CD1   1 
ATOM   2411 N  N     . SER A 1 313 ? 132.648 146.335 181.960 1.00 40.08  ? 314  SER A N     1 
ATOM   2412 C  CA    . SER A 1 313 ? 131.473 147.182 182.142 1.00 40.08  ? 314  SER A CA    1 
ATOM   2413 C  C     . SER A 1 313 ? 131.755 148.652 181.878 1.00 40.08  ? 314  SER A C     1 
ATOM   2414 O  O     . SER A 1 313 ? 130.886 149.359 181.358 1.00 40.08  ? 314  SER A O     1 
ATOM   2415 C  CB    . SER A 1 313 ? 130.943 147.028 183.562 1.00 40.08  ? 314  SER A CB    1 
ATOM   2416 O  OG    . SER A 1 313 ? 129.899 147.949 183.820 1.00 40.08  ? 314  SER A OG    1 
ATOM   2417 N  N     . GLN A 1 314 ? 132.930 149.140 182.266 1.00 32.76  ? 315  GLN A N     1 
ATOM   2418 C  CA    . GLN A 1 314 ? 133.255 150.551 182.094 1.00 32.76  ? 315  GLN A CA    1 
ATOM   2419 C  C     . GLN A 1 314 ? 133.360 150.928 180.618 1.00 32.76  ? 315  GLN A C     1 
ATOM   2420 O  O     . GLN A 1 314 ? 133.623 150.093 179.750 1.00 32.76  ? 315  GLN A O     1 
ATOM   2421 C  CB    . GLN A 1 314 ? 134.541 150.890 182.848 1.00 32.76  ? 315  GLN A CB    1 
ATOM   2422 C  CG    . GLN A 1 314 ? 135.796 150.319 182.246 1.00 32.76  ? 315  GLN A CG    1 
ATOM   2423 C  CD    . GLN A 1 314 ? 136.894 150.131 183.269 1.00 32.76  ? 315  GLN A CD    1 
ATOM   2424 O  OE1   . GLN A 1 314 ? 136.852 150.713 184.348 1.00 32.76  ? 315  GLN A OE1   1 
ATOM   2425 N  NE2   . GLN A 1 314 ? 137.875 149.301 182.943 1.00 32.76  ? 315  GLN A NE2   1 
ATOM   2426 N  N     . GLY A 1 315 ? 133.136 152.207 180.342 1.00 32.33  ? 316  GLY A N     1 
ATOM   2427 C  CA    . GLY A 1 315 ? 132.946 152.669 178.983 1.00 32.33  ? 316  GLY A CA    1 
ATOM   2428 C  C     . GLY A 1 315 ? 131.562 152.350 178.454 1.00 32.33  ? 316  GLY A C     1 
ATOM   2429 O  O     . GLY A 1 315 ? 130.570 152.535 179.163 1.00 32.33  ? 316  GLY A O     1 
ATOM   2430 N  N     . GLU A 1 316 ? 131.477 151.872 177.217 1.00 34.84  ? 317  GLU A N     1 
ATOM   2431 C  CA    . GLU A 1 316 ? 130.210 151.534 176.581 1.00 34.84  ? 317  GLU A CA    1 
ATOM   2432 C  C     . GLU A 1 316 ? 130.218 150.064 176.200 1.00 34.84  ? 317  GLU A C     1 
ATOM   2433 O  O     . GLU A 1 316 ? 131.165 149.594 175.565 1.00 34.84  ? 317  GLU A O     1 
ATOM   2434 C  CB    . GLU A 1 316 ? 129.950 152.395 175.344 1.00 34.84  ? 317  GLU A CB    1 
ATOM   2435 C  CG    . GLU A 1 316 ? 129.498 153.804 175.655 1.00 34.84  ? 317  GLU A CG    1 
ATOM   2436 C  CD    . GLU A 1 316 ? 129.567 154.714 174.449 1.00 34.84  ? 317  GLU A CD    1 
ATOM   2437 O  OE1   . GLU A 1 316 ? 129.777 154.200 173.331 1.00 34.84  ? 317  GLU A OE1   1 
ATOM   2438 O  OE2   . GLU A 1 316 ? 129.419 155.942 174.616 1.00 34.84  ? 317  GLU A OE2   1 
ATOM   2439 N  N     . THR A 1 317 ? 129.192 149.330 176.630 1.00 38.22  ? 318  THR A N     1 
ATOM   2440 C  CA    . THR A 1 317 ? 129.101 147.916 176.298 1.00 38.22  ? 318  THR A CA    1 
ATOM   2441 C  C     . THR A 1 317 ? 128.462 147.632 174.943 1.00 38.22  ? 318  THR A C     1 
ATOM   2442 O  O     . THR A 1 317 ? 128.626 146.522 174.431 1.00 38.22  ? 318  THR A O     1 
ATOM   2443 C  CB    . THR A 1 317 ? 128.336 147.158 177.380 1.00 38.22  ? 318  THR A CB    1 
ATOM   2444 O  OG1   . THR A 1 317 ? 128.414 145.757 177.104 1.00 38.22  ? 318  THR A OG1   1 
ATOM   2445 C  CG2   . THR A 1 317 ? 126.883 147.577 177.419 1.00 38.22  ? 318  THR A CG2   1 
ATOM   2446 N  N     . THR A 1 318 ? 127.732 148.576 174.352 1.00 39.04  ? 319  THR A N     1 
ATOM   2447 C  CA    . THR A 1 318 ? 126.972 148.253 173.152 1.00 39.04  ? 319  THR A CA    1 
ATOM   2448 C  C     . THR A 1 318 ? 126.863 149.477 172.255 1.00 39.04  ? 319  THR A C     1 
ATOM   2449 O  O     . THR A 1 318 ? 127.003 150.620 172.702 1.00 39.04  ? 319  THR A O     1 
ATOM   2450 C  CB    . THR A 1 318 ? 125.581 147.698 173.488 1.00 39.04  ? 319  THR A CB    1 
ATOM   2451 O  OG1   . THR A 1 318 ? 124.995 147.139 172.306 1.00 39.04  ? 319  THR A OG1   1 
ATOM   2452 C  CG2   . THR A 1 318 ? 124.667 148.782 174.043 1.00 39.04  ? 319  THR A CG2   1 
ATOM   2453 N  N     . VAL A 1 319 ? 126.647 149.215 170.963 1.00 41.20  ? 320  VAL A N     1 
ATOM   2454 C  CA    . VAL A 1 319 ? 126.659 150.225 169.908 1.00 41.20  ? 320  VAL A CA    1 
ATOM   2455 C  C     . VAL A 1 319 ? 125.600 149.864 168.876 1.00 41.20  ? 320  VAL A C     1 
ATOM   2456 O  O     . VAL A 1 319 ? 125.220 148.699 168.722 1.00 41.20  ? 320  VAL A O     1 
ATOM   2457 C  CB    . VAL A 1 319 ? 128.030 150.373 169.194 1.00 41.20  ? 320  VAL A CB    1 
ATOM   2458 C  CG1   . VAL A 1 319 ? 129.105 150.878 170.118 1.00 41.20  ? 320  VAL A CG1   1 
ATOM   2459 C  CG2   . VAL A 1 319 ? 128.463 149.051 168.602 1.00 41.20  ? 320  VAL A CG2   1 
ATOM   2460 N  N     . ALA A 1 320 ? 125.094 150.889 168.190 1.00 44.09  ? 321  ALA A N     1 
ATOM   2461 C  CA    . ALA A 1 320 ? 124.091 150.683 167.152 1.00 44.09  ? 321  ALA A CA    1 
ATOM   2462 C  C     . ALA A 1 320 ? 124.652 150.002 165.909 1.00 44.09  ? 321  ALA A C     1 
ATOM   2463 O  O     . ALA A 1 320 ? 123.889 149.383 165.162 1.00 44.09  ? 321  ALA A O     1 
ATOM   2464 C  CB    . ALA A 1 320 ? 123.457 152.019 166.769 1.00 44.09  ? 321  ALA A CB    1 
ATOM   2465 N  N     . SER A 1 321 ? 125.959 150.102 165.670 1.00 44.75  ? 322  SER A N     1 
ATOM   2466 C  CA    . SER A 1 321 ? 126.523 149.660 164.400 1.00 44.75  ? 322  SER A CA    1 
ATOM   2467 C  C     . SER A 1 321 ? 126.668 148.147 164.295 1.00 44.75  ? 322  SER A C     1 
ATOM   2468 O  O     . SER A 1 321 ? 126.563 147.603 163.192 1.00 44.75  ? 322  SER A O     1 
ATOM   2469 C  CB    . SER A 1 321 ? 127.886 150.317 164.176 1.00 44.75  ? 322  SER A CB    1 
ATOM   2470 O  OG    . SER A 1 321 ? 127.834 151.709 164.433 1.00 44.75  ? 322  SER A OG    1 
ATOM   2471 N  N     . ILE A 1 322 ? 126.902 147.448 165.403 1.00 44.60  ? 323  ILE A N     1 
ATOM   2472 C  CA    . ILE A 1 322 ? 127.391 146.074 165.370 1.00 44.60  ? 323  ILE A CA    1 
ATOM   2473 C  C     . ILE A 1 322 ? 126.321 145.145 165.922 1.00 44.60  ? 323  ILE A C     1 
ATOM   2474 O  O     . ILE A 1 322 ? 125.827 145.344 167.038 1.00 44.60  ? 323  ILE A O     1 
ATOM   2475 C  CB    . ILE A 1 322 ? 128.700 145.920 166.161 1.00 44.60  ? 323  ILE A CB    1 
ATOM   2476 C  CG1   . ILE A 1 322 ? 129.697 147.010 165.774 1.00 44.60  ? 323  ILE A CG1   1 
ATOM   2477 C  CG2   . ILE A 1 322 ? 129.308 144.559 165.901 1.00 44.60  ? 323  ILE A CG2   1 
ATOM   2478 C  CD1   . ILE A 1 322 ? 130.931 147.025 166.631 1.00 44.60  ? 323  ILE A CD1   1 
ATOM   2479 N  N     . ASP A 1 323 ? 125.972 144.126 165.135 1.00 49.54  ? 324  ASP A N     1 
ATOM   2480 C  CA    . ASP A 1 323 ? 125.058 143.062 165.549 1.00 49.54  ? 324  ASP A CA    1 
ATOM   2481 C  C     . ASP A 1 323 ? 125.876 141.851 165.989 1.00 49.54  ? 324  ASP A C     1 
ATOM   2482 O  O     . ASP A 1 323 ? 126.112 140.918 165.221 1.00 49.54  ? 324  ASP A O     1 
ATOM   2483 C  CB    . ASP A 1 323 ? 124.094 142.711 164.421 1.00 49.54  ? 324  ASP A CB    1 
ATOM   2484 C  CG    . ASP A 1 323 ? 122.967 141.807 164.881 1.00 49.54  ? 324  ASP A CG    1 
ATOM   2485 O  OD1   . ASP A 1 323 ? 122.485 141.992 166.018 1.00 49.54  ? 324  ASP A OD1   1 
ATOM   2486 O  OD2   . ASP A 1 323 ? 122.565 140.912 164.108 1.00 49.54  ? 324  ASP A OD2   1 
ATOM   2487 N  N     . ASP A 1 324 ? 126.374 141.929 167.234 1.00 44.34  ? 325  ASP A N     1 
ATOM   2488 C  CA    . ASP A 1 324 ? 127.231 140.905 167.842 1.00 44.34  ? 325  ASP A CA    1 
ATOM   2489 C  C     . ASP A 1 324 ? 126.663 139.490 167.762 1.00 44.34  ? 325  ASP A C     1 
ATOM   2490 O  O     . ASP A 1 324 ? 127.429 138.523 167.681 1.00 44.34  ? 325  ASP A O     1 
ATOM   2491 C  CB    . ASP A 1 324 ? 127.492 141.257 169.304 1.00 44.34  ? 325  ASP A CB    1 
ATOM   2492 C  CG    . ASP A 1 324 ? 128.196 142.577 169.466 1.00 44.34  ? 325  ASP A CG    1 
ATOM   2493 O  OD1   . ASP A 1 324 ? 129.370 142.679 169.056 1.00 44.34  ? 325  ASP A OD1   1 
ATOM   2494 O  OD2   . ASP A 1 324 ? 127.576 143.515 170.006 1.00 44.34  ? 325  ASP A OD2   1 
ATOM   2495 N  N     . ALA A 1 325 ? 125.333 139.351 167.816 1.00 46.44  ? 326  ALA A N     1 
ATOM   2496 C  CA    . ALA A 1 325 ? 124.691 138.038 167.798 1.00 46.44  ? 326  ALA A CA    1 
ATOM   2497 C  C     . ALA A 1 325 ? 124.963 137.276 166.508 1.00 46.44  ? 326  ALA A C     1 
ATOM   2498 O  O     . ALA A 1 325 ? 125.010 136.042 166.519 1.00 46.44  ? 326  ALA A O     1 
ATOM   2499 C  CB    . ALA A 1 325 ? 123.186 138.193 168.005 1.00 46.44  ? 326  ALA A CB    1 
ATOM   2500 N  N     . GLU A 1 326 ? 125.135 137.982 165.394 1.00 47.65  ? 327  GLU A N     1 
ATOM   2501 C  CA    . GLU A 1 326 ? 125.563 137.345 164.157 1.00 47.65  ? 327  GLU A CA    1 
ATOM   2502 C  C     . GLU A 1 326 ? 127.077 137.294 164.019 1.00 47.65  ? 327  GLU A C     1 
ATOM   2503 O  O     . GLU A 1 326 ? 127.602 136.361 163.400 1.00 47.65  ? 327  GLU A O     1 
ATOM   2504 C  CB    . GLU A 1 326 ? 124.963 138.070 162.948 1.00 47.65  ? 327  GLU A CB    1 
ATOM   2505 C  CG    . GLU A 1 326 ? 123.467 137.831 162.725 1.00 47.65  ? 327  GLU A CG    1 
ATOM   2506 C  CD    . GLU A 1 326 ? 123.104 136.381 162.399 1.00 47.65  ? 327  GLU A CD    1 
ATOM   2507 O  OE1   . GLU A 1 326 ? 123.967 135.617 161.915 1.00 47.65  ? 327  GLU A OE1   1 
ATOM   2508 O  OE2   . GLU A 1 326 ? 121.936 136.005 162.630 1.00 47.65  ? 327  GLU A OE2   1 
ATOM   2509 N  N     . GLU A 1 327 ? 127.781 138.296 164.556 1.00 43.91  ? 328  GLU A N     1 
ATOM   2510 C  CA    . GLU A 1 327 ? 129.239 138.319 164.487 1.00 43.91  ? 328  GLU A CA    1 
ATOM   2511 C  C     . GLU A 1 327 ? 129.880 137.182 165.269 1.00 43.91  ? 328  GLU A C     1 
ATOM   2512 O  O     . GLU A 1 327 ? 130.966 136.728 164.897 1.00 43.91  ? 328  GLU A O     1 
ATOM   2513 C  CB    . GLU A 1 327 ? 129.775 139.664 164.984 1.00 43.91  ? 328  GLU A CB    1 
ATOM   2514 C  CG    . GLU A 1 327 ? 129.396 140.875 164.130 1.00 43.91  ? 328  GLU A CG    1 
ATOM   2515 C  CD    . GLU A 1 327 ? 129.895 140.799 162.693 1.00 43.91  ? 328  GLU A CD    1 
ATOM   2516 O  OE1   . GLU A 1 327 ? 130.961 140.194 162.444 1.00 43.91  ? 328  GLU A OE1   1 
ATOM   2517 O  OE2   . GLU A 1 327 ? 129.213 141.351 161.804 1.00 43.91  ? 328  GLU A OE2   1 
ATOM   2518 N  N     . LEU A 1 328 ? 129.253 136.737 166.365 1.00 41.48  ? 329  LEU A N     1 
ATOM   2519 C  CA    . LEU A 1 328 ? 129.753 135.578 167.107 1.00 41.48  ? 329  LEU A CA    1 
ATOM   2520 C  C     . LEU A 1 328 ? 129.767 134.328 166.238 1.00 41.48  ? 329  LEU A C     1 
ATOM   2521 O  O     . LEU A 1 328 ? 130.769 133.604 166.193 1.00 41.48  ? 329  LEU A O     1 
ATOM   2522 C  CB    . LEU A 1 328 ? 128.931 135.341 168.371 1.00 41.48  ? 329  LEU A CB    1 
ATOM   2523 C  CG    . LEU A 1 328 ? 129.414 134.103 169.130 1.00 41.48  ? 329  LEU A CG    1 
ATOM   2524 C  CD1   . LEU A 1 328 ? 130.767 134.353 169.753 1.00 41.48  ? 329  LEU A CD1   1 
ATOM   2525 C  CD2   . LEU A 1 328 ? 128.433 133.685 170.186 1.00 41.48  ? 329  LEU A CD2   1 
ATOM   2526 N  N     . MET A 1 329 ? 128.635 134.036 165.587 1.00 45.50  ? 330  MET A N     1 
ATOM   2527 C  CA    . MET A 1 329 ? 128.524 132.883 164.697 1.00 45.50  ? 330  MET A CA    1 
ATOM   2528 C  C     . MET A 1 329 ? 129.546 132.958 163.567 1.00 45.50  ? 330  MET A C     1 
ATOM   2529 O  O     . MET A 1 329 ? 130.107 131.934 163.161 1.00 45.50  ? 330  MET A O     1 
ATOM   2530 C  CB    . MET A 1 329 ? 127.107 132.802 164.137 1.00 45.50  ? 330  MET A CB    1 
ATOM   2531 C  CG    . MET A 1 329 ? 126.046 132.630 165.206 1.00 45.50  ? 330  MET A CG    1 
ATOM   2532 S  SD    . MET A 1 329 ? 124.482 132.001 164.575 1.00 45.50  ? 330  MET A SD    1 
ATOM   2533 C  CE    . MET A 1 329 ? 123.406 132.315 165.974 1.00 45.50  ? 330  MET A CE    1 
ATOM   2534 N  N     . ALA A 1 330 ? 129.761 134.164 163.026 1.00 41.06  ? 331  ALA A N     1 
ATOM   2535 C  CA    . ALA A 1 330 ? 130.745 134.376 161.967 1.00 41.06  ? 331  ALA A CA    1 
ATOM   2536 C  C     . ALA A 1 330 ? 132.161 134.031 162.419 1.00 41.06  ? 331  ALA A C     1 
ATOM   2537 O  O     . ALA A 1 330 ? 132.931 133.431 161.660 1.00 41.06  ? 331  ALA A O     1 
ATOM   2538 C  CB    . ALA A 1 330 ? 130.684 135.823 161.485 1.00 41.06  ? 331  ALA A CB    1 
ATOM   2539 N  N     . THR A 1 331 ? 132.529 134.406 163.646 1.00 37.28  ? 332  THR A N     1 
ATOM   2540 C  CA    . THR A 1 331 ? 133.883 134.130 164.113 1.00 37.28  ? 332  THR A CA    1 
ATOM   2541 C  C     . THR A 1 331 ? 134.017 132.723 164.666 1.00 37.28  ? 332  THR A C     1 
ATOM   2542 O  O     . THR A 1 331 ? 135.104 132.143 164.599 1.00 37.28  ? 332  THR A O     1 
ATOM   2543 C  CB    . THR A 1 331 ? 134.310 135.127 165.187 1.00 37.28  ? 332  THR A CB    1 
ATOM   2544 O  OG1   . THR A 1 331 ? 133.441 135.017 166.316 1.00 37.28  ? 332  THR A OG1   1 
ATOM   2545 C  CG2   . THR A 1 331 ? 134.236 136.532 164.642 1.00 37.28  ? 332  THR A CG2   1 
ATOM   2546 N  N     . ASP A 1 332 ? 132.941 132.169 165.226 1.00 37.52  ? 333  ASP A N     1 
ATOM   2547 C  CA    . ASP A 1 332 ? 132.934 130.757 165.592 1.00 37.52  ? 333  ASP A CA    1 
ATOM   2548 C  C     . ASP A 1 332 ? 133.086 129.867 164.364 1.00 37.52  ? 333  ASP A C     1 
ATOM   2549 O  O     . ASP A 1 332 ? 133.772 128.839 164.412 1.00 37.52  ? 333  ASP A O     1 
ATOM   2550 C  CB    . ASP A 1 332 ? 131.647 130.432 166.348 1.00 37.52  ? 333  ASP A CB    1 
ATOM   2551 C  CG    . ASP A 1 332 ? 131.747 129.156 167.149 1.00 37.52  ? 333  ASP A CG    1 
ATOM   2552 O  OD1   . ASP A 1 332 ? 132.870 128.638 167.296 1.00 37.52  ? 333  ASP A OD1   1 
ATOM   2553 O  OD2   . ASP A 1 332 ? 130.704 128.682 167.646 1.00 37.52  ? 333  ASP A OD2   1 
ATOM   2554 N  N     . ASN A 1 333 ? 132.458 130.252 163.250 1.00 36.16  ? 334  ASN A N     1 
ATOM   2555 C  CA    . ASN A 1 333 ? 132.690 129.570 161.980 1.00 36.16  ? 334  ASN A CA    1 
ATOM   2556 C  C     . ASN A 1 333 ? 134.082 129.843 161.421 1.00 36.16  ? 334  ASN A C     1 
ATOM   2557 O  O     . ASN A 1 333 ? 134.658 128.969 160.766 1.00 36.16  ? 334  ASN A O     1 
ATOM   2558 C  CB    . ASN A 1 333 ? 131.626 129.980 160.962 1.00 36.16  ? 334  ASN A CB    1 
ATOM   2559 C  CG    . ASN A 1 333 ? 131.859 129.368 159.599 1.00 36.16  ? 334  ASN A CG    1 
ATOM   2560 O  OD1   . ASN A 1 333 ? 132.157 130.067 158.636 1.00 36.16  ? 334  ASN A OD1   1 
ATOM   2561 N  ND2   . ASN A 1 333 ? 131.752 128.051 159.519 1.00 36.16  ? 334  ASN A ND2   1 
ATOM   2562 N  N     . ALA A 1 334 ? 134.617 131.051 161.637 1.00 32.29  ? 335  ALA A N     1 
ATOM   2563 C  CA    . ALA A 1 334 ? 135.939 131.401 161.120 1.00 32.29  ? 335  ALA A CA    1 
ATOM   2564 C  C     . ALA A 1 334 ? 137.037 130.522 161.699 1.00 32.29  ? 335  ALA A C     1 
ATOM   2565 O  O     . ALA A 1 334 ? 137.966 130.134 160.985 1.00 32.29  ? 335  ALA A O     1 
ATOM   2566 C  CB    . ALA A 1 334 ? 136.239 132.868 161.404 1.00 32.29  ? 335  ALA A CB    1 
ATOM   2567 N  N     . PHE A 1 335 ? 136.967 130.221 162.996 1.00 33.39  ? 336  PHE A N     1 
ATOM   2568 C  CA    . PHE A 1 335 ? 137.882 129.246 163.584 1.00 33.39  ? 336  PHE A CA    1 
ATOM   2569 C  C     . PHE A 1 335 ? 137.680 127.831 163.049 1.00 33.39  ? 336  PHE A C     1 
ATOM   2570 O  O     . PHE A 1 335 ? 138.643 127.058 162.985 1.00 33.39  ? 336  PHE A O     1 
ATOM   2571 C  CB    . PHE A 1 335 ? 137.770 129.261 165.104 1.00 33.39  ? 336  PHE A CB    1 
ATOM   2572 C  CG    . PHE A 1 335 ? 138.296 130.509 165.718 1.00 33.39  ? 336  PHE A CG    1 
ATOM   2573 C  CD1   . PHE A 1 335 ? 139.615 130.868 165.526 1.00 33.39  ? 336  PHE A CD1   1 
ATOM   2574 C  CD2   . PHE A 1 335 ? 137.491 131.311 166.501 1.00 33.39  ? 336  PHE A CD2   1 
ATOM   2575 C  CE1   . PHE A 1 335 ? 140.114 132.013 166.078 1.00 33.39  ? 336  PHE A CE1   1 
ATOM   2576 C  CE2   . PHE A 1 335 ? 137.984 132.458 167.062 1.00 33.39  ? 336  PHE A CE2   1 
ATOM   2577 C  CZ    . PHE A 1 335 ? 139.298 132.810 166.848 1.00 33.39  ? 336  PHE A CZ    1 
ATOM   2578 N  N     . ASP A 1 336 ? 136.444 127.456 162.714 1.00 32.79  ? 337  ASP A N     1 
ATOM   2579 C  CA    . ASP A 1 336 ? 136.204 126.170 162.061 1.00 32.79  ? 337  ASP A CA    1 
ATOM   2580 C  C     . ASP A 1 336 ? 136.902 126.075 160.707 1.00 32.79  ? 337  ASP A C     1 
ATOM   2581 O  O     . ASP A 1 336 ? 137.507 125.046 160.389 1.00 32.79  ? 337  ASP A O     1 
ATOM   2582 C  CB    . ASP A 1 336 ? 134.704 125.924 161.921 1.00 32.79  ? 337  ASP A CB    1 
ATOM   2583 C  CG    . ASP A 1 336 ? 134.332 124.481 162.161 1.00 32.79  ? 337  ASP A CG    1 
ATOM   2584 O  OD1   . ASP A 1 336 ? 135.207 123.609 161.990 1.00 32.79  ? 337  ASP A OD1   1 
ATOM   2585 O  OD2   . ASP A 1 336 ? 133.167 124.216 162.525 1.00 32.79  ? 337  ASP A OD2   1 
ATOM   2586 N  N     . VAL A 1 337 ? 136.805 127.126 159.885 1.00 30.58  ? 338  VAL A N     1 
ATOM   2587 C  CA    . VAL A 1 337 ? 137.382 127.087 158.541 1.00 30.58  ? 338  VAL A CA    1 
ATOM   2588 C  C     . VAL A 1 337 ? 138.905 127.073 158.608 1.00 30.58  ? 338  VAL A C     1 
ATOM   2589 O  O     . VAL A 1 337 ? 139.570 126.368 157.840 1.00 30.58  ? 338  VAL A O     1 
ATOM   2590 C  CB    . VAL A 1 337 ? 136.856 128.265 157.699 1.00 30.58  ? 338  VAL A CB    1 
ATOM   2591 C  CG1   . VAL A 1 337 ? 137.431 128.230 156.301 1.00 30.58  ? 338  VAL A CG1   1 
ATOM   2592 C  CG2   . VAL A 1 337 ? 135.344 128.231 157.628 1.00 30.58  ? 338  VAL A CG2   1 
ATOM   2593 N  N     . LEU A 1 338 ? 139.482 127.809 159.557 1.00 30.07  ? 339  LEU A N     1 
ATOM   2594 C  CA    . LEU A 1 338 ? 140.916 127.731 159.816 1.00 30.07  ? 339  LEU A CA    1 
ATOM   2595 C  C     . LEU A 1 338 ? 141.339 126.415 160.457 1.00 30.07  ? 339  LEU A C     1 
ATOM   2596 O  O     . LEU A 1 338 ? 142.541 126.148 160.531 1.00 30.07  ? 339  LEU A O     1 
ATOM   2597 C  CB    . LEU A 1 338 ? 141.356 128.907 160.679 1.00 30.07  ? 339  LEU A CB    1 
ATOM   2598 C  CG    . LEU A 1 338 ? 141.125 130.225 159.945 1.00 30.07  ? 339  LEU A CG    1 
ATOM   2599 C  CD1   . LEU A 1 338 ? 141.110 131.373 160.908 1.00 30.07  ? 339  LEU A CD1   1 
ATOM   2600 C  CD2   . LEU A 1 338 ? 142.179 130.435 158.885 1.00 30.07  ? 339  LEU A CD2   1 
ATOM   2601 N  N     . GLY A 1 339 ? 140.397 125.597 160.917 1.00 32.43  ? 340  GLY A N     1 
ATOM   2602 C  CA    . GLY A 1 339 ? 140.711 124.265 161.387 1.00 32.43  ? 340  GLY A CA    1 
ATOM   2603 C  C     . GLY A 1 339 ? 140.995 124.138 162.862 1.00 32.43  ? 340  GLY A C     1 
ATOM   2604 O  O     . GLY A 1 339 ? 141.677 123.189 163.263 1.00 32.43  ? 340  GLY A O     1 
ATOM   2605 N  N     . PHE A 1 340 ? 140.517 125.072 163.680 1.00 31.88  ? 341  PHE A N     1 
ATOM   2606 C  CA    . PHE A 1 340 ? 140.669 124.963 165.125 1.00 31.88  ? 341  PHE A CA    1 
ATOM   2607 C  C     . PHE A 1 340 ? 139.801 123.819 165.633 1.00 31.88  ? 341  PHE A C     1 
ATOM   2608 O  O     . PHE A 1 340 ? 138.587 123.813 165.405 1.00 31.88  ? 341  PHE A O     1 
ATOM   2609 C  CB    . PHE A 1 340 ? 140.274 126.265 165.820 1.00 31.88  ? 341  PHE A CB    1 
ATOM   2610 C  CG    . PHE A 1 340 ? 141.280 127.383 165.681 1.00 31.88  ? 341  PHE A CG    1 
ATOM   2611 C  CD1   . PHE A 1 340 ? 141.515 127.996 164.462 1.00 31.88  ? 341  PHE A CD1   1 
ATOM   2612 C  CD2   . PHE A 1 340 ? 141.984 127.824 166.785 1.00 31.88  ? 341  PHE A CD2   1 
ATOM   2613 C  CE1   . PHE A 1 340 ? 142.430 129.019 164.350 1.00 31.88  ? 341  PHE A CE1   1 
ATOM   2614 C  CE2   . PHE A 1 340 ? 142.900 128.846 166.675 1.00 31.88  ? 341  PHE A CE2   1 
ATOM   2615 C  CZ    . PHE A 1 340 ? 143.120 129.442 165.457 1.00 31.88  ? 341  PHE A CZ    1 
ATOM   2616 N  N     . THR A 1 341 ? 140.423 122.845 166.296 1.00 37.68  ? 342  THR A N     1 
ATOM   2617 C  CA    . THR A 1 341 ? 139.690 121.710 166.842 1.00 37.68  ? 342  THR A CA    1 
ATOM   2618 C  C     . THR A 1 341 ? 138.772 122.170 167.969 1.00 37.68  ? 342  THR A C     1 
ATOM   2619 O  O     . THR A 1 341 ? 139.012 123.198 168.605 1.00 37.68  ? 342  THR A O     1 
ATOM   2620 C  CB    . THR A 1 341 ? 140.653 120.642 167.348 1.00 37.68  ? 342  THR A CB    1 
ATOM   2621 O  OG1   . THR A 1 341 ? 141.370 121.142 168.478 1.00 37.68  ? 342  THR A OG1   1 
ATOM   2622 C  CG2   . THR A 1 341 ? 141.652 120.289 166.265 1.00 37.68  ? 342  THR A CG2   1 
ATOM   2623 N  N     . SER A 1 342 ? 137.700 121.399 168.190 1.00 39.49  ? 343  SER A N     1 
ATOM   2624 C  CA    . SER A 1 342 ? 136.588 121.848 169.030 1.00 39.49  ? 343  SER A CA    1 
ATOM   2625 C  C     . SER A 1 342 ? 136.999 122.060 170.483 1.00 39.49  ? 343  SER A C     1 
ATOM   2626 O  O     . SER A 1 342 ? 136.502 122.980 171.141 1.00 39.49  ? 343  SER A O     1 
ATOM   2627 C  CB    . SER A 1 342 ? 135.431 120.853 168.948 1.00 39.49  ? 343  SER A CB    1 
ATOM   2628 O  OG    . SER A 1 342 ? 134.269 121.386 169.560 1.00 39.49  ? 343  SER A OG    1 
ATOM   2629 N  N     . GLU A 1 343 ? 137.880 121.206 171.011 1.00 38.82  ? 344  GLU A N     1 
ATOM   2630 C  CA    . GLU A 1 343 ? 138.373 121.427 172.367 1.00 38.82  ? 344  GLU A CA    1 
ATOM   2631 C  C     . GLU A 1 343 ? 139.269 122.658 172.441 1.00 38.82  ? 344  GLU A C     1 
ATOM   2632 O  O     . GLU A 1 343 ? 139.264 123.362 173.453 1.00 38.82  ? 344  GLU A O     1 
ATOM   2633 C  CB    . GLU A 1 343 ? 139.096 120.173 172.883 1.00 38.82  ? 344  GLU A CB    1 
ATOM   2634 C  CG    . GLU A 1 343 ? 140.422 119.803 172.207 1.00 38.82  ? 344  GLU A CG    1 
ATOM   2635 C  CD    . GLU A 1 343 ? 140.255 118.928 170.976 1.00 38.82  ? 344  GLU A CD    1 
ATOM   2636 O  OE1   . GLU A 1 343 ? 141.180 118.141 170.685 1.00 38.82  ? 344  GLU A OE1   1 
ATOM   2637 O  OE2   . GLU A 1 343 ? 139.212 119.021 170.295 1.00 38.82  ? 344  GLU A OE2   1 
ATOM   2638 N  N     . GLU A 1 344 ? 140.021 122.935 171.375 1.00 35.16  ? 345  GLU A N     1 
ATOM   2639 C  CA    . GLU A 1 344 ? 140.927 124.078 171.340 1.00 35.16  ? 345  GLU A CA    1 
ATOM   2640 C  C     . GLU A 1 344 ? 140.161 125.377 171.159 1.00 35.16  ? 345  GLU A C     1 
ATOM   2641 O  O     . GLU A 1 344 ? 140.512 126.407 171.743 1.00 35.16  ? 345  GLU A O     1 
ATOM   2642 C  CB    . GLU A 1 344 ? 141.930 123.871 170.214 1.00 35.16  ? 345  GLU A CB    1 
ATOM   2643 C  CG    . GLU A 1 344 ? 142.979 124.911 170.059 1.00 35.16  ? 345  GLU A CG    1 
ATOM   2644 C  CD    . GLU A 1 344 ? 144.142 124.368 169.266 1.00 35.16  ? 345  GLU A CD    1 
ATOM   2645 O  OE1   . GLU A 1 344 ? 144.917 123.565 169.825 1.00 35.16  ? 345  GLU A OE1   1 
ATOM   2646 O  OE2   . GLU A 1 344 ? 144.276 124.730 168.081 1.00 35.16  ? 345  GLU A OE2   1 
ATOM   2647 N  N     . LYS A 1 345 ? 139.113 125.338 170.344 1.00 36.73  ? 346  LYS A N     1 
ATOM   2648 C  CA    . LYS A 1 345 ? 138.218 126.475 170.178 1.00 36.73  ? 346  LYS A CA    1 
ATOM   2649 C  C     . LYS A 1 345 ? 137.436 126.772 171.451 1.00 36.73  ? 346  LYS A C     1 
ATOM   2650 O  O     . LYS A 1 345 ? 137.257 127.939 171.809 1.00 36.73  ? 346  LYS A O     1 
ATOM   2651 C  CB    . LYS A 1 345 ? 137.278 126.189 169.010 1.00 36.73  ? 346  LYS A CB    1 
ATOM   2652 C  CG    . LYS A 1 345 ? 136.452 127.344 168.531 1.00 36.73  ? 346  LYS A CG    1 
ATOM   2653 C  CD    . LYS A 1 345 ? 135.687 126.924 167.293 1.00 36.73  ? 346  LYS A CD    1 
ATOM   2654 C  CE    . LYS A 1 345 ? 134.674 125.847 167.605 1.00 36.73  ? 346  LYS A CE    1 
ATOM   2655 N  NZ    . LYS A 1 345 ? 133.538 125.884 166.648 1.00 36.73  ? 346  LYS A NZ    1 
ATOM   2656 N  N     . ASN A 1 346 ? 136.925 125.734 172.117 1.00 37.11  ? 347  ASN A N     1 
ATOM   2657 C  CA    . ASN A 1 346 ? 136.298 125.906 173.427 1.00 37.11  ? 347  ASN A CA    1 
ATOM   2658 C  C     . ASN A 1 346 ? 137.273 126.456 174.462 1.00 37.11  ? 347  ASN A C     1 
ATOM   2659 O  O     . ASN A 1 346 ? 136.887 127.262 175.317 1.00 37.11  ? 347  ASN A O     1 
ATOM   2660 C  CB    . ASN A 1 346 ? 135.732 124.573 173.912 1.00 37.11  ? 347  ASN A CB    1 
ATOM   2661 C  CG    . ASN A 1 346 ? 134.415 124.223 173.256 1.00 37.11  ? 347  ASN A CG    1 
ATOM   2662 O  OD1   . ASN A 1 346 ? 133.473 125.013 173.263 1.00 37.11  ? 347  ASN A OD1   1 
ATOM   2663 N  ND2   . ASN A 1 346 ? 134.345 123.031 172.677 1.00 37.11  ? 347  ASN A ND2   1 
ATOM   2664 N  N     . SER A 1 347 ? 138.525 125.987 174.428 1.00 34.43  ? 348  SER A N     1 
ATOM   2665 C  CA    . SER A 1 347 ? 139.532 126.383 175.412 1.00 34.43  ? 348  SER A CA    1 
ATOM   2666 C  C     . SER A 1 347 ? 139.835 127.879 175.392 1.00 34.43  ? 348  SER A C     1 
ATOM   2667 O  O     . SER A 1 347 ? 140.059 128.481 176.445 1.00 34.43  ? 348  SER A O     1 
ATOM   2668 C  CB    . SER A 1 347 ? 140.816 125.593 175.200 1.00 34.43  ? 348  SER A CB    1 
ATOM   2669 O  OG    . SER A 1 347 ? 141.874 126.194 175.910 1.00 34.43  ? 348  SER A OG    1 
ATOM   2670 N  N     . MET A 1 348 ? 139.896 128.491 174.214 1.00 30.86  ? 349  MET A N     1 
ATOM   2671 C  CA    . MET A 1 348 ? 140.185 129.919 174.187 1.00 30.86  ? 349  MET A CA    1 
ATOM   2672 C  C     . MET A 1 348 ? 138.988 130.775 174.573 1.00 30.86  ? 349  MET A C     1 
ATOM   2673 O  O     . MET A 1 348 ? 139.176 131.928 174.963 1.00 30.86  ? 349  MET A O     1 
ATOM   2674 C  CB    . MET A 1 348 ? 140.727 130.332 172.821 1.00 30.86  ? 349  MET A CB    1 
ATOM   2675 C  CG    . MET A 1 348 ? 139.844 130.027 171.654 1.00 30.86  ? 349  MET A CG    1 
ATOM   2676 S  SD    . MET A 1 348 ? 140.533 130.781 170.183 1.00 30.86  ? 349  MET A SD    1 
ATOM   2677 C  CE    . MET A 1 348 ? 142.113 129.949 170.126 1.00 30.86  ? 349  MET A CE    1 
ATOM   2678 N  N     . TYR A 1 349 ? 137.769 130.260 174.452 1.00 33.71  ? 350  TYR A N     1 
ATOM   2679 C  CA    . TYR A 1 349 ? 136.644 130.888 175.136 1.00 33.71  ? 350  TYR A CA    1 
ATOM   2680 C  C     . TYR A 1 349 ? 136.759 130.789 176.654 1.00 33.71  ? 350  TYR A C     1 
ATOM   2681 O  O     . TYR A 1 349 ? 136.265 131.675 177.359 1.00 33.71  ? 350  TYR A O     1 
ATOM   2682 C  CB    . TYR A 1 349 ? 135.320 130.285 174.675 1.00 33.71  ? 350  TYR A CB    1 
ATOM   2683 C  CG    . TYR A 1 349 ? 135.046 130.411 173.197 1.00 33.71  ? 350  TYR A CG    1 
ATOM   2684 C  CD1   . TYR A 1 349 ? 135.322 131.590 172.517 1.00 33.71  ? 350  TYR A CD1   1 
ATOM   2685 C  CD2   . TYR A 1 349 ? 134.500 129.352 172.483 1.00 33.71  ? 350  TYR A CD2   1 
ATOM   2686 C  CE1   . TYR A 1 349 ? 135.063 131.707 171.165 1.00 33.71  ? 350  TYR A CE1   1 
ATOM   2687 C  CE2   . TYR A 1 349 ? 134.244 129.457 171.134 1.00 33.71  ? 350  TYR A CE2   1 
ATOM   2688 C  CZ    . TYR A 1 349 ? 134.526 130.635 170.482 1.00 33.71  ? 350  TYR A CZ    1 
ATOM   2689 O  OH    . TYR A 1 349 ? 134.270 130.734 169.137 1.00 33.71  ? 350  TYR A OH    1 
ATOM   2690 N  N     . LYS A 1 350 ? 137.340 129.702 177.173 1.00 32.24  ? 351  LYS A N     1 
ATOM   2691 C  CA    . LYS A 1 350 ? 137.512 129.552 178.620 1.00 32.24  ? 351  LYS A CA    1 
ATOM   2692 C  C     . LYS A 1 350 ? 138.409 130.633 179.214 1.00 32.24  ? 351  LYS A C     1 
ATOM   2693 O  O     . LYS A 1 350 ? 138.081 131.213 180.256 1.00 32.24  ? 351  LYS A O     1 
ATOM   2694 C  CB    . LYS A 1 350 ? 138.051 128.161 178.946 1.00 32.24  ? 351  LYS A CB    1 
ATOM   2695 C  CG    . LYS A 1 350 ? 137.028 127.053 178.801 1.00 32.24  ? 351  LYS A CG    1 
ATOM   2696 C  CD    . LYS A 1 350 ? 137.645 125.696 179.073 1.00 32.24  ? 351  LYS A CD    1 
ATOM   2697 C  CE    . LYS A 1 350 ? 136.615 124.592 178.948 1.00 32.24  ? 351  LYS A CE    1 
ATOM   2698 N  NZ    . LYS A 1 350 ? 137.208 123.253 179.199 1.00 32.24  ? 351  LYS A NZ    1 
ATOM   2699 N  N     . LEU A 1 351 ? 139.550 130.907 178.581 1.00 27.57  ? 352  LEU A N     1 
ATOM   2700 C  CA    . LEU A 1 351 ? 140.416 131.982 179.059 1.00 27.57  ? 352  LEU A CA    1 
ATOM   2701 C  C     . LEU A 1 351 ? 139.763 133.347 178.876 1.00 27.57  ? 352  LEU A C     1 
ATOM   2702 O  O     . LEU A 1 351 ? 139.836 134.198 179.767 1.00 27.57  ? 352  LEU A O     1 
ATOM   2703 C  CB    . LEU A 1 351 ? 141.763 131.924 178.354 1.00 27.57  ? 352  LEU A CB    1 
ATOM   2704 C  CG    . LEU A 1 351 ? 142.511 130.617 178.590 1.00 27.57  ? 352  LEU A CG    1 
ATOM   2705 C  CD1   . LEU A 1 351 ? 143.859 130.691 177.936 1.00 27.57  ? 352  LEU A CD1   1 
ATOM   2706 C  CD2   . LEU A 1 351 ? 142.652 130.320 180.064 1.00 27.57  ? 352  LEU A CD2   1 
ATOM   2707 N  N     . THR A 1 352 ? 139.114 133.572 177.730 1.00 27.08  ? 353  THR A N     1 
ATOM   2708 C  CA    . THR A 1 352 ? 138.341 134.790 177.508 1.00 27.08  ? 353  THR A CA    1 
ATOM   2709 C  C     . THR A 1 352 ? 137.114 134.856 178.419 1.00 27.08  ? 353  THR A C     1 
ATOM   2710 O  O     . THR A 1 352 ? 136.568 135.938 178.643 1.00 27.08  ? 353  THR A O     1 
ATOM   2711 C  CB    . THR A 1 352 ? 137.954 134.849 176.024 1.00 27.08  ? 353  THR A CB    1 
ATOM   2712 O  OG1   . THR A 1 352 ? 139.129 134.632 175.236 1.00 27.08  ? 353  THR A OG1   1 
ATOM   2713 C  CG2   . THR A 1 352 ? 137.400 136.202 175.615 1.00 27.08  ? 353  THR A CG2   1 
ATOM   2714 N  N     . GLY A 1 353 ? 136.710 133.733 179.003 1.00 31.03  ? 354  GLY A N     1 
ATOM   2715 C  CA    . GLY A 1 353 ? 135.731 133.711 180.069 1.00 31.03  ? 354  GLY A CA    1 
ATOM   2716 C  C     . GLY A 1 353 ? 136.330 134.019 181.425 1.00 31.03  ? 354  GLY A C     1 
ATOM   2717 O  O     . GLY A 1 353 ? 135.739 134.766 182.208 1.00 31.03  ? 354  GLY A O     1 
ATOM   2718 N  N     . ALA A 1 354 ? 137.467 133.378 181.725 1.00 32.93  ? 355  ALA A N     1 
ATOM   2719 C  CA    . ALA A 1 354 ? 138.171 133.576 182.992 1.00 32.93  ? 355  ALA A CA    1 
ATOM   2720 C  C     . ALA A 1 354 ? 138.554 135.032 183.229 1.00 32.93  ? 355  ALA A C     1 
ATOM   2721 O  O     . ALA A 1 354 ? 138.477 135.515 184.363 1.00 32.93  ? 355  ALA A O     1 
ATOM   2722 C  CB    . ALA A 1 354 ? 139.416 132.697 183.036 1.00 32.93  ? 355  ALA A CB    1 
ATOM   2723 N  N     . ILE A 1 355 ? 139.000 135.732 182.180 1.00 29.57  ? 356  ILE A N     1 
ATOM   2724 C  CA    . ILE A 1 355 ? 139.374 137.147 182.259 1.00 29.57  ? 356  ILE A CA    1 
ATOM   2725 C  C     . ILE A 1 355 ? 138.208 138.032 182.707 1.00 29.57  ? 356  ILE A C     1 
ATOM   2726 O  O     . ILE A 1 355 ? 138.409 139.013 183.432 1.00 29.57  ? 356  ILE A O     1 
ATOM   2727 C  CB    . ILE A 1 355 ? 139.963 137.564 180.892 1.00 29.57  ? 356  ILE A CB    1 
ATOM   2728 C  CG1   . ILE A 1 355 ? 141.366 136.985 180.732 1.00 29.57  ? 356  ILE A CG1   1 
ATOM   2729 C  CG2   . ILE A 1 355 ? 140.023 139.062 180.695 1.00 29.57  ? 356  ILE A CG2   1 
ATOM   2730 C  CD1   . ILE A 1 355 ? 141.893 137.075 179.333 1.00 29.57  ? 356  ILE A CD1   1 
ATOM   2731 N  N     . MET A 1 356 ? 136.973 137.662 182.360 1.00 34.87  ? 357  MET A N     1 
ATOM   2732 C  CA    . MET A 1 356 ? 135.809 138.411 182.833 1.00 34.87  ? 357  MET A CA    1 
ATOM   2733 C  C     . MET A 1 356 ? 135.608 138.240 184.333 1.00 34.87  ? 357  MET A C     1 
ATOM   2734 O  O     . MET A 1 356 ? 135.268 139.200 185.031 1.00 34.87  ? 357  MET A O     1 
ATOM   2735 C  CB    . MET A 1 356 ? 134.558 137.964 182.081 1.00 34.87  ? 357  MET A CB    1 
ATOM   2736 C  CG    . MET A 1 356 ? 134.782 137.763 180.606 1.00 34.87  ? 357  MET A CG    1 
ATOM   2737 S  SD    . MET A 1 356 ? 133.377 137.139 179.669 1.00 34.87  ? 357  MET A SD    1 
ATOM   2738 C  CE    . MET A 1 356 ? 132.219 138.495 179.737 1.00 34.87  ? 357  MET A CE    1 
ATOM   2739 N  N     . HIS A 1 357 ? 135.808 137.023 184.841 1.00 38.04  ? 358  HIS A N     1 
ATOM   2740 C  CA    . HIS A 1 357 ? 135.719 136.782 186.277 1.00 38.04  ? 358  HIS A CA    1 
ATOM   2741 C  C     . HIS A 1 357 ? 136.883 137.408 187.023 1.00 38.04  ? 358  HIS A C     1 
ATOM   2742 O  O     . HIS A 1 357 ? 136.718 137.847 188.166 1.00 38.04  ? 358  HIS A O     1 
ATOM   2743 C  CB    . HIS A 1 357 ? 135.689 135.283 186.570 1.00 38.04  ? 358  HIS A CB    1 
ATOM   2744 C  CG    . HIS A 1 357 ? 134.519 134.568 185.980 1.00 38.04  ? 358  HIS A CG    1 
ATOM   2745 N  ND1   . HIS A 1 357 ? 134.656 133.435 185.209 1.00 38.04  ? 358  HIS A ND1   1 
ATOM   2746 C  CD2   . HIS A 1 357 ? 133.191 134.813 186.058 1.00 38.04  ? 358  HIS A CD2   1 
ATOM   2747 C  CE1   . HIS A 1 357 ? 133.463 133.017 184.830 1.00 38.04  ? 358  HIS A CE1   1 
ATOM   2748 N  NE2   . HIS A 1 357 ? 132.556 133.836 185.332 1.00 38.04  ? 358  HIS A NE2   1 
ATOM   2749 N  N     . PHE A 1 358 ? 138.060 137.438 186.391 1.00 36.96  ? 359  PHE A N     1 
ATOM   2750 C  CA    . PHE A 1 358 ? 139.321 137.677 187.083 1.00 36.96  ? 359  PHE A CA    1 
ATOM   2751 C  C     . PHE A 1 358 ? 139.402 139.089 187.642 1.00 36.96  ? 359  PHE A C     1 
ATOM   2752 O  O     . PHE A 1 358 ? 140.074 139.319 188.650 1.00 36.96  ? 359  PHE A O     1 
ATOM   2753 C  CB    . PHE A 1 358 ? 140.466 137.427 186.107 1.00 36.96  ? 359  PHE A CB    1 
ATOM   2754 C  CG    . PHE A 1 358 ? 141.763 137.072 186.751 1.00 36.96  ? 359  PHE A CG    1 
ATOM   2755 C  CD1   . PHE A 1 358 ? 141.972 135.791 187.227 1.00 36.96  ? 359  PHE A CD1   1 
ATOM   2756 C  CD2   . PHE A 1 358 ? 142.787 137.990 186.839 1.00 36.96  ? 359  PHE A CD2   1 
ATOM   2757 C  CE1   . PHE A 1 358 ? 143.167 135.437 187.803 1.00 36.96  ? 359  PHE A CE1   1 
ATOM   2758 C  CE2   . PHE A 1 358 ? 143.987 137.640 187.416 1.00 36.96  ? 359  PHE A CE2   1 
ATOM   2759 C  CZ    . PHE A 1 358 ? 144.174 136.362 187.900 1.00 36.96  ? 359  PHE A CZ    1 
ATOM   2760 N  N     . GLY A 1 359 ? 138.721 140.042 187.006 1.00 37.94  ? 360  GLY A N     1 
ATOM   2761 C  CA    . GLY A 1 359 ? 138.606 141.384 187.545 1.00 37.94  ? 360  GLY A CA    1 
ATOM   2762 C  C     . GLY A 1 359 ? 137.592 141.554 188.649 1.00 37.94  ? 360  GLY A C     1 
ATOM   2763 O  O     . GLY A 1 359 ? 137.640 142.557 189.367 1.00 37.94  ? 360  GLY A O     1 
ATOM   2764 N  N     . ASN A 1 360 ? 136.671 140.609 188.801 1.00 44.25  ? 361  ASN A N     1 
ATOM   2765 C  CA    . ASN A 1 360 ? 135.670 140.713 189.851 1.00 44.25  ? 361  ASN A CA    1 
ATOM   2766 C  C     . ASN A 1 360 ? 136.161 140.222 191.203 1.00 44.25  ? 361  ASN A C     1 
ATOM   2767 O  O     . ASN A 1 360 ? 135.433 140.387 192.188 1.00 44.25  ? 361  ASN A O     1 
ATOM   2768 C  CB    . ASN A 1 360 ? 134.409 139.952 189.451 1.00 44.25  ? 361  ASN A CB    1 
ATOM   2769 C  CG    . ASN A 1 360 ? 133.506 140.767 188.560 1.00 44.25  ? 361  ASN A CG    1 
ATOM   2770 O  OD1   . ASN A 1 360 ? 133.955 141.697 187.894 1.00 44.25  ? 361  ASN A OD1   1 
ATOM   2771 N  ND2   . ASN A 1 360 ? 132.224 140.430 188.547 1.00 44.25  ? 361  ASN A ND2   1 
ATOM   2772 N  N     . MET A 1 361 ? 137.321 139.562 191.251 1.00 48.95  ? 362  MET A N     1 
ATOM   2773 C  CA    . MET A 1 361 ? 137.901 139.106 192.509 1.00 48.95  ? 362  MET A CA    1 
ATOM   2774 C  C     . MET A 1 361 ? 138.133 140.266 193.470 1.00 48.95  ? 362  MET A C     1 
ATOM   2775 O  O     . MET A 1 361 ? 138.792 141.251 193.129 1.00 48.95  ? 362  MET A O     1 
ATOM   2776 C  CB    . MET A 1 361 ? 139.220 138.384 192.246 1.00 48.95  ? 362  MET A CB    1 
ATOM   2777 C  CG    . MET A 1 361 ? 139.099 137.159 191.373 1.00 48.95  ? 362  MET A CG    1 
ATOM   2778 S  SD    . MET A 1 361 ? 140.563 136.114 191.476 1.00 48.95  ? 362  MET A SD    1 
ATOM   2779 C  CE    . MET A 1 361 ? 141.827 137.244 190.914 1.00 48.95  ? 362  MET A CE    1 
ATOM   2780 N  N     . LYS A 1 362 ? 137.593 140.142 194.677 1.00 56.68  ? 363  LYS A N     1 
ATOM   2781 C  CA    . LYS A 1 362 ? 137.667 141.183 195.692 1.00 56.68  ? 363  LYS A CA    1 
ATOM   2782 C  C     . LYS A 1 362 ? 138.764 140.838 196.689 1.00 56.68  ? 363  LYS A C     1 
ATOM   2783 O  O     . LYS A 1 362 ? 138.935 139.672 197.056 1.00 56.68  ? 363  LYS A O     1 
ATOM   2784 C  CB    . LYS A 1 362 ? 136.331 141.337 196.424 1.00 56.68  ? 363  LYS A CB    1 
ATOM   2785 C  CG    . LYS A 1 362 ? 135.121 141.620 195.548 1.00 56.68  ? 363  LYS A CG    1 
ATOM   2786 C  CD    . LYS A 1 362 ? 135.296 142.879 194.728 1.00 56.68  ? 363  LYS A CD    1 
ATOM   2787 C  CE    . LYS A 1 362 ? 134.000 143.253 194.025 1.00 56.68  ? 363  LYS A CE    1 
ATOM   2788 N  NZ    . LYS A 1 362 ? 133.489 142.147 193.170 1.00 56.68  ? 363  LYS A NZ    1 
ATOM   2789 N  N     . PHE A 1 363 ? 139.514 141.848 197.120 1.00 59.82  ? 364  PHE A N     1 
ATOM   2790 C  CA    . PHE A 1 363 ? 140.556 141.660 198.119 1.00 59.82  ? 364  PHE A CA    1 
ATOM   2791 C  C     . PHE A 1 363 ? 140.430 142.729 199.194 1.00 59.82  ? 364  PHE A C     1 
ATOM   2792 O  O     . PHE A 1 363 ? 140.049 143.868 198.916 1.00 59.82  ? 364  PHE A O     1 
ATOM   2793 C  CB    . PHE A 1 363 ? 141.951 141.701 197.492 1.00 59.82  ? 364  PHE A CB    1 
ATOM   2794 C  CG    . PHE A 1 363 ? 142.195 140.606 196.502 1.00 59.82  ? 364  PHE A CG    1 
ATOM   2795 C  CD1   . PHE A 1 363 ? 142.696 139.386 196.915 1.00 59.82  ? 364  PHE A CD1   1 
ATOM   2796 C  CD2   . PHE A 1 363 ? 141.914 140.790 195.159 1.00 59.82  ? 364  PHE A CD2   1 
ATOM   2797 C  CE1   . PHE A 1 363 ? 142.918 138.372 196.009 1.00 59.82  ? 364  PHE A CE1   1 
ATOM   2798 C  CE2   . PHE A 1 363 ? 142.134 139.779 194.250 1.00 59.82  ? 364  PHE A CE2   1 
ATOM   2799 C  CZ    . PHE A 1 363 ? 142.634 138.569 194.677 1.00 59.82  ? 364  PHE A CZ    1 
ATOM   2800 N  N     . LYS A 1 364 ? 140.749 142.350 200.430 1.00 63.64  ? 365  LYS A N     1 
ATOM   2801 C  CA    . LYS A 1 364 ? 140.681 143.267 201.558 1.00 63.64  ? 365  LYS A CA    1 
ATOM   2802 C  C     . LYS A 1 364 ? 141.939 143.187 202.410 1.00 63.64  ? 365  LYS A C     1 
ATOM   2803 O  O     . LYS A 1 364 ? 142.553 142.125 202.545 1.00 63.64  ? 365  LYS A O     1 
ATOM   2804 C  CB    . LYS A 1 364 ? 139.439 142.991 202.418 1.00 63.64  ? 365  LYS A CB    1 
ATOM   2805 C  CG    . LYS A 1 364 ? 139.380 141.606 203.040 1.00 63.64  ? 365  LYS A CG    1 
ATOM   2806 C  CD    . LYS A 1 364 ? 138.102 141.423 203.839 1.00 63.64  ? 365  LYS A CD    1 
ATOM   2807 C  CE    . LYS A 1 364 ? 137.986 140.012 204.386 1.00 63.64  ? 365  LYS A CE    1 
ATOM   2808 N  NZ    . LYS A 1 364 ? 136.669 139.791 205.040 1.00 63.64  ? 365  LYS A NZ    1 
ATOM   2809 N  N     . LEU A 1 365 ? 142.331 144.338 202.949 1.00 69.11  ? 366  LEU A N     1 
ATOM   2810 C  CA    . LEU A 1 365 ? 143.419 144.412 203.914 1.00 69.11  ? 366  LEU A CA    1 
ATOM   2811 C  C     . LEU A 1 365 ? 143.020 143.765 205.231 1.00 69.11  ? 366  LEU A C     1 
ATOM   2812 O  O     . LEU A 1 365 ? 141.931 144.016 205.755 1.00 69.11  ? 366  LEU A O     1 
ATOM   2813 C  CB    . LEU A 1 365 ? 143.818 145.863 204.166 1.00 69.11  ? 366  LEU A CB    1 
ATOM   2814 C  CG    . LEU A 1 365 ? 144.489 146.625 203.032 1.00 69.11  ? 366  LEU A CG    1 
ATOM   2815 C  CD1   . LEU A 1 365 ? 144.618 148.095 203.383 1.00 69.11  ? 366  LEU A CD1   1 
ATOM   2816 C  CD2   . LEU A 1 365 ? 145.850 146.022 202.751 1.00 69.11  ? 366  LEU A CD2   1 
ATOM   2817 N  N     . LYS A 1 366 ? 143.902 142.924 205.761 1.00 75.37  ? 367  LYS A N     1 
ATOM   2818 C  CA    . LYS A 1 366 ? 143.813 142.567 207.168 1.00 75.37  ? 367  LYS A CA    1 
ATOM   2819 C  C     . LYS A 1 366 ? 144.109 143.797 208.021 1.00 75.37  ? 367  LYS A C     1 
ATOM   2820 O  O     . LYS A 1 366 ? 145.021 144.573 207.720 1.00 75.37  ? 367  LYS A O     1 
ATOM   2821 C  CB    . LYS A 1 366 ? 144.791 141.438 207.485 1.00 75.37  ? 367  LYS A CB    1 
ATOM   2822 C  CG    . LYS A 1 366 ? 144.513 140.141 206.749 1.00 75.37  ? 367  LYS A CG    1 
ATOM   2823 C  CD    . LYS A 1 366 ? 143.087 139.679 206.984 1.00 75.37  ? 367  LYS A CD    1 
ATOM   2824 C  CE    . LYS A 1 366 ? 142.845 138.309 206.382 1.00 75.37  ? 367  LYS A CE    1 
ATOM   2825 N  NZ    . LYS A 1 366 ? 143.639 137.245 207.057 1.00 75.37  ? 367  LYS A NZ    1 
ATOM   2826 N  N     . GLN A 1 367 ? 143.325 143.959 209.096 1.00 82.05  ? 368  GLN A N     1 
ATOM   2827 C  CA    . GLN A 1 367 ? 143.052 145.280 209.666 1.00 82.05  ? 368  GLN A CA    1 
ATOM   2828 C  C     . GLN A 1 367 ? 144.273 145.931 210.310 1.00 82.05  ? 368  GLN A C     1 
ATOM   2829 O  O     . GLN A 1 367 ? 144.366 147.163 210.343 1.00 82.05  ? 368  GLN A O     1 
ATOM   2830 C  CB    . GLN A 1 367 ? 141.916 145.174 210.683 1.00 82.05  ? 368  GLN A CB    1 
ATOM   2831 C  CG    . GLN A 1 367 ? 140.603 144.704 210.080 1.00 82.05  ? 368  GLN A CG    1 
ATOM   2832 C  CD    . GLN A 1 367 ? 139.911 143.657 210.926 1.00 82.05  ? 368  GLN A CD    1 
ATOM   2833 O  OE1   . GLN A 1 367 ? 140.421 143.247 211.968 1.00 82.05  ? 368  GLN A OE1   1 
ATOM   2834 N  NE2   . GLN A 1 367 ? 138.742 143.214 210.478 1.00 82.05  ? 368  GLN A NE2   1 
ATOM   2835 N  N     . ARG A 1 368 ? 145.212 145.139 210.827 1.00 80.82  ? 369  ARG A N     1 
ATOM   2836 C  CA    . ARG A 1 368 ? 146.443 145.684 211.385 1.00 80.82  ? 369  ARG A CA    1 
ATOM   2837 C  C     . ARG A 1 368 ? 147.691 145.298 210.608 1.00 80.82  ? 369  ARG A C     1 
ATOM   2838 O  O     . ARG A 1 368 ? 148.734 145.931 210.795 1.00 80.82  ? 369  ARG A O     1 
ATOM   2839 C  CB    . ARG A 1 368 ? 146.603 145.264 212.856 1.00 80.82  ? 369  ARG A CB    1 
ATOM   2840 C  CG    . ARG A 1 368 ? 145.771 146.103 213.837 1.00 80.82  ? 369  ARG A CG    1 
ATOM   2841 C  CD    . ARG A 1 368 ? 144.326 145.632 213.958 1.00 80.82  ? 369  ARG A CD    1 
ATOM   2842 N  NE    . ARG A 1 368 ? 143.596 146.336 215.006 1.00 80.82  ? 369  ARG A NE    1 
ATOM   2843 C  CZ    . ARG A 1 368 ? 142.271 146.427 215.054 1.00 80.82  ? 369  ARG A CZ    1 
ATOM   2844 N  NH1   . ARG A 1 368 ? 141.681 147.042 216.069 1.00 80.82  ? 369  ARG A NH1   1 
ATOM   2845 N  NH2   . ARG A 1 368 ? 141.533 145.873 214.102 1.00 80.82  ? 369  ARG A NH2   1 
ATOM   2846 N  N     . GLU A 1 369 ? 147.609 144.284 209.754 1.00 80.73  ? 370  GLU A N     1 
ATOM   2847 C  CA    . GLU A 1 369 ? 148.768 143.640 209.155 1.00 80.73  ? 370  GLU A CA    1 
ATOM   2848 C  C     . GLU A 1 369 ? 149.221 144.290 207.853 1.00 80.73  ? 370  GLU A C     1 
ATOM   2849 O  O     . GLU A 1 369 ? 150.322 143.974 207.386 1.00 80.73  ? 370  GLU A O     1 
ATOM   2850 C  CB    . GLU A 1 369 ? 148.466 142.154 208.934 1.00 80.73  ? 370  GLU A CB    1 
ATOM   2851 C  CG    . GLU A 1 369 ? 148.193 141.369 210.226 1.00 80.73  ? 370  GLU A CG    1 
ATOM   2852 C  CD    . GLU A 1 369 ? 146.733 141.366 210.669 1.00 80.73  ? 370  GLU A CD    1 
ATOM   2853 O  OE1   . GLU A 1 369 ? 146.000 142.329 210.363 1.00 80.73  ? 370  GLU A OE1   1 
ATOM   2854 O  OE2   . GLU A 1 369 ? 146.318 140.390 211.327 1.00 80.73  ? 370  GLU A OE2   1 
ATOM   2855 N  N     . GLU A 1 370 ? 148.406 145.192 207.282 1.00 75.86  ? 371  GLU A N     1 
ATOM   2856 C  CA    . GLU A 1 370 ? 148.698 145.949 206.050 1.00 75.86  ? 371  GLU A CA    1 
ATOM   2857 C  C     . GLU A 1 370 ? 149.013 145.012 204.872 1.00 75.86  ? 371  GLU A C     1 
ATOM   2858 O  O     . GLU A 1 370 ? 149.858 145.290 204.018 1.00 75.86  ? 371  GLU A O     1 
ATOM   2859 C  CB    . GLU A 1 370 ? 149.815 146.980 206.304 1.00 75.86  ? 371  GLU A CB    1 
ATOM   2860 C  CG    . GLU A 1 370 ? 149.947 148.152 205.307 1.00 75.86  ? 371  GLU A CG    1 
ATOM   2861 C  CD    . GLU A 1 370 ? 148.723 149.047 205.275 1.00 75.86  ? 371  GLU A CD    1 
ATOM   2862 O  OE1   . GLU A 1 370 ? 148.436 149.616 204.201 1.00 75.86  ? 371  GLU A OE1   1 
ATOM   2863 O  OE2   . GLU A 1 370 ? 148.056 149.194 206.320 1.00 75.86  ? 371  GLU A OE2   1 
ATOM   2864 N  N     . GLN A 1 371 ? 148.355 143.859 204.844 1.00 70.61  ? 372  GLN A N     1 
ATOM   2865 C  CA    . GLN A 1 371 ? 148.535 142.866 203.799 1.00 70.61  ? 372  GLN A CA    1 
ATOM   2866 C  C     . GLN A 1 371 ? 147.152 142.404 203.363 1.00 70.61  ? 372  GLN A C     1 
ATOM   2867 O  O     . GLN A 1 371 ? 146.217 142.361 204.166 1.00 70.61  ? 372  GLN A O     1 
ATOM   2868 C  CB    . GLN A 1 371 ? 149.436 141.699 204.288 1.00 70.61  ? 372  GLN A CB    1 
ATOM   2869 C  CG    . GLN A 1 371 ? 149.764 140.604 203.263 1.00 70.61  ? 372  GLN A CG    1 
ATOM   2870 C  CD    . GLN A 1 371 ? 148.704 139.529 203.144 1.00 70.61  ? 372  GLN A CD    1 
ATOM   2871 O  OE1   . GLN A 1 371 ? 147.808 139.429 203.980 1.00 70.61  ? 372  GLN A OE1   1 
ATOM   2872 N  NE2   . GLN A 1 371 ? 148.774 138.748 202.076 1.00 70.61  ? 372  GLN A NE2   1 
ATOM   2873 N  N     . ALA A 1 372 ? 147.021 142.077 202.083 1.00 68.70  ? 373  ALA A N     1 
ATOM   2874 C  CA    . ALA A 1 372 ? 145.726 141.848 201.462 1.00 68.70  ? 373  ALA A CA    1 
ATOM   2875 C  C     . ALA A 1 372 ? 145.468 140.354 201.332 1.00 68.70  ? 373  ALA A C     1 
ATOM   2876 O  O     . ALA A 1 372 ? 146.381 139.577 201.042 1.00 68.70  ? 373  ALA A O     1 
ATOM   2877 C  CB    . ALA A 1 372 ? 145.657 142.508 200.086 1.00 68.70  ? 373  ALA A CB    1 
ATOM   2878 N  N     . GLU A 1 373 ? 144.222 139.962 201.558 1.00 68.92  ? 374  GLU A N     1 
ATOM   2879 C  CA    . GLU A 1 373 ? 143.779 138.583 201.445 1.00 68.92  ? 374  GLU A CA    1 
ATOM   2880 C  C     . GLU A 1 373 ? 142.406 138.600 200.785 1.00 68.92  ? 374  GLU A C     1 
ATOM   2881 O  O     . GLU A 1 373 ? 141.748 139.646 200.765 1.00 68.92  ? 374  GLU A O     1 
ATOM   2882 C  CB    . GLU A 1 373 ? 143.731 137.966 202.854 1.00 68.92  ? 374  GLU A CB    1 
ATOM   2883 C  CG    . GLU A 1 373 ? 145.077 137.485 203.415 1.00 68.92  ? 374  GLU A CG    1 
ATOM   2884 C  CD    . GLU A 1 373 ? 145.855 136.567 202.483 1.00 68.92  ? 374  GLU A CD    1 
ATOM   2885 O  OE1   . GLU A 1 373 ? 145.255 135.643 201.900 1.00 68.92  ? 374  GLU A OE1   1 
ATOM   2886 O  OE2   . GLU A 1 373 ? 147.081 136.769 202.344 1.00 68.92  ? 374  GLU A OE2   1 
ATOM   2887 N  N     . PRO A 1 374 ? 141.950 137.473 200.218 1.00 65.46  ? 375  PRO A N     1 
ATOM   2888 C  CA    . PRO A 1 374 ? 140.708 137.503 199.422 1.00 65.46  ? 375  PRO A CA    1 
ATOM   2889 C  C     . PRO A 1 374 ? 139.447 137.738 200.245 1.00 65.46  ? 375  PRO A C     1 
ATOM   2890 O  O     . PRO A 1 374 ? 139.182 137.034 201.221 1.00 65.46  ? 375  PRO A O     1 
ATOM   2891 C  CB    . PRO A 1 374 ? 140.704 136.134 198.736 1.00 65.46  ? 375  PRO A CB    1 
ATOM   2892 C  CG    . PRO A 1 374 ? 141.409 135.265 199.675 1.00 65.46  ? 375  PRO A CG    1 
ATOM   2893 C  CD    . PRO A 1 374 ? 142.556 136.125 200.122 1.00 65.46  ? 375  PRO A CD    1 
ATOM   2894 N  N     . ASP A 1 375 ? 138.708 138.787 199.866 1.00 63.87  ? 376  ASP A N     1 
ATOM   2895 C  CA    . ASP A 1 375 ? 137.453 139.146 200.524 1.00 63.87  ? 376  ASP A CA    1 
ATOM   2896 C  C     . ASP A 1 375 ? 136.442 138.011 200.399 1.00 63.87  ? 376  ASP A C     1 
ATOM   2897 O  O     . ASP A 1 375 ? 135.724 137.700 201.356 1.00 63.87  ? 376  ASP A O     1 
ATOM   2898 C  CB    . ASP A 1 375 ? 136.929 140.456 199.915 1.00 63.87  ? 376  ASP A CB    1 
ATOM   2899 C  CG    . ASP A 1 375 ? 135.711 141.053 200.645 1.00 63.87  ? 376  ASP A CG    1 
ATOM   2900 O  OD1   . ASP A 1 375 ? 134.702 140.373 200.925 1.00 63.87  ? 376  ASP A OD1   1 
ATOM   2901 O  OD2   . ASP A 1 375 ? 135.771 142.265 200.941 1.00 63.87  ? 376  ASP A OD2   1 
ATOM   2902 N  N     . GLY A 1 376 ? 136.387 137.372 199.236 1.00 62.28  ? 377  GLY A N     1 
ATOM   2903 C  CA    . GLY A 1 376 ? 135.538 136.214 199.048 1.00 62.28  ? 377  GLY A CA    1 
ATOM   2904 C  C     . GLY A 1 376 ? 136.327 135.137 198.338 1.00 62.28  ? 377  GLY A C     1 
ATOM   2905 O  O     . GLY A 1 376 ? 137.556 135.225 198.293 1.00 62.28  ? 377  GLY A O     1 
ATOM   2906 N  N     . THR A 1 377 ? 135.676 134.115 197.786 1.00 56.09  ? 378  THR A N     1 
ATOM   2907 C  CA    . THR A 1 377 ? 136.433 133.148 196.997 1.00 56.09  ? 378  THR A CA    1 
ATOM   2908 C  C     . THR A 1 377 ? 135.766 132.743 195.687 1.00 56.09  ? 378  THR A C     1 
ATOM   2909 O  O     . THR A 1 377 ? 136.479 132.290 194.785 1.00 56.09  ? 378  THR A O     1 
ATOM   2910 C  CB    . THR A 1 377 ? 136.677 131.885 197.848 1.00 56.09  ? 378  THR A CB    1 
ATOM   2911 O  OG1   . THR A 1 377 ? 136.926 132.264 199.206 1.00 56.09  ? 378  THR A OG1   1 
ATOM   2912 C  CG2   . THR A 1 377 ? 137.904 131.114 197.384 1.00 56.09  ? 378  THR A CG2   1 
ATOM   2913 N  N     . GLU A 1 378 ? 134.448 132.935 195.533 1.00 53.16  ? 379  GLU A N     1 
ATOM   2914 C  CA    . GLU A 1 378 ? 133.675 132.279 194.474 1.00 53.16  ? 379  GLU A CA    1 
ATOM   2915 C  C     . GLU A 1 378 ? 134.119 132.681 193.067 1.00 53.16  ? 379  GLU A C     1 
ATOM   2916 O  O     . GLU A 1 378 ? 134.185 131.834 192.167 1.00 53.16  ? 379  GLU A O     1 
ATOM   2917 C  CB    . GLU A 1 378 ? 132.182 132.567 194.669 1.00 53.16  ? 379  GLU A CB    1 
ATOM   2918 C  CG    . GLU A 1 378 ? 131.217 131.968 193.618 1.00 53.16  ? 379  GLU A CG    1 
ATOM   2919 C  CD    . GLU A 1 378 ? 131.260 130.438 193.446 1.00 53.16  ? 379  GLU A CD    1 
ATOM   2920 O  OE1   . GLU A 1 378 ? 130.648 129.955 192.471 1.00 53.16  ? 379  GLU A OE1   1 
ATOM   2921 O  OE2   . GLU A 1 378 ? 131.809 129.703 194.296 1.00 53.16  ? 379  GLU A OE2   1 
ATOM   2922 N  N     . GLU A 1 379 ? 134.450 133.960 192.862 1.00 50.70  ? 380  GLU A N     1 
ATOM   2923 C  CA    . GLU A 1 379 ? 134.960 134.401 191.565 1.00 50.70  ? 380  GLU A CA    1 
ATOM   2924 C  C     . GLU A 1 379 ? 136.360 133.874 191.279 1.00 50.70  ? 380  GLU A C     1 
ATOM   2925 O  O     . GLU A 1 379 ? 136.695 133.626 190.117 1.00 50.70  ? 380  GLU A O     1 
ATOM   2926 C  CB    . GLU A 1 379 ? 134.922 135.924 191.467 1.00 50.70  ? 380  GLU A CB    1 
ATOM   2927 C  CG    . GLU A 1 379 ? 133.518 136.512 191.532 1.00 50.70  ? 380  GLU A CG    1 
ATOM   2928 C  CD    . GLU A 1 379 ? 133.048 136.811 192.940 1.00 50.70  ? 380  GLU A CD    1 
ATOM   2929 O  OE1   . GLU A 1 379 ? 133.738 136.416 193.901 1.00 50.70  ? 380  GLU A OE1   1 
ATOM   2930 O  OE2   . GLU A 1 379 ? 131.979 137.439 193.083 1.00 50.70  ? 380  GLU A OE2   1 
ATOM   2931 N  N     . ALA A 1 380 ? 137.196 133.722 192.304 1.00 49.30  ? 381  ALA A N     1 
ATOM   2932 C  CA    . ALA A 1 380 ? 138.450 132.999 192.121 1.00 49.30  ? 381  ALA A CA    1 
ATOM   2933 C  C     . ALA A 1 380 ? 138.200 131.525 191.819 1.00 49.30  ? 381  ALA A C     1 
ATOM   2934 O  O     . ALA A 1 380 ? 138.923 130.922 191.018 1.00 49.30  ? 381  ALA A O     1 
ATOM   2935 C  CB    . ALA A 1 380 ? 139.337 133.155 193.353 1.00 49.30  ? 381  ALA A CB    1 
ATOM   2936 N  N     . ASP A 1 381 ? 137.203 130.926 192.480 1.00 48.97  ? 382  ASP A N     1 
ATOM   2937 C  CA    . ASP A 1 381 ? 136.863 129.521 192.253 1.00 48.97  ? 382  ASP A CA    1 
ATOM   2938 C  C     . ASP A 1 381 ? 136.383 129.255 190.831 1.00 48.97  ? 382  ASP A C     1 
ATOM   2939 O  O     . ASP A 1 381 ? 136.677 128.196 190.265 1.00 48.97  ? 382  ASP A O     1 
ATOM   2940 C  CB    . ASP A 1 381 ? 135.802 129.067 193.254 1.00 48.97  ? 382  ASP A CB    1 
ATOM   2941 C  CG    . ASP A 1 381 ? 136.259 129.200 194.687 1.00 48.97  ? 382  ASP A CG    1 
ATOM   2942 O  OD1   . ASP A 1 381 ? 137.446 128.928 194.952 1.00 48.97  ? 382  ASP A OD1   1 
ATOM   2943 O  OD2   . ASP A 1 381 ? 135.436 129.577 195.547 1.00 48.97  ? 382  ASP A OD2   1 
ATOM   2944 N  N     . LYS A 1 382 ? 135.606 130.174 190.258 1.00 43.27  ? 383  LYS A N     1 
ATOM   2945 C  CA    . LYS A 1 382 ? 135.243 130.066 188.847 1.00 43.27  ? 383  LYS A CA    1 
ATOM   2946 C  C     . LYS A 1 382 ? 136.462 130.141 187.932 1.00 43.27  ? 383  LYS A C     1 
ATOM   2947 O  O     . LYS A 1 382 ? 136.617 129.310 187.029 1.00 43.27  ? 383  LYS A O     1 
ATOM   2948 C  CB    . LYS A 1 382 ? 134.225 131.145 188.481 1.00 43.27  ? 383  LYS A CB    1 
ATOM   2949 C  CG    . LYS A 1 382 ? 132.863 130.934 189.107 1.00 43.27  ? 383  LYS A CG    1 
ATOM   2950 C  CD    . LYS A 1 382 ? 131.960 132.131 188.907 1.00 43.27  ? 383  LYS A CD    1 
ATOM   2951 C  CE    . LYS A 1 382 ? 130.813 132.118 189.896 1.00 43.27  ? 383  LYS A CE    1 
ATOM   2952 N  NZ    . LYS A 1 382 ? 129.932 133.306 189.748 1.00 43.27  ? 383  LYS A NZ    1 
ATOM   2953 N  N     . SER A 1 383 ? 137.307 131.161 188.125 1.00 43.64  ? 384  SER A N     1 
ATOM   2954 C  CA    . SER A 1 383 ? 138.501 131.352 187.299 1.00 43.64  ? 384  SER A CA    1 
ATOM   2955 C  C     . SER A 1 383 ? 139.452 130.163 187.361 1.00 43.64  ? 384  SER A C     1 
ATOM   2956 O  O     . SER A 1 383 ? 139.964 129.716 186.330 1.00 43.64  ? 384  SER A O     1 
ATOM   2957 C  CB    . SER A 1 383 ? 139.226 132.628 187.715 1.00 43.64  ? 384  SER A CB    1 
ATOM   2958 O  OG    . SER A 1 383 ? 138.366 133.744 187.625 1.00 43.64  ? 384  SER A OG    1 
ATOM   2959 N  N     . ALA A 1 384 ? 139.725 129.661 188.566 1.00 42.54  ? 385  ALA A N     1 
ATOM   2960 C  CA    . ALA A 1 384 ? 140.625 128.522 188.718 1.00 42.54  ? 385  ALA A CA    1 
ATOM   2961 C  C     . ALA A 1 384 ? 140.082 127.250 188.080 1.00 42.54  ? 385  ALA A C     1 
ATOM   2962 O  O     . ALA A 1 384 ? 140.865 126.384 187.678 1.00 42.54  ? 385  ALA A O     1 
ATOM   2963 C  CB    . ALA A 1 384 ? 140.927 128.281 190.191 1.00 42.54  ? 385  ALA A CB    1 
ATOM   2964 N  N     . TYR A 1 385 ? 138.759 127.093 188.015 1.00 42.19  ? 386  TYR A N     1 
ATOM   2965 C  CA    . TYR A 1 385 ? 138.204 125.957 187.285 1.00 42.19  ? 386  TYR A CA    1 
ATOM   2966 C  C     . TYR A 1 385 ? 138.425 126.091 185.784 1.00 42.19  ? 386  TYR A C     1 
ATOM   2967 O  O     . TYR A 1 385 ? 138.775 125.112 185.115 1.00 42.19  ? 386  TYR A O     1 
ATOM   2968 C  CB    . TYR A 1 385 ? 136.718 125.790 187.584 1.00 42.19  ? 386  TYR A CB    1 
ATOM   2969 C  CG    . TYR A 1 385 ? 136.102 124.681 186.769 1.00 42.19  ? 386  TYR A CG    1 
ATOM   2970 C  CD1   . TYR A 1 385 ? 136.482 123.362 186.968 1.00 42.19  ? 386  TYR A CD1   1 
ATOM   2971 C  CD2   . TYR A 1 385 ? 135.150 124.950 185.797 1.00 42.19  ? 386  TYR A CD2   1 
ATOM   2972 C  CE1   . TYR A 1 385 ? 135.929 122.338 186.223 1.00 42.19  ? 386  TYR A CE1   1 
ATOM   2973 C  CE2   . TYR A 1 385 ? 134.589 123.931 185.045 1.00 42.19  ? 386  TYR A CE2   1 
ATOM   2974 C  CZ    . TYR A 1 385 ? 134.984 122.629 185.264 1.00 42.19  ? 386  TYR A CZ    1 
ATOM   2975 O  OH    . TYR A 1 385 ? 134.433 121.612 184.522 1.00 42.19  ? 386  TYR A OH    1 
ATOM   2976 N  N     . LEU A 1 386 ? 138.191 127.286 185.234 1.00 37.56  ? 387  LEU A N     1 
ATOM   2977 C  CA    . LEU A 1 386 ? 138.370 127.502 183.801 1.00 37.56  ? 387  LEU A CA    1 
ATOM   2978 C  C     . LEU A 1 386 ? 139.838 127.430 183.402 1.00 37.56  ? 387  LEU A C     1 
ATOM   2979 O  O     . LEU A 1 386 ? 140.193 126.772 182.419 1.00 37.56  ? 387  LEU A O     1 
ATOM   2980 C  CB    . LEU A 1 386 ? 137.774 128.850 183.405 1.00 37.56  ? 387  LEU A CB    1 
ATOM   2981 C  CG    . LEU A 1 386 ? 136.262 128.950 183.570 1.00 37.56  ? 387  LEU A CG    1 
ATOM   2982 C  CD1   . LEU A 1 386 ? 135.787 130.357 183.303 1.00 37.56  ? 387  LEU A CD1   1 
ATOM   2983 C  CD2   . LEU A 1 386 ? 135.580 127.978 182.641 1.00 37.56  ? 387  LEU A CD2   1 
ATOM   2984 N  N     . MET A 1 387 ? 140.709 128.080 184.166 1.00 38.65  ? 388  MET A N     1 
ATOM   2985 C  CA    . MET A 1 387 ? 142.144 128.035 183.923 1.00 38.65  ? 388  MET A CA    1 
ATOM   2986 C  C     . MET A 1 387 ? 142.795 126.738 184.384 1.00 38.65  ? 388  MET A C     1 
ATOM   2987 O  O     . MET A 1 387 ? 143.987 126.545 184.127 1.00 38.65  ? 388  MET A O     1 
ATOM   2988 C  CB    . MET A 1 387 ? 142.820 129.219 184.615 1.00 38.65  ? 388  MET A CB    1 
ATOM   2989 C  CG    . MET A 1 387 ? 142.469 130.567 184.023 1.00 38.65  ? 388  MET A CG    1 
ATOM   2990 S  SD    . MET A 1 387 ? 142.941 131.920 185.110 1.00 38.65  ? 388  MET A SD    1 
ATOM   2991 C  CE    . MET A 1 387 ? 143.017 133.277 183.951 1.00 38.65  ? 388  MET A CE    1 
ATOM   2992 N  N     . GLY A 1 388 ? 142.050 125.845 185.029 1.00 39.96  ? 389  GLY A N     1 
ATOM   2993 C  CA    . GLY A 1 388 ? 142.591 124.591 185.517 1.00 39.96  ? 389  GLY A CA    1 
ATOM   2994 C  C     . GLY A 1 388 ? 143.629 124.763 186.607 1.00 39.96  ? 389  GLY A C     1 
ATOM   2995 O  O     . GLY A 1 388 ? 144.780 124.352 186.447 1.00 39.96  ? 389  GLY A O     1 
ATOM   2996 N  N     . LEU A 1 389 ? 143.235 125.381 187.719 1.00 42.96  ? 390  LEU A N     1 
ATOM   2997 C  CA    . LEU A 1 389 ? 144.153 125.711 188.797 1.00 42.96  ? 390  LEU A CA    1 
ATOM   2998 C  C     . LEU A 1 389 ? 143.565 125.271 190.130 1.00 42.96  ? 390  LEU A C     1 
ATOM   2999 O  O     . LEU A 1 389 ? 142.361 125.040 190.260 1.00 42.96  ? 390  LEU A O     1 
ATOM   3000 C  CB    . LEU A 1 389 ? 144.454 127.214 188.848 1.00 42.96  ? 390  LEU A CB    1 
ATOM   3001 C  CG    . LEU A 1 389 ? 144.940 127.906 187.578 1.00 42.96  ? 390  LEU A CG    1 
ATOM   3002 C  CD1   . LEU A 1 389 ? 145.041 129.400 187.796 1.00 42.96  ? 390  LEU A CD1   1 
ATOM   3003 C  CD2   . LEU A 1 389 ? 146.274 127.337 187.161 1.00 42.96  ? 390  LEU A CD2   1 
ATOM   3004 N  N     . ASN A 1 390 ? 144.440 125.158 191.125 1.00 51.08  ? 391  ASN A N     1 
ATOM   3005 C  CA    . ASN A 1 390 ? 144.030 125.049 192.521 1.00 51.08  ? 391  ASN A CA    1 
ATOM   3006 C  C     . ASN A 1 390 ? 143.714 126.438 193.063 1.00 51.08  ? 391  ASN A C     1 
ATOM   3007 O  O     . ASN A 1 390 ? 144.592 127.307 193.088 1.00 51.08  ? 391  ASN A O     1 
ATOM   3008 C  CB    . ASN A 1 390 ? 145.116 124.372 193.354 1.00 51.08  ? 391  ASN A CB    1 
ATOM   3009 C  CG    . ASN A 1 390 ? 144.695 124.149 194.802 1.00 51.08  ? 391  ASN A CG    1 
ATOM   3010 O  OD1   . ASN A 1 390 ? 143.509 124.174 195.132 1.00 51.08  ? 391  ASN A OD1   1 
ATOM   3011 N  ND2   . ASN A 1 390 ? 145.669 123.910 195.668 1.00 51.08  ? 391  ASN A ND2   1 
ATOM   3012 N  N     . SER A 1 391 ? 142.443 126.654 193.428 1.00 53.86  ? 392  SER A N     1 
ATOM   3013 C  CA    . SER A 1 391 ? 141.992 127.938 193.964 1.00 53.86  ? 392  SER A CA    1 
ATOM   3014 C  C     . SER A 1 391 ? 142.770 128.352 195.209 1.00 53.86  ? 392  SER A C     1 
ATOM   3015 O  O     . SER A 1 391 ? 143.044 129.541 195.410 1.00 53.86  ? 392  SER A O     1 
ATOM   3016 C  CB    . SER A 1 391 ? 140.505 127.862 194.307 1.00 53.86  ? 392  SER A CB    1 
ATOM   3017 O  OG    . SER A 1 391 ? 139.680 128.001 193.170 1.00 53.86  ? 392  SER A OG    1 
ATOM   3018 N  N     . ALA A 1 392 ? 143.102 127.390 196.073 1.00 56.95  ? 393  ALA A N     1 
ATOM   3019 C  CA    . ALA A 1 392 ? 143.857 127.698 197.283 1.00 56.95  ? 393  ALA A CA    1 
ATOM   3020 C  C     . ALA A 1 392 ? 145.282 128.143 196.974 1.00 56.95  ? 393  ALA A C     1 
ATOM   3021 O  O     . ALA A 1 392 ? 145.810 129.040 197.638 1.00 56.95  ? 393  ALA A O     1 
ATOM   3022 C  CB    . ALA A 1 392 ? 143.869 126.486 198.213 1.00 56.95  ? 393  ALA A CB    1 
ATOM   3023 N  N     . ASP A 1 393 ? 145.918 127.537 195.970 1.00 58.18  ? 394  ASP A N     1 
ATOM   3024 C  CA    . ASP A 1 393 ? 147.250 127.971 195.559 1.00 58.18  ? 394  ASP A CA    1 
ATOM   3025 C  C     . ASP A 1 393 ? 147.237 129.252 194.737 1.00 58.18  ? 394  ASP A C     1 
ATOM   3026 O  O     . ASP A 1 393 ? 148.220 130.002 194.769 1.00 58.18  ? 394  ASP A O     1 
ATOM   3027 C  CB    . ASP A 1 393 ? 147.949 126.864 194.771 1.00 58.18  ? 394  ASP A CB    1 
ATOM   3028 C  CG    . ASP A 1 393 ? 148.328 125.684 195.638 1.00 58.18  ? 394  ASP A CG    1 
ATOM   3029 O  OD1   . ASP A 1 393 ? 148.422 125.858 196.871 1.00 58.18  ? 394  ASP A OD1   1 
ATOM   3030 O  OD2   . ASP A 1 393 ? 148.533 124.582 195.090 1.00 58.18  ? 394  ASP A OD2   1 
ATOM   3031 N  N     . LEU A 1 394 ? 146.174 129.487 193.963 1.00 55.54  ? 395  LEU A N     1 
ATOM   3032 C  CA    . LEU A 1 394 ? 146.051 130.718 193.187 1.00 55.54  ? 395  LEU A CA    1 
ATOM   3033 C  C     . LEU A 1 394 ? 146.033 131.952 194.082 1.00 55.54  ? 395  LEU A C     1 
ATOM   3034 O  O     . LEU A 1 394 ? 146.867 132.850 193.932 1.00 55.54  ? 395  LEU A O     1 
ATOM   3035 C  CB    . LEU A 1 394 ? 144.791 130.661 192.325 1.00 55.54  ? 395  LEU A CB    1 
ATOM   3036 C  CG    . LEU A 1 394 ? 144.458 131.930 191.545 1.00 55.54  ? 395  LEU A CG    1 
ATOM   3037 C  CD1   . LEU A 1 394 ? 145.550 132.231 190.543 1.00 55.54  ? 395  LEU A CD1   1 
ATOM   3038 C  CD2   . LEU A 1 394 ? 143.125 131.786 190.847 1.00 55.54  ? 395  LEU A CD2   1 
ATOM   3039 N  N     . LEU A 1 395 ? 145.082 132.011 195.016 1.00 58.59  ? 396  LEU A N     1 
ATOM   3040 C  CA    . LEU A 1 395 ? 144.957 133.164 195.907 1.00 58.59  ? 396  LEU A CA    1 
ATOM   3041 C  C     . LEU A 1 395 ? 146.154 133.311 196.843 1.00 58.59  ? 396  LEU A C     1 
ATOM   3042 O  O     . LEU A 1 395 ? 146.520 134.435 197.206 1.00 58.59  ? 396  LEU A O     1 
ATOM   3043 C  CB    . LEU A 1 395 ? 143.657 133.069 196.701 1.00 58.59  ? 396  LEU A CB    1 
ATOM   3044 C  CG    . LEU A 1 395 ? 142.387 133.265 195.876 1.00 58.59  ? 396  LEU A CG    1 
ATOM   3045 C  CD1   . LEU A 1 395 ? 141.190 132.774 196.647 1.00 58.59  ? 396  LEU A CD1   1 
ATOM   3046 C  CD2   . LEU A 1 395 ? 142.214 134.726 195.515 1.00 58.59  ? 396  LEU A CD2   1 
ATOM   3047 N  N     . LYS A 1 396 ? 146.734 132.192 197.291 1.00 61.52  ? 397  LYS A N     1 
ATOM   3048 C  CA    . LYS A 1 396 ? 147.966 132.250 198.077 1.00 61.52  ? 397  LYS A CA    1 
ATOM   3049 C  C     . LYS A 1 396 ? 149.110 132.867 197.284 1.00 61.52  ? 397  LYS A C     1 
ATOM   3050 O  O     . LYS A 1 396 ? 149.752 133.817 197.743 1.00 61.52  ? 397  LYS A O     1 
ATOM   3051 C  CB    . LYS A 1 396 ? 148.359 130.857 198.564 1.00 61.52  ? 397  LYS A CB    1 
ATOM   3052 C  CG    . LYS A 1 396 ? 149.650 130.843 199.364 1.00 61.52  ? 397  LYS A CG    1 
ATOM   3053 C  CD    . LYS A 1 396 ? 150.256 129.454 199.426 1.00 61.52  ? 397  LYS A CD    1 
ATOM   3054 C  CE    . LYS A 1 396 ? 149.331 128.470 200.119 1.00 61.52  ? 397  LYS A CE    1 
ATOM   3055 N  NZ    . LYS A 1 396 ? 149.823 127.069 199.993 1.00 61.52  ? 397  LYS A NZ    1 
ATOM   3056 N  N     . GLY A 1 397 ? 149.392 132.320 196.098 1.00 60.94  ? 398  GLY A N     1 
ATOM   3057 C  CA    . GLY A 1 397 ? 150.494 132.817 195.289 1.00 60.94  ? 398  GLY A CA    1 
ATOM   3058 C  C     . GLY A 1 397 ? 150.295 134.233 194.788 1.00 60.94  ? 398  GLY A C     1 
ATOM   3059 O  O     . GLY A 1 397 ? 151.268 134.960 194.569 1.00 60.94  ? 398  GLY A O     1 
ATOM   3060 N  N     . LEU A 1 398 ? 149.041 134.638 194.590 1.00 58.05  ? 399  LEU A N     1 
ATOM   3061 C  CA    . LEU A 1 398 ? 148.748 136.002 194.169 1.00 58.05  ? 399  LEU A CA    1 
ATOM   3062 C  C     . LEU A 1 398 ? 149.007 136.998 195.291 1.00 58.05  ? 399  LEU A C     1 
ATOM   3063 O  O     . LEU A 1 398 ? 149.557 138.078 195.052 1.00 58.05  ? 399  LEU A O     1 
ATOM   3064 C  CB    . LEU A 1 398 ? 147.306 136.081 193.680 1.00 58.05  ? 399  LEU A CB    1 
ATOM   3065 C  CG    . LEU A 1 398 ? 146.728 137.412 193.237 1.00 58.05  ? 399  LEU A CG    1 
ATOM   3066 C  CD1   . LEU A 1 398 ? 147.548 137.976 192.109 1.00 58.05  ? 399  LEU A CD1   1 
ATOM   3067 C  CD2   . LEU A 1 398 ? 145.323 137.153 192.769 1.00 58.05  ? 399  LEU A CD2   1 
ATOM   3068 N  N     . CYS A 1 399 ? 148.619 136.657 196.519 1.00 62.87  ? 400  CYS A N     1 
ATOM   3069 C  CA    . CYS A 1 399 ? 148.850 137.523 197.668 1.00 62.87  ? 400  CYS A CA    1 
ATOM   3070 C  C     . CYS A 1 399 ? 150.223 137.338 198.300 1.00 62.87  ? 400  CYS A C     1 
ATOM   3071 O  O     . CYS A 1 399 ? 150.648 138.196 199.079 1.00 62.87  ? 400  CYS A O     1 
ATOM   3072 C  CB    . CYS A 1 399 ? 147.769 137.288 198.724 1.00 62.87  ? 400  CYS A CB    1 
ATOM   3073 S  SG    . CYS A 1 399 ? 146.157 137.950 198.260 1.00 62.87  ? 400  CYS A SG    1 
ATOM   3074 N  N     . HIS A 1 400 ? 150.917 136.242 198.002 1.00 65.12  ? 401  HIS A N     1 
ATOM   3075 C  CA    . HIS A 1 400 ? 152.236 135.948 198.574 1.00 65.12  ? 401  HIS A CA    1 
ATOM   3076 C  C     . HIS A 1 400 ? 153.183 135.441 197.491 1.00 65.12  ? 401  HIS A C     1 
ATOM   3077 O  O     . HIS A 1 400 ? 153.521 134.253 197.456 1.00 65.12  ? 401  HIS A O     1 
ATOM   3078 C  CB    . HIS A 1 400 ? 152.134 134.934 199.714 1.00 65.12  ? 401  HIS A CB    1 
ATOM   3079 C  CG    . HIS A 1 400 ? 151.243 135.362 200.836 1.00 65.12  ? 401  HIS A CG    1 
ATOM   3080 N  ND1   . HIS A 1 400 ? 151.693 136.128 201.888 1.00 65.12  ? 401  HIS A ND1   1 
ATOM   3081 C  CD2   . HIS A 1 400 ? 149.931 135.127 201.075 1.00 65.12  ? 401  HIS A CD2   1 
ATOM   3082 C  CE1   . HIS A 1 400 ? 150.699 136.343 202.730 1.00 65.12  ? 401  HIS A CE1   1 
ATOM   3083 N  NE2   . HIS A 1 400 ? 149.617 135.751 202.258 1.00 65.12  ? 401  HIS A NE2   1 
ATOM   3084 N  N     . PRO A 1 401 ? 153.589 136.307 196.552 1.00 72.16  ? 402  PRO A N     1 
ATOM   3085 C  CA    . PRO A 1 401 ? 154.577 135.886 195.550 1.00 72.16  ? 402  PRO A CA    1 
ATOM   3086 C  C     . PRO A 1 401 ? 155.921 135.554 196.180 1.00 72.16  ? 402  PRO A C     1 
ATOM   3087 O  O     . PRO A 1 401 ? 156.395 136.244 197.083 1.00 72.16  ? 402  PRO A O     1 
ATOM   3088 C  CB    . PRO A 1 401 ? 154.694 137.102 194.628 1.00 72.16  ? 402  PRO A CB    1 
ATOM   3089 C  CG    . PRO A 1 401 ? 154.303 138.243 195.465 1.00 72.16  ? 402  PRO A CG    1 
ATOM   3090 C  CD    . PRO A 1 401 ? 153.278 137.743 196.417 1.00 72.16  ? 402  PRO A CD    1 
ATOM   3091 N  N     . ARG A 1 402 ? 156.527 134.476 195.700 1.00 87.27  ? 403  ARG A N     1 
ATOM   3092 C  CA    . ARG A 1 402 ? 157.895 134.132 196.055 1.00 87.27  ? 403  ARG A CA    1 
ATOM   3093 C  C     . ARG A 1 402 ? 158.800 134.618 194.933 1.00 87.27  ? 403  ARG A C     1 
ATOM   3094 O  O     . ARG A 1 402 ? 158.678 134.163 193.791 1.00 87.27  ? 403  ARG A O     1 
ATOM   3095 C  CB    . ARG A 1 402 ? 158.021 132.620 196.254 1.00 87.27  ? 403  ARG A CB    1 
ATOM   3096 C  CG    . ARG A 1 402 ? 157.860 132.154 197.699 1.00 87.27  ? 403  ARG A CG    1 
ATOM   3097 C  CD    . ARG A 1 402 ? 157.990 130.637 197.834 1.00 87.27  ? 403  ARG A CD    1 
ATOM   3098 N  NE    . ARG A 1 402 ? 159.351 130.147 197.642 1.00 87.27  ? 403  ARG A NE    1 
ATOM   3099 C  CZ    . ARG A 1 402 ? 160.085 129.561 198.584 1.00 87.27  ? 403  ARG A CZ    1 
ATOM   3100 N  NH1   . ARG A 1 402 ? 161.326 129.181 198.316 1.00 87.27  ? 403  ARG A NH1   1 
ATOM   3101 N  NH2   . ARG A 1 402 ? 159.586 129.371 199.797 1.00 87.27  ? 403  ARG A NH2   1 
ATOM   3102 N  N     . VAL A 1 403 ? 159.709 135.533 195.259 1.00 97.01  ? 404  VAL A N     1 
ATOM   3103 C  CA    . VAL A 1 403 ? 160.665 136.085 194.305 1.00 97.01  ? 404  VAL A CA    1 
ATOM   3104 C  C     . VAL A 1 403 ? 162.055 135.563 194.656 1.00 97.01  ? 404  VAL A C     1 
ATOM   3105 O  O     . VAL A 1 403 ? 162.442 135.528 195.832 1.00 97.01  ? 404  VAL A O     1 
ATOM   3106 C  CB    . VAL A 1 403 ? 160.585 137.626 194.239 1.00 97.01  ? 404  VAL A CB    1 
ATOM   3107 C  CG1   . VAL A 1 403 ? 160.892 138.301 195.569 1.00 97.01  ? 404  VAL A CG1   1 
ATOM   3108 C  CG2   . VAL A 1 403 ? 161.500 138.169 193.148 1.00 97.01  ? 404  VAL A CG2   1 
ATOM   3109 N  N     . LYS A 1 404 ? 162.767 135.071 193.647 1.00 101.68 ? 405  LYS A N     1 
ATOM   3110 C  CA    . LYS A 1 404 ? 164.067 134.459 193.871 1.00 101.68 ? 405  LYS A CA    1 
ATOM   3111 C  C     . LYS A 1 404 ? 165.163 135.504 194.058 1.00 101.68 ? 405  LYS A C     1 
ATOM   3112 O  O     . LYS A 1 404 ? 165.276 136.457 193.280 1.00 101.68 ? 405  LYS A O     1 
ATOM   3113 C  CB    . LYS A 1 404 ? 164.403 133.502 192.720 1.00 101.68 ? 405  LYS A CB    1 
ATOM   3114 C  CG    . LYS A 1 404 ? 164.423 134.071 191.307 1.00 101.68 ? 405  LYS A CG    1 
ATOM   3115 C  CD    . LYS A 1 404 ? 164.751 132.971 190.307 1.00 101.68 ? 405  LYS A CD    1 
ATOM   3116 C  CE    . LYS A 1 404 ? 164.838 133.499 188.888 1.00 101.68 ? 405  LYS A CE    1 
ATOM   3117 N  NZ    . LYS A 1 404 ? 164.395 132.476 187.900 1.00 101.68 ? 405  LYS A NZ    1 
ATOM   3118 N  N     . VAL A 1 405 ? 165.935 135.352 195.138 1.00 105.15 ? 406  VAL A N     1 
ATOM   3119 C  CA    . VAL A 1 405 ? 167.050 136.244 195.448 1.00 105.15 ? 406  VAL A CA    1 
ATOM   3120 C  C     . VAL A 1 405 ? 168.209 135.320 195.802 1.00 105.15 ? 406  VAL A C     1 
ATOM   3121 O  O     . VAL A 1 405 ? 168.562 135.153 196.975 1.00 105.15 ? 406  VAL A O     1 
ATOM   3122 C  CB    . VAL A 1 405 ? 166.754 137.237 196.599 1.00 105.15 ? 406  VAL A CB    1 
ATOM   3123 C  CG1   . VAL A 1 405 ? 167.863 138.293 196.704 1.00 105.15 ? 406  VAL A CG1   1 
ATOM   3124 C  CG2   . VAL A 1 405 ? 165.404 137.938 196.446 1.00 105.15 ? 406  VAL A CG2   1 
ATOM   3125 N  N     . GLY A 1 406 ? 168.776 134.678 194.783 1.00 104.32 ? 407  GLY A N     1 
ATOM   3126 C  CA    . GLY A 1 406 ? 169.866 133.738 194.953 1.00 104.32 ? 407  GLY A CA    1 
ATOM   3127 C  C     . GLY A 1 406 ? 169.510 132.466 195.697 1.00 104.32 ? 407  GLY A C     1 
ATOM   3128 O  O     . GLY A 1 406 ? 168.639 131.699 195.274 1.00 104.32 ? 407  GLY A O     1 
ATOM   3129 N  N     . ASN A 1 407 ? 170.200 132.241 196.818 1.00 108.47 ? 408  ASN A N     1 
ATOM   3130 C  CA    . ASN A 1 407 ? 170.015 131.044 197.633 1.00 108.47 ? 408  ASN A CA    1 
ATOM   3131 C  C     . ASN A 1 407 ? 168.677 131.006 198.363 1.00 108.47 ? 408  ASN A C     1 
ATOM   3132 O  O     . ASN A 1 407 ? 168.219 129.919 198.728 1.00 108.47 ? 408  ASN A O     1 
ATOM   3133 C  CB    . ASN A 1 407 ? 171.155 130.924 198.644 1.00 108.47 ? 408  ASN A CB    1 
ATOM   3134 C  CG    . ASN A 1 407 ? 172.501 130.722 197.981 1.00 108.47 ? 408  ASN A CG    1 
ATOM   3135 O  OD1   . ASN A 1 407 ? 173.449 131.465 198.232 1.00 108.47 ? 408  ASN A OD1   1 
ATOM   3136 N  ND2   . ASN A 1 407 ? 172.590 129.713 197.123 1.00 108.47 ? 408  ASN A ND2   1 
ATOM   3137 N  N     . GLU A 1 408 ? 168.041 132.154 198.582 1.00 105.63 ? 409  GLU A N     1 
ATOM   3138 C  CA    . GLU A 1 408 ? 166.789 132.224 199.320 1.00 105.63 ? 409  GLU A CA    1 
ATOM   3139 C  C     . GLU A 1 408 ? 165.736 132.920 198.467 1.00 105.63 ? 409  GLU A C     1 
ATOM   3140 O  O     . GLU A 1 408 ? 166.056 133.783 197.645 1.00 105.63 ? 409  GLU A O     1 
ATOM   3141 C  CB    . GLU A 1 408 ? 167.047 132.950 200.668 1.00 105.63 ? 409  GLU A CB    1 
ATOM   3142 C  CG    . GLU A 1 408 ? 165.862 133.246 201.576 1.00 105.63 ? 409  GLU A CG    1 
ATOM   3143 C  CD    . GLU A 1 408 ? 165.300 134.637 201.358 1.00 105.63 ? 409  GLU A CD    1 
ATOM   3144 O  OE1   . GLU A 1 408 ? 164.342 135.012 202.067 1.00 105.63 ? 409  GLU A OE1   1 
ATOM   3145 O  OE2   . GLU A 1 408 ? 165.814 135.356 200.475 1.00 105.63 ? 409  GLU A OE2   1 
ATOM   3146 N  N     . TYR A 1 409 ? 164.471 132.544 198.670 1.00 100.00 ? 410  TYR A N     1 
ATOM   3147 C  CA    . TYR A 1 409 ? 163.341 133.304 198.148 1.00 100.00 ? 410  TYR A CA    1 
ATOM   3148 C  C     . TYR A 1 409 ? 162.735 134.111 199.291 1.00 100.00 ? 410  TYR A C     1 
ATOM   3149 O  O     . TYR A 1 409 ? 162.496 133.570 200.375 1.00 100.00 ? 410  TYR A O     1 
ATOM   3150 C  CB    . TYR A 1 409 ? 162.259 132.392 197.549 1.00 100.00 ? 410  TYR A CB    1 
ATOM   3151 C  CG    . TYR A 1 409 ? 162.566 131.604 196.267 1.00 100.00 ? 410  TYR A CG    1 
ATOM   3152 C  CD1   . TYR A 1 409 ? 163.868 131.343 195.843 1.00 100.00 ? 410  TYR A CD1   1 
ATOM   3153 C  CD2   . TYR A 1 409 ? 161.525 131.131 195.475 1.00 100.00 ? 410  TYR A CD2   1 
ATOM   3154 C  CE1   . TYR A 1 409 ? 164.118 130.617 194.691 1.00 100.00 ? 410  TYR A CE1   1 
ATOM   3155 C  CE2   . TYR A 1 409 ? 161.765 130.412 194.318 1.00 100.00 ? 410  TYR A CE2   1 
ATOM   3156 C  CZ    . TYR A 1 409 ? 163.062 130.167 193.927 1.00 100.00 ? 410  TYR A CZ    1 
ATOM   3157 O  OH    . TYR A 1 409 ? 163.301 129.446 192.780 1.00 100.00 ? 410  TYR A OH    1 
ATOM   3158 N  N     . VAL A 1 410 ? 162.453 135.384 199.039 1.00 96.84  ? 411  VAL A N     1 
ATOM   3159 C  CA    . VAL A 1 410 ? 161.788 136.252 200.006 1.00 96.84  ? 411  VAL A CA    1 
ATOM   3160 C  C     . VAL A 1 410 ? 160.329 136.430 199.596 1.00 96.84  ? 411  VAL A C     1 
ATOM   3161 O  O     . VAL A 1 410 ? 160.005 136.509 198.403 1.00 96.84  ? 411  VAL A O     1 
ATOM   3162 C  CB    . VAL A 1 410 ? 162.541 137.596 200.160 1.00 96.84  ? 411  VAL A CB    1 
ATOM   3163 C  CG1   . VAL A 1 410 ? 162.570 138.402 198.870 1.00 96.84  ? 411  VAL A CG1   1 
ATOM   3164 C  CG2   . VAL A 1 410 ? 161.987 138.428 201.319 1.00 96.84  ? 411  VAL A CG2   1 
ATOM   3165 N  N     . THR A 1 411 ? 159.435 136.428 200.584 1.00 88.92  ? 412  THR A N     1 
ATOM   3166 C  CA    . THR A 1 411 ? 158.004 136.580 200.357 1.00 88.92  ? 412  THR A CA    1 
ATOM   3167 C  C     . THR A 1 411 ? 157.587 138.015 200.651 1.00 88.92  ? 412  THR A C     1 
ATOM   3168 O  O     . THR A 1 411 ? 157.923 138.561 201.706 1.00 88.92  ? 412  THR A O     1 
ATOM   3169 C  CB    . THR A 1 411 ? 157.209 135.616 201.236 1.00 88.92  ? 412  THR A CB    1 
ATOM   3170 O  OG1   . THR A 1 411 ? 157.652 135.734 202.593 1.00 88.92  ? 412  THR A OG1   1 
ATOM   3171 C  CG2   . THR A 1 411 ? 157.412 134.186 200.774 1.00 88.92  ? 412  THR A CG2   1 
ATOM   3172 N  N     . LYS A 1 412 ? 156.864 138.618 199.713 1.00 79.04  ? 413  LYS A N     1 
ATOM   3173 C  CA    . LYS A 1 412 ? 156.510 140.030 199.756 1.00 79.04  ? 413  LYS A CA    1 
ATOM   3174 C  C     . LYS A 1 412 ? 155.044 140.187 200.135 1.00 79.04  ? 413  LYS A C     1 
ATOM   3175 O  O     . LYS A 1 412 ? 154.181 139.498 199.585 1.00 79.04  ? 413  LYS A O     1 
ATOM   3176 C  CB    . LYS A 1 412 ? 156.777 140.688 198.402 1.00 79.04  ? 413  LYS A CB    1 
ATOM   3177 C  CG    . LYS A 1 412 ? 158.222 140.578 197.941 1.00 79.04  ? 413  LYS A CG    1 
ATOM   3178 C  CD    . LYS A 1 412 ? 158.446 141.311 196.630 1.00 79.04  ? 413  LYS A CD    1 
ATOM   3179 C  CE    . LYS A 1 412 ? 157.707 140.630 195.491 1.00 79.04  ? 413  LYS A CE    1 
ATOM   3180 N  NZ    . LYS A 1 412 ? 157.826 141.392 194.219 1.00 79.04  ? 413  LYS A NZ    1 
ATOM   3181 N  N     . GLY A 1 413 ? 154.768 141.091 201.070 1.00 71.88  ? 414  GLY A N     1 
ATOM   3182 C  CA    . GLY A 1 413 ? 153.408 141.362 201.497 1.00 71.88  ? 414  GLY A CA    1 
ATOM   3183 C  C     . GLY A 1 413 ? 152.676 142.343 200.606 1.00 71.88  ? 414  GLY A C     1 
ATOM   3184 O  O     . GLY A 1 413 ? 152.951 143.545 200.641 1.00 71.88  ? 414  GLY A O     1 
ATOM   3185 N  N     . GLN A 1 414 ? 151.745 141.847 199.797 1.00 65.54  ? 415  GLN A N     1 
ATOM   3186 C  CA    . GLN A 1 414 ? 151.041 142.684 198.834 1.00 65.54  ? 415  GLN A CA    1 
ATOM   3187 C  C     . GLN A 1 414 ? 149.933 143.473 199.521 1.00 65.54  ? 415  GLN A C     1 
ATOM   3188 O  O     . GLN A 1 414 ? 149.000 142.888 200.081 1.00 65.54  ? 415  GLN A O     1 
ATOM   3189 C  CB    . GLN A 1 414 ? 150.459 141.825 197.715 1.00 65.54  ? 415  GLN A CB    1 
ATOM   3190 C  CG    . GLN A 1 414 ? 151.438 140.881 197.014 1.00 65.54  ? 415  GLN A CG    1 
ATOM   3191 C  CD    . GLN A 1 414 ? 152.604 141.576 196.327 1.00 65.54  ? 415  GLN A CD    1 
ATOM   3192 O  OE1   . GLN A 1 414 ? 153.586 141.969 196.961 1.00 65.54  ? 415  GLN A OE1   1 
ATOM   3193 N  NE2   . GLN A 1 414 ? 152.500 141.723 195.012 1.00 65.54  ? 415  GLN A NE2   1 
ATOM   3194 N  N     . ASN A 1 415 ? 150.029 144.798 199.470 1.00 60.75  ? 416  ASN A N     1 
ATOM   3195 C  CA    . ASN A 1 415 ? 148.913 145.648 199.850 1.00 60.75  ? 416  ASN A CA    1 
ATOM   3196 C  C     . ASN A 1 415 ? 147.813 145.593 198.791 1.00 60.75  ? 416  ASN A C     1 
ATOM   3197 O  O     . ASN A 1 415 ? 148.021 145.122 197.669 1.00 60.75  ? 416  ASN A O     1 
ATOM   3198 C  CB    . ASN A 1 415 ? 149.379 147.086 200.074 1.00 60.75  ? 416  ASN A CB    1 
ATOM   3199 C  CG    . ASN A 1 415 ? 150.020 147.689 198.847 1.00 60.75  ? 416  ASN A CG    1 
ATOM   3200 O  OD1   . ASN A 1 415 ? 151.095 147.269 198.426 1.00 60.75  ? 416  ASN A OD1   1 
ATOM   3201 N  ND2   . ASN A 1 415 ? 149.361 148.681 198.262 1.00 60.75  ? 416  ASN A ND2   1 
ATOM   3202 N  N     . VAL A 1 416 ? 146.618 146.043 199.197 1.00 56.48  ? 417  VAL A N     1 
ATOM   3203 C  CA    . VAL A 1 416 ? 145.383 145.855 198.428 1.00 56.48  ? 417  VAL A CA    1 
ATOM   3204 C  C     . VAL A 1 416 ? 145.457 146.511 197.046 1.00 56.48  ? 417  VAL A C     1 
ATOM   3205 O  O     . VAL A 1 416 ? 144.904 145.989 196.072 1.00 56.48  ? 417  VAL A O     1 
ATOM   3206 C  CB    . VAL A 1 416 ? 144.165 146.332 199.254 1.00 56.48  ? 417  VAL A CB    1 
ATOM   3207 C  CG1   . VAL A 1 416 ? 144.178 147.840 199.525 1.00 56.48  ? 417  VAL A CG1   1 
ATOM   3208 C  CG2   . VAL A 1 416 ? 142.852 145.904 198.605 1.00 56.48  ? 417  VAL A CG2   1 
ATOM   3209 N  N     . GLN A 1 417 ? 146.141 147.653 196.931 1.00 55.58  ? 418  GLN A N     1 
ATOM   3210 C  CA    . GLN A 1 417 ? 146.276 148.309 195.633 1.00 55.58  ? 418  GLN A CA    1 
ATOM   3211 C  C     . GLN A 1 417 ? 147.157 147.519 194.671 1.00 55.58  ? 418  GLN A C     1 
ATOM   3212 O  O     . GLN A 1 417 ? 146.809 147.362 193.497 1.00 55.58  ? 418  GLN A O     1 
ATOM   3213 C  CB    . GLN A 1 417 ? 146.824 149.727 195.808 1.00 55.58  ? 418  GLN A CB    1 
ATOM   3214 C  CG    . GLN A 1 417 ? 145.950 150.673 196.637 1.00 55.58  ? 418  GLN A CG    1 
ATOM   3215 C  CD    . GLN A 1 417 ? 146.163 150.550 198.137 1.00 55.58  ? 418  GLN A CD    1 
ATOM   3216 O  OE1   . GLN A 1 417 ? 146.912 149.691 198.603 1.00 55.58  ? 418  GLN A OE1   1 
ATOM   3217 N  NE2   . GLN A 1 417 ? 145.499 151.409 198.900 1.00 55.58  ? 418  GLN A NE2   1 
ATOM   3218 N  N     . GLN A 1 418 ? 148.294 147.014 195.143 1.00 54.83  ? 419  GLN A N     1 
ATOM   3219 C  CA    . GLN A 1 418 ? 149.228 146.340 194.247 1.00 54.83  ? 419  GLN A CA    1 
ATOM   3220 C  C     . GLN A 1 418 ? 148.819 144.908 193.903 1.00 54.83  ? 419  GLN A C     1 
ATOM   3221 O  O     . GLN A 1 418 ? 149.204 144.409 192.840 1.00 54.83  ? 419  GLN A O     1 
ATOM   3222 C  CB    . GLN A 1 418 ? 150.643 146.391 194.834 1.00 54.83  ? 419  GLN A CB    1 
ATOM   3223 C  CG    . GLN A 1 418 ? 151.010 145.296 195.814 1.00 54.83  ? 419  GLN A CG    1 
ATOM   3224 C  CD    . GLN A 1 418 ? 152.486 145.294 196.145 1.00 54.83  ? 419  GLN A CD    1 
ATOM   3225 O  OE1   . GLN A 1 418 ? 153.309 144.798 195.376 1.00 54.83  ? 419  GLN A OE1   1 
ATOM   3226 N  NE2   . GLN A 1 418 ? 152.833 145.862 197.294 1.00 54.83  ? 419  GLN A NE2   1 
ATOM   3227 N  N     . VAL A 1 419 ? 148.071 144.221 194.773 1.00 50.37  ? 420  VAL A N     1 
ATOM   3228 C  CA    . VAL A 1 419 ? 147.508 142.925 194.396 1.00 50.37  ? 420  VAL A CA    1 
ATOM   3229 C  C     . VAL A 1 419 ? 146.451 143.074 193.298 1.00 50.37  ? 420  VAL A C     1 
ATOM   3230 O  O     . VAL A 1 419 ? 146.323 142.198 192.437 1.00 50.37  ? 420  VAL A O     1 
ATOM   3231 C  CB    . VAL A 1 419 ? 146.998 142.161 195.641 1.00 50.37  ? 420  VAL A CB    1 
ATOM   3232 C  CG1   . VAL A 1 419 ? 145.754 142.774 196.267 1.00 50.37  ? 420  VAL A CG1   1 
ATOM   3233 C  CG2   . VAL A 1 419 ? 146.762 140.690 195.316 1.00 50.37  ? 420  VAL A CG2   1 
ATOM   3234 N  N     . ILE A 1 420 ? 145.666 144.159 193.322 1.00 45.62  ? 421  ILE A N     1 
ATOM   3235 C  CA    . ILE A 1 420 ? 144.727 144.450 192.236 1.00 45.62  ? 421  ILE A CA    1 
ATOM   3236 C  C     . ILE A 1 420 ? 145.463 144.650 190.914 1.00 45.62  ? 421  ILE A C     1 
ATOM   3237 O  O     . ILE A 1 420 ? 145.056 144.112 189.876 1.00 45.62  ? 421  ILE A O     1 
ATOM   3238 C  CB    . ILE A 1 420 ? 143.846 145.661 192.597 1.00 45.62  ? 421  ILE A CB    1 
ATOM   3239 C  CG1   . ILE A 1 420 ? 142.821 145.265 193.659 1.00 45.62  ? 421  ILE A CG1   1 
ATOM   3240 C  CG2   . ILE A 1 420 ? 143.132 146.230 191.378 1.00 45.62  ? 421  ILE A CG2   1 
ATOM   3241 C  CD1   . ILE A 1 420 ? 142.093 146.431 194.266 1.00 45.62  ? 421  ILE A CD1   1 
ATOM   3242 N  N     . TYR A 1 421 ? 146.535 145.449 190.931 1.00 42.69  ? 422  TYR A N     1 
ATOM   3243 C  CA    . TYR A 1 421 ? 147.410 145.594 189.766 1.00 42.69  ? 422  TYR A CA    1 
ATOM   3244 C  C     . TYR A 1 421 ? 147.967 144.253 189.288 1.00 42.69  ? 422  TYR A C     1 
ATOM   3245 O  O     . TYR A 1 421 ? 148.050 144.009 188.078 1.00 42.69  ? 422  TYR A O     1 
ATOM   3246 C  CB    . TYR A 1 421 ? 148.548 146.569 190.072 1.00 42.69  ? 422  TYR A CB    1 
ATOM   3247 C  CG    . TYR A 1 421 ? 149.681 146.513 189.072 1.00 42.69  ? 422  TYR A CG    1 
ATOM   3248 C  CD1   . TYR A 1 421 ? 149.537 147.078 187.811 1.00 42.69  ? 422  TYR A CD1   1 
ATOM   3249 C  CD2   . TYR A 1 421 ? 150.893 145.911 189.388 1.00 42.69  ? 422  TYR A CD2   1 
ATOM   3250 C  CE1   . TYR A 1 421 ? 150.560 147.034 186.889 1.00 42.69  ? 422  TYR A CE1   1 
ATOM   3251 C  CE2   . TYR A 1 421 ? 151.921 145.859 188.470 1.00 42.69  ? 422  TYR A CE2   1 
ATOM   3252 C  CZ    . TYR A 1 421 ? 151.749 146.424 187.224 1.00 42.69  ? 422  TYR A CZ    1 
ATOM   3253 O  OH    . TYR A 1 421 ? 152.775 146.374 186.310 1.00 42.69  ? 422  TYR A OH    1 
ATOM   3254 N  N     . ALA A 1 422 ? 148.394 143.396 190.222 1.00 40.66  ? 423  ALA A N     1 
ATOM   3255 C  CA    . ALA A 1 422 ? 148.925 142.079 189.871 1.00 40.66  ? 423  ALA A CA    1 
ATOM   3256 C  C     . ALA A 1 422 ? 147.908 141.202 189.148 1.00 40.66  ? 423  ALA A C     1 
ATOM   3257 O  O     . ALA A 1 422 ? 148.295 140.395 188.297 1.00 40.66  ? 423  ALA A O     1 
ATOM   3258 C  CB    . ALA A 1 422 ? 149.429 141.366 191.123 1.00 40.66  ? 423  ALA A CB    1 
ATOM   3259 N  N     . THR A 1 423 ? 146.621 141.308 189.490 1.00 37.60  ? 424  THR A N     1 
ATOM   3260 C  CA    . THR A 1 423 ? 145.598 140.621 188.704 1.00 37.60  ? 424  THR A CA    1 
ATOM   3261 C  C     . THR A 1 423 ? 145.484 141.212 187.307 1.00 37.60  ? 424  THR A C     1 
ATOM   3262 O  O     . THR A 1 423 ? 145.304 140.474 186.331 1.00 37.60  ? 424  THR A O     1 
ATOM   3263 C  CB    . THR A 1 423 ? 144.240 140.678 189.397 1.00 37.60  ? 424  THR A CB    1 
ATOM   3264 O  OG1   . THR A 1 423 ? 143.763 142.029 189.418 1.00 37.60  ? 424  THR A OG1   1 
ATOM   3265 C  CG2   . THR A 1 423 ? 144.335 140.148 190.802 1.00 37.60  ? 424  THR A CG2   1 
ATOM   3266 N  N     . GLY A 1 424 ? 145.542 142.543 187.206 1.00 31.68  ? 425  GLY A N     1 
ATOM   3267 C  CA    . GLY A 1 424 ? 145.519 143.198 185.908 1.00 31.68  ? 425  GLY A CA    1 
ATOM   3268 C  C     . GLY A 1 424 ? 146.683 142.808 185.019 1.00 31.68  ? 425  GLY A C     1 
ATOM   3269 O  O     . GLY A 1 424 ? 146.505 142.583 183.822 1.00 31.68  ? 425  GLY A O     1 
ATOM   3270 N  N     . ALA A 1 425 ? 147.892 142.774 185.586 1.00 32.54  ? 426  ALA A N     1 
ATOM   3271 C  CA    . ALA A 1 425 ? 149.079 142.340 184.850 1.00 32.54  ? 426  ALA A CA    1 
ATOM   3272 C  C     . ALA A 1 425 ? 148.948 140.911 184.336 1.00 32.54  ? 426  ALA A C     1 
ATOM   3273 O  O     . ALA A 1 425 ? 149.387 140.604 183.224 1.00 32.54  ? 426  ALA A O     1 
ATOM   3274 C  CB    . ALA A 1 425 ? 150.318 142.471 185.730 1.00 32.54  ? 426  ALA A CB    1 
ATOM   3275 N  N     . LEU A 1 426 ? 148.385 140.018 185.149 1.00 31.50  ? 427  LEU A N     1 
ATOM   3276 C  CA    . LEU A 1 426 ? 148.167 138.642 184.712 1.00 31.50  ? 427  LEU A CA    1 
ATOM   3277 C  C     . LEU A 1 426 ? 147.098 138.542 183.632 1.00 31.50  ? 427  LEU A C     1 
ATOM   3278 O  O     . LEU A 1 426 ? 147.239 137.748 182.698 1.00 31.50  ? 427  LEU A O     1 
ATOM   3279 C  CB    . LEU A 1 426 ? 147.801 137.771 185.908 1.00 31.50  ? 427  LEU A CB    1 
ATOM   3280 C  CG    . LEU A 1 426 ? 148.968 137.460 186.835 1.00 31.50  ? 427  LEU A CG    1 
ATOM   3281 C  CD1   . LEU A 1 426 ? 148.462 137.028 188.185 1.00 31.50  ? 427  LEU A CD1   1 
ATOM   3282 C  CD2   . LEU A 1 426 ? 149.821 136.377 186.219 1.00 31.50  ? 427  LEU A CD2   1 
ATOM   3283 N  N     . ALA A 1 427 ? 146.022 139.324 183.750 1.00 27.25  ? 428  ALA A N     1 
ATOM   3284 C  CA    . ALA A 1 427 ? 144.943 139.291 182.762 1.00 27.25  ? 428  ALA A CA    1 
ATOM   3285 C  C     . ALA A 1 427 ? 145.414 139.758 181.388 1.00 27.25  ? 428  ALA A C     1 
ATOM   3286 O  O     . ALA A 1 427 ? 145.060 139.157 180.367 1.00 27.25  ? 428  ALA A O     1 
ATOM   3287 C  CB    . ALA A 1 427 ? 143.771 140.139 183.244 1.00 27.25  ? 428  ALA A CB    1 
ATOM   3288 N  N     . LYS A 1 428 ? 146.132 140.883 181.346 1.00 23.87  ? 429  LYS A N     1 
ATOM   3289 C  CA    . LYS A 1 428 ? 146.805 141.354 180.137 1.00 23.87  ? 429  LYS A CA    1 
ATOM   3290 C  C     . LYS A 1 428 ? 147.678 140.275 179.506 1.00 23.87  ? 429  LYS A C     1 
ATOM   3291 O  O     . LYS A 1 428 ? 147.612 140.031 178.298 1.00 23.87  ? 429  LYS A O     1 
ATOM   3292 C  CB    . LYS A 1 428 ? 147.675 142.559 180.482 1.00 23.87  ? 429  LYS A CB    1 
ATOM   3293 C  CG    . LYS A 1 428 ? 146.966 143.843 180.824 1.00 23.87  ? 429  LYS A CG    1 
ATOM   3294 C  CD    . LYS A 1 428 ? 147.963 144.732 181.544 1.00 23.87  ? 429  LYS A CD    1 
ATOM   3295 C  CE    . LYS A 1 428 ? 147.636 146.200 181.443 1.00 23.87  ? 429  LYS A CE    1 
ATOM   3296 N  NZ    . LYS A 1 428 ? 148.645 147.024 182.163 1.00 23.87  ? 429  LYS A NZ    1 
ATOM   3297 N  N     . ALA A 1 429 ? 148.519 139.634 180.321 1.00 26.37  ? 430  ALA A N     1 
ATOM   3298 C  CA    . ALA A 1 429 ? 149.527 138.702 179.820 1.00 26.37  ? 430  ALA A CA    1 
ATOM   3299 C  C     . ALA A 1 429 ? 148.924 137.417 179.261 1.00 26.37  ? 430  ALA A C     1 
ATOM   3300 O  O     . ALA A 1 429 ? 149.458 136.862 178.295 1.00 26.37  ? 430  ALA A O     1 
ATOM   3301 C  CB    . ALA A 1 429 ? 150.527 138.375 180.923 1.00 26.37  ? 430  ALA A CB    1 
ATOM   3302 N  N     . VAL A 1 430 ? 147.870 136.888 179.895 1.00 24.32  ? 431  VAL A N     1 
ATOM   3303 C  CA    . VAL A 1 430 ? 147.146 135.749 179.323 1.00 24.32  ? 431  VAL A CA    1 
ATOM   3304 C  C     . VAL A 1 430 ? 146.574 136.115 177.960 1.00 24.32  ? 431  VAL A C     1 
ATOM   3305 O  O     . VAL A 1 430 ? 146.709 135.358 176.994 1.00 24.32  ? 431  VAL A O     1 
ATOM   3306 C  CB    . VAL A 1 430 ? 146.047 135.250 180.280 1.00 24.32  ? 431  VAL A CB    1 
ATOM   3307 C  CG1   . VAL A 1 430 ? 145.274 134.121 179.646 1.00 24.32  ? 431  VAL A CG1   1 
ATOM   3308 C  CG2   . VAL A 1 430 ? 146.645 134.752 181.568 1.00 24.32  ? 431  VAL A CG2   1 
ATOM   3309 N  N     . TYR A 1 431 ? 145.928 137.281 177.866 1.00 21.92  ? 432  TYR A N     1 
ATOM   3310 C  CA    . TYR A 1 431 ? 145.271 137.689 176.625 1.00 21.92  ? 432  TYR A CA    1 
ATOM   3311 C  C     . TYR A 1 431 ? 146.270 137.912 175.493 1.00 21.92  ? 432  TYR A C     1 
ATOM   3312 O  O     . TYR A 1 431 ? 146.044 137.474 174.360 1.00 21.92  ? 432  TYR A O     1 
ATOM   3313 C  CB    . TYR A 1 431 ? 144.441 138.951 176.856 1.00 21.92  ? 432  TYR A CB    1 
ATOM   3314 C  CG    . TYR A 1 431 ? 143.458 139.241 175.746 1.00 21.92  ? 432  TYR A CG    1 
ATOM   3315 C  CD1   . TYR A 1 431 ? 142.193 138.686 175.760 1.00 21.92  ? 432  TYR A CD1   1 
ATOM   3316 C  CD2   . TYR A 1 431 ? 143.802 140.054 174.678 1.00 21.92  ? 432  TYR A CD2   1 
ATOM   3317 C  CE1   . TYR A 1 431 ? 141.298 138.939 174.749 1.00 21.92  ? 432  TYR A CE1   1 
ATOM   3318 C  CE2   . TYR A 1 431 ? 142.913 140.313 173.668 1.00 21.92  ? 432  TYR A CE2   1 
ATOM   3319 C  CZ    . TYR A 1 431 ? 141.663 139.753 173.707 1.00 21.92  ? 432  TYR A CZ    1 
ATOM   3320 O  OH    . TYR A 1 431 ? 140.773 140.005 172.693 1.00 21.92  ? 432  TYR A OH    1 
ATOM   3321 N  N     . GLU A 1 432 ? 147.373 138.608 175.774 1.00 24.05  ? 433  GLU A N     1 
ATOM   3322 C  CA    . GLU A 1 432 ? 148.364 138.879 174.737 1.00 24.05  ? 433  GLU A CA    1 
ATOM   3323 C  C     . GLU A 1 432 ? 149.096 137.619 174.293 1.00 24.05  ? 433  GLU A C     1 
ATOM   3324 O  O     . GLU A 1 432 ? 149.437 137.490 173.113 1.00 24.05  ? 433  GLU A O     1 
ATOM   3325 C  CB    . GLU A 1 432 ? 149.345 139.936 175.246 1.00 24.05  ? 433  GLU A CB    1 
ATOM   3326 C  CG    . GLU A 1 432 ? 150.483 140.294 174.313 1.00 24.05  ? 433  GLU A CG    1 
ATOM   3327 C  CD    . GLU A 1 432 ? 151.778 139.586 174.663 1.00 24.05  ? 433  GLU A CD    1 
ATOM   3328 O  OE1   . GLU A 1 432 ? 152.266 139.763 175.799 1.00 24.05  ? 433  GLU A OE1   1 
ATOM   3329 O  OE2   . GLU A 1 432 ? 152.306 138.857 173.798 1.00 24.05  ? 433  GLU A OE2   1 
ATOM   3330 N  N     . ARG A 1 433 ? 149.342 136.681 175.205 1.00 24.63  ? 434  ARG A N     1 
ATOM   3331 C  CA    . ARG A 1 433 ? 149.961 135.425 174.798 1.00 24.63  ? 434  ARG A CA    1 
ATOM   3332 C  C     . ARG A 1 433 ? 148.984 134.513 174.061 1.00 24.63  ? 434  ARG A C     1 
ATOM   3333 O  O     . ARG A 1 433 ? 149.399 133.763 173.174 1.00 24.63  ? 434  ARG A O     1 
ATOM   3334 C  CB    . ARG A 1 433 ? 150.563 134.730 176.011 1.00 24.63  ? 434  ARG A CB    1 
ATOM   3335 C  CG    . ARG A 1 433 ? 151.815 135.427 176.491 1.00 24.63  ? 434  ARG A CG    1 
ATOM   3336 C  CD    . ARG A 1 433 ? 152.282 134.904 177.827 1.00 24.63  ? 434  ARG A CD    1 
ATOM   3337 N  NE    . ARG A 1 433 ? 153.607 135.399 178.181 1.00 24.63  ? 434  ARG A NE    1 
ATOM   3338 C  CZ    . ARG A 1 433 ? 154.748 134.877 177.750 1.00 24.63  ? 434  ARG A CZ    1 
ATOM   3339 N  NH1   . ARG A 1 433 ? 155.896 135.451 178.070 1.00 24.63  ? 434  ARG A NH1   1 
ATOM   3340 N  NH2   . ARG A 1 433 ? 154.743 133.814 176.959 1.00 24.63  ? 434  ARG A NH2   1 
ATOM   3341 N  N     . MET A 1 434 ? 147.698 134.551 174.419 1.00 21.57  ? 435  MET A N     1 
ATOM   3342 C  CA    . MET A 1 434 ? 146.671 133.800 173.694 1.00 21.57  ? 435  MET A CA    1 
ATOM   3343 C  C     . MET A 1 434 ? 146.471 134.322 172.276 1.00 21.57  ? 435  MET A C     1 
ATOM   3344 O  O     . MET A 1 434 ? 146.339 133.539 171.330 1.00 21.57  ? 435  MET A O     1 
ATOM   3345 C  CB    . MET A 1 434 ? 145.355 133.843 174.469 1.00 21.57  ? 435  MET A CB    1 
ATOM   3346 C  CG    . MET A 1 434 ? 144.201 133.115 173.835 1.00 21.57  ? 435  MET A CG    1 
ATOM   3347 S  SD    . MET A 1 434 ? 142.696 133.393 174.782 1.00 21.57  ? 435  MET A SD    1 
ATOM   3348 C  CE    . MET A 1 434 ? 142.325 135.081 174.341 1.00 21.57  ? 435  MET A CE    1 
ATOM   3349 N  N     . PHE A 1 435 ? 146.394 135.645 172.126 1.00 19.98  ? 436  PHE A N     1 
ATOM   3350 C  CA    . PHE A 1 435 ? 146.316 136.277 170.811 1.00 19.98  ? 436  PHE A CA    1 
ATOM   3351 C  C     . PHE A 1 435 ? 147.532 135.958 169.946 1.00 19.98  ? 436  PHE A C     1 
ATOM   3352 O  O     . PHE A 1 435 ? 147.387 135.599 168.775 1.00 19.98  ? 436  PHE A O     1 
ATOM   3353 C  CB    . PHE A 1 435 ? 146.152 137.787 171.006 1.00 19.98  ? 436  PHE A CB    1 
ATOM   3354 C  CG    . PHE A 1 435 ? 145.932 138.573 169.741 1.00 19.98  ? 436  PHE A CG    1 
ATOM   3355 C  CD1   . PHE A 1 435 ? 146.993 139.076 169.006 1.00 19.98  ? 436  PHE A CD1   1 
ATOM   3356 C  CD2   . PHE A 1 435 ? 144.649 138.856 169.321 1.00 19.98  ? 436  PHE A CD2   1 
ATOM   3357 C  CE1   . PHE A 1 435 ? 146.775 139.806 167.867 1.00 19.98  ? 436  PHE A CE1   1 
ATOM   3358 C  CE2   . PHE A 1 435 ? 144.427 139.591 168.183 1.00 19.98  ? 436  PHE A CE2   1 
ATOM   3359 C  CZ    . PHE A 1 435 ? 145.492 140.066 167.457 1.00 19.98  ? 436  PHE A CZ    1 
ATOM   3360 N  N     . ASN A 1 436 ? 148.740 136.116 170.493 1.00 20.76  ? 437  ASN A N     1 
ATOM   3361 C  CA    . ASN A 1 436 ? 149.954 135.835 169.726 1.00 20.76  ? 437  ASN A CA    1 
ATOM   3362 C  C     . ASN A 1 436 ? 150.133 134.355 169.413 1.00 20.76  ? 437  ASN A C     1 
ATOM   3363 O  O     . ASN A 1 436 ? 150.806 134.012 168.436 1.00 20.76  ? 437  ASN A O     1 
ATOM   3364 C  CB    . ASN A 1 436 ? 151.177 136.361 170.465 1.00 20.76  ? 437  ASN A CB    1 
ATOM   3365 C  CG    . ASN A 1 436 ? 151.325 137.855 170.339 1.00 20.76  ? 437  ASN A CG    1 
ATOM   3366 O  OD1   . ASN A 1 436 ? 151.110 138.422 169.269 1.00 20.76  ? 437  ASN A OD1   1 
ATOM   3367 N  ND2   . ASN A 1 436 ? 151.699 138.506 171.431 1.00 20.76  ? 437  ASN A ND2   1 
ATOM   3368 N  N     . TRP A 1 437 ? 149.586 133.466 170.239 1.00 20.33  ? 438  TRP A N     1 
ATOM   3369 C  CA    . TRP A 1 437 ? 149.557 132.048 169.888 1.00 20.33  ? 438  TRP A CA    1 
ATOM   3370 C  C     . TRP A 1 437 ? 148.610 131.774 168.730 1.00 20.33  ? 438  TRP A C     1 
ATOM   3371 O  O     . TRP A 1 437 ? 148.893 130.919 167.884 1.00 20.33  ? 438  TRP A O     1 
ATOM   3372 C  CB    . TRP A 1 437 ? 149.164 131.224 171.105 1.00 20.33  ? 438  TRP A CB    1 
ATOM   3373 C  CG    . TRP A 1 437 ? 148.991 129.769 170.857 1.00 20.33  ? 438  TRP A CG    1 
ATOM   3374 C  CD1   . TRP A 1 437 ? 149.946 128.804 170.936 1.00 20.33  ? 438  TRP A CD1   1 
ATOM   3375 C  CD2   . TRP A 1 437 ? 147.770 129.101 170.548 1.00 20.33  ? 438  TRP A CD2   1 
ATOM   3376 N  NE1   . TRP A 1 437 ? 149.400 127.576 170.666 1.00 20.33  ? 438  TRP A NE1   1 
ATOM   3377 C  CE2   . TRP A 1 437 ? 148.062 127.734 170.426 1.00 20.33  ? 438  TRP A CE2   1 
ATOM   3378 C  CE3   . TRP A 1 437 ? 146.458 129.530 170.350 1.00 20.33  ? 438  TRP A CE3   1 
ATOM   3379 C  CZ2   . TRP A 1 437 ? 147.093 126.795 170.115 1.00 20.33  ? 438  TRP A CZ2   1 
ATOM   3380 C  CZ3   . TRP A 1 437 ? 145.500 128.598 170.044 1.00 20.33  ? 438  TRP A CZ3   1 
ATOM   3381 C  CH2   . TRP A 1 437 ? 145.820 127.248 169.928 1.00 20.33  ? 438  TRP A CH2   1 
ATOM   3382 N  N     . MET A 1 438 ? 147.460 132.448 168.718 1.00 20.49  ? 439  MET A N     1 
ATOM   3383 C  CA    . MET A 1 438 ? 146.455 132.261 167.674 1.00 20.49  ? 439  MET A CA    1 
ATOM   3384 C  C     . MET A 1 438 ? 146.987 132.615 166.289 1.00 20.49  ? 439  MET A C     1 
ATOM   3385 O  O     . MET A 1 438 ? 146.699 131.914 165.312 1.00 20.49  ? 439  MET A O     1 
ATOM   3386 C  CB    . MET A 1 438 ? 145.231 133.104 168.019 1.00 20.49  ? 439  MET A CB    1 
ATOM   3387 C  CG    . MET A 1 438 ? 144.156 133.146 166.979 1.00 20.49  ? 439  MET A CG    1 
ATOM   3388 S  SD    . MET A 1 438 ? 143.065 134.510 167.359 1.00 20.49  ? 439  MET A SD    1 
ATOM   3389 C  CE    . MET A 1 438 ? 142.540 133.988 168.981 1.00 20.49  ? 439  MET A CE    1 
ATOM   3390 N  N     . VAL A 1 439 ? 147.762 133.697 166.189 1.00 19.19  ? 440  VAL A N     1 
ATOM   3391 C  CA    . VAL A 1 439 ? 148.467 134.033 164.952 1.00 19.19  ? 440  VAL A CA    1 
ATOM   3392 C  C     . VAL A 1 439 ? 149.446 132.930 164.562 1.00 19.19  ? 440  VAL A C     1 
ATOM   3393 O  O     . VAL A 1 439 ? 149.547 132.563 163.385 1.00 19.19  ? 440  VAL A O     1 
ATOM   3394 C  CB    . VAL A 1 439 ? 149.159 135.402 165.106 1.00 19.19  ? 440  VAL A CB    1 
ATOM   3395 C  CG1   . VAL A 1 439 ? 150.160 135.653 164.008 1.00 19.19  ? 440  VAL A CG1   1 
ATOM   3396 C  CG2   . VAL A 1 439 ? 148.126 136.502 165.104 1.00 19.19  ? 440  VAL A CG2   1 
ATOM   3397 N  N     . THR A 1 440 ? 150.140 132.346 165.541 1.00 19.23  ? 441  THR A N     1 
ATOM   3398 C  CA    . THR A 1 440 ? 151.020 131.217 165.244 1.00 19.23  ? 441  THR A CA    1 
ATOM   3399 C  C     . THR A 1 440 ? 150.230 129.965 164.872 1.00 19.23  ? 441  THR A C     1 
ATOM   3400 O  O     . THR A 1 440 ? 150.709 129.140 164.085 1.00 19.23  ? 441  THR A O     1 
ATOM   3401 C  CB    . THR A 1 440 ? 151.923 130.946 166.450 1.00 19.23  ? 441  THR A CB    1 
ATOM   3402 O  OG1   . THR A 1 440 ? 152.499 132.180 166.891 1.00 19.23  ? 441  THR A OG1   1 
ATOM   3403 C  CG2   . THR A 1 440 ? 153.064 129.997 166.095 1.00 19.23  ? 441  THR A CG2   1 
ATOM   3404 N  N     . ARG A 1 441 ? 149.011 129.820 165.390 1.00 20.88  ? 442  ARG A N     1 
ATOM   3405 C  CA    . ARG A 1 441 ? 148.153 128.722 164.955 1.00 20.88  ? 442  ARG A CA    1 
ATOM   3406 C  C     . ARG A 1 441 ? 147.642 128.928 163.534 1.00 20.88  ? 442  ARG A C     1 
ATOM   3407 O  O     . ARG A 1 441 ? 147.592 127.974 162.750 1.00 20.88  ? 442  ARG A O     1 
ATOM   3408 C  CB    . ARG A 1 441 ? 146.984 128.545 165.920 1.00 20.88  ? 442  ARG A CB    1 
ATOM   3409 C  CG    . ARG A 1 441 ? 146.072 127.385 165.569 1.00 20.88  ? 442  ARG A CG    1 
ATOM   3410 C  CD    . ARG A 1 441 ? 146.844 126.089 165.448 1.00 20.88  ? 442  ARG A CD    1 
ATOM   3411 N  NE    . ARG A 1 441 ? 145.954 124.938 165.468 1.00 20.88  ? 442  ARG A NE    1 
ATOM   3412 C  CZ    . ARG A 1 441 ? 145.933 124.005 164.526 1.00 20.88  ? 442  ARG A CZ    1 
ATOM   3413 N  NH1   . ARG A 1 441 ? 145.087 122.990 164.611 1.00 20.88  ? 442  ARG A NH1   1 
ATOM   3414 N  NH2   . ARG A 1 441 ? 146.761 124.086 163.499 1.00 20.88  ? 442  ARG A NH2   1 
ATOM   3415 N  N     . ILE A 1 442 ? 147.233 130.156 163.201 1.00 20.50  ? 443  ILE A N     1 
ATOM   3416 C  CA    . ILE A 1 442 ? 146.767 130.475 161.851 1.00 20.50  ? 443  ILE A CA    1 
ATOM   3417 C  C     . ILE A 1 442 ? 147.859 130.230 160.813 1.00 20.50  ? 443  ILE A C     1 
ATOM   3418 O  O     . ILE A 1 442 ? 147.617 129.577 159.791 1.00 20.50  ? 443  ILE A O     1 
ATOM   3419 C  CB    . ILE A 1 442 ? 146.226 131.915 161.800 1.00 20.50  ? 443  ILE A CB    1 
ATOM   3420 C  CG1   . ILE A 1 442 ? 144.827 131.958 162.408 1.00 20.50  ? 443  ILE A CG1   1 
ATOM   3421 C  CG2   . ILE A 1 442 ? 146.180 132.454 160.389 1.00 20.50  ? 443  ILE A CG2   1 
ATOM   3422 C  CD1   . ILE A 1 442 ? 144.221 133.331 162.453 1.00 20.50  ? 443  ILE A CD1   1 
ATOM   3423 N  N     . ASN A 1 443 ? 149.063 130.769 161.049 1.00 20.69  ? 444  ASN A N     1 
ATOM   3424 C  CA    . ASN A 1 443 ? 150.190 130.584 160.131 1.00 20.69  ? 444  ASN A CA    1 
ATOM   3425 C  C     . ASN A 1 443 ? 150.542 129.119 159.899 1.00 20.69  ? 444  ASN A C     1 
ATOM   3426 O  O     . ASN A 1 443 ? 150.963 128.761 158.797 1.00 20.69  ? 444  ASN A O     1 
ATOM   3427 C  CB    . ASN A 1 443 ? 151.421 131.330 160.633 1.00 20.69  ? 444  ASN A CB    1 
ATOM   3428 C  CG    . ASN A 1 443 ? 151.271 132.820 160.526 1.00 20.69  ? 444  ASN A CG    1 
ATOM   3429 O  OD1   . ASN A 1 443 ? 150.356 133.315 159.875 1.00 20.69  ? 444  ASN A OD1   1 
ATOM   3430 N  ND2   . ASN A 1 443 ? 152.174 133.551 161.159 1.00 20.69  ? 444  ASN A ND2   1 
ATOM   3431 N  N     . ALA A 1 444 ? 150.393 128.265 160.915 1.00 21.52  ? 445  ALA A N     1 
ATOM   3432 C  CA    . ALA A 1 444 ? 150.679 126.843 160.739 1.00 21.52  ? 445  ALA A CA    1 
ATOM   3433 C  C     . ALA A 1 444 ? 149.662 126.142 159.840 1.00 21.52  ? 445  ALA A C     1 
ATOM   3434 O  O     . ALA A 1 444 ? 150.006 125.164 159.170 1.00 21.52  ? 445  ALA A O     1 
ATOM   3435 C  CB    . ALA A 1 444 ? 150.745 126.150 162.097 1.00 21.52  ? 445  ALA A CB    1 
ATOM   3436 N  N     . THR A 1 445 ? 148.404 126.584 159.845 1.00 21.91  ? 446  THR A N     1 
ATOM   3437 C  CA    . THR A 1 445 ? 147.426 126.044 158.903 1.00 21.91  ? 446  THR A CA    1 
ATOM   3438 C  C     . THR A 1 445 ? 147.647 126.555 157.482 1.00 21.91  ? 446  THR A C     1 
ATOM   3439 O  O     . THR A 1 445 ? 147.428 125.820 156.513 1.00 21.91  ? 446  THR A O     1 
ATOM   3440 C  CB    . THR A 1 445 ? 146.009 126.363 159.367 1.00 21.91  ? 446  THR A CB    1 
ATOM   3441 O  OG1   . THR A 1 445 ? 145.781 127.772 159.279 1.00 21.91  ? 446  THR A OG1   1 
ATOM   3442 C  CG2   . THR A 1 445 ? 145.818 125.914 160.790 1.00 21.91  ? 446  THR A CG2   1 
ATOM   3443 N  N     . LEU A 1 446 ? 148.066 127.813 157.336 1.00 25.24  ? 447  LEU A N     1 
ATOM   3444 C  CA    . LEU A 1 446 ? 148.238 128.422 156.021 1.00 25.24  ? 447  LEU A CA    1 
ATOM   3445 C  C     . LEU A 1 446 ? 149.508 128.005 155.285 1.00 25.24  ? 447  LEU A C     1 
ATOM   3446 O  O     . LEU A 1 446 ? 149.586 128.215 154.074 1.00 25.24  ? 447  LEU A O     1 
ATOM   3447 C  CB    . LEU A 1 446 ? 148.201 129.943 156.136 1.00 25.24  ? 447  LEU A CB    1 
ATOM   3448 C  CG    . LEU A 1 446 ? 146.877 130.522 156.623 1.00 25.24  ? 447  LEU A CG    1 
ATOM   3449 C  CD1   . LEU A 1 446 ? 146.989 132.020 156.780 1.00 25.24  ? 447  LEU A CD1   1 
ATOM   3450 C  CD2   . LEU A 1 446 ? 145.760 130.165 155.675 1.00 25.24  ? 447  LEU A CD2   1 
ATOM   3451 N  N     . GLU A 1 447 ? 150.516 127.455 155.962 1.00 29.92  ? 448  GLU A N     1 
ATOM   3452 C  CA    . GLU A 1 447 ? 151.754 127.041 155.288 1.00 29.92  ? 448  GLU A CA    1 
ATOM   3453 C  C     . GLU A 1 447 ? 151.540 125.736 154.508 1.00 29.92  ? 448  GLU A C     1 
ATOM   3454 O  O     . GLU A 1 447 ? 151.946 124.642 154.902 1.00 29.92  ? 448  GLU A O     1 
ATOM   3455 C  CB    . GLU A 1 447 ? 152.912 126.968 156.280 1.00 29.92  ? 448  GLU A CB    1 
ATOM   3456 C  CG    . GLU A 1 447 ? 152.656 126.267 157.612 1.00 29.92  ? 448  GLU A CG    1 
ATOM   3457 C  CD    . GLU A 1 447 ? 153.151 124.840 157.666 1.00 29.92  ? 448  GLU A CD    1 
ATOM   3458 O  OE1   . GLU A 1 447 ? 154.051 124.496 156.875 1.00 29.92  ? 448  GLU A OE1   1 
ATOM   3459 O  OE2   . GLU A 1 447 ? 152.638 124.061 158.496 1.00 29.92  ? 448  GLU A OE2   1 
ATOM   3460 N  N     . THR A 1 448 ? 150.862 125.871 153.361 1.00 34.79  ? 449  THR A N     1 
ATOM   3461 C  CA    . THR A 1 448 ? 150.386 124.743 152.555 1.00 34.79  ? 449  THR A CA    1 
ATOM   3462 C  C     . THR A 1 448 ? 151.503 123.891 151.954 1.00 34.79  ? 449  THR A C     1 
ATOM   3463 O  O     . THR A 1 448 ? 151.191 122.837 151.387 1.00 34.79  ? 449  THR A O     1 
ATOM   3464 C  CB    . THR A 1 448 ? 149.486 125.230 151.419 1.00 34.79  ? 449  THR A CB    1 
ATOM   3465 O  OG1   . THR A 1 448 ? 150.258 126.015 150.503 1.00 34.79  ? 449  THR A OG1   1 
ATOM   3466 C  CG2   . THR A 1 448 ? 148.316 126.047 151.955 1.00 34.79  ? 449  THR A CG2   1 
ATOM   3467 N  N     . LYS A 1 449 ? 152.759 124.366 151.985 1.00 38.84  ? 450  LYS A N     1 
ATOM   3468 C  CA    . LYS A 1 449 ? 153.949 123.756 151.373 1.00 38.84  ? 450  LYS A CA    1 
ATOM   3469 C  C     . LYS A 1 449 ? 153.873 123.694 149.849 1.00 38.84  ? 450  LYS A C     1 
ATOM   3470 O  O     . LYS A 1 449 ? 154.627 122.940 149.224 1.00 38.84  ? 450  LYS A O     1 
ATOM   3471 C  CB    . LYS A 1 449 ? 154.248 122.355 151.937 1.00 38.84  ? 450  LYS A CB    1 
ATOM   3472 C  CG    . LYS A 1 449 ? 154.245 122.248 153.454 1.00 38.84  ? 450  LYS A CG    1 
ATOM   3473 C  CD    . LYS A 1 449 ? 155.655 122.217 154.021 1.00 38.84  ? 450  LYS A CD    1 
ATOM   3474 C  CE    . LYS A 1 449 ? 155.638 121.923 155.516 1.00 38.84  ? 450  LYS A CE    1 
ATOM   3475 N  NZ    . LYS A 1 449 ? 156.961 121.469 156.032 1.00 38.84  ? 450  LYS A NZ    1 
ATOM   3476 N  N     . GLN A 1 450 ? 152.971 124.460 149.238 1.00 41.50  ? 451  GLN A N     1 
ATOM   3477 C  CA    . GLN A 1 450 ? 152.982 124.650 147.795 1.00 41.50  ? 451  GLN A CA    1 
ATOM   3478 C  C     . GLN A 1 450 ? 154.257 125.389 147.368 1.00 41.50  ? 451  GLN A C     1 
ATOM   3479 O  O     . GLN A 1 450 ? 154.835 126.137 148.164 1.00 41.50  ? 451  GLN A O     1 
ATOM   3480 C  CB    . GLN A 1 450 ? 151.725 125.425 147.384 1.00 41.50  ? 451  GLN A CB    1 
ATOM   3481 C  CG    . GLN A 1 450 ? 150.441 124.599 147.470 1.00 41.50  ? 451  GLN A CG    1 
ATOM   3482 C  CD    . GLN A 1 450 ? 149.251 125.265 146.802 1.00 41.50  ? 451  GLN A CD    1 
ATOM   3483 O  OE1   . GLN A 1 450 ? 148.836 124.881 145.710 1.00 41.50  ? 451  GLN A OE1   1 
ATOM   3484 N  NE2   . GLN A 1 450 ? 148.693 126.270 147.465 1.00 41.50  ? 451  GLN A NE2   1 
ATOM   3485 N  N     . PRO A 1 451 ? 154.727 125.190 146.128 1.00 42.63  ? 452  PRO A N     1 
ATOM   3486 C  CA    . PRO A 1 451 ? 155.979 125.831 145.700 1.00 42.63  ? 452  PRO A CA    1 
ATOM   3487 C  C     . PRO A 1 451 ? 155.855 127.343 145.587 1.00 42.63  ? 452  PRO A C     1 
ATOM   3488 O  O     . PRO A 1 451 ? 154.782 127.884 145.317 1.00 42.63  ? 452  PRO A O     1 
ATOM   3489 C  CB    . PRO A 1 451 ? 156.266 125.184 144.342 1.00 42.63  ? 452  PRO A CB    1 
ATOM   3490 C  CG    . PRO A 1 451 ? 154.956 124.729 143.851 1.00 42.63  ? 452  PRO A CG    1 
ATOM   3491 C  CD    . PRO A 1 451 ? 154.194 124.308 145.072 1.00 42.63  ? 452  PRO A CD    1 
ATOM   3492 N  N     . ARG A 1 452 ? 156.986 128.022 145.782 1.00 39.20  ? 453  ARG A N     1 
ATOM   3493 C  CA    . ARG A 1 452 ? 156.998 129.434 146.133 1.00 39.20  ? 453  ARG A CA    1 
ATOM   3494 C  C     . ARG A 1 452 ? 158.232 130.103 145.548 1.00 39.20  ? 453  ARG A C     1 
ATOM   3495 O  O     . ARG A 1 452 ? 159.305 129.497 145.486 1.00 39.20  ? 453  ARG A O     1 
ATOM   3496 C  CB    . ARG A 1 452 ? 156.998 129.553 147.660 1.00 39.20  ? 453  ARG A CB    1 
ATOM   3497 C  CG    . ARG A 1 452 ? 156.894 130.927 148.261 1.00 39.20  ? 453  ARG A CG    1 
ATOM   3498 C  CD    . ARG A 1 452 ? 156.929 130.796 149.778 1.00 39.20  ? 453  ARG A CD    1 
ATOM   3499 N  NE    . ARG A 1 452 ? 155.833 129.970 150.282 1.00 39.20  ? 453  ARG A NE    1 
ATOM   3500 C  CZ    . ARG A 1 452 ? 155.995 128.817 150.924 1.00 39.20  ? 453  ARG A CZ    1 
ATOM   3501 N  NH1   . ARG A 1 452 ? 154.940 128.127 151.325 1.00 39.20  ? 453  ARG A NH1   1 
ATOM   3502 N  NH2   . ARG A 1 452 ? 157.212 128.346 151.147 1.00 39.20  ? 453  ARG A NH2   1 
ATOM   3503 N  N     . GLN A 1 453 ? 158.078 131.373 145.131 1.00 41.38  ? 454  GLN A N     1 
ATOM   3504 C  CA    . GLN A 1 453 ? 159.218 132.209 144.749 1.00 41.38  ? 454  GLN A CA    1 
ATOM   3505 C  C     . GLN A 1 453 ? 159.137 133.665 145.197 1.00 41.38  ? 454  GLN A C     1 
ATOM   3506 O  O     . GLN A 1 453 ? 160.182 134.246 145.502 1.00 41.38  ? 454  GLN A O     1 
ATOM   3507 C  CB    . GLN A 1 453 ? 159.416 132.186 143.226 1.00 41.38  ? 454  GLN A CB    1 
ATOM   3508 C  CG    . GLN A 1 453 ? 160.116 130.952 142.652 1.00 41.38  ? 454  GLN A CG    1 
ATOM   3509 C  CD    . GLN A 1 453 ? 161.557 130.799 143.124 1.00 41.38  ? 454  GLN A CD    1 
ATOM   3510 O  OE1   . GLN A 1 453 ? 161.827 130.271 144.203 1.00 41.38  ? 454  GLN A OE1   1 
ATOM   3511 N  NE2   . GLN A 1 453 ? 162.491 131.270 142.307 1.00 41.38  ? 454  GLN A NE2   1 
ATOM   3512 N  N     . TYR A 1 454 ? 157.960 134.281 145.250 1.00 36.14  ? 455  TYR A N     1 
ATOM   3513 C  CA    . TYR A 1 454 ? 157.824 135.714 145.470 1.00 36.14  ? 455  TYR A CA    1 
ATOM   3514 C  C     . TYR A 1 454 ? 156.737 135.951 146.505 1.00 36.14  ? 455  TYR A C     1 
ATOM   3515 O  O     . TYR A 1 454 ? 155.946 135.056 146.807 1.00 36.14  ? 455  TYR A O     1 
ATOM   3516 C  CB    . TYR A 1 454 ? 157.482 136.470 144.177 1.00 36.14  ? 455  TYR A CB    1 
ATOM   3517 C  CG    . TYR A 1 454 ? 158.255 136.013 142.965 1.00 36.14  ? 455  TYR A CG    1 
ATOM   3518 C  CD1   . TYR A 1 454 ? 159.611 136.276 142.842 1.00 36.14  ? 455  TYR A CD1   1 
ATOM   3519 C  CD2   . TYR A 1 454 ? 157.627 135.314 141.943 1.00 36.14  ? 455  TYR A CD2   1 
ATOM   3520 C  CE1   . TYR A 1 454 ? 160.319 135.866 141.730 1.00 36.14  ? 455  TYR A CE1   1 
ATOM   3521 C  CE2   . TYR A 1 454 ? 158.326 134.889 140.833 1.00 36.14  ? 455  TYR A CE2   1 
ATOM   3522 C  CZ    . TYR A 1 454 ? 159.671 135.170 140.730 1.00 36.14  ? 455  TYR A CZ    1 
ATOM   3523 O  OH    . TYR A 1 454 ? 160.374 134.742 139.628 1.00 36.14  ? 455  TYR A OH    1 
ATOM   3524 N  N     . PHE A 1 455 ? 156.686 137.164 147.052 1.00 25.91  ? 456  PHE A N     1 
ATOM   3525 C  CA    . PHE A 1 455 ? 155.604 137.480 147.970 1.00 25.91  ? 456  PHE A CA    1 
ATOM   3526 C  C     . PHE A 1 455 ? 155.042 138.866 147.689 1.00 25.91  ? 456  PHE A C     1 
ATOM   3527 O  O     . PHE A 1 455 ? 155.698 139.726 147.100 1.00 25.91  ? 456  PHE A O     1 
ATOM   3528 C  CB    . PHE A 1 455 ? 156.075 137.319 149.439 1.00 25.91  ? 456  PHE A CB    1 
ATOM   3529 C  CG    . PHE A 1 455 ? 156.719 138.547 150.059 1.00 25.91  ? 456  PHE A CG    1 
ATOM   3530 C  CD1   . PHE A 1 455 ? 155.965 139.506 150.737 1.00 25.91  ? 456  PHE A CD1   1 
ATOM   3531 C  CD2   . PHE A 1 455 ? 158.085 138.726 149.980 1.00 25.91  ? 456  PHE A CD2   1 
ATOM   3532 C  CE1   . PHE A 1 455 ? 156.563 140.610 151.297 1.00 25.91  ? 456  PHE A CE1   1 
ATOM   3533 C  CE2   . PHE A 1 455 ? 158.687 139.835 150.544 1.00 25.91  ? 456  PHE A CE2   1 
ATOM   3534 C  CZ    . PHE A 1 455 ? 157.923 140.774 151.202 1.00 25.91  ? 456  PHE A CZ    1 
ATOM   3535 N  N     . ILE A 1 456 ? 153.800 139.057 148.130 1.00 22.44  ? 457  ILE A N     1 
ATOM   3536 C  CA    . ILE A 1 456 ? 153.122 140.348 148.148 1.00 22.44  ? 457  ILE A CA    1 
ATOM   3537 C  C     . ILE A 1 456 ? 152.714 140.610 149.590 1.00 22.44  ? 457  ILE A C     1 
ATOM   3538 O  O     . ILE A 1 456 ? 151.825 139.934 150.119 1.00 22.44  ? 457  ILE A O     1 
ATOM   3539 C  CB    . ILE A 1 456 ? 151.903 140.386 147.219 1.00 22.44  ? 457  ILE A CB    1 
ATOM   3540 C  CG1   . ILE A 1 456 ? 152.293 139.973 145.801 1.00 22.44  ? 457  ILE A CG1   1 
ATOM   3541 C  CG2   . ILE A 1 456 ? 151.282 141.763 147.227 1.00 22.44  ? 457  ILE A CG2   1 
ATOM   3542 C  CD1   . ILE A 1 456 ? 151.186 140.126 144.788 1.00 22.44  ? 457  ILE A CD1   1 
ATOM   3543 N  N     . GLY A 1 457 ? 153.340 141.595 150.222 1.00 19.25  ? 458  GLY A N     1 
ATOM   3544 C  CA    . GLY A 1 457 ? 153.023 141.931 151.595 1.00 19.25  ? 458  GLY A CA    1 
ATOM   3545 C  C     . GLY A 1 457 ? 152.117 143.130 151.781 1.00 19.25  ? 458  GLY A C     1 
ATOM   3546 O  O     . GLY A 1 457 ? 152.515 144.253 151.478 1.00 19.25  ? 458  GLY A O     1 
ATOM   3547 N  N     . VAL A 1 458 ? 150.915 142.925 152.303 1.00 17.05  ? 459  VAL A N     1 
ATOM   3548 C  CA    . VAL A 1 458 ? 149.945 143.998 152.480 1.00 17.05  ? 459  VAL A CA    1 
ATOM   3549 C  C     . VAL A 1 458 ? 149.997 144.460 153.928 1.00 17.05  ? 459  VAL A C     1 
ATOM   3550 O  O     . VAL A 1 458 ? 149.820 143.658 154.850 1.00 17.05  ? 459  VAL A O     1 
ATOM   3551 C  CB    . VAL A 1 458 ? 148.531 143.537 152.105 1.00 17.05  ? 459  VAL A CB    1 
ATOM   3552 C  CG1   . VAL A 1 458 ? 147.594 144.711 152.066 1.00 17.05  ? 459  VAL A CG1   1 
ATOM   3553 C  CG2   . VAL A 1 458 ? 148.553 142.822 150.778 1.00 17.05  ? 459  VAL A CG2   1 
ATOM   3554 N  N     . LEU A 1 459 ? 150.226 145.754 154.132 1.00 18.77  ? 460  LEU A N     1 
ATOM   3555 C  CA    . LEU A 1 459 ? 150.435 146.333 155.455 1.00 18.77  ? 460  LEU A CA    1 
ATOM   3556 C  C     . LEU A 1 459 ? 149.312 147.301 155.784 1.00 18.77  ? 460  LEU A C     1 
ATOM   3557 O  O     . LEU A 1 459 ? 149.080 148.261 155.044 1.00 18.77  ? 460  LEU A O     1 
ATOM   3558 C  CB    . LEU A 1 459 ? 151.779 147.053 155.520 1.00 18.77  ? 460  LEU A CB    1 
ATOM   3559 C  CG    . LEU A 1 459 ? 152.238 147.665 156.835 1.00 18.77  ? 460  LEU A CG    1 
ATOM   3560 C  CD1   . LEU A 1 459 ? 152.708 146.615 157.794 1.00 18.77  ? 460  LEU A CD1   1 
ATOM   3561 C  CD2   . LEU A 1 459 ? 153.360 148.603 156.536 1.00 18.77  ? 460  LEU A CD2   1 
ATOM   3562 N  N     . ASP A 1 460 ? 148.640 147.069 156.909 1.00 21.53  ? 461  ASP A N     1 
ATOM   3563 C  CA    . ASP A 1 460 ? 147.795 148.078 157.545 1.00 21.53  ? 461  ASP A CA    1 
ATOM   3564 C  C     . ASP A 1 460 ? 148.205 148.237 159.013 1.00 21.53  ? 461  ASP A C     1 
ATOM   3565 O  O     . ASP A 1 460 ? 147.760 147.524 159.914 1.00 21.53  ? 461  ASP A O     1 
ATOM   3566 C  CB    . ASP A 1 460 ? 146.304 147.733 157.338 1.00 21.53  ? 461  ASP A CB    1 
ATOM   3567 C  CG    . ASP A 1 460 ? 145.920 146.367 157.874 1.00 21.53  ? 461  ASP A CG    1 
ATOM   3568 O  OD1   . ASP A 1 460 ? 145.385 146.281 158.998 1.00 21.53  ? 461  ASP A OD1   1 
ATOM   3569 O  OD2   . ASP A 1 460 ? 146.189 145.372 157.183 1.00 21.53  ? 461  ASP A OD2   1 
ATOM   3570 N  N     . ILE A 1 461 ? 149.126 149.169 159.254 1.00 22.63  ? 462  ILE A N     1 
ATOM   3571 C  CA    . ILE A 1 461 ? 149.435 149.580 160.616 1.00 22.63  ? 462  ILE A CA    1 
ATOM   3572 C  C     . ILE A 1 461 ? 148.227 150.282 161.218 1.00 22.63  ? 462  ILE A C     1 
ATOM   3573 O  O     . ILE A 1 461 ? 147.365 150.800 160.498 1.00 22.63  ? 462  ILE A O     1 
ATOM   3574 C  CB    . ILE A 1 461 ? 150.663 150.500 160.669 1.00 22.63  ? 462  ILE A CB    1 
ATOM   3575 C  CG1   . ILE A 1 461 ? 150.412 151.752 159.829 1.00 22.63  ? 462  ILE A CG1   1 
ATOM   3576 C  CG2   . ILE A 1 461 ? 151.893 149.743 160.202 1.00 22.63  ? 462  ILE A CG2   1 
ATOM   3577 C  CD1   . ILE A 1 461 ? 151.314 152.892 160.175 1.00 22.63  ? 462  ILE A CD1   1 
ATOM   3578 N  N     . ALA A 1 462 ? 148.101 150.191 162.542 1.00 21.73  ? 463  ALA A N     1 
ATOM   3579 C  CA    . ALA A 1 462 ? 147.137 150.998 163.278 1.00 21.73  ? 463  ALA A CA    1 
ATOM   3580 C  C     . ALA A 1 462 ? 147.312 152.472 162.941 1.00 21.73  ? 463  ALA A C     1 
ATOM   3581 O  O     . ALA A 1 462 ? 148.428 152.994 162.962 1.00 21.73  ? 463  ALA A O     1 
ATOM   3582 C  CB    . ALA A 1 462 ? 147.299 150.778 164.779 1.00 21.73  ? 463  ALA A CB    1 
ATOM   3583 N  N     . GLY A 1 463 ? 146.205 153.125 162.601 1.00 23.78  ? 464  GLY A N     1 
ATOM   3584 C  CA    . GLY A 1 463 ? 146.257 154.484 162.097 1.00 23.78  ? 464  GLY A CA    1 
ATOM   3585 C  C     . GLY A 1 463 ? 146.652 155.486 163.159 1.00 23.78  ? 464  GLY A C     1 
ATOM   3586 O  O     . GLY A 1 463 ? 146.656 155.183 164.340 1.00 23.78  ? 464  GLY A O     1 
ATOM   3587 N  N     . PHE A 1 464 ? 147.130 156.641 162.702 1.00 22.39  ? 465  PHE A N     1 
ATOM   3588 C  CA    . PHE A 1 464 ? 147.468 157.749 163.588 1.00 22.39  ? 465  PHE A CA    1 
ATOM   3589 C  C     . PHE A 1 464 ? 146.259 158.150 164.435 1.00 22.39  ? 465  PHE A C     1 
ATOM   3590 O  O     . PHE A 1 464 ? 145.134 158.228 163.938 1.00 22.39  ? 465  PHE A O     1 
ATOM   3591 C  CB    . PHE A 1 464 ? 147.966 158.927 162.749 1.00 22.39  ? 465  PHE A CB    1 
ATOM   3592 C  CG    . PHE A 1 464 ? 148.331 160.147 163.539 1.00 22.39  ? 465  PHE A CG    1 
ATOM   3593 C  CD1   . PHE A 1 464 ? 149.569 160.246 164.140 1.00 22.39  ? 465  PHE A CD1   1 
ATOM   3594 C  CD2   . PHE A 1 464 ? 147.464 161.219 163.627 1.00 22.39  ? 465  PHE A CD2   1 
ATOM   3595 C  CE1   . PHE A 1 464 ? 149.919 161.370 164.849 1.00 22.39  ? 465  PHE A CE1   1 
ATOM   3596 C  CE2   . PHE A 1 464 ? 147.810 162.347 164.338 1.00 22.39  ? 465  PHE A CE2   1 
ATOM   3597 C  CZ    . PHE A 1 464 ? 149.041 162.421 164.948 1.00 22.39  ? 465  PHE A CZ    1 
ATOM   3598 N  N     . GLU A 1 465 ? 146.499 158.410 165.724 1.00 22.97  ? 466  GLU A N     1 
ATOM   3599 C  CA    . GLU A 1 465 ? 145.445 158.574 166.721 1.00 22.97  ? 466  GLU A CA    1 
ATOM   3600 C  C     . GLU A 1 465 ? 145.681 159.811 167.565 1.00 22.97  ? 466  GLU A C     1 
ATOM   3601 O  O     . GLU A 1 465 ? 146.818 160.112 167.934 1.00 22.97  ? 466  GLU A O     1 
ATOM   3602 C  CB    . GLU A 1 465 ? 145.371 157.395 167.688 1.00 22.97  ? 466  GLU A CB    1 
ATOM   3603 C  CG    . GLU A 1 465 ? 145.397 156.037 167.094 1.00 22.97  ? 466  GLU A CG    1 
ATOM   3604 C  CD    . GLU A 1 465 ? 145.089 154.962 168.092 1.00 22.97  ? 466  GLU A CD    1 
ATOM   3605 O  OE1   . GLU A 1 465 ? 145.803 154.886 169.107 1.00 22.97  ? 466  GLU A OE1   1 
ATOM   3606 O  OE2   . GLU A 1 465 ? 144.140 154.190 167.864 1.00 22.97  ? 466  GLU A OE2   1 
ATOM   3607 N  N     . ILE A 1 466 ? 144.596 160.507 167.896 1.00 25.35  ? 467  ILE A N     1 
ATOM   3608 C  CA    . ILE A 1 466 ? 144.611 161.547 168.920 1.00 25.35  ? 467  ILE A CA    1 
ATOM   3609 C  C     . ILE A 1 466 ? 143.384 161.340 169.796 1.00 25.35  ? 467  ILE A C     1 
ATOM   3610 O  O     . ILE A 1 466 ? 142.265 161.682 169.402 1.00 25.35  ? 467  ILE A O     1 
ATOM   3611 C  CB    . ILE A 1 466 ? 144.605 162.975 168.334 1.00 25.35  ? 467  ILE A CB    1 
ATOM   3612 C  CG1   . ILE A 1 466 ? 145.758 163.219 167.359 1.00 25.35  ? 467  ILE A CG1   1 
ATOM   3613 C  CG2   . ILE A 1 466 ? 144.669 163.999 169.454 1.00 25.35  ? 467  ILE A CG2   1 
ATOM   3614 C  CD1   . ILE A 1 466 ? 145.778 164.609 166.780 1.00 25.35  ? 467  ILE A CD1   1 
ATOM   3615 N  N     . PHE A 1 467 ? 143.556 160.635 170.908 1.00 27.53  ? 468  PHE A N     1 
ATOM   3616 C  CA    . PHE A 1 467 ? 142.425 160.448 171.838 1.00 27.53  ? 468  PHE A CA    1 
ATOM   3617 C  C     . PHE A 1 467 ? 142.508 161.612 172.822 1.00 27.53  ? 468  PHE A C     1 
ATOM   3618 O  O     . PHE A 1 467 ? 143.101 162.633 172.465 1.00 27.53  ? 468  PHE A O     1 
ATOM   3619 C  CB    . PHE A 1 467 ? 142.481 159.068 172.493 1.00 27.53  ? 468  PHE A CB    1 
ATOM   3620 C  CG    . PHE A 1 467 ? 142.361 157.899 171.562 1.00 27.53  ? 468  PHE A CG    1 
ATOM   3621 C  CD1   . PHE A 1 467 ? 141.894 158.067 170.273 1.00 27.53  ? 468  PHE A CD1   1 
ATOM   3622 C  CD2   . PHE A 1 467 ? 142.707 156.633 171.985 1.00 27.53  ? 468  PHE A CD2   1 
ATOM   3623 C  CE1   . PHE A 1 467 ? 141.785 156.988 169.416 1.00 27.53  ? 468  PHE A CE1   1 
ATOM   3624 C  CE2   . PHE A 1 467 ? 142.608 155.556 171.125 1.00 27.53  ? 468  PHE A CE2   1 
ATOM   3625 C  CZ    . PHE A 1 467 ? 142.145 155.736 169.846 1.00 27.53  ? 468  PHE A CZ    1 
ATOM   3626 N  N     . ASP A 1 468 ? 141.959 161.463 174.025 1.00 35.90  ? 469  ASP A N     1 
ATOM   3627 C  CA    . ASP A 1 468 ? 142.073 162.510 175.067 1.00 35.90  ? 469  ASP A CA    1 
ATOM   3628 C  C     . ASP A 1 468 ? 142.718 161.891 176.303 1.00 35.90  ? 469  ASP A C     1 
ATOM   3629 O  O     . ASP A 1 468 ? 142.235 162.170 177.399 1.00 35.90  ? 469  ASP A O     1 
ATOM   3630 C  CB    . ASP A 1 468 ? 140.708 163.094 175.412 1.00 35.90  ? 469  ASP A CB    1 
ATOM   3631 C  CG    . ASP A 1 468 ? 139.947 163.661 174.229 1.00 35.90  ? 469  ASP A CG    1 
ATOM   3632 O  OD1   . ASP A 1 468 ? 140.265 163.286 173.087 1.00 35.90  ? 469  ASP A OD1   1 
ATOM   3633 O  OD2   . ASP A 1 468 ? 139.032 164.473 174.463 1.00 35.90  ? 469  ASP A OD2   1 
ATOM   3634 N  N     . PHE A 1 469 ? 143.728 161.051 176.129 1.00 33.21  ? 470  PHE A N     1 
ATOM   3635 C  CA    . PHE A 1 469 ? 144.484 160.442 177.248 1.00 33.21  ? 470  PHE A CA    1 
ATOM   3636 C  C     . PHE A 1 469 ? 145.601 159.680 176.582 1.00 33.21  ? 470  PHE A C     1 
ATOM   3637 O  O     . PHE A 1 469 ? 145.734 158.465 176.728 1.00 33.21  ? 470  PHE A O     1 
ATOM   3638 C  CB    . PHE A 1 469 ? 143.672 159.468 178.084 1.00 33.21  ? 470  PHE A CB    1 
ATOM   3639 C  CG    . PHE A 1 469 ? 144.485 158.903 179.218 1.00 33.21  ? 470  PHE A CG    1 
ATOM   3640 C  CD1   . PHE A 1 469 ? 145.081 159.746 180.137 1.00 33.21  ? 470  PHE A CD1   1 
ATOM   3641 C  CD2   . PHE A 1 469 ? 144.711 157.542 179.326 1.00 33.21  ? 470  PHE A CD2   1 
ATOM   3642 C  CE1   . PHE A 1 469 ? 145.855 159.234 181.163 1.00 33.21  ? 470  PHE A CE1   1 
ATOM   3643 C  CE2   . PHE A 1 469 ? 145.487 157.031 180.351 1.00 33.21  ? 470  PHE A CE2   1 
ATOM   3644 C  CZ    . PHE A 1 469 ? 146.057 157.879 181.268 1.00 33.21  ? 470  PHE A CZ    1 
ATOM   3645 N  N     . ASN A 1 470 ? 146.394 160.417 175.853 1.00 31.62  ? 471  ASN A N     1 
ATOM   3646 C  CA    . ASN A 1 470 ? 147.423 159.799 175.021 1.00 31.62  ? 471  ASN A CA    1 
ATOM   3647 C  C     . ASN A 1 470 ? 148.469 159.142 175.909 1.00 31.62  ? 471  ASN A C     1 
ATOM   3648 O  O     . ASN A 1 470 ? 149.492 159.733 176.242 1.00 31.62  ? 471  ASN A O     1 
ATOM   3649 C  CB    . ASN A 1 470 ? 148.047 160.833 174.097 1.00 31.62  ? 471  ASN A CB    1 
ATOM   3650 C  CG    . ASN A 1 470 ? 147.016 161.699 173.423 1.00 31.62  ? 471  ASN A CG    1 
ATOM   3651 O  OD1   . ASN A 1 470 ? 147.020 162.916 173.569 1.00 31.62  ? 471  ASN A OD1   1 
ATOM   3652 N  ND2   . ASN A 1 470 ? 146.128 161.075 172.671 1.00 31.62  ? 471  ASN A ND2   1 
ATOM   3653 N  N     . SER A 1 471 ? 148.222 157.903 176.297 1.00 30.00  ? 472  SER A N     1 
ATOM   3654 C  CA    . SER A 1 471 ? 149.187 157.179 177.109 1.00 30.00  ? 472  SER A CA    1 
ATOM   3655 C  C     . SER A 1 471 ? 150.206 156.500 176.199 1.00 30.00  ? 472  SER A C     1 
ATOM   3656 O  O     . SER A 1 471 ? 150.255 156.761 174.995 1.00 30.00  ? 472  SER A O     1 
ATOM   3657 C  CB    . SER A 1 471 ? 148.490 156.180 178.023 1.00 30.00  ? 472  SER A CB    1 
ATOM   3658 O  OG    . SER A 1 471 ? 149.354 155.785 179.075 1.00 30.00  ? 472  SER A OG    1 
ATOM   3659 N  N     . PHE A 1 472 ? 151.080 155.684 176.803 1.00 28.35  ? 473  PHE A N     1 
ATOM   3660 C  CA    . PHE A 1 472 ? 152.176 155.010 176.105 1.00 28.35  ? 473  PHE A CA    1 
ATOM   3661 C  C     . PHE A 1 472 ? 151.705 154.188 174.913 1.00 28.35  ? 473  PHE A C     1 
ATOM   3662 O  O     . PHE A 1 472 ? 152.417 154.091 173.909 1.00 28.35  ? 473  PHE A O     1 
ATOM   3663 C  CB    . PHE A 1 472 ? 152.938 154.132 177.092 1.00 28.35  ? 473  PHE A CB    1 
ATOM   3664 C  CG    . PHE A 1 472 ? 154.038 153.327 176.476 1.00 28.35  ? 473  PHE A CG    1 
ATOM   3665 C  CD1   . PHE A 1 472 ? 155.164 153.943 175.974 1.00 28.35  ? 473  PHE A CD1   1 
ATOM   3666 C  CD2   . PHE A 1 472 ? 153.961 151.950 176.436 1.00 28.35  ? 473  PHE A CD2   1 
ATOM   3667 C  CE1   . PHE A 1 472 ? 156.182 153.202 175.421 1.00 28.35  ? 473  PHE A CE1   1 
ATOM   3668 C  CE2   . PHE A 1 472 ? 154.977 151.207 175.885 1.00 28.35  ? 473  PHE A CE2   1 
ATOM   3669 C  CZ    . PHE A 1 472 ? 156.090 151.835 175.383 1.00 28.35  ? 473  PHE A CZ    1 
ATOM   3670 N  N     . GLU A 1 473 ? 150.505 153.605 174.995 1.00 27.70  ? 474  GLU A N     1 
ATOM   3671 C  CA    . GLU A 1 473 ? 149.922 152.833 173.900 1.00 27.70  ? 474  GLU A CA    1 
ATOM   3672 C  C     . GLU A 1 473 ? 149.607 153.668 172.665 1.00 27.70  ? 474  GLU A C     1 
ATOM   3673 O  O     . GLU A 1 473 ? 149.267 153.092 171.630 1.00 27.70  ? 474  GLU A O     1 
ATOM   3674 C  CB    . GLU A 1 473 ? 148.632 152.146 174.343 1.00 27.70  ? 474  GLU A CB    1 
ATOM   3675 C  CG    . GLU A 1 473 ? 148.747 151.249 175.549 1.00 27.70  ? 474  GLU A CG    1 
ATOM   3676 C  CD    . GLU A 1 473 ? 148.356 151.967 176.812 1.00 27.70  ? 474  GLU A CD    1 
ATOM   3677 O  OE1   . GLU A 1 473 ? 149.063 152.920 177.193 1.00 27.70  ? 474  GLU A OE1   1 
ATOM   3678 O  OE2   . GLU A 1 473 ? 147.317 151.609 177.401 1.00 27.70  ? 474  GLU A OE2   1 
ATOM   3679 N  N     . GLN A 1 474 ? 149.665 154.994 172.752 1.00 27.33  ? 475  GLN A N     1 
ATOM   3680 C  CA    . GLN A 1 474 ? 149.558 155.846 171.583 1.00 27.33  ? 475  GLN A CA    1 
ATOM   3681 C  C     . GLN A 1 474 ? 150.885 156.420 171.128 1.00 27.33  ? 475  GLN A C     1 
ATOM   3682 O  O     . GLN A 1 474 ? 150.937 157.020 170.055 1.00 27.33  ? 475  GLN A O     1 
ATOM   3683 C  CB    . GLN A 1 474 ? 148.609 157.004 171.845 1.00 27.33  ? 475  GLN A CB    1 
ATOM   3684 C  CG    . GLN A 1 474 ? 147.244 156.577 172.201 1.00 27.33  ? 475  GLN A CG    1 
ATOM   3685 C  CD    . GLN A 1 474 ? 146.246 157.586 171.762 1.00 27.33  ? 475  GLN A CD    1 
ATOM   3686 O  OE1   . GLN A 1 474 ? 146.331 158.758 172.109 1.00 27.33  ? 475  GLN A OE1   1 
ATOM   3687 N  NE2   . GLN A 1 474 ? 145.290 157.145 170.977 1.00 27.33  ? 475  GLN A NE2   1 
ATOM   3688 N  N     . LEU A 1 475 ? 151.946 156.285 171.913 1.00 24.80  ? 476  LEU A N     1 
ATOM   3689 C  CA    . LEU A 1 475 ? 153.242 156.668 171.379 1.00 24.80  ? 476  LEU A CA    1 
ATOM   3690 C  C     . LEU A 1 475 ? 153.740 155.618 170.406 1.00 24.80  ? 476  LEU A C     1 
ATOM   3691 O  O     . LEU A 1 475 ? 154.303 155.956 169.365 1.00 24.80  ? 476  LEU A O     1 
ATOM   3692 C  CB    . LEU A 1 475 ? 154.248 156.869 172.506 1.00 24.80  ? 476  LEU A CB    1 
ATOM   3693 C  CG    . LEU A 1 475 ? 155.575 157.473 172.068 1.00 24.80  ? 476  LEU A CG    1 
ATOM   3694 C  CD1   . LEU A 1 475 ? 155.382 158.944 171.855 1.00 24.80  ? 476  LEU A CD1   1 
ATOM   3695 C  CD2   . LEU A 1 475 ? 156.651 157.217 173.097 1.00 24.80  ? 476  LEU A CD2   1 
ATOM   3696 N  N     . CYS A 1 476 ? 153.535 154.346 170.738 1.00 24.47  ? 477  CYS A N     1 
ATOM   3697 C  CA    . CYS A 1 476 ? 153.975 153.244 169.891 1.00 24.47  ? 477  CYS A CA    1 
ATOM   3698 C  C     . CYS A 1 476 ? 153.224 153.210 168.565 1.00 24.47  ? 477  CYS A C     1 
ATOM   3699 O  O     . CYS A 1 476 ? 153.795 152.850 167.530 1.00 24.47  ? 477  CYS A O     1 
ATOM   3700 C  CB    . CYS A 1 476 ? 153.796 151.931 170.635 1.00 24.47  ? 477  CYS A CB    1 
ATOM   3701 S  SG    . CYS A 1 476 ? 154.691 151.835 172.180 1.00 24.47  ? 477  CYS A SG    1 
ATOM   3702 N  N     . ILE A 1 477 ? 151.936 153.546 168.586 1.00 22.90  ? 478  ILE A N     1 
ATOM   3703 C  CA    . ILE A 1 477 ? 151.141 153.589 167.364 1.00 22.90  ? 478  ILE A CA    1 
ATOM   3704 C  C     . ILE A 1 477 ? 151.494 154.803 166.508 1.00 22.90  ? 478  ILE A C     1 
ATOM   3705 O  O     . ILE A 1 477 ? 151.636 154.692 165.285 1.00 22.90  ? 478  ILE A O     1 
ATOM   3706 C  CB    . ILE A 1 477 ? 149.647 153.567 167.736 1.00 22.90  ? 478  ILE A CB    1 
ATOM   3707 C  CG1   . ILE A 1 477 ? 149.267 152.249 168.427 1.00 22.90  ? 478  ILE A CG1   1 
ATOM   3708 C  CG2   . ILE A 1 477 ? 148.776 153.805 166.536 1.00 22.90  ? 478  ILE A CG2   1 
ATOM   3709 C  CD1   . ILE A 1 477 ? 149.772 150.990 167.743 1.00 22.90  ? 478  ILE A CD1   1 
ATOM   3710 N  N     . ASN A 1 478 ? 151.653 155.976 167.127 1.00 21.19  ? 479  ASN A N     1 
ATOM   3711 C  CA    . ASN A 1 478 ? 152.048 157.174 166.385 1.00 21.19  ? 479  ASN A CA    1 
ATOM   3712 C  C     . ASN A 1 478 ? 153.498 157.156 165.914 1.00 21.19  ? 479  ASN A C     1 
ATOM   3713 O  O     . ASN A 1 478 ? 153.816 157.804 164.914 1.00 21.19  ? 479  ASN A O     1 
ATOM   3714 C  CB    . ASN A 1 478 ? 151.813 158.412 167.234 1.00 21.19  ? 479  ASN A CB    1 
ATOM   3715 C  CG    . ASN A 1 478 ? 150.356 158.695 167.433 1.00 21.19  ? 479  ASN A CG    1 
ATOM   3716 O  OD1   . ASN A 1 478 ? 149.513 158.146 166.735 1.00 21.19  ? 479  ASN A OD1   1 
ATOM   3717 N  ND2   . ASN A 1 478 ? 150.044 159.548 168.396 1.00 21.19  ? 479  ASN A ND2   1 
ATOM   3718 N  N     . PHE A 1 479 ? 154.399 156.483 166.629 1.00 19.51  ? 480  PHE A N     1 
ATOM   3719 C  CA    . PHE A 1 479 ? 155.757 156.311 166.118 1.00 19.51  ? 480  PHE A CA    1 
ATOM   3720 C  C     . PHE A 1 479 ? 155.790 155.417 164.885 1.00 19.51  ? 480  PHE A C     1 
ATOM   3721 O  O     . PHE A 1 479 ? 156.580 155.656 163.967 1.00 19.51  ? 480  PHE A O     1 
ATOM   3722 C  CB    . PHE A 1 479 ? 156.658 155.749 167.209 1.00 19.51  ? 480  PHE A CB    1 
ATOM   3723 C  CG    . PHE A 1 479 ? 158.022 155.357 166.744 1.00 19.51  ? 480  PHE A CG    1 
ATOM   3724 C  CD1   . PHE A 1 479 ? 158.853 156.279 166.144 1.00 19.51  ? 480  PHE A CD1   1 
ATOM   3725 C  CD2   . PHE A 1 479 ? 158.484 154.068 166.926 1.00 19.51  ? 480  PHE A CD2   1 
ATOM   3726 C  CE1   . PHE A 1 479 ? 160.117 155.918 165.732 1.00 19.51  ? 480  PHE A CE1   1 
ATOM   3727 C  CE2   . PHE A 1 479 ? 159.745 153.704 166.513 1.00 19.51  ? 480  PHE A CE2   1 
ATOM   3728 C  CZ    . PHE A 1 479 ? 160.560 154.631 165.917 1.00 19.51  ? 480  PHE A CZ    1 
ATOM   3729 N  N     . THR A 1 480 ? 154.974 154.357 164.868 1.00 21.26  ? 481  THR A N     1 
ATOM   3730 C  CA    . THR A 1 480 ? 154.884 153.475 163.704 1.00 21.26  ? 481  THR A CA    1 
ATOM   3731 C  C     . THR A 1 480 ? 154.410 154.215 162.455 1.00 21.26  ? 481  THR A C     1 
ATOM   3732 O  O     . THR A 1 480 ? 154.922 153.970 161.357 1.00 21.26  ? 481  THR A O     1 
ATOM   3733 C  CB    . THR A 1 480 ? 153.963 152.297 164.018 1.00 21.26  ? 481  THR A CB    1 
ATOM   3734 O  OG1   . THR A 1 480 ? 154.404 151.666 165.223 1.00 21.26  ? 481  THR A OG1   1 
ATOM   3735 C  CG2   . THR A 1 480 ? 154.019 151.267 162.913 1.00 21.26  ? 481  THR A CG2   1 
ATOM   3736 N  N     . ASN A 1 481 ? 153.422 155.104 162.598 1.00 20.94  ? 482  ASN A N     1 
ATOM   3737 C  CA    . ASN A 1 481 ? 153.005 155.959 161.487 1.00 20.94  ? 482  ASN A CA    1 
ATOM   3738 C  C     . ASN A 1 481 ? 154.143 156.844 161.001 1.00 20.94  ? 482  ASN A C     1 
ATOM   3739 O  O     . ASN A 1 481 ? 154.361 156.978 159.794 1.00 20.94  ? 482  ASN A O     1 
ATOM   3740 C  CB    . ASN A 1 481 ? 151.811 156.820 161.886 1.00 20.94  ? 482  ASN A CB    1 
ATOM   3741 C  CG    . ASN A 1 481 ? 150.517 156.053 161.890 1.00 20.94  ? 482  ASN A CG    1 
ATOM   3742 O  OD1   . ASN A 1 481 ? 149.788 156.050 160.903 1.00 20.94  ? 482  ASN A OD1   1 
ATOM   3743 N  ND2   . ASN A 1 481 ? 150.215 155.407 163.003 1.00 20.94  ? 482  ASN A ND2   1 
ATOM   3744 N  N     . GLU A 1 482 ? 154.859 157.475 161.930 1.00 22.32  ? 483  GLU A N     1 
ATOM   3745 C  CA    . GLU A 1 482 ? 155.918 158.409 161.568 1.00 22.32  ? 483  GLU A CA    1 
ATOM   3746 C  C     . GLU A 1 482 ? 157.080 157.727 160.859 1.00 22.32  ? 483  GLU A C     1 
ATOM   3747 O  O     . GLU A 1 482 ? 157.729 158.345 160.012 1.00 22.32  ? 483  GLU A O     1 
ATOM   3748 C  CB    . GLU A 1 482 ? 156.432 159.109 162.818 1.00 22.32  ? 483  GLU A CB    1 
ATOM   3749 C  CG    . GLU A 1 482 ? 157.308 160.292 162.552 1.00 22.32  ? 483  GLU A CG    1 
ATOM   3750 C  CD    . GLU A 1 482 ? 157.458 161.162 163.765 1.00 22.32  ? 483  GLU A CD    1 
ATOM   3751 O  OE1   . GLU A 1 482 ? 156.621 162.066 163.959 1.00 22.32  ? 483  GLU A OE1   1 
ATOM   3752 O  OE2   . GLU A 1 482 ? 158.423 160.936 164.523 1.00 22.32  ? 483  GLU A OE2   1 
ATOM   3753 N  N     . LYS A 1 483 ? 157.359 156.464 161.179 1.00 19.92  ? 484  LYS A N     1 
ATOM   3754 C  CA    . LYS A 1 483 ? 158.330 155.709 160.393 1.00 19.92  ? 484  LYS A CA    1 
ATOM   3755 C  C     . LYS A 1 483 ? 157.801 155.343 159.014 1.00 19.92  ? 484  LYS A C     1 
ATOM   3756 O  O     . LYS A 1 483 ? 158.542 155.411 158.027 1.00 19.92  ? 484  LYS A O     1 
ATOM   3757 C  CB    . LYS A 1 483 ? 158.755 154.447 161.135 1.00 19.92  ? 484  LYS A CB    1 
ATOM   3758 C  CG    . LYS A 1 483 ? 159.615 154.690 162.342 1.00 19.92  ? 484  LYS A CG    1 
ATOM   3759 C  CD    . LYS A 1 483 ? 160.658 153.604 162.480 1.00 19.92  ? 484  LYS A CD    1 
ATOM   3760 C  CE    . LYS A 1 483 ? 161.696 153.687 161.388 1.00 19.92  ? 484  LYS A CE    1 
ATOM   3761 N  NZ    . LYS A 1 483 ? 162.951 152.981 161.764 1.00 19.92  ? 484  LYS A NZ    1 
ATOM   3762 N  N     . LEU A 1 484 ? 156.542 154.913 158.927 1.00 18.04  ? 485  LEU A N     1 
ATOM   3763 C  CA    . LEU A 1 484 ? 156.006 154.463 157.646 1.00 18.04  ? 485  LEU A CA    1 
ATOM   3764 C  C     . LEU A 1 484 ? 155.785 155.605 156.657 1.00 18.04  ? 485  LEU A C     1 
ATOM   3765 O  O     . LEU A 1 484 ? 155.938 155.403 155.449 1.00 18.04  ? 485  LEU A O     1 
ATOM   3766 C  CB    . LEU A 1 484 ? 154.720 153.672 157.866 1.00 18.04  ? 485  LEU A CB    1 
ATOM   3767 C  CG    . LEU A 1 484 ? 154.193 152.950 156.632 1.00 18.04  ? 485  LEU A CG    1 
ATOM   3768 C  CD1   . LEU A 1 484 ? 155.232 151.956 156.187 1.00 18.04  ? 485  LEU A CD1   1 
ATOM   3769 C  CD2   . LEU A 1 484 ? 152.932 152.233 156.951 1.00 18.04  ? 485  LEU A CD2   1 
ATOM   3770 N  N     . GLN A 1 485 ? 155.444 156.806 157.123 1.00 19.12  ? 486  GLN A N     1 
ATOM   3771 C  CA    . GLN A 1 485 ? 155.469 157.938 156.202 1.00 19.12  ? 486  GLN A CA    1 
ATOM   3772 C  C     . GLN A 1 485 ? 156.896 158.300 155.808 1.00 19.12  ? 486  GLN A C     1 
ATOM   3773 O  O     . GLN A 1 485 ? 157.159 158.604 154.639 1.00 19.12  ? 486  GLN A O     1 
ATOM   3774 C  CB    . GLN A 1 485 ? 154.732 159.139 156.783 1.00 19.12  ? 486  GLN A CB    1 
ATOM   3775 C  CG    . GLN A 1 485 ? 154.873 160.365 155.919 1.00 19.12  ? 486  GLN A CG    1 
ATOM   3776 C  CD    . GLN A 1 485 ? 153.634 161.185 155.847 1.00 19.12  ? 486  GLN A CD    1 
ATOM   3777 O  OE1   . GLN A 1 485 ? 152.540 160.656 155.668 1.00 19.12  ? 486  GLN A OE1   1 
ATOM   3778 N  NE2   . GLN A 1 485 ? 153.790 162.495 155.947 1.00 19.12  ? 486  GLN A NE2   1 
ATOM   3779 N  N     . GLN A 1 486 ? 157.835 158.270 156.759 1.00 19.56  ? 487  GLN A N     1 
ATOM   3780 C  CA    . GLN A 1 486 ? 159.244 158.480 156.423 1.00 19.56  ? 487  GLN A CA    1 
ATOM   3781 C  C     . GLN A 1 486 ? 159.771 157.430 155.446 1.00 19.56  ? 487  GLN A C     1 
ATOM   3782 O  O     . GLN A 1 486 ? 160.679 157.718 154.665 1.00 19.56  ? 487  GLN A O     1 
ATOM   3783 C  CB    . GLN A 1 486 ? 160.091 158.512 157.694 1.00 19.56  ? 487  GLN A CB    1 
ATOM   3784 C  CG    . GLN A 1 486 ? 161.567 158.851 157.496 1.00 19.56  ? 487  GLN A CG    1 
ATOM   3785 C  CD    . GLN A 1 486 ? 161.823 160.253 156.968 1.00 19.56  ? 487  GLN A CD    1 
ATOM   3786 O  OE1   . GLN A 1 486 ? 160.961 161.129 157.016 1.00 19.56  ? 487  GLN A OE1   1 
ATOM   3787 N  NE2   . GLN A 1 486 ? 163.019 160.461 156.433 1.00 19.56  ? 487  GLN A NE2   1 
ATOM   3788 N  N     . PHE A 1 487 ? 159.205 156.222 155.453 1.00 17.95  ? 488  PHE A N     1 
ATOM   3789 C  CA    . PHE A 1 487 ? 159.483 155.267 154.383 1.00 17.95  ? 488  PHE A CA    1 
ATOM   3790 C  C     . PHE A 1 487 ? 158.960 155.771 153.042 1.00 17.95  ? 488  PHE A C     1 
ATOM   3791 O  O     . PHE A 1 487 ? 159.642 155.658 152.018 1.00 17.95  ? 488  PHE A O     1 
ATOM   3792 C  CB    . PHE A 1 487 ? 158.870 153.911 154.722 1.00 17.95  ? 488  PHE A CB    1 
ATOM   3793 C  CG    . PHE A 1 487 ? 159.142 152.853 153.705 1.00 17.95  ? 488  PHE A CG    1 
ATOM   3794 C  CD1   . PHE A 1 487 ? 160.318 152.138 153.747 1.00 17.95  ? 488  PHE A CD1   1 
ATOM   3795 C  CD2   . PHE A 1 487 ? 158.209 152.541 152.737 1.00 17.95  ? 488  PHE A CD2   1 
ATOM   3796 C  CE1   . PHE A 1 487 ? 160.573 151.156 152.823 1.00 17.95  ? 488  PHE A CE1   1 
ATOM   3797 C  CE2   . PHE A 1 487 ? 158.466 151.565 151.808 1.00 17.95  ? 488  PHE A CE2   1 
ATOM   3798 C  CZ    . PHE A 1 487 ? 159.644 150.867 151.855 1.00 17.95  ? 488  PHE A CZ    1 
ATOM   3799 N  N     . PHE A 1 488 ? 157.725 156.276 153.025 1.00 16.82  ? 489  PHE A N     1 
ATOM   3800 C  CA    . PHE A 1 488 ? 157.146 156.868 151.822 1.00 16.82  ? 489  PHE A CA    1 
ATOM   3801 C  C     . PHE A 1 488 ? 157.954 158.070 151.345 1.00 16.82  ? 489  PHE A C     1 
ATOM   3802 O  O     . PHE A 1 488 ? 158.318 158.145 150.168 1.00 16.82  ? 489  PHE A O     1 
ATOM   3803 C  CB    . PHE A 1 488 ? 155.682 157.230 152.093 1.00 16.82  ? 489  PHE A CB    1 
ATOM   3804 C  CG    . PHE A 1 488 ? 155.056 158.150 151.083 1.00 16.82  ? 489  PHE A CG    1 
ATOM   3805 C  CD1   . PHE A 1 488 ? 154.504 157.648 149.925 1.00 16.82  ? 489  PHE A CD1   1 
ATOM   3806 C  CD2   . PHE A 1 488 ? 154.926 159.504 151.340 1.00 16.82  ? 489  PHE A CD2   1 
ATOM   3807 C  CE1   . PHE A 1 488 ? 153.898 158.487 149.014 1.00 16.82  ? 489  PHE A CE1   1 
ATOM   3808 C  CE2   . PHE A 1 488 ? 154.325 160.343 150.431 1.00 16.82  ? 489  PHE A CE2   1 
ATOM   3809 C  CZ    . PHE A 1 488 ? 153.810 159.833 149.271 1.00 16.82  ? 489  PHE A CZ    1 
ATOM   3810 N  N     . ASN A 1 489 ? 158.211 159.034 152.241 1.00 17.57  ? 490  ASN A N     1 
ATOM   3811 C  CA    . ASN A 1 489 ? 159.040 160.197 151.916 1.00 17.57  ? 490  ASN A CA    1 
ATOM   3812 C  C     . ASN A 1 489 ? 160.434 159.815 151.437 1.00 17.57  ? 490  ASN A C     1 
ATOM   3813 O  O     . ASN A 1 489 ? 161.003 160.500 150.583 1.00 17.57  ? 490  ASN A O     1 
ATOM   3814 C  CB    . ASN A 1 489 ? 159.153 161.135 153.113 1.00 17.57  ? 490  ASN A CB    1 
ATOM   3815 C  CG    . ASN A 1 489 ? 157.880 161.889 153.386 1.00 17.57  ? 490  ASN A CG    1 
ATOM   3816 O  OD1   . ASN A 1 489 ? 157.743 162.547 154.413 1.00 17.57  ? 490  ASN A OD1   1 
ATOM   3817 N  ND2   . ASN A 1 489 ? 156.944 161.816 152.458 1.00 17.57  ? 490  ASN A ND2   1 
ATOM   3818 N  N     . HIS A 1 490 ? 161.029 158.770 152.008 1.00 17.76  ? 491  HIS A N     1 
ATOM   3819 C  CA    . HIS A 1 490 ? 162.317 158.319 151.494 1.00 17.76  ? 491  HIS A CA    1 
ATOM   3820 C  C     . HIS A 1 490 ? 162.189 157.709 150.110 1.00 17.76  ? 491  HIS A C     1 
ATOM   3821 O  O     . HIS A 1 490 ? 163.048 157.930 149.252 1.00 17.76  ? 491  HIS A O     1 
ATOM   3822 C  CB    . HIS A 1 490 ? 162.966 157.315 152.433 1.00 17.76  ? 491  HIS A CB    1 
ATOM   3823 C  CG    . HIS A 1 490 ? 164.340 156.911 152.012 1.00 17.76  ? 491  HIS A CG    1 
ATOM   3824 N  ND1   . HIS A 1 490 ? 164.585 155.783 151.262 1.00 17.76  ? 491  HIS A ND1   1 
ATOM   3825 C  CD2   . HIS A 1 490 ? 165.543 157.491 152.226 1.00 17.76  ? 491  HIS A CD2   1 
ATOM   3826 C  CE1   . HIS A 1 490 ? 165.882 155.680 151.038 1.00 17.76  ? 491  HIS A CE1   1 
ATOM   3827 N  NE2   . HIS A 1 490 ? 166.486 156.704 151.613 1.00 17.76  ? 491  HIS A NE2   1 
ATOM   3828 N  N     . HIS A 1 491 ? 161.159 156.896 149.888 1.00 17.32  ? 492  HIS A N     1 
ATOM   3829 C  CA    . HIS A 1 491 ? 160.995 156.248 148.591 1.00 17.32  ? 492  HIS A CA    1 
ATOM   3830 C  C     . HIS A 1 491 ? 160.626 157.232 147.488 1.00 17.32  ? 492  HIS A C     1 
ATOM   3831 O  O     . HIS A 1 491 ? 161.259 157.254 146.429 1.00 17.32  ? 492  HIS A O     1 
ATOM   3832 C  CB    . HIS A 1 491 ? 159.947 155.147 148.691 1.00 17.32  ? 492  HIS A CB    1 
ATOM   3833 C  CG    . HIS A 1 491 ? 159.797 154.349 147.438 1.00 17.32  ? 492  HIS A CG    1 
ATOM   3834 N  ND1   . HIS A 1 491 ? 160.604 153.274 147.143 1.00 17.32  ? 492  HIS A ND1   1 
ATOM   3835 C  CD2   . HIS A 1 491 ? 158.933 154.468 146.405 1.00 17.32  ? 492  HIS A CD2   1 
ATOM   3836 C  CE1   . HIS A 1 491 ? 160.249 152.772 145.975 1.00 17.32  ? 492  HIS A CE1   1 
ATOM   3837 N  NE2   . HIS A 1 491 ? 159.233 153.474 145.510 1.00 17.32  ? 492  HIS A NE2   1 
ATOM   3838 N  N     . MET A 1 492 ? 159.611 158.056 147.710 1.00 17.04  ? 493  MET A N     1 
ATOM   3839 C  CA    . MET A 1 492 ? 159.144 158.924 146.638 1.00 17.04  ? 493  MET A CA    1 
ATOM   3840 C  C     . MET A 1 492 ? 160.009 160.157 146.418 1.00 17.04  ? 493  MET A C     1 
ATOM   3841 O  O     . MET A 1 492 ? 160.074 160.655 145.294 1.00 17.04  ? 493  MET A O     1 
ATOM   3842 C  CB    . MET A 1 492 ? 157.697 159.346 146.887 1.00 17.04  ? 493  MET A CB    1 
ATOM   3843 C  CG    . MET A 1 492 ? 156.717 158.199 146.805 1.00 17.04  ? 493  MET A CG    1 
ATOM   3844 S  SD    . MET A 1 492 ? 156.538 157.571 145.131 1.00 17.04  ? 493  MET A SD    1 
ATOM   3845 C  CE    . MET A 1 492 ? 155.440 156.184 145.394 1.00 17.04  ? 493  MET A CE    1 
ATOM   3846 N  N     . PHE A 1 493 ? 160.638 160.709 147.450 1.00 17.42  ? 494  PHE A N     1 
ATOM   3847 C  CA    . PHE A 1 493 ? 161.224 162.030 147.293 1.00 17.42  ? 494  PHE A CA    1 
ATOM   3848 C  C     . PHE A 1 493 ? 162.740 162.075 147.378 1.00 17.42  ? 494  PHE A C     1 
ATOM   3849 O  O     . PHE A 1 493 ? 163.327 163.069 146.949 1.00 17.42  ? 494  PHE A O     1 
ATOM   3850 C  CB    . PHE A 1 493 ? 160.655 163.004 148.332 1.00 17.42  ? 494  PHE A CB    1 
ATOM   3851 C  CG    . PHE A 1 493 ? 159.161 163.104 148.324 1.00 17.42  ? 494  PHE A CG    1 
ATOM   3852 C  CD1   . PHE A 1 493 ? 158.451 163.068 147.143 1.00 17.42  ? 494  PHE A CD1   1 
ATOM   3853 C  CD2   . PHE A 1 493 ? 158.466 163.257 149.507 1.00 17.42  ? 494  PHE A CD2   1 
ATOM   3854 C  CE1   . PHE A 1 493 ? 157.077 163.159 147.146 1.00 17.42  ? 494  PHE A CE1   1 
ATOM   3855 C  CE2   . PHE A 1 493 ? 157.093 163.354 149.514 1.00 17.42  ? 494  PHE A CE2   1 
ATOM   3856 C  CZ    . PHE A 1 493 ? 156.401 163.305 148.334 1.00 17.42  ? 494  PHE A CZ    1 
ATOM   3857 N  N     . VAL A 1 494 ? 163.391 161.059 147.922 1.00 18.28  ? 495  VAL A N     1 
ATOM   3858 C  CA    . VAL A 1 494 ? 164.844 161.050 148.066 1.00 18.28  ? 495  VAL A CA    1 
ATOM   3859 C  C     . VAL A 1 494 ? 165.478 159.995 147.169 1.00 18.28  ? 495  VAL A C     1 
ATOM   3860 O  O     . VAL A 1 494 ? 166.399 160.293 146.409 1.00 18.28  ? 495  VAL A O     1 
ATOM   3861 C  CB    . VAL A 1 494 ? 165.262 160.862 149.539 1.00 18.28  ? 495  VAL A CB    1 
ATOM   3862 C  CG1   . VAL A 1 494 ? 166.758 160.985 149.665 1.00 18.28  ? 495  VAL A CG1   1 
ATOM   3863 C  CG2   . VAL A 1 494 ? 164.576 161.890 150.415 1.00 18.28  ? 495  VAL A CG2   1 
ATOM   3864 N  N     . LEU A 1 495 ? 165.044 158.739 147.297 1.00 19.95  ? 496  LEU A N     1 
ATOM   3865 C  CA    . LEU A 1 495 ? 165.555 157.657 146.457 1.00 19.95  ? 496  LEU A CA    1 
ATOM   3866 C  C     . LEU A 1 495 ? 165.236 157.887 144.982 1.00 19.95  ? 496  LEU A C     1 
ATOM   3867 O  O     . LEU A 1 495 ? 166.042 157.558 144.106 1.00 19.95  ? 496  LEU A O     1 
ATOM   3868 C  CB    . LEU A 1 495 ? 164.976 156.328 146.933 1.00 19.95  ? 496  LEU A CB    1 
ATOM   3869 C  CG    . LEU A 1 495 ? 165.405 155.054 146.218 1.00 19.95  ? 496  LEU A CG    1 
ATOM   3870 C  CD1   . LEU A 1 495 ? 166.907 154.881 146.322 1.00 19.95  ? 496  LEU A CD1   1 
ATOM   3871 C  CD2   . LEU A 1 495 ? 164.691 153.859 146.816 1.00 19.95  ? 496  LEU A CD2   1 
ATOM   3872 N  N     . GLU A 1 496 ? 164.057 158.442 144.690 1.00 22.16  ? 497  GLU A N     1 
ATOM   3873 C  CA    . GLU A 1 496 ? 163.697 158.873 143.339 1.00 22.16  ? 497  GLU A CA    1 
ATOM   3874 C  C     . GLU A 1 496 ? 164.573 160.020 142.824 1.00 22.16  ? 497  GLU A C     1 
ATOM   3875 O  O     . GLU A 1 496 ? 164.609 160.265 141.616 1.00 22.16  ? 497  GLU A O     1 
ATOM   3876 C  CB    . GLU A 1 496 ? 162.211 159.242 143.327 1.00 22.16  ? 497  GLU A CB    1 
ATOM   3877 C  CG    . GLU A 1 496 ? 161.553 159.486 141.981 1.00 22.16  ? 497  GLU A CG    1 
ATOM   3878 C  CD    . GLU A 1 496 ? 160.128 158.971 141.941 1.00 22.16  ? 497  GLU A CD    1 
ATOM   3879 O  OE1   . GLU A 1 496 ? 159.490 158.904 143.008 1.00 22.16  ? 497  GLU A OE1   1 
ATOM   3880 O  OE2   . GLU A 1 496 ? 159.642 158.626 140.847 1.00 22.16  ? 497  GLU A OE2   1 
ATOM   3881 N  N     . GLN A 1 497 ? 165.310 160.707 143.695 1.00 22.93  ? 498  GLN A N     1 
ATOM   3882 C  CA    . GLN A 1 497 ? 166.236 161.745 143.271 1.00 22.93  ? 498  GLN A CA    1 
ATOM   3883 C  C     . GLN A 1 497 ? 167.694 161.348 143.452 1.00 22.93  ? 498  GLN A C     1 
ATOM   3884 O  O     . GLN A 1 497 ? 168.578 162.082 143.004 1.00 22.93  ? 498  GLN A O     1 
ATOM   3885 C  CB    . GLN A 1 497 ? 165.972 163.046 144.036 1.00 22.93  ? 498  GLN A CB    1 
ATOM   3886 C  CG    . GLN A 1 497 ? 164.592 163.610 143.834 1.00 22.93  ? 498  GLN A CG    1 
ATOM   3887 C  CD    . GLN A 1 497 ? 164.487 165.041 144.303 1.00 22.93  ? 498  GLN A CD    1 
ATOM   3888 O  OE1   . GLN A 1 497 ? 164.842 165.968 143.584 1.00 22.93  ? 498  GLN A OE1   1 
ATOM   3889 N  NE2   . GLN A 1 497 ? 164.008 165.228 145.522 1.00 22.93  ? 498  GLN A NE2   1 
ATOM   3890 N  N     . GLU A 1 498 ? 167.965 160.229 144.122 1.00 25.87  ? 499  GLU A N     1 
ATOM   3891 C  CA    . GLU A 1 498 ? 169.299 159.640 144.104 1.00 25.87  ? 499  GLU A CA    1 
ATOM   3892 C  C     . GLU A 1 498 ? 169.526 158.845 142.829 1.00 25.87  ? 499  GLU A C     1 
ATOM   3893 O  O     . GLU A 1 498 ? 170.647 158.799 142.318 1.00 25.87  ? 499  GLU A O     1 
ATOM   3894 C  CB    . GLU A 1 498 ? 169.512 158.732 145.315 1.00 25.87  ? 499  GLU A CB    1 
ATOM   3895 C  CG    . GLU A 1 498 ? 169.663 159.435 146.648 1.00 25.87  ? 499  GLU A CG    1 
ATOM   3896 C  CD    . GLU A 1 498 ? 169.842 158.451 147.792 1.00 25.87  ? 499  GLU A CD    1 
ATOM   3897 O  OE1   . GLU A 1 498 ? 169.639 158.841 148.960 1.00 25.87  ? 499  GLU A OE1   1 
ATOM   3898 O  OE2   . GLU A 1 498 ? 170.177 157.280 147.522 1.00 25.87  ? 499  GLU A OE2   1 
ATOM   3899 N  N     . GLU A 1 499 ? 168.476 158.181 142.339 1.00 27.83  ? 500  GLU A N     1 
ATOM   3900 C  CA    . GLU A 1 499 ? 168.553 157.404 141.104 1.00 27.83  ? 500  GLU A CA    1 
ATOM   3901 C  C     . GLU A 1 499 ? 168.902 158.267 139.899 1.00 27.83  ? 500  GLU A C     1 
ATOM   3902 O  O     . GLU A 1 499 ? 169.670 157.841 139.029 1.00 27.83  ? 500  GLU A O     1 
ATOM   3903 C  CB    . GLU A 1 499 ? 167.223 156.697 140.862 1.00 27.83  ? 500  GLU A CB    1 
ATOM   3904 C  CG    . GLU A 1 499 ? 167.198 155.803 139.646 1.00 27.83  ? 500  GLU A CG    1 
ATOM   3905 C  CD    . GLU A 1 499 ? 166.054 154.828 139.684 1.00 27.83  ? 500  GLU A CD    1 
ATOM   3906 O  OE1   . GLU A 1 499 ? 165.026 155.164 140.301 1.00 27.83  ? 500  GLU A OE1   1 
ATOM   3907 O  OE2   . GLU A 1 499 ? 166.174 153.733 139.098 1.00 27.83  ? 500  GLU A OE2   1 
ATOM   3908 N  N     . TYR A 1 500 ? 168.322 159.466 139.817 1.00 27.66  ? 501  TYR A N     1 
ATOM   3909 C  CA    . TYR A 1 500 ? 168.598 160.371 138.703 1.00 27.66  ? 501  TYR A CA    1 
ATOM   3910 C  C     . TYR A 1 500 ? 170.068 160.773 138.645 1.00 27.66  ? 501  TYR A C     1 
ATOM   3911 O  O     . TYR A 1 500 ? 170.696 160.705 137.583 1.00 27.66  ? 501  TYR A O     1 
ATOM   3912 C  CB    . TYR A 1 500 ? 167.715 161.618 138.795 1.00 27.66  ? 501  TYR A CB    1 
ATOM   3913 C  CG    . TYR A 1 500 ? 166.212 161.413 138.686 1.00 27.66  ? 501  TYR A CG    1 
ATOM   3914 C  CD1   . TYR A 1 500 ? 165.662 160.206 138.276 1.00 27.66  ? 501  TYR A CD1   1 
ATOM   3915 C  CD2   . TYR A 1 500 ? 165.345 162.442 139.010 1.00 27.66  ? 501  TYR A CD2   1 
ATOM   3916 C  CE1   . TYR A 1 500 ? 164.300 160.053 138.153 1.00 27.66  ? 501  TYR A CE1   1 
ATOM   3917 C  CE2   . TYR A 1 500 ? 163.984 162.286 138.919 1.00 27.66  ? 501  TYR A CE2   1 
ATOM   3918 C  CZ    . TYR A 1 500 ? 163.467 161.095 138.485 1.00 27.66  ? 501  TYR A CZ    1 
ATOM   3919 O  OH    . TYR A 1 500 ? 162.106 160.937 138.428 1.00 27.66  ? 501  TYR A OH    1 
ATOM   3920 N  N     . LYS A 1 501 ? 170.633 161.198 139.777 1.00 30.98  ? 502  LYS A N     1 
ATOM   3921 C  CA    . LYS A 1 501 ? 172.040 161.595 139.800 1.00 30.98  ? 502  LYS A CA    1 
ATOM   3922 C  C     . LYS A 1 501 ? 172.972 160.401 139.624 1.00 30.98  ? 502  LYS A C     1 
ATOM   3923 O  O     . LYS A 1 501 ? 174.051 160.540 139.038 1.00 30.98  ? 502  LYS A O     1 
ATOM   3924 C  CB    . LYS A 1 501 ? 172.351 162.356 141.087 1.00 30.98  ? 502  LYS A CB    1 
ATOM   3925 C  CG    . LYS A 1 501 ? 171.589 163.665 141.196 1.00 30.98  ? 502  LYS A CG    1 
ATOM   3926 C  CD    . LYS A 1 501 ? 172.095 164.534 142.333 1.00 30.98  ? 502  LYS A CD    1 
ATOM   3927 C  CE    . LYS A 1 501 ? 172.037 163.807 143.661 1.00 30.98  ? 502  LYS A CE    1 
ATOM   3928 N  NZ    . LYS A 1 501 ? 170.634 163.677 144.145 1.00 30.98  ? 502  LYS A NZ    1 
ATOM   3929 N  N     . LYS A 1 502 ? 172.598 159.239 140.168 1.00 32.13  ? 503  LYS A N     1 
ATOM   3930 C  CA    . LYS A 1 502 ? 173.387 158.024 139.969 1.00 32.13  ? 503  LYS A CA    1 
ATOM   3931 C  C     . LYS A 1 502 ? 173.446 157.619 138.500 1.00 32.13  ? 503  LYS A C     1 
ATOM   3932 O  O     . LYS A 1 502 ? 174.499 157.198 138.009 1.00 32.13  ? 503  LYS A O     1 
ATOM   3933 C  CB    . LYS A 1 502 ? 172.824 156.885 140.818 1.00 32.13  ? 503  LYS A CB    1 
ATOM   3934 C  CG    . LYS A 1 502 ? 173.653 155.616 140.795 1.00 32.13  ? 503  LYS A CG    1 
ATOM   3935 C  CD    . LYS A 1 502 ? 173.122 154.592 141.785 1.00 32.13  ? 503  LYS A CD    1 
ATOM   3936 C  CE    . LYS A 1 502 ? 171.758 154.066 141.372 1.00 32.13  ? 503  LYS A CE    1 
ATOM   3937 N  NZ    . LYS A 1 502 ? 171.842 153.151 140.202 1.00 32.13  ? 503  LYS A NZ    1 
ATOM   3938 N  N     . GLU A 1 503 ? 172.333 157.742 137.781 1.00 35.64  ? 504  GLU A N     1 
ATOM   3939 C  CA    . GLU A 1 503 ? 172.321 157.452 136.354 1.00 35.64  ? 504  GLU A CA    1 
ATOM   3940 C  C     . GLU A 1 503 ? 172.705 158.647 135.495 1.00 35.64  ? 504  GLU A C     1 
ATOM   3941 O  O     . GLU A 1 503 ? 172.678 158.539 134.266 1.00 35.64  ? 504  GLU A O     1 
ATOM   3942 C  CB    . GLU A 1 503 ? 170.943 156.941 135.927 1.00 35.64  ? 504  GLU A CB    1 
ATOM   3943 C  CG    . GLU A 1 503 ? 170.491 155.686 136.647 1.00 35.64  ? 504  GLU A CG    1 
ATOM   3944 C  CD    . GLU A 1 503 ? 171.536 154.590 136.677 1.00 35.64  ? 504  GLU A CD    1 
ATOM   3945 O  OE1   . GLU A 1 503 ? 172.160 154.308 135.631 1.00 35.64  ? 504  GLU A OE1   1 
ATOM   3946 O  OE2   . GLU A 1 503 ? 171.742 154.003 137.758 1.00 35.64  ? 504  GLU A OE2   1 
ATOM   3947 N  N     . GLY A 1 504 ? 173.061 159.774 136.103 1.00 33.11  ? 505  GLY A N     1 
ATOM   3948 C  CA    . GLY A 1 504 ? 173.624 160.879 135.357 1.00 33.11  ? 505  GLY A CA    1 
ATOM   3949 C  C     . GLY A 1 504 ? 172.645 161.694 134.549 1.00 33.11  ? 505  GLY A C     1 
ATOM   3950 O  O     . GLY A 1 504 ? 173.054 162.313 133.563 1.00 33.11  ? 505  GLY A O     1 
ATOM   3951 N  N     . ILE A 1 505 ? 171.356 161.666 134.904 1.00 30.78  ? 506  ILE A N     1 
ATOM   3952 C  CA    . ILE A 1 505 ? 170.362 162.503 134.243 1.00 30.78  ? 506  ILE A CA    1 
ATOM   3953 C  C     . ILE A 1 505 ? 170.711 163.974 134.503 1.00 30.78  ? 506  ILE A C     1 
ATOM   3954 O  O     . ILE A 1 505 ? 171.264 164.325 135.552 1.00 30.78  ? 506  ILE A O     1 
ATOM   3955 C  CB    . ILE A 1 505 ? 168.958 162.139 134.763 1.00 30.78  ? 506  ILE A CB    1 
ATOM   3956 C  CG1   . ILE A 1 505 ? 168.709 160.644 134.608 1.00 30.78  ? 506  ILE A CG1   1 
ATOM   3957 C  CG2   . ILE A 1 505 ? 167.854 162.844 133.997 1.00 30.78  ? 506  ILE A CG2   1 
ATOM   3958 C  CD1   . ILE A 1 505 ? 168.694 160.176 133.190 1.00 30.78  ? 506  ILE A CD1   1 
ATOM   3959 N  N     . GLU A 1 506 ? 170.397 164.843 133.541 1.00 35.91  ? 507  GLU A N     1 
ATOM   3960 C  CA    . GLU A 1 506 ? 170.568 166.281 133.729 1.00 35.91  ? 507  GLU A CA    1 
ATOM   3961 C  C     . GLU A 1 506 ? 169.483 166.794 134.675 1.00 35.91  ? 507  GLU A C     1 
ATOM   3962 O  O     . GLU A 1 506 ? 168.495 167.399 134.246 1.00 35.91  ? 507  GLU A O     1 
ATOM   3963 C  CB    . GLU A 1 506 ? 170.544 167.008 132.379 1.00 35.91  ? 507  GLU A CB    1 
ATOM   3964 C  CG    . GLU A 1 506 ? 170.905 168.497 132.427 1.00 35.91  ? 507  GLU A CG    1 
ATOM   3965 C  CD    . GLU A 1 506 ? 171.076 169.103 131.044 1.00 35.91  ? 507  GLU A CD    1 
ATOM   3966 O  OE1   . GLU A 1 506 ? 170.284 168.762 130.140 1.00 35.91  ? 507  GLU A OE1   1 
ATOM   3967 O  OE2   . GLU A 1 506 ? 172.005 169.917 130.859 1.00 35.91  ? 507  GLU A OE2   1 
ATOM   3968 N  N     . TRP A 1 507 ? 169.641 166.506 135.964 1.00 31.78  ? 508  TRP A N     1 
ATOM   3969 C  CA    . TRP A 1 507 ? 168.623 166.741 136.976 1.00 31.78  ? 508  TRP A CA    1 
ATOM   3970 C  C     . TRP A 1 507 ? 169.186 167.607 138.091 1.00 31.78  ? 508  TRP A C     1 
ATOM   3971 O  O     . TRP A 1 507 ? 170.351 167.466 138.475 1.00 31.78  ? 508  TRP A O     1 
ATOM   3972 C  CB    . TRP A 1 507 ? 168.123 165.414 137.551 1.00 31.78  ? 508  TRP A CB    1 
ATOM   3973 C  CG    . TRP A 1 507 ? 167.045 165.561 138.554 1.00 31.78  ? 508  TRP A CG    1 
ATOM   3974 C  CD1   . TRP A 1 507 ? 167.182 165.520 139.901 1.00 31.78  ? 508  TRP A CD1   1 
ATOM   3975 C  CD2   . TRP A 1 507 ? 165.656 165.773 138.296 1.00 31.78  ? 508  TRP A CD2   1 
ATOM   3976 N  NE1   . TRP A 1 507 ? 165.966 165.696 140.506 1.00 31.78  ? 508  TRP A NE1   1 
ATOM   3977 C  CE2   . TRP A 1 507 ? 165.010 165.852 139.539 1.00 31.78  ? 508  TRP A CE2   1 
ATOM   3978 C  CE3   . TRP A 1 507 ? 164.896 165.902 137.134 1.00 31.78  ? 508  TRP A CE3   1 
ATOM   3979 C  CZ2   . TRP A 1 507 ? 163.644 166.057 139.658 1.00 31.78  ? 508  TRP A CZ2   1 
ATOM   3980 C  CZ3   . TRP A 1 507 ? 163.540 166.103 137.254 1.00 31.78  ? 508  TRP A CZ3   1 
ATOM   3981 C  CH2   . TRP A 1 507 ? 162.928 166.182 138.507 1.00 31.78  ? 508  TRP A CH2   1 
ATOM   3982 N  N     . THR A 1 508 ? 168.353 168.501 138.605 1.00 32.00  ? 509  THR A N     1 
ATOM   3983 C  CA    . THR A 1 508 ? 168.662 169.293 139.784 1.00 32.00  ? 509  THR A CA    1 
ATOM   3984 C  C     . THR A 1 508 ? 167.778 168.834 140.932 1.00 32.00  ? 509  THR A C     1 
ATOM   3985 O  O     . THR A 1 508 ? 166.563 168.700 140.756 1.00 32.00  ? 509  THR A O     1 
ATOM   3986 C  CB    . THR A 1 508 ? 168.449 170.782 139.514 1.00 32.00  ? 509  THR A CB    1 
ATOM   3987 O  OG1   . THR A 1 508 ? 167.107 170.997 139.063 1.00 32.00  ? 509  THR A OG1   1 
ATOM   3988 C  CG2   . THR A 1 508 ? 169.414 171.267 138.449 1.00 32.00  ? 509  THR A CG2   1 
ATOM   3989 N  N     . PHE A 1 509 ? 168.405 168.513 142.066 1.00 29.07  ? 510  PHE A N     1 
ATOM   3990 C  CA    . PHE A 1 509 ? 167.690 168.076 143.261 1.00 29.07  ? 510  PHE A CA    1 
ATOM   3991 C  C     . PHE A 1 509 ? 166.665 169.111 143.716 1.00 29.07  ? 510  PHE A C     1 
ATOM   3992 O  O     . PHE A 1 509 ? 166.996 170.279 143.933 1.00 29.07  ? 510  PHE A O     1 
ATOM   3993 C  CB    . PHE A 1 509 ? 168.690 167.793 144.381 1.00 29.07  ? 510  PHE A CB    1 
ATOM   3994 C  CG    . PHE A 1 509 ? 168.052 167.456 145.695 1.00 29.07  ? 510  PHE A CG    1 
ATOM   3995 C  CD1   . PHE A 1 509 ? 167.425 166.237 145.884 1.00 29.07  ? 510  PHE A CD1   1 
ATOM   3996 C  CD2   . PHE A 1 509 ? 168.100 168.353 146.751 1.00 29.07  ? 510  PHE A CD2   1 
ATOM   3997 C  CE1   . PHE A 1 509 ? 166.840 165.925 147.096 1.00 29.07  ? 510  PHE A CE1   1 
ATOM   3998 C  CE2   . PHE A 1 509 ? 167.519 168.046 147.965 1.00 29.07  ? 510  PHE A CE2   1 
ATOM   3999 C  CZ    . PHE A 1 509 ? 166.887 166.830 148.136 1.00 29.07  ? 510  PHE A CZ    1 
ATOM   4000 N  N     . ILE A 1 510 ? 165.418 168.671 143.863 1.00 30.34  ? 511  ILE A N     1 
ATOM   4001 C  CA    . ILE A 1 510 ? 164.309 169.525 144.277 1.00 30.34  ? 511  ILE A CA    1 
ATOM   4002 C  C     . ILE A 1 510 ? 164.043 169.289 145.756 1.00 30.34  ? 511  ILE A C     1 
ATOM   4003 O  O     . ILE A 1 510 ? 163.993 168.138 146.209 1.00 30.34  ? 511  ILE A O     1 
ATOM   4004 C  CB    . ILE A 1 510 ? 163.051 169.250 143.439 1.00 30.34  ? 511  ILE A CB    1 
ATOM   4005 C  CG1   . ILE A 1 510 ? 163.379 169.307 141.951 1.00 30.34  ? 511  ILE A CG1   1 
ATOM   4006 C  CG2   . ILE A 1 510 ? 161.968 170.264 143.755 1.00 30.34  ? 511  ILE A CG2   1 
ATOM   4007 C  CD1   . ILE A 1 510 ? 163.933 170.639 141.499 1.00 30.34  ? 511  ILE A CD1   1 
ATOM   4008 N  N     . ASP A 1 511 ? 163.887 170.371 146.514 1.00 30.77  ? 512  ASP A N     1 
ATOM   4009 C  CA    . ASP A 1 511 ? 163.599 170.286 147.943 1.00 30.77  ? 512  ASP A CA    1 
ATOM   4010 C  C     . ASP A 1 511 ? 162.082 170.286 148.101 1.00 30.77  ? 512  ASP A C     1 
ATOM   4011 O  O     . ASP A 1 511 ? 161.446 171.342 148.113 1.00 30.77  ? 512  ASP A O     1 
ATOM   4012 C  CB    . ASP A 1 511 ? 164.255 171.451 148.678 1.00 30.77  ? 512  ASP A CB    1 
ATOM   4013 C  CG    . ASP A 1 511 ? 164.147 171.348 150.194 1.00 30.77  ? 512  ASP A CG    1 
ATOM   4014 O  OD1   . ASP A 1 511 ? 163.637 170.337 150.719 1.00 30.77  ? 512  ASP A OD1   1 
ATOM   4015 O  OD2   . ASP A 1 511 ? 164.586 172.301 150.869 1.00 30.77  ? 512  ASP A OD2   1 
ATOM   4016 N  N     . PHE A 1 512 ? 161.497 169.091 148.212 1.00 26.98  ? 513  PHE A N     1 
ATOM   4017 C  CA    . PHE A 1 512 ? 160.061 168.969 148.431 1.00 26.98  ? 513  PHE A CA    1 
ATOM   4018 C  C     . PHE A 1 512 ? 159.628 169.349 149.842 1.00 26.98  ? 513  PHE A C     1 
ATOM   4019 O  O     . PHE A 1 512 ? 158.434 169.575 150.058 1.00 26.98  ? 513  PHE A O     1 
ATOM   4020 C  CB    . PHE A 1 512 ? 159.604 167.545 148.122 1.00 26.98  ? 513  PHE A CB    1 
ATOM   4021 C  CG    . PHE A 1 512 ? 159.677 167.193 146.672 1.00 26.98  ? 513  PHE A CG    1 
ATOM   4022 C  CD1   . PHE A 1 512 ? 158.870 167.835 145.754 1.00 26.98  ? 513  PHE A CD1   1 
ATOM   4023 C  CD2   . PHE A 1 512 ? 160.543 166.211 146.224 1.00 26.98  ? 513  PHE A CD2   1 
ATOM   4024 C  CE1   . PHE A 1 512 ? 158.935 167.517 144.415 1.00 26.98  ? 513  PHE A CE1   1 
ATOM   4025 C  CE2   . PHE A 1 512 ? 160.609 165.886 144.880 1.00 26.98  ? 513  PHE A CE2   1 
ATOM   4026 C  CZ    . PHE A 1 512 ? 159.805 166.541 143.980 1.00 26.98  ? 513  PHE A CZ    1 
ATOM   4027 N  N     . GLY A 1 513 ? 160.556 169.448 150.793 1.00 27.03  ? 514  GLY A N     1 
ATOM   4028 C  CA    . GLY A 1 513 ? 160.210 169.834 152.147 1.00 27.03  ? 514  GLY A CA    1 
ATOM   4029 C  C     . GLY A 1 513 ? 159.417 168.822 152.942 1.00 27.03  ? 514  GLY A C     1 
ATOM   4030 O  O     . GLY A 1 513 ? 158.775 169.195 153.925 1.00 27.03  ? 514  GLY A O     1 
ATOM   4031 N  N     . MET A 1 514 ? 159.426 167.554 152.544 1.00 24.83  ? 515  MET A N     1 
ATOM   4032 C  CA    . MET A 1 514 ? 158.702 166.491 153.242 1.00 24.83  ? 515  MET A CA    1 
ATOM   4033 C  C     . MET A 1 514 ? 159.708 165.502 153.825 1.00 24.83  ? 515  MET A C     1 
ATOM   4034 O  O     . MET A 1 514 ? 160.109 164.543 153.167 1.00 24.83  ? 515  MET A O     1 
ATOM   4035 C  CB    . MET A 1 514 ? 157.715 165.794 152.316 1.00 24.83  ? 515  MET A CB    1 
ATOM   4036 C  CG    . MET A 1 514 ? 156.518 166.643 151.940 1.00 24.83  ? 515  MET A CG    1 
ATOM   4037 S  SD    . MET A 1 514 ? 155.358 166.827 153.306 1.00 24.83  ? 515  MET A SD    1 
ATOM   4038 C  CE    . MET A 1 514 ? 154.281 168.108 152.675 1.00 24.83  ? 515  MET A CE    1 
ATOM   4039 N  N     . ASP A 1 515 ? 160.111 165.741 155.072 1.00 24.04  ? 516  ASP A N     1 
ATOM   4040 C  CA    . ASP A 1 515 ? 161.055 164.867 155.750 1.00 24.04  ? 516  ASP A CA    1 
ATOM   4041 C  C     . ASP A 1 515 ? 160.813 164.958 157.248 1.00 24.04  ? 516  ASP A C     1 
ATOM   4042 O  O     . ASP A 1 515 ? 160.463 166.019 157.770 1.00 24.04  ? 516  ASP A O     1 
ATOM   4043 C  CB    . ASP A 1 515 ? 162.503 165.238 155.419 1.00 24.04  ? 516  ASP A CB    1 
ATOM   4044 C  CG    . ASP A 1 515 ? 163.492 164.179 155.852 1.00 24.04  ? 516  ASP A CG    1 
ATOM   4045 O  OD1   . ASP A 1 515 ? 163.056 163.070 156.218 1.00 24.04  ? 516  ASP A OD1   1 
ATOM   4046 O  OD2   . ASP A 1 515 ? 164.710 164.453 155.818 1.00 24.04  ? 516  ASP A OD2   1 
ATOM   4047 N  N     . LEU A 1 516 ? 161.007 163.826 157.936 1.00 24.35  ? 517  LEU A N     1 
ATOM   4048 C  CA    . LEU A 1 516 ? 160.571 163.665 159.317 1.00 24.35  ? 517  LEU A CA    1 
ATOM   4049 C  C     . LEU A 1 516 ? 161.635 163.126 160.252 1.00 24.35  ? 517  LEU A C     1 
ATOM   4050 O  O     . LEU A 1 516 ? 161.328 162.907 161.427 1.00 24.35  ? 517  LEU A O     1 
ATOM   4051 C  CB    . LEU A 1 516 ? 159.358 162.735 159.408 1.00 24.35  ? 517  LEU A CB    1 
ATOM   4052 C  CG    . LEU A 1 516 ? 158.101 163.188 158.690 1.00 24.35  ? 517  LEU A CG    1 
ATOM   4053 C  CD1   . LEU A 1 516 ? 157.084 162.070 158.689 1.00 24.35  ? 517  LEU A CD1   1 
ATOM   4054 C  CD2   . LEU A 1 516 ? 157.574 164.428 159.372 1.00 24.35  ? 517  LEU A CD2   1 
ATOM   4055 N  N     . GLN A 1 517 ? 162.853 162.870 159.763 1.00 24.40  ? 518  GLN A N     1 
ATOM   4056 C  CA    . GLN A 1 517 ? 163.921 162.269 160.560 1.00 24.40  ? 518  GLN A CA    1 
ATOM   4057 C  C     . GLN A 1 517 ? 164.287 163.102 161.789 1.00 24.40  ? 518  GLN A C     1 
ATOM   4058 O  O     . GLN A 1 517 ? 164.801 162.552 162.764 1.00 24.40  ? 518  GLN A O     1 
ATOM   4059 C  CB    . GLN A 1 517 ? 165.148 162.057 159.667 1.00 24.40  ? 518  GLN A CB    1 
ATOM   4060 C  CG    . GLN A 1 517 ? 166.239 161.157 160.225 1.00 24.40  ? 518  GLN A CG    1 
ATOM   4061 C  CD    . GLN A 1 517 ? 165.782 159.723 160.390 1.00 24.40  ? 518  GLN A CD    1 
ATOM   4062 O  OE1   . GLN A 1 517 ? 165.164 159.154 159.494 1.00 24.40  ? 518  GLN A OE1   1 
ATOM   4063 N  NE2   . GLN A 1 517 ? 166.098 159.124 161.530 1.00 24.40  ? 518  GLN A NE2   1 
ATOM   4064 N  N     . ALA A 1 518 ? 164.015 164.409 161.770 1.00 26.12  ? 519  ALA A N     1 
ATOM   4065 C  CA    . ALA A 1 518 ? 164.214 165.244 162.952 1.00 26.12  ? 519  ALA A CA    1 
ATOM   4066 C  C     . ALA A 1 518 ? 163.295 164.860 164.108 1.00 26.12  ? 519  ALA A C     1 
ATOM   4067 O  O     . ALA A 1 518 ? 163.623 165.130 165.268 1.00 26.12  ? 519  ALA A O     1 
ATOM   4068 C  CB    . ALA A 1 518 ? 164.006 166.714 162.592 1.00 26.12  ? 519  ALA A CB    1 
ATOM   4069 N  N     . CYS A 1 519 ? 162.143 164.253 163.823 1.00 25.24  ? 520  CYS A N     1 
ATOM   4070 C  CA    . CYS A 1 519 ? 161.228 163.834 164.881 1.00 25.24  ? 520  CYS A CA    1 
ATOM   4071 C  C     . CYS A 1 519 ? 161.429 162.379 165.293 1.00 25.24  ? 520  CYS A C     1 
ATOM   4072 O  O     . CYS A 1 519 ? 161.271 162.048 166.469 1.00 25.24  ? 520  CYS A O     1 
ATOM   4073 C  CB    . CYS A 1 519 ? 159.779 164.067 164.455 1.00 25.24  ? 520  CYS A CB    1 
ATOM   4074 S  SG    . CYS A 1 519 ? 158.597 163.852 165.794 1.00 25.24  ? 520  CYS A SG    1 
ATOM   4075 N  N     . ILE A 1 520 ? 161.720 161.494 164.338 1.00 23.05  ? 521  ILE A N     1 
ATOM   4076 C  CA    . ILE A 1 520 ? 162.092 160.116 164.654 1.00 23.05  ? 521  ILE A CA    1 
ATOM   4077 C  C     . ILE A 1 520 ? 163.370 160.064 165.491 1.00 23.05  ? 521  ILE A C     1 
ATOM   4078 O  O     . ILE A 1 520 ? 163.513 159.196 166.363 1.00 23.05  ? 521  ILE A O     1 
ATOM   4079 C  CB    . ILE A 1 520 ? 162.199 159.310 163.340 1.00 23.05  ? 521  ILE A CB    1 
ATOM   4080 C  CG1   . ILE A 1 520 ? 160.814 159.104 162.744 1.00 23.05  ? 521  ILE A CG1   1 
ATOM   4081 C  CG2   . ILE A 1 520 ? 162.842 157.950 163.519 1.00 23.05  ? 521  ILE A CG2   1 
ATOM   4082 C  CD1   . ILE A 1 520 ? 160.846 158.607 161.343 1.00 23.05  ? 521  ILE A CD1   1 
ATOM   4083 N  N     . ASP A 1 521 ? 164.292 161.011 165.287 1.00 26.56  ? 522  ASP A N     1 
ATOM   4084 C  CA    . ASP A 1 521 ? 165.471 161.114 166.148 1.00 26.56  ? 522  ASP A CA    1 
ATOM   4085 C  C     . ASP A 1 521 ? 165.126 161.438 167.598 1.00 26.56  ? 522  ASP A C     1 
ATOM   4086 O  O     . ASP A 1 521 ? 165.903 161.107 168.498 1.00 26.56  ? 522  ASP A O     1 
ATOM   4087 C  CB    . ASP A 1 521 ? 166.434 162.180 165.620 1.00 26.56  ? 522  ASP A CB    1 
ATOM   4088 C  CG    . ASP A 1 521 ? 167.245 161.704 164.435 1.00 26.56  ? 522  ASP A CG    1 
ATOM   4089 O  OD1   . ASP A 1 521 ? 166.890 160.662 163.847 1.00 26.56  ? 522  ASP A OD1   1 
ATOM   4090 O  OD2   . ASP A 1 521 ? 168.241 162.372 164.090 1.00 26.56  ? 522  ASP A OD2   1 
ATOM   4091 N  N     . LEU A 1 522 ? 163.984 162.070 167.844 1.00 27.55  ? 523  LEU A N     1 
ATOM   4092 C  CA    . LEU A 1 522 ? 163.545 162.331 169.203 1.00 27.55  ? 523  LEU A CA    1 
ATOM   4093 C  C     . LEU A 1 522 ? 163.008 161.075 169.877 1.00 27.55  ? 523  LEU A C     1 
ATOM   4094 O  O     . LEU A 1 522 ? 162.944 161.023 171.106 1.00 27.55  ? 523  LEU A O     1 
ATOM   4095 C  CB    . LEU A 1 522 ? 162.505 163.451 169.185 1.00 27.55  ? 523  LEU A CB    1 
ATOM   4096 C  CG    . LEU A 1 522 ? 161.838 163.967 170.448 1.00 27.55  ? 523  LEU A CG    1 
ATOM   4097 C  CD1   . LEU A 1 522 ? 162.898 164.536 171.361 1.00 27.55  ? 523  LEU A CD1   1 
ATOM   4098 C  CD2   . LEU A 1 522 ? 160.874 165.030 170.068 1.00 27.55  ? 523  LEU A CD2   1 
ATOM   4099 N  N     . ILE A 1 523 ? 162.595 160.077 169.109 1.00 23.22  ? 524  ILE A N     1 
ATOM   4100 C  CA    . ILE A 1 523 ? 161.996 158.860 169.642 1.00 23.22  ? 524  ILE A CA    1 
ATOM   4101 C  C     . ILE A 1 523 ? 162.963 157.681 169.577 1.00 23.22  ? 524  ILE A C     1 
ATOM   4102 O  O     . ILE A 1 523 ? 163.197 157.005 170.575 1.00 23.22  ? 524  ILE A O     1 
ATOM   4103 C  CB    . ILE A 1 523 ? 160.672 158.532 168.921 1.00 23.22  ? 524  ILE A CB    1 
ATOM   4104 C  CG1   . ILE A 1 523 ? 159.637 159.618 169.193 1.00 23.22  ? 524  ILE A CG1   1 
ATOM   4105 C  CG2   . ILE A 1 523 ? 160.145 157.208 169.377 1.00 23.22  ? 524  ILE A CG2   1 
ATOM   4106 C  CD1   . ILE A 1 523 ? 158.341 159.416 168.470 1.00 23.22  ? 524  ILE A CD1   1 
ATOM   4107 N  N     . GLU A 1 524 ? 163.550 157.434 168.408 1.00 26.93  ? 525  GLU A N     1 
ATOM   4108 C  CA    . GLU A 1 524 ? 164.233 156.167 168.168 1.00 26.93  ? 525  GLU A CA    1 
ATOM   4109 C  C     . GLU A 1 524 ? 165.664 156.136 168.704 1.00 26.93  ? 525  GLU A C     1 
ATOM   4110 O  O     . GLU A 1 524 ? 166.125 155.083 169.157 1.00 26.93  ? 525  GLU A O     1 
ATOM   4111 C  CB    . GLU A 1 524 ? 164.215 155.853 166.669 1.00 26.93  ? 525  GLU A CB    1 
ATOM   4112 C  CG    . GLU A 1 524 ? 164.564 154.407 166.338 1.00 26.93  ? 525  GLU A CG    1 
ATOM   4113 C  CD    . GLU A 1 524 ? 164.577 154.108 164.855 1.00 26.93  ? 525  GLU A CD    1 
ATOM   4114 O  OE1   . GLU A 1 524 ? 163.915 154.843 164.097 1.00 26.93  ? 525  GLU A OE1   1 
ATOM   4115 O  OE2   . GLU A 1 524 ? 165.241 153.133 164.445 1.00 26.93  ? 525  GLU A OE2   1 
ATOM   4116 N  N     . LYS A 1 525 ? 166.380 157.259 168.652 1.00 31.33  ? 526  LYS A N     1 
ATOM   4117 C  CA    . LYS A 1 525 ? 167.807 157.291 168.962 1.00 31.33  ? 526  LYS A CA    1 
ATOM   4118 C  C     . LYS A 1 525 ? 168.098 156.987 170.438 1.00 31.33  ? 526  LYS A C     1 
ATOM   4119 O  O     . LYS A 1 525 ? 167.226 157.146 171.294 1.00 31.33  ? 526  LYS A O     1 
ATOM   4120 C  CB    . LYS A 1 525 ? 168.378 158.648 168.547 1.00 31.33  ? 526  LYS A CB    1 
ATOM   4121 C  CG    . LYS A 1 525 ? 168.715 158.683 167.074 1.00 31.33  ? 526  LYS A CG    1 
ATOM   4122 C  CD    . LYS A 1 525 ? 169.356 159.984 166.661 1.00 31.33  ? 526  LYS A CD    1 
ATOM   4123 C  CE    . LYS A 1 525 ? 170.144 159.793 165.374 1.00 31.33  ? 526  LYS A CE    1 
ATOM   4124 N  NZ    . LYS A 1 525 ? 169.305 159.285 164.254 1.00 31.33  ? 526  LYS A NZ    1 
ATOM   4125 N  N     . PRO A 1 526 ? 169.357 156.530 170.771 1.00 36.41  ? 527  PRO A N     1 
ATOM   4126 C  CA    . PRO A 1 526 ? 169.671 156.157 172.163 1.00 36.41  ? 527  PRO A CA    1 
ATOM   4127 C  C     . PRO A 1 526 ? 169.800 157.279 173.191 1.00 36.41  ? 527  PRO A C     1 
ATOM   4128 O  O     . PRO A 1 526 ? 170.420 157.072 174.238 1.00 36.41  ? 527  PRO A O     1 
ATOM   4129 C  CB    . PRO A 1 526 ? 170.996 155.398 172.025 1.00 36.41  ? 527  PRO A CB    1 
ATOM   4130 C  CG    . PRO A 1 526 ? 171.613 155.924 170.815 1.00 36.41  ? 527  PRO A CG    1 
ATOM   4131 C  CD    . PRO A 1 526 ? 170.473 156.156 169.875 1.00 36.41  ? 527  PRO A CD    1 
ATOM   4132 N  N     . MET A 1 527 ? 169.236 158.457 172.925 1.00 38.45  ? 528  MET A N     1 
ATOM   4133 C  CA    . MET A 1 527 ? 168.941 159.395 174.001 1.00 38.45  ? 528  MET A CA    1 
ATOM   4134 C  C     . MET A 1 527 ? 167.577 160.034 173.732 1.00 38.45  ? 528  MET A C     1 
ATOM   4135 O  O     . MET A 1 527 ? 167.242 161.080 174.298 1.00 38.45  ? 528  MET A O     1 
ATOM   4136 C  CB    . MET A 1 527 ? 170.098 160.408 174.132 1.00 38.45  ? 528  MET A CB    1 
ATOM   4137 C  CG    . MET A 1 527 ? 170.165 161.212 175.434 1.00 38.45  ? 528  MET A CG    1 
ATOM   4138 S  SD    . MET A 1 527 ? 169.957 160.173 176.894 1.00 38.45  ? 528  MET A SD    1 
ATOM   4139 C  CE    . MET A 1 527 ? 171.430 159.160 176.818 1.00 38.45  ? 528  MET A CE    1 
ATOM   4140 N  N     . GLY A 1 528 ? 166.775 159.399 172.888 1.00 32.30  ? 529  GLY A N     1 
ATOM   4141 C  CA    . GLY A 1 528 ? 165.401 159.785 172.695 1.00 32.30  ? 529  GLY A CA    1 
ATOM   4142 C  C     . GLY A 1 528 ? 164.475 159.193 173.735 1.00 32.30  ? 529  GLY A C     1 
ATOM   4143 O  O     . GLY A 1 528 ? 164.904 158.511 174.665 1.00 32.30  ? 529  GLY A O     1 
ATOM   4144 N  N     . ILE A 1 529 ? 163.187 159.544 173.591 1.00 29.44  ? 530  ILE A N     1 
ATOM   4145 C  CA    . ILE A 1 529 ? 162.136 159.216 174.563 1.00 29.44  ? 530  ILE A CA    1 
ATOM   4146 C  C     . ILE A 1 529 ? 162.081 157.719 174.865 1.00 29.44  ? 530  ILE A C     1 
ATOM   4147 O  O     . ILE A 1 529 ? 162.059 157.303 176.028 1.00 29.44  ? 530  ILE A O     1 
ATOM   4148 C  CB    . ILE A 1 529 ? 160.779 159.743 174.067 1.00 29.44  ? 530  ILE A CB    1 
ATOM   4149 C  CG1   . ILE A 1 529 ? 160.790 161.266 174.034 1.00 29.44  ? 530  ILE A CG1   1 
ATOM   4150 C  CG2   . ILE A 1 529 ? 159.659 159.267 174.953 1.00 29.44  ? 530  ILE A CG2   1 
ATOM   4151 C  CD1   . ILE A 1 529 ? 159.552 161.857 173.442 1.00 29.44  ? 530  ILE A CD1   1 
ATOM   4152 N  N     . MET A 1 530 ? 162.091 156.886 173.830 1.00 30.34  ? 531  MET A N     1 
ATOM   4153 C  CA    . MET A 1 530 ? 162.040 155.443 174.040 1.00 30.34  ? 531  MET A CA    1 
ATOM   4154 C  C     . MET A 1 530 ? 163.370 154.850 174.479 1.00 30.34  ? 531  MET A C     1 
ATOM   4155 O  O     . MET A 1 530 ? 163.434 153.642 174.726 1.00 30.34  ? 531  MET A O     1 
ATOM   4156 C  CB    . MET A 1 530 ? 161.557 154.720 172.783 1.00 30.34  ? 531  MET A CB    1 
ATOM   4157 C  CG    . MET A 1 530 ? 160.100 154.954 172.451 1.00 30.34  ? 531  MET A CG    1 
ATOM   4158 S  SD    . MET A 1 530 ? 159.568 153.903 171.091 1.00 30.34  ? 531  MET A SD    1 
ATOM   4159 C  CE    . MET A 1 530 ? 157.863 154.411 170.932 1.00 30.34  ? 531  MET A CE    1 
ATOM   4160 N  N     . SER A 1 531 ? 164.434 155.643 174.550 1.00 34.04  ? 532  SER A N     1 
ATOM   4161 C  CA    . SER A 1 531 ? 165.652 155.207 175.215 1.00 34.04  ? 532  SER A CA    1 
ATOM   4162 C  C     . SER A 1 531 ? 165.686 155.566 176.694 1.00 34.04  ? 532  SER A C     1 
ATOM   4163 O  O     . SER A 1 531 ? 166.331 154.861 177.476 1.00 34.04  ? 532  SER A O     1 
ATOM   4164 C  CB    . SER A 1 531 ? 166.873 155.801 174.522 1.00 34.04  ? 532  SER A CB    1 
ATOM   4165 O  OG    . SER A 1 531 ? 168.062 155.210 175.009 1.00 34.04  ? 532  SER A OG    1 
ATOM   4166 N  N     . ILE A 1 532 ? 165.052 156.673 177.086 1.00 35.93  ? 533  ILE A N     1 
ATOM   4167 C  CA    . ILE A 1 532 ? 164.967 157.029 178.500 1.00 35.93  ? 533  ILE A CA    1 
ATOM   4168 C  C     . ILE A 1 532 ? 164.088 156.037 179.262 1.00 35.93  ? 533  ILE A C     1 
ATOM   4169 O  O     . ILE A 1 532 ? 164.401 155.661 180.397 1.00 35.93  ? 533  ILE A O     1 
ATOM   4170 C  CB    . ILE A 1 532 ? 164.501 158.487 178.646 1.00 35.93  ? 533  ILE A CB    1 
ATOM   4171 C  CG1   . ILE A 1 532 ? 165.505 159.394 177.938 1.00 35.93  ? 533  ILE A CG1   1 
ATOM   4172 C  CG2   . ILE A 1 532 ? 164.436 158.896 180.093 1.00 35.93  ? 533  ILE A CG2   1 
ATOM   4173 C  CD1   . ILE A 1 532 ? 165.092 160.826 177.838 1.00 35.93  ? 533  ILE A CD1   1 
ATOM   4174 N  N     . LEU A 1 533 ? 162.991 155.572 178.647 1.00 36.26  ? 534  LEU A N     1 
ATOM   4175 C  CA    . LEU A 1 533 ? 162.204 154.473 179.217 1.00 36.26  ? 534  LEU A CA    1 
ATOM   4176 C  C     . LEU A 1 533 ? 162.975 153.167 179.346 1.00 36.26  ? 534  LEU A C     1 
ATOM   4177 O  O     . LEU A 1 533 ? 162.531 152.275 180.071 1.00 36.26  ? 534  LEU A O     1 
ATOM   4178 C  CB    . LEU A 1 533 ? 160.958 154.192 178.382 1.00 36.26  ? 534  LEU A CB    1 
ATOM   4179 C  CG    . LEU A 1 533 ? 159.780 155.143 178.412 1.00 36.26  ? 534  LEU A CG    1 
ATOM   4180 C  CD1   . LEU A 1 533 ? 158.842 154.777 177.311 1.00 36.26  ? 534  LEU A CD1   1 
ATOM   4181 C  CD2   . LEU A 1 533 ? 159.087 154.930 179.725 1.00 36.26  ? 534  LEU A CD2   1 
ATOM   4182 N  N     . GLU A 1 534 ? 164.101 153.023 178.662 1.00 38.21  ? 535  GLU A N     1 
ATOM   4183 C  CA    . GLU A 1 534 ? 164.911 151.825 178.780 1.00 38.21  ? 535  GLU A CA    1 
ATOM   4184 C  C     . GLU A 1 534 ? 166.016 151.993 179.808 1.00 38.21  ? 535  GLU A C     1 
ATOM   4185 O  O     . GLU A 1 534 ? 166.451 151.007 180.413 1.00 38.21  ? 535  GLU A O     1 
ATOM   4186 C  CB    . GLU A 1 534 ? 165.503 151.472 177.418 1.00 38.21  ? 535  GLU A CB    1 
ATOM   4187 C  CG    . GLU A 1 534 ? 164.463 150.978 176.439 1.00 38.21  ? 535  GLU A CG    1 
ATOM   4188 C  CD    . GLU A 1 534 ? 165.005 150.846 175.038 1.00 38.21  ? 535  GLU A CD    1 
ATOM   4189 O  OE1   . GLU A 1 534 ? 166.240 150.866 174.876 1.00 38.21  ? 535  GLU A OE1   1 
ATOM   4190 O  OE2   . GLU A 1 534 ? 164.194 150.728 174.097 1.00 38.21  ? 535  GLU A OE2   1 
ATOM   4191 N  N     . GLU A 1 535 ? 166.481 153.225 180.008 1.00 47.75  ? 536  GLU A N     1 
ATOM   4192 C  CA    . GLU A 1 535 ? 167.406 153.515 181.097 1.00 47.75  ? 536  GLU A CA    1 
ATOM   4193 C  C     . GLU A 1 535 ? 166.714 153.459 182.453 1.00 47.75  ? 536  GLU A C     1 
ATOM   4194 O  O     . GLU A 1 535 ? 167.233 152.859 183.399 1.00 47.75  ? 536  GLU A O     1 
ATOM   4195 C  CB    . GLU A 1 535 ? 168.040 154.888 180.884 1.00 47.75  ? 536  GLU A CB    1 
ATOM   4196 C  CG    . GLU A 1 535 ? 169.141 155.217 181.864 1.00 47.75  ? 536  GLU A CG    1 
ATOM   4197 C  CD    . GLU A 1 535 ? 170.056 156.303 181.350 1.00 47.75  ? 536  GLU A CD    1 
ATOM   4198 O  OE1   . GLU A 1 535 ? 171.001 156.681 182.073 1.00 47.75  ? 536  GLU A OE1   1 
ATOM   4199 O  OE2   . GLU A 1 535 ? 169.826 156.781 180.220 1.00 47.75  ? 536  GLU A OE2   1 
ATOM   4200 N  N     . GLU A 1 536 ? 165.544 154.090 182.573 1.00 49.40  ? 537  GLU A N     1 
ATOM   4201 C  CA    . GLU A 1 536 ? 164.838 154.156 183.850 1.00 49.40  ? 537  GLU A CA    1 
ATOM   4202 C  C     . GLU A 1 536 ? 164.203 152.841 184.296 1.00 49.40  ? 537  GLU A C     1 
ATOM   4203 O  O     . GLU A 1 536 ? 163.664 152.793 185.406 1.00 49.40  ? 537  GLU A O     1 
ATOM   4204 C  CB    . GLU A 1 536 ? 163.771 155.245 183.791 1.00 49.40  ? 537  GLU A CB    1 
ATOM   4205 C  CG    . GLU A 1 536 ? 164.334 156.624 183.552 1.00 49.40  ? 537  GLU A CG    1 
ATOM   4206 C  CD    . GLU A 1 536 ? 165.522 156.919 184.437 1.00 49.40  ? 537  GLU A CD    1 
ATOM   4207 O  OE1   . GLU A 1 536 ? 165.362 156.913 185.675 1.00 49.40  ? 537  GLU A OE1   1 
ATOM   4208 O  OE2   . GLU A 1 536 ? 166.623 157.142 183.893 1.00 49.40  ? 537  GLU A OE2   1 
ATOM   4209 N  N     . CYS A 1 537 ? 164.232 151.783 183.487 1.00 46.54  ? 538  CYS A N     1 
ATOM   4210 C  CA    . CYS A 1 537 ? 163.912 150.463 184.015 1.00 46.54  ? 538  CYS A CA    1 
ATOM   4211 C  C     . CYS A 1 537 ? 165.065 149.844 184.791 1.00 46.54  ? 538  CYS A C     1 
ATOM   4212 O  O     . CYS A 1 537 ? 164.843 148.902 185.557 1.00 46.54  ? 538  CYS A O     1 
ATOM   4213 C  CB    . CYS A 1 537 ? 163.493 149.525 182.886 1.00 46.54  ? 538  CYS A CB    1 
ATOM   4214 S  SG    . CYS A 1 537 ? 161.868 149.887 182.214 1.00 46.54  ? 538  CYS A SG    1 
ATOM   4215 N  N     . MET A 1 538 ? 166.284 150.353 184.615 1.00 54.04  ? 539  MET A N     1 
ATOM   4216 C  CA    . MET A 1 538 ? 167.456 149.838 185.312 1.00 54.04  ? 539  MET A CA    1 
ATOM   4217 C  C     . MET A 1 538 ? 167.585 150.357 186.739 1.00 54.04  ? 539  MET A C     1 
ATOM   4218 O  O     . MET A 1 538 ? 168.393 149.816 187.502 1.00 54.04  ? 539  MET A O     1 
ATOM   4219 C  CB    . MET A 1 538 ? 168.727 150.171 184.528 1.00 54.04  ? 539  MET A CB    1 
ATOM   4220 C  CG    . MET A 1 538 ? 168.706 149.693 183.086 1.00 54.04  ? 539  MET A CG    1 
ATOM   4221 S  SD    . MET A 1 538 ? 170.338 149.702 182.324 1.00 54.04  ? 539  MET A SD    1 
ATOM   4222 C  CE    . MET A 1 538 ? 170.856 151.382 182.659 1.00 54.04  ? 539  MET A CE    1 
ATOM   4223 N  N     . PHE A 1 539 ? 166.827 151.386 187.118 1.00 57.03  ? 540  PHE A N     1 
ATOM   4224 C  CA    . PHE A 1 539 ? 166.984 152.012 188.423 1.00 57.03  ? 540  PHE A CA    1 
ATOM   4225 C  C     . PHE A 1 539 ? 165.789 151.678 189.300 1.00 57.03  ? 540  PHE A C     1 
ATOM   4226 O  O     . PHE A 1 539 ? 164.648 151.981 188.921 1.00 57.03  ? 540  PHE A O     1 
ATOM   4227 C  CB    . PHE A 1 539 ? 167.124 153.528 188.287 1.00 57.03  ? 540  PHE A CB    1 
ATOM   4228 C  CG    . PHE A 1 539 ? 168.379 153.971 187.593 1.00 57.03  ? 540  PHE A CG    1 
ATOM   4229 C  CD1   . PHE A 1 539 ? 168.422 154.092 186.213 1.00 57.03  ? 540  PHE A CD1   1 
ATOM   4230 C  CD2   . PHE A 1 539 ? 169.514 154.281 188.325 1.00 57.03  ? 540  PHE A CD2   1 
ATOM   4231 C  CE1   . PHE A 1 539 ? 169.577 154.506 185.575 1.00 57.03  ? 540  PHE A CE1   1 
ATOM   4232 C  CE2   . PHE A 1 539 ? 170.673 154.697 187.694 1.00 57.03  ? 540  PHE A CE2   1 
ATOM   4233 C  CZ    . PHE A 1 539 ? 170.703 154.809 186.317 1.00 57.03  ? 540  PHE A CZ    1 
ATOM   4234 N  N     . PRO A 1 540 ? 166.004 151.020 190.445 1.00 57.15  ? 541  PRO A N     1 
ATOM   4235 C  CA    . PRO A 1 540 ? 164.892 150.743 191.374 1.00 57.15  ? 541  PRO A CA    1 
ATOM   4236 C  C     . PRO A 1 540 ? 164.210 151.980 191.939 1.00 57.15  ? 541  PRO A C     1 
ATOM   4237 O  O     . PRO A 1 540 ? 163.048 151.888 192.354 1.00 57.15  ? 541  PRO A O     1 
ATOM   4238 C  CB    . PRO A 1 540 ? 165.569 149.937 192.490 1.00 57.15  ? 541  PRO A CB    1 
ATOM   4239 C  CG    . PRO A 1 540 ? 166.755 149.314 191.838 1.00 57.15  ? 541  PRO A CG    1 
ATOM   4240 C  CD    . PRO A 1 540 ? 167.240 150.322 190.838 1.00 57.15  ? 541  PRO A CD    1 
ATOM   4241 N  N     . LYS A 1 541 ? 164.887 153.126 191.974 1.00 55.15  ? 542  LYS A N     1 
ATOM   4242 C  CA    . LYS A 1 541 ? 164.377 154.324 192.623 1.00 55.15  ? 542  LYS A CA    1 
ATOM   4243 C  C     . LYS A 1 541 ? 163.764 155.290 191.601 1.00 55.15  ? 542  LYS A C     1 
ATOM   4244 O  O     . LYS A 1 541 ? 163.237 156.345 191.973 1.00 55.15  ? 542  LYS A O     1 
ATOM   4245 C  CB    . LYS A 1 541 ? 165.546 154.933 193.438 1.00 55.15  ? 542  LYS A CB    1 
ATOM   4246 C  CG    . LYS A 1 541 ? 165.458 156.316 194.115 1.00 55.15  ? 542  LYS A CG    1 
ATOM   4247 C  CD    . LYS A 1 541 ? 164.498 156.300 195.290 1.00 55.15  ? 542  LYS A CD    1 
ATOM   4248 C  CE    . LYS A 1 541 ? 165.085 155.545 196.469 1.00 55.15  ? 542  LYS A CE    1 
ATOM   4249 N  NZ    . LYS A 1 541 ? 164.026 155.062 197.395 1.00 55.15  ? 542  LYS A NZ    1 
ATOM   4250 N  N     . ALA A 1 542 ? 163.701 154.885 190.334 1.00 50.21  ? 543  ALA A N     1 
ATOM   4251 C  CA    . ALA A 1 542 ? 163.044 155.695 189.318 1.00 50.21  ? 543  ALA A CA    1 
ATOM   4252 C  C     . ALA A 1 542 ? 161.536 155.758 189.535 1.00 50.21  ? 543  ALA A C     1 
ATOM   4253 O  O     . ALA A 1 542 ? 160.907 154.784 189.955 1.00 50.21  ? 543  ALA A O     1 
ATOM   4254 C  CB    . ALA A 1 542 ? 163.345 155.143 187.928 1.00 50.21  ? 543  ALA A CB    1 
ATOM   4255 N  N     . THR A 1 543 ? 160.965 156.920 189.241 1.00 45.07  ? 544  THR A N     1 
ATOM   4256 C  CA    . THR A 1 543 ? 159.534 157.162 189.332 1.00 45.07  ? 544  THR A CA    1 
ATOM   4257 C  C     . THR A 1 543 ? 159.176 158.147 188.234 1.00 45.07  ? 544  THR A C     1 
ATOM   4258 O  O     . THR A 1 543 ? 160.042 158.850 187.708 1.00 45.07  ? 544  THR A O     1 
ATOM   4259 C  CB    . THR A 1 543 ? 159.094 157.672 190.709 1.00 45.07  ? 544  THR A CB    1 
ATOM   4260 O  OG1   . THR A 1 543 ? 157.663 157.726 190.754 1.00 45.07  ? 544  THR A OG1   1 
ATOM   4261 C  CG2   . THR A 1 543 ? 159.644 159.046 190.984 1.00 45.07  ? 544  THR A CG2   1 
ATOM   4262 N  N     . ASP A 1 544 ? 157.898 158.141 187.848 1.00 45.91  ? 545  ASP A N     1 
ATOM   4263 C  CA    . ASP A 1 544 ? 157.470 158.827 186.630 1.00 45.91  ? 545  ASP A CA    1 
ATOM   4264 C  C     . ASP A 1 544 ? 157.625 160.346 186.705 1.00 45.91  ? 545  ASP A C     1 
ATOM   4265 O  O     . ASP A 1 544 ? 157.824 160.993 185.671 1.00 45.91  ? 545  ASP A O     1 
ATOM   4266 C  CB    . ASP A 1 544 ? 156.028 158.435 186.301 1.00 45.91  ? 545  ASP A CB    1 
ATOM   4267 C  CG    . ASP A 1 544 ? 155.076 158.592 187.481 1.00 45.91  ? 545  ASP A CG    1 
ATOM   4268 O  OD1   . ASP A 1 544 ? 155.375 159.326 188.445 1.00 45.91  ? 545  ASP A OD1   1 
ATOM   4269 O  OD2   . ASP A 1 544 ? 154.001 157.962 187.439 1.00 45.91  ? 545  ASP A OD2   1 
ATOM   4270 N  N     . MET A 1 545 ? 157.532 160.933 187.899 1.00 46.46  ? 546  MET A N     1 
ATOM   4271 C  CA    . MET A 1 545 ? 157.893 162.340 188.052 1.00 46.46  ? 546  MET A CA    1 
ATOM   4272 C  C     . MET A 1 545 ? 159.384 162.575 187.834 1.00 46.46  ? 546  MET A C     1 
ATOM   4273 O  O     . MET A 1 545 ? 159.775 163.600 187.268 1.00 46.46  ? 546  MET A O     1 
ATOM   4274 C  CB    . MET A 1 545 ? 157.482 162.826 189.439 1.00 46.46  ? 546  MET A CB    1 
ATOM   4275 C  CG    . MET A 1 545 ? 157.508 164.329 189.617 1.00 46.46  ? 546  MET A CG    1 
ATOM   4276 S  SD    . MET A 1 545 ? 156.459 165.185 188.434 1.00 46.46  ? 546  MET A SD    1 
ATOM   4277 C  CE    . MET A 1 545 ? 154.865 164.443 188.778 1.00 46.46  ? 546  MET A CE    1 
ATOM   4278 N  N     . THR A 1 546 ? 160.232 161.649 188.286 1.00 42.59  ? 547  THR A N     1 
ATOM   4279 C  CA    . THR A 1 546 ? 161.665 161.743 188.010 1.00 42.59  ? 547  THR A CA    1 
ATOM   4280 C  C     . THR A 1 546 ? 161.971 161.452 186.544 1.00 42.59  ? 547  THR A C     1 
ATOM   4281 O  O     . THR A 1 546 ? 162.870 162.067 185.956 1.00 42.59  ? 547  THR A O     1 
ATOM   4282 C  CB    . THR A 1 546 ? 162.440 160.809 188.942 1.00 42.59  ? 547  THR A CB    1 
ATOM   4283 O  OG1   . THR A 1 546 ? 162.094 161.110 190.297 1.00 42.59  ? 547  THR A OG1   1 
ATOM   4284 C  CG2   . THR A 1 546 ? 163.944 160.983 188.791 1.00 42.59  ? 547  THR A CG2   1 
ATOM   4285 N  N     . PHE A 1 547 ? 161.218 160.533 185.937 1.00 41.53  ? 548  PHE A N     1 
ATOM   4286 C  CA    . PHE A 1 547 ? 161.357 160.252 184.509 1.00 41.53  ? 548  PHE A CA    1 
ATOM   4287 C  C     . PHE A 1 547 ? 160.982 161.460 183.654 1.00 41.53  ? 548  PHE A C     1 
ATOM   4288 O  O     . PHE A 1 547 ? 161.712 161.810 182.719 1.00 41.53  ? 548  PHE A O     1 
ATOM   4289 C  CB    . PHE A 1 547 ? 160.513 159.020 184.153 1.00 41.53  ? 548  PHE A CB    1 
ATOM   4290 C  CG    . PHE A 1 547 ? 160.277 158.825 182.680 1.00 41.53  ? 548  PHE A CG    1 
ATOM   4291 C  CD1   . PHE A 1 547 ? 161.198 158.146 181.910 1.00 41.53  ? 548  PHE A CD1   1 
ATOM   4292 C  CD2   . PHE A 1 547 ? 159.094 159.234 182.084 1.00 41.53  ? 548  PHE A CD2   1 
ATOM   4293 C  CE1   . PHE A 1 547 ? 160.975 157.946 180.562 1.00 41.53  ? 548  PHE A CE1   1 
ATOM   4294 C  CE2   . PHE A 1 547 ? 158.880 159.034 180.743 1.00 41.53  ? 548  PHE A CE2   1 
ATOM   4295 C  CZ    . PHE A 1 547 ? 159.810 158.392 179.987 1.00 41.53  ? 548  PHE A CZ    1 
ATOM   4296 N  N     . LYS A 1 548 ? 159.821 162.069 183.932 1.00 44.66  ? 549  LYS A N     1 
ATOM   4297 C  CA    . LYS A 1 548 ? 159.369 163.273 183.227 1.00 44.66  ? 549  LYS A CA    1 
ATOM   4298 C  C     . LYS A 1 548 ? 160.385 164.408 183.300 1.00 44.66  ? 549  LYS A C     1 
ATOM   4299 O  O     . LYS A 1 548 ? 160.601 165.121 182.314 1.00 44.66  ? 549  LYS A O     1 
ATOM   4300 C  CB    . LYS A 1 548 ? 158.038 163.744 183.805 1.00 44.66  ? 549  LYS A CB    1 
ATOM   4301 C  CG    . LYS A 1 548 ? 157.417 164.883 183.035 1.00 44.66  ? 549  LYS A CG    1 
ATOM   4302 C  CD    . LYS A 1 548 ? 156.170 165.397 183.708 1.00 44.66  ? 549  LYS A CD    1 
ATOM   4303 C  CE    . LYS A 1 548 ? 156.515 166.178 184.952 1.00 44.66  ? 549  LYS A CE    1 
ATOM   4304 N  NZ    . LYS A 1 548 ? 157.051 167.526 184.631 1.00 44.66  ? 549  LYS A NZ    1 
ATOM   4305 N  N     . ALA A 1 549 ? 160.995 164.602 184.471 1.00 45.47  ? 550  ALA A N     1 
ATOM   4306 C  CA    . ALA A 1 549 ? 162.063 165.584 184.629 1.00 45.47  ? 550  ALA A CA    1 
ATOM   4307 C  C     . ALA A 1 549 ? 163.272 165.262 183.758 1.00 45.47  ? 550  ALA A C     1 
ATOM   4308 O  O     . ALA A 1 549 ? 163.911 166.172 183.218 1.00 45.47  ? 550  ALA A O     1 
ATOM   4309 C  CB    . ALA A 1 549 ? 162.476 165.676 186.098 1.00 45.47  ? 550  ALA A CB    1 
ATOM   4310 N  N     . LYS A 1 550 ? 163.631 163.980 183.654 1.00 44.12  ? 551  LYS A N     1 
ATOM   4311 C  CA    . LYS A 1 550 ? 164.754 163.576 182.811 1.00 44.12  ? 551  LYS A CA    1 
ATOM   4312 C  C     . LYS A 1 550 ? 164.514 163.871 181.330 1.00 44.12  ? 551  LYS A C     1 
ATOM   4313 O  O     . LYS A 1 550 ? 165.456 164.212 180.604 1.00 44.12  ? 551  LYS A O     1 
ATOM   4314 C  CB    . LYS A 1 550 ? 165.056 162.095 183.024 1.00 44.12  ? 551  LYS A CB    1 
ATOM   4315 C  CG    . LYS A 1 550 ? 166.414 161.684 182.492 1.00 44.12  ? 551  LYS A CG    1 
ATOM   4316 C  CD    . LYS A 1 550 ? 166.853 160.339 183.030 1.00 44.12  ? 551  LYS A CD    1 
ATOM   4317 C  CE    . LYS A 1 550 ? 168.205 159.948 182.459 1.00 44.12  ? 551  LYS A CE    1 
ATOM   4318 N  NZ    . LYS A 1 550 ? 168.756 158.741 183.124 1.00 44.12  ? 551  LYS A NZ    1 
ATOM   4319 N  N     . LEU A 1 551 ? 163.275 163.710 180.856 1.00 42.83  ? 552  LEU A N     1 
ATOM   4320 C  CA    . LEU A 1 551 ? 162.915 164.124 179.498 1.00 42.83  ? 552  LEU A CA    1 
ATOM   4321 C  C     . LEU A 1 551 ? 163.129 165.614 179.265 1.00 42.83  ? 552  LEU A C     1 
ATOM   4322 O  O     . LEU A 1 551 ? 163.813 166.007 178.313 1.00 42.83  ? 552  LEU A O     1 
ATOM   4323 C  CB    . LEU A 1 551 ? 161.464 163.755 179.192 1.00 42.83  ? 552  LEU A CB    1 
ATOM   4324 C  CG    . LEU A 1 551 ? 161.212 162.469 178.411 1.00 42.83  ? 552  LEU A CG    1 
ATOM   4325 C  CD1   . LEU A 1 551 ? 161.679 161.279 179.178 1.00 42.83  ? 552  LEU A CD1   1 
ATOM   4326 C  CD2   . LEU A 1 551 ? 159.744 162.344 178.114 1.00 42.83  ? 552  LEU A CD2   1 
ATOM   4327 N  N     . PHE A 1 552 ? 162.495 166.452 180.097 1.00 45.13  ? 553  PHE A N     1 
ATOM   4328 C  CA    . PHE A 1 552 ? 162.553 167.908 179.947 1.00 45.13  ? 553  PHE A CA    1 
ATOM   4329 C  C     . PHE A 1 552 ? 163.981 168.438 179.995 1.00 45.13  ? 553  PHE A C     1 
ATOM   4330 O  O     . PHE A 1 552 ? 164.351 169.306 179.199 1.00 45.13  ? 553  PHE A O     1 
ATOM   4331 C  CB    . PHE A 1 552 ? 161.701 168.578 181.023 1.00 45.13  ? 553  PHE A CB    1 
ATOM   4332 C  CG    . PHE A 1 552 ? 160.287 168.842 180.602 1.00 45.13  ? 553  PHE A CG    1 
ATOM   4333 C  CD1   . PHE A 1 552 ? 159.470 167.809 180.187 1.00 45.13  ? 553  PHE A CD1   1 
ATOM   4334 C  CD2   . PHE A 1 552 ? 159.766 170.121 180.655 1.00 45.13  ? 553  PHE A CD2   1 
ATOM   4335 C  CE1   . PHE A 1 552 ? 158.166 168.053 179.809 1.00 45.13  ? 553  PHE A CE1   1 
ATOM   4336 C  CE2   . PHE A 1 552 ? 158.462 170.369 180.283 1.00 45.13  ? 553  PHE A CE2   1 
ATOM   4337 C  CZ    . PHE A 1 552 ? 157.662 169.334 179.861 1.00 45.13  ? 553  PHE A CZ    1 
ATOM   4338 N  N     . ASP A 1 553 ? 164.780 167.954 180.944 1.00 44.84  ? 554  ASP A N     1 
ATOM   4339 C  CA    . ASP A 1 553 ? 166.165 168.397 181.052 1.00 44.84  ? 554  ASP A CA    1 
ATOM   4340 C  C     . ASP A 1 553 ? 166.982 168.009 179.822 1.00 44.84  ? 554  ASP A C     1 
ATOM   4341 O  O     . ASP A 1 553 ? 167.850 168.770 179.381 1.00 44.84  ? 554  ASP A O     1 
ATOM   4342 C  CB    . ASP A 1 553 ? 166.787 167.829 182.324 1.00 44.84  ? 554  ASP A CB    1 
ATOM   4343 C  CG    . ASP A 1 553 ? 166.150 168.394 183.578 1.00 44.84  ? 554  ASP A CG    1 
ATOM   4344 O  OD1   . ASP A 1 553 ? 165.528 169.474 183.493 1.00 44.84  ? 554  ASP A OD1   1 
ATOM   4345 O  OD2   . ASP A 1 553 ? 166.264 167.758 184.644 1.00 44.84  ? 554  ASP A OD2   1 
ATOM   4346 N  N     . ASN A 1 554 ? 166.735 166.822 179.265 1.00 45.38  ? 555  ASN A N     1 
ATOM   4347 C  CA    . ASN A 1 554 ? 167.450 166.403 178.065 1.00 45.38  ? 555  ASN A CA    1 
ATOM   4348 C  C     . ASN A 1 554 ? 166.938 167.047 176.778 1.00 45.38  ? 555  ASN A C     1 
ATOM   4349 O  O     . ASN A 1 554 ? 167.738 167.298 175.871 1.00 45.38  ? 555  ASN A O     1 
ATOM   4350 C  CB    . ASN A 1 554 ? 167.387 164.884 177.924 1.00 45.38  ? 555  ASN A CB    1 
ATOM   4351 C  CG    . ASN A 1 554 ? 168.294 164.176 178.894 1.00 45.38  ? 555  ASN A CG    1 
ATOM   4352 O  OD1   . ASN A 1 554 ? 169.006 164.810 179.668 1.00 45.38  ? 555  ASN A OD1   1 
ATOM   4353 N  ND2   . ASN A 1 554 ? 168.275 162.852 178.862 1.00 45.38  ? 555  ASN A ND2   1 
ATOM   4354 N  N     . HIS A 1 555 ? 165.632 167.300 176.651 1.00 43.53  ? 556  HIS A N     1 
ATOM   4355 C  CA    . HIS A 1 555 ? 165.066 167.622 175.343 1.00 43.53  ? 556  HIS A CA    1 
ATOM   4356 C  C     . HIS A 1 555 ? 164.460 169.008 175.181 1.00 43.53  ? 556  HIS A C     1 
ATOM   4357 O  O     . HIS A 1 555 ? 164.413 169.480 174.043 1.00 43.53  ? 556  HIS A O     1 
ATOM   4358 C  CB    . HIS A 1 555 ? 164.016 166.585 174.936 1.00 43.53  ? 556  HIS A CB    1 
ATOM   4359 C  CG    . HIS A 1 555 ? 164.573 165.210 174.775 1.00 43.53  ? 556  HIS A CG    1 
ATOM   4360 N  ND1   . HIS A 1 555 ? 163.887 164.076 175.145 1.00 43.53  ? 556  HIS A ND1   1 
ATOM   4361 C  CD2   . HIS A 1 555 ? 165.751 164.788 174.261 1.00 43.53  ? 556  HIS A CD2   1 
ATOM   4362 C  CE1   . HIS A 1 555 ? 164.624 163.013 174.876 1.00 43.53  ? 556  HIS A CE1   1 
ATOM   4363 N  NE2   . HIS A 1 555 ? 165.759 163.417 174.338 1.00 43.53  ? 556  HIS A NE2   1 
ATOM   4364 N  N     . LEU A 1 556 ? 163.937 169.637 176.239 1.00 46.71  ? 557  LEU A N     1 
ATOM   4365 C  CA    . LEU A 1 556 ? 163.326 170.962 176.100 1.00 46.71  ? 557  LEU A CA    1 
ATOM   4366 C  C     . LEU A 1 556 ? 164.346 171.989 175.625 1.00 46.71  ? 557  LEU A C     1 
ATOM   4367 O  O     . LEU A 1 556 ? 165.386 172.190 176.258 1.00 46.71  ? 557  LEU A O     1 
ATOM   4368 C  CB    . LEU A 1 556 ? 162.695 171.416 177.410 1.00 46.71  ? 557  LEU A CB    1 
ATOM   4369 C  CG    . LEU A 1 556 ? 161.890 172.701 177.254 1.00 46.71  ? 557  LEU A CG    1 
ATOM   4370 C  CD1   . LEU A 1 556 ? 160.578 172.395 176.575 1.00 46.71  ? 557  LEU A CD1   1 
ATOM   4371 C  CD2   . LEU A 1 556 ? 161.660 173.361 178.599 1.00 46.71  ? 557  LEU A CD2   1 
ATOM   4372 N  N     . GLY A 1 557 ? 164.041 172.628 174.496 1.00 46.63  ? 558  GLY A N     1 
ATOM   4373 C  CA    . GLY A 1 557 ? 164.953 173.517 173.807 1.00 46.63  ? 558  GLY A CA    1 
ATOM   4374 C  C     . GLY A 1 557 ? 166.093 172.841 173.076 1.00 46.63  ? 558  GLY A C     1 
ATOM   4375 O  O     . GLY A 1 557 ? 166.807 173.517 172.325 1.00 46.63  ? 558  GLY A O     1 
ATOM   4376 N  N     . LYS A 1 558 ? 166.291 171.539 173.262 1.00 43.88  ? 559  LYS A N     1 
ATOM   4377 C  CA    . LYS A 1 558 ? 167.293 170.762 172.550 1.00 43.88  ? 559  LYS A CA    1 
ATOM   4378 C  C     . LYS A 1 558 ? 166.692 169.932 171.425 1.00 43.88  ? 559  LYS A C     1 
ATOM   4379 O  O     . LYS A 1 558 ? 167.412 169.157 170.786 1.00 43.88  ? 559  LYS A O     1 
ATOM   4380 C  CB    . LYS A 1 558 ? 168.079 169.873 173.523 1.00 43.88  ? 559  LYS A CB    1 
ATOM   4381 C  CG    . LYS A 1 558 ? 169.201 170.601 174.279 1.00 43.88  ? 559  LYS A CG    1 
ATOM   4382 C  CD    . LYS A 1 558 ? 168.730 171.386 175.493 1.00 43.88  ? 559  LYS A CD    1 
ATOM   4383 C  CE    . LYS A 1 558 ? 168.290 170.474 176.608 1.00 43.88  ? 559  LYS A CE    1 
ATOM   4384 N  NZ    . LYS A 1 558 ? 167.732 171.245 177.749 1.00 43.88  ? 559  LYS A NZ    1 
ATOM   4385 N  N     . SER A 1 559 ? 165.391 170.070 171.180 1.00 43.36  ? 560  SER A N     1 
ATOM   4386 C  CA    . SER A 1 559 ? 164.774 169.610 169.946 1.00 43.36  ? 560  SER A CA    1 
ATOM   4387 C  C     . SER A 1 559 ? 163.570 170.495 169.667 1.00 43.36  ? 560  SER A C     1 
ATOM   4388 O  O     . SER A 1 559 ? 162.940 171.019 170.590 1.00 43.36  ? 560  SER A O     1 
ATOM   4389 C  CB    . SER A 1 559 ? 164.353 168.138 170.032 1.00 43.36  ? 560  SER A CB    1 
ATOM   4390 O  OG    . SER A 1 559 ? 165.482 167.283 170.030 1.00 43.36  ? 560  SER A OG    1 
ATOM   4391 N  N     . ALA A 1 560 ? 163.263 170.671 168.381 1.00 42.54  ? 561  ALA A N     1 
ATOM   4392 C  CA    . ALA A 1 560 ? 162.102 171.470 168.009 1.00 42.54  ? 561  ALA A CA    1 
ATOM   4393 C  C     . ALA A 1 560 ? 160.801 170.718 168.247 1.00 42.54  ? 561  ALA A C     1 
ATOM   4394 O  O     . ALA A 1 560 ? 159.793 171.319 168.631 1.00 42.54  ? 561  ALA A O     1 
ATOM   4395 C  CB    . ALA A 1 560 ? 162.211 171.902 166.549 1.00 42.54  ? 561  ALA A CB    1 
ATOM   4396 N  N     . ASN A 1 561 ? 160.804 169.403 168.030 1.00 39.13  ? 562  ASN A N     1 
ATOM   4397 C  CA    . ASN A 1 561 ? 159.576 168.627 168.097 1.00 39.13  ? 562  ASN A CA    1 
ATOM   4398 C  C     . ASN A 1 561 ? 159.095 168.377 169.518 1.00 39.13  ? 562  ASN A C     1 
ATOM   4399 O  O     . ASN A 1 561 ? 157.957 167.935 169.696 1.00 39.13  ? 562  ASN A O     1 
ATOM   4400 C  CB    . ASN A 1 561 ? 159.765 167.283 167.401 1.00 39.13  ? 562  ASN A CB    1 
ATOM   4401 C  CG    . ASN A 1 561 ? 160.170 167.428 165.963 1.00 39.13  ? 562  ASN A CG    1 
ATOM   4402 O  OD1   . ASN A 1 561 ? 161.347 167.599 165.656 1.00 39.13  ? 562  ASN A OD1   1 
ATOM   4403 N  ND2   . ASN A 1 561 ? 159.197 167.377 165.068 1.00 39.13  ? 562  ASN A ND2   1 
ATOM   4404 N  N     . PHE A 1 562 ? 159.916 168.634 170.528 1.00 44.99  ? 563  PHE A N     1 
ATOM   4405 C  CA    . PHE A 1 562 ? 159.533 168.416 171.914 1.00 44.99  ? 563  PHE A CA    1 
ATOM   4406 C  C     . PHE A 1 562 ? 159.156 169.752 172.536 1.00 44.99  ? 563  PHE A C     1 
ATOM   4407 O  O     . PHE A 1 562 ? 159.985 170.665 172.602 1.00 44.99  ? 563  PHE A O     1 
ATOM   4408 C  CB    . PHE A 1 562 ? 160.654 167.754 172.710 1.00 44.99  ? 563  PHE A CB    1 
ATOM   4409 C  CG    . PHE A 1 562 ? 160.277 167.445 174.124 1.00 44.99  ? 563  PHE A CG    1 
ATOM   4410 C  CD1   . PHE A 1 562 ? 159.468 166.358 174.408 1.00 44.99  ? 563  PHE A CD1   1 
ATOM   4411 C  CD2   . PHE A 1 562 ? 160.716 168.242 175.167 1.00 44.99  ? 563  PHE A CD2   1 
ATOM   4412 C  CE1   . PHE A 1 562 ? 159.105 166.067 175.703 1.00 44.99  ? 563  PHE A CE1   1 
ATOM   4413 C  CE2   . PHE A 1 562 ? 160.355 167.957 176.468 1.00 44.99  ? 563  PHE A CE2   1 
ATOM   4414 C  CZ    . PHE A 1 562 ? 159.548 166.867 176.735 1.00 44.99  ? 563  PHE A CZ    1 
ATOM   4415 N  N     . GLN A 1 563 ? 157.913 169.862 172.987 1.00 46.45  ? 564  GLN A N     1 
ATOM   4416 C  CA    . GLN A 1 563 ? 157.370 171.110 173.494 1.00 46.45  ? 564  GLN A CA    1 
ATOM   4417 C  C     . GLN A 1 563 ? 156.733 170.866 174.852 1.00 46.45  ? 564  GLN A C     1 
ATOM   4418 O  O     . GLN A 1 563 ? 156.477 169.728 175.250 1.00 46.45  ? 564  GLN A O     1 
ATOM   4419 C  CB    . GLN A 1 563 ? 156.341 171.736 172.545 1.00 46.45  ? 564  GLN A CB    1 
ATOM   4420 C  CG    . GLN A 1 563 ? 156.812 171.929 171.120 1.00 46.45  ? 564  GLN A CG    1 
ATOM   4421 C  CD    . GLN A 1 563 ? 155.870 172.802 170.318 1.00 46.45  ? 564  GLN A CD    1 
ATOM   4422 O  OE1   . GLN A 1 563 ? 154.658 172.780 170.530 1.00 46.45  ? 564  GLN A OE1   1 
ATOM   4423 N  NE2   . GLN A 1 563 ? 156.419 173.564 169.380 1.00 46.45  ? 564  GLN A NE2   1 
ATOM   4424 N  N     . LYS A 1 564 ? 156.473 171.960 175.553 1.00 47.47  ? 565  LYS A N     1 
ATOM   4425 C  CA    . LYS A 1 564 ? 155.772 171.895 176.815 1.00 47.47  ? 565  LYS A CA    1 
ATOM   4426 C  C     . LYS A 1 564 ? 154.302 171.588 176.540 1.00 47.47  ? 565  LYS A C     1 
ATOM   4427 O  O     . LYS A 1 564 ? 153.812 171.855 175.441 1.00 47.47  ? 565  LYS A O     1 
ATOM   4428 C  CB    . LYS A 1 564 ? 155.935 173.227 177.553 1.00 47.47  ? 565  LYS A CB    1 
ATOM   4429 C  CG    . LYS A 1 564 ? 157.355 173.514 177.997 1.00 47.47  ? 565  LYS A CG    1 
ATOM   4430 C  CD    . LYS A 1 564 ? 157.388 174.525 179.126 1.00 47.47  ? 565  LYS A CD    1 
ATOM   4431 C  CE    . LYS A 1 564 ? 157.664 175.923 178.620 1.00 47.47  ? 565  LYS A CE    1 
ATOM   4432 N  NZ    . LYS A 1 564 ? 157.650 176.906 179.737 1.00 47.47  ? 565  LYS A NZ    1 
ATOM   4433 N  N     . PRO A 1 565 ? 153.581 170.992 177.497 1.00 50.16  ? 566  PRO A N     1 
ATOM   4434 C  CA    . PRO A 1 565 ? 152.172 170.684 177.238 1.00 50.16  ? 566  PRO A CA    1 
ATOM   4435 C  C     . PRO A 1 565 ? 151.305 171.927 177.152 1.00 50.16  ? 566  PRO A C     1 
ATOM   4436 O  O     . PRO A 1 565 ? 151.564 172.954 177.782 1.00 50.16  ? 566  PRO A O     1 
ATOM   4437 C  CB    . PRO A 1 565 ? 151.761 169.806 178.423 1.00 50.16  ? 566  PRO A CB    1 
ATOM   4438 C  CG    . PRO A 1 565 ? 152.753 170.017 179.458 1.00 50.16  ? 566  PRO A CG    1 
ATOM   4439 C  CD    . PRO A 1 565 ? 153.996 170.560 178.846 1.00 50.16  ? 566  PRO A CD    1 
ATOM   4440 N  N     . ARG A 1 566 ? 150.265 171.807 176.337 1.00 54.33  ? 567  ARG A N     1 
ATOM   4441 C  CA    . ARG A 1 566 ? 149.224 172.807 176.160 1.00 54.33  ? 567  ARG A CA    1 
ATOM   4442 C  C     . ARG A 1 566 ? 147.920 172.292 176.768 1.00 54.33  ? 567  ARG A C     1 
ATOM   4443 O  O     . ARG A 1 566 ? 147.030 171.793 176.080 1.00 54.33  ? 567  ARG A O     1 
ATOM   4444 C  CB    . ARG A 1 566 ? 149.132 173.141 174.641 1.00 54.33  ? 567  ARG A CB    1 
ATOM   4445 C  CG    . ARG A 1 566 ? 149.121 171.911 173.717 1.00 54.33  ? 567  ARG A CG    1 
ATOM   4446 C  CD    . ARG A 1 566 ? 148.635 172.232 172.324 1.00 54.33  ? 567  ARG A CD    1 
ATOM   4447 N  NE    . ARG A 1 566 ? 148.195 171.032 171.631 1.00 54.33  ? 567  ARG A NE    1 
ATOM   4448 C  CZ    . ARG A 1 566 ? 147.243 171.002 170.706 1.00 54.33  ? 567  ARG A CZ    1 
ATOM   4449 N  NH1   . ARG A 1 566 ? 146.759 169.846 170.283 1.00 54.33  ? 567  ARG A NH1   1 
ATOM   4450 N  NH2   . ARG A 1 566 ? 146.677 172.133 170.312 1.00 54.33  ? 567  ARG A NH2   1 
ATOM   4451 N  N     . ASN A 1 567 ? 147.804 172.427 178.087 1.00 58.95  ? 568  ASN A N     1 
ATOM   4452 C  CA    . ASN A 1 567 ? 146.597 171.967 178.763 1.00 58.95  ? 568  ASN A CA    1 
ATOM   4453 C  C     . ASN A 1 567 ? 145.447 172.920 178.464 1.00 58.95  ? 568  ASN A C     1 
ATOM   4454 O  O     . ASN A 1 567 ? 145.406 174.047 178.967 1.00 58.95  ? 568  ASN A O     1 
ATOM   4455 C  CB    . ASN A 1 567 ? 146.844 171.853 180.263 1.00 58.95  ? 568  ASN A CB    1 
ATOM   4456 C  CG    . ASN A 1 567 ? 148.058 171.009 180.586 1.00 58.95  ? 568  ASN A CG    1 
ATOM   4457 O  OD1   . ASN A 1 567 ? 147.985 169.780 180.600 1.00 58.95  ? 568  ASN A OD1   1 
ATOM   4458 N  ND2   . ASN A 1 567 ? 149.183 171.663 180.850 1.00 58.95  ? 568  ASN A ND2   1 
ATOM   4459 N  N     . ILE A 1 568 ? 144.517 172.455 177.643 1.00 64.43  ? 569  ILE A N     1 
ATOM   4460 C  CA    . ILE A 1 568 ? 143.269 173.154 177.363 1.00 64.43  ? 569  ILE A CA    1 
ATOM   4461 C  C     . ILE A 1 568 ? 142.307 172.894 178.517 1.00 64.43  ? 569  ILE A C     1 
ATOM   4462 O  O     . ILE A 1 568 ? 142.448 171.906 179.247 1.00 64.43  ? 569  ILE A O     1 
ATOM   4463 C  CB    . ILE A 1 568 ? 142.703 172.687 176.001 1.00 64.43  ? 569  ILE A CB    1 
ATOM   4464 C  CG1   . ILE A 1 568 ? 143.800 172.639 174.929 1.00 64.43  ? 569  ILE A CG1   1 
ATOM   4465 C  CG2   . ILE A 1 568 ? 141.626 173.630 175.469 1.00 64.43  ? 569  ILE A CG2   1 
ATOM   4466 C  CD1   . ILE A 1 568 ? 144.552 173.961 174.706 1.00 64.43  ? 569  ILE A CD1   1 
ATOM   4467 N  N     . LYS A 1 569 ? 141.362 173.815 178.730 1.00 66.82  ? 570  LYS A N     1 
ATOM   4468 C  CA    . LYS A 1 569 ? 140.358 173.641 179.771 1.00 66.82  ? 570  LYS A CA    1 
ATOM   4469 C  C     . LYS A 1 569 ? 139.476 172.434 179.464 1.00 66.82  ? 570  LYS A C     1 
ATOM   4470 O  O     . LYS A 1 569 ? 139.222 172.101 178.304 1.00 66.82  ? 570  LYS A O     1 
ATOM   4471 C  CB    . LYS A 1 569 ? 139.485 174.892 179.888 1.00 66.82  ? 570  LYS A CB    1 
ATOM   4472 C  CG    . LYS A 1 569 ? 140.219 176.160 180.288 1.00 66.82  ? 570  LYS A CG    1 
ATOM   4473 C  CD    . LYS A 1 569 ? 141.120 175.940 181.489 1.00 66.82  ? 570  LYS A CD    1 
ATOM   4474 C  CE    . LYS A 1 569 ? 141.778 177.240 181.914 1.00 66.82  ? 570  LYS A CE    1 
ATOM   4475 N  NZ    . LYS A 1 569 ? 142.105 178.100 180.745 1.00 66.82  ? 570  LYS A NZ    1 
ATOM   4476 N  N     . GLY A 1 570 ? 139.208 171.649 180.510 1.00 66.86  ? 571  GLY A N     1 
ATOM   4477 C  CA    . GLY A 1 570 ? 138.475 170.387 180.307 1.00 66.86  ? 571  GLY A CA    1 
ATOM   4478 C  C     . GLY A 1 570 ? 139.452 169.249 180.071 1.00 66.86  ? 571  GLY A C     1 
ATOM   4479 O  O     . GLY A 1 570 ? 139.606 168.416 180.984 1.00 66.86  ? 571  GLY A O     1 
ATOM   4480 N  N     . LYS A 1 571 ? 140.121 169.233 178.913 1.00 62.41  ? 572  LYS A N     1 
ATOM   4481 C  CA    . LYS A 1 571 ? 141.028 168.107 178.559 1.00 62.41  ? 572  LYS A CA    1 
ATOM   4482 C  C     . LYS A 1 571 ? 141.870 167.695 179.761 1.00 62.41  ? 572  LYS A C     1 
ATOM   4483 O  O     . LYS A 1 571 ? 142.381 168.576 180.459 1.00 62.41  ? 572  LYS A O     1 
ATOM   4484 C  CB    . LYS A 1 571 ? 141.946 168.493 177.401 1.00 62.41  ? 572  LYS A CB    1 
ATOM   4485 C  CG    . LYS A 1 571 ? 142.959 167.433 176.990 1.00 62.41  ? 572  LYS A CG    1 
ATOM   4486 C  CD    . LYS A 1 571 ? 142.419 166.458 175.966 1.00 62.41  ? 572  LYS A CD    1 
ATOM   4487 C  CE    . LYS A 1 571 ? 140.995 166.762 175.555 1.00 62.41  ? 572  LYS A CE    1 
ATOM   4488 N  NZ    . LYS A 1 571 ? 140.807 166.662 174.089 1.00 62.41  ? 572  LYS A NZ    1 
ATOM   4489 N  N     . PRO A 1 572 ? 142.022 166.384 180.011 1.00 60.08  ? 573  PRO A N     1 
ATOM   4490 C  CA    . PRO A 1 572 ? 142.805 165.906 181.138 1.00 60.08  ? 573  PRO A CA    1 
ATOM   4491 C  C     . PRO A 1 572 ? 144.205 166.530 181.232 1.00 60.08  ? 573  PRO A C     1 
ATOM   4492 O  O     . PRO A 1 572 ? 144.624 167.159 180.283 1.00 60.08  ? 573  PRO A O     1 
ATOM   4493 C  CB    . PRO A 1 572 ? 142.945 164.423 180.786 1.00 60.08  ? 573  PRO A CB    1 
ATOM   4494 C  CG    . PRO A 1 572 ? 141.654 164.091 180.091 1.00 60.08  ? 573  PRO A CG    1 
ATOM   4495 C  CD    . PRO A 1 572 ? 141.396 165.311 179.239 1.00 60.08  ? 573  PRO A CD    1 
ATOM   4496 N  N     . GLU A 1 573 ? 144.903 166.332 182.358 1.00 56.36  ? 574  GLU A N     1 
ATOM   4497 C  CA    . GLU A 1 573 ? 146.260 166.837 182.499 1.00 56.36  ? 574  GLU A CA    1 
ATOM   4498 C  C     . GLU A 1 573 ? 147.187 166.042 181.588 1.00 56.36  ? 574  GLU A C     1 
ATOM   4499 O  O     . GLU A 1 573 ? 147.122 164.810 181.538 1.00 56.36  ? 574  GLU A O     1 
ATOM   4500 C  CB    . GLU A 1 573 ? 146.724 166.735 183.952 1.00 56.36  ? 574  GLU A CB    1 
ATOM   4501 C  CG    . GLU A 1 573 ? 148.107 167.325 184.236 1.00 56.36  ? 574  GLU A CG    1 
ATOM   4502 C  CD    . GLU A 1 573 ? 148.092 168.832 184.452 1.00 56.36  ? 574  GLU A CD    1 
ATOM   4503 O  OE1   . GLU A 1 573 ? 148.330 169.271 185.598 1.00 56.36  ? 574  GLU A OE1   1 
ATOM   4504 O  OE2   . GLU A 1 573 ? 147.849 169.581 183.485 1.00 56.36  ? 574  GLU A OE2   1 
ATOM   4505 N  N     . ALA A 1 574 ? 148.046 166.753 180.869 1.00 51.22  ? 575  ALA A N     1 
ATOM   4506 C  CA    . ALA A 1 574 ? 149.015 166.163 179.963 1.00 51.22  ? 575  ALA A CA    1 
ATOM   4507 C  C     . ALA A 1 574 ? 150.385 166.710 180.318 1.00 51.22  ? 575  ALA A C     1 
ATOM   4508 O  O     . ALA A 1 574 ? 150.510 167.850 180.769 1.00 51.22  ? 575  ALA A O     1 
ATOM   4509 C  CB    . ALA A 1 574 ? 148.683 166.470 178.506 1.00 51.22  ? 575  ALA A CB    1 
ATOM   4510 N  N     . HIS A 1 575 ? 151.414 165.884 180.141 1.00 47.23  ? 576  HIS A N     1 
ATOM   4511 C  CA    . HIS A 1 575 ? 152.737 166.265 180.603 1.00 47.23  ? 576  HIS A CA    1 
ATOM   4512 C  C     . HIS A 1 575 ? 153.734 166.669 179.523 1.00 47.23  ? 576  HIS A C     1 
ATOM   4513 O  O     . HIS A 1 575 ? 154.747 167.286 179.871 1.00 47.23  ? 576  HIS A O     1 
ATOM   4514 C  CB    . HIS A 1 575 ? 153.304 165.123 181.446 1.00 47.23  ? 576  HIS A CB    1 
ATOM   4515 C  CG    . HIS A 1 575 ? 152.461 164.811 182.640 1.00 47.23  ? 576  HIS A CG    1 
ATOM   4516 N  ND1   . HIS A 1 575 ? 152.277 165.707 183.670 1.00 47.23  ? 576  HIS A ND1   1 
ATOM   4517 C  CD2   . HIS A 1 575 ? 151.706 163.729 182.945 1.00 47.23  ? 576  HIS A CD2   1 
ATOM   4518 C  CE1   . HIS A 1 575 ? 151.472 165.177 184.574 1.00 47.23  ? 576  HIS A CE1   1 
ATOM   4519 N  NE2   . HIS A 1 575 ? 151.114 163.976 184.159 1.00 47.23  ? 576  HIS A NE2   1 
ATOM   4520 N  N     . PHE A 1 576 ? 153.481 166.384 178.243 1.00 44.34  ? 577  PHE A N     1 
ATOM   4521 C  CA    . PHE A 1 576 ? 154.208 167.060 177.170 1.00 44.34  ? 577  PHE A CA    1 
ATOM   4522 C  C     . PHE A 1 576 ? 153.373 167.016 175.899 1.00 44.34  ? 577  PHE A C     1 
ATOM   4523 O  O     . PHE A 1 576 ? 152.314 166.392 175.845 1.00 44.34  ? 577  PHE A O     1 
ATOM   4524 C  CB    . PHE A 1 576 ? 155.627 166.490 176.925 1.00 44.34  ? 577  PHE A CB    1 
ATOM   4525 C  CG    . PHE A 1 576 ? 155.702 165.010 176.620 1.00 44.34  ? 577  PHE A CG    1 
ATOM   4526 C  CD1   . PHE A 1 576 ? 155.378 164.499 175.366 1.00 44.34  ? 577  PHE A CD1   1 
ATOM   4527 C  CD2   . PHE A 1 576 ? 156.146 164.133 177.585 1.00 44.34  ? 577  PHE A CD2   1 
ATOM   4528 C  CE1   . PHE A 1 576 ? 155.477 163.153 175.099 1.00 44.34  ? 577  PHE A CE1   1 
ATOM   4529 C  CE2   . PHE A 1 576 ? 156.242 162.790 177.316 1.00 44.34  ? 577  PHE A CE2   1 
ATOM   4530 C  CZ    . PHE A 1 576 ? 155.904 162.297 176.077 1.00 44.34  ? 577  PHE A CZ    1 
ATOM   4531 N  N     . SER A 1 577 ? 153.876 167.703 174.879 1.00 43.55  ? 578  SER A N     1 
ATOM   4532 C  CA    . SER A 1 577 ? 153.278 167.755 173.554 1.00 43.55  ? 578  SER A CA    1 
ATOM   4533 C  C     . SER A 1 577 ? 154.365 167.416 172.545 1.00 43.55  ? 578  SER A C     1 
ATOM   4534 O  O     . SER A 1 577 ? 155.469 167.963 172.620 1.00 43.55  ? 578  SER A O     1 
ATOM   4535 C  CB    . SER A 1 577 ? 152.663 169.120 173.255 1.00 43.55  ? 578  SER A CB    1 
ATOM   4536 O  OG    . SER A 1 577 ? 153.612 169.979 172.663 1.00 43.55  ? 578  SER A OG    1 
ATOM   4537 N  N     . LEU A 1 578 ? 154.060 166.525 171.608 1.00 36.39  ? 579  LEU A N     1 
ATOM   4538 C  CA    . LEU A 1 578 ? 154.957 166.204 170.506 1.00 36.39  ? 579  LEU A CA    1 
ATOM   4539 C  C     . LEU A 1 578 ? 154.425 166.799 169.215 1.00 36.39  ? 579  LEU A C     1 
ATOM   4540 O  O     . LEU A 1 578 ? 153.212 166.868 169.008 1.00 36.39  ? 579  LEU A O     1 
ATOM   4541 C  CB    . LEU A 1 578 ? 155.129 164.701 170.335 1.00 36.39  ? 579  LEU A CB    1 
ATOM   4542 C  CG    . LEU A 1 578 ? 156.029 164.091 171.390 1.00 36.39  ? 579  LEU A CG    1 
ATOM   4543 C  CD1   . LEU A 1 578 ? 155.957 162.590 171.356 1.00 36.39  ? 579  LEU A CD1   1 
ATOM   4544 C  CD2   . LEU A 1 578 ? 157.419 164.559 171.134 1.00 36.39  ? 579  LEU A CD2   1 
ATOM   4545 N  N     . ILE A 1 579 ? 155.336 167.229 168.347 1.00 32.67  ? 580  ILE A N     1 
ATOM   4546 C  CA    . ILE A 1 579 ? 154.939 167.651 167.012 1.00 32.67  ? 580  ILE A CA    1 
ATOM   4547 C  C     . ILE A 1 579 ? 155.107 166.489 166.047 1.00 32.67  ? 580  ILE A C     1 
ATOM   4548 O  O     . ILE A 1 579 ? 156.084 166.416 165.295 1.00 32.67  ? 580  ILE A O     1 
ATOM   4549 C  CB    . ILE A 1 579 ? 155.762 168.869 166.555 1.00 32.67  ? 580  ILE A CB    1 
ATOM   4550 C  CG1   . ILE A 1 579 ? 155.834 169.914 167.665 1.00 32.67  ? 580  ILE A CG1   1 
ATOM   4551 C  CG2   . ILE A 1 579 ? 155.135 169.517 165.332 1.00 32.67  ? 580  ILE A CG2   1 
ATOM   4552 C  CD1   . ILE A 1 579 ? 154.495 170.463 168.079 1.00 32.67  ? 580  ILE A CD1   1 
ATOM   4553 N  N     . HIS A 1 580 ? 154.169 165.548 166.098 1.00 27.61  ? 581  HIS A N     1 
ATOM   4554 C  CA    . HIS A 1 580 ? 154.072 164.502 165.095 1.00 27.61  ? 581  HIS A CA    1 
ATOM   4555 C  C     . HIS A 1 580 ? 153.679 165.102 163.751 1.00 27.61  ? 581  HIS A C     1 
ATOM   4556 O  O     . HIS A 1 580 ? 153.219 166.244 163.668 1.00 27.61  ? 581  HIS A O     1 
ATOM   4557 C  CB    . HIS A 1 580 ? 153.081 163.427 165.523 1.00 27.61  ? 581  HIS A CB    1 
ATOM   4558 C  CG    . HIS A 1 580 ? 153.645 162.459 166.511 1.00 27.61  ? 581  HIS A CG    1 
ATOM   4559 N  ND1   . HIS A 1 580 ? 153.525 162.630 167.872 1.00 27.61  ? 581  HIS A ND1   1 
ATOM   4560 C  CD2   . HIS A 1 580 ? 154.351 161.319 166.337 1.00 27.61  ? 581  HIS A CD2   1 
ATOM   4561 C  CE1   . HIS A 1 580 ? 154.123 161.631 168.494 1.00 27.61  ? 581  HIS A CE1   1 
ATOM   4562 N  NE2   . HIS A 1 580 ? 154.633 160.822 167.585 1.00 27.61  ? 581  HIS A NE2   1 
ATOM   4563 N  N     . TYR A 1 581 ? 153.900 164.316 162.690 1.00 24.44  ? 582  TYR A N     1 
ATOM   4564 C  CA    . TYR A 1 581 ? 153.703 164.785 161.318 1.00 24.44  ? 582  TYR A CA    1 
ATOM   4565 C  C     . TYR A 1 581 ? 152.277 165.262 161.047 1.00 24.44  ? 582  TYR A C     1 
ATOM   4566 O  O     . TYR A 1 581 ? 152.078 166.262 160.349 1.00 24.44  ? 582  TYR A O     1 
ATOM   4567 C  CB    . TYR A 1 581 ? 154.115 163.683 160.339 1.00 24.44  ? 582  TYR A CB    1 
ATOM   4568 C  CG    . TYR A 1 581 ? 153.170 162.509 160.187 1.00 24.44  ? 582  TYR A CG    1 
ATOM   4569 C  CD1   . TYR A 1 581 ? 153.253 161.415 161.034 1.00 24.44  ? 582  TYR A CD1   1 
ATOM   4570 C  CD2   . TYR A 1 581 ? 152.233 162.471 159.167 1.00 24.44  ? 582  TYR A CD2   1 
ATOM   4571 C  CE1   . TYR A 1 581 ? 152.402 160.336 160.890 1.00 24.44  ? 582  TYR A CE1   1 
ATOM   4572 C  CE2   . TYR A 1 581 ? 151.381 161.398 159.016 1.00 24.44  ? 582  TYR A CE2   1 
ATOM   4573 C  CZ    . TYR A 1 581 ? 151.471 160.336 159.877 1.00 24.44  ? 582  TYR A CZ    1 
ATOM   4574 O  OH    . TYR A 1 581 ? 150.626 159.267 159.707 1.00 24.44  ? 582  TYR A OH    1 
ATOM   4575 N  N     . ALA A 1 582 ? 151.275 164.581 161.595 1.00 29.60  ? 583  ALA A N     1 
ATOM   4576 C  CA    . ALA A 1 582 ? 149.888 164.945 161.348 1.00 29.60  ? 583  ALA A CA    1 
ATOM   4577 C  C     . ALA A 1 582 ? 149.237 165.738 162.475 1.00 29.60  ? 583  ALA A C     1 
ATOM   4578 O  O     . ALA A 1 582 ? 148.035 166.002 162.399 1.00 29.60  ? 583  ALA A O     1 
ATOM   4579 C  CB    . ALA A 1 582 ? 149.063 163.691 161.064 1.00 29.60  ? 583  ALA A CB    1 
ATOM   4580 N  N     . GLY A 1 583 ? 149.967 166.119 163.510 1.00 30.17  ? 584  GLY A N     1 
ATOM   4581 C  CA    . GLY A 1 583 ? 149.325 166.906 164.544 1.00 30.17  ? 584  GLY A CA    1 
ATOM   4582 C  C     . GLY A 1 583 ? 150.113 166.946 165.829 1.00 30.17  ? 584  GLY A C     1 
ATOM   4583 O  O     . GLY A 1 583 ? 151.074 166.207 166.032 1.00 30.17  ? 584  GLY A O     1 
ATOM   4584 N  N     . ILE A 1 584 ? 149.681 167.858 166.696 1.00 34.90  ? 585  ILE A N     1 
ATOM   4585 C  CA    . ILE A 1 584 ? 150.285 168.086 168.004 1.00 34.90  ? 585  ILE A CA    1 
ATOM   4586 C  C     . ILE A 1 584 ? 149.559 167.208 169.022 1.00 34.90  ? 585  ILE A C     1 
ATOM   4587 O  O     . ILE A 1 584 ? 148.377 167.422 169.298 1.00 34.90  ? 585  ILE A O     1 
ATOM   4588 C  CB    . ILE A 1 584 ? 150.202 169.564 168.392 1.00 34.90  ? 585  ILE A CB    1 
ATOM   4589 C  CG1   . ILE A 1 584 ? 150.883 170.420 167.324 1.00 34.90  ? 585  ILE A CG1   1 
ATOM   4590 C  CG2   . ILE A 1 584 ? 150.832 169.784 169.752 1.00 34.90  ? 585  ILE A CG2   1 
ATOM   4591 C  CD1   . ILE A 1 584 ? 151.009 171.881 167.682 1.00 34.90  ? 585  ILE A CD1   1 
ATOM   4592 N  N     . VAL A 1 585 ? 150.259 166.229 169.593 1.00 33.22  ? 586  VAL A N     1 
ATOM   4593 C  CA    . VAL A 1 585 ? 149.654 165.216 170.455 1.00 33.22  ? 586  VAL A CA    1 
ATOM   4594 C  C     . VAL A 1 585 ? 150.140 165.428 171.884 1.00 33.22  ? 586  VAL A C     1 
ATOM   4595 O  O     . VAL A 1 585 ? 151.350 165.459 172.132 1.00 33.22  ? 586  VAL A O     1 
ATOM   4596 C  CB    . VAL A 1 585 ? 149.988 163.799 169.963 1.00 33.22  ? 586  VAL A CB    1 
ATOM   4597 C  CG1   . VAL A 1 585 ? 149.239 162.773 170.771 1.00 33.22  ? 586  VAL A CG1   1 
ATOM   4598 C  CG2   . VAL A 1 585 ? 149.649 163.656 168.495 1.00 33.22  ? 586  VAL A CG2   1 
ATOM   4599 N  N     . ASP A 1 586 ? 149.195 165.566 172.824 1.00 38.11  ? 587  ASP A N     1 
ATOM   4600 C  CA    . ASP A 1 586 ? 149.481 165.930 174.220 1.00 38.11  ? 587  ASP A CA    1 
ATOM   4601 C  C     . ASP A 1 586 ? 149.471 164.713 175.154 1.00 38.11  ? 587  ASP A C     1 
ATOM   4602 O  O     . ASP A 1 586 ? 148.504 164.434 175.860 1.00 38.11  ? 587  ASP A O     1 
ATOM   4603 C  CB    . ASP A 1 586 ? 148.509 167.022 174.669 1.00 38.11  ? 587  ASP A CB    1 
ATOM   4604 C  CG    . ASP A 1 586 ? 147.060 166.676 174.383 1.00 38.11  ? 587  ASP A CG    1 
ATOM   4605 O  OD1   . ASP A 1 586 ? 146.788 166.119 173.301 1.00 38.11  ? 587  ASP A OD1   1 
ATOM   4606 O  OD2   . ASP A 1 586 ? 146.193 166.970 175.232 1.00 38.11  ? 587  ASP A OD2   1 
ATOM   4607 N  N     . TYR A 1 587 ? 150.578 163.969 175.124 1.00 36.09  ? 588  TYR A N     1 
ATOM   4608 C  CA    . TYR A 1 587 ? 150.774 162.749 175.911 1.00 36.09  ? 588  TYR A CA    1 
ATOM   4609 C  C     . TYR A 1 587 ? 150.667 162.967 177.423 1.00 36.09  ? 588  TYR A C     1 
ATOM   4610 O  O     . TYR A 1 587 ? 150.972 164.040 177.947 1.00 36.09  ? 588  TYR A O     1 
ATOM   4611 C  CB    . TYR A 1 587 ? 152.117 162.120 175.568 1.00 36.09  ? 588  TYR A CB    1 
ATOM   4612 C  CG    . TYR A 1 587 ? 152.117 161.501 174.200 1.00 36.09  ? 588  TYR A CG    1 
ATOM   4613 C  CD1   . TYR A 1 587 ? 151.705 160.195 174.015 1.00 36.09  ? 588  TYR A CD1   1 
ATOM   4614 C  CD2   . TYR A 1 587 ? 152.498 162.230 173.088 1.00 36.09  ? 588  TYR A CD2   1 
ATOM   4615 C  CE1   . TYR A 1 587 ? 151.690 159.626 172.767 1.00 36.09  ? 588  TYR A CE1   1 
ATOM   4616 C  CE2   . TYR A 1 587 ? 152.484 161.667 171.835 1.00 36.09  ? 588  TYR A CE2   1 
ATOM   4617 C  CZ    . TYR A 1 587 ? 152.078 160.366 171.682 1.00 36.09  ? 588  TYR A CZ    1 
ATOM   4618 O  OH    . TYR A 1 587 ? 152.059 159.802 170.434 1.00 36.09  ? 588  TYR A OH    1 
ATOM   4619 N  N     . ASN A 1 588 ? 150.213 161.918 178.118 1.00 38.47  ? 589  ASN A N     1 
ATOM   4620 C  CA    . ASN A 1 588 ? 150.119 161.851 179.577 1.00 38.47  ? 589  ASN A CA    1 
ATOM   4621 C  C     . ASN A 1 588 ? 151.049 160.743 180.059 1.00 38.47  ? 589  ASN A C     1 
ATOM   4622 O  O     . ASN A 1 588 ? 150.908 159.589 179.644 1.00 38.47  ? 589  ASN A O     1 
ATOM   4623 C  CB    . ASN A 1 588 ? 148.664 161.599 180.003 1.00 38.47  ? 589  ASN A CB    1 
ATOM   4624 C  CG    . ASN A 1 588 ? 148.429 161.674 181.522 1.00 38.47  ? 589  ASN A CG    1 
ATOM   4625 O  OD1   . ASN A 1 588 ? 149.237 161.246 182.346 1.00 38.47  ? 589  ASN A OD1   1 
ATOM   4626 N  ND2   . ASN A 1 588 ? 147.288 162.245 181.886 1.00 38.47  ? 589  ASN A ND2   1 
ATOM   4627 N  N     . ILE A 1 589 ? 151.985 161.091 180.950 1.00 38.09  ? 590  ILE A N     1 
ATOM   4628 C  CA    . ILE A 1 589 ? 153.173 160.281 181.210 1.00 38.09  ? 590  ILE A CA    1 
ATOM   4629 C  C     . ILE A 1 589 ? 153.034 159.377 182.436 1.00 38.09  ? 590  ILE A C     1 
ATOM   4630 O  O     . ILE A 1 589 ? 153.920 158.541 182.681 1.00 38.09  ? 590  ILE A O     1 
ATOM   4631 C  CB    . ILE A 1 589 ? 154.397 161.213 181.366 1.00 38.09  ? 590  ILE A CB    1 
ATOM   4632 C  CG1   . ILE A 1 589 ? 155.680 160.520 180.950 1.00 38.09  ? 590  ILE A CG1   1 
ATOM   4633 C  CG2   . ILE A 1 589 ? 154.541 161.726 182.793 1.00 38.09  ? 590  ILE A CG2   1 
ATOM   4634 C  CD1   . ILE A 1 589 ? 155.670 160.137 179.552 1.00 38.09  ? 590  ILE A CD1   1 
ATOM   4635 N  N     . ILE A 1 590 ? 151.936 159.489 183.189 1.00 38.77  ? 591  ILE A N     1 
ATOM   4636 C  CA    . ILE A 1 590 ? 151.655 158.670 184.372 1.00 38.77  ? 591  ILE A CA    1 
ATOM   4637 C  C     . ILE A 1 590 ? 151.691 157.166 184.113 1.00 38.77  ? 591  ILE A C     1 
ATOM   4638 O  O     . ILE A 1 590 ? 150.884 156.632 183.344 1.00 38.77  ? 591  ILE A O     1 
ATOM   4639 C  CB    . ILE A 1 590 ? 150.299 159.058 184.984 1.00 38.77  ? 591  ILE A CB    1 
ATOM   4640 C  CG1   . ILE A 1 590 ? 150.318 160.509 185.455 1.00 38.77  ? 591  ILE A CG1   1 
ATOM   4641 C  CG2   . ILE A 1 590 ? 149.972 158.157 186.157 1.00 38.77  ? 591  ILE A CG2   1 
ATOM   4642 C  CD1   . ILE A 1 590 ? 148.962 161.013 185.887 1.00 38.77  ? 591  ILE A CD1   1 
ATOM   4643 N  N     . GLY A 1 591 ? 152.620 156.475 184.764 1.00 36.70  ? 592  GLY A N     1 
ATOM   4644 C  CA    . GLY A 1 591 ? 152.648 155.031 184.749 1.00 36.70  ? 592  GLY A CA    1 
ATOM   4645 C  C     . GLY A 1 591 ? 153.420 154.346 183.641 1.00 36.70  ? 592  GLY A C     1 
ATOM   4646 O  O     . GLY A 1 591 ? 153.320 153.118 183.532 1.00 36.70  ? 592  GLY A O     1 
ATOM   4647 N  N     . TRP A 1 592 ? 154.131 155.085 182.781 1.00 33.76  ? 593  TRP A N     1 
ATOM   4648 C  CA    . TRP A 1 592 ? 154.838 154.453 181.665 1.00 33.76  ? 593  TRP A CA    1 
ATOM   4649 C  C     . TRP A 1 592 ? 155.937 153.504 182.125 1.00 33.76  ? 593  TRP A C     1 
ATOM   4650 O  O     . TRP A 1 592 ? 156.240 152.532 181.427 1.00 33.76  ? 593  TRP A O     1 
ATOM   4651 C  CB    . TRP A 1 592 ? 155.471 155.481 180.737 1.00 33.76  ? 593  TRP A CB    1 
ATOM   4652 C  CG    . TRP A 1 592 ? 154.546 156.249 179.875 1.00 33.76  ? 593  TRP A CG    1 
ATOM   4653 C  CD1   . TRP A 1 592 ? 153.220 156.463 180.069 1.00 33.76  ? 593  TRP A CD1   1 
ATOM   4654 C  CD2   . TRP A 1 592 ? 154.880 156.882 178.640 1.00 33.76  ? 593  TRP A CD2   1 
ATOM   4655 N  NE1   . TRP A 1 592 ? 152.711 157.222 179.047 1.00 33.76  ? 593  TRP A NE1   1 
ATOM   4656 C  CE2   . TRP A 1 592 ? 153.714 157.492 178.155 1.00 33.76  ? 593  TRP A CE2   1 
ATOM   4657 C  CE3   . TRP A 1 592 ? 156.062 157.011 177.907 1.00 33.76  ? 593  TRP A CE3   1 
ATOM   4658 C  CZ2   . TRP A 1 592 ? 153.690 158.211 176.967 1.00 33.76  ? 593  TRP A CZ2   1 
ATOM   4659 C  CZ3   . TRP A 1 592 ? 156.038 157.731 176.734 1.00 33.76  ? 593  TRP A CZ3   1 
ATOM   4660 C  CH2   . TRP A 1 592 ? 154.861 158.319 176.273 1.00 33.76  ? 593  TRP A CH2   1 
ATOM   4661 N  N     . LEU A 1 593 ? 156.556 153.782 183.275 1.00 35.60  ? 594  LEU A N     1 
ATOM   4662 C  CA    . LEU A 1 593 ? 157.640 152.942 183.784 1.00 35.60  ? 594  LEU A CA    1 
ATOM   4663 C  C     . LEU A 1 593 ? 157.202 151.530 184.152 1.00 35.60  ? 594  LEU A C     1 
ATOM   4664 O  O     . LEU A 1 593 ? 158.016 150.603 184.071 1.00 35.60  ? 594  LEU A O     1 
ATOM   4665 C  CB    . LEU A 1 593 ? 158.293 153.612 184.984 1.00 35.60  ? 594  LEU A CB    1 
ATOM   4666 C  CG    . LEU A 1 593 ? 159.010 154.892 184.590 1.00 35.60  ? 594  LEU A CG    1 
ATOM   4667 C  CD1   . LEU A 1 593 ? 159.491 155.610 185.816 1.00 35.60  ? 594  LEU A CD1   1 
ATOM   4668 C  CD2   . LEU A 1 593 ? 160.161 154.548 183.687 1.00 35.60  ? 594  LEU A CD2   1 
ATOM   4669 N  N     . GLN A 1 594 ? 155.951 151.326 184.563 1.00 34.58  ? 595  GLN A N     1 
ATOM   4670 C  CA    . GLN A 1 594 ? 155.510 149.940 184.677 1.00 34.58  ? 595  GLN A CA    1 
ATOM   4671 C  C     . GLN A 1 594 ? 155.043 149.390 183.335 1.00 34.58  ? 595  GLN A C     1 
ATOM   4672 O  O     . GLN A 1 594 ? 155.275 148.216 183.045 1.00 34.58  ? 595  GLN A O     1 
ATOM   4673 C  CB    . GLN A 1 594 ? 154.437 149.776 185.760 1.00 34.58  ? 595  GLN A CB    1 
ATOM   4674 C  CG    . GLN A 1 594 ? 153.138 150.527 185.583 1.00 34.58  ? 595  GLN A CG    1 
ATOM   4675 C  CD    . GLN A 1 594 ? 153.090 151.787 186.419 1.00 34.58  ? 595  GLN A CD    1 
ATOM   4676 O  OE1   . GLN A 1 594 ? 154.117 152.277 186.884 1.00 34.58  ? 595  GLN A OE1   1 
ATOM   4677 N  NE2   . GLN A 1 594 ? 151.888 152.304 186.636 1.00 34.58  ? 595  GLN A NE2   1 
ATOM   4678 N  N     . LYS A 1 595 ? 154.388 150.211 182.506 1.00 30.42  ? 596  LYS A N     1 
ATOM   4679 C  CA    . LYS A 1 595 ? 153.890 149.752 181.210 1.00 30.42  ? 596  LYS A CA    1 
ATOM   4680 C  C     . LYS A 1 595 ? 154.998 149.327 180.255 1.00 30.42  ? 596  LYS A C     1 
ATOM   4681 O  O     . LYS A 1 595 ? 154.746 148.526 179.352 1.00 30.42  ? 596  LYS A O     1 
ATOM   4682 C  CB    . LYS A 1 595 ? 153.062 150.847 180.543 1.00 30.42  ? 596  LYS A CB    1 
ATOM   4683 C  CG    . LYS A 1 595 ? 151.704 151.058 181.160 1.00 30.42  ? 596  LYS A CG    1 
ATOM   4684 C  CD    . LYS A 1 595 ? 150.859 151.985 180.318 1.00 30.42  ? 596  LYS A CD    1 
ATOM   4685 C  CE    . LYS A 1 595 ? 149.446 152.048 180.853 1.00 30.42  ? 596  LYS A CE    1 
ATOM   4686 N  NZ    . LYS A 1 595 ? 148.555 152.838 179.971 1.00 30.42  ? 596  LYS A NZ    1 
ATOM   4687 N  N     . ASN A 1 596 ? 156.212 149.836 180.434 1.00 34.66  ? 597  ASN A N     1 
ATOM   4688 C  CA    . ASN A 1 596 ? 157.328 149.485 179.570 1.00 34.66  ? 597  ASN A CA    1 
ATOM   4689 C  C     . ASN A 1 596 ? 158.013 148.175 179.946 1.00 34.66  ? 597  ASN A C     1 
ATOM   4690 O  O     . ASN A 1 596 ? 158.879 147.716 179.196 1.00 34.66  ? 597  ASN A O     1 
ATOM   4691 C  CB    . ASN A 1 596 ? 158.339 150.635 179.585 1.00 34.66  ? 597  ASN A CB    1 
ATOM   4692 C  CG    . ASN A 1 596 ? 159.209 150.672 178.354 1.00 34.66  ? 597  ASN A CG    1 
ATOM   4693 O  OD1   . ASN A 1 596 ? 160.306 150.128 178.345 1.00 34.66  ? 597  ASN A OD1   1 
ATOM   4694 N  ND2   . ASN A 1 596 ? 158.724 151.321 177.304 1.00 34.66  ? 597  ASN A ND2   1 
ATOM   4695 N  N     . LYS A 1 597 ? 157.656 147.549 181.066 1.00 36.50  ? 598  LYS A N     1 
ATOM   4696 C  CA    . LYS A 1 597 ? 158.328 146.310 181.441 1.00 36.50  ? 598  LYS A CA    1 
ATOM   4697 C  C     . LYS A 1 597 ? 157.351 145.252 181.942 1.00 36.50  ? 598  LYS A C     1 
ATOM   4698 O  O     . LYS A 1 597 ? 157.514 144.064 181.645 1.00 36.50  ? 598  LYS A O     1 
ATOM   4699 C  CB    . LYS A 1 597 ? 159.392 146.587 182.503 1.00 36.50  ? 598  LYS A CB    1 
ATOM   4700 C  CG    . LYS A 1 597 ? 160.385 145.452 182.686 1.00 36.50  ? 598  LYS A CG    1 
ATOM   4701 C  CD    . LYS A 1 597 ? 161.454 145.811 183.704 1.00 36.50  ? 598  LYS A CD    1 
ATOM   4702 C  CE    . LYS A 1 597 ? 162.498 144.714 183.823 1.00 36.50  ? 598  LYS A CE    1 
ATOM   4703 N  NZ    . LYS A 1 597 ? 163.504 145.022 184.877 1.00 36.50  ? 598  LYS A NZ    1 
ATOM   4704 N  N     . ASP A 1 598 ? 156.324 145.699 182.679 1.00 41.62  ? 599  ASP A N     1 
ATOM   4705 C  CA    . ASP A 1 598 ? 155.129 145.000 183.160 1.00 41.62  ? 599  ASP A CA    1 
ATOM   4706 C  C     . ASP A 1 598 ? 155.402 143.613 183.733 1.00 41.62  ? 599  ASP A C     1 
ATOM   4707 O  O     . ASP A 1 598 ? 154.992 142.611 183.134 1.00 41.62  ? 599  ASP A O     1 
ATOM   4708 C  CB    . ASP A 1 598 ? 154.104 144.908 182.028 1.00 41.62  ? 599  ASP A CB    1 
ATOM   4709 C  CG    . ASP A 1 598 ? 152.677 145.020 182.527 1.00 41.62  ? 599  ASP A CG    1 
ATOM   4710 O  OD1   . ASP A 1 598 ? 152.473 145.008 183.758 1.00 41.62  ? 599  ASP A OD1   1 
ATOM   4711 O  OD2   . ASP A 1 598 ? 151.760 145.142 181.690 1.00 41.62  ? 599  ASP A OD2   1 
ATOM   4712 N  N     . PRO A 1 599 ? 156.119 143.505 184.854 1.00 42.66  ? 600  PRO A N     1 
ATOM   4713 C  CA    . PRO A 1 599 ? 156.566 142.186 185.314 1.00 42.66  ? 600  PRO A CA    1 
ATOM   4714 C  C     . PRO A 1 599 ? 155.434 141.393 185.950 1.00 42.66  ? 600  PRO A C     1 
ATOM   4715 O  O     . PRO A 1 599 ? 154.568 141.939 186.638 1.00 42.66  ? 600  PRO A O     1 
ATOM   4716 C  CB    . PRO A 1 599 ? 157.649 142.529 186.341 1.00 42.66  ? 600  PRO A CB    1 
ATOM   4717 C  CG    . PRO A 1 599 ? 157.194 143.827 186.906 1.00 42.66  ? 600  PRO A CG    1 
ATOM   4718 C  CD    . PRO A 1 599 ? 156.555 144.576 185.769 1.00 42.66  ? 600  PRO A CD    1 
ATOM   4719 N  N     . LEU A 1 600 ? 155.427 140.094 185.684 1.00 42.83  ? 601  LEU A N     1 
ATOM   4720 C  CA    . LEU A 1 600 ? 154.394 139.218 186.213 1.00 42.83  ? 601  LEU A CA    1 
ATOM   4721 C  C     . LEU A 1 600 ? 154.775 138.700 187.598 1.00 42.83  ? 601  LEU A C     1 
ATOM   4722 O  O     . LEU A 1 600 ? 155.944 138.693 187.988 1.00 42.83  ? 601  LEU A O     1 
ATOM   4723 C  CB    . LEU A 1 600 ? 154.129 138.058 185.255 1.00 42.83  ? 601  LEU A CB    1 
ATOM   4724 C  CG    . LEU A 1 600 ? 153.887 138.440 183.795 1.00 42.83  ? 601  LEU A CG    1 
ATOM   4725 C  CD1   . LEU A 1 600 ? 153.475 137.227 183.013 1.00 42.83  ? 601  LEU A CD1   1 
ATOM   4726 C  CD2   . LEU A 1 600 ? 152.805 139.498 183.692 1.00 42.83  ? 601  LEU A CD2   1 
ATOM   4727 N  N     . ASN A 1 601 ? 153.760 138.259 188.338 1.00 48.87  ? 602  ASN A N     1 
ATOM   4728 C  CA    . ASN A 1 601 ? 153.959 137.487 189.560 1.00 48.87  ? 602  ASN A CA    1 
ATOM   4729 C  C     . ASN A 1 601 ? 154.499 136.122 189.150 1.00 48.87  ? 602  ASN A C     1 
ATOM   4730 O  O     . ASN A 1 601 ? 153.771 135.318 188.564 1.00 48.87  ? 602  ASN A O     1 
ATOM   4731 C  CB    . ASN A 1 601 ? 152.635 137.401 190.323 1.00 48.87  ? 602  ASN A CB    1 
ATOM   4732 C  CG    . ASN A 1 601 ? 152.706 136.616 191.654 1.00 48.87  ? 602  ASN A CG    1 
ATOM   4733 O  OD1   . ASN A 1 601 ? 153.409 135.620 191.823 1.00 48.87  ? 602  ASN A OD1   1 
ATOM   4734 N  ND2   . ASN A 1 601 ? 151.933 137.098 192.617 1.00 48.87  ? 602  ASN A ND2   1 
ATOM   4735 N  N     . GLU A 1 602 ? 155.781 135.881 189.448 1.00 46.80  ? 603  GLU A N     1 
ATOM   4736 C  CA    . GLU A 1 602 ? 156.484 134.668 189.027 1.00 46.80  ? 603  GLU A CA    1 
ATOM   4737 C  C     . GLU A 1 602 ? 155.847 133.384 189.557 1.00 46.80  ? 603  GLU A C     1 
ATOM   4738 O  O     . GLU A 1 602 ? 155.903 132.347 188.886 1.00 46.80  ? 603  GLU A O     1 
ATOM   4739 C  CB    . GLU A 1 602 ? 157.944 134.742 189.470 1.00 46.80  ? 603  GLU A CB    1 
ATOM   4740 C  CG    . GLU A 1 602 ? 158.692 135.953 188.942 1.00 46.80  ? 603  GLU A CG    1 
ATOM   4741 C  CD    . GLU A 1 602 ? 159.073 135.821 187.482 1.00 46.80  ? 603  GLU A CD    1 
ATOM   4742 O  OE1   . GLU A 1 602 ? 159.984 135.024 187.177 1.00 46.80  ? 603  GLU A OE1   1 
ATOM   4743 O  OE2   . GLU A 1 602 ? 158.468 136.519 186.641 1.00 46.80  ? 603  GLU A OE2   1 
ATOM   4744 N  N     . THR A 1 603 ? 155.248 133.426 190.748 1.00 51.38  ? 604  THR A N     1 
ATOM   4745 C  CA    . THR A 1 603 ? 154.661 132.222 191.333 1.00 51.38  ? 604  THR A CA    1 
ATOM   4746 C  C     . THR A 1 603 ? 153.372 131.820 190.623 1.00 51.38  ? 604  THR A C     1 
ATOM   4747 O  O     . THR A 1 603 ? 153.173 130.641 190.307 1.00 51.38  ? 604  THR A O     1 
ATOM   4748 C  CB    . THR A 1 603 ? 154.413 132.438 192.829 1.00 51.38  ? 604  THR A CB    1 
ATOM   4749 O  OG1   . THR A 1 603 ? 155.665 132.650 193.491 1.00 51.38  ? 604  THR A OG1   1 
ATOM   4750 C  CG2   . THR A 1 603 ? 153.728 131.237 193.456 1.00 51.38  ? 604  THR A CG2   1 
ATOM   4751 N  N     . VAL A 1 604 ? 152.489 132.789 190.360 1.00 47.32  ? 605  VAL A N     1 
ATOM   4752 C  CA    . VAL A 1 604 ? 151.222 132.509 189.686 1.00 47.32  ? 605  VAL A CA    1 
ATOM   4753 C  C     . VAL A 1 604 ? 151.460 132.033 188.255 1.00 47.32  ? 605  VAL A C     1 
ATOM   4754 O  O     . VAL A 1 604 ? 150.733 131.170 187.745 1.00 47.32  ? 605  VAL A O     1 
ATOM   4755 C  CB    . VAL A 1 604 ? 150.316 133.753 189.739 1.00 47.32  ? 605  VAL A CB    1 
ATOM   4756 C  CG1   . VAL A 1 604 ? 148.956 133.474 189.125 1.00 47.32  ? 605  VAL A CG1   1 
ATOM   4757 C  CG2   . VAL A 1 604 ? 150.157 134.211 191.162 1.00 47.32  ? 605  VAL A CG2   1 
ATOM   4758 N  N     . VAL A 1 605 ? 152.477 132.586 187.588 1.00 45.53  ? 606  VAL A N     1 
ATOM   4759 C  CA    . VAL A 1 605 ? 152.901 132.084 186.281 1.00 45.53  ? 606  VAL A CA    1 
ATOM   4760 C  C     . VAL A 1 605 ? 153.353 130.629 186.379 1.00 45.53  ? 606  VAL A C     1 
ATOM   4761 O  O     . VAL A 1 605 ? 153.076 129.814 185.487 1.00 45.53  ? 606  VAL A O     1 
ATOM   4762 C  CB    . VAL A 1 605 ? 153.998 133.003 185.710 1.00 45.53  ? 606  VAL A CB    1 
ATOM   4763 C  CG1   . VAL A 1 605 ? 154.606 132.437 184.442 1.00 45.53  ? 606  VAL A CG1   1 
ATOM   4764 C  CG2   . VAL A 1 605 ? 153.421 134.369 185.433 1.00 45.53  ? 606  VAL A CG2   1 
ATOM   4765 N  N     . GLY A 1 606 ? 154.012 130.269 187.484 1.00 47.97  ? 607  GLY A N     1 
ATOM   4766 C  CA    . GLY A 1 606 ? 154.320 128.870 187.745 1.00 47.97  ? 607  GLY A CA    1 
ATOM   4767 C  C     . GLY A 1 606 ? 153.099 127.984 187.905 1.00 47.97  ? 607  GLY A C     1 
ATOM   4768 O  O     . GLY A 1 606 ? 153.151 126.791 187.598 1.00 47.97  ? 607  GLY A O     1 
ATOM   4769 N  N     . LEU A 1 607 ? 151.985 128.547 188.377 1.00 46.11  ? 608  LEU A N     1 
ATOM   4770 C  CA    . LEU A 1 607 ? 150.733 127.797 188.394 1.00 46.11  ? 608  LEU A CA    1 
ATOM   4771 C  C     . LEU A 1 607 ? 150.150 127.648 186.994 1.00 46.11  ? 608  LEU A C     1 
ATOM   4772 O  O     . LEU A 1 607 ? 149.589 126.595 186.667 1.00 46.11  ? 608  LEU A O     1 
ATOM   4773 C  CB    . LEU A 1 607 ? 149.728 128.462 189.329 1.00 46.11  ? 608  LEU A CB    1 
ATOM   4774 C  CG    . LEU A 1 607 ? 150.239 128.737 190.740 1.00 46.11  ? 608  LEU A CG    1 
ATOM   4775 C  CD1   . LEU A 1 607 ? 149.150 129.378 191.570 1.00 46.11  ? 608  LEU A CD1   1 
ATOM   4776 C  CD2   . LEU A 1 607 ? 150.732 127.461 191.391 1.00 46.11  ? 608  LEU A CD2   1 
ATOM   4777 N  N     . TYR A 1 608 ? 150.222 128.708 186.178 1.00 41.76  ? 609  TYR A N     1 
ATOM   4778 C  CA    . TYR A 1 608 ? 149.771 128.624 184.788 1.00 41.76  ? 609  TYR A CA    1 
ATOM   4779 C  C     . TYR A 1 608 ? 150.575 127.595 184.009 1.00 41.76  ? 609  TYR A C     1 
ATOM   4780 O  O     . TYR A 1 608 ? 150.026 126.877 183.167 1.00 41.76  ? 609  TYR A O     1 
ATOM   4781 C  CB    . TYR A 1 608 ? 149.872 129.983 184.090 1.00 41.76  ? 609  TYR A CB    1 
ATOM   4782 C  CG    . TYR A 1 608 ? 148.972 131.098 184.588 1.00 41.76  ? 609  TYR A CG    1 
ATOM   4783 C  CD1   . TYR A 1 608 ? 147.959 130.867 185.504 1.00 41.76  ? 609  TYR A CD1   1 
ATOM   4784 C  CD2   . TYR A 1 608 ? 149.137 132.391 184.116 1.00 41.76  ? 609  TYR A CD2   1 
ATOM   4785 C  CE1   . TYR A 1 608 ? 147.151 131.894 185.940 1.00 41.76  ? 609  TYR A CE1   1 
ATOM   4786 C  CE2   . TYR A 1 608 ? 148.335 133.417 184.544 1.00 41.76  ? 609  TYR A CE2   1 
ATOM   4787 C  CZ    . TYR A 1 608 ? 147.346 133.164 185.454 1.00 41.76  ? 609  TYR A CZ    1 
ATOM   4788 O  OH    . TYR A 1 608 ? 146.544 134.190 185.882 1.00 41.76  ? 609  TYR A OH    1 
ATOM   4789 N  N     . GLN A 1 609 ? 151.884 127.525 184.259 1.00 44.98  ? 610  GLN A N     1 
ATOM   4790 C  CA    . GLN A 1 609 ? 152.700 126.447 183.712 1.00 44.98  ? 610  GLN A CA    1 
ATOM   4791 C  C     . GLN A 1 609 ? 152.320 125.067 184.241 1.00 44.98  ? 610  GLN A C     1 
ATOM   4792 O  O     . GLN A 1 609 ? 152.669 124.063 183.612 1.00 44.98  ? 610  GLN A O     1 
ATOM   4793 C  CB    . GLN A 1 609 ? 154.174 126.705 184.011 1.00 44.98  ? 610  GLN A CB    1 
ATOM   4794 C  CG    . GLN A 1 609 ? 154.785 127.822 183.203 1.00 44.98  ? 610  GLN A CG    1 
ATOM   4795 C  CD    . GLN A 1 609 ? 156.271 127.955 183.445 1.00 44.98  ? 610  GLN A CD    1 
ATOM   4796 O  OE1   . GLN A 1 609 ? 156.803 127.420 184.416 1.00 44.98  ? 610  GLN A OE1   1 
ATOM   4797 N  NE2   . GLN A 1 609 ? 156.953 128.662 182.554 1.00 44.98  ? 610  GLN A NE2   1 
ATOM   4798 N  N     . LYS A 1 610 ? 151.614 124.984 185.370 1.00 44.96  ? 611  LYS A N     1 
ATOM   4799 C  CA    . LYS A 1 610 ? 151.149 123.712 185.903 1.00 44.96  ? 611  LYS A CA    1 
ATOM   4800 C  C     . LYS A 1 610 ? 149.636 123.547 185.723 1.00 44.96  ? 611  LYS A C     1 
ATOM   4801 O  O     . LYS A 1 610 ? 149.016 122.695 186.367 1.00 44.96  ? 611  LYS A O     1 
ATOM   4802 C  CB    . LYS A 1 610 ? 151.571 123.609 187.375 1.00 44.96  ? 611  LYS A CB    1 
ATOM   4803 C  CG    . LYS A 1 610 ? 151.679 122.201 187.971 1.00 44.96  ? 611  LYS A CG    1 
ATOM   4804 C  CD    . LYS A 1 610 ? 151.986 122.254 189.453 1.00 44.96  ? 611  LYS A CD    1 
ATOM   4805 C  CE    . LYS A 1 610 ? 150.801 122.808 190.223 1.00 44.96  ? 611  LYS A CE    1 
ATOM   4806 N  NZ    . LYS A 1 610 ? 149.623 121.901 190.148 1.00 44.96  ? 611  LYS A NZ    1 
ATOM   4807 N  N     . SER A 1 611 ? 149.025 124.370 184.874 1.00 40.90  ? 612  SER A N     1 
ATOM   4808 C  CA    . SER A 1 611 ? 147.607 124.222 184.567 1.00 40.90  ? 612  SER A CA    1 
ATOM   4809 C  C     . SER A 1 611 ? 147.330 122.905 183.849 1.00 40.90  ? 612  SER A C     1 
ATOM   4810 O  O     . SER A 1 611 ? 148.160 122.391 183.096 1.00 40.90  ? 612  SER A O     1 
ATOM   4811 C  CB    . SER A 1 611 ? 147.112 125.386 183.715 1.00 40.90  ? 612  SER A CB    1 
ATOM   4812 O  OG    . SER A 1 611 ? 145.773 125.167 183.306 1.00 40.90  ? 612  SER A OG    1 
ATOM   4813 N  N     . SER A 1 612 ? 146.141 122.356 184.102 1.00 39.70  ? 613  SER A N     1 
ATOM   4814 C  CA    . SER A 1 612 ? 145.658 121.211 183.341 1.00 39.70  ? 613  SER A CA    1 
ATOM   4815 C  C     . SER A 1 612 ? 145.278 121.573 181.913 1.00 39.70  ? 613  SER A C     1 
ATOM   4816 O  O     . SER A 1 612 ? 145.256 120.690 181.050 1.00 39.70  ? 613  SER A O     1 
ATOM   4817 C  CB    . SER A 1 612 ? 144.454 120.584 184.044 1.00 39.70  ? 613  SER A CB    1 
ATOM   4818 O  OG    . SER A 1 612 ? 143.470 121.562 184.336 1.00 39.70  ? 613  SER A OG    1 
ATOM   4819 N  N     . LEU A 1 613 ? 144.973 122.840 181.647 1.00 35.10  ? 614  LEU A N     1 
ATOM   4820 C  CA    . LEU A 1 613 ? 144.501 123.259 180.334 1.00 35.10  ? 614  LEU A CA    1 
ATOM   4821 C  C     . LEU A 1 613 ? 145.689 123.348 179.383 1.00 35.10  ? 614  LEU A C     1 
ATOM   4822 O  O     . LEU A 1 613 ? 146.611 124.136 179.615 1.00 35.10  ? 614  LEU A O     1 
ATOM   4823 C  CB    . LEU A 1 613 ? 143.775 124.598 180.444 1.00 35.10  ? 614  LEU A CB    1 
ATOM   4824 C  CG    . LEU A 1 613 ? 142.902 125.058 179.281 1.00 35.10  ? 614  LEU A CG    1 
ATOM   4825 C  CD1   . LEU A 1 613 ? 141.621 124.262 179.261 1.00 35.10  ? 614  LEU A CD1   1 
ATOM   4826 C  CD2   . LEU A 1 613 ? 142.590 126.530 179.404 1.00 35.10  ? 614  LEU A CD2   1 
ATOM   4827 N  N     . LYS A 1 614 ? 145.679 122.493 178.350 1.00 34.17  ? 615  LYS A N     1 
ATOM   4828 C  CA    . LYS A 1 614 ? 146.799 122.347 177.416 1.00 34.17  ? 615  LYS A CA    1 
ATOM   4829 C  C     . LYS A 1 614 ? 147.144 123.653 176.705 1.00 34.17  ? 615  LYS A C     1 
ATOM   4830 O  O     . LYS A 1 614 ? 148.314 123.887 176.379 1.00 34.17  ? 615  LYS A O     1 
ATOM   4831 C  CB    . LYS A 1 614 ? 146.471 121.217 176.424 1.00 34.17  ? 615  LYS A CB    1 
ATOM   4832 C  CG    . LYS A 1 614 ? 147.441 120.949 175.248 1.00 34.17  ? 615  LYS A CG    1 
ATOM   4833 C  CD    . LYS A 1 614 ? 147.063 121.676 173.948 1.00 34.17  ? 615  LYS A CD    1 
ATOM   4834 C  CE    . LYS A 1 614 ? 147.997 121.315 172.807 1.00 34.17  ? 615  LYS A CE    1 
ATOM   4835 N  NZ    . LYS A 1 614 ? 147.414 121.691 171.490 1.00 34.17  ? 615  LYS A NZ    1 
ATOM   4836 N  N     . LEU A 1 615 ? 146.144 124.493 176.430 1.00 30.34  ? 616  LEU A N     1 
ATOM   4837 C  CA    . LEU A 1 615 ? 146.400 125.822 175.883 1.00 30.34  ? 616  LEU A CA    1 
ATOM   4838 C  C     . LEU A 1 615 ? 147.205 126.679 176.853 1.00 30.34  ? 616  LEU A C     1 
ATOM   4839 O  O     . LEU A 1 615 ? 148.264 127.202 176.499 1.00 30.34  ? 616  LEU A O     1 
ATOM   4840 C  CB    . LEU A 1 615 ? 145.086 126.510 175.526 1.00 30.34  ? 616  LEU A CB    1 
ATOM   4841 C  CG    . LEU A 1 615 ? 145.228 127.922 174.969 1.00 30.34  ? 616  LEU A CG    1 
ATOM   4842 C  CD1   . LEU A 1 615 ? 145.973 127.871 173.662 1.00 30.34  ? 616  LEU A CD1   1 
ATOM   4843 C  CD2   . LEU A 1 615 ? 143.875 128.562 174.775 1.00 30.34  ? 616  LEU A CD2   1 
ATOM   4844 N  N     . LEU A 1 616 ? 146.683 126.869 178.070 1.00 34.14  ? 617  LEU A N     1 
ATOM   4845 C  CA    . LEU A 1 616 ? 147.295 127.771 179.046 1.00 34.14  ? 617  LEU A CA    1 
ATOM   4846 C  C     . LEU A 1 616 ? 148.693 127.317 179.462 1.00 34.14  ? 617  LEU A C     1 
ATOM   4847 O  O     . LEU A 1 616 ? 149.572 128.149 179.712 1.00 34.14  ? 617  LEU A O     1 
ATOM   4848 C  CB    . LEU A 1 616 ? 146.390 127.890 180.267 1.00 34.14  ? 617  LEU A CB    1 
ATOM   4849 C  CG    . LEU A 1 616 ? 146.798 128.921 181.309 1.00 34.14  ? 617  LEU A CG    1 
ATOM   4850 C  CD1   . LEU A 1 616 ? 146.692 130.299 180.707 1.00 34.14  ? 617  LEU A CD1   1 
ATOM   4851 C  CD2   . LEU A 1 616 ? 145.933 128.806 182.538 1.00 34.14  ? 617  LEU A CD2   1 
ATOM   4852 N  N     . SER A 1 617 ? 148.915 126.004 179.550 1.00 37.12  ? 618  SER A N     1 
ATOM   4853 C  CA    . SER A 1 617 ? 150.263 125.479 179.758 1.00 37.12  ? 618  SER A CA    1 
ATOM   4854 C  C     . SER A 1 617 ? 151.195 125.787 178.593 1.00 37.12  ? 618  SER A C     1 
ATOM   4855 O  O     . SER A 1 617 ? 152.400 125.972 178.796 1.00 37.12  ? 618  SER A O     1 
ATOM   4856 C  CB    . SER A 1 617 ? 150.214 123.973 179.992 1.00 37.12  ? 618  SER A CB    1 
ATOM   4857 O  OG    . SER A 1 617 ? 151.525 123.444 180.085 1.00 37.12  ? 618  SER A OG    1 
ATOM   4858 N  N     . THR A 1 618 ? 150.668 125.819 177.369 1.00 33.65  ? 619  THR A N     1 
ATOM   4859 C  CA    . THR A 1 618 ? 151.478 126.207 176.219 1.00 33.65  ? 619  THR A CA    1 
ATOM   4860 C  C     . THR A 1 618 ? 151.779 127.704 176.226 1.00 33.65  ? 619  THR A C     1 
ATOM   4861 O  O     . THR A 1 618 ? 152.900 128.112 175.898 1.00 33.65  ? 619  THR A O     1 
ATOM   4862 C  CB    . THR A 1 618 ? 150.770 125.794 174.928 1.00 33.65  ? 619  THR A CB    1 
ATOM   4863 O  OG1   . THR A 1 618 ? 150.485 124.392 174.976 1.00 33.65  ? 619  THR A OG1   1 
ATOM   4864 C  CG2   . THR A 1 618 ? 151.631 126.072 173.709 1.00 33.65  ? 619  THR A CG2   1 
ATOM   4865 N  N     . LEU A 1 619 ? 150.785 128.531 176.589 1.00 30.95  ? 620  LEU A N     1 
ATOM   4866 C  CA    . LEU A 1 619 ? 150.915 129.988 176.527 1.00 30.95  ? 620  LEU A CA    1 
ATOM   4867 C  C     . LEU A 1 619 ? 152.033 130.534 177.405 1.00 30.95  ? 620  LEU A C     1 
ATOM   4868 O  O     . LEU A 1 619 ? 152.666 131.530 177.042 1.00 30.95  ? 620  LEU A O     1 
ATOM   4869 C  CB    . LEU A 1 619 ? 149.607 130.653 176.943 1.00 30.95  ? 620  LEU A CB    1 
ATOM   4870 C  CG    . LEU A 1 619 ? 148.355 130.449 176.106 1.00 30.95  ? 620  LEU A CG    1 
ATOM   4871 C  CD1   . LEU A 1 619 ? 147.274 131.383 176.577 1.00 30.95  ? 620  LEU A CD1   1 
ATOM   4872 C  CD2   . LEU A 1 619 ? 148.672 130.706 174.680 1.00 30.95  ? 620  LEU A CD2   1 
ATOM   4873 N  N     . PHE A 1 620 ? 152.293 129.915 178.552 1.00 35.93  ? 621  PHE A N     1 
ATOM   4874 C  CA    . PHE A 1 620 ? 153.341 130.390 179.445 1.00 35.93  ? 621  PHE A CA    1 
ATOM   4875 C  C     . PHE A 1 620 ? 154.542 129.460 179.522 1.00 35.93  ? 621  PHE A C     1 
ATOM   4876 O  O     . PHE A 1 620 ? 155.368 129.616 180.428 1.00 35.93  ? 621  PHE A O     1 
ATOM   4877 C  CB    . PHE A 1 620 ? 152.776 130.646 180.842 1.00 35.93  ? 621  PHE A CB    1 
ATOM   4878 C  CG    . PHE A 1 620 ? 151.894 131.854 180.921 1.00 35.93  ? 621  PHE A CG    1 
ATOM   4879 C  CD1   . PHE A 1 620 ? 150.548 131.773 180.626 1.00 35.93  ? 621  PHE A CD1   1 
ATOM   4880 C  CD2   . PHE A 1 620 ? 152.423 133.078 181.287 1.00 35.93  ? 621  PHE A CD2   1 
ATOM   4881 C  CE1   . PHE A 1 620 ? 149.747 132.891 180.699 1.00 35.93  ? 621  PHE A CE1   1 
ATOM   4882 C  CE2   . PHE A 1 620 ? 151.626 134.194 181.363 1.00 35.93  ? 621  PHE A CE2   1 
ATOM   4883 C  CZ    . PHE A 1 620 ? 150.289 134.101 181.070 1.00 35.93  ? 621  PHE A CZ    1 
ATOM   4884 N  N     . ALA A 1 621 ? 154.643 128.482 178.625 1.00 39.80  ? 622  ALA A N     1 
ATOM   4885 C  CA    . ALA A 1 621 ? 155.841 127.657 178.550 1.00 39.80  ? 622  ALA A CA    1 
ATOM   4886 C  C     . ALA A 1 621 ? 157.044 128.502 178.150 1.00 39.80  ? 622  ALA A C     1 
ATOM   4887 O  O     . ALA A 1 621 ? 156.963 129.307 177.217 1.00 39.80  ? 622  ALA A O     1 
ATOM   4888 C  CB    . ALA A 1 621 ? 155.638 126.519 177.552 1.00 39.80  ? 622  ALA A CB    1 
ATOM   4889 N  N     . ASN A 1 622 ? 158.161 128.291 178.861 1.00 44.95  ? 623  ASN A N     1 
ATOM   4890 C  CA    . ASN A 1 622 ? 159.443 128.984 178.650 1.00 44.95  ? 623  ASN A CA    1 
ATOM   4891 C  C     . ASN A 1 622 ? 159.299 130.507 178.681 1.00 44.95  ? 623  ASN A C     1 
ATOM   4892 O  O     . ASN A 1 622 ? 159.961 131.230 177.934 1.00 44.95  ? 623  ASN A O     1 
ATOM   4893 C  CB    . ASN A 1 622 ? 160.109 128.529 177.350 1.00 44.95  ? 623  ASN A CB    1 
ATOM   4894 C  CG    . ASN A 1 622 ? 161.619 128.511 177.449 1.00 44.95  ? 623  ASN A CG    1 
ATOM   4895 O  OD1   . ASN A 1 622 ? 162.189 127.838 178.308 1.00 44.95  ? 623  ASN A OD1   1 
ATOM   4896 N  ND2   . ASN A 1 622 ? 162.278 129.255 176.570 1.00 44.95  ? 623  ASN A ND2   1 
ATOM   4897 N  N     . TYR A 1 623 ? 158.407 130.993 179.539 1.00 42.38  ? 624  TYR A N     1 
ATOM   4898 C  CA    . TYR A 1 623 ? 158.419 132.383 179.982 1.00 42.38  ? 624  TYR A CA    1 
ATOM   4899 C  C     . TYR A 1 623 ? 159.747 132.730 180.649 1.00 42.38  ? 624  TYR A C     1 
ATOM   4900 O  O     . TYR A 1 623 ? 160.117 132.141 181.662 1.00 42.38  ? 624  TYR A O     1 
ATOM   4901 C  CB    . TYR A 1 623 ? 157.232 132.636 180.925 1.00 42.38  ? 624  TYR A CB    1 
ATOM   4902 C  CG    . TYR A 1 623 ? 157.290 133.905 181.747 1.00 42.38  ? 624  TYR A CG    1 
ATOM   4903 C  CD1   . TYR A 1 623 ? 156.810 135.101 181.234 1.00 42.38  ? 624  TYR A CD1   1 
ATOM   4904 C  CD2   . TYR A 1 623 ? 157.748 133.893 183.061 1.00 42.38  ? 624  TYR A CD2   1 
ATOM   4905 C  CE1   . TYR A 1 623 ? 156.832 136.260 181.984 1.00 42.38  ? 624  TYR A CE1   1 
ATOM   4906 C  CE2   . TYR A 1 623 ? 157.780 135.048 183.815 1.00 42.38  ? 624  TYR A CE2   1 
ATOM   4907 C  CZ    . TYR A 1 623 ? 157.315 136.226 183.273 1.00 42.38  ? 624  TYR A CZ    1 
ATOM   4908 O  OH    . TYR A 1 623 ? 157.348 137.378 184.021 1.00 42.38  ? 624  TYR A OH    1 
ATOM   4909 N  N     . PHE A 1 643 ? 164.260 141.247 180.772 1.00 53.01  ? 644  PHE A N     1 
ATOM   4910 C  CA    . PHE A 1 643 ? 165.521 141.404 180.056 1.00 53.01  ? 644  PHE A CA    1 
ATOM   4911 C  C     . PHE A 1 643 ? 165.316 142.194 178.771 1.00 53.01  ? 644  PHE A C     1 
ATOM   4912 O  O     . PHE A 1 643 ? 166.274 142.667 178.160 1.00 53.01  ? 644  PHE A O     1 
ATOM   4913 C  CB    . PHE A 1 643 ? 166.141 140.031 179.756 1.00 53.01  ? 644  PHE A CB    1 
ATOM   4914 C  CG    . PHE A 1 643 ? 165.446 139.266 178.657 1.00 53.01  ? 644  PHE A CG    1 
ATOM   4915 C  CD1   . PHE A 1 643 ? 164.289 138.548 178.923 1.00 53.01  ? 644  PHE A CD1   1 
ATOM   4916 C  CD2   . PHE A 1 643 ? 165.977 139.221 177.372 1.00 53.01  ? 644  PHE A CD2   1 
ATOM   4917 C  CE1   . PHE A 1 643 ? 163.652 137.835 177.923 1.00 53.01  ? 644  PHE A CE1   1 
ATOM   4918 C  CE2   . PHE A 1 643 ? 165.344 138.510 176.370 1.00 53.01  ? 644  PHE A CE2   1 
ATOM   4919 C  CZ    . PHE A 1 643 ? 164.181 137.814 176.648 1.00 53.01  ? 644  PHE A CZ    1 
ATOM   4920 N  N     . GLN A 1 644 ? 164.056 142.331 178.366 1.00 45.57  ? 645  GLN A N     1 
ATOM   4921 C  CA    . GLN A 1 644 ? 163.722 142.910 177.068 1.00 45.57  ? 645  GLN A CA    1 
ATOM   4922 C  C     . GLN A 1 644 ? 162.433 143.699 177.238 1.00 45.57  ? 645  GLN A C     1 
ATOM   4923 O  O     . GLN A 1 644 ? 161.372 143.111 177.461 1.00 45.57  ? 645  GLN A O     1 
ATOM   4924 C  CB    . GLN A 1 644 ? 163.574 141.824 176.001 1.00 45.57  ? 645  GLN A CB    1 
ATOM   4925 C  CG    . GLN A 1 644 ? 163.219 142.306 174.586 1.00 45.57  ? 645  GLN A CG    1 
ATOM   4926 C  CD    . GLN A 1 644 ? 164.389 142.885 173.786 1.00 45.57  ? 645  GLN A CD    1 
ATOM   4927 O  OE1   . GLN A 1 644 ? 165.323 143.477 174.329 1.00 45.57  ? 645  GLN A OE1   1 
ATOM   4928 N  NE2   . GLN A 1 644 ? 164.329 142.710 172.472 1.00 45.57  ? 645  GLN A NE2   1 
ATOM   4929 N  N     . THR A 1 645 ? 162.531 145.021 177.142 1.00 36.18  ? 646  THR A N     1 
ATOM   4930 C  CA    . THR A 1 645 ? 161.385 145.881 177.377 1.00 36.18  ? 646  THR A CA    1 
ATOM   4931 C  C     . THR A 1 645 ? 160.390 145.795 176.223 1.00 36.18  ? 646  THR A C     1 
ATOM   4932 O  O     . THR A 1 645 ? 160.683 145.264 175.149 1.00 36.18  ? 646  THR A O     1 
ATOM   4933 C  CB    . THR A 1 645 ? 161.827 147.329 177.578 1.00 36.18  ? 646  THR A CB    1 
ATOM   4934 O  OG1   . THR A 1 645 ? 162.357 147.846 176.356 1.00 36.18  ? 646  THR A OG1   1 
ATOM   4935 C  CG2   . THR A 1 645 ? 162.893 147.412 178.645 1.00 36.18  ? 646  THR A CG2   1 
ATOM   4936 N  N     . VAL A 1 646 ? 159.177 146.282 176.494 1.00 33.60  ? 647  VAL A N     1 
ATOM   4937 C  CA    . VAL A 1 646 ? 158.144 146.434 175.470 1.00 33.60  ? 647  VAL A CA    1 
ATOM   4938 C  C     . VAL A 1 646 ? 158.618 147.322 174.325 1.00 33.60  ? 647  VAL A C     1 
ATOM   4939 O  O     . VAL A 1 646 ? 158.385 147.018 173.150 1.00 33.60  ? 647  VAL A O     1 
ATOM   4940 C  CB    . VAL A 1 646 ? 156.856 146.984 176.112 1.00 33.60  ? 647  VAL A CB    1 
ATOM   4941 C  CG1   . VAL A 1 646 ? 155.766 147.185 175.076 1.00 33.60  ? 647  VAL A CG1   1 
ATOM   4942 C  CG2   . VAL A 1 646 ? 156.382 146.057 177.211 1.00 33.60  ? 647  VAL A CG2   1 
ATOM   4943 N  N     . SER A 1 647 ? 159.312 148.418 174.645 1.00 32.34  ? 648  SER A N     1 
ATOM   4944 C  CA    . SER A 1 647 ? 159.819 149.315 173.608 1.00 32.34  ? 648  SER A CA    1 
ATOM   4945 C  C     . SER A 1 647 ? 160.947 148.693 172.795 1.00 32.34  ? 648  SER A C     1 
ATOM   4946 O  O     . SER A 1 647 ? 161.005 148.889 171.578 1.00 32.34  ? 648  SER A O     1 
ATOM   4947 C  CB    . SER A 1 647 ? 160.295 150.623 174.231 1.00 32.34  ? 648  SER A CB    1 
ATOM   4948 O  OG    . SER A 1 647 ? 161.277 150.376 175.216 1.00 32.34  ? 648  SER A OG    1 
ATOM   4949 N  N     . ALA A 1 648 ? 161.867 147.979 173.449 1.00 33.75  ? 649  ALA A N     1 
ATOM   4950 C  CA    . ALA A 1 648 ? 162.975 147.338 172.738 1.00 33.75  ? 649  ALA A CA    1 
ATOM   4951 C  C     . ALA A 1 648 ? 162.489 146.291 171.744 1.00 33.75  ? 649  ALA A C     1 
ATOM   4952 O  O     . ALA A 1 648 ? 162.959 146.243 170.602 1.00 33.75  ? 649  ALA A O     1 
ATOM   4953 C  CB    . ALA A 1 648 ? 163.951 146.709 173.729 1.00 33.75  ? 649  ALA A CB    1 
ATOM   4954 N  N     . LEU A 1 649 ? 161.578 145.417 172.178 1.00 33.61  ? 650  LEU A N     1 
ATOM   4955 C  CA    . LEU A 1 649 ? 161.005 144.416 171.282 1.00 33.61  ? 650  LEU A CA    1 
ATOM   4956 C  C     . LEU A 1 649 ? 160.202 145.061 170.157 1.00 33.61  ? 650  LEU A C     1 
ATOM   4957 O  O     . LEU A 1 649 ? 160.215 144.575 169.022 1.00 33.61  ? 650  LEU A O     1 
ATOM   4958 C  CB    . LEU A 1 649 ? 160.132 143.448 172.077 1.00 33.61  ? 650  LEU A CB    1 
ATOM   4959 C  CG    . LEU A 1 649 ? 159.486 142.301 171.307 1.00 33.61  ? 650  LEU A CG    1 
ATOM   4960 C  CD1   . LEU A 1 649 ? 160.552 141.367 170.769 1.00 33.61  ? 650  LEU A CD1   1 
ATOM   4961 C  CD2   . LEU A 1 649 ? 158.507 141.550 172.186 1.00 33.61  ? 650  LEU A CD2   1 
ATOM   4962 N  N     . HIS A 1 650 ? 159.495 146.153 170.456 1.00 30.65  ? 651  HIS A N     1 
ATOM   4963 C  CA    . HIS A 1 650 ? 158.782 146.901 169.423 1.00 30.65  ? 651  HIS A CA    1 
ATOM   4964 C  C     . HIS A 1 650 ? 159.726 147.544 168.417 1.00 30.65  ? 651  HIS A C     1 
ATOM   4965 O  O     . HIS A 1 650 ? 159.542 147.391 167.204 1.00 30.65  ? 651  HIS A O     1 
ATOM   4966 C  CB    . HIS A 1 650 ? 157.903 147.971 170.066 1.00 30.65  ? 651  HIS A CB    1 
ATOM   4967 C  CG    . HIS A 1 650 ? 157.230 148.871 169.079 1.00 30.65  ? 651  HIS A CG    1 
ATOM   4968 N  ND1   . HIS A 1 650 ? 156.359 148.406 168.120 1.00 30.65  ? 651  HIS A ND1   1 
ATOM   4969 C  CD2   . HIS A 1 650 ? 157.300 150.211 168.906 1.00 30.65  ? 651  HIS A CD2   1 
ATOM   4970 C  CE1   . HIS A 1 650 ? 155.918 149.421 167.400 1.00 30.65  ? 651  HIS A CE1   1 
ATOM   4971 N  NE2   . HIS A 1 650 ? 156.475 150.527 167.857 1.00 30.65  ? 651  HIS A NE2   1 
ATOM   4972 N  N     . ARG A 1 651 ? 160.710 148.310 168.903 1.00 31.79  ? 652  ARG A N     1 
ATOM   4973 C  CA    . ARG A 1 651 ? 161.606 149.063 168.024 1.00 31.79  ? 652  ARG A CA    1 
ATOM   4974 C  C     . ARG A 1 651 ? 162.442 148.148 167.136 1.00 31.79  ? 652  ARG A C     1 
ATOM   4975 O  O     . ARG A 1 651 ? 162.671 148.456 165.960 1.00 31.79  ? 652  ARG A O     1 
ATOM   4976 C  CB    . ARG A 1 651 ? 162.515 149.969 168.853 1.00 31.79  ? 652  ARG A CB    1 
ATOM   4977 C  CG    . ARG A 1 651 ? 163.366 150.912 168.030 1.00 31.79  ? 652  ARG A CG    1 
ATOM   4978 C  CD    . ARG A 1 651 ? 164.237 151.827 168.883 1.00 31.79  ? 652  ARG A CD    1 
ATOM   4979 N  NE    . ARG A 1 651 ? 165.205 151.091 169.688 1.00 31.79  ? 652  ARG A NE    1 
ATOM   4980 C  CZ    . ARG A 1 651 ? 165.158 150.990 171.009 1.00 31.79  ? 652  ARG A CZ    1 
ATOM   4981 N  NH1   . ARG A 1 651 ? 166.081 150.292 171.655 1.00 31.79  ? 652  ARG A NH1   1 
ATOM   4982 N  NH2   . ARG A 1 651 ? 164.196 151.602 171.684 1.00 31.79  ? 652  ARG A NH2   1 
ATOM   4983 N  N     . GLU A 1 652 ? 162.918 147.028 167.683 1.00 30.21  ? 653  GLU A N     1 
ATOM   4984 C  CA    . GLU A 1 652 ? 163.636 146.046 166.874 1.00 30.21  ? 653  GLU A CA    1 
ATOM   4985 C  C     . GLU A 1 652 ? 162.743 145.405 165.815 1.00 30.21  ? 653  GLU A C     1 
ATOM   4986 O  O     . GLU A 1 652 ? 163.173 145.219 164.671 1.00 30.21  ? 653  GLU A O     1 
ATOM   4987 C  CB    . GLU A 1 652 ? 164.255 144.978 167.772 1.00 30.21  ? 653  GLU A CB    1 
ATOM   4988 C  CG    . GLU A 1 652 ? 165.183 144.023 167.039 1.00 30.21  ? 653  GLU A CG    1 
ATOM   4989 C  CD    . GLU A 1 652 ? 166.039 143.197 167.976 1.00 30.21  ? 653  GLU A CD    1 
ATOM   4990 O  OE1   . GLU A 1 652 ? 166.709 142.253 167.503 1.00 30.21  ? 653  GLU A OE1   1 
ATOM   4991 O  OE2   . GLU A 1 652 ? 166.044 143.491 169.190 1.00 30.21  ? 653  GLU A OE2   1 
ATOM   4992 N  N     . ASN A 1 653 ? 161.511 145.035 166.180 1.00 29.31  ? 654  ASN A N     1 
ATOM   4993 C  CA    . ASN A 1 653 ? 160.574 144.485 165.200 1.00 29.31  ? 654  ASN A CA    1 
ATOM   4994 C  C     . ASN A 1 653 ? 160.187 145.494 164.126 1.00 29.31  ? 654  ASN A C     1 
ATOM   4995 O  O     . ASN A 1 653 ? 160.027 145.126 162.958 1.00 29.31  ? 654  ASN A O     1 
ATOM   4996 C  CB    . ASN A 1 653 ? 159.314 143.968 165.892 1.00 29.31  ? 654  ASN A CB    1 
ATOM   4997 C  CG    . ASN A 1 653 ? 159.443 142.535 166.343 1.00 29.31  ? 654  ASN A CG    1 
ATOM   4998 O  OD1   . ASN A 1 653 ? 159.413 141.615 165.531 1.00 29.31  ? 654  ASN A OD1   1 
ATOM   4999 N  ND2   . ASN A 1 653 ? 159.566 142.333 167.645 1.00 29.31  ? 654  ASN A ND2   1 
ATOM   5000 N  N     . LEU A 1 654 ? 159.984 146.758 164.502 1.00 24.77  ? 655  LEU A N     1 
ATOM   5001 C  CA    . LEU A 1 654 ? 159.618 147.769 163.515 1.00 24.77  ? 655  LEU A CA    1 
ATOM   5002 C  C     . LEU A 1 654 ? 160.750 148.049 162.536 1.00 24.77  ? 655  LEU A C     1 
ATOM   5003 O  O     . LEU A 1 654 ? 160.506 148.249 161.343 1.00 24.77  ? 655  LEU A O     1 
ATOM   5004 C  CB    . LEU A 1 654 ? 159.188 149.052 164.218 1.00 24.77  ? 655  LEU A CB    1 
ATOM   5005 C  CG    . LEU A 1 654 ? 158.683 150.181 163.326 1.00 24.77  ? 655  LEU A CG    1 
ATOM   5006 C  CD1   . LEU A 1 654 ? 157.544 149.687 162.473 1.00 24.77  ? 655  LEU A CD1   1 
ATOM   5007 C  CD2   . LEU A 1 654 ? 158.225 151.336 164.174 1.00 24.77  ? 655  LEU A CD2   1 
ATOM   5008 N  N     . ASN A 1 655 ? 161.996 148.050 163.010 1.00 26.94  ? 656  ASN A N     1 
ATOM   5009 C  CA    . ASN A 1 655 ? 163.126 148.180 162.096 1.00 26.94  ? 656  ASN A CA    1 
ATOM   5010 C  C     . ASN A 1 655 ? 163.364 146.915 161.281 1.00 26.94  ? 656  ASN A C     1 
ATOM   5011 O  O     . ASN A 1 655 ? 163.906 146.996 160.176 1.00 26.94  ? 656  ASN A O     1 
ATOM   5012 C  CB    . ASN A 1 655 ? 164.388 148.563 162.866 1.00 26.94  ? 656  ASN A CB    1 
ATOM   5013 C  CG    . ASN A 1 655 ? 164.362 149.999 163.344 1.00 26.94  ? 656  ASN A CG    1 
ATOM   5014 O  OD1   . ASN A 1 655 ? 163.533 150.794 162.906 1.00 26.94  ? 656  ASN A OD1   1 
ATOM   5015 N  ND2   . ASN A 1 655 ? 165.271 150.339 164.248 1.00 26.94  ? 656  ASN A ND2   1 
ATOM   5016 N  N     . LYS A 1 656 ? 162.993 145.747 161.809 1.00 27.27  ? 657  LYS A N     1 
ATOM   5017 C  CA    . LYS A 1 656 ? 162.962 144.533 160.995 1.00 27.27  ? 657  LYS A CA    1 
ATOM   5018 C  C     . LYS A 1 656 ? 161.944 144.632 159.866 1.00 27.27  ? 657  LYS A C     1 
ATOM   5019 O  O     . LYS A 1 656 ? 162.199 144.155 158.754 1.00 27.27  ? 657  LYS A O     1 
ATOM   5020 C  CB    . LYS A 1 656 ? 162.661 143.317 161.864 1.00 27.27  ? 657  LYS A CB    1 
ATOM   5021 C  CG    . LYS A 1 656 ? 162.839 141.999 161.140 1.00 27.27  ? 657  LYS A CG    1 
ATOM   5022 C  CD    . LYS A 1 656 ? 162.084 140.884 161.831 1.00 27.27  ? 657  LYS A CD    1 
ATOM   5023 C  CE    . LYS A 1 656 ? 160.598 140.970 161.525 1.00 27.27  ? 657  LYS A CE    1 
ATOM   5024 N  NZ    . LYS A 1 656 ? 159.838 139.843 162.130 1.00 27.27  ? 657  LYS A NZ    1 
ATOM   5025 N  N     . LEU A 1 657 ? 160.759 145.179 160.156 1.00 24.27  ? 658  LEU A N     1 
ATOM   5026 C  CA    . LEU A 1 657 ? 159.730 145.376 159.136 1.00 24.27  ? 658  LEU A CA    1 
ATOM   5027 C  C     . LEU A 1 657 ? 160.206 146.288 158.011 1.00 24.27  ? 658  LEU A C     1 
ATOM   5028 O  O     . LEU A 1 657 ? 160.142 145.921 156.834 1.00 24.27  ? 658  LEU A O     1 
ATOM   5029 C  CB    . LEU A 1 657 ? 158.465 145.945 159.776 1.00 24.27  ? 658  LEU A CB    1 
ATOM   5030 C  CG    . LEU A 1 657 ? 157.348 146.357 158.821 1.00 24.27  ? 658  LEU A CG    1 
ATOM   5031 C  CD1   . LEU A 1 657 ? 156.830 145.161 158.084 1.00 24.27  ? 658  LEU A CD1   1 
ATOM   5032 C  CD2   . LEU A 1 657 ? 156.223 147.039 159.562 1.00 24.27  ? 658  LEU A CD2   1 
ATOM   5033 N  N     . MET A 1 658 ? 160.696 147.476 158.349 1.00 25.07  ? 659  MET A N     1 
ATOM   5034 C  CA    . MET A 1 658 ? 161.103 148.422 157.319 1.00 25.07  ? 659  MET A CA    1 
ATOM   5035 C  C     . MET A 1 658 ? 162.502 148.176 156.773 1.00 25.07  ? 659  MET A C     1 
ATOM   5036 O  O     . MET A 1 658 ? 162.933 148.916 155.886 1.00 25.07  ? 659  MET A O     1 
ATOM   5037 C  CB    . MET A 1 658 ? 160.982 149.850 157.835 1.00 25.07  ? 659  MET A CB    1 
ATOM   5038 C  CG    . MET A 1 658 ? 159.560 150.349 157.777 1.00 25.07  ? 659  MET A CG    1 
ATOM   5039 S  SD    . MET A 1 658 ? 159.350 151.938 158.570 1.00 25.07  ? 659  MET A SD    1 
ATOM   5040 C  CE    . MET A 1 658 ? 160.757 152.816 157.899 1.00 25.07  ? 659  MET A CE    1 
ATOM   5041 N  N     . THR A 1 659 ? 163.232 147.185 157.280 1.00 26.66  ? 660  THR A N     1 
ATOM   5042 C  CA    . THR A 1 659 ? 164.321 146.616 156.493 1.00 26.66  ? 660  THR A CA    1 
ATOM   5043 C  C     . THR A 1 659 ? 163.775 145.727 155.383 1.00 26.66  ? 660  THR A C     1 
ATOM   5044 O  O     . THR A 1 659 ? 164.271 145.761 154.250 1.00 26.66  ? 660  THR A O     1 
ATOM   5045 C  CB    . THR A 1 659 ? 165.278 145.844 157.405 1.00 26.66  ? 660  THR A CB    1 
ATOM   5046 O  OG1   . THR A 1 659 ? 165.854 146.747 158.355 1.00 26.66  ? 660  THR A OG1   1 
ATOM   5047 C  CG2   . THR A 1 659 ? 166.401 145.190 156.620 1.00 26.66  ? 660  THR A CG2   1 
ATOM   5048 N  N     . ASN A 1 660 ? 162.738 144.946 155.686 1.00 24.34  ? 661  ASN A N     1 
ATOM   5049 C  CA    . ASN A 1 660 ? 162.155 144.035 154.705 1.00 24.34  ? 661  ASN A CA    1 
ATOM   5050 C  C     . ASN A 1 660 ? 161.478 144.789 153.568 1.00 24.34  ? 661  ASN A C     1 
ATOM   5051 O  O     . ASN A 1 660 ? 161.631 144.421 152.398 1.00 24.34  ? 661  ASN A O     1 
ATOM   5052 C  CB    . ASN A 1 660 ? 161.167 143.096 155.389 1.00 24.34  ? 661  ASN A CB    1 
ATOM   5053 C  CG    . ASN A 1 660 ? 160.584 142.083 154.440 1.00 24.34  ? 661  ASN A CG    1 
ATOM   5054 O  OD1   . ASN A 1 660 ? 161.309 141.413 153.708 1.00 24.34  ? 661  ASN A OD1   1 
ATOM   5055 N  ND2   . ASN A 1 660 ? 159.264 141.960 154.446 1.00 24.34  ? 661  ASN A ND2   1 
ATOM   5056 N  N     . LEU A 1 661 ? 160.692 145.819 153.901 1.00 21.83  ? 662  LEU A N     1 
ATOM   5057 C  CA    . LEU A 1 661 ? 159.987 146.622 152.901 1.00 21.83  ? 662  LEU A CA    1 
ATOM   5058 C  C     . LEU A 1 661 ? 160.928 147.307 151.918 1.00 21.83  ? 662  LEU A C     1 
ATOM   5059 O  O     . LEU A 1 661 ? 160.560 147.507 150.757 1.00 21.83  ? 662  LEU A O     1 
ATOM   5060 C  CB    . LEU A 1 661 ? 159.108 147.666 153.583 1.00 21.83  ? 662  LEU A CB    1 
ATOM   5061 C  CG    . LEU A 1 661 ? 157.629 147.370 153.802 1.00 21.83  ? 662  LEU A CG    1 
ATOM   5062 C  CD1   . LEU A 1 661 ? 157.418 146.073 154.520 1.00 21.83  ? 662  LEU A CD1   1 
ATOM   5063 C  CD2   . LEU A 1 661 ? 157.049 148.492 154.614 1.00 21.83  ? 662  LEU A CD2   1 
ATOM   5064 N  N     . ARG A 1 662 ? 162.127 147.698 152.361 1.00 24.03  ? 663  ARG A N     1 
ATOM   5065 C  CA    . ARG A 1 662 ? 163.097 148.300 151.451 1.00 24.03  ? 663  ARG A CA    1 
ATOM   5066 C  C     . ARG A 1 662 ? 163.610 147.328 150.396 1.00 24.03  ? 663  ARG A C     1 
ATOM   5067 O  O     . ARG A 1 662 ? 164.084 147.774 149.347 1.00 24.03  ? 663  ARG A O     1 
ATOM   5068 C  CB    . ARG A 1 662 ? 164.284 148.864 152.231 1.00 24.03  ? 663  ARG A CB    1 
ATOM   5069 C  CG    . ARG A 1 662 ? 163.990 150.152 152.967 1.00 24.03  ? 663  ARG A CG    1 
ATOM   5070 C  CD    . ARG A 1 662 ? 165.217 150.673 153.686 1.00 24.03  ? 663  ARG A CD    1 
ATOM   5071 N  NE    . ARG A 1 662 ? 165.019 152.037 154.159 1.00 24.03  ? 663  ARG A NE    1 
ATOM   5072 C  CZ    . ARG A 1 662 ? 164.688 152.349 155.406 1.00 24.03  ? 663  ARG A CZ    1 
ATOM   5073 N  NH1   . ARG A 1 662 ? 164.599 153.616 155.778 1.00 24.03  ? 663  ARG A NH1   1 
ATOM   5074 N  NH2   . ARG A 1 662 ? 164.501 151.388 156.296 1.00 24.03  ? 663  ARG A NH2   1 
ATOM   5075 N  N     . SER A 1 663 ? 163.527 146.021 150.638 1.00 24.72  ? 664  SER A N     1 
ATOM   5076 C  CA    . SER A 1 663 ? 163.841 145.021 149.628 1.00 24.72  ? 664  SER A CA    1 
ATOM   5077 C  C     . SER A 1 663 ? 162.638 144.639 148.769 1.00 24.72  ? 664  SER A C     1 
ATOM   5078 O  O     . SER A 1 663 ? 162.627 143.551 148.185 1.00 24.72  ? 664  SER A O     1 
ATOM   5079 C  CB    . SER A 1 663 ? 164.422 143.774 150.295 1.00 24.72  ? 664  SER A CB    1 
ATOM   5080 O  OG    . SER A 1 663 ? 164.328 142.648 149.443 1.00 24.72  ? 664  SER A OG    1 
ATOM   5081 N  N     . THR A 1 664 ? 161.625 145.503 148.680 1.00 23.38  ? 665  THR A N     1 
ATOM   5082 C  CA    . THR A 1 664 ? 160.438 145.263 147.868 1.00 23.38  ? 665  THR A CA    1 
ATOM   5083 C  C     . THR A 1 664 ? 160.082 146.537 147.120 1.00 23.38  ? 665  THR A C     1 
ATOM   5084 O  O     . THR A 1 664 ? 160.510 147.633 147.483 1.00 23.38  ? 665  THR A O     1 
ATOM   5085 C  CB    . THR A 1 664 ? 159.210 144.825 148.685 1.00 23.38  ? 665  THR A CB    1 
ATOM   5086 O  OG1   . THR A 1 664 ? 158.720 145.930 149.454 1.00 23.38  ? 665  THR A OG1   1 
ATOM   5087 C  CG2   . THR A 1 664 ? 159.479 143.628 149.593 1.00 23.38  ? 665  THR A CG2   1 
ATOM   5088 N  N     . HIS A 1 665 ? 159.296 146.377 146.056 1.00 22.56  ? 666  HIS A N     1 
ATOM   5089 C  CA    . HIS A 1 665 ? 158.776 147.512 145.305 1.00 22.56  ? 666  HIS A CA    1 
ATOM   5090 C  C     . HIS A 1 665 ? 157.410 147.907 145.858 1.00 22.56  ? 666  HIS A C     1 
ATOM   5091 O  O     . HIS A 1 665 ? 156.434 147.178 145.638 1.00 22.56  ? 666  HIS A O     1 
ATOM   5092 C  CB    . HIS A 1 665 ? 158.684 147.149 143.829 1.00 22.56  ? 666  HIS A CB    1 
ATOM   5093 C  CG    . HIS A 1 665 ? 158.045 148.194 142.974 1.00 22.56  ? 666  HIS A CG    1 
ATOM   5094 N  ND1   . HIS A 1 665 ? 156.736 148.117 142.554 1.00 22.56  ? 666  HIS A ND1   1 
ATOM   5095 C  CD2   . HIS A 1 665 ? 158.548 149.331 142.439 1.00 22.56  ? 666  HIS A CD2   1 
ATOM   5096 C  CE1   . HIS A 1 665 ? 156.456 149.169 141.805 1.00 22.56  ? 666  HIS A CE1   1 
ATOM   5097 N  NE2   . HIS A 1 665 ? 157.537 149.922 141.722 1.00 22.56  ? 666  HIS A NE2   1 
ATOM   5098 N  N     . PRO A 1 666 ? 157.284 149.042 146.547 1.00 20.27  ? 667  PRO A N     1 
ATOM   5099 C  CA    . PRO A 1 666 ? 156.025 149.374 147.225 1.00 20.27  ? 667  PRO A CA    1 
ATOM   5100 C  C     . PRO A 1 666 ? 154.974 149.990 146.316 1.00 20.27  ? 667  PRO A C     1 
ATOM   5101 O  O     . PRO A 1 666 ? 155.270 150.827 145.462 1.00 20.27  ? 667  PRO A O     1 
ATOM   5102 C  CB    . PRO A 1 666 ? 156.470 150.372 148.297 1.00 20.27  ? 667  PRO A CB    1 
ATOM   5103 C  CG    . PRO A 1 666 ? 157.634 151.047 147.689 1.00 20.27  ? 667  PRO A CG    1 
ATOM   5104 C  CD    . PRO A 1 666 ? 158.348 150.000 146.879 1.00 20.27  ? 667  PRO A CD    1 
ATOM   5105 N  N     . HIS A 1 667 ? 153.730 149.564 146.506 1.00 20.54  ? 668  HIS A N     1 
ATOM   5106 C  CA    . HIS A 1 667 ? 152.562 150.253 145.968 1.00 20.54  ? 668  HIS A CA    1 
ATOM   5107 C  C     . HIS A 1 667 ? 151.814 150.917 147.116 1.00 20.54  ? 668  HIS A C     1 
ATOM   5108 O  O     . HIS A 1 667 ? 151.216 150.232 147.946 1.00 20.54  ? 668  HIS A O     1 
ATOM   5109 C  CB    . HIS A 1 667 ? 151.650 149.274 145.241 1.00 20.54  ? 668  HIS A CB    1 
ATOM   5110 C  CG    . HIS A 1 667 ? 152.164 148.846 143.907 1.00 20.54  ? 668  HIS A CG    1 
ATOM   5111 N  ND1   . HIS A 1 667 ? 153.257 148.020 143.766 1.00 20.54  ? 668  HIS A ND1   1 
ATOM   5112 C  CD2   . HIS A 1 667 ? 151.740 149.129 142.655 1.00 20.54  ? 668  HIS A CD2   1 
ATOM   5113 C  CE1   . HIS A 1 667 ? 153.483 147.811 142.483 1.00 20.54  ? 668  HIS A CE1   1 
ATOM   5114 N  NE2   . HIS A 1 667 ? 152.579 148.475 141.787 1.00 20.54  ? 668  HIS A NE2   1 
ATOM   5115 N  N     . PHE A 1 668 ? 151.819 152.241 147.163 1.00 20.76  ? 669  PHE A N     1 
ATOM   5116 C  CA    . PHE A 1 668 ? 151.054 152.918 148.197 1.00 20.76  ? 669  PHE A CA    1 
ATOM   5117 C  C     . PHE A 1 668 ? 149.594 153.062 147.786 1.00 20.76  ? 669  PHE A C     1 
ATOM   5118 O  O     . PHE A 1 668 ? 149.268 153.149 146.602 1.00 20.76  ? 669  PHE A O     1 
ATOM   5119 C  CB    . PHE A 1 668 ? 151.667 154.282 148.508 1.00 20.76  ? 669  PHE A CB    1 
ATOM   5120 C  CG    . PHE A 1 668 ? 153.053 154.192 149.069 1.00 20.76  ? 669  PHE A CG    1 
ATOM   5121 C  CD1   . PHE A 1 668 ? 153.251 154.028 150.426 1.00 20.76  ? 669  PHE A CD1   1 
ATOM   5122 C  CD2   . PHE A 1 668 ? 154.155 154.263 148.242 1.00 20.76  ? 669  PHE A CD2   1 
ATOM   5123 C  CE1   . PHE A 1 668 ? 154.520 153.932 150.943 1.00 20.76  ? 669  PHE A CE1   1 
ATOM   5124 C  CE2   . PHE A 1 668 ? 155.424 154.170 148.757 1.00 20.76  ? 669  PHE A CE2   1 
ATOM   5125 C  CZ    . PHE A 1 668 ? 155.605 154.006 150.106 1.00 20.76  ? 669  PHE A CZ    1 
ATOM   5126 N  N     . VAL A 1 669 ? 148.707 153.051 148.782 1.00 19.50  ? 670  VAL A N     1 
ATOM   5127 C  CA    . VAL A 1 669 ? 147.307 153.460 148.648 1.00 19.50  ? 670  VAL A CA    1 
ATOM   5128 C  C     . VAL A 1 669 ? 146.990 154.355 149.834 1.00 19.50  ? 670  VAL A C     1 
ATOM   5129 O  O     . VAL A 1 669 ? 146.836 153.860 150.954 1.00 19.50  ? 670  VAL A O     1 
ATOM   5130 C  CB    . VAL A 1 669 ? 146.330 152.274 148.615 1.00 19.50  ? 670  VAL A CB    1 
ATOM   5131 C  CG1   . VAL A 1 669 ? 144.933 152.772 148.348 1.00 19.50  ? 670  VAL A CG1   1 
ATOM   5132 C  CG2   . VAL A 1 669 ? 146.703 151.244 147.570 1.00 19.50  ? 670  VAL A CG2   1 
ATOM   5133 N  N     . ARG A 1 670 ? 146.887 155.659 149.604 1.00 21.71  ? 671  ARG A N     1 
ATOM   5134 C  CA    . ARG A 1 670 ? 146.538 156.581 150.677 1.00 21.71  ? 671  ARG A CA    1 
ATOM   5135 C  C     . ARG A 1 670 ? 145.043 156.508 150.977 1.00 21.71  ? 671  ARG A C     1 
ATOM   5136 O  O     . ARG A 1 670 ? 144.222 156.411 150.064 1.00 21.71  ? 671  ARG A O     1 
ATOM   5137 C  CB    . ARG A 1 670 ? 146.898 158.012 150.289 1.00 21.71  ? 671  ARG A CB    1 
ATOM   5138 C  CG    . ARG A 1 670 ? 148.353 158.235 149.947 1.00 21.71  ? 671  ARG A CG    1 
ATOM   5139 C  CD    . ARG A 1 670 ? 149.258 157.770 151.040 1.00 21.71  ? 671  ARG A CD    1 
ATOM   5140 N  NE    . ARG A 1 670 ? 150.359 158.686 151.266 1.00 21.71  ? 671  ARG A NE    1 
ATOM   5141 C  CZ    . ARG A 1 670 ? 150.977 158.840 152.429 1.00 21.71  ? 671  ARG A CZ    1 
ATOM   5142 N  NH1   . ARG A 1 670 ? 151.804 159.850 152.612 1.00 21.71  ? 671  ARG A NH1   1 
ATOM   5143 N  NH2   . ARG A 1 670 ? 150.651 158.068 153.455 1.00 21.71  ? 671  ARG A NH2   1 
ATOM   5144 N  N     . CYS A 1 671 ? 144.688 156.550 152.260 1.00 20.87  ? 672  CYS A N     1 
ATOM   5145 C  CA    . CYS A 1 671 ? 143.294 156.556 152.694 1.00 20.87  ? 672  CYS A CA    1 
ATOM   5146 C  C     . CYS A 1 671 ? 142.963 157.856 153.411 1.00 20.87  ? 672  CYS A C     1 
ATOM   5147 O  O     . CYS A 1 671 ? 143.694 158.276 154.312 1.00 20.87  ? 672  CYS A O     1 
ATOM   5148 C  CB    . CYS A 1 671 ? 142.986 155.365 153.588 1.00 20.87  ? 672  CYS A CB    1 
ATOM   5149 S  SG    . CYS A 1 671 ? 143.255 153.805 152.787 1.00 20.87  ? 672  CYS A SG    1 
ATOM   5150 N  N     . ILE A 1 672 ? 141.857 158.481 153.017 1.00 21.82  ? 673  ILE A N     1 
ATOM   5151 C  CA    . ILE A 1 672 ? 141.444 159.786 153.522 1.00 21.82  ? 673  ILE A CA    1 
ATOM   5152 C  C     . ILE A 1 672 ? 140.118 159.638 154.262 1.00 21.82  ? 673  ILE A C     1 
ATOM   5153 O  O     . ILE A 1 672 ? 139.132 159.180 153.677 1.00 21.82  ? 673  ILE A O     1 
ATOM   5154 C  CB    . ILE A 1 672 ? 141.306 160.796 152.376 1.00 21.82  ? 673  ILE A CB    1 
ATOM   5155 C  CG1   . ILE A 1 672 ? 142.651 161.031 151.690 1.00 21.82  ? 673  ILE A CG1   1 
ATOM   5156 C  CG2   . ILE A 1 672 ? 140.735 162.082 152.887 1.00 21.82  ? 673  ILE A CG2   1 
ATOM   5157 C  CD1   . ILE A 1 672 ? 143.647 161.767 152.515 1.00 21.82  ? 673  ILE A CD1   1 
ATOM   5158 N  N     . ILE A 1 673 ? 140.086 160.018 155.538 1.00 23.62  ? 674  ILE A N     1 
ATOM   5159 C  CA    . ILE A 1 673 ? 138.816 160.150 156.258 1.00 23.62  ? 674  ILE A CA    1 
ATOM   5160 C  C     . ILE A 1 673 ? 138.161 161.497 155.954 1.00 23.62  ? 674  ILE A C     1 
ATOM   5161 O  O     . ILE A 1 673 ? 138.702 162.553 156.311 1.00 23.62  ? 674  ILE A O     1 
ATOM   5162 C  CB    . ILE A 1 673 ? 138.991 159.916 157.774 1.00 23.62  ? 674  ILE A CB    1 
ATOM   5163 C  CG1   . ILE A 1 673 ? 137.727 160.302 158.536 1.00 23.62  ? 674  ILE A CG1   1 
ATOM   5164 C  CG2   . ILE A 1 673 ? 140.213 160.591 158.355 1.00 23.62  ? 674  ILE A CG2   1 
ATOM   5165 C  CD1   . ILE A 1 673 ? 137.682 159.746 159.929 1.00 23.62  ? 674  ILE A CD1   1 
ATOM   5166 N  N     . PRO A 1 674 ? 137.013 161.517 155.267 1.00 24.55  ? 675  PRO A N     1 
ATOM   5167 C  CA    . PRO A 1 674 ? 136.419 162.795 154.870 1.00 24.55  ? 675  PRO A CA    1 
ATOM   5168 C  C     . PRO A 1 674 ? 135.585 163.471 155.934 1.00 24.55  ? 675  PRO A C     1 
ATOM   5169 O  O     . PRO A 1 674 ? 135.351 164.680 155.817 1.00 24.55  ? 675  PRO A O     1 
ATOM   5170 C  CB    . PRO A 1 674 ? 135.532 162.406 153.693 1.00 24.55  ? 675  PRO A CB    1 
ATOM   5171 C  CG    . PRO A 1 674 ? 135.088 161.085 154.051 1.00 24.55  ? 675  PRO A CG    1 
ATOM   5172 C  CD    . PRO A 1 674 ? 136.244 160.400 154.718 1.00 24.55  ? 675  PRO A CD    1 
ATOM   5173 N  N     . ASN A 1 675 ? 135.123 162.759 156.959 1.00 28.45  ? 676  ASN A N     1 
ATOM   5174 C  CA    . ASN A 1 675 ? 134.156 163.353 157.871 1.00 28.45  ? 676  ASN A CA    1 
ATOM   5175 C  C     . ASN A 1 675 ? 134.255 162.625 159.202 1.00 28.45  ? 676  ASN A C     1 
ATOM   5176 O  O     . ASN A 1 675 ? 134.162 161.395 159.245 1.00 28.45  ? 676  ASN A O     1 
ATOM   5177 C  CB    . ASN A 1 675 ? 132.744 163.248 157.285 1.00 28.45  ? 676  ASN A CB    1 
ATOM   5178 C  CG    . ASN A 1 675 ? 131.778 164.238 157.893 1.00 28.45  ? 676  ASN A CG    1 
ATOM   5179 O  OD1   . ASN A 1 675 ? 131.920 164.643 159.042 1.00 28.45  ? 676  ASN A OD1   1 
ATOM   5180 N  ND2   . ASN A 1 675 ? 130.781 164.636 157.113 1.00 28.45  ? 676  ASN A ND2   1 
ATOM   5181 N  N     . GLU A 1 676 ? 134.454 163.387 160.279 1.00 32.65  ? 677  GLU A N     1 
ATOM   5182 C  CA    . GLU A 1 676 ? 134.484 162.837 161.630 1.00 32.65  ? 677  GLU A CA    1 
ATOM   5183 C  C     . GLU A 1 676 ? 133.113 162.442 162.164 1.00 32.65  ? 677  GLU A C     1 
ATOM   5184 O  O     . GLU A 1 676 ? 133.044 161.728 163.168 1.00 32.65  ? 677  GLU A O     1 
ATOM   5185 C  CB    . GLU A 1 676 ? 135.138 163.846 162.581 1.00 32.65  ? 677  GLU A CB    1 
ATOM   5186 C  CG    . GLU A 1 676 ? 136.667 163.960 162.462 1.00 32.65  ? 677  GLU A CG    1 
ATOM   5187 C  CD    . GLU A 1 676 ? 137.461 162.877 163.197 1.00 32.65  ? 677  GLU A CD    1 
ATOM   5188 O  OE1   . GLU A 1 676 ? 137.048 161.699 163.234 1.00 32.65  ? 677  GLU A OE1   1 
ATOM   5189 O  OE2   . GLU A 1 676 ? 138.531 163.217 163.740 1.00 32.65  ? 677  GLU A OE2   1 
ATOM   5190 N  N     . THR A 1 677 ? 132.031 162.882 161.528 1.00 31.73  ? 678  THR A N     1 
ATOM   5191 C  CA    . THR A 1 677 ? 130.678 162.624 162.004 1.00 31.73  ? 678  THR A CA    1 
ATOM   5192 C  C     . THR A 1 677 ? 130.208 161.209 161.650 1.00 31.73  ? 678  THR A C     1 
ATOM   5193 O  O     . THR A 1 677 ? 129.184 160.753 162.175 1.00 31.73  ? 678  THR A O     1 
ATOM   5194 C  CB    . THR A 1 677 ? 129.763 163.717 161.414 1.00 31.73  ? 678  THR A CB    1 
ATOM   5195 O  OG1   . THR A 1 677 ? 130.374 164.991 161.642 1.00 31.73  ? 678  THR A OG1   1 
ATOM   5196 C  CG2   . THR A 1 677 ? 128.395 163.793 162.094 1.00 31.73  ? 678  THR A CG2   1 
ATOM   5197 N  N     . LYS A 1 678 ? 130.971 160.490 160.818 1.00 30.26  ? 679  LYS A N     1 
ATOM   5198 C  CA    . LYS A 1 678 ? 130.664 159.189 160.216 1.00 30.26  ? 679  LYS A CA    1 
ATOM   5199 C  C     . LYS A 1 678 ? 129.412 159.197 159.346 1.00 30.26  ? 679  LYS A C     1 
ATOM   5200 O  O     . LYS A 1 678 ? 128.907 158.127 158.998 1.00 30.26  ? 679  LYS A O     1 
ATOM   5201 C  CB    . LYS A 1 678 ? 130.551 158.057 161.253 1.00 30.26  ? 679  LYS A CB    1 
ATOM   5202 C  CG    . LYS A 1 678 ? 131.711 157.951 162.217 1.00 30.26  ? 679  LYS A CG    1 
ATOM   5203 C  CD    . LYS A 1 678 ? 131.519 156.779 163.160 1.00 30.26  ? 679  LYS A CD    1 
ATOM   5204 C  CE    . LYS A 1 678 ? 132.577 156.771 164.244 1.00 30.26  ? 679  LYS A CE    1 
ATOM   5205 N  NZ    . LYS A 1 678 ? 132.393 157.894 165.202 1.00 30.26  ? 679  LYS A NZ    1 
ATOM   5206 N  N     . SER A 1 679 ? 128.896 160.365 158.980 1.00 30.47  ? 680  SER A N     1 
ATOM   5207 C  CA    . SER A 1 679 ? 127.801 160.359 158.024 1.00 30.47  ? 680  SER A CA    1 
ATOM   5208 C  C     . SER A 1 679 ? 128.358 160.309 156.606 1.00 30.47  ? 680  SER A C     1 
ATOM   5209 O  O     . SER A 1 679 ? 129.402 160.905 156.333 1.00 30.47  ? 680  SER A O     1 
ATOM   5210 C  CB    . SER A 1 679 ? 126.944 161.610 158.200 1.00 30.47  ? 680  SER A CB    1 
ATOM   5211 O  OG    . SER A 1 679 ? 125.931 161.702 157.217 1.00 30.47  ? 680  SER A OG    1 
ATOM   5212 N  N     . PRO A 1 680 ? 127.707 159.614 155.677 1.00 28.61  ? 681  PRO A N     1 
ATOM   5213 C  CA    . PRO A 1 680 ? 128.296 159.439 154.348 1.00 28.61  ? 681  PRO A CA    1 
ATOM   5214 C  C     . PRO A 1 680 ? 128.105 160.657 153.463 1.00 28.61  ? 681  PRO A C     1 
ATOM   5215 O  O     . PRO A 1 680 ? 127.135 161.407 153.588 1.00 28.61  ? 681  PRO A O     1 
ATOM   5216 C  CB    . PRO A 1 680 ? 127.543 158.227 153.791 1.00 28.61  ? 681  PRO A CB    1 
ATOM   5217 C  CG    . PRO A 1 680 ? 126.231 158.292 154.447 1.00 28.61  ? 681  PRO A CG    1 
ATOM   5218 C  CD    . PRO A 1 680 ? 126.483 158.811 155.833 1.00 28.61  ? 681  PRO A CD    1 
ATOM   5219 N  N     . GLY A 1 681 ? 129.051 160.833 152.544 1.00 27.20  ? 682  GLY A N     1 
ATOM   5220 C  CA    . GLY A 1 681 ? 128.901 161.770 151.450 1.00 27.20  ? 682  GLY A CA    1 
ATOM   5221 C  C     . GLY A 1 681 ? 129.203 163.224 151.752 1.00 27.20  ? 682  GLY A C     1 
ATOM   5222 O  O     . GLY A 1 681 ? 129.712 163.933 150.882 1.00 27.20  ? 682  GLY A O     1 
ATOM   5223 N  N     . VAL A 1 682 ? 128.905 163.686 152.962 1.00 29.99  ? 683  VAL A N     1 
ATOM   5224 C  CA    . VAL A 1 682 ? 129.289 165.028 153.389 1.00 29.99  ? 683  VAL A CA    1 
ATOM   5225 C  C     . VAL A 1 682 ? 130.772 165.041 153.741 1.00 29.99  ? 683  VAL A C     1 
ATOM   5226 O  O     . VAL A 1 682 ? 131.264 164.149 154.441 1.00 29.99  ? 683  VAL A O     1 
ATOM   5227 C  CB    . VAL A 1 682 ? 128.418 165.483 154.575 1.00 29.99  ? 683  VAL A CB    1 
ATOM   5228 C  CG1   . VAL A 1 682 ? 128.875 166.816 155.138 1.00 29.99  ? 683  VAL A CG1   1 
ATOM   5229 C  CG2   . VAL A 1 682 ? 126.969 165.591 154.145 1.00 29.99  ? 683  VAL A CG2   1 
ATOM   5230 N  N     . MET A 1 683 ? 131.488 166.058 153.254 1.00 31.44  ? 684  MET A N     1 
ATOM   5231 C  CA    . MET A 1 683 ? 132.932 166.168 153.394 1.00 31.44  ? 684  MET A CA    1 
ATOM   5232 C  C     . MET A 1 683 ? 133.275 167.528 153.986 1.00 31.44  ? 684  MET A C     1 
ATOM   5233 O  O     . MET A 1 683 ? 132.728 168.550 153.564 1.00 31.44  ? 684  MET A O     1 
ATOM   5234 C  CB    . MET A 1 683 ? 133.620 165.988 152.033 1.00 31.44  ? 684  MET A CB    1 
ATOM   5235 C  CG    . MET A 1 683 ? 135.103 166.281 152.019 1.00 31.44  ? 684  MET A CG    1 
ATOM   5236 S  SD    . MET A 1 683 ? 135.816 166.189 150.370 1.00 31.44  ? 684  MET A SD    1 
ATOM   5237 C  CE    . MET A 1 683 ? 136.165 164.442 150.250 1.00 31.44  ? 684  MET A CE    1 
ATOM   5238 N  N     . ASP A 1 684 ? 134.178 167.536 154.968 1.00 32.37  ? 685  ASP A N     1 
ATOM   5239 C  CA    . ASP A 1 684 ? 134.675 168.760 155.589 1.00 32.37  ? 685  ASP A CA    1 
ATOM   5240 C  C     . ASP A 1 684 ? 135.989 169.153 154.933 1.00 32.37  ? 685  ASP A C     1 
ATOM   5241 O  O     . ASP A 1 684 ? 136.980 168.430 155.057 1.00 32.37  ? 685  ASP A O     1 
ATOM   5242 C  CB    . ASP A 1 684 ? 134.865 168.576 157.092 1.00 32.37  ? 685  ASP A CB    1 
ATOM   5243 C  CG    . ASP A 1 684 ? 133.596 168.822 157.874 1.00 32.37  ? 685  ASP A CG    1 
ATOM   5244 O  OD1   . ASP A 1 684 ? 132.686 169.486 157.336 1.00 32.37  ? 685  ASP A OD1   1 
ATOM   5245 O  OD2   . ASP A 1 684 ? 133.510 168.357 159.029 1.00 32.37  ? 685  ASP A OD2   1 
ATOM   5246 N  N     . ASN A 1 685 ? 135.983 170.292 154.230 1.00 32.67  ? 686  ASN A N     1 
ATOM   5247 C  CA    . ASN A 1 685 ? 137.159 170.755 153.487 1.00 32.67  ? 686  ASN A CA    1 
ATOM   5248 C  C     . ASN A 1 685 ? 138.425 170.965 154.327 1.00 32.67  ? 686  ASN A C     1 
ATOM   5249 O  O     . ASN A 1 685 ? 139.501 170.563 153.851 1.00 32.67  ? 686  ASN A O     1 
ATOM   5250 C  CB    . ASN A 1 685 ? 136.803 172.019 152.693 1.00 32.67  ? 686  ASN A CB    1 
ATOM   5251 C  CG    . ASN A 1 685 ? 135.772 171.762 151.621 1.00 32.67  ? 686  ASN A CG    1 
ATOM   5252 O  OD1   . ASN A 1 685 ? 135.888 170.815 150.847 1.00 32.67  ? 686  ASN A OD1   1 
ATOM   5253 N  ND2   . ASN A 1 685 ? 134.755 172.610 151.565 1.00 32.67  ? 686  ASN A ND2   1 
ATOM   5254 N  N     . PRO A 1 686 ? 138.415 171.634 155.503 1.00 30.91  ? 687  PRO A N     1 
ATOM   5255 C  CA    . PRO A 1 686 ? 139.684 171.755 156.252 1.00 30.91  ? 687  PRO A CA    1 
ATOM   5256 C  C     . PRO A 1 686 ? 140.266 170.432 156.727 1.00 30.91  ? 687  PRO A C     1 
ATOM   5257 O  O     . PRO A 1 686 ? 141.492 170.277 156.772 1.00 30.91  ? 687  PRO A O     1 
ATOM   5258 C  CB    . PRO A 1 686 ? 139.316 172.660 157.434 1.00 30.91  ? 687  PRO A CB    1 
ATOM   5259 C  CG    . PRO A 1 686 ? 138.107 173.347 157.036 1.00 30.91  ? 687  PRO A CG    1 
ATOM   5260 C  CD    . PRO A 1 686 ? 137.356 172.396 156.198 1.00 30.91  ? 687  PRO A CD    1 
ATOM   5261 N  N     . LEU A 1 687 ? 139.411 169.485 157.112 1.00 32.75  ? 688  LEU A N     1 
ATOM   5262 C  CA    . LEU A 1 687 ? 139.868 168.191 157.613 1.00 32.75  ? 688  LEU A CA    1 
ATOM   5263 C  C     . LEU A 1 687 ? 140.561 167.361 156.537 1.00 32.75  ? 688  LEU A C     1 
ATOM   5264 O  O     . LEU A 1 687 ? 141.594 166.738 156.803 1.00 32.75  ? 688  LEU A O     1 
ATOM   5265 C  CB    . LEU A 1 687 ? 138.685 167.424 158.198 1.00 32.75  ? 688  LEU A CB    1 
ATOM   5266 C  CG    . LEU A 1 687 ? 138.888 165.961 158.584 1.00 32.75  ? 688  LEU A CG    1 
ATOM   5267 C  CD1   . LEU A 1 687 ? 139.917 165.829 159.686 1.00 32.75  ? 688  LEU A CD1   1 
ATOM   5268 C  CD2   . LEU A 1 687 ? 137.566 165.365 159.013 1.00 32.75  ? 688  LEU A CD2   1 
ATOM   5269 N  N     . VAL A 1 688 ? 140.012 167.328 155.324 1.00 29.35  ? 689  VAL A N     1 
ATOM   5270 C  CA    . VAL A 1 688 ? 140.668 166.598 154.244 1.00 29.35  ? 689  VAL A CA    1 
ATOM   5271 C  C     . VAL A 1 688 ? 141.921 167.330 153.758 1.00 29.35  ? 689  VAL A C     1 
ATOM   5272 O  O     . VAL A 1 688 ? 142.921 166.691 153.410 1.00 29.35  ? 689  VAL A O     1 
ATOM   5273 C  CB    . VAL A 1 688 ? 139.649 166.302 153.123 1.00 29.35  ? 689  VAL A CB    1 
ATOM   5274 C  CG1   . VAL A 1 688 ? 138.981 167.546 152.651 1.00 29.35  ? 689  VAL A CG1   1 
ATOM   5275 C  CG2   . VAL A 1 688 ? 140.287 165.595 151.948 1.00 29.35  ? 689  VAL A CG2   1 
ATOM   5276 N  N     . MET A 1 689 ? 141.902 168.668 153.744 1.00 30.41  ? 690  MET A N     1 
ATOM   5277 C  CA    . MET A 1 689 ? 143.091 169.435 153.363 1.00 30.41  ? 690  MET A CA    1 
ATOM   5278 C  C     . MET A 1 689 ? 144.256 169.215 154.324 1.00 30.41  ? 690  MET A C     1 
ATOM   5279 O  O     . MET A 1 689 ? 145.420 169.228 153.907 1.00 30.41  ? 690  MET A O     1 
ATOM   5280 C  CB    . MET A 1 689 ? 142.759 170.922 153.274 1.00 30.41  ? 690  MET A CB    1 
ATOM   5281 C  CG    . MET A 1 689 ? 142.141 171.347 151.959 1.00 30.41  ? 690  MET A CG    1 
ATOM   5282 S  SD    . MET A 1 689 ? 143.151 170.976 150.514 1.00 30.41  ? 690  MET A SD    1 
ATOM   5283 C  CE    . MET A 1 689 ? 144.689 171.779 150.951 1.00 30.41  ? 690  MET A CE    1 
ATOM   5284 N  N     . HIS A 1 690 ? 143.967 169.078 155.619 1.00 27.50  ? 691  HIS A N     1 
ATOM   5285 C  CA    . HIS A 1 690 ? 144.996 168.706 156.588 1.00 27.50  ? 691  HIS A CA    1 
ATOM   5286 C  C     . HIS A 1 690 ? 145.588 167.329 156.300 1.00 27.50  ? 691  HIS A C     1 
ATOM   5287 O  O     . HIS A 1 690 ? 146.792 167.118 156.473 1.00 27.50  ? 691  HIS A O     1 
ATOM   5288 C  CB    . HIS A 1 690 ? 144.420 168.773 158.000 1.00 27.50  ? 691  HIS A CB    1 
ATOM   5289 C  CG    . HIS A 1 690 ? 145.203 168.005 159.017 1.00 27.50  ? 691  HIS A CG    1 
ATOM   5290 N  ND1   . HIS A 1 690 ? 144.892 166.712 159.375 1.00 27.50  ? 691  HIS A ND1   1 
ATOM   5291 C  CD2   . HIS A 1 690 ? 146.284 168.351 159.754 1.00 27.50  ? 691  HIS A CD2   1 
ATOM   5292 C  CE1   . HIS A 1 690 ? 145.744 166.295 160.293 1.00 27.50  ? 691  HIS A CE1   1 
ATOM   5293 N  NE2   . HIS A 1 690 ? 146.600 167.269 160.539 1.00 27.50  ? 691  HIS A NE2   1 
ATOM   5294 N  N     . GLN A 1 691 ? 144.760 166.378 155.869 1.00 25.90  ? 692  GLN A N     1 
ATOM   5295 C  CA    . GLN A 1 691 ? 145.266 165.054 155.515 1.00 25.90  ? 692  GLN A CA    1 
ATOM   5296 C  C     . GLN A 1 691 ? 146.050 165.050 154.211 1.00 25.90  ? 692  GLN A C     1 
ATOM   5297 O  O     . GLN A 1 691 ? 147.026 164.305 154.085 1.00 25.90  ? 692  GLN A O     1 
ATOM   5298 C  CB    . GLN A 1 691 ? 144.126 164.054 155.424 1.00 25.90  ? 692  GLN A CB    1 
ATOM   5299 C  CG    . GLN A 1 691 ? 143.489 163.720 156.732 1.00 25.90  ? 692  GLN A CG    1 
ATOM   5300 C  CD    . GLN A 1 691 ? 142.154 163.083 156.531 1.00 25.90  ? 692  GLN A CD    1 
ATOM   5301 O  OE1   . GLN A 1 691 ? 142.075 161.945 156.080 1.00 25.90  ? 692  GLN A OE1   1 
ATOM   5302 N  NE2   . GLN A 1 691 ? 141.091 163.797 156.875 1.00 25.90  ? 692  GLN A NE2   1 
ATOM   5303 N  N     . LEU A 1 692 ? 145.598 165.806 153.208 1.00 26.17  ? 693  LEU A N     1 
ATOM   5304 C  CA    . LEU A 1 692 ? 146.328 165.890 151.944 1.00 26.17  ? 693  LEU A CA    1 
ATOM   5305 C  C     . LEU A 1 692 ? 147.717 166.486 152.124 1.00 26.17  ? 693  LEU A C     1 
ATOM   5306 O  O     . LEU A 1 692 ? 148.683 165.995 151.532 1.00 26.17  ? 693  LEU A O     1 
ATOM   5307 C  CB    . LEU A 1 692 ? 145.534 166.700 150.924 1.00 26.17  ? 693  LEU A CB    1 
ATOM   5308 C  CG    . LEU A 1 692 ? 144.279 166.015 150.402 1.00 26.17  ? 693  LEU A CG    1 
ATOM   5309 C  CD1   . LEU A 1 692 ? 143.468 166.976 149.576 1.00 26.17  ? 693  LEU A CD1   1 
ATOM   5310 C  CD2   . LEU A 1 692 ? 144.667 164.809 149.584 1.00 26.17  ? 693  LEU A CD2   1 
ATOM   5311 N  N     . ARG A 1 693 ? 147.826 167.568 152.897 1.00 29.46  ? 694  ARG A N     1 
ATOM   5312 C  CA    . ARG A 1 693 ? 149.127 168.173 153.170 1.00 29.46  ? 694  ARG A CA    1 
ATOM   5313 C  C     . ARG A 1 693 ? 150.066 167.220 153.905 1.00 29.46  ? 694  ARG A C     1 
ATOM   5314 O  O     . ARG A 1 693 ? 151.185 166.968 153.448 1.00 29.46  ? 694  ARG A O     1 
ATOM   5315 C  CB    . ARG A 1 693 ? 148.955 169.471 153.954 1.00 29.46  ? 694  ARG A CB    1 
ATOM   5316 C  CG    . ARG A 1 693 ? 148.412 170.621 153.136 1.00 29.46  ? 694  ARG A CG    1 
ATOM   5317 C  CD    . ARG A 1 693 ? 148.320 171.878 153.981 1.00 29.46  ? 694  ARG A CD    1 
ATOM   5318 N  NE    . ARG A 1 693 ? 147.655 172.975 153.284 1.00 29.46  ? 694  ARG A NE    1 
ATOM   5319 C  CZ    . ARG A 1 693 ? 146.583 173.609 153.744 1.00 29.46  ? 694  ARG A CZ    1 
ATOM   5320 N  NH1   . ARG A 1 693 ? 146.045 174.597 153.046 1.00 29.46  ? 694  ARG A NH1   1 
ATOM   5321 N  NH2   . ARG A 1 693 ? 146.049 173.255 154.904 1.00 29.46  ? 694  ARG A NH2   1 
ATOM   5322 N  N     . CYS A 1 694 ? 149.633 166.674 155.044 1.00 26.32  ? 695  CYS A N     1 
ATOM   5323 C  CA    . CYS A 1 694 ? 150.549 165.887 155.862 1.00 26.32  ? 695  CYS A CA    1 
ATOM   5324 C  C     . CYS A 1 694 ? 150.833 164.500 155.303 1.00 26.32  ? 695  CYS A C     1 
ATOM   5325 O  O     . CYS A 1 694 ? 151.875 163.930 155.628 1.00 26.32  ? 695  CYS A O     1 
ATOM   5326 C  CB    . CYS A 1 694 ? 150.014 165.746 157.285 1.00 26.32  ? 695  CYS A CB    1 
ATOM   5327 S  SG    . CYS A 1 694 ? 148.712 164.527 157.468 1.00 26.32  ? 695  CYS A SG    1 
ATOM   5328 N  N     . ASN A 1 695 ? 149.955 163.937 154.474 1.00 24.76  ? 696  ASN A N     1 
ATOM   5329 C  CA    . ASN A 1 695 ? 150.365 162.776 153.690 1.00 24.76  ? 696  ASN A CA    1 
ATOM   5330 C  C     . ASN A 1 695 ? 151.291 163.132 152.536 1.00 24.76  ? 696  ASN A C     1 
ATOM   5331 O  O     . ASN A 1 695 ? 151.845 162.221 151.914 1.00 24.76  ? 696  ASN A O     1 
ATOM   5332 C  CB    . ASN A 1 695 ? 149.154 162.028 153.131 1.00 24.76  ? 696  ASN A CB    1 
ATOM   5333 C  CG    . ASN A 1 695 ? 148.451 161.187 154.171 1.00 24.76  ? 696  ASN A CG    1 
ATOM   5334 O  OD1   . ASN A 1 695 ? 148.908 160.101 154.514 1.00 24.76  ? 696  ASN A OD1   1 
ATOM   5335 N  ND2   . ASN A 1 695 ? 147.320 161.672 154.658 1.00 24.76  ? 696  ASN A ND2   1 
ATOM   5336 N  N     . GLY A 1 696 ? 151.486 164.416 152.244 1.00 24.70  ? 697  GLY A N     1 
ATOM   5337 C  CA    . GLY A 1 696 ? 152.352 164.821 151.155 1.00 24.70  ? 697  GLY A CA    1 
ATOM   5338 C  C     . GLY A 1 696 ? 151.847 164.471 149.775 1.00 24.70  ? 697  GLY A C     1 
ATOM   5339 O  O     . GLY A 1 696 ? 152.658 164.236 148.876 1.00 24.70  ? 697  GLY A O     1 
ATOM   5340 N  N     . VAL A 1 697 ? 150.525 164.378 149.604 1.00 24.16  ? 698  VAL A N     1 
ATOM   5341 C  CA    . VAL A 1 697 ? 149.929 163.936 148.343 1.00 24.16  ? 698  VAL A CA    1 
ATOM   5342 C  C     . VAL A 1 697 ? 150.258 164.906 147.213 1.00 24.16  ? 698  VAL A C     1 
ATOM   5343 O  O     . VAL A 1 697 ? 150.546 164.491 146.085 1.00 24.16  ? 698  VAL A O     1 
ATOM   5344 C  CB    . VAL A 1 697 ? 148.409 163.759 148.525 1.00 24.16  ? 698  VAL A CB    1 
ATOM   5345 C  CG1   . VAL A 1 697 ? 147.713 163.483 147.209 1.00 24.16  ? 698  VAL A CG1   1 
ATOM   5346 C  CG2   . VAL A 1 697 ? 148.130 162.636 149.496 1.00 24.16  ? 698  VAL A CG2   1 
ATOM   5347 N  N     . LEU A 1 698 ? 150.283 166.204 147.515 1.00 24.63  ? 699  LEU A N     1 
ATOM   5348 C  CA    . LEU A 1 698 ? 150.580 167.224 146.512 1.00 24.63  ? 699  LEU A CA    1 
ATOM   5349 C  C     . LEU A 1 698 ? 152.012 167.125 145.995 1.00 24.63  ? 699  LEU A C     1 
ATOM   5350 O  O     . LEU A 1 698 ? 152.249 167.232 144.788 1.00 24.63  ? 699  LEU A O     1 
ATOM   5351 C  CB    . LEU A 1 698 ? 150.319 168.600 147.107 1.00 24.63  ? 699  LEU A CB    1 
ATOM   5352 C  CG    . LEU A 1 698 ? 148.933 168.680 147.736 1.00 24.63  ? 699  LEU A CG    1 
ATOM   5353 C  CD1   . LEU A 1 698 ? 148.763 169.987 148.449 1.00 24.63  ? 699  LEU A CD1   1 
ATOM   5354 C  CD2   . LEU A 1 698 ? 147.871 168.523 146.679 1.00 24.63  ? 699  LEU A CD2   1 
ATOM   5355 N  N     . GLU A 1 699 ? 152.984 166.969 146.899 1.00 23.57  ? 700  GLU A N     1 
ATOM   5356 C  CA    . GLU A 1 699 ? 154.361 166.694 146.489 1.00 23.57  ? 700  GLU A CA    1 
ATOM   5357 C  C     . GLU A 1 699 ? 154.482 165.368 145.747 1.00 23.57  ? 700  GLU A C     1 
ATOM   5358 O  O     . GLU A 1 699 ? 155.264 165.253 144.798 1.00 23.57  ? 700  GLU A O     1 
ATOM   5359 C  CB    . GLU A 1 699 ? 155.298 166.712 147.695 1.00 23.57  ? 700  GLU A CB    1 
ATOM   5360 C  CG    . GLU A 1 699 ? 155.695 168.097 148.220 1.00 23.57  ? 700  GLU A CG    1 
ATOM   5361 C  CD    . GLU A 1 699 ? 154.562 168.877 148.854 1.00 23.57  ? 700  GLU A CD    1 
ATOM   5362 O  OE1   . GLU A 1 699 ? 153.621 168.249 149.377 1.00 23.57  ? 700  GLU A OE1   1 
ATOM   5363 O  OE2   . GLU A 1 699 ? 154.623 170.122 148.845 1.00 23.57  ? 700  GLU A OE2   1 
ATOM   5364 N  N     . GLY A 1 700 ? 153.752 164.347 146.198 1.00 21.43  ? 701  GLY A N     1 
ATOM   5365 C  CA    . GLY A 1 700 ? 153.756 163.050 145.532 1.00 21.43  ? 701  GLY A CA    1 
ATOM   5366 C  C     . GLY A 1 700 ? 153.294 163.065 144.086 1.00 21.43  ? 701  GLY A C     1 
ATOM   5367 O  O     . GLY A 1 700 ? 153.684 162.199 143.301 1.00 21.43  ? 701  GLY A O     1 
ATOM   5368 N  N     . ILE A 1 701 ? 152.422 164.005 143.726 1.00 23.21  ? 702  ILE A N     1 
ATOM   5369 C  CA    . ILE A 1 701 ? 152.047 164.183 142.327 1.00 23.21  ? 702  ILE A CA    1 
ATOM   5370 C  C     . ILE A 1 701 ? 153.081 165.010 141.569 1.00 23.21  ? 702  ILE A C     1 
ATOM   5371 O  O     . ILE A 1 701 ? 153.384 164.718 140.407 1.00 23.21  ? 702  ILE A O     1 
ATOM   5372 C  CB    . ILE A 1 701 ? 150.655 164.825 142.246 1.00 23.21  ? 702  ILE A CB    1 
ATOM   5373 C  CG1   . ILE A 1 701 ? 149.651 163.995 143.009 1.00 23.21  ? 702  ILE A CG1   1 
ATOM   5374 C  CG2   . ILE A 1 701 ? 150.164 164.822 140.847 1.00 23.21  ? 702  ILE A CG2   1 
ATOM   5375 C  CD1   . ILE A 1 701 ? 148.484 164.787 143.471 1.00 23.21  ? 702  ILE A CD1   1 
ATOM   5376 N  N     . ARG A 1 702 ? 153.609 166.066 142.202 1.00 23.21  ? 703  ARG A N     1 
ATOM   5377 C  CA    . ARG A 1 702 ? 154.601 166.938 141.572 1.00 23.21  ? 703  ARG A CA    1 
ATOM   5378 C  C     . ARG A 1 702 ? 155.865 166.202 141.144 1.00 23.21  ? 703  ARG A C     1 
ATOM   5379 O  O     . ARG A 1 702 ? 156.425 166.507 140.088 1.00 23.21  ? 703  ARG A O     1 
ATOM   5380 C  CB    . ARG A 1 702 ? 154.956 168.092 142.501 1.00 23.21  ? 703  ARG A CB    1 
ATOM   5381 C  CG    . ARG A 1 702 ? 153.915 169.168 142.498 1.00 23.21  ? 703  ARG A CG    1 
ATOM   5382 C  CD    . ARG A 1 702 ? 154.137 170.199 143.572 1.00 23.21  ? 703  ARG A CD    1 
ATOM   5383 N  NE    . ARG A 1 702 ? 153.204 171.307 143.416 1.00 23.21  ? 703  ARG A NE    1 
ATOM   5384 C  CZ    . ARG A 1 702 ? 152.847 172.122 144.398 1.00 23.21  ? 703  ARG A CZ    1 
ATOM   5385 N  NH1   . ARG A 1 702 ? 152.029 173.132 144.158 1.00 23.21  ? 703  ARG A NH1   1 
ATOM   5386 N  NH2   . ARG A 1 702 ? 153.333 171.943 145.615 1.00 23.21  ? 703  ARG A NH2   1 
ATOM   5387 N  N     . ILE A 1 703 ? 156.340 165.248 141.949 1.00 23.06  ? 704  ILE A N     1 
ATOM   5388 C  CA    . ILE A 1 703 ? 157.500 164.451 141.548 1.00 23.06  ? 704  ILE A CA    1 
ATOM   5389 C  C     . ILE A 1 703 ? 157.201 163.606 140.308 1.00 23.06  ? 704  ILE A C     1 
ATOM   5390 O  O     . ILE A 1 703 ? 158.095 163.360 139.489 1.00 23.06  ? 704  ILE A O     1 
ATOM   5391 C  CB    . ILE A 1 703 ? 157.993 163.612 142.750 1.00 23.06  ? 704  ILE A CB    1 
ATOM   5392 C  CG1   . ILE A 1 703 ? 159.248 162.808 142.419 1.00 23.06  ? 704  ILE A CG1   1 
ATOM   5393 C  CG2   . ILE A 1 703 ? 156.914 162.701 143.267 1.00 23.06  ? 704  ILE A CG2   1 
ATOM   5394 C  CD1   . ILE A 1 703 ? 160.395 163.642 141.952 1.00 23.06  ? 704  ILE A CD1   1 
ATOM   5395 N  N     . CYS A 1 704 ? 155.945 163.192 140.114 1.00 24.94  ? 705  CYS A N     1 
ATOM   5396 C  CA    . CYS A 1 704 ? 155.586 162.495 138.882 1.00 24.94  ? 705  CYS A CA    1 
ATOM   5397 C  C     . CYS A 1 704 ? 155.591 163.428 137.675 1.00 24.94  ? 705  CYS A C     1 
ATOM   5398 O  O     . CYS A 1 704 ? 156.035 163.040 136.590 1.00 24.94  ? 705  CYS A O     1 
ATOM   5399 C  CB    . CYS A 1 704 ? 154.222 161.828 139.026 1.00 24.94  ? 705  CYS A CB    1 
ATOM   5400 S  SG    . CYS A 1 704 ? 153.687 160.955 137.546 1.00 24.94  ? 705  CYS A SG    1 
ATOM   5401 N  N     . ARG A 1 705 ? 155.097 164.655 137.836 1.00 25.12  ? 706  ARG A N     1 
ATOM   5402 C  CA    . ARG A 1 705 ? 155.108 165.602 136.725 1.00 25.12  ? 706  ARG A CA    1 
ATOM   5403 C  C     . ARG A 1 705 ? 156.503 166.155 136.462 1.00 25.12  ? 706  ARG A C     1 
ATOM   5404 O  O     . ARG A 1 705 ? 156.891 166.334 135.303 1.00 25.12  ? 706  ARG A O     1 
ATOM   5405 C  CB    . ARG A 1 705 ? 154.120 166.734 137.001 1.00 25.12  ? 706  ARG A CB    1 
ATOM   5406 C  CG    . ARG A 1 705 ? 152.684 166.257 137.092 1.00 25.12  ? 706  ARG A CG    1 
ATOM   5407 C  CD    . ARG A 1 705 ? 151.715 167.366 137.450 1.00 25.12  ? 706  ARG A CD    1 
ATOM   5408 N  NE    . ARG A 1 705 ? 151.215 168.077 136.285 1.00 25.12  ? 706  ARG A NE    1 
ATOM   5409 C  CZ    . ARG A 1 705 ? 151.686 169.246 135.873 1.00 25.12  ? 706  ARG A CZ    1 
ATOM   5410 N  NH1   . ARG A 1 705 ? 151.138 169.851 134.830 1.00 25.12  ? 706  ARG A NH1   1 
ATOM   5411 N  NH2   . ARG A 1 705 ? 152.675 169.832 136.533 1.00 25.12  ? 706  ARG A NH2   1 
ATOM   5412 N  N     . LYS A 1 706 ? 157.273 166.432 137.516 1.00 26.95  ? 707  LYS A N     1 
ATOM   5413 C  CA    . LYS A 1 706 ? 158.632 166.937 137.330 1.00 26.95  ? 707  LYS A CA    1 
ATOM   5414 C  C     . LYS A 1 706 ? 159.579 165.840 136.859 1.00 26.95  ? 707  LYS A C     1 
ATOM   5415 O  O     . LYS A 1 706 ? 160.279 166.001 135.853 1.00 26.95  ? 707  LYS A O     1 
ATOM   5416 C  CB    . LYS A 1 706 ? 159.156 167.555 138.625 1.00 26.95  ? 707  LYS A CB    1 
ATOM   5417 C  CG    . LYS A 1 706 ? 158.476 168.832 139.058 1.00 26.95  ? 707  LYS A CG    1 
ATOM   5418 C  CD    . LYS A 1 706 ? 158.932 170.013 138.241 1.00 26.95  ? 707  LYS A CD    1 
ATOM   5419 C  CE    . LYS A 1 706 ? 158.479 171.307 138.889 1.00 26.95  ? 707  LYS A CE    1 
ATOM   5420 N  NZ    . LYS A 1 706 ? 158.977 172.502 138.158 1.00 26.95  ? 707  LYS A NZ    1 
ATOM   5421 N  N     . GLY A 1 707 ? 159.619 164.722 137.571 1.00 29.05  ? 708  GLY A N     1 
ATOM   5422 C  CA    . GLY A 1 707 ? 160.622 163.705 137.338 1.00 29.05  ? 708  GLY A CA    1 
ATOM   5423 C  C     . GLY A 1 707 ? 160.291 162.756 136.209 1.00 29.05  ? 708  GLY A C     1 
ATOM   5424 O  O     . GLY A 1 707 ? 159.499 163.052 135.313 1.00 29.05  ? 708  GLY A O     1 
ATOM   5425 N  N     . PHE A 1 708 ? 160.919 161.587 136.266 1.00 31.55  ? 709  PHE A N     1 
ATOM   5426 C  CA    . PHE A 1 708 ? 160.848 160.589 135.202 1.00 31.55  ? 709  PHE A CA    1 
ATOM   5427 C  C     . PHE A 1 708 ? 160.398 159.264 135.800 1.00 31.55  ? 709  PHE A C     1 
ATOM   5428 O  O     . PHE A 1 708 ? 161.225 158.392 136.093 1.00 31.55  ? 709  PHE A O     1 
ATOM   5429 C  CB    . PHE A 1 708 ? 162.192 160.447 134.485 1.00 31.55  ? 709  PHE A CB    1 
ATOM   5430 C  CG    . PHE A 1 708 ? 162.695 161.725 133.857 1.00 31.55  ? 709  PHE A CG    1 
ATOM   5431 C  CD1   . PHE A 1 708 ? 162.179 162.174 132.653 1.00 31.55  ? 709  PHE A CD1   1 
ATOM   5432 C  CD2   . PHE A 1 708 ? 163.702 162.460 134.461 1.00 31.55  ? 709  PHE A CD2   1 
ATOM   5433 C  CE1   . PHE A 1 708 ? 162.643 163.335 132.077 1.00 31.55  ? 709  PHE A CE1   1 
ATOM   5434 C  CE2   . PHE A 1 708 ? 164.169 163.621 133.888 1.00 31.55  ? 709  PHE A CE2   1 
ATOM   5435 C  CZ    . PHE A 1 708 ? 163.639 164.058 132.695 1.00 31.55  ? 709  PHE A CZ    1 
ATOM   5436 N  N     . PRO A 1 709 ? 159.090 159.087 136.007 1.00 32.43  ? 710  PRO A N     1 
ATOM   5437 C  CA    . PRO A 1 709 ? 158.620 157.993 136.872 1.00 32.43  ? 710  PRO A CA    1 
ATOM   5438 C  C     . PRO A 1 709 ? 158.765 156.602 136.276 1.00 32.43  ? 710  PRO A C     1 
ATOM   5439 O  O     . PRO A 1 709 ? 158.871 155.632 137.034 1.00 32.43  ? 710  PRO A O     1 
ATOM   5440 C  CB    . PRO A 1 709 ? 157.146 158.346 137.097 1.00 32.43  ? 710  PRO A CB    1 
ATOM   5441 C  CG    . PRO A 1 709 ? 156.783 159.157 135.912 1.00 32.43  ? 710  PRO A CG    1 
ATOM   5442 C  CD    . PRO A 1 709 ? 157.989 159.972 135.602 1.00 32.43  ? 710  PRO A CD    1 
ATOM   5443 N  N     . ASN A 1 710 ? 158.775 156.468 134.955 1.00 36.74  ? 711  ASN A N     1 
ATOM   5444 C  CA    . ASN A 1 710 ? 158.890 155.177 134.287 1.00 36.74  ? 711  ASN A CA    1 
ATOM   5445 C  C     . ASN A 1 710 ? 160.274 155.046 133.674 1.00 36.74  ? 711  ASN A C     1 
ATOM   5446 O  O     . ASN A 1 710 ? 160.738 155.954 132.978 1.00 36.74  ? 711  ASN A O     1 
ATOM   5447 C  CB    . ASN A 1 710 ? 157.823 155.007 133.211 1.00 36.74  ? 711  ASN A CB    1 
ATOM   5448 C  CG    . ASN A 1 710 ? 156.433 155.035 133.775 1.00 36.74  ? 711  ASN A CG    1 
ATOM   5449 O  OD1   . ASN A 1 710 ? 156.114 154.285 134.693 1.00 36.74  ? 711  ASN A OD1   1 
ATOM   5450 N  ND2   . ASN A 1 710 ? 155.588 155.898 133.229 1.00 36.74  ? 711  ASN A ND2   1 
ATOM   5451 N  N     . ARG A 1 711 ? 160.919 153.912 133.913 1.00 36.42  ? 712  ARG A N     1 
ATOM   5452 C  CA    . ARG A 1 711 ? 162.297 153.707 133.503 1.00 36.42  ? 712  ARG A CA    1 
ATOM   5453 C  C     . ARG A 1 711 ? 162.512 152.229 133.239 1.00 36.42  ? 712  ARG A C     1 
ATOM   5454 O  O     . ARG A 1 711 ? 161.935 151.381 133.923 1.00 36.42  ? 712  ARG A O     1 
ATOM   5455 C  CB    . ARG A 1 711 ? 163.223 154.257 134.582 1.00 36.42  ? 712  ARG A CB    1 
ATOM   5456 C  CG    . ARG A 1 711 ? 162.797 153.823 135.965 1.00 36.42  ? 712  ARG A CG    1 
ATOM   5457 C  CD    . ARG A 1 711 ? 163.489 154.632 137.038 1.00 36.42  ? 712  ARG A CD    1 
ATOM   5458 N  NE    . ARG A 1 711 ? 162.994 154.305 138.361 1.00 36.42  ? 712  ARG A NE    1 
ATOM   5459 C  CZ    . ARG A 1 711 ? 162.176 155.075 139.073 1.00 36.42  ? 712  ARG A CZ    1 
ATOM   5460 N  NH1   . ARG A 1 711 ? 162.031 154.888 140.367 1.00 36.42  ? 712  ARG A NH1   1 
ATOM   5461 N  NH2   . ARG A 1 711 ? 161.690 156.177 138.524 1.00 36.42  ? 712  ARG A NH2   1 
ATOM   5462 N  N     . ILE A 1 712 ? 163.329 151.926 132.228 1.00 44.65  ? 713  ILE A N     1 
ATOM   5463 C  CA    . ILE A 1 712 ? 163.477 150.571 131.698 1.00 44.65  ? 713  ILE A CA    1 
ATOM   5464 C  C     . ILE A 1 712 ? 164.952 150.310 131.410 1.00 44.65  ? 713  ILE A C     1 
ATOM   5465 O  O     . ILE A 1 712 ? 165.668 151.196 130.933 1.00 44.65  ? 713  ILE A O     1 
ATOM   5466 C  CB    . ILE A 1 712 ? 162.637 150.386 130.399 1.00 44.65  ? 713  ILE A CB    1 
ATOM   5467 C  CG1   . ILE A 1 712 ? 161.140 150.649 130.616 1.00 44.65  ? 713  ILE A CG1   1 
ATOM   5468 C  CG2   . ILE A 1 712 ? 162.799 148.997 129.796 1.00 44.65  ? 713  ILE A CG2   1 
ATOM   5469 C  CD1   . ILE A 1 712 ? 160.263 150.353 129.429 1.00 44.65  ? 713  ILE A CD1   1 
ATOM   5470 N  N     . LEU A 1 713 ? 165.410 149.100 131.733 1.00 52.04  ? 714  LEU A N     1 
ATOM   5471 C  CA    . LEU A 1 713 ? 166.740 148.643 131.353 1.00 52.04  ? 714  LEU A CA    1 
ATOM   5472 C  C     . LEU A 1 713 ? 166.818 148.442 129.843 1.00 52.04  ? 714  LEU A C     1 
ATOM   5473 O  O     . LEU A 1 713 ? 165.882 147.917 129.232 1.00 52.04  ? 714  LEU A O     1 
ATOM   5474 C  CB    . LEU A 1 713 ? 167.073 147.336 132.065 1.00 52.04  ? 714  LEU A CB    1 
ATOM   5475 C  CG    . LEU A 1 713 ? 167.226 147.392 133.581 1.00 52.04  ? 714  LEU A CG    1 
ATOM   5476 C  CD1   . LEU A 1 713 ? 167.095 146.003 134.169 1.00 52.04  ? 714  LEU A CD1   1 
ATOM   5477 C  CD2   . LEU A 1 713 ? 168.569 147.991 133.940 1.00 52.04  ? 714  LEU A CD2   1 
ATOM   5478 N  N     . TYR A 1 714 ? 167.931 148.899 129.244 1.00 54.34  ? 715  TYR A N     1 
ATOM   5479 C  CA    . TYR A 1 714 ? 168.121 148.866 127.789 1.00 54.34  ? 715  TYR A CA    1 
ATOM   5480 C  C     . TYR A 1 714 ? 168.000 147.470 127.188 1.00 54.34  ? 715  TYR A C     1 
ATOM   5481 O  O     . TYR A 1 714 ? 167.601 147.338 126.025 1.00 54.34  ? 715  TYR A O     1 
ATOM   5482 C  CB    . TYR A 1 714 ? 169.487 149.426 127.402 1.00 54.34  ? 715  TYR A CB    1 
ATOM   5483 C  CG    . TYR A 1 714 ? 169.701 150.897 127.616 1.00 54.34  ? 715  TYR A CG    1 
ATOM   5484 C  CD1   . TYR A 1 714 ? 169.062 151.827 126.817 1.00 54.34  ? 715  TYR A CD1   1 
ATOM   5485 C  CD2   . TYR A 1 714 ? 170.591 151.355 128.570 1.00 54.34  ? 715  TYR A CD2   1 
ATOM   5486 C  CE1   . TYR A 1 714 ? 169.272 153.173 126.989 1.00 54.34  ? 715  TYR A CE1   1 
ATOM   5487 C  CE2   . TYR A 1 714 ? 170.809 152.698 128.748 1.00 54.34  ? 715  TYR A CE2   1 
ATOM   5488 C  CZ    . TYR A 1 714 ? 170.146 153.602 127.955 1.00 54.34  ? 715  TYR A CZ    1 
ATOM   5489 O  OH    . TYR A 1 714 ? 170.366 154.946 128.126 1.00 54.34  ? 715  TYR A OH    1 
ATOM   5490 N  N     . GLY A 1 715 ? 168.391 146.432 127.931 1.00 59.06  ? 716  GLY A N     1 
ATOM   5491 C  CA    . GLY A 1 715 ? 168.194 145.071 127.452 1.00 59.06  ? 716  GLY A CA    1 
ATOM   5492 C  C     . GLY A 1 715 ? 166.733 144.718 127.249 1.00 59.06  ? 716  GLY A C     1 
ATOM   5493 O  O     . GLY A 1 715 ? 166.355 144.147 126.223 1.00 59.06  ? 716  GLY A O     1 
ATOM   5494 N  N     . ASP A 1 716 ? 165.891 145.057 128.226 1.00 61.17  ? 717  ASP A N     1 
ATOM   5495 C  CA    . ASP A 1 716 ? 164.455 144.854 128.066 1.00 61.17  ? 717  ASP A CA    1 
ATOM   5496 C  C     . ASP A 1 716 ? 163.839 145.830 127.071 1.00 61.17  ? 717  ASP A C     1 
ATOM   5497 O  O     . ASP A 1 716 ? 162.843 145.494 126.421 1.00 61.17  ? 717  ASP A O     1 
ATOM   5498 C  CB    . ASP A 1 716 ? 163.752 144.955 129.419 1.00 61.17  ? 717  ASP A CB    1 
ATOM   5499 C  CG    . ASP A 1 716 ? 163.896 143.689 130.248 1.00 61.17  ? 717  ASP A CG    1 
ATOM   5500 O  OD1   . ASP A 1 716 ? 164.303 142.651 129.684 1.00 61.17  ? 717  ASP A OD1   1 
ATOM   5501 O  OD2   . ASP A 1 716 ? 163.596 143.726 131.459 1.00 61.17  ? 717  ASP A OD2   1 
ATOM   5502 N  N     . PHE A 1 717 ? 164.394 147.042 126.964 1.00 60.25  ? 718  PHE A N     1 
ATOM   5503 C  CA    . PHE A 1 717 ? 163.901 148.019 125.993 1.00 60.25  ? 718  PHE A CA    1 
ATOM   5504 C  C     . PHE A 1 717 ? 164.084 147.550 124.553 1.00 60.25  ? 718  PHE A C     1 
ATOM   5505 O  O     . PHE A 1 717 ? 163.187 147.729 123.722 1.00 60.25  ? 718  PHE A O     1 
ATOM   5506 C  CB    . PHE A 1 717 ? 164.590 149.365 126.201 1.00 60.25  ? 718  PHE A CB    1 
ATOM   5507 C  CG    . PHE A 1 717 ? 164.003 150.468 125.378 1.00 60.25  ? 718  PHE A CG    1 
ATOM   5508 C  CD1   . PHE A 1 717 ? 162.723 150.929 125.635 1.00 60.25  ? 718  PHE A CD1   1 
ATOM   5509 C  CD2   . PHE A 1 717 ? 164.720 151.040 124.345 1.00 60.25  ? 718  PHE A CD2   1 
ATOM   5510 C  CE1   . PHE A 1 717 ? 162.165 151.938 124.876 1.00 60.25  ? 718  PHE A CE1   1 
ATOM   5511 C  CE2   . PHE A 1 717 ? 164.172 152.058 123.584 1.00 60.25  ? 718  PHE A CE2   1 
ATOM   5512 C  CZ    . PHE A 1 717 ? 162.891 152.502 123.852 1.00 60.25  ? 718  PHE A CZ    1 
ATOM   5513 N  N     . ARG A 1 718 ? 165.256 146.999 124.229 1.00 65.50  ? 719  ARG A N     1 
ATOM   5514 C  CA    . ARG A 1 718 ? 165.443 146.321 122.947 1.00 65.50  ? 719  ARG A CA    1 
ATOM   5515 C  C     . ARG A 1 718 ? 164.485 145.144 122.790 1.00 65.50  ? 719  ARG A C     1 
ATOM   5516 O  O     . ARG A 1 718 ? 163.891 144.954 121.723 1.00 65.50  ? 719  ARG A O     1 
ATOM   5517 C  CB    . ARG A 1 718 ? 166.895 145.864 122.796 1.00 65.50  ? 719  ARG A CB    1 
ATOM   5518 C  CG    . ARG A 1 718 ? 167.171 145.119 121.497 1.00 65.50  ? 719  ARG A CG    1 
ATOM   5519 C  CD    . ARG A 1 718 ? 168.646 144.776 121.337 1.00 65.50  ? 719  ARG A CD    1 
ATOM   5520 N  NE    . ARG A 1 718 ? 169.137 143.910 122.403 1.00 65.50  ? 719  ARG A NE    1 
ATOM   5521 C  CZ    . ARG A 1 718 ? 169.005 142.588 122.416 1.00 65.50  ? 719  ARG A CZ    1 
ATOM   5522 N  NH1   . ARG A 1 718 ? 169.489 141.882 123.428 1.00 65.50  ? 719  ARG A NH1   1 
ATOM   5523 N  NH2   . ARG A 1 718 ? 168.400 141.967 121.412 1.00 65.50  ? 719  ARG A NH2   1 
ATOM   5524 N  N     . GLN A 1 719 ? 164.350 144.328 123.840 1.00 66.92  ? 720  GLN A N     1 
ATOM   5525 C  CA    . GLN A 1 719 ? 163.548 143.106 123.775 1.00 66.92  ? 720  GLN A CA    1 
ATOM   5526 C  C     . GLN A 1 719 ? 162.069 143.394 123.542 1.00 66.92  ? 720  GLN A C     1 
ATOM   5527 O  O     . GLN A 1 719 ? 161.437 142.781 122.675 1.00 66.92  ? 720  GLN A O     1 
ATOM   5528 C  CB    . GLN A 1 719 ? 163.732 142.297 125.062 1.00 66.92  ? 720  GLN A CB    1 
ATOM   5529 C  CG    . GLN A 1 719 ? 162.853 141.042 125.185 1.00 66.92  ? 720  GLN A CG    1 
ATOM   5530 C  CD    . GLN A 1 719 ? 163.134 139.953 124.153 1.00 66.92  ? 720  GLN A CD    1 
ATOM   5531 O  OE1   . GLN A 1 719 ? 164.171 139.943 123.487 1.00 66.92  ? 720  GLN A OE1   1 
ATOM   5532 N  NE2   . GLN A 1 719 ? 162.193 139.026 124.019 1.00 66.92  ? 720  GLN A NE2   1 
ATOM   5533 N  N     . ARG A 1 720 ? 161.498 144.323 124.302 1.00 70.21  ? 721  ARG A N     1 
ATOM   5534 C  CA    . ARG A 1 720 ? 160.061 144.554 124.206 1.00 70.21  ? 721  ARG A CA    1 
ATOM   5535 C  C     . ARG A 1 720 ? 159.671 145.433 123.020 1.00 70.21  ? 721  ARG A C     1 
ATOM   5536 O  O     . ARG A 1 720 ? 158.669 145.156 122.351 1.00 70.21  ? 721  ARG A O     1 
ATOM   5537 C  CB    . ARG A 1 720 ? 159.540 145.161 125.511 1.00 70.21  ? 721  ARG A CB    1 
ATOM   5538 C  CG    . ARG A 1 720 ? 158.029 145.334 125.526 1.00 70.21  ? 721  ARG A CG    1 
ATOM   5539 C  CD    . ARG A 1 720 ? 157.460 145.679 126.889 1.00 70.21  ? 721  ARG A CD    1 
ATOM   5540 N  NE    . ARG A 1 720 ? 156.007 145.833 126.826 1.00 70.21  ? 721  ARG A NE    1 
ATOM   5541 C  CZ    . ARG A 1 720 ? 155.131 144.835 126.819 1.00 70.21  ? 721  ARG A CZ    1 
ATOM   5542 N  NH1   . ARG A 1 720 ? 153.835 145.101 126.751 1.00 70.21  ? 721  ARG A NH1   1 
ATOM   5543 N  NH2   . ARG A 1 720 ? 155.540 143.576 126.882 1.00 70.21  ? 721  ARG A NH2   1 
ATOM   5544 N  N     . TYR A 1 721 ? 160.450 146.465 122.711 1.00 68.24  ? 722  TYR A N     1 
ATOM   5545 C  CA    . TYR A 1 721 ? 159.974 147.519 121.826 1.00 68.24  ? 722  TYR A CA    1 
ATOM   5546 C  C     . TYR A 1 721 ? 160.586 147.554 120.432 1.00 68.24  ? 722  TYR A C     1 
ATOM   5547 O  O     . TYR A 1 721 ? 160.263 148.472 119.674 1.00 68.24  ? 722  TYR A O     1 
ATOM   5548 C  CB    . TYR A 1 721 ? 160.145 148.876 122.507 1.00 68.24  ? 722  TYR A CB    1 
ATOM   5549 C  CG    . TYR A 1 721 ? 159.378 148.974 123.802 1.00 68.24  ? 722  TYR A CG    1 
ATOM   5550 C  CD1   . TYR A 1 721 ? 158.000 149.156 123.788 1.00 68.24  ? 722  TYR A CD1   1 
ATOM   5551 C  CD2   . TYR A 1 721 ? 160.012 148.865 125.026 1.00 68.24  ? 722  TYR A CD2   1 
ATOM   5552 C  CE1   . TYR A 1 721 ? 157.280 149.255 124.956 1.00 68.24  ? 722  TYR A CE1   1 
ATOM   5553 C  CE2   . TYR A 1 721 ? 159.299 148.957 126.205 1.00 68.24  ? 722  TYR A CE2   1 
ATOM   5554 C  CZ    . TYR A 1 721 ? 157.932 149.153 126.161 1.00 68.24  ? 722  TYR A CZ    1 
ATOM   5555 O  OH    . TYR A 1 721 ? 157.208 149.237 127.327 1.00 68.24  ? 722  TYR A OH    1 
ATOM   5556 N  N     . ARG A 1 722 ? 161.495 146.637 120.080 1.00 77.43  ? 723  ARG A N     1 
ATOM   5557 C  CA    . ARG A 1 722 ? 162.023 146.610 118.712 1.00 77.43  ? 723  ARG A CA    1 
ATOM   5558 C  C     . ARG A 1 722 ? 160.940 146.299 117.669 1.00 77.43  ? 723  ARG A C     1 
ATOM   5559 O  O     . ARG A 1 722 ? 161.131 146.591 116.481 1.00 77.43  ? 723  ARG A O     1 
ATOM   5560 C  CB    . ARG A 1 722 ? 163.155 145.587 118.592 1.00 77.43  ? 723  ARG A CB    1 
ATOM   5561 C  CG    . ARG A 1 722 ? 164.072 145.816 117.395 1.00 77.43  ? 723  ARG A CG    1 
ATOM   5562 C  CD    . ARG A 1 722 ? 165.143 144.763 117.277 1.00 77.43  ? 723  ARG A CD    1 
ATOM   5563 N  NE    . ARG A 1 722 ? 164.593 143.539 116.706 1.00 77.43  ? 723  ARG A NE    1 
ATOM   5564 C  CZ    . ARG A 1 722 ? 164.410 143.329 115.406 1.00 77.43  ? 723  ARG A CZ    1 
ATOM   5565 N  NH1   . ARG A 1 722 ? 163.845 142.204 114.993 1.00 77.43  ? 723  ARG A NH1   1 
ATOM   5566 N  NH2   . ARG A 1 722 ? 164.760 144.250 114.519 1.00 77.43  ? 723  ARG A NH2   1 
ATOM   5567 N  N     . ILE A 1 723 ? 159.812 145.718 118.100 1.00 74.98  ? 724  ILE A N     1 
ATOM   5568 C  CA    . ILE A 1 723 ? 158.658 145.446 117.239 1.00 74.98  ? 724  ILE A CA    1 
ATOM   5569 C  C     . ILE A 1 723 ? 158.148 146.733 116.592 1.00 74.98  ? 724  ILE A C     1 
ATOM   5570 O  O     . ILE A 1 723 ? 157.670 146.722 115.449 1.00 74.98  ? 724  ILE A O     1 
ATOM   5571 C  CB    . ILE A 1 723 ? 157.562 144.726 118.060 1.00 74.98  ? 724  ILE A CB    1 
ATOM   5572 C  CG1   . ILE A 1 723 ? 158.027 143.364 118.614 1.00 74.98  ? 724  ILE A CG1   1 
ATOM   5573 C  CG2   . ILE A 1 723 ? 156.291 144.482 117.251 1.00 74.98  ? 724  ILE A CG2   1 
ATOM   5574 C  CD1   . ILE A 1 723 ? 159.012 142.558 117.751 1.00 74.98  ? 724  ILE A CD1   1 
ATOM   5575 N  N     . LEU A 1 724 ? 158.166 147.836 117.353 1.00 73.73  ? 725  LEU A N     1 
ATOM   5576 C  CA    . LEU A 1 724 ? 157.755 149.162 116.877 1.00 73.73  ? 725  LEU A CA    1 
ATOM   5577 C  C     . LEU A 1 724 ? 158.396 149.573 115.550 1.00 73.73  ? 725  LEU A C     1 
ATOM   5578 O  O     . LEU A 1 724 ? 157.703 150.029 114.635 1.00 73.73  ? 725  LEU A O     1 
ATOM   5579 C  CB    . LEU A 1 724 ? 158.028 150.224 117.948 1.00 73.73  ? 725  LEU A CB    1 
ATOM   5580 C  CG    . LEU A 1 724 ? 157.137 150.371 119.196 1.00 73.73  ? 725  LEU A CG    1 
ATOM   5581 C  CD1   . LEU A 1 724 ? 155.747 150.743 118.744 1.00 73.73  ? 725  LEU A CD1   1 
ATOM   5582 C  CD2   . LEU A 1 724 ? 157.068 149.182 120.151 1.00 73.73  ? 725  LEU A CD2   1 
ATOM   5583 N  N     . ASN A 1 725 ? 159.713 149.424 115.416 1.00 75.76  ? 726  ASN A N     1 
ATOM   5584 C  CA    . ASN A 1 725 ? 160.393 149.705 114.148 1.00 75.76  ? 726  ASN A CA    1 
ATOM   5585 C  C     . ASN A 1 725 ? 161.578 148.763 113.971 1.00 75.76  ? 726  ASN A C     1 
ATOM   5586 O  O     . ASN A 1 725 ? 162.720 149.119 114.287 1.00 75.76  ? 726  ASN A O     1 
ATOM   5587 C  CB    . ASN A 1 725 ? 160.838 151.169 114.078 1.00 75.76  ? 726  ASN A CB    1 
ATOM   5588 C  CG    . ASN A 1 725 ? 161.498 151.540 112.747 1.00 75.76  ? 726  ASN A CG    1 
ATOM   5589 O  OD1   . ASN A 1 725 ? 161.430 150.804 111.760 1.00 75.76  ? 726  ASN A OD1   1 
ATOM   5590 N  ND2   . ASN A 1 725 ? 162.140 152.700 112.723 1.00 75.76  ? 726  ASN A ND2   1 
ATOM   5591 N  N     . PRO A 1 726 ? 161.320 147.504 113.569 1.00 78.34  ? 727  PRO A N     1 
ATOM   5592 C  CA    . PRO A 1 726 ? 162.405 146.521 113.349 1.00 78.34  ? 727  PRO A CA    1 
ATOM   5593 C  C     . PRO A 1 726 ? 163.532 146.979 112.430 1.00 78.34  ? 727  PRO A C     1 
ATOM   5594 O  O     . PRO A 1 726 ? 164.679 146.549 112.603 1.00 78.34  ? 727  PRO A O     1 
ATOM   5595 C  CB    . PRO A 1 726 ? 161.664 145.333 112.723 1.00 78.34  ? 727  PRO A CB    1 
ATOM   5596 C  CG    . PRO A 1 726 ? 160.275 145.452 113.201 1.00 78.34  ? 727  PRO A CG    1 
ATOM   5597 C  CD    . PRO A 1 726 ? 160.002 146.926 113.257 1.00 78.34  ? 727  PRO A CD    1 
ATOM   5598 N  N     . ALA A 1 727 ? 163.232 147.851 111.464 1.00 79.26  ? 728  ALA A N     1 
ATOM   5599 C  CA    . ALA A 1 727 ? 164.226 148.333 110.513 1.00 79.26  ? 728  ALA A CA    1 
ATOM   5600 C  C     . ALA A 1 727 ? 165.232 149.292 111.134 1.00 79.26  ? 728  ALA A C     1 
ATOM   5601 O  O     . ALA A 1 727 ? 166.285 149.528 110.533 1.00 79.26  ? 728  ALA A O     1 
ATOM   5602 C  CB    . ALA A 1 727 ? 163.533 149.007 109.330 1.00 79.26  ? 728  ALA A CB    1 
ATOM   5603 N  N     . ALA A 1 728 ? 164.927 149.869 112.299 1.00 80.35  ? 729  ALA A N     1 
ATOM   5604 C  CA    . ALA A 1 728 ? 165.853 150.815 112.915 1.00 80.35  ? 729  ALA A CA    1 
ATOM   5605 C  C     . ALA A 1 728 ? 167.094 150.108 113.446 1.00 80.35  ? 729  ALA A C     1 
ATOM   5606 O  O     . ALA A 1 728 ? 168.204 150.643 113.349 1.00 80.35  ? 729  ALA A O     1 
ATOM   5607 C  CB    . ALA A 1 728 ? 165.154 151.585 114.032 1.00 80.35  ? 729  ALA A CB    1 
ATOM   5608 N  N     . ILE A 1 729 ? 166.931 148.895 113.969 1.00 81.51  ? 730  ILE A N     1 
ATOM   5609 C  CA    . ILE A 1 729 ? 168.027 148.093 114.516 1.00 81.51  ? 730  ILE A CA    1 
ATOM   5610 C  C     . ILE A 1 729 ? 167.811 146.625 114.144 1.00 81.51  ? 730  ILE A C     1 
ATOM   5611 O  O     . ILE A 1 729 ? 167.084 145.884 114.821 1.00 81.51  ? 730  ILE A O     1 
ATOM   5612 C  CB    . ILE A 1 729 ? 168.220 148.325 116.035 1.00 81.51  ? 730  ILE A CB    1 
ATOM   5613 C  CG1   . ILE A 1 729 ? 166.919 148.250 116.852 1.00 81.51  ? 730  ILE A CG1   1 
ATOM   5614 C  CG2   . ILE A 1 729 ? 169.002 149.608 116.331 1.00 81.51  ? 730  ILE A CG2   1 
ATOM   5615 C  CD1   . ILE A 1 729 ? 167.168 147.991 118.316 1.00 81.51  ? 730  ILE A CD1   1 
ATOM   5616 N  N     . PRO A 1 730 ? 168.401 146.170 113.042 1.00 85.22  ? 731  PRO A N     1 
ATOM   5617 C  CA    . PRO A 1 730 ? 168.219 144.773 112.623 1.00 85.22  ? 731  PRO A CA    1 
ATOM   5618 C  C     . PRO A 1 730 ? 169.006 143.776 113.464 1.00 85.22  ? 731  PRO A C     1 
ATOM   5619 O  O     . PRO A 1 730 ? 170.239 143.739 113.392 1.00 85.22  ? 731  PRO A O     1 
ATOM   5620 C  CB    . PRO A 1 730 ? 168.686 144.789 111.161 1.00 85.22  ? 731  PRO A CB    1 
ATOM   5621 C  CG    . PRO A 1 730 ? 169.661 145.919 111.086 1.00 85.22  ? 731  PRO A CG    1 
ATOM   5622 C  CD    . PRO A 1 730 ? 169.178 146.954 112.063 1.00 85.22  ? 731  PRO A CD    1 
ATOM   5623 N  N     . GLU A 1 731 ? 168.311 143.016 114.316 1.00 85.36  ? 732  GLU A N     1 
ATOM   5624 C  CA    . GLU A 1 731 ? 168.957 141.920 115.030 1.00 85.36  ? 732  GLU A CA    1 
ATOM   5625 C  C     . GLU A 1 731 ? 169.503 140.888 114.050 1.00 85.36  ? 732  GLU A C     1 
ATOM   5626 O  O     . GLU A 1 731 ? 168.892 140.594 113.019 1.00 85.36  ? 732  GLU A O     1 
ATOM   5627 C  CB    . GLU A 1 731 ? 167.995 141.247 116.011 1.00 85.36  ? 732  GLU A CB    1 
ATOM   5628 C  CG    . GLU A 1 731 ? 167.771 142.002 117.314 1.00 85.36  ? 732  GLU A CG    1 
ATOM   5629 C  CD    . GLU A 1 731 ? 166.784 141.296 118.228 1.00 85.36  ? 732  GLU A CD    1 
ATOM   5630 O  OE1   . GLU A 1 731 ? 166.936 140.073 118.431 1.00 85.36  ? 732  GLU A OE1   1 
ATOM   5631 O  OE2   . GLU A 1 731 ? 165.872 141.956 118.764 1.00 85.36  ? 732  GLU A OE2   1 
ATOM   5632 N  N     . GLY A 1 732 ? 170.669 140.345 114.385 1.00 89.31  ? 733  GLY A N     1 
ATOM   5633 C  CA    . GLY A 1 732 ? 171.522 139.656 113.450 1.00 89.31  ? 733  GLY A CA    1 
ATOM   5634 C  C     . GLY A 1 732 ? 172.607 140.533 112.862 1.00 89.31  ? 733  GLY A C     1 
ATOM   5635 O  O     . GLY A 1 732 ? 173.591 140.010 112.328 1.00 89.31  ? 733  GLY A O     1 
ATOM   5636 N  N     . GLN A 1 733 ? 172.444 141.851 112.943 1.00 91.80  ? 734  GLN A N     1 
ATOM   5637 C  CA    . GLN A 1 733 ? 173.524 142.808 112.756 1.00 91.80  ? 734  GLN A CA    1 
ATOM   5638 C  C     . GLN A 1 733 ? 173.832 143.438 114.107 1.00 91.80  ? 734  GLN A C     1 
ATOM   5639 O  O     . GLN A 1 733 ? 172.926 143.959 114.768 1.00 91.80  ? 734  GLN A O     1 
ATOM   5640 C  CB    . GLN A 1 733 ? 173.135 143.877 111.733 1.00 91.80  ? 734  GLN A CB    1 
ATOM   5641 C  CG    . GLN A 1 733 ? 172.594 143.303 110.433 1.00 91.80  ? 734  GLN A CG    1 
ATOM   5642 C  CD    . GLN A 1 733 ? 172.413 144.353 109.358 1.00 91.80  ? 734  GLN A CD    1 
ATOM   5643 O  OE1   . GLN A 1 733 ? 172.643 145.540 109.587 1.00 91.80  ? 734  GLN A OE1   1 
ATOM   5644 N  NE2   . GLN A 1 733 ? 171.994 143.921 108.175 1.00 91.80  ? 734  GLN A NE2   1 
ATOM   5645 N  N     . PHE A 1 734 ? 175.096 143.372 114.520 1.00 90.92  ? 735  PHE A N     1 
ATOM   5646 C  CA    . PHE A 1 734 ? 175.470 143.780 115.869 1.00 90.92  ? 735  PHE A CA    1 
ATOM   5647 C  C     . PHE A 1 734 ? 175.369 145.290 116.057 1.00 90.92  ? 735  PHE A C     1 
ATOM   5648 O  O     . PHE A 1 734 ? 175.784 146.072 115.197 1.00 90.92  ? 735  PHE A O     1 
ATOM   5649 C  CB    . PHE A 1 734 ? 176.884 143.310 116.209 1.00 90.92  ? 735  PHE A CB    1 
ATOM   5650 C  CG    . PHE A 1 734 ? 177.307 143.648 117.615 1.00 90.92  ? 735  PHE A CG    1 
ATOM   5651 C  CD1   . PHE A 1 734 ? 176.842 142.899 118.687 1.00 90.92  ? 735  PHE A CD1   1 
ATOM   5652 C  CD2   . PHE A 1 734 ? 178.175 144.704 117.865 1.00 90.92  ? 735  PHE A CD2   1 
ATOM   5653 C  CE1   . PHE A 1 734 ? 177.222 143.203 119.984 1.00 90.92  ? 735  PHE A CE1   1 
ATOM   5654 C  CE2   . PHE A 1 734 ? 178.560 145.012 119.159 1.00 90.92  ? 735  PHE A CE2   1 
ATOM   5655 C  CZ    . PHE A 1 734 ? 178.083 144.259 120.219 1.00 90.92  ? 735  PHE A CZ    1 
ATOM   5656 N  N     . ILE A 1 735 ? 174.819 145.690 117.204 1.00 85.05  ? 736  ILE A N     1 
ATOM   5657 C  CA    . ILE A 1 735 ? 174.885 147.069 117.671 1.00 85.05  ? 736  ILE A CA    1 
ATOM   5658 C  C     . ILE A 1 735 ? 174.892 147.025 119.196 1.00 85.05  ? 736  ILE A C     1 
ATOM   5659 O  O     . ILE A 1 735 ? 174.375 146.086 119.810 1.00 85.05  ? 736  ILE A O     1 
ATOM   5660 C  CB    . ILE A 1 735 ? 173.716 147.917 117.094 1.00 85.05  ? 736  ILE A CB    1 
ATOM   5661 C  CG1   . ILE A 1 735 ? 173.953 149.419 117.286 1.00 85.05  ? 736  ILE A CG1   1 
ATOM   5662 C  CG2   . ILE A 1 735 ? 172.369 147.493 117.674 1.00 85.05  ? 736  ILE A CG2   1 
ATOM   5663 C  CD1   . ILE A 1 735 ? 175.157 149.949 116.543 1.00 85.05  ? 736  ILE A CD1   1 
ATOM   5664 N  N     . ASP A 1 736 ? 175.560 148.008 119.802 1.00 74.72  ? 737  ASP A N     1 
ATOM   5665 C  CA    . ASP A 1 736 ? 175.444 148.249 121.235 1.00 74.72  ? 737  ASP A CA    1 
ATOM   5666 C  C     . ASP A 1 736 ? 173.995 148.531 121.621 1.00 74.72  ? 737  ASP A C     1 
ATOM   5667 O  O     . ASP A 1 736 ? 173.299 149.291 120.941 1.00 74.72  ? 737  ASP A O     1 
ATOM   5668 C  CB    . ASP A 1 736 ? 176.358 149.406 121.642 1.00 74.72  ? 737  ASP A CB    1 
ATOM   5669 C  CG    . ASP A 1 736 ? 176.091 149.903 123.047 1.00 74.72  ? 737  ASP A CG    1 
ATOM   5670 O  OD1   . ASP A 1 736 ? 175.927 149.068 123.963 1.00 74.72  ? 737  ASP A OD1   1 
ATOM   5671 O  OD2   . ASP A 1 736 ? 176.076 151.131 123.246 1.00 74.72  ? 737  ASP A OD2   1 
ATOM   5672 N  N     . SER A 1 737 ? 173.542 147.872 122.695 1.00 68.85  ? 738  SER A N     1 
ATOM   5673 C  CA    . SER A 1 737 ? 172.153 147.979 123.142 1.00 68.85  ? 738  SER A CA    1 
ATOM   5674 C  C     . SER A 1 737 ? 171.792 149.401 123.559 1.00 68.85  ? 738  SER A C     1 
ATOM   5675 O  O     . SER A 1 737 ? 170.656 149.844 123.352 1.00 68.85  ? 738  SER A O     1 
ATOM   5676 C  CB    . SER A 1 737 ? 171.901 147.010 124.297 1.00 68.85  ? 738  SER A CB    1 
ATOM   5677 O  OG    . SER A 1 737 ? 171.860 145.669 123.842 1.00 68.85  ? 738  SER A OG    1 
ATOM   5678 N  N     . ARG A 1 738 ? 172.734 150.116 124.179 1.00 64.64  ? 739  ARG A N     1 
ATOM   5679 C  CA    . ARG A 1 738 ? 172.560 151.542 124.443 1.00 64.64  ? 739  ARG A CA    1 
ATOM   5680 C  C     . ARG A 1 738 ? 172.440 152.310 123.126 1.00 64.64  ? 739  ARG A C     1 
ATOM   5681 O  O     . ARG A 1 738 ? 171.486 153.070 122.920 1.00 64.64  ? 739  ARG A O     1 
ATOM   5682 C  CB    . ARG A 1 738 ? 173.724 152.044 125.304 1.00 64.64  ? 739  ARG A CB    1 
ATOM   5683 C  CG    . ARG A 1 738 ? 174.031 153.536 125.284 1.00 64.64  ? 739  ARG A CG    1 
ATOM   5684 C  CD    . ARG A 1 738 ? 172.870 154.374 125.825 1.00 64.64  ? 739  ARG A CD    1 
ATOM   5685 N  NE    . ARG A 1 738 ? 173.118 155.800 125.652 1.00 64.64  ? 739  ARG A NE    1 
ATOM   5686 C  CZ    . ARG A 1 738 ? 173.816 156.547 126.501 1.00 64.64  ? 739  ARG A CZ    1 
ATOM   5687 N  NH1   . ARG A 1 738 ? 173.999 157.836 126.251 1.00 64.64  ? 739  ARG A NH1   1 
ATOM   5688 N  NH2   . ARG A 1 738 ? 174.332 156.009 127.596 1.00 64.64  ? 739  ARG A NH2   1 
ATOM   5689 N  N     . LYS A 1 739 ? 173.438 152.158 122.245 1.00 69.46  ? 740  LYS A N     1 
ATOM   5690 C  CA    . LYS A 1 739 ? 173.432 152.812 120.934 1.00 69.46  ? 740  LYS A CA    1 
ATOM   5691 C  C     . LYS A 1 739 ? 172.257 152.369 120.067 1.00 69.46  ? 740  LYS A C     1 
ATOM   5692 O  O     . LYS A 1 739 ? 171.771 153.148 119.239 1.00 69.46  ? 740  LYS A O     1 
ATOM   5693 C  CB    . LYS A 1 739 ? 174.744 152.514 120.194 1.00 69.46  ? 740  LYS A CB    1 
ATOM   5694 C  CG    . LYS A 1 739 ? 176.054 153.161 120.698 1.00 69.46  ? 740  LYS A CG    1 
ATOM   5695 C  CD    . LYS A 1 739 ? 175.987 154.601 121.232 1.00 69.46  ? 740  LYS A CD    1 
ATOM   5696 C  CE    . LYS A 1 739 ? 175.578 155.595 120.125 1.00 69.46  ? 740  LYS A CE    1 
ATOM   5697 N  NZ    . LYS A 1 739 ? 175.129 156.921 120.612 1.00 69.46  ? 740  LYS A NZ    1 
ATOM   5698 N  N     . GLY A 1 740 ? 171.799 151.126 120.235 1.00 68.39  ? 741  GLY A N     1 
ATOM   5699 C  CA    . GLY A 1 740 ? 170.606 150.674 119.532 1.00 68.39  ? 741  GLY A CA    1 
ATOM   5700 C  C     . GLY A 1 740 ? 169.338 151.398 119.946 1.00 68.39  ? 741  GLY A C     1 
ATOM   5701 O  O     . GLY A 1 740 ? 168.528 151.784 119.098 1.00 68.39  ? 741  GLY A O     1 
ATOM   5702 N  N     . ALA A 1 741 ? 169.129 151.553 121.255 1.00 62.62  ? 742  ALA A N     1 
ATOM   5703 C  CA    . ALA A 1 741 ? 167.998 152.328 121.757 1.00 62.62  ? 742  ALA A CA    1 
ATOM   5704 C  C     . ALA A 1 741 ? 168.059 153.789 121.329 1.00 62.62  ? 742  ALA A C     1 
ATOM   5705 O  O     . ALA A 1 741 ? 167.021 154.402 121.060 1.00 62.62  ? 742  ALA A O     1 
ATOM   5706 C  CB    . ALA A 1 741 ? 167.941 152.229 123.278 1.00 62.62  ? 742  ALA A CB    1 
ATOM   5707 N  N     . GLU A 1 742 ? 169.261 154.372 121.299 1.00 64.32  ? 743  GLU A N     1 
ATOM   5708 C  CA    . GLU A 1 742 ? 169.422 155.766 120.889 1.00 64.32  ? 743  GLU A CA    1 
ATOM   5709 C  C     . GLU A 1 742 ? 169.022 156.001 119.439 1.00 64.32  ? 743  GLU A C     1 
ATOM   5710 O  O     . GLU A 1 742 ? 168.445 157.043 119.109 1.00 64.32  ? 743  GLU A O     1 
ATOM   5711 C  CB    . GLU A 1 742 ? 170.865 156.219 121.085 1.00 64.32  ? 743  GLU A CB    1 
ATOM   5712 C  CG    . GLU A 1 742 ? 171.251 156.516 122.509 1.00 64.32  ? 743  GLU A CG    1 
ATOM   5713 C  CD    . GLU A 1 742 ? 172.722 156.827 122.629 1.00 64.32  ? 743  GLU A CD    1 
ATOM   5714 O  OE1   . GLU A 1 742 ? 173.125 157.939 122.229 1.00 64.32  ? 743  GLU A OE1   1 
ATOM   5715 O  OE2   . GLU A 1 742 ? 173.489 155.956 123.078 1.00 64.32  ? 743  GLU A OE2   1 
ATOM   5716 N  N     . LYS A 1 743 ? 169.342 155.057 118.556 1.00 64.44  ? 744  LYS A N     1 
ATOM   5717 C  CA    . LYS A 1 743 ? 168.821 155.098 117.194 1.00 64.44  ? 744  LYS A CA    1 
ATOM   5718 C  C     . LYS A 1 743 ? 167.305 154.922 117.154 1.00 64.44  ? 744  LYS A C     1 
ATOM   5719 O  O     . LYS A 1 743 ? 166.616 155.646 116.425 1.00 64.44  ? 744  LYS A O     1 
ATOM   5720 C  CB    . LYS A 1 743 ? 169.518 154.035 116.343 1.00 64.44  ? 744  LYS A CB    1 
ATOM   5721 C  CG    . LYS A 1 743 ? 170.929 154.415 115.848 1.00 64.44  ? 744  LYS A CG    1 
ATOM   5722 C  CD    . LYS A 1 743 ? 171.190 155.924 115.695 1.00 64.44  ? 744  LYS A CD    1 
ATOM   5723 C  CE    . LYS A 1 743 ? 170.673 156.498 114.375 1.00 64.44  ? 744  LYS A CE    1 
ATOM   5724 N  NZ    . LYS A 1 743 ? 171.131 157.902 114.175 1.00 64.44  ? 744  LYS A NZ    1 
ATOM   5725 N  N     . LEU A 1 744 ? 166.785 153.934 117.893 1.00 64.78  ? 745  LEU A N     1 
ATOM   5726 C  CA    . LEU A 1 744 ? 165.408 153.459 117.731 1.00 64.78  ? 745  LEU A CA    1 
ATOM   5727 C  C     . LEU A 1 744 ? 164.376 154.544 118.022 1.00 64.78  ? 745  LEU A C     1 
ATOM   5728 O  O     . LEU A 1 744 ? 163.487 154.801 117.203 1.00 64.78  ? 745  LEU A O     1 
ATOM   5729 C  CB    . LEU A 1 744 ? 165.168 152.230 118.615 1.00 64.78  ? 745  LEU A CB    1 
ATOM   5730 C  CG    . LEU A 1 744 ? 163.829 151.489 118.487 1.00 64.78  ? 745  LEU A CG    1 
ATOM   5731 C  CD1   . LEU A 1 744 ? 164.048 149.998 118.543 1.00 64.78  ? 745  LEU A CD1   1 
ATOM   5732 C  CD2   . LEU A 1 744 ? 162.869 151.868 119.598 1.00 64.78  ? 745  LEU A CD2   1 
ATOM   5733 N  N     . LEU A 1 745 ? 164.450 155.148 119.212 1.00 57.44  ? 746  LEU A N     1 
ATOM   5734 C  CA    . LEU A 1 745 ? 163.478 156.157 119.631 1.00 57.44  ? 746  LEU A CA    1 
ATOM   5735 C  C     . LEU A 1 745 ? 163.447 157.378 118.720 1.00 57.44  ? 746  LEU A C     1 
ATOM   5736 O  O     . LEU A 1 745 ? 162.383 157.983 118.547 1.00 57.44  ? 746  LEU A O     1 
ATOM   5737 C  CB    . LEU A 1 745 ? 163.768 156.597 121.063 1.00 57.44  ? 746  LEU A CB    1 
ATOM   5738 C  CG    . LEU A 1 745 ? 163.303 155.638 122.153 1.00 57.44  ? 746  LEU A CG    1 
ATOM   5739 C  CD1   . LEU A 1 745 ? 163.969 155.968 123.472 1.00 57.44  ? 746  LEU A CD1   1 
ATOM   5740 C  CD2   . LEU A 1 745 ? 161.804 155.649 122.287 1.00 57.44  ? 746  LEU A CD2   1 
ATOM   5741 N  N     . SER A 1 746 ? 164.601 157.775 118.169 1.00 63.54  ? 747  SER A N     1 
ATOM   5742 C  CA    . SER A 1 746 ? 164.651 158.864 117.192 1.00 63.54  ? 747  SER A CA    1 
ATOM   5743 C  C     . SER A 1 746 ? 163.785 158.600 115.964 1.00 63.54  ? 747  SER A C     1 
ATOM   5744 O  O     . SER A 1 746 ? 163.243 159.541 115.375 1.00 63.54  ? 747  SER A O     1 
ATOM   5745 C  CB    . SER A 1 746 ? 166.096 159.110 116.763 1.00 63.54  ? 747  SER A CB    1 
ATOM   5746 O  OG    . SER A 1 746 ? 166.624 157.973 116.107 1.00 63.54  ? 747  SER A OG    1 
ATOM   5747 N  N     . SER A 1 747 ? 163.641 157.339 115.565 1.00 64.98  ? 748  SER A N     1 
ATOM   5748 C  CA    . SER A 1 747 ? 162.827 156.982 114.412 1.00 64.98  ? 748  SER A CA    1 
ATOM   5749 C  C     . SER A 1 747 ? 161.344 156.829 114.729 1.00 64.98  ? 748  SER A C     1 
ATOM   5750 O  O     . SER A 1 747 ? 160.548 156.678 113.796 1.00 64.98  ? 748  SER A O     1 
ATOM   5751 C  CB    . SER A 1 747 ? 163.348 155.686 113.788 1.00 64.98  ? 748  SER A CB    1 
ATOM   5752 O  OG    . SER A 1 747 ? 162.878 154.555 114.496 1.00 64.98  ? 748  SER A OG    1 
ATOM   5753 N  N     . LEU A 1 748 ? 160.945 156.862 116.000 1.00 63.33  ? 749  LEU A N     1 
ATOM   5754 C  CA    . LEU A 1 748 ? 159.566 156.581 116.374 1.00 63.33  ? 749  LEU A CA    1 
ATOM   5755 C  C     . LEU A 1 748 ? 158.655 157.808 116.395 1.00 63.33  ? 749  LEU A C     1 
ATOM   5756 O  O     . LEU A 1 748 ? 157.555 157.709 116.951 1.00 63.33  ? 749  LEU A O     1 
ATOM   5757 C  CB    . LEU A 1 748 ? 159.523 155.880 117.733 1.00 63.33  ? 749  LEU A CB    1 
ATOM   5758 C  CG    . LEU A 1 748 ? 160.015 154.430 117.768 1.00 63.33  ? 749  LEU A CG    1 
ATOM   5759 C  CD1   . LEU A 1 748 ? 159.692 153.799 119.106 1.00 63.33  ? 749  LEU A CD1   1 
ATOM   5760 C  CD2   . LEU A 1 748 ? 159.423 153.607 116.636 1.00 63.33  ? 749  LEU A CD2   1 
ATOM   5761 N  N     . ASP A 1 749 ? 159.054 158.906 115.736 1.00 63.13  ? 750  ASP A N     1 
ATOM   5762 C  CA    . ASP A 1 749 ? 158.315 160.189 115.596 1.00 63.13  ? 750  ASP A CA    1 
ATOM   5763 C  C     . ASP A 1 749 ? 157.606 160.647 116.878 1.00 63.13  ? 750  ASP A C     1 
ATOM   5764 O  O     . ASP A 1 749 ? 156.449 161.073 116.872 1.00 63.13  ? 750  ASP A O     1 
ATOM   5765 C  CB    . ASP A 1 749 ? 157.337 160.180 114.404 1.00 63.13  ? 750  ASP A CB    1 
ATOM   5766 C  CG    . ASP A 1 749 ? 156.253 159.109 114.488 1.00 63.13  ? 750  ASP A CG    1 
ATOM   5767 O  OD1   . ASP A 1 749 ? 155.076 159.487 114.666 1.00 63.13  ? 750  ASP A OD1   1 
ATOM   5768 O  OD2   . ASP A 1 749 ? 156.537 157.917 114.254 1.00 63.13  ? 750  ASP A OD2   1 
ATOM   5769 N  N     . ILE A 1 750 ? 158.332 160.574 117.988 1.00 55.93  ? 751  ILE A N     1 
ATOM   5770 C  CA    . ILE A 1 750 ? 157.843 160.948 119.308 1.00 55.93  ? 751  ILE A CA    1 
ATOM   5771 C  C     . ILE A 1 750 ? 158.766 162.024 119.855 1.00 55.93  ? 751  ILE A C     1 
ATOM   5772 O  O     . ILE A 1 750 ? 159.917 162.151 119.426 1.00 55.93  ? 751  ILE A O     1 
ATOM   5773 C  CB    . ILE A 1 750 ? 157.730 159.757 120.283 1.00 55.93  ? 751  ILE A CB    1 
ATOM   5774 C  CG1   . ILE A 1 750 ? 159.045 158.993 120.377 1.00 55.93  ? 751  ILE A CG1   1 
ATOM   5775 C  CG2   . ILE A 1 750 ? 156.593 158.845 119.878 1.00 55.93  ? 751  ILE A CG2   1 
ATOM   5776 C  CD1   . ILE A 1 750 ? 159.008 157.908 121.413 1.00 55.93  ? 751  ILE A CD1   1 
ATOM   5777 N  N     . ASP A 1 751 ? 158.239 162.828 120.777 1.00 48.38  ? 752  ASP A N     1 
ATOM   5778 C  CA    . ASP A 1 751 ? 158.924 164.023 121.262 1.00 48.38  ? 752  ASP A CA    1 
ATOM   5779 C  C     . ASP A 1 751 ? 160.122 163.618 122.115 1.00 48.38  ? 752  ASP A C     1 
ATOM   5780 O  O     . ASP A 1 751 ? 159.969 163.084 123.216 1.00 48.38  ? 752  ASP A O     1 
ATOM   5781 C  CB    . ASP A 1 751 ? 157.943 164.882 122.057 1.00 48.38  ? 752  ASP A CB    1 
ATOM   5782 C  CG    . ASP A 1 751 ? 158.567 166.159 122.629 1.00 48.38  ? 752  ASP A CG    1 
ATOM   5783 O  OD1   . ASP A 1 751 ? 159.677 166.571 122.226 1.00 48.38  ? 752  ASP A OD1   1 
ATOM   5784 O  OD2   . ASP A 1 751 ? 157.926 166.763 123.513 1.00 48.38  ? 752  ASP A OD2   1 
ATOM   5785 N  N     . HIS A 1 752 ? 161.318 163.874 121.575 1.00 50.38  ? 753  HIS A N     1 
ATOM   5786 C  CA    . HIS A 1 752 ? 162.618 163.597 122.185 1.00 50.38  ? 753  HIS A CA    1 
ATOM   5787 C  C     . HIS A 1 752 ? 162.897 164.379 123.467 1.00 50.38  ? 753  HIS A C     1 
ATOM   5788 O  O     . HIS A 1 752 ? 163.940 164.148 124.088 1.00 50.38  ? 753  HIS A O     1 
ATOM   5789 C  CB    . HIS A 1 752 ? 163.715 163.871 121.160 1.00 50.38  ? 753  HIS A CB    1 
ATOM   5790 C  CG    . HIS A 1 752 ? 163.523 163.140 119.869 1.00 50.38  ? 753  HIS A CG    1 
ATOM   5791 N  ND1   . HIS A 1 752 ? 163.949 163.640 118.657 1.00 50.38  ? 753  HIS A ND1   1 
ATOM   5792 C  CD2   . HIS A 1 752 ? 162.972 161.933 119.604 1.00 50.38  ? 753  HIS A CD2   1 
ATOM   5793 C  CE1   . HIS A 1 752 ? 163.651 162.780 117.699 1.00 50.38  ? 753  HIS A CE1   1 
ATOM   5794 N  NE2   . HIS A 1 752 ? 163.057 161.736 118.247 1.00 50.38  ? 753  HIS A NE2   1 
ATOM   5795 N  N     . ASN A 1 753 ? 162.027 165.305 123.868 1.00 47.03  ? 754  ASN A N     1 
ATOM   5796 C  CA    . ASN A 1 753 ? 162.164 165.939 125.171 1.00 47.03  ? 754  ASN A CA    1 
ATOM   5797 C  C     . ASN A 1 753 ? 161.545 165.104 126.282 1.00 47.03  ? 754  ASN A C     1 
ATOM   5798 O  O     . ASN A 1 753 ? 161.819 165.362 127.458 1.00 47.03  ? 754  ASN A O     1 
ATOM   5799 C  CB    . ASN A 1 753 ? 161.534 167.331 125.155 1.00 47.03  ? 754  ASN A CB    1 
ATOM   5800 C  CG    . ASN A 1 753 ? 162.163 168.240 124.123 1.00 47.03  ? 754  ASN A CG    1 
ATOM   5801 O  OD1   . ASN A 1 753 ? 162.348 167.854 122.970 1.00 47.03  ? 754  ASN A OD1   1 
ATOM   5802 N  ND2   . ASN A 1 753 ? 162.500 169.457 124.534 1.00 47.03  ? 754  ASN A ND2   1 
ATOM   5803 N  N     . GLN A 1 754 ? 160.710 164.126 125.938 1.00 42.90  ? 755  GLN A N     1 
ATOM   5804 C  CA    . GLN A 1 754 ? 159.976 163.338 126.915 1.00 42.90  ? 755  GLN A CA    1 
ATOM   5805 C  C     . GLN A 1 754 ? 160.774 162.160 127.453 1.00 42.90  ? 755  GLN A C     1 
ATOM   5806 O  O     . GLN A 1 754 ? 160.308 161.496 128.380 1.00 42.90  ? 755  GLN A O     1 
ATOM   5807 C  CB    . GLN A 1 754 ? 158.672 162.813 126.311 1.00 42.90  ? 755  GLN A CB    1 
ATOM   5808 C  CG    . GLN A 1 754 ? 157.740 163.878 125.754 1.00 42.90  ? 755  GLN A CG    1 
ATOM   5809 C  CD    . GLN A 1 754 ? 157.193 164.807 126.818 1.00 42.90  ? 755  GLN A CD    1 
ATOM   5810 O  OE1   . GLN A 1 754 ? 156.837 164.372 127.912 1.00 42.90  ? 755  GLN A OE1   1 
ATOM   5811 N  NE2   . GLN A 1 754 ? 157.124 166.094 126.502 1.00 42.90  ? 755  GLN A NE2   1 
ATOM   5812 N  N     . TYR A 1 755 ? 161.940 161.857 126.893 1.00 43.91  ? 756  TYR A N     1 
ATOM   5813 C  CA    . TYR A 1 755 ? 162.730 160.746 127.394 1.00 43.91  ? 756  TYR A CA    1 
ATOM   5814 C  C     . TYR A 1 755 ? 164.175 161.185 127.579 1.00 43.91  ? 756  TYR A C     1 
ATOM   5815 O  O     . TYR A 1 755 ? 164.632 162.161 126.981 1.00 43.91  ? 756  TYR A O     1 
ATOM   5816 C  CB    . TYR A 1 755 ? 162.621 159.509 126.484 1.00 43.91  ? 756  TYR A CB    1 
ATOM   5817 C  CG    . TYR A 1 755 ? 163.178 159.622 125.084 1.00 43.91  ? 756  TYR A CG    1 
ATOM   5818 C  CD1   . TYR A 1 755 ? 164.515 159.371 124.816 1.00 43.91  ? 756  TYR A CD1   1 
ATOM   5819 C  CD2   . TYR A 1 755 ? 162.356 159.956 124.024 1.00 43.91  ? 756  TYR A CD2   1 
ATOM   5820 C  CE1   . TYR A 1 755 ? 165.014 159.465 123.540 1.00 43.91  ? 756  TYR A CE1   1 
ATOM   5821 C  CE2   . TYR A 1 755 ? 162.852 160.049 122.740 1.00 43.91  ? 756  TYR A CE2   1 
ATOM   5822 C  CZ    . TYR A 1 755 ? 164.182 159.803 122.507 1.00 43.91  ? 756  TYR A CZ    1 
ATOM   5823 O  OH    . TYR A 1 755 ? 164.691 159.898 121.235 1.00 43.91  ? 756  TYR A OH    1 
ATOM   5824 N  N     . LYS A 1 756 ? 164.892 160.450 128.427 1.00 36.03  ? 757  LYS A N     1 
ATOM   5825 C  CA    . LYS A 1 756 ? 166.297 160.714 128.689 1.00 36.03  ? 757  LYS A CA    1 
ATOM   5826 C  C     . LYS A 1 756 ? 167.070 159.408 128.754 1.00 36.03  ? 757  LYS A C     1 
ATOM   5827 O  O     . LYS A 1 756 ? 166.537 158.370 129.151 1.00 36.03  ? 757  LYS A O     1 
ATOM   5828 C  CB    . LYS A 1 756 ? 166.494 161.495 129.990 1.00 36.03  ? 757  LYS A CB    1 
ATOM   5829 C  CG    . LYS A 1 756 ? 166.122 162.959 129.902 1.00 36.03  ? 757  LYS A CG    1 
ATOM   5830 C  CD    . LYS A 1 756 ? 167.130 163.723 129.079 1.00 36.03  ? 757  LYS A CD    1 
ATOM   5831 C  CE    . LYS A 1 756 ? 166.793 165.198 129.039 1.00 36.03  ? 757  LYS A CE    1 
ATOM   5832 N  NZ    . LYS A 1 756 ? 165.686 165.472 128.086 1.00 36.03  ? 757  LYS A NZ    1 
ATOM   5833 N  N     . PHE A 1 757 ? 168.335 159.477 128.357 1.00 43.65  ? 758  PHE A N     1 
ATOM   5834 C  CA    . PHE A 1 757 ? 169.252 158.348 128.409 1.00 43.65  ? 758  PHE A CA    1 
ATOM   5835 C  C     . PHE A 1 757 ? 170.171 158.451 129.619 1.00 43.65  ? 758  PHE A C     1 
ATOM   5836 O  O     . PHE A 1 757 ? 170.971 159.386 129.720 1.00 43.65  ? 758  PHE A O     1 
ATOM   5837 C  CB    . PHE A 1 757 ? 170.076 158.277 127.129 1.00 43.65  ? 758  PHE A CB    1 
ATOM   5838 C  CG    . PHE A 1 757 ? 169.268 157.978 125.913 1.00 43.65  ? 758  PHE A CG    1 
ATOM   5839 C  CD1   . PHE A 1 757 ? 168.500 156.830 125.855 1.00 43.65  ? 758  PHE A CD1   1 
ATOM   5840 C  CD2   . PHE A 1 757 ? 169.262 158.845 124.836 1.00 43.65  ? 758  PHE A CD2   1 
ATOM   5841 C  CE1   . PHE A 1 757 ? 167.754 156.539 124.742 1.00 43.65  ? 758  PHE A CE1   1 
ATOM   5842 C  CE2   . PHE A 1 757 ? 168.512 158.563 123.718 1.00 43.65  ? 758  PHE A CE2   1 
ATOM   5843 C  CZ    . PHE A 1 757 ? 167.762 157.403 123.672 1.00 43.65  ? 758  PHE A CZ    1 
ATOM   5844 N  N     . GLY A 1 758 ? 170.058 157.483 130.526 1.00 44.06  ? 759  GLY A N     1 
ATOM   5845 C  CA    . GLY A 1 758 ? 171.003 157.327 131.609 1.00 44.06  ? 759  GLY A CA    1 
ATOM   5846 C  C     . GLY A 1 758 ? 172.105 156.351 131.242 1.00 44.06  ? 759  GLY A C     1 
ATOM   5847 O  O     . GLY A 1 758 ? 172.178 155.848 130.122 1.00 44.06  ? 759  GLY A O     1 
ATOM   5848 N  N     . HIS A 1 759 ? 173.008 156.129 132.203 1.00 44.56  ? 760  HIS A N     1 
ATOM   5849 C  CA    . HIS A 1 759 ? 174.109 155.192 131.990 1.00 44.56  ? 760  HIS A CA    1 
ATOM   5850 C  C     . HIS A 1 759 ? 173.602 153.764 131.815 1.00 44.56  ? 760  HIS A C     1 
ATOM   5851 O  O     . HIS A 1 759 ? 174.011 153.060 130.887 1.00 44.56  ? 760  HIS A O     1 
ATOM   5852 C  CB    . HIS A 1 759 ? 175.102 155.264 133.151 1.00 44.56  ? 760  HIS A CB    1 
ATOM   5853 C  CG    . HIS A 1 759 ? 175.745 156.605 133.330 1.00 44.56  ? 760  HIS A CG    1 
ATOM   5854 N  ND1   . HIS A 1 759 ? 176.605 156.878 134.371 1.00 44.56  ? 760  HIS A ND1   1 
ATOM   5855 C  CD2   . HIS A 1 759 ? 175.681 157.737 132.590 1.00 44.56  ? 760  HIS A CD2   1 
ATOM   5856 C  CE1   . HIS A 1 759 ? 177.027 158.126 134.276 1.00 44.56  ? 760  HIS A CE1   1 
ATOM   5857 N  NE2   . HIS A 1 759 ? 176.481 158.669 133.204 1.00 44.56  ? 760  HIS A NE2   1 
ATOM   5858 N  N     . THR A 1 760 ? 172.709 153.318 132.699 1.00 46.72  ? 761  THR A N     1 
ATOM   5859 C  CA    . THR A 1 760 ? 172.236 151.941 132.676 1.00 46.72  ? 761  THR A CA    1 
ATOM   5860 C  C     . THR A 1 760 ? 170.822 151.789 132.139 1.00 46.72  ? 761  THR A C     1 
ATOM   5861 O  O     . THR A 1 760 ? 170.460 150.691 131.710 1.00 46.72  ? 761  THR A O     1 
ATOM   5862 C  CB    . THR A 1 760 ? 172.303 151.315 134.076 1.00 46.72  ? 761  THR A CB    1 
ATOM   5863 O  OG1   . THR A 1 760 ? 171.449 152.036 134.966 1.00 46.72  ? 761  THR A OG1   1 
ATOM   5864 C  CG2   . THR A 1 760 ? 173.722 151.367 134.605 1.00 46.72  ? 761  THR A CG2   1 
ATOM   5865 N  N     . LYS A 1 761 ? 170.017 152.847 132.162 1.00 44.10  ? 762  LYS A N     1 
ATOM   5866 C  CA    . LYS A 1 761 ? 168.584 152.756 131.934 1.00 44.10  ? 762  LYS A CA    1 
ATOM   5867 C  C     . LYS A 1 761 ? 168.171 153.916 131.048 1.00 44.10  ? 762  LYS A C     1 
ATOM   5868 O  O     . LYS A 1 761 ? 168.805 154.971 131.052 1.00 44.10  ? 762  LYS A O     1 
ATOM   5869 C  CB    . LYS A 1 761 ? 167.784 152.837 133.238 1.00 44.10  ? 762  LYS A CB    1 
ATOM   5870 C  CG    . LYS A 1 761 ? 167.940 151.682 134.195 1.00 44.10  ? 762  LYS A CG    1 
ATOM   5871 C  CD    . LYS A 1 761 ? 167.110 151.941 135.439 1.00 44.10  ? 762  LYS A CD    1 
ATOM   5872 C  CE    . LYS A 1 761 ? 167.317 150.872 136.487 1.00 44.10  ? 762  LYS A CE    1 
ATOM   5873 N  NZ    . LYS A 1 761 ? 166.408 151.073 137.645 1.00 44.10  ? 762  LYS A NZ    1 
ATOM   5874 N  N     . VAL A 1 762 ? 167.102 153.727 130.309 1.00 39.80  ? 763  VAL A N     1 
ATOM   5875 C  CA    . VAL A 1 762 ? 166.383 154.838 129.701 1.00 39.80  ? 763  VAL A CA    1 
ATOM   5876 C  C     . VAL A 1 762 ? 165.301 155.311 130.667 1.00 39.80  ? 763  VAL A C     1 
ATOM   5877 O  O     . VAL A 1 762 ? 164.747 154.517 131.434 1.00 39.80  ? 763  VAL A O     1 
ATOM   5878 C  CB    . VAL A 1 762 ? 165.832 154.430 128.316 1.00 39.80  ? 763  VAL A CB    1 
ATOM   5879 C  CG1   . VAL A 1 762 ? 164.731 153.392 128.407 1.00 39.80  ? 763  VAL A CG1   1 
ATOM   5880 C  CG2   . VAL A 1 762 ? 165.417 155.636 127.508 1.00 39.80  ? 763  VAL A CG2   1 
ATOM   5881 N  N     . PHE A 1 763 ? 165.049 156.618 130.689 1.00 37.72  ? 764  PHE A N     1 
ATOM   5882 C  CA    . PHE A 1 763 ? 164.094 157.236 131.601 1.00 37.72  ? 764  PHE A CA    1 
ATOM   5883 C  C     . PHE A 1 763 ? 163.024 157.960 130.801 1.00 37.72  ? 764  PHE A C     1 
ATOM   5884 O  O     . PHE A 1 763 ? 163.335 158.648 129.830 1.00 37.72  ? 764  PHE A O     1 
ATOM   5885 C  CB    . PHE A 1 763 ? 164.763 158.246 132.533 1.00 37.72  ? 764  PHE A CB    1 
ATOM   5886 C  CG    . PHE A 1 763 ? 165.584 157.634 133.621 1.00 37.72  ? 764  PHE A CG    1 
ATOM   5887 C  CD1   . PHE A 1 763 ? 166.823 157.078 133.351 1.00 37.72  ? 764  PHE A CD1   1 
ATOM   5888 C  CD2   . PHE A 1 763 ? 165.125 157.635 134.922 1.00 37.72  ? 764  PHE A CD2   1 
ATOM   5889 C  CE1   . PHE A 1 763 ? 167.583 156.523 134.357 1.00 37.72  ? 764  PHE A CE1   1 
ATOM   5890 C  CE2   . PHE A 1 763 ? 165.878 157.084 135.930 1.00 37.72  ? 764  PHE A CE2   1 
ATOM   5891 C  CZ    . PHE A 1 763 ? 167.108 156.524 135.646 1.00 37.72  ? 764  PHE A CZ    1 
ATOM   5892 N  N     . PHE A 1 764 ? 161.768 157.822 131.216 1.00 35.48  ? 765  PHE A N     1 
ATOM   5893 C  CA    . PHE A 1 764 ? 160.633 158.367 130.484 1.00 35.48  ? 765  PHE A CA    1 
ATOM   5894 C  C     . PHE A 1 764 ? 159.823 159.306 131.357 1.00 35.48  ? 765  PHE A C     1 
ATOM   5895 O  O     . PHE A 1 764 ? 159.645 159.057 132.548 1.00 35.48  ? 765  PHE A O     1 
ATOM   5896 C  CB    . PHE A 1 764 ? 159.683 157.275 129.990 1.00 35.48  ? 765  PHE A CB    1 
ATOM   5897 C  CG    . PHE A 1 764 ? 160.305 156.269 129.078 1.00 35.48  ? 765  PHE A CG    1 
ATOM   5898 C  CD1   . PHE A 1 764 ? 161.310 156.621 128.209 1.00 35.48  ? 765  PHE A CD1   1 
ATOM   5899 C  CD2   . PHE A 1 764 ? 159.847 154.968 129.070 1.00 35.48  ? 765  PHE A CD2   1 
ATOM   5900 C  CE1   . PHE A 1 764 ? 161.859 155.698 127.368 1.00 35.48  ? 765  PHE A CE1   1 
ATOM   5901 C  CE2   . PHE A 1 764 ? 160.396 154.040 128.232 1.00 35.48  ? 765  PHE A CE2   1 
ATOM   5902 C  CZ    . PHE A 1 764 ? 161.406 154.407 127.379 1.00 35.48  ? 765  PHE A CZ    1 
ATOM   5903 N  N     . LYS A 1 765 ? 159.297 160.364 130.744 1.00 38.23  ? 766  LYS A N     1 
ATOM   5904 C  CA    . LYS A 1 765 ? 158.262 161.187 131.359 1.00 38.23  ? 766  LYS A CA    1 
ATOM   5905 C  C     . LYS A 1 765 ? 156.963 160.401 131.545 1.00 38.23  ? 766  LYS A C     1 
ATOM   5906 O  O     . LYS A 1 765 ? 156.814 159.265 131.084 1.00 38.23  ? 766  LYS A O     1 
ATOM   5907 C  CB    . LYS A 1 765 ? 157.984 162.441 130.531 1.00 38.23  ? 766  LYS A CB    1 
ATOM   5908 C  CG    . LYS A 1 765 ? 159.043 163.531 130.593 1.00 38.23  ? 766  LYS A CG    1 
ATOM   5909 C  CD    . LYS A 1 765 ? 158.916 164.371 131.849 1.00 38.23  ? 766  LYS A CD    1 
ATOM   5910 C  CE    . LYS A 1 765 ? 159.840 165.571 131.776 1.00 38.23  ? 766  LYS A CE    1 
ATOM   5911 N  NZ    . LYS A 1 765 ? 159.615 166.533 132.884 1.00 38.23  ? 766  LYS A NZ    1 
ATOM   5912 N  N     . ALA A 1 766 ? 156.034 161.050 132.262 1.00 42.74  ? 767  ALA A N     1 
ATOM   5913 C  CA    . ALA A 1 766 ? 154.835 160.424 132.825 1.00 42.74  ? 767  ALA A CA    1 
ATOM   5914 C  C     . ALA A 1 766 ? 153.995 159.677 131.793 1.00 42.74  ? 767  ALA A C     1 
ATOM   5915 O  O     . ALA A 1 766 ? 153.620 158.518 132.001 1.00 42.74  ? 767  ALA A O     1 
ATOM   5916 C  CB    . ALA A 1 766 ? 153.986 161.491 133.513 1.00 42.74  ? 767  ALA A CB    1 
ATOM   5917 N  N     . GLY A 1 767 ? 153.689 160.326 130.676 1.00 48.25  ? 768  GLY A N     1 
ATOM   5918 C  CA    . GLY A 1 767 ? 152.766 159.749 129.719 1.00 48.25  ? 768  GLY A CA    1 
ATOM   5919 C  C     . GLY A 1 767 ? 153.397 158.899 128.637 1.00 48.25  ? 768  GLY A C     1 
ATOM   5920 O  O     . GLY A 1 767 ? 152.689 158.157 127.951 1.00 48.25  ? 768  GLY A O     1 
ATOM   5921 N  N     . LEU A 1 768 ? 154.717 159.016 128.460 1.00 50.47  ? 769  LEU A N     1 
ATOM   5922 C  CA    . LEU A 1 768 ? 155.362 158.464 127.273 1.00 50.47  ? 769  LEU A CA    1 
ATOM   5923 C  C     . LEU A 1 768 ? 155.389 156.941 127.274 1.00 50.47  ? 769  LEU A C     1 
ATOM   5924 O  O     . LEU A 1 768 ? 155.373 156.334 126.198 1.00 50.47  ? 769  LEU A O     1 
ATOM   5925 C  CB    . LEU A 1 768 ? 156.777 159.012 127.132 1.00 50.47  ? 769  LEU A CB    1 
ATOM   5926 C  CG    . LEU A 1 768 ? 157.298 158.943 125.699 1.00 50.47  ? 769  LEU A CG    1 
ATOM   5927 C  CD1   . LEU A 1 768 ? 156.698 160.061 124.884 1.00 50.47  ? 769  LEU A CD1   1 
ATOM   5928 C  CD2   . LEU A 1 768 ? 158.808 159.004 125.666 1.00 50.47  ? 769  LEU A CD2   1 
ATOM   5929 N  N     . LEU A 1 769 ? 155.481 156.312 128.451 1.00 52.35  ? 770  LEU A N     1 
ATOM   5930 C  CA    . LEU A 1 769 ? 155.399 154.854 128.524 1.00 52.35  ? 770  LEU A CA    1 
ATOM   5931 C  C     . LEU A 1 769 ? 154.058 154.341 128.009 1.00 52.35  ? 770  LEU A C     1 
ATOM   5932 O  O     . LEU A 1 769 ? 153.998 153.301 127.342 1.00 52.35  ? 770  LEU A O     1 
ATOM   5933 C  CB    . LEU A 1 769 ? 155.637 154.381 129.956 1.00 52.35  ? 770  LEU A CB    1 
ATOM   5934 C  CG    . LEU A 1 769 ? 155.791 152.866 130.104 1.00 52.35  ? 770  LEU A CG    1 
ATOM   5935 C  CD1   . LEU A 1 769 ? 157.190 152.438 129.707 1.00 52.35  ? 770  LEU A CD1   1 
ATOM   5936 C  CD2   . LEU A 1 769 ? 155.461 152.414 131.519 1.00 52.35  ? 770  LEU A CD2   1 
ATOM   5937 N  N     . GLY A 1 770 ? 152.974 155.051 128.327 1.00 59.66  ? 771  GLY A N     1 
ATOM   5938 C  CA    . GLY A 1 770 ? 151.677 154.722 127.757 1.00 59.66  ? 771  GLY A CA    1 
ATOM   5939 C  C     . GLY A 1 770 ? 151.636 154.863 126.247 1.00 59.66  ? 771  GLY A C     1 
ATOM   5940 O  O     . GLY A 1 770 ? 151.022 154.047 125.556 1.00 59.66  ? 771  GLY A O     1 
ATOM   5941 N  N     . LEU A 1 771 ? 152.259 155.926 125.725 1.00 59.52  ? 772  LEU A N     1 
ATOM   5942 C  CA    . LEU A 1 771 ? 152.341 156.152 124.283 1.00 59.52  ? 772  LEU A CA    1 
ATOM   5943 C  C     . LEU A 1 771 ? 153.054 155.019 123.557 1.00 59.52  ? 772  LEU A C     1 
ATOM   5944 O  O     . LEU A 1 771 ? 152.634 154.619 122.466 1.00 59.52  ? 772  LEU A O     1 
ATOM   5945 C  CB    . LEU A 1 771 ? 153.035 157.483 124.009 1.00 59.52  ? 772  LEU A CB    1 
ATOM   5946 C  CG    . LEU A 1 771 ? 153.165 157.908 122.549 1.00 59.52  ? 772  LEU A CG    1 
ATOM   5947 C  CD1   . LEU A 1 771 ? 151.797 158.038 121.923 1.00 59.52  ? 772  LEU A CD1   1 
ATOM   5948 C  CD2   . LEU A 1 771 ? 153.910 159.224 122.461 1.00 59.52  ? 772  LEU A CD2   1 
ATOM   5949 N  N     . LEU A 1 772 ? 154.140 154.498 124.133 1.00 59.96  ? 773  LEU A N     1 
ATOM   5950 C  CA    . LEU A 1 772 ? 154.808 153.344 123.536 1.00 59.96  ? 773  LEU A CA    1 
ATOM   5951 C  C     . LEU A 1 772 ? 153.941 152.091 123.581 1.00 59.96  ? 773  LEU A C     1 
ATOM   5952 O  O     . LEU A 1 772 ? 153.915 151.325 122.611 1.00 59.96  ? 773  LEU A O     1 
ATOM   5953 C  CB    . LEU A 1 772 ? 156.152 153.084 124.212 1.00 59.96  ? 773  LEU A CB    1 
ATOM   5954 C  CG    . LEU A 1 772 ? 157.231 154.159 124.102 1.00 59.96  ? 773  LEU A CG    1 
ATOM   5955 C  CD1   . LEU A 1 772 ? 158.550 153.606 124.602 1.00 59.96  ? 773  LEU A CD1   1 
ATOM   5956 C  CD2   . LEU A 1 772 ? 157.364 154.656 122.680 1.00 59.96  ? 773  LEU A CD2   1 
ATOM   5957 N  N     . GLU A 1 773 ? 153.261 151.846 124.707 1.00 67.00  ? 774  GLU A N     1 
ATOM   5958 C  CA    . GLU A 1 773 ? 152.378 150.685 124.827 1.00 67.00  ? 774  GLU A CA    1 
ATOM   5959 C  C     . GLU A 1 773 ? 151.227 150.734 123.827 1.00 67.00  ? 774  GLU A C     1 
ATOM   5960 O  O     . GLU A 1 773 ? 150.883 149.713 123.221 1.00 67.00  ? 774  GLU A O     1 
ATOM   5961 C  CB    . GLU A 1 773 ? 151.831 150.586 126.251 1.00 67.00  ? 774  GLU A CB    1 
ATOM   5962 C  CG    . GLU A 1 773 ? 152.856 150.180 127.286 1.00 67.00  ? 774  GLU A CG    1 
ATOM   5963 C  CD    . GLU A 1 773 ? 153.407 148.795 127.040 1.00 67.00  ? 774  GLU A CD    1 
ATOM   5964 O  OE1   . GLU A 1 773 ? 154.595 148.686 126.674 1.00 67.00  ? 774  GLU A OE1   1 
ATOM   5965 O  OE2   . GLU A 1 773 ? 152.652 147.816 127.209 1.00 67.00  ? 774  GLU A OE2   1 
ATOM   5966 N  N     . GLU A 1 774 ? 150.606 151.908 123.666 1.00 69.46  ? 775  GLU A N     1 
ATOM   5967 C  CA    . GLU A 1 774 ? 149.542 152.078 122.678 1.00 69.46  ? 775  GLU A CA    1 
ATOM   5968 C  C     . GLU A 1 774 ? 150.053 151.868 121.258 1.00 69.46  ? 775  GLU A C     1 
ATOM   5969 O  O     . GLU A 1 774 ? 149.367 151.265 120.427 1.00 69.46  ? 775  GLU A O     1 
ATOM   5970 C  CB    . GLU A 1 774 ? 148.916 153.464 122.811 1.00 69.46  ? 775  GLU A CB    1 
ATOM   5971 C  CG    . GLU A 1 774 ? 148.118 153.678 124.077 1.00 69.46  ? 775  GLU A CG    1 
ATOM   5972 C  CD    . GLU A 1 774 ? 147.869 155.146 124.349 1.00 69.46  ? 775  GLU A CD    1 
ATOM   5973 O  OE1   . GLU A 1 774 ? 148.580 155.723 125.198 1.00 69.46  ? 775  GLU A OE1   1 
ATOM   5974 O  OE2   . GLU A 1 774 ? 146.969 155.728 123.708 1.00 69.46  ? 775  GLU A OE2   1 
ATOM   5975 N  N     . MET A 1 775 ? 151.227 152.412 120.943 1.00 68.88  ? 776  MET A N     1 
ATOM   5976 C  CA    . MET A 1 775 ? 151.821 152.180 119.632 1.00 68.88  ? 776  MET A CA    1 
ATOM   5977 C  C     . MET A 1 775 ? 152.224 150.722 119.430 1.00 68.88  ? 776  MET A C     1 
ATOM   5978 O  O     . MET A 1 775 ? 152.175 150.220 118.301 1.00 68.88  ? 776  MET A O     1 
ATOM   5979 C  CB    . MET A 1 775 ? 153.022 153.104 119.439 1.00 68.88  ? 776  MET A CB    1 
ATOM   5980 C  CG    . MET A 1 775 ? 152.663 154.559 119.183 1.00 68.88  ? 776  MET A CG    1 
ATOM   5981 S  SD    . MET A 1 775 ? 154.127 155.584 118.954 1.00 68.88  ? 776  MET A SD    1 
ATOM   5982 C  CE    . MET A 1 775 ? 153.422 157.005 118.133 1.00 68.88  ? 776  MET A CE    1 
ATOM   5983 N  N     . ARG A 1 776 ? 152.644 150.040 120.499 1.00 72.99  ? 777  ARG A N     1 
ATOM   5984 C  CA    . ARG A 1 776 ? 153.014 148.628 120.410 1.00 72.99  ? 777  ARG A CA    1 
ATOM   5985 C  C     . ARG A 1 776 ? 151.830 147.718 120.087 1.00 72.99  ? 777  ARG A C     1 
ATOM   5986 O  O     . ARG A 1 776 ? 151.930 146.855 119.206 1.00 72.99  ? 777  ARG A O     1 
ATOM   5987 C  CB    . ARG A 1 776 ? 153.668 148.193 121.720 1.00 72.99  ? 777  ARG A CB    1 
ATOM   5988 C  CG    . ARG A 1 776 ? 154.298 146.812 121.718 1.00 72.99  ? 777  ARG A CG    1 
ATOM   5989 C  CD    . ARG A 1 776 ? 154.915 146.543 123.084 1.00 72.99  ? 777  ARG A CD    1 
ATOM   5990 N  NE    . ARG A 1 776 ? 155.667 145.298 123.148 1.00 72.99  ? 777  ARG A NE    1 
ATOM   5991 C  CZ    . ARG A 1 776 ? 155.122 144.106 123.352 1.00 72.99  ? 777  ARG A CZ    1 
ATOM   5992 N  NH1   . ARG A 1 776 ? 155.883 143.021 123.364 1.00 72.99  ? 777  ARG A NH1   1 
ATOM   5993 N  NH2   . ARG A 1 776 ? 153.815 143.995 123.536 1.00 72.99  ? 777  ARG A NH2   1 
ATOM   5994 N  N     . ASP A 1 777 ? 150.712 147.872 120.806 1.00 74.35  ? 778  ASP A N     1 
ATOM   5995 C  CA    . ASP A 1 777 ? 149.527 147.054 120.536 1.00 74.35  ? 778  ASP A CA    1 
ATOM   5996 C  C     . ASP A 1 777 ? 148.914 147.342 119.166 1.00 74.35  ? 778  ASP A C     1 
ATOM   5997 O  O     . ASP A 1 777 ? 148.372 146.434 118.524 1.00 74.35  ? 778  ASP A O     1 
ATOM   5998 C  CB    . ASP A 1 777 ? 148.499 147.201 121.671 1.00 74.35  ? 778  ASP A CB    1 
ATOM   5999 C  CG    . ASP A 1 777 ? 148.000 148.630 121.883 1.00 74.35  ? 778  ASP A CG    1 
ATOM   6000 O  OD1   . ASP A 1 777 ? 148.041 149.085 123.044 1.00 74.35  ? 778  ASP A OD1   1 
ATOM   6001 O  OD2   . ASP A 1 777 ? 147.459 149.260 120.951 1.00 74.35  ? 778  ASP A OD2   1 
ATOM   6002 N  N     . GLU A 1 778 ? 148.949 148.604 118.731 1.00 75.78  ? 779  GLU A N     1 
ATOM   6003 C  CA    . GLU A 1 778 ? 148.422 148.978 117.420 1.00 75.78  ? 779  GLU A CA    1 
ATOM   6004 C  C     . GLU A 1 778 ? 149.176 148.301 116.279 1.00 75.78  ? 779  GLU A C     1 
ATOM   6005 O  O     . GLU A 1 778 ? 148.559 147.776 115.346 1.00 75.78  ? 779  GLU A O     1 
ATOM   6006 C  CB    . GLU A 1 778 ? 148.459 150.502 117.271 1.00 75.78  ? 779  GLU A CB    1 
ATOM   6007 C  CG    . GLU A 1 778 ? 147.704 151.060 116.068 1.00 75.78  ? 779  GLU A CG    1 
ATOM   6008 C  CD    . GLU A 1 778 ? 148.580 151.232 114.836 1.00 75.78  ? 779  GLU A CD    1 
ATOM   6009 O  OE1   . GLU A 1 778 ? 149.811 151.054 114.942 1.00 75.78  ? 779  GLU A OE1   1 
ATOM   6010 O  OE2   . GLU A 1 778 ? 148.034 151.540 113.756 1.00 75.78  ? 779  GLU A OE2   1 
ATOM   6011 N  N     . ARG A 1 779 ? 150.511 148.334 116.319 1.00 75.21  ? 780  ARG A N     1 
ATOM   6012 C  CA    . ARG A 1 779 ? 151.307 147.680 115.279 1.00 75.21  ? 780  ARG A CA    1 
ATOM   6013 C  C     . ARG A 1 779 ? 151.139 146.164 115.271 1.00 75.21  ? 780  ARG A C     1 
ATOM   6014 O  O     . ARG A 1 779 ? 151.053 145.559 114.196 1.00 75.21  ? 780  ARG A O     1 
ATOM   6015 C  CB    . ARG A 1 779 ? 152.778 148.059 115.414 1.00 75.21  ? 780  ARG A CB    1 
ATOM   6016 C  CG    . ARG A 1 779 ? 153.097 149.420 114.827 1.00 75.21  ? 780  ARG A CG    1 
ATOM   6017 C  CD    . ARG A 1 779 ? 154.482 149.897 115.238 1.00 75.21  ? 780  ARG A CD    1 
ATOM   6018 N  NE    . ARG A 1 779 ? 155.023 151.013 114.450 1.00 75.21  ? 780  ARG A NE    1 
ATOM   6019 C  CZ    . ARG A 1 779 ? 154.538 152.254 114.381 1.00 75.21  ? 780  ARG A CZ    1 
ATOM   6020 N  NH1   . ARG A 1 779 ? 155.196 153.162 113.675 1.00 75.21  ? 780  ARG A NH1   1 
ATOM   6021 N  NH2   . ARG A 1 779 ? 153.473 152.635 115.079 1.00 75.21  ? 780  ARG A NH2   1 
ATOM   6022 N  N     . LEU A 1 780 ? 151.142 145.532 116.451 1.00 77.06  ? 781  LEU A N     1 
ATOM   6023 C  CA    . LEU A 1 780 ? 150.941 144.085 116.542 1.00 77.06  ? 781  LEU A CA    1 
ATOM   6024 C  C     . LEU A 1 780 ? 149.591 143.658 115.972 1.00 77.06  ? 781  LEU A C     1 
ATOM   6025 O  O     . LEU A 1 780 ? 149.501 142.632 115.288 1.00 77.06  ? 781  LEU A O     1 
ATOM   6026 C  CB    . LEU A 1 780 ? 151.092 143.634 118.001 1.00 77.06  ? 781  LEU A CB    1 
ATOM   6027 C  CG    . LEU A 1 780 ? 150.893 142.174 118.430 1.00 77.06  ? 781  LEU A CG    1 
ATOM   6028 C  CD1   . LEU A 1 780 ? 151.884 141.839 119.527 1.00 77.06  ? 781  LEU A CD1   1 
ATOM   6029 C  CD2   . LEU A 1 780 ? 149.483 141.907 118.948 1.00 77.06  ? 781  LEU A CD2   1 
ATOM   6030 N  N     . SER A 1 781 ? 148.532 144.414 116.280 1.00 77.78  ? 782  SER A N     1 
ATOM   6031 C  CA    . SER A 1 781 ? 147.202 144.147 115.734 1.00 77.78  ? 782  SER A CA    1 
ATOM   6032 C  C     . SER A 1 781 ? 147.184 144.216 114.209 1.00 77.78  ? 782  SER A C     1 
ATOM   6033 O  O     . SER A 1 781 ? 146.531 143.395 113.556 1.00 77.78  ? 782  SER A O     1 
ATOM   6034 C  CB    . SER A 1 781 ? 146.189 145.125 116.327 1.00 77.78  ? 782  SER A CB    1 
ATOM   6035 O  OG    . SER A 1 781 ? 146.143 145.014 117.738 1.00 77.78  ? 782  SER A OG    1 
ATOM   6036 N  N     . ARG A 1 782 ? 147.862 145.216 113.635 1.00 77.70  ? 783  ARG A N     1 
ATOM   6037 C  CA    . ARG A 1 782 ? 148.015 145.313 112.183 1.00 77.70  ? 783  ARG A CA    1 
ATOM   6038 C  C     . ARG A 1 782 ? 148.719 144.091 111.601 1.00 77.70  ? 783  ARG A C     1 
ATOM   6039 O  O     . ARG A 1 782 ? 148.319 143.586 110.544 1.00 77.70  ? 783  ARG A O     1 
ATOM   6040 C  CB    . ARG A 1 782 ? 148.766 146.599 111.828 1.00 77.70  ? 783  ARG A CB    1 
ATOM   6041 C  CG    . ARG A 1 782 ? 149.138 146.736 110.354 1.00 77.70  ? 783  ARG A CG    1 
ATOM   6042 C  CD    . ARG A 1 782 ? 149.440 148.172 109.873 1.00 77.70  ? 783  ARG A CD    1 
ATOM   6043 N  NE    . ARG A 1 782 ? 150.364 148.950 110.703 1.00 77.70  ? 783  ARG A NE    1 
ATOM   6044 C  CZ    . ARG A 1 782 ? 149.995 149.809 111.650 1.00 77.70  ? 783  ARG A CZ    1 
ATOM   6045 N  NH1   . ARG A 1 782 ? 150.905 150.389 112.418 1.00 77.70  ? 783  ARG A NH1   1 
ATOM   6046 N  NH2   . ARG A 1 782 ? 148.708 150.039 111.868 1.00 77.70  ? 783  ARG A NH2   1 
ATOM   6047 N  N     . ILE A 1 783 ? 149.796 143.640 112.256 1.00 77.84  ? 784  ILE A N     1 
ATOM   6048 C  CA    . ILE A 1 783 ? 150.521 142.433 111.849 1.00 77.84  ? 784  ILE A CA    1 
ATOM   6049 C  C     . ILE A 1 783 ? 149.595 141.217 111.816 1.00 77.84  ? 784  ILE A C     1 
ATOM   6050 O  O     . ILE A 1 783 ? 149.622 140.426 110.864 1.00 77.84  ? 784  ILE A O     1 
ATOM   6051 C  CB    . ILE A 1 783 ? 151.731 142.210 112.776 1.00 77.84  ? 784  ILE A CB    1 
ATOM   6052 C  CG1   . ILE A 1 783 ? 152.781 143.295 112.537 1.00 77.84  ? 784  ILE A CG1   1 
ATOM   6053 C  CG2   . ILE A 1 783 ? 152.348 140.833 112.576 1.00 77.84  ? 784  ILE A CG2   1 
ATOM   6054 C  CD1   . ILE A 1 783 ? 153.416 143.244 111.169 1.00 77.84  ? 784  ILE A CD1   1 
ATOM   6055 N  N     . ILE A 1 784 ? 148.768 141.057 112.859 1.00 81.02  ? 785  ILE A N     1 
ATOM   6056 C  CA    . ILE A 1 784 ? 147.803 139.956 112.951 1.00 81.02  ? 785  ILE A CA    1 
ATOM   6057 C  C     . ILE A 1 784 ? 146.830 139.961 111.772 1.00 81.02  ? 785  ILE A C     1 
ATOM   6058 O  O     . ILE A 1 784 ? 146.527 138.907 111.195 1.00 81.02  ? 785  ILE A O     1 
ATOM   6059 C  CB    . ILE A 1 784 ? 147.067 140.027 114.305 1.00 81.02  ? 785  ILE A CB    1 
ATOM   6060 C  CG1   . ILE A 1 784 ? 148.028 139.692 115.448 1.00 81.02  ? 785  ILE A CG1   1 
ATOM   6061 C  CG2   . ILE A 1 784 ? 145.849 139.110 114.349 1.00 81.02  ? 785  ILE A CG2   1 
ATOM   6062 C  CD1   . ILE A 1 784 ? 148.513 138.262 115.439 1.00 81.02  ? 785  ILE A CD1   1 
ATOM   6063 N  N     . THR A 1 785 ? 146.349 141.145 111.380 1.00 83.58  ? 786  THR A N     1 
ATOM   6064 C  CA    . THR A 1 785 ? 145.513 141.254 110.185 1.00 83.58  ? 786  THR A CA    1 
ATOM   6065 C  C     . THR A 1 785 ? 146.280 140.893 108.917 1.00 83.58  ? 786  THR A C     1 
ATOM   6066 O  O     . THR A 1 785 ? 145.707 140.323 107.980 1.00 83.58  ? 786  THR A O     1 
ATOM   6067 C  CB    . THR A 1 785 ? 144.935 142.664 110.070 1.00 83.58  ? 786  THR A CB    1 
ATOM   6068 O  OG1   . THR A 1 785 ? 146.000 143.605 109.877 1.00 83.58  ? 786  THR A OG1   1 
ATOM   6069 C  CG2   . THR A 1 785 ? 144.134 143.023 111.312 1.00 83.58  ? 786  THR A CG2   1 
ATOM   6070 N  N     . ARG A 1 786 ? 147.571 141.229 108.860 1.00 81.47  ? 787  ARG A N     1 
ATOM   6071 C  CA    . ARG A 1 786 ? 148.396 140.795 107.737 1.00 81.47  ? 787  ARG A CA    1 
ATOM   6072 C  C     . ARG A 1 786 ? 148.600 139.285 107.723 1.00 81.47  ? 787  ARG A C     1 
ATOM   6073 O  O     . ARG A 1 786 ? 148.703 138.695 106.643 1.00 81.47  ? 787  ARG A O     1 
ATOM   6074 C  CB    . ARG A 1 786 ? 149.736 141.526 107.739 1.00 81.47  ? 787  ARG A CB    1 
ATOM   6075 C  CG    . ARG A 1 786 ? 149.643 142.926 107.156 1.00 81.47  ? 787  ARG A CG    1 
ATOM   6076 C  CD    . ARG A 1 786 ? 151.010 143.549 106.973 1.00 81.47  ? 787  ARG A CD    1 
ATOM   6077 N  NE    . ARG A 1 786 ? 150.952 144.739 106.130 1.00 81.47  ? 787  ARG A NE    1 
ATOM   6078 C  CZ    . ARG A 1 786 ? 151.957 145.165 105.372 1.00 81.47  ? 787  ARG A CZ    1 
ATOM   6079 N  NH1   . ARG A 1 786 ? 151.801 146.227 104.594 1.00 81.47  ? 787  ARG A NH1   1 
ATOM   6080 N  NH2   . ARG A 1 786 ? 153.107 144.505 105.363 1.00 81.47  ? 787  ARG A NH2   1 
ATOM   6081 N  N     . ILE A 1 787 ? 148.690 138.657 108.899 1.00 82.47  ? 788  ILE A N     1 
ATOM   6082 C  CA    . ILE A 1 787 ? 148.803 137.200 108.982 1.00 82.47  ? 788  ILE A CA    1 
ATOM   6083 C  C     . ILE A 1 787 ? 147.552 136.525 108.423 1.00 82.47  ? 788  ILE A C     1 
ATOM   6084 O  O     . ILE A 1 787 ? 147.637 135.517 107.709 1.00 82.47  ? 788  ILE A O     1 
ATOM   6085 C  CB    . ILE A 1 787 ? 149.087 136.780 110.439 1.00 82.47  ? 788  ILE A CB    1 
ATOM   6086 C  CG1   . ILE A 1 787 ? 150.467 137.275 110.877 1.00 82.47  ? 788  ILE A CG1   1 
ATOM   6087 C  CG2   . ILE A 1 787 ? 149.000 135.268 110.625 1.00 82.47  ? 788  ILE A CG2   1 
ATOM   6088 C  CD1   . ILE A 1 787 ? 151.596 136.849 109.960 1.00 82.47  ? 788  ILE A CD1   1 
ATOM   6089 N  N     . GLN A 1 788 ? 146.375 137.064 108.744 1.00 83.07  ? 789  GLN A N     1 
ATOM   6090 C  CA    . GLN A 1 788 ? 145.134 136.571 108.151 1.00 83.07  ? 789  GLN A CA    1 
ATOM   6091 C  C     . GLN A 1 788 ? 145.105 136.780 106.637 1.00 83.07  ? 789  GLN A C     1 
ATOM   6092 O  O     . GLN A 1 788 ? 144.705 135.882 105.886 1.00 83.07  ? 789  GLN A O     1 
ATOM   6093 C  CB    . GLN A 1 788 ? 143.930 137.247 108.812 1.00 83.07  ? 789  GLN A CB    1 
ATOM   6094 C  CG    . GLN A 1 788 ? 143.685 136.824 110.256 1.00 83.07  ? 789  GLN A CG    1 
ATOM   6095 C  CD    . GLN A 1 788 ? 142.209 136.808 110.623 1.00 83.07  ? 789  GLN A CD    1 
ATOM   6096 O  OE1   . GLN A 1 788 ? 141.403 136.149 109.968 1.00 83.07  ? 789  GLN A OE1   1 
ATOM   6097 N  NE2   . GLN A 1 788 ? 141.852 137.533 111.677 1.00 83.07  ? 789  GLN A NE2   1 
ATOM   6098 N  N     . ALA A 1 789 ? 145.493 137.976 106.179 1.00 83.59  ? 790  ALA A N     1 
ATOM   6099 C  CA    . ALA A 1 789 ? 145.464 138.297 104.751 1.00 83.59  ? 790  ALA A CA    1 
ATOM   6100 C  C     . ALA A 1 789 ? 146.414 137.436 103.922 1.00 83.59  ? 790  ALA A C     1 
ATOM   6101 O  O     . ALA A 1 789 ? 146.070 137.039 102.802 1.00 83.59  ? 790  ALA A O     1 
ATOM   6102 C  CB    . ALA A 1 789 ? 145.785 139.777 104.547 1.00 83.59  ? 790  ALA A CB    1 
ATOM   6103 N  N     . GLN A 1 790 ? 147.626 137.173 104.427 1.00 84.04  ? 791  GLN A N     1 
ATOM   6104 C  CA    . GLN A 1 790 ? 148.545 136.286 103.711 1.00 84.04  ? 791  GLN A CA    1 
ATOM   6105 C  C     . GLN A 1 790 ? 148.015 134.857 103.637 1.00 84.04  ? 791  GLN A C     1 
ATOM   6106 O  O     . GLN A 1 790 ? 148.256 134.155 102.648 1.00 84.04  ? 791  GLN A O     1 
ATOM   6107 C  CB    . GLN A 1 790 ? 149.961 136.355 104.313 1.00 84.04  ? 791  GLN A CB    1 
ATOM   6108 C  CG    . GLN A 1 790 ? 150.196 135.934 105.772 1.00 84.04  ? 791  GLN A CG    1 
ATOM   6109 C  CD    . GLN A 1 790 ? 150.211 134.434 106.020 1.00 84.04  ? 791  GLN A CD    1 
ATOM   6110 O  OE1   . GLN A 1 790 ? 150.462 133.642 105.112 1.00 84.04  ? 791  GLN A OE1   1 
ATOM   6111 N  NE2   . GLN A 1 790 ? 149.929 134.039 107.254 1.00 84.04  ? 791  GLN A NE2   1 
ATOM   6112 N  N     . SER A 1 791 ? 147.337 134.397 104.696 1.00 84.69  ? 792  SER A N     1 
ATOM   6113 C  CA    . SER A 1 791 ? 146.706 133.079 104.684 1.00 84.69  ? 792  SER A CA    1 
ATOM   6114 C  C     . SER A 1 791 ? 145.662 132.970 103.578 1.00 84.69  ? 792  SER A C     1 
ATOM   6115 O  O     . SER A 1 791 ? 145.592 131.957 102.875 1.00 84.69  ? 792  SER A O     1 
ATOM   6116 C  CB    . SER A 1 791 ? 146.080 132.787 106.047 1.00 84.69  ? 792  SER A CB    1 
ATOM   6117 O  OG    . SER A 1 791 ? 144.957 133.617 106.283 1.00 84.69  ? 792  SER A OG    1 
ATOM   6118 N  N     . ARG A 1 792 ? 144.816 133.993 103.435 1.00 85.99  ? 793  ARG A N     1 
ATOM   6119 C  CA    . ARG A 1 792 ? 143.901 134.054 102.298 1.00 85.99  ? 793  ARG A CA    1 
ATOM   6120 C  C     . ARG A 1 792 ? 144.657 134.153 100.973 1.00 85.99  ? 793  ARG A C     1 
ATOM   6121 O  O     . ARG A 1 792 ? 144.229 133.574 99.966  1.00 85.99  ? 793  ARG A O     1 
ATOM   6122 C  CB    . ARG A 1 792 ? 142.939 135.235 102.484 1.00 85.99  ? 793  ARG A CB    1 
ATOM   6123 C  CG    . ARG A 1 792 ? 142.234 135.738 101.228 1.00 85.99  ? 793  ARG A CG    1 
ATOM   6124 C  CD    . ARG A 1 792 ? 140.977 136.525 101.564 1.00 85.99  ? 793  ARG A CD    1 
ATOM   6125 N  NE    . ARG A 1 792 ? 140.328 137.051 100.366 1.00 85.99  ? 793  ARG A NE    1 
ATOM   6126 C  CZ    . ARG A 1 792 ? 139.389 136.408 99.678  1.00 85.99  ? 793  ARG A CZ    1 
ATOM   6127 N  NH1   . ARG A 1 792 ? 138.834 136.980 98.619  1.00 85.99  ? 793  ARG A NH1   1 
ATOM   6128 N  NH2   . ARG A 1 792 ? 138.987 135.204 100.062 1.00 85.99  ? 793  ARG A NH2   1 
ATOM   6129 N  N     . GLY A 1 793 ? 145.816 134.817 100.976 1.00 85.59  ? 794  GLY A N     1 
ATOM   6130 C  CA    . GLY A 1 793 ? 146.605 134.931 99.759  1.00 85.59  ? 794  GLY A CA    1 
ATOM   6131 C  C     . GLY A 1 793 ? 147.257 133.636 99.308  1.00 85.59  ? 794  GLY A C     1 
ATOM   6132 O  O     . GLY A 1 793 ? 147.316 133.354 98.107  1.00 85.59  ? 794  GLY A O     1 
ATOM   6133 N  N     . VAL A 1 794 ? 147.764 132.836 100.250 1.00 87.20  ? 795  VAL A N     1 
ATOM   6134 C  CA    . VAL A 1 794 ? 148.395 131.577 99.858  1.00 87.20  ? 795  VAL A CA    1 
ATOM   6135 C  C     . VAL A 1 794 ? 147.361 130.540 99.421  1.00 87.20  ? 795  VAL A C     1 
ATOM   6136 O  O     . VAL A 1 794 ? 147.665 129.677 98.588  1.00 87.20  ? 795  VAL A O     1 
ATOM   6137 C  CB    . VAL A 1 794 ? 149.326 131.052 100.973 1.00 87.20  ? 795  VAL A CB    1 
ATOM   6138 C  CG1   . VAL A 1 794 ? 150.417 132.068 101.263 1.00 87.20  ? 795  VAL A CG1   1 
ATOM   6139 C  CG2   . VAL A 1 794 ? 148.567 130.739 102.250 1.00 87.20  ? 795  VAL A CG2   1 
ATOM   6140 N  N     . LEU A 1 795 ? 146.154 130.575 99.984  1.00 85.12  ? 796  LEU A N     1 
ATOM   6141 C  CA    . LEU A 1 795 ? 145.095 129.636 99.611  1.00 85.12  ? 796  LEU A CA    1 
ATOM   6142 C  C     . LEU A 1 795 ? 144.641 129.818 98.163  1.00 85.12  ? 796  LEU A C     1 
ATOM   6143 O  O     . LEU A 1 795 ? 144.618 128.869 97.379  1.00 85.12  ? 796  LEU A O     1 
ATOM   6144 C  CB    . LEU A 1 795 ? 143.899 129.774 100.554 1.00 85.12  ? 796  LEU A CB    1 
ATOM   6145 C  CG    . LEU A 1 795 ? 144.085 129.188 101.955 1.00 85.12  ? 796  LEU A CG    1 
ATOM   6146 C  CD1   . LEU A 1 795 ? 142.998 129.685 102.891 1.00 85.12  ? 796  LEU A CD1   1 
ATOM   6147 C  CD2   . LEU A 1 795 ? 144.102 127.668 101.905 1.00 85.12  ? 796  LEU A CD2   1 
HETATM 6148 MG MG    . MG  B 2 .   ? 142.593 149.341 160.633 1.00 20.75  ? 1201 MG  A MG    1 
HETATM 6149 P  PB    . ADP C 3 .   ? 140.218 151.409 159.725 1.00 22.72  ? 1202 ADP A PB    1 
HETATM 6150 O  O1B   . ADP C 3 .   ? 140.671 150.094 160.290 1.00 22.72  ? 1202 ADP A O1B   1 
HETATM 6151 O  O2B   . ADP C 3 .   ? 139.443 152.269 160.680 1.00 22.72  ? 1202 ADP A O2B   1 
HETATM 6152 O  O3B   . ADP C 3 .   ? 141.298 152.159 158.995 1.00 22.72  ? 1202 ADP A O3B   1 
HETATM 6153 P  PA    . ADP C 3 .   ? 137.819 150.200 158.908 1.00 22.72  ? 1202 ADP A PA    1 
HETATM 6154 O  O1A   . ADP C 3 .   ? 137.812 148.938 158.099 1.00 22.72  ? 1202 ADP A O1A   1 
HETATM 6155 O  O2A   . ADP C 3 .   ? 137.637 150.079 160.393 1.00 22.72  ? 1202 ADP A O2A   1 
HETATM 6156 O  O3A   . ADP C 3 .   ? 139.170 151.004 158.577 1.00 22.72  ? 1202 ADP A O3A   1 
HETATM 6157 O  "O5'" . ADP C 3 .   ? 136.631 151.115 158.340 1.00 22.72  ? 1202 ADP A "O5'" 1 
HETATM 6158 C  "C5'" . ADP C 3 .   ? 136.003 152.009 159.238 1.00 22.72  ? 1202 ADP A "C5'" 1 
HETATM 6159 C  "C4'" . ADP C 3 .   ? 134.527 152.126 158.905 1.00 22.72  ? 1202 ADP A "C4'" 1 
HETATM 6160 O  "O4'" . ADP C 3 .   ? 134.327 153.100 157.876 1.00 22.72  ? 1202 ADP A "O4'" 1 
HETATM 6161 C  "C3'" . ADP C 3 .   ? 133.899 150.856 158.386 1.00 22.72  ? 1202 ADP A "C3'" 1 
HETATM 6162 O  "O3'" . ADP C 3 .   ? 133.425 150.080 159.481 1.00 22.72  ? 1202 ADP A "O3'" 1 
HETATM 6163 C  "C2'" . ADP C 3 .   ? 132.740 151.451 157.632 1.00 22.72  ? 1202 ADP A "C2'" 1 
HETATM 6164 O  "O2'" . ADP C 3 .   ? 131.783 151.956 158.560 1.00 22.72  ? 1202 ADP A "O2'" 1 
HETATM 6165 C  "C1'" . ADP C 3 .   ? 133.381 152.617 156.921 1.00 22.72  ? 1202 ADP A "C1'" 1 
HETATM 6166 N  N9    . ADP C 3 .   ? 134.125 152.264 155.689 1.00 22.72  ? 1202 ADP A N9    1 
HETATM 6167 C  C8    . ADP C 3 .   ? 135.460 152.328 155.549 1.00 22.72  ? 1202 ADP A C8    1 
HETATM 6168 N  N7    . ADP C 3 .   ? 135.832 151.983 154.299 1.00 22.72  ? 1202 ADP A N7    1 
HETATM 6169 C  C5    . ADP C 3 .   ? 134.733 151.651 153.618 1.00 22.72  ? 1202 ADP A C5    1 
HETATM 6170 C  C6    . ADP C 3 .   ? 134.450 151.184 152.249 1.00 22.72  ? 1202 ADP A C6    1 
HETATM 6171 N  N6    . ADP C 3 .   ? 135.451 150.983 151.364 1.00 22.72  ? 1202 ADP A N6    1 
HETATM 6172 N  N1    . ADP C 3 .   ? 133.164 150.969 151.921 1.00 22.72  ? 1202 ADP A N1    1 
HETATM 6173 C  C2    . ADP C 3 .   ? 132.174 151.171 152.806 1.00 22.72  ? 1202 ADP A C2    1 
HETATM 6174 N  N3    . ADP C 3 .   ? 132.363 151.594 154.068 1.00 22.72  ? 1202 ADP A N3    1 
HETATM 6175 C  C4    . ADP C 3 .   ? 133.604 151.850 154.531 1.00 22.72  ? 1202 ADP A C4    1 
HETATM 6176 P  P     . PO4 D 4 .   ? 142.635 151.931 163.027 1.00 28.28  ? 1203 PO4 A P     1 
HETATM 6177 O  O1    . PO4 D 4 .   ? 142.607 152.544 161.649 1.00 28.28  ? 1203 PO4 A O1    1 
HETATM 6178 O  O2    . PO4 D 4 .   ? 142.291 150.468 162.907 1.00 28.28  ? 1203 PO4 A O2    1 
HETATM 6179 O  O3    . PO4 D 4 .   ? 144.008 152.070 163.634 1.00 28.28  ? 1203 PO4 A O3    1 
HETATM 6180 O  O4    . PO4 D 4 .   ? 141.637 152.629 163.914 1.00 28.28  ? 1203 PO4 A O4    1 
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